data_9BMY
# 
_entry.id   9BMY 
# 
_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   9BMY         pdb_00009bmy 10.2210/pdb9bmy/pdb 
WWPDB D_1000283542 ?            ?                   
EMDB  EMD-44715    ?            ?                   
# 
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                        9BMY 
_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-1 of motor domain from full-length human dynein-1 in apo condition' 
_pdbx_database_related.db_id          EMD-44715 
_pdbx_database_related.content_type   'associated EM volume' 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              jack.zhang@yale.edu 
_pdbx_contact_author.name_first         Jack 
_pdbx_contact_author.name_last          Zhang 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-8617-2855 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Chai, P.'  1 0000-0001-9702-978X 
'Zhang, K.' 2 0000-0001-8617-2855 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Nat.Struct.Mol.Biol. 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1545-9985 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'The mechanochemical cycle of reactive full-length human dynein 1.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s41594-025-01543-3 
_citation.pdbx_database_id_PubMed   40263469 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Chai, P.'       1 0000-0001-9702-978X 
primary 'Yang, J.'       2 ?                   
primary 'Geohring, I.C.' 3 ?                   
primary 'Markus, S.M.'   4 0000-0002-3098-0236 
primary 'Wang, Y.'       5 0000-0002-8020-3937 
primary 'Zhang, K.'      6 0000-0001-8617-2855 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Cytoplasmic dynein 1 heavy chain 1' 533083.250 1 ? ? ? ? 
2 non-polymer syn "ADENOSINE-5'-DIPHOSPHATE"           427.201    3 ? ? ? ? 
3 non-polymer syn "ADENOSINE-5'-TRIPHOSPHATE"          507.181    1 ? ? ? ? 
4 non-polymer syn 'MAGNESIUM ION'                      24.305     2 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Cytoplasmic dynein heavy chain 1,Dynein heavy chain,cytosolic' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MSEPGGGGGEDGSAGLEVSAVQNVADVSVLQKHLRKLVPLLLEDGGEAPAALEAALEEKSALEQMRKFLSDPQVHTVLVE
RSTLKEDVGDEGEEEKEFISYNINIDIHYGVKSNSLAFIKRTPVIDADKPVSSQLRVLTLSEDSPYETLHSFISNAVAPF
FKSYIRESGKADRDGDKMAPSVEKKIAELEMGLLHLQQNIEIPEISLPIHPMITNVAKQCYERGEKPKVTDFGDKVEDPT
FLNQLQSGVNRWIREIQKVTKLDRDPASGTALQEISFWLNLERALYRIQEKRESPEVLLTLDILKHGKRFHATVSFDTDT
GLKQALETVNDYNPLMKDFPLNDLLSATELDKIRQALVAIFTHLRKIRNTKYPIQRALRLVEAISRDLSSQLLKVLGTRK
LMHVAYEEFEKVMVACFEVFQTWDDEYEKLQVLLRDIVKRKREENLKMVWRINPAHRKLQARLDQMRKFRRQHEQLRAVI
VRVLRPQVTAVAQQNQGEVPEPQDMKVAEVLFDAADANAIEEVNLAYENVKEVDGLDVSKEGTEAWEAAMKRYDERIDRV
ETRITARLRDQLGTAKNANEMFRIFSRFNALFVRPHIRGAIREYQTQLIQRVKDDIESLHDKFKVQYPQSQACKMSHVRD
LPPVSGSIIWAKQIDRQLTAYMKRVEDVLGKGWENHVEGQKLKQDGDSFRMKLNTQEIFDDWARKVQQRNLGVSGRIFTI
ESTRVRGRTGNVLKLKVNFLPEIITLSKEVRNLKWLGFRVPLAIVNKAHQANQLYPFAISLIESVRTYERTCEKVEERNT
ISLLVAGLKKEVQALIAEGIALVWESYKLDPYVQRLAETVFNFQEKVDDLLIIEEKIDLEVRSLETCMYDHKTFSEILNR
VQKAVDDLNLHSYSNLPIWVNKLDMEIERILGVRLQAGLRAWTQVLLGQAEDKAEVDMDTDAPQVSHKPGGEPKIKNVVH
ELRITNQVIYLNPPIEECRYKLYQEMFAWKMVVLSLPRIQSQRYQVGVHYELTEEEKFYRNALTRMPDGPVALEESYSAV
MGIVSEVEQYVKVWLQYQCLWDMQAENIYNRLGEDLNKWQALLVQIRKARGTFDNAETKKEFGPVVIDYGKVQSKVNLKY
DSWHKEVLSKFGQMLGSNMTEFHSQISKSRQELEQHSVDTASTSDAVTFITYVQSLKRKIKQFEKQVELYRNGQRLLEKQ
RFQFPPSWLYIDNIEGEWGAFNDIMRRKDSAIQQQVANLQMKIVQEDRAVESRTTDLLTDWEKTKPVTGNLRPEEALQAL
TIYEGKFGRLKDDREKCAKAKEALELTDTGLLSGSEERVQVALEELQDLKGVWSELSKVWEQIDQMKEQPWVSVQPRKLR
QNLDALLNQLKSFPARLRQYASYEFVQRLLKGYMKINMLVIELKSEALKDRHWKQLMKRLHVNWVVSELTLGQIWDVDLQ
KNEAIVKDVLLVAQGEMALEEFLKQIREVWNTYELDLVNYQNKCRLIRGWDDLFNKVKEHINSVSAMKLSPYYKVFEEDA
LSWEDKLNRIMALFDVWIDVQRRWVYLEGIFTGSADIKHLLPVETQRFQSISTEFLALMKKVSKSPLVMDVLNIQGVQRS
LERLADLLGKIQKALGEYLERERSSFPRFYFVGDEDLLEIIGNSKNVAKLQKHFKKMFAGVSSIILNEDNSVVLGISSRE
GEEVMFKTPVSITEHPKINEWLTLVEKEMRVTLAKLLAESVTEVEIFGKATSIDPNTYITWIDKYQAQLVVLSAQIAWSE
NVETALSSMGGGGDAAPLHSVLSNVEVTLNVLADSVLMEQPPLRRRKLEHLITELVHQRDVTRSLIKSKIDNAKSFEWLS
QMRFYFDPKQTDVLQQLSIQMANAKFNYGFEYLGVQDKLVQTPLTDRCYLTMTQALEARLGGSPFGPAGTGKTESVKALG
HQLGRFVLVFNCDETFDFQAMGRIFVGLCQVGAWGCFDEFNRLEERMLSAVSQQVQCIQEALREHSNPNYDKTSAPITCE
LLNKQVKVSPDMAIFITMNPGYAGRSNLPDNLKKLFRSLAMTKPDRQLIAQVMLYSQGFRTAEVLANKIVPFFKLCDEQL
SSQSHYDFGLRALKSVLVSAGNVKRERIQKIKREKEERGEAVDEGEIAENLPEQEILIQSVCETMVPKLVAEDIPLLFSL
LSDVFPGVQYHRGEMTALREELKKVCQEMYLTYGDGEEVGGMWVEKVLQLYQITQINHGLMMVGPSGSGKSMAWRVLLKA
LERLEGVEGVAHIIDPKAISKDHLYGTLDPNTREWTDGLFTHVLRKIIDSVRGELQKRQWIVFDGDVDPEWVENLNSVLD
DNKLLTLPNGERLSLPPNVRIMFEVQDLKYATLATVSRCGMVWFSEDVLSTDMIFNNFLARLRSIPLDEGEDEAQRRRKG
KEDEGEEAASPMLQIQRDAATIMQPYFTSNGLVTKALEHAFQLEHIMDLTRLRCLGSLFSMLHQACRNVAQYNANHPDFP
MQIEQLERYIQRYLVYAILWSLSGDSRLKMRAELGEYIRRITTVPLPTAPNIPIIDYEVSISGEWSPWQAKVPQIEVETH
KVAAPDVVVPTLDTVRHEALLYTWLAEHKPLVLCGPPGSGKTMTLFSALRALPDMEVVGLNFSSATTPELLLKTFDHYCE
YRRTPNGVVLAPVQLGKWLVLFCDEINLPDMDKYGTQRVISFIRQMVEHGGFYRTSDQTWVKLERIQFVGACNPPTDPGR
KPLSHRFLRHVPVVYVDYPGPASLTQIYGTFNRAMLRLIPSLRTYAEPLTAAMVEFYTMSQERFTQDTQPHYIYSPREMT
RWVRGIFEALRPLETLPVEGLIRIWAHEALRLFQDRLVEDEERRWTDENIDTVALKHFPNIDREKAMSRPILYSNWLSKD
YIPVDQEELRDYVKARLKVFYEEELDVPLVLFNEVLDHVLRIDRIFRQPQGHLLLIGVSGAGKTTLSRFVAWMNGLSVYQ
IKVHRKYTGEDFDEDLRTVLRRSGCKNEKIAFIMDESNVLDSGFLERMNTLLANGEVPGLFEGDEYATLMTQCKEGAQKE
GLMLDSHEELYKWFTSQVIRNLHVVFTMNPSSEGLKDRAATSPALFNRCVLNWFGDWSTEALYQVGKEFTSKMDLEKPNY
IVPDYMPVVYDKLPQPPSHREAIVNSCVFVHQTLHQANARLAKRGGRTMAITPRHYLDFINHYANLFHEKRSELEEQQMH
LNVGLRKIKETVDQVEELRRDLRIKSQELEVKNAAANDKLKKMVKDQQEAEKKKVMSQEIQEQLHKQQEVIADKQMSVKE
DLDKVEPAVIEAQNAVKSIKKQHLVEVRSMANPPAAVKLALESICLLLGESTTDWKQIRSIIMRENFIPTIVNFSAEEIS
DAIREKMKKNYMSNPSYNYEIVNRASLACGPMVKWAIAQLNYADMLKRVEPLRNELQKLEDDAKDNQQKANEVEQMIRDL
EASIARYKEEYAVLISEAQAIKADLAAVEAKVNRSTALLKSLSAERERWEKTSETFKNQMSTIAGDCLLSAAFIAYAGYF
DQQMRQNLFTTWSHHLQQANIQFRTDIARTEYLSNADERLRWQASSLPADDLCTENAIMLKRFNRYPLIIDPSGQATEFI
MNEYKDRKITRTSFLDDAFRKNLESALRFGNPLLVQDVESYDPVLNPVLNREVRRTGGRVLITLGDQDIDLSPSFVIFLS
TRDPTVEFPPDLCSRVTFVNFTVTRSSLQSQCLNEVLKAERPDVDEKRSDLLKLQGEFQLRLRQLEKSLLQALNEVKGRI
LDDDTIITTLENLKREAAEVTRKVEETDIVMQEVETVSQQYLPLSTACSSIYFTMESLKQIHFLYQYSLQFFLDIYHNVL
YENPNLKGVTDHTQRLSIITKDLFQVAFNRVARGMLHQDHITFAMLLARIKLKGTVGEPTYDAEFQHFLRGNEIVLSAGS
TPRIQGLTVEQAEAVVRLSCLPAFKDLIAKVQADEQFGIWLDSSSPEQTVPYLWSEETPATPIGQAIHRLLLIQAFRPDR
LLAMAHMFVSTNLGESFMSIMEQPLDLTHIVGTEVKPNTPVLMCSVPGYDASGHVEDLAAEQNTQITSIAIGSAEGFNQA
DKAINTAVKSGRWVMLKNVHLAPGWLMQLEKKLHSLQPHACFRLFLTMEINPKVPVNLLRAGRIFVFEPPPGVKANMLRT
FSSIPVSRICKSPNERARLYFLLAWFHAIIQERLRYAPLGWSKKYEFGESDLRSACDTVDTWLDDTAKGRQNISPDKIPW
SALKTLMAQSIYGGRVDNEFDQRLLNTFLERLFTTRSFDSEFKLACKVDGHKDIQMPDGIRREEFVQWVELLPDTQTPSW
LGLPNNAERVLLTTQGVDMISKMLKMQMLEDEDDLAYAETEKKTRTDSTSDGRPAWMRTLHTTASNWLHLIPQTLSHLKR
TVENIKDPLFRFFEREVKMGAKLLQDVRQDLADVVQVCEGKKKQTNYLRTLINELVKGILPRSWSHYTVPAGMTVIQWVS
DFSERIKQLQNISLAAASGGAKELKNIHVCLGGLFVPEAYITATRQYVAQANSWSLEELCLEVNVTTSQGATLDACSFGV
TGLKLQGATCNNNKLSLSNAISTALPLTQLRWVKQTNTEKKASVVTLPVYLNFTRADLIFTVDFEIATKEDPRSFYERGV
AVLCTE
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MSEPGGGGGEDGSAGLEVSAVQNVADVSVLQKHLRKLVPLLLEDGGEAPAALEAALEEKSALEQMRKFLSDPQVHTVLVE
RSTLKEDVGDEGEEEKEFISYNINIDIHYGVKSNSLAFIKRTPVIDADKPVSSQLRVLTLSEDSPYETLHSFISNAVAPF
FKSYIRESGKADRDGDKMAPSVEKKIAELEMGLLHLQQNIEIPEISLPIHPMITNVAKQCYERGEKPKVTDFGDKVEDPT
FLNQLQSGVNRWIREIQKVTKLDRDPASGTALQEISFWLNLERALYRIQEKRESPEVLLTLDILKHGKRFHATVSFDTDT
GLKQALETVNDYNPLMKDFPLNDLLSATELDKIRQALVAIFTHLRKIRNTKYPIQRALRLVEAISRDLSSQLLKVLGTRK
LMHVAYEEFEKVMVACFEVFQTWDDEYEKLQVLLRDIVKRKREENLKMVWRINPAHRKLQARLDQMRKFRRQHEQLRAVI
VRVLRPQVTAVAQQNQGEVPEPQDMKVAEVLFDAADANAIEEVNLAYENVKEVDGLDVSKEGTEAWEAAMKRYDERIDRV
ETRITARLRDQLGTAKNANEMFRIFSRFNALFVRPHIRGAIREYQTQLIQRVKDDIESLHDKFKVQYPQSQACKMSHVRD
LPPVSGSIIWAKQIDRQLTAYMKRVEDVLGKGWENHVEGQKLKQDGDSFRMKLNTQEIFDDWARKVQQRNLGVSGRIFTI
ESTRVRGRTGNVLKLKVNFLPEIITLSKEVRNLKWLGFRVPLAIVNKAHQANQLYPFAISLIESVRTYERTCEKVEERNT
ISLLVAGLKKEVQALIAEGIALVWESYKLDPYVQRLAETVFNFQEKVDDLLIIEEKIDLEVRSLETCMYDHKTFSEILNR
VQKAVDDLNLHSYSNLPIWVNKLDMEIERILGVRLQAGLRAWTQVLLGQAEDKAEVDMDTDAPQVSHKPGGEPKIKNVVH
ELRITNQVIYLNPPIEECRYKLYQEMFAWKMVVLSLPRIQSQRYQVGVHYELTEEEKFYRNALTRMPDGPVALEESYSAV
MGIVSEVEQYVKVWLQYQCLWDMQAENIYNRLGEDLNKWQALLVQIRKARGTFDNAETKKEFGPVVIDYGKVQSKVNLKY
DSWHKEVLSKFGQMLGSNMTEFHSQISKSRQELEQHSVDTASTSDAVTFITYVQSLKRKIKQFEKQVELYRNGQRLLEKQ
RFQFPPSWLYIDNIEGEWGAFNDIMRRKDSAIQQQVANLQMKIVQEDRAVESRTTDLLTDWEKTKPVTGNLRPEEALQAL
TIYEGKFGRLKDDREKCAKAKEALELTDTGLLSGSEERVQVALEELQDLKGVWSELSKVWEQIDQMKEQPWVSVQPRKLR
QNLDALLNQLKSFPARLRQYASYEFVQRLLKGYMKINMLVIELKSEALKDRHWKQLMKRLHVNWVVSELTLGQIWDVDLQ
KNEAIVKDVLLVAQGEMALEEFLKQIREVWNTYELDLVNYQNKCRLIRGWDDLFNKVKEHINSVSAMKLSPYYKVFEEDA
LSWEDKLNRIMALFDVWIDVQRRWVYLEGIFTGSADIKHLLPVETQRFQSISTEFLALMKKVSKSPLVMDVLNIQGVQRS
LERLADLLGKIQKALGEYLERERSSFPRFYFVGDEDLLEIIGNSKNVAKLQKHFKKMFAGVSSIILNEDNSVVLGISSRE
GEEVMFKTPVSITEHPKINEWLTLVEKEMRVTLAKLLAESVTEVEIFGKATSIDPNTYITWIDKYQAQLVVLSAQIAWSE
NVETALSSMGGGGDAAPLHSVLSNVEVTLNVLADSVLMEQPPLRRRKLEHLITELVHQRDVTRSLIKSKIDNAKSFEWLS
QMRFYFDPKQTDVLQQLSIQMANAKFNYGFEYLGVQDKLVQTPLTDRCYLTMTQALEARLGGSPFGPAGTGKTESVKALG
HQLGRFVLVFNCDETFDFQAMGRIFVGLCQVGAWGCFDEFNRLEERMLSAVSQQVQCIQEALREHSNPNYDKTSAPITCE
LLNKQVKVSPDMAIFITMNPGYAGRSNLPDNLKKLFRSLAMTKPDRQLIAQVMLYSQGFRTAEVLANKIVPFFKLCDEQL
SSQSHYDFGLRALKSVLVSAGNVKRERIQKIKREKEERGEAVDEGEIAENLPEQEILIQSVCETMVPKLVAEDIPLLFSL
LSDVFPGVQYHRGEMTALREELKKVCQEMYLTYGDGEEVGGMWVEKVLQLYQITQINHGLMMVGPSGSGKSMAWRVLLKA
LERLEGVEGVAHIIDPKAISKDHLYGTLDPNTREWTDGLFTHVLRKIIDSVRGELQKRQWIVFDGDVDPEWVENLNSVLD
DNKLLTLPNGERLSLPPNVRIMFEVQDLKYATLATVSRCGMVWFSEDVLSTDMIFNNFLARLRSIPLDEGEDEAQRRRKG
KEDEGEEAASPMLQIQRDAATIMQPYFTSNGLVTKALEHAFQLEHIMDLTRLRCLGSLFSMLHQACRNVAQYNANHPDFP
MQIEQLERYIQRYLVYAILWSLSGDSRLKMRAELGEYIRRITTVPLPTAPNIPIIDYEVSISGEWSPWQAKVPQIEVETH
KVAAPDVVVPTLDTVRHEALLYTWLAEHKPLVLCGPPGSGKTMTLFSALRALPDMEVVGLNFSSATTPELLLKTFDHYCE
YRRTPNGVVLAPVQLGKWLVLFCDEINLPDMDKYGTQRVISFIRQMVEHGGFYRTSDQTWVKLERIQFVGACNPPTDPGR
KPLSHRFLRHVPVVYVDYPGPASLTQIYGTFNRAMLRLIPSLRTYAEPLTAAMVEFYTMSQERFTQDTQPHYIYSPREMT
RWVRGIFEALRPLETLPVEGLIRIWAHEALRLFQDRLVEDEERRWTDENIDTVALKHFPNIDREKAMSRPILYSNWLSKD
YIPVDQEELRDYVKARLKVFYEEELDVPLVLFNEVLDHVLRIDRIFRQPQGHLLLIGVSGAGKTTLSRFVAWMNGLSVYQ
IKVHRKYTGEDFDEDLRTVLRRSGCKNEKIAFIMDESNVLDSGFLERMNTLLANGEVPGLFEGDEYATLMTQCKEGAQKE
GLMLDSHEELYKWFTSQVIRNLHVVFTMNPSSEGLKDRAATSPALFNRCVLNWFGDWSTEALYQVGKEFTSKMDLEKPNY
IVPDYMPVVYDKLPQPPSHREAIVNSCVFVHQTLHQANARLAKRGGRTMAITPRHYLDFINHYANLFHEKRSELEEQQMH
LNVGLRKIKETVDQVEELRRDLRIKSQELEVKNAAANDKLKKMVKDQQEAEKKKVMSQEIQEQLHKQQEVIADKQMSVKE
DLDKVEPAVIEAQNAVKSIKKQHLVEVRSMANPPAAVKLALESICLLLGESTTDWKQIRSIIMRENFIPTIVNFSAEEIS
DAIREKMKKNYMSNPSYNYEIVNRASLACGPMVKWAIAQLNYADMLKRVEPLRNELQKLEDDAKDNQQKANEVEQMIRDL
EASIARYKEEYAVLISEAQAIKADLAAVEAKVNRSTALLKSLSAERERWEKTSETFKNQMSTIAGDCLLSAAFIAYAGYF
DQQMRQNLFTTWSHHLQQANIQFRTDIARTEYLSNADERLRWQASSLPADDLCTENAIMLKRFNRYPLIIDPSGQATEFI
MNEYKDRKITRTSFLDDAFRKNLESALRFGNPLLVQDVESYDPVLNPVLNREVRRTGGRVLITLGDQDIDLSPSFVIFLS
TRDPTVEFPPDLCSRVTFVNFTVTRSSLQSQCLNEVLKAERPDVDEKRSDLLKLQGEFQLRLRQLEKSLLQALNEVKGRI
LDDDTIITTLENLKREAAEVTRKVEETDIVMQEVETVSQQYLPLSTACSSIYFTMESLKQIHFLYQYSLQFFLDIYHNVL
YENPNLKGVTDHTQRLSIITKDLFQVAFNRVARGMLHQDHITFAMLLARIKLKGTVGEPTYDAEFQHFLRGNEIVLSAGS
TPRIQGLTVEQAEAVVRLSCLPAFKDLIAKVQADEQFGIWLDSSSPEQTVPYLWSEETPATPIGQAIHRLLLIQAFRPDR
LLAMAHMFVSTNLGESFMSIMEQPLDLTHIVGTEVKPNTPVLMCSVPGYDASGHVEDLAAEQNTQITSIAIGSAEGFNQA
DKAINTAVKSGRWVMLKNVHLAPGWLMQLEKKLHSLQPHACFRLFLTMEINPKVPVNLLRAGRIFVFEPPPGVKANMLRT
FSSIPVSRICKSPNERARLYFLLAWFHAIIQERLRYAPLGWSKKYEFGESDLRSACDTVDTWLDDTAKGRQNISPDKIPW
SALKTLMAQSIYGGRVDNEFDQRLLNTFLERLFTTRSFDSEFKLACKVDGHKDIQMPDGIRREEFVQWVELLPDTQTPSW
LGLPNNAERVLLTTQGVDMISKMLKMQMLEDEDDLAYAETEKKTRTDSTSDGRPAWMRTLHTTASNWLHLIPQTLSHLKR
TVENIKDPLFRFFEREVKMGAKLLQDVRQDLADVVQVCEGKKKQTNYLRTLINELVKGILPRSWSHYTVPAGMTVIQWVS
DFSERIKQLQNISLAAASGGAKELKNIHVCLGGLFVPEAYITATRQYVAQANSWSLEELCLEVNVTTSQGATLDACSFGV
TGLKLQGATCNNNKLSLSNAISTALPLTQLRWVKQTNTEKKASVVTLPVYLNFTRADLIFTVDFEIATKEDPRSFYERGV
AVLCTE
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 "ADENOSINE-5'-DIPHOSPHATE"  ADP 
3 "ADENOSINE-5'-TRIPHOSPHATE" ATP 
4 'MAGNESIUM ION'             MG  
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1    MET n 
1 2    SER n 
1 3    GLU n 
1 4    PRO n 
1 5    GLY n 
1 6    GLY n 
1 7    GLY n 
1 8    GLY n 
1 9    GLY n 
1 10   GLU n 
1 11   ASP n 
1 12   GLY n 
1 13   SER n 
1 14   ALA n 
1 15   GLY n 
1 16   LEU n 
1 17   GLU n 
1 18   VAL n 
1 19   SER n 
1 20   ALA n 
1 21   VAL n 
1 22   GLN n 
1 23   ASN n 
1 24   VAL n 
1 25   ALA n 
1 26   ASP n 
1 27   VAL n 
1 28   SER n 
1 29   VAL n 
1 30   LEU n 
1 31   GLN n 
1 32   LYS n 
1 33   HIS n 
1 34   LEU n 
1 35   ARG n 
1 36   LYS n 
1 37   LEU n 
1 38   VAL n 
1 39   PRO n 
1 40   LEU n 
1 41   LEU n 
1 42   LEU n 
1 43   GLU n 
1 44   ASP n 
1 45   GLY n 
1 46   GLY n 
1 47   GLU n 
1 48   ALA n 
1 49   PRO n 
1 50   ALA n 
1 51   ALA n 
1 52   LEU n 
1 53   GLU n 
1 54   ALA n 
1 55   ALA n 
1 56   LEU n 
1 57   GLU n 
1 58   GLU n 
1 59   LYS n 
1 60   SER n 
1 61   ALA n 
1 62   LEU n 
1 63   GLU n 
1 64   GLN n 
1 65   MET n 
1 66   ARG n 
1 67   LYS n 
1 68   PHE n 
1 69   LEU n 
1 70   SER n 
1 71   ASP n 
1 72   PRO n 
1 73   GLN n 
1 74   VAL n 
1 75   HIS n 
1 76   THR n 
1 77   VAL n 
1 78   LEU n 
1 79   VAL n 
1 80   GLU n 
1 81   ARG n 
1 82   SER n 
1 83   THR n 
1 84   LEU n 
1 85   LYS n 
1 86   GLU n 
1 87   ASP n 
1 88   VAL n 
1 89   GLY n 
1 90   ASP n 
1 91   GLU n 
1 92   GLY n 
1 93   GLU n 
1 94   GLU n 
1 95   GLU n 
1 96   LYS n 
1 97   GLU n 
1 98   PHE n 
1 99   ILE n 
1 100  SER n 
1 101  TYR n 
1 102  ASN n 
1 103  ILE n 
1 104  ASN n 
1 105  ILE n 
1 106  ASP n 
1 107  ILE n 
1 108  HIS n 
1 109  TYR n 
1 110  GLY n 
1 111  VAL n 
1 112  LYS n 
1 113  SER n 
1 114  ASN n 
1 115  SER n 
1 116  LEU n 
1 117  ALA n 
1 118  PHE n 
1 119  ILE n 
1 120  LYS n 
1 121  ARG n 
1 122  THR n 
1 123  PRO n 
1 124  VAL n 
1 125  ILE n 
1 126  ASP n 
1 127  ALA n 
1 128  ASP n 
1 129  LYS n 
1 130  PRO n 
1 131  VAL n 
1 132  SER n 
1 133  SER n 
1 134  GLN n 
1 135  LEU n 
1 136  ARG n 
1 137  VAL n 
1 138  LEU n 
1 139  THR n 
1 140  LEU n 
1 141  SER n 
1 142  GLU n 
1 143  ASP n 
1 144  SER n 
1 145  PRO n 
1 146  TYR n 
1 147  GLU n 
1 148  THR n 
1 149  LEU n 
1 150  HIS n 
1 151  SER n 
1 152  PHE n 
1 153  ILE n 
1 154  SER n 
1 155  ASN n 
1 156  ALA n 
1 157  VAL n 
1 158  ALA n 
1 159  PRO n 
1 160  PHE n 
1 161  PHE n 
1 162  LYS n 
1 163  SER n 
1 164  TYR n 
1 165  ILE n 
1 166  ARG n 
1 167  GLU n 
1 168  SER n 
1 169  GLY n 
1 170  LYS n 
1 171  ALA n 
1 172  ASP n 
1 173  ARG n 
1 174  ASP n 
1 175  GLY n 
1 176  ASP n 
1 177  LYS n 
1 178  MET n 
1 179  ALA n 
1 180  PRO n 
1 181  SER n 
1 182  VAL n 
1 183  GLU n 
1 184  LYS n 
1 185  LYS n 
1 186  ILE n 
1 187  ALA n 
1 188  GLU n 
1 189  LEU n 
1 190  GLU n 
1 191  MET n 
1 192  GLY n 
1 193  LEU n 
1 194  LEU n 
1 195  HIS n 
1 196  LEU n 
1 197  GLN n 
1 198  GLN n 
1 199  ASN n 
1 200  ILE n 
1 201  GLU n 
1 202  ILE n 
1 203  PRO n 
1 204  GLU n 
1 205  ILE n 
1 206  SER n 
1 207  LEU n 
1 208  PRO n 
1 209  ILE n 
1 210  HIS n 
1 211  PRO n 
1 212  MET n 
1 213  ILE n 
1 214  THR n 
1 215  ASN n 
1 216  VAL n 
1 217  ALA n 
1 218  LYS n 
1 219  GLN n 
1 220  CYS n 
1 221  TYR n 
1 222  GLU n 
1 223  ARG n 
1 224  GLY n 
1 225  GLU n 
1 226  LYS n 
1 227  PRO n 
1 228  LYS n 
1 229  VAL n 
1 230  THR n 
1 231  ASP n 
1 232  PHE n 
1 233  GLY n 
1 234  ASP n 
1 235  LYS n 
1 236  VAL n 
1 237  GLU n 
1 238  ASP n 
1 239  PRO n 
1 240  THR n 
1 241  PHE n 
1 242  LEU n 
1 243  ASN n 
1 244  GLN n 
1 245  LEU n 
1 246  GLN n 
1 247  SER n 
1 248  GLY n 
1 249  VAL n 
1 250  ASN n 
1 251  ARG n 
1 252  TRP n 
1 253  ILE n 
1 254  ARG n 
1 255  GLU n 
1 256  ILE n 
1 257  GLN n 
1 258  LYS n 
1 259  VAL n 
1 260  THR n 
1 261  LYS n 
1 262  LEU n 
1 263  ASP n 
1 264  ARG n 
1 265  ASP n 
1 266  PRO n 
1 267  ALA n 
1 268  SER n 
1 269  GLY n 
1 270  THR n 
1 271  ALA n 
1 272  LEU n 
1 273  GLN n 
1 274  GLU n 
1 275  ILE n 
1 276  SER n 
1 277  PHE n 
1 278  TRP n 
1 279  LEU n 
1 280  ASN n 
1 281  LEU n 
1 282  GLU n 
1 283  ARG n 
1 284  ALA n 
1 285  LEU n 
1 286  TYR n 
1 287  ARG n 
1 288  ILE n 
1 289  GLN n 
1 290  GLU n 
1 291  LYS n 
1 292  ARG n 
1 293  GLU n 
1 294  SER n 
1 295  PRO n 
1 296  GLU n 
1 297  VAL n 
1 298  LEU n 
1 299  LEU n 
1 300  THR n 
1 301  LEU n 
1 302  ASP n 
1 303  ILE n 
1 304  LEU n 
1 305  LYS n 
1 306  HIS n 
1 307  GLY n 
1 308  LYS n 
1 309  ARG n 
1 310  PHE n 
1 311  HIS n 
1 312  ALA n 
1 313  THR n 
1 314  VAL n 
1 315  SER n 
1 316  PHE n 
1 317  ASP n 
1 318  THR n 
1 319  ASP n 
1 320  THR n 
1 321  GLY n 
1 322  LEU n 
1 323  LYS n 
1 324  GLN n 
1 325  ALA n 
1 326  LEU n 
1 327  GLU n 
1 328  THR n 
1 329  VAL n 
1 330  ASN n 
1 331  ASP n 
1 332  TYR n 
1 333  ASN n 
1 334  PRO n 
1 335  LEU n 
1 336  MET n 
1 337  LYS n 
1 338  ASP n 
1 339  PHE n 
1 340  PRO n 
1 341  LEU n 
1 342  ASN n 
1 343  ASP n 
1 344  LEU n 
1 345  LEU n 
1 346  SER n 
1 347  ALA n 
1 348  THR n 
1 349  GLU n 
1 350  LEU n 
1 351  ASP n 
1 352  LYS n 
1 353  ILE n 
1 354  ARG n 
1 355  GLN n 
1 356  ALA n 
1 357  LEU n 
1 358  VAL n 
1 359  ALA n 
1 360  ILE n 
1 361  PHE n 
1 362  THR n 
1 363  HIS n 
1 364  LEU n 
1 365  ARG n 
1 366  LYS n 
1 367  ILE n 
1 368  ARG n 
1 369  ASN n 
1 370  THR n 
1 371  LYS n 
1 372  TYR n 
1 373  PRO n 
1 374  ILE n 
1 375  GLN n 
1 376  ARG n 
1 377  ALA n 
1 378  LEU n 
1 379  ARG n 
1 380  LEU n 
1 381  VAL n 
1 382  GLU n 
1 383  ALA n 
1 384  ILE n 
1 385  SER n 
1 386  ARG n 
1 387  ASP n 
1 388  LEU n 
1 389  SER n 
1 390  SER n 
1 391  GLN n 
1 392  LEU n 
1 393  LEU n 
1 394  LYS n 
1 395  VAL n 
1 396  LEU n 
1 397  GLY n 
1 398  THR n 
1 399  ARG n 
1 400  LYS n 
1 401  LEU n 
1 402  MET n 
1 403  HIS n 
1 404  VAL n 
1 405  ALA n 
1 406  TYR n 
1 407  GLU n 
1 408  GLU n 
1 409  PHE n 
1 410  GLU n 
1 411  LYS n 
1 412  VAL n 
1 413  MET n 
1 414  VAL n 
1 415  ALA n 
1 416  CYS n 
1 417  PHE n 
1 418  GLU n 
1 419  VAL n 
1 420  PHE n 
1 421  GLN n 
1 422  THR n 
1 423  TRP n 
1 424  ASP n 
1 425  ASP n 
1 426  GLU n 
1 427  TYR n 
1 428  GLU n 
1 429  LYS n 
1 430  LEU n 
1 431  GLN n 
1 432  VAL n 
1 433  LEU n 
1 434  LEU n 
1 435  ARG n 
1 436  ASP n 
1 437  ILE n 
1 438  VAL n 
1 439  LYS n 
1 440  ARG n 
1 441  LYS n 
1 442  ARG n 
1 443  GLU n 
1 444  GLU n 
1 445  ASN n 
1 446  LEU n 
1 447  LYS n 
1 448  MET n 
1 449  VAL n 
1 450  TRP n 
1 451  ARG n 
1 452  ILE n 
1 453  ASN n 
1 454  PRO n 
1 455  ALA n 
1 456  HIS n 
1 457  ARG n 
1 458  LYS n 
1 459  LEU n 
1 460  GLN n 
1 461  ALA n 
1 462  ARG n 
1 463  LEU n 
1 464  ASP n 
1 465  GLN n 
1 466  MET n 
1 467  ARG n 
1 468  LYS n 
1 469  PHE n 
1 470  ARG n 
1 471  ARG n 
1 472  GLN n 
1 473  HIS n 
1 474  GLU n 
1 475  GLN n 
1 476  LEU n 
1 477  ARG n 
1 478  ALA n 
1 479  VAL n 
1 480  ILE n 
1 481  VAL n 
1 482  ARG n 
1 483  VAL n 
1 484  LEU n 
1 485  ARG n 
1 486  PRO n 
1 487  GLN n 
1 488  VAL n 
1 489  THR n 
1 490  ALA n 
1 491  VAL n 
1 492  ALA n 
1 493  GLN n 
1 494  GLN n 
1 495  ASN n 
1 496  GLN n 
1 497  GLY n 
1 498  GLU n 
1 499  VAL n 
1 500  PRO n 
1 501  GLU n 
1 502  PRO n 
1 503  GLN n 
1 504  ASP n 
1 505  MET n 
1 506  LYS n 
1 507  VAL n 
1 508  ALA n 
1 509  GLU n 
1 510  VAL n 
1 511  LEU n 
1 512  PHE n 
1 513  ASP n 
1 514  ALA n 
1 515  ALA n 
1 516  ASP n 
1 517  ALA n 
1 518  ASN n 
1 519  ALA n 
1 520  ILE n 
1 521  GLU n 
1 522  GLU n 
1 523  VAL n 
1 524  ASN n 
1 525  LEU n 
1 526  ALA n 
1 527  TYR n 
1 528  GLU n 
1 529  ASN n 
1 530  VAL n 
1 531  LYS n 
1 532  GLU n 
1 533  VAL n 
1 534  ASP n 
1 535  GLY n 
1 536  LEU n 
1 537  ASP n 
1 538  VAL n 
1 539  SER n 
1 540  LYS n 
1 541  GLU n 
1 542  GLY n 
1 543  THR n 
1 544  GLU n 
1 545  ALA n 
1 546  TRP n 
1 547  GLU n 
1 548  ALA n 
1 549  ALA n 
1 550  MET n 
1 551  LYS n 
1 552  ARG n 
1 553  TYR n 
1 554  ASP n 
1 555  GLU n 
1 556  ARG n 
1 557  ILE n 
1 558  ASP n 
1 559  ARG n 
1 560  VAL n 
1 561  GLU n 
1 562  THR n 
1 563  ARG n 
1 564  ILE n 
1 565  THR n 
1 566  ALA n 
1 567  ARG n 
1 568  LEU n 
1 569  ARG n 
1 570  ASP n 
1 571  GLN n 
1 572  LEU n 
1 573  GLY n 
1 574  THR n 
1 575  ALA n 
1 576  LYS n 
1 577  ASN n 
1 578  ALA n 
1 579  ASN n 
1 580  GLU n 
1 581  MET n 
1 582  PHE n 
1 583  ARG n 
1 584  ILE n 
1 585  PHE n 
1 586  SER n 
1 587  ARG n 
1 588  PHE n 
1 589  ASN n 
1 590  ALA n 
1 591  LEU n 
1 592  PHE n 
1 593  VAL n 
1 594  ARG n 
1 595  PRO n 
1 596  HIS n 
1 597  ILE n 
1 598  ARG n 
1 599  GLY n 
1 600  ALA n 
1 601  ILE n 
1 602  ARG n 
1 603  GLU n 
1 604  TYR n 
1 605  GLN n 
1 606  THR n 
1 607  GLN n 
1 608  LEU n 
1 609  ILE n 
1 610  GLN n 
1 611  ARG n 
1 612  VAL n 
1 613  LYS n 
1 614  ASP n 
1 615  ASP n 
1 616  ILE n 
1 617  GLU n 
1 618  SER n 
1 619  LEU n 
1 620  HIS n 
1 621  ASP n 
1 622  LYS n 
1 623  PHE n 
1 624  LYS n 
1 625  VAL n 
1 626  GLN n 
1 627  TYR n 
1 628  PRO n 
1 629  GLN n 
1 630  SER n 
1 631  GLN n 
1 632  ALA n 
1 633  CYS n 
1 634  LYS n 
1 635  MET n 
1 636  SER n 
1 637  HIS n 
1 638  VAL n 
1 639  ARG n 
1 640  ASP n 
1 641  LEU n 
1 642  PRO n 
1 643  PRO n 
1 644  VAL n 
1 645  SER n 
1 646  GLY n 
1 647  SER n 
1 648  ILE n 
1 649  ILE n 
1 650  TRP n 
1 651  ALA n 
1 652  LYS n 
1 653  GLN n 
1 654  ILE n 
1 655  ASP n 
1 656  ARG n 
1 657  GLN n 
1 658  LEU n 
1 659  THR n 
1 660  ALA n 
1 661  TYR n 
1 662  MET n 
1 663  LYS n 
1 664  ARG n 
1 665  VAL n 
1 666  GLU n 
1 667  ASP n 
1 668  VAL n 
1 669  LEU n 
1 670  GLY n 
1 671  LYS n 
1 672  GLY n 
1 673  TRP n 
1 674  GLU n 
1 675  ASN n 
1 676  HIS n 
1 677  VAL n 
1 678  GLU n 
1 679  GLY n 
1 680  GLN n 
1 681  LYS n 
1 682  LEU n 
1 683  LYS n 
1 684  GLN n 
1 685  ASP n 
1 686  GLY n 
1 687  ASP n 
1 688  SER n 
1 689  PHE n 
1 690  ARG n 
1 691  MET n 
1 692  LYS n 
1 693  LEU n 
1 694  ASN n 
1 695  THR n 
1 696  GLN n 
1 697  GLU n 
1 698  ILE n 
1 699  PHE n 
1 700  ASP n 
1 701  ASP n 
1 702  TRP n 
1 703  ALA n 
1 704  ARG n 
1 705  LYS n 
1 706  VAL n 
1 707  GLN n 
1 708  GLN n 
1 709  ARG n 
1 710  ASN n 
1 711  LEU n 
1 712  GLY n 
1 713  VAL n 
1 714  SER n 
1 715  GLY n 
1 716  ARG n 
1 717  ILE n 
1 718  PHE n 
1 719  THR n 
1 720  ILE n 
1 721  GLU n 
1 722  SER n 
1 723  THR n 
1 724  ARG n 
1 725  VAL n 
1 726  ARG n 
1 727  GLY n 
1 728  ARG n 
1 729  THR n 
1 730  GLY n 
1 731  ASN n 
1 732  VAL n 
1 733  LEU n 
1 734  LYS n 
1 735  LEU n 
1 736  LYS n 
1 737  VAL n 
1 738  ASN n 
1 739  PHE n 
1 740  LEU n 
1 741  PRO n 
1 742  GLU n 
1 743  ILE n 
1 744  ILE n 
1 745  THR n 
1 746  LEU n 
1 747  SER n 
1 748  LYS n 
1 749  GLU n 
1 750  VAL n 
1 751  ARG n 
1 752  ASN n 
1 753  LEU n 
1 754  LYS n 
1 755  TRP n 
1 756  LEU n 
1 757  GLY n 
1 758  PHE n 
1 759  ARG n 
1 760  VAL n 
1 761  PRO n 
1 762  LEU n 
1 763  ALA n 
1 764  ILE n 
1 765  VAL n 
1 766  ASN n 
1 767  LYS n 
1 768  ALA n 
1 769  HIS n 
1 770  GLN n 
1 771  ALA n 
1 772  ASN n 
1 773  GLN n 
1 774  LEU n 
1 775  TYR n 
1 776  PRO n 
1 777  PHE n 
1 778  ALA n 
1 779  ILE n 
1 780  SER n 
1 781  LEU n 
1 782  ILE n 
1 783  GLU n 
1 784  SER n 
1 785  VAL n 
1 786  ARG n 
1 787  THR n 
1 788  TYR n 
1 789  GLU n 
1 790  ARG n 
1 791  THR n 
1 792  CYS n 
1 793  GLU n 
1 794  LYS n 
1 795  VAL n 
1 796  GLU n 
1 797  GLU n 
1 798  ARG n 
1 799  ASN n 
1 800  THR n 
1 801  ILE n 
1 802  SER n 
1 803  LEU n 
1 804  LEU n 
1 805  VAL n 
1 806  ALA n 
1 807  GLY n 
1 808  LEU n 
1 809  LYS n 
1 810  LYS n 
1 811  GLU n 
1 812  VAL n 
1 813  GLN n 
1 814  ALA n 
1 815  LEU n 
1 816  ILE n 
1 817  ALA n 
1 818  GLU n 
1 819  GLY n 
1 820  ILE n 
1 821  ALA n 
1 822  LEU n 
1 823  VAL n 
1 824  TRP n 
1 825  GLU n 
1 826  SER n 
1 827  TYR n 
1 828  LYS n 
1 829  LEU n 
1 830  ASP n 
1 831  PRO n 
1 832  TYR n 
1 833  VAL n 
1 834  GLN n 
1 835  ARG n 
1 836  LEU n 
1 837  ALA n 
1 838  GLU n 
1 839  THR n 
1 840  VAL n 
1 841  PHE n 
1 842  ASN n 
1 843  PHE n 
1 844  GLN n 
1 845  GLU n 
1 846  LYS n 
1 847  VAL n 
1 848  ASP n 
1 849  ASP n 
1 850  LEU n 
1 851  LEU n 
1 852  ILE n 
1 853  ILE n 
1 854  GLU n 
1 855  GLU n 
1 856  LYS n 
1 857  ILE n 
1 858  ASP n 
1 859  LEU n 
1 860  GLU n 
1 861  VAL n 
1 862  ARG n 
1 863  SER n 
1 864  LEU n 
1 865  GLU n 
1 866  THR n 
1 867  CYS n 
1 868  MET n 
1 869  TYR n 
1 870  ASP n 
1 871  HIS n 
1 872  LYS n 
1 873  THR n 
1 874  PHE n 
1 875  SER n 
1 876  GLU n 
1 877  ILE n 
1 878  LEU n 
1 879  ASN n 
1 880  ARG n 
1 881  VAL n 
1 882  GLN n 
1 883  LYS n 
1 884  ALA n 
1 885  VAL n 
1 886  ASP n 
1 887  ASP n 
1 888  LEU n 
1 889  ASN n 
1 890  LEU n 
1 891  HIS n 
1 892  SER n 
1 893  TYR n 
1 894  SER n 
1 895  ASN n 
1 896  LEU n 
1 897  PRO n 
1 898  ILE n 
1 899  TRP n 
1 900  VAL n 
1 901  ASN n 
1 902  LYS n 
1 903  LEU n 
1 904  ASP n 
1 905  MET n 
1 906  GLU n 
1 907  ILE n 
1 908  GLU n 
1 909  ARG n 
1 910  ILE n 
1 911  LEU n 
1 912  GLY n 
1 913  VAL n 
1 914  ARG n 
1 915  LEU n 
1 916  GLN n 
1 917  ALA n 
1 918  GLY n 
1 919  LEU n 
1 920  ARG n 
1 921  ALA n 
1 922  TRP n 
1 923  THR n 
1 924  GLN n 
1 925  VAL n 
1 926  LEU n 
1 927  LEU n 
1 928  GLY n 
1 929  GLN n 
1 930  ALA n 
1 931  GLU n 
1 932  ASP n 
1 933  LYS n 
1 934  ALA n 
1 935  GLU n 
1 936  VAL n 
1 937  ASP n 
1 938  MET n 
1 939  ASP n 
1 940  THR n 
1 941  ASP n 
1 942  ALA n 
1 943  PRO n 
1 944  GLN n 
1 945  VAL n 
1 946  SER n 
1 947  HIS n 
1 948  LYS n 
1 949  PRO n 
1 950  GLY n 
1 951  GLY n 
1 952  GLU n 
1 953  PRO n 
1 954  LYS n 
1 955  ILE n 
1 956  LYS n 
1 957  ASN n 
1 958  VAL n 
1 959  VAL n 
1 960  HIS n 
1 961  GLU n 
1 962  LEU n 
1 963  ARG n 
1 964  ILE n 
1 965  THR n 
1 966  ASN n 
1 967  GLN n 
1 968  VAL n 
1 969  ILE n 
1 970  TYR n 
1 971  LEU n 
1 972  ASN n 
1 973  PRO n 
1 974  PRO n 
1 975  ILE n 
1 976  GLU n 
1 977  GLU n 
1 978  CYS n 
1 979  ARG n 
1 980  TYR n 
1 981  LYS n 
1 982  LEU n 
1 983  TYR n 
1 984  GLN n 
1 985  GLU n 
1 986  MET n 
1 987  PHE n 
1 988  ALA n 
1 989  TRP n 
1 990  LYS n 
1 991  MET n 
1 992  VAL n 
1 993  VAL n 
1 994  LEU n 
1 995  SER n 
1 996  LEU n 
1 997  PRO n 
1 998  ARG n 
1 999  ILE n 
1 1000 GLN n 
1 1001 SER n 
1 1002 GLN n 
1 1003 ARG n 
1 1004 TYR n 
1 1005 GLN n 
1 1006 VAL n 
1 1007 GLY n 
1 1008 VAL n 
1 1009 HIS n 
1 1010 TYR n 
1 1011 GLU n 
1 1012 LEU n 
1 1013 THR n 
1 1014 GLU n 
1 1015 GLU n 
1 1016 GLU n 
1 1017 LYS n 
1 1018 PHE n 
1 1019 TYR n 
1 1020 ARG n 
1 1021 ASN n 
1 1022 ALA n 
1 1023 LEU n 
1 1024 THR n 
1 1025 ARG n 
1 1026 MET n 
1 1027 PRO n 
1 1028 ASP n 
1 1029 GLY n 
1 1030 PRO n 
1 1031 VAL n 
1 1032 ALA n 
1 1033 LEU n 
1 1034 GLU n 
1 1035 GLU n 
1 1036 SER n 
1 1037 TYR n 
1 1038 SER n 
1 1039 ALA n 
1 1040 VAL n 
1 1041 MET n 
1 1042 GLY n 
1 1043 ILE n 
1 1044 VAL n 
1 1045 SER n 
1 1046 GLU n 
1 1047 VAL n 
1 1048 GLU n 
1 1049 GLN n 
1 1050 TYR n 
1 1051 VAL n 
1 1052 LYS n 
1 1053 VAL n 
1 1054 TRP n 
1 1055 LEU n 
1 1056 GLN n 
1 1057 TYR n 
1 1058 GLN n 
1 1059 CYS n 
1 1060 LEU n 
1 1061 TRP n 
1 1062 ASP n 
1 1063 MET n 
1 1064 GLN n 
1 1065 ALA n 
1 1066 GLU n 
1 1067 ASN n 
1 1068 ILE n 
1 1069 TYR n 
1 1070 ASN n 
1 1071 ARG n 
1 1072 LEU n 
1 1073 GLY n 
1 1074 GLU n 
1 1075 ASP n 
1 1076 LEU n 
1 1077 ASN n 
1 1078 LYS n 
1 1079 TRP n 
1 1080 GLN n 
1 1081 ALA n 
1 1082 LEU n 
1 1083 LEU n 
1 1084 VAL n 
1 1085 GLN n 
1 1086 ILE n 
1 1087 ARG n 
1 1088 LYS n 
1 1089 ALA n 
1 1090 ARG n 
1 1091 GLY n 
1 1092 THR n 
1 1093 PHE n 
1 1094 ASP n 
1 1095 ASN n 
1 1096 ALA n 
1 1097 GLU n 
1 1098 THR n 
1 1099 LYS n 
1 1100 LYS n 
1 1101 GLU n 
1 1102 PHE n 
1 1103 GLY n 
1 1104 PRO n 
1 1105 VAL n 
1 1106 VAL n 
1 1107 ILE n 
1 1108 ASP n 
1 1109 TYR n 
1 1110 GLY n 
1 1111 LYS n 
1 1112 VAL n 
1 1113 GLN n 
1 1114 SER n 
1 1115 LYS n 
1 1116 VAL n 
1 1117 ASN n 
1 1118 LEU n 
1 1119 LYS n 
1 1120 TYR n 
1 1121 ASP n 
1 1122 SER n 
1 1123 TRP n 
1 1124 HIS n 
1 1125 LYS n 
1 1126 GLU n 
1 1127 VAL n 
1 1128 LEU n 
1 1129 SER n 
1 1130 LYS n 
1 1131 PHE n 
1 1132 GLY n 
1 1133 GLN n 
1 1134 MET n 
1 1135 LEU n 
1 1136 GLY n 
1 1137 SER n 
1 1138 ASN n 
1 1139 MET n 
1 1140 THR n 
1 1141 GLU n 
1 1142 PHE n 
1 1143 HIS n 
1 1144 SER n 
1 1145 GLN n 
1 1146 ILE n 
1 1147 SER n 
1 1148 LYS n 
1 1149 SER n 
1 1150 ARG n 
1 1151 GLN n 
1 1152 GLU n 
1 1153 LEU n 
1 1154 GLU n 
1 1155 GLN n 
1 1156 HIS n 
1 1157 SER n 
1 1158 VAL n 
1 1159 ASP n 
1 1160 THR n 
1 1161 ALA n 
1 1162 SER n 
1 1163 THR n 
1 1164 SER n 
1 1165 ASP n 
1 1166 ALA n 
1 1167 VAL n 
1 1168 THR n 
1 1169 PHE n 
1 1170 ILE n 
1 1171 THR n 
1 1172 TYR n 
1 1173 VAL n 
1 1174 GLN n 
1 1175 SER n 
1 1176 LEU n 
1 1177 LYS n 
1 1178 ARG n 
1 1179 LYS n 
1 1180 ILE n 
1 1181 LYS n 
1 1182 GLN n 
1 1183 PHE n 
1 1184 GLU n 
1 1185 LYS n 
1 1186 GLN n 
1 1187 VAL n 
1 1188 GLU n 
1 1189 LEU n 
1 1190 TYR n 
1 1191 ARG n 
1 1192 ASN n 
1 1193 GLY n 
1 1194 GLN n 
1 1195 ARG n 
1 1196 LEU n 
1 1197 LEU n 
1 1198 GLU n 
1 1199 LYS n 
1 1200 GLN n 
1 1201 ARG n 
1 1202 PHE n 
1 1203 GLN n 
1 1204 PHE n 
1 1205 PRO n 
1 1206 PRO n 
1 1207 SER n 
1 1208 TRP n 
1 1209 LEU n 
1 1210 TYR n 
1 1211 ILE n 
1 1212 ASP n 
1 1213 ASN n 
1 1214 ILE n 
1 1215 GLU n 
1 1216 GLY n 
1 1217 GLU n 
1 1218 TRP n 
1 1219 GLY n 
1 1220 ALA n 
1 1221 PHE n 
1 1222 ASN n 
1 1223 ASP n 
1 1224 ILE n 
1 1225 MET n 
1 1226 ARG n 
1 1227 ARG n 
1 1228 LYS n 
1 1229 ASP n 
1 1230 SER n 
1 1231 ALA n 
1 1232 ILE n 
1 1233 GLN n 
1 1234 GLN n 
1 1235 GLN n 
1 1236 VAL n 
1 1237 ALA n 
1 1238 ASN n 
1 1239 LEU n 
1 1240 GLN n 
1 1241 MET n 
1 1242 LYS n 
1 1243 ILE n 
1 1244 VAL n 
1 1245 GLN n 
1 1246 GLU n 
1 1247 ASP n 
1 1248 ARG n 
1 1249 ALA n 
1 1250 VAL n 
1 1251 GLU n 
1 1252 SER n 
1 1253 ARG n 
1 1254 THR n 
1 1255 THR n 
1 1256 ASP n 
1 1257 LEU n 
1 1258 LEU n 
1 1259 THR n 
1 1260 ASP n 
1 1261 TRP n 
1 1262 GLU n 
1 1263 LYS n 
1 1264 THR n 
1 1265 LYS n 
1 1266 PRO n 
1 1267 VAL n 
1 1268 THR n 
1 1269 GLY n 
1 1270 ASN n 
1 1271 LEU n 
1 1272 ARG n 
1 1273 PRO n 
1 1274 GLU n 
1 1275 GLU n 
1 1276 ALA n 
1 1277 LEU n 
1 1278 GLN n 
1 1279 ALA n 
1 1280 LEU n 
1 1281 THR n 
1 1282 ILE n 
1 1283 TYR n 
1 1284 GLU n 
1 1285 GLY n 
1 1286 LYS n 
1 1287 PHE n 
1 1288 GLY n 
1 1289 ARG n 
1 1290 LEU n 
1 1291 LYS n 
1 1292 ASP n 
1 1293 ASP n 
1 1294 ARG n 
1 1295 GLU n 
1 1296 LYS n 
1 1297 CYS n 
1 1298 ALA n 
1 1299 LYS n 
1 1300 ALA n 
1 1301 LYS n 
1 1302 GLU n 
1 1303 ALA n 
1 1304 LEU n 
1 1305 GLU n 
1 1306 LEU n 
1 1307 THR n 
1 1308 ASP n 
1 1309 THR n 
1 1310 GLY n 
1 1311 LEU n 
1 1312 LEU n 
1 1313 SER n 
1 1314 GLY n 
1 1315 SER n 
1 1316 GLU n 
1 1317 GLU n 
1 1318 ARG n 
1 1319 VAL n 
1 1320 GLN n 
1 1321 VAL n 
1 1322 ALA n 
1 1323 LEU n 
1 1324 GLU n 
1 1325 GLU n 
1 1326 LEU n 
1 1327 GLN n 
1 1328 ASP n 
1 1329 LEU n 
1 1330 LYS n 
1 1331 GLY n 
1 1332 VAL n 
1 1333 TRP n 
1 1334 SER n 
1 1335 GLU n 
1 1336 LEU n 
1 1337 SER n 
1 1338 LYS n 
1 1339 VAL n 
1 1340 TRP n 
1 1341 GLU n 
1 1342 GLN n 
1 1343 ILE n 
1 1344 ASP n 
1 1345 GLN n 
1 1346 MET n 
1 1347 LYS n 
1 1348 GLU n 
1 1349 GLN n 
1 1350 PRO n 
1 1351 TRP n 
1 1352 VAL n 
1 1353 SER n 
1 1354 VAL n 
1 1355 GLN n 
1 1356 PRO n 
1 1357 ARG n 
1 1358 LYS n 
1 1359 LEU n 
1 1360 ARG n 
1 1361 GLN n 
1 1362 ASN n 
1 1363 LEU n 
1 1364 ASP n 
1 1365 ALA n 
1 1366 LEU n 
1 1367 LEU n 
1 1368 ASN n 
1 1369 GLN n 
1 1370 LEU n 
1 1371 LYS n 
1 1372 SER n 
1 1373 PHE n 
1 1374 PRO n 
1 1375 ALA n 
1 1376 ARG n 
1 1377 LEU n 
1 1378 ARG n 
1 1379 GLN n 
1 1380 TYR n 
1 1381 ALA n 
1 1382 SER n 
1 1383 TYR n 
1 1384 GLU n 
1 1385 PHE n 
1 1386 VAL n 
1 1387 GLN n 
1 1388 ARG n 
1 1389 LEU n 
1 1390 LEU n 
1 1391 LYS n 
1 1392 GLY n 
1 1393 TYR n 
1 1394 MET n 
1 1395 LYS n 
1 1396 ILE n 
1 1397 ASN n 
1 1398 MET n 
1 1399 LEU n 
1 1400 VAL n 
1 1401 ILE n 
1 1402 GLU n 
1 1403 LEU n 
1 1404 LYS n 
1 1405 SER n 
1 1406 GLU n 
1 1407 ALA n 
1 1408 LEU n 
1 1409 LYS n 
1 1410 ASP n 
1 1411 ARG n 
1 1412 HIS n 
1 1413 TRP n 
1 1414 LYS n 
1 1415 GLN n 
1 1416 LEU n 
1 1417 MET n 
1 1418 LYS n 
1 1419 ARG n 
1 1420 LEU n 
1 1421 HIS n 
1 1422 VAL n 
1 1423 ASN n 
1 1424 TRP n 
1 1425 VAL n 
1 1426 VAL n 
1 1427 SER n 
1 1428 GLU n 
1 1429 LEU n 
1 1430 THR n 
1 1431 LEU n 
1 1432 GLY n 
1 1433 GLN n 
1 1434 ILE n 
1 1435 TRP n 
1 1436 ASP n 
1 1437 VAL n 
1 1438 ASP n 
1 1439 LEU n 
1 1440 GLN n 
1 1441 LYS n 
1 1442 ASN n 
1 1443 GLU n 
1 1444 ALA n 
1 1445 ILE n 
1 1446 VAL n 
1 1447 LYS n 
1 1448 ASP n 
1 1449 VAL n 
1 1450 LEU n 
1 1451 LEU n 
1 1452 VAL n 
1 1453 ALA n 
1 1454 GLN n 
1 1455 GLY n 
1 1456 GLU n 
1 1457 MET n 
1 1458 ALA n 
1 1459 LEU n 
1 1460 GLU n 
1 1461 GLU n 
1 1462 PHE n 
1 1463 LEU n 
1 1464 LYS n 
1 1465 GLN n 
1 1466 ILE n 
1 1467 ARG n 
1 1468 GLU n 
1 1469 VAL n 
1 1470 TRP n 
1 1471 ASN n 
1 1472 THR n 
1 1473 TYR n 
1 1474 GLU n 
1 1475 LEU n 
1 1476 ASP n 
1 1477 LEU n 
1 1478 VAL n 
1 1479 ASN n 
1 1480 TYR n 
1 1481 GLN n 
1 1482 ASN n 
1 1483 LYS n 
1 1484 CYS n 
1 1485 ARG n 
1 1486 LEU n 
1 1487 ILE n 
1 1488 ARG n 
1 1489 GLY n 
1 1490 TRP n 
1 1491 ASP n 
1 1492 ASP n 
1 1493 LEU n 
1 1494 PHE n 
1 1495 ASN n 
1 1496 LYS n 
1 1497 VAL n 
1 1498 LYS n 
1 1499 GLU n 
1 1500 HIS n 
1 1501 ILE n 
1 1502 ASN n 
1 1503 SER n 
1 1504 VAL n 
1 1505 SER n 
1 1506 ALA n 
1 1507 MET n 
1 1508 LYS n 
1 1509 LEU n 
1 1510 SER n 
1 1511 PRO n 
1 1512 TYR n 
1 1513 TYR n 
1 1514 LYS n 
1 1515 VAL n 
1 1516 PHE n 
1 1517 GLU n 
1 1518 GLU n 
1 1519 ASP n 
1 1520 ALA n 
1 1521 LEU n 
1 1522 SER n 
1 1523 TRP n 
1 1524 GLU n 
1 1525 ASP n 
1 1526 LYS n 
1 1527 LEU n 
1 1528 ASN n 
1 1529 ARG n 
1 1530 ILE n 
1 1531 MET n 
1 1532 ALA n 
1 1533 LEU n 
1 1534 PHE n 
1 1535 ASP n 
1 1536 VAL n 
1 1537 TRP n 
1 1538 ILE n 
1 1539 ASP n 
1 1540 VAL n 
1 1541 GLN n 
1 1542 ARG n 
1 1543 ARG n 
1 1544 TRP n 
1 1545 VAL n 
1 1546 TYR n 
1 1547 LEU n 
1 1548 GLU n 
1 1549 GLY n 
1 1550 ILE n 
1 1551 PHE n 
1 1552 THR n 
1 1553 GLY n 
1 1554 SER n 
1 1555 ALA n 
1 1556 ASP n 
1 1557 ILE n 
1 1558 LYS n 
1 1559 HIS n 
1 1560 LEU n 
1 1561 LEU n 
1 1562 PRO n 
1 1563 VAL n 
1 1564 GLU n 
1 1565 THR n 
1 1566 GLN n 
1 1567 ARG n 
1 1568 PHE n 
1 1569 GLN n 
1 1570 SER n 
1 1571 ILE n 
1 1572 SER n 
1 1573 THR n 
1 1574 GLU n 
1 1575 PHE n 
1 1576 LEU n 
1 1577 ALA n 
1 1578 LEU n 
1 1579 MET n 
1 1580 LYS n 
1 1581 LYS n 
1 1582 VAL n 
1 1583 SER n 
1 1584 LYS n 
1 1585 SER n 
1 1586 PRO n 
1 1587 LEU n 
1 1588 VAL n 
1 1589 MET n 
1 1590 ASP n 
1 1591 VAL n 
1 1592 LEU n 
1 1593 ASN n 
1 1594 ILE n 
1 1595 GLN n 
1 1596 GLY n 
1 1597 VAL n 
1 1598 GLN n 
1 1599 ARG n 
1 1600 SER n 
1 1601 LEU n 
1 1602 GLU n 
1 1603 ARG n 
1 1604 LEU n 
1 1605 ALA n 
1 1606 ASP n 
1 1607 LEU n 
1 1608 LEU n 
1 1609 GLY n 
1 1610 LYS n 
1 1611 ILE n 
1 1612 GLN n 
1 1613 LYS n 
1 1614 ALA n 
1 1615 LEU n 
1 1616 GLY n 
1 1617 GLU n 
1 1618 TYR n 
1 1619 LEU n 
1 1620 GLU n 
1 1621 ARG n 
1 1622 GLU n 
1 1623 ARG n 
1 1624 SER n 
1 1625 SER n 
1 1626 PHE n 
1 1627 PRO n 
1 1628 ARG n 
1 1629 PHE n 
1 1630 TYR n 
1 1631 PHE n 
1 1632 VAL n 
1 1633 GLY n 
1 1634 ASP n 
1 1635 GLU n 
1 1636 ASP n 
1 1637 LEU n 
1 1638 LEU n 
1 1639 GLU n 
1 1640 ILE n 
1 1641 ILE n 
1 1642 GLY n 
1 1643 ASN n 
1 1644 SER n 
1 1645 LYS n 
1 1646 ASN n 
1 1647 VAL n 
1 1648 ALA n 
1 1649 LYS n 
1 1650 LEU n 
1 1651 GLN n 
1 1652 LYS n 
1 1653 HIS n 
1 1654 PHE n 
1 1655 LYS n 
1 1656 LYS n 
1 1657 MET n 
1 1658 PHE n 
1 1659 ALA n 
1 1660 GLY n 
1 1661 VAL n 
1 1662 SER n 
1 1663 SER n 
1 1664 ILE n 
1 1665 ILE n 
1 1666 LEU n 
1 1667 ASN n 
1 1668 GLU n 
1 1669 ASP n 
1 1670 ASN n 
1 1671 SER n 
1 1672 VAL n 
1 1673 VAL n 
1 1674 LEU n 
1 1675 GLY n 
1 1676 ILE n 
1 1677 SER n 
1 1678 SER n 
1 1679 ARG n 
1 1680 GLU n 
1 1681 GLY n 
1 1682 GLU n 
1 1683 GLU n 
1 1684 VAL n 
1 1685 MET n 
1 1686 PHE n 
1 1687 LYS n 
1 1688 THR n 
1 1689 PRO n 
1 1690 VAL n 
1 1691 SER n 
1 1692 ILE n 
1 1693 THR n 
1 1694 GLU n 
1 1695 HIS n 
1 1696 PRO n 
1 1697 LYS n 
1 1698 ILE n 
1 1699 ASN n 
1 1700 GLU n 
1 1701 TRP n 
1 1702 LEU n 
1 1703 THR n 
1 1704 LEU n 
1 1705 VAL n 
1 1706 GLU n 
1 1707 LYS n 
1 1708 GLU n 
1 1709 MET n 
1 1710 ARG n 
1 1711 VAL n 
1 1712 THR n 
1 1713 LEU n 
1 1714 ALA n 
1 1715 LYS n 
1 1716 LEU n 
1 1717 LEU n 
1 1718 ALA n 
1 1719 GLU n 
1 1720 SER n 
1 1721 VAL n 
1 1722 THR n 
1 1723 GLU n 
1 1724 VAL n 
1 1725 GLU n 
1 1726 ILE n 
1 1727 PHE n 
1 1728 GLY n 
1 1729 LYS n 
1 1730 ALA n 
1 1731 THR n 
1 1732 SER n 
1 1733 ILE n 
1 1734 ASP n 
1 1735 PRO n 
1 1736 ASN n 
1 1737 THR n 
1 1738 TYR n 
1 1739 ILE n 
1 1740 THR n 
1 1741 TRP n 
1 1742 ILE n 
1 1743 ASP n 
1 1744 LYS n 
1 1745 TYR n 
1 1746 GLN n 
1 1747 ALA n 
1 1748 GLN n 
1 1749 LEU n 
1 1750 VAL n 
1 1751 VAL n 
1 1752 LEU n 
1 1753 SER n 
1 1754 ALA n 
1 1755 GLN n 
1 1756 ILE n 
1 1757 ALA n 
1 1758 TRP n 
1 1759 SER n 
1 1760 GLU n 
1 1761 ASN n 
1 1762 VAL n 
1 1763 GLU n 
1 1764 THR n 
1 1765 ALA n 
1 1766 LEU n 
1 1767 SER n 
1 1768 SER n 
1 1769 MET n 
1 1770 GLY n 
1 1771 GLY n 
1 1772 GLY n 
1 1773 GLY n 
1 1774 ASP n 
1 1775 ALA n 
1 1776 ALA n 
1 1777 PRO n 
1 1778 LEU n 
1 1779 HIS n 
1 1780 SER n 
1 1781 VAL n 
1 1782 LEU n 
1 1783 SER n 
1 1784 ASN n 
1 1785 VAL n 
1 1786 GLU n 
1 1787 VAL n 
1 1788 THR n 
1 1789 LEU n 
1 1790 ASN n 
1 1791 VAL n 
1 1792 LEU n 
1 1793 ALA n 
1 1794 ASP n 
1 1795 SER n 
1 1796 VAL n 
1 1797 LEU n 
1 1798 MET n 
1 1799 GLU n 
1 1800 GLN n 
1 1801 PRO n 
1 1802 PRO n 
1 1803 LEU n 
1 1804 ARG n 
1 1805 ARG n 
1 1806 ARG n 
1 1807 LYS n 
1 1808 LEU n 
1 1809 GLU n 
1 1810 HIS n 
1 1811 LEU n 
1 1812 ILE n 
1 1813 THR n 
1 1814 GLU n 
1 1815 LEU n 
1 1816 VAL n 
1 1817 HIS n 
1 1818 GLN n 
1 1819 ARG n 
1 1820 ASP n 
1 1821 VAL n 
1 1822 THR n 
1 1823 ARG n 
1 1824 SER n 
1 1825 LEU n 
1 1826 ILE n 
1 1827 LYS n 
1 1828 SER n 
1 1829 LYS n 
1 1830 ILE n 
1 1831 ASP n 
1 1832 ASN n 
1 1833 ALA n 
1 1834 LYS n 
1 1835 SER n 
1 1836 PHE n 
1 1837 GLU n 
1 1838 TRP n 
1 1839 LEU n 
1 1840 SER n 
1 1841 GLN n 
1 1842 MET n 
1 1843 ARG n 
1 1844 PHE n 
1 1845 TYR n 
1 1846 PHE n 
1 1847 ASP n 
1 1848 PRO n 
1 1849 LYS n 
1 1850 GLN n 
1 1851 THR n 
1 1852 ASP n 
1 1853 VAL n 
1 1854 LEU n 
1 1855 GLN n 
1 1856 GLN n 
1 1857 LEU n 
1 1858 SER n 
1 1859 ILE n 
1 1860 GLN n 
1 1861 MET n 
1 1862 ALA n 
1 1863 ASN n 
1 1864 ALA n 
1 1865 LYS n 
1 1866 PHE n 
1 1867 ASN n 
1 1868 TYR n 
1 1869 GLY n 
1 1870 PHE n 
1 1871 GLU n 
1 1872 TYR n 
1 1873 LEU n 
1 1874 GLY n 
1 1875 VAL n 
1 1876 GLN n 
1 1877 ASP n 
1 1878 LYS n 
1 1879 LEU n 
1 1880 VAL n 
1 1881 GLN n 
1 1882 THR n 
1 1883 PRO n 
1 1884 LEU n 
1 1885 THR n 
1 1886 ASP n 
1 1887 ARG n 
1 1888 CYS n 
1 1889 TYR n 
1 1890 LEU n 
1 1891 THR n 
1 1892 MET n 
1 1893 THR n 
1 1894 GLN n 
1 1895 ALA n 
1 1896 LEU n 
1 1897 GLU n 
1 1898 ALA n 
1 1899 ARG n 
1 1900 LEU n 
1 1901 GLY n 
1 1902 GLY n 
1 1903 SER n 
1 1904 PRO n 
1 1905 PHE n 
1 1906 GLY n 
1 1907 PRO n 
1 1908 ALA n 
1 1909 GLY n 
1 1910 THR n 
1 1911 GLY n 
1 1912 LYS n 
1 1913 THR n 
1 1914 GLU n 
1 1915 SER n 
1 1916 VAL n 
1 1917 LYS n 
1 1918 ALA n 
1 1919 LEU n 
1 1920 GLY n 
1 1921 HIS n 
1 1922 GLN n 
1 1923 LEU n 
1 1924 GLY n 
1 1925 ARG n 
1 1926 PHE n 
1 1927 VAL n 
1 1928 LEU n 
1 1929 VAL n 
1 1930 PHE n 
1 1931 ASN n 
1 1932 CYS n 
1 1933 ASP n 
1 1934 GLU n 
1 1935 THR n 
1 1936 PHE n 
1 1937 ASP n 
1 1938 PHE n 
1 1939 GLN n 
1 1940 ALA n 
1 1941 MET n 
1 1942 GLY n 
1 1943 ARG n 
1 1944 ILE n 
1 1945 PHE n 
1 1946 VAL n 
1 1947 GLY n 
1 1948 LEU n 
1 1949 CYS n 
1 1950 GLN n 
1 1951 VAL n 
1 1952 GLY n 
1 1953 ALA n 
1 1954 TRP n 
1 1955 GLY n 
1 1956 CYS n 
1 1957 PHE n 
1 1958 ASP n 
1 1959 GLU n 
1 1960 PHE n 
1 1961 ASN n 
1 1962 ARG n 
1 1963 LEU n 
1 1964 GLU n 
1 1965 GLU n 
1 1966 ARG n 
1 1967 MET n 
1 1968 LEU n 
1 1969 SER n 
1 1970 ALA n 
1 1971 VAL n 
1 1972 SER n 
1 1973 GLN n 
1 1974 GLN n 
1 1975 VAL n 
1 1976 GLN n 
1 1977 CYS n 
1 1978 ILE n 
1 1979 GLN n 
1 1980 GLU n 
1 1981 ALA n 
1 1982 LEU n 
1 1983 ARG n 
1 1984 GLU n 
1 1985 HIS n 
1 1986 SER n 
1 1987 ASN n 
1 1988 PRO n 
1 1989 ASN n 
1 1990 TYR n 
1 1991 ASP n 
1 1992 LYS n 
1 1993 THR n 
1 1994 SER n 
1 1995 ALA n 
1 1996 PRO n 
1 1997 ILE n 
1 1998 THR n 
1 1999 CYS n 
1 2000 GLU n 
1 2001 LEU n 
1 2002 LEU n 
1 2003 ASN n 
1 2004 LYS n 
1 2005 GLN n 
1 2006 VAL n 
1 2007 LYS n 
1 2008 VAL n 
1 2009 SER n 
1 2010 PRO n 
1 2011 ASP n 
1 2012 MET n 
1 2013 ALA n 
1 2014 ILE n 
1 2015 PHE n 
1 2016 ILE n 
1 2017 THR n 
1 2018 MET n 
1 2019 ASN n 
1 2020 PRO n 
1 2021 GLY n 
1 2022 TYR n 
1 2023 ALA n 
1 2024 GLY n 
1 2025 ARG n 
1 2026 SER n 
1 2027 ASN n 
1 2028 LEU n 
1 2029 PRO n 
1 2030 ASP n 
1 2031 ASN n 
1 2032 LEU n 
1 2033 LYS n 
1 2034 LYS n 
1 2035 LEU n 
1 2036 PHE n 
1 2037 ARG n 
1 2038 SER n 
1 2039 LEU n 
1 2040 ALA n 
1 2041 MET n 
1 2042 THR n 
1 2043 LYS n 
1 2044 PRO n 
1 2045 ASP n 
1 2046 ARG n 
1 2047 GLN n 
1 2048 LEU n 
1 2049 ILE n 
1 2050 ALA n 
1 2051 GLN n 
1 2052 VAL n 
1 2053 MET n 
1 2054 LEU n 
1 2055 TYR n 
1 2056 SER n 
1 2057 GLN n 
1 2058 GLY n 
1 2059 PHE n 
1 2060 ARG n 
1 2061 THR n 
1 2062 ALA n 
1 2063 GLU n 
1 2064 VAL n 
1 2065 LEU n 
1 2066 ALA n 
1 2067 ASN n 
1 2068 LYS n 
1 2069 ILE n 
1 2070 VAL n 
1 2071 PRO n 
1 2072 PHE n 
1 2073 PHE n 
1 2074 LYS n 
1 2075 LEU n 
1 2076 CYS n 
1 2077 ASP n 
1 2078 GLU n 
1 2079 GLN n 
1 2080 LEU n 
1 2081 SER n 
1 2082 SER n 
1 2083 GLN n 
1 2084 SER n 
1 2085 HIS n 
1 2086 TYR n 
1 2087 ASP n 
1 2088 PHE n 
1 2089 GLY n 
1 2090 LEU n 
1 2091 ARG n 
1 2092 ALA n 
1 2093 LEU n 
1 2094 LYS n 
1 2095 SER n 
1 2096 VAL n 
1 2097 LEU n 
1 2098 VAL n 
1 2099 SER n 
1 2100 ALA n 
1 2101 GLY n 
1 2102 ASN n 
1 2103 VAL n 
1 2104 LYS n 
1 2105 ARG n 
1 2106 GLU n 
1 2107 ARG n 
1 2108 ILE n 
1 2109 GLN n 
1 2110 LYS n 
1 2111 ILE n 
1 2112 LYS n 
1 2113 ARG n 
1 2114 GLU n 
1 2115 LYS n 
1 2116 GLU n 
1 2117 GLU n 
1 2118 ARG n 
1 2119 GLY n 
1 2120 GLU n 
1 2121 ALA n 
1 2122 VAL n 
1 2123 ASP n 
1 2124 GLU n 
1 2125 GLY n 
1 2126 GLU n 
1 2127 ILE n 
1 2128 ALA n 
1 2129 GLU n 
1 2130 ASN n 
1 2131 LEU n 
1 2132 PRO n 
1 2133 GLU n 
1 2134 GLN n 
1 2135 GLU n 
1 2136 ILE n 
1 2137 LEU n 
1 2138 ILE n 
1 2139 GLN n 
1 2140 SER n 
1 2141 VAL n 
1 2142 CYS n 
1 2143 GLU n 
1 2144 THR n 
1 2145 MET n 
1 2146 VAL n 
1 2147 PRO n 
1 2148 LYS n 
1 2149 LEU n 
1 2150 VAL n 
1 2151 ALA n 
1 2152 GLU n 
1 2153 ASP n 
1 2154 ILE n 
1 2155 PRO n 
1 2156 LEU n 
1 2157 LEU n 
1 2158 PHE n 
1 2159 SER n 
1 2160 LEU n 
1 2161 LEU n 
1 2162 SER n 
1 2163 ASP n 
1 2164 VAL n 
1 2165 PHE n 
1 2166 PRO n 
1 2167 GLY n 
1 2168 VAL n 
1 2169 GLN n 
1 2170 TYR n 
1 2171 HIS n 
1 2172 ARG n 
1 2173 GLY n 
1 2174 GLU n 
1 2175 MET n 
1 2176 THR n 
1 2177 ALA n 
1 2178 LEU n 
1 2179 ARG n 
1 2180 GLU n 
1 2181 GLU n 
1 2182 LEU n 
1 2183 LYS n 
1 2184 LYS n 
1 2185 VAL n 
1 2186 CYS n 
1 2187 GLN n 
1 2188 GLU n 
1 2189 MET n 
1 2190 TYR n 
1 2191 LEU n 
1 2192 THR n 
1 2193 TYR n 
1 2194 GLY n 
1 2195 ASP n 
1 2196 GLY n 
1 2197 GLU n 
1 2198 GLU n 
1 2199 VAL n 
1 2200 GLY n 
1 2201 GLY n 
1 2202 MET n 
1 2203 TRP n 
1 2204 VAL n 
1 2205 GLU n 
1 2206 LYS n 
1 2207 VAL n 
1 2208 LEU n 
1 2209 GLN n 
1 2210 LEU n 
1 2211 TYR n 
1 2212 GLN n 
1 2213 ILE n 
1 2214 THR n 
1 2215 GLN n 
1 2216 ILE n 
1 2217 ASN n 
1 2218 HIS n 
1 2219 GLY n 
1 2220 LEU n 
1 2221 MET n 
1 2222 MET n 
1 2223 VAL n 
1 2224 GLY n 
1 2225 PRO n 
1 2226 SER n 
1 2227 GLY n 
1 2228 SER n 
1 2229 GLY n 
1 2230 LYS n 
1 2231 SER n 
1 2232 MET n 
1 2233 ALA n 
1 2234 TRP n 
1 2235 ARG n 
1 2236 VAL n 
1 2237 LEU n 
1 2238 LEU n 
1 2239 LYS n 
1 2240 ALA n 
1 2241 LEU n 
1 2242 GLU n 
1 2243 ARG n 
1 2244 LEU n 
1 2245 GLU n 
1 2246 GLY n 
1 2247 VAL n 
1 2248 GLU n 
1 2249 GLY n 
1 2250 VAL n 
1 2251 ALA n 
1 2252 HIS n 
1 2253 ILE n 
1 2254 ILE n 
1 2255 ASP n 
1 2256 PRO n 
1 2257 LYS n 
1 2258 ALA n 
1 2259 ILE n 
1 2260 SER n 
1 2261 LYS n 
1 2262 ASP n 
1 2263 HIS n 
1 2264 LEU n 
1 2265 TYR n 
1 2266 GLY n 
1 2267 THR n 
1 2268 LEU n 
1 2269 ASP n 
1 2270 PRO n 
1 2271 ASN n 
1 2272 THR n 
1 2273 ARG n 
1 2274 GLU n 
1 2275 TRP n 
1 2276 THR n 
1 2277 ASP n 
1 2278 GLY n 
1 2279 LEU n 
1 2280 PHE n 
1 2281 THR n 
1 2282 HIS n 
1 2283 VAL n 
1 2284 LEU n 
1 2285 ARG n 
1 2286 LYS n 
1 2287 ILE n 
1 2288 ILE n 
1 2289 ASP n 
1 2290 SER n 
1 2291 VAL n 
1 2292 ARG n 
1 2293 GLY n 
1 2294 GLU n 
1 2295 LEU n 
1 2296 GLN n 
1 2297 LYS n 
1 2298 ARG n 
1 2299 GLN n 
1 2300 TRP n 
1 2301 ILE n 
1 2302 VAL n 
1 2303 PHE n 
1 2304 ASP n 
1 2305 GLY n 
1 2306 ASP n 
1 2307 VAL n 
1 2308 ASP n 
1 2309 PRO n 
1 2310 GLU n 
1 2311 TRP n 
1 2312 VAL n 
1 2313 GLU n 
1 2314 ASN n 
1 2315 LEU n 
1 2316 ASN n 
1 2317 SER n 
1 2318 VAL n 
1 2319 LEU n 
1 2320 ASP n 
1 2321 ASP n 
1 2322 ASN n 
1 2323 LYS n 
1 2324 LEU n 
1 2325 LEU n 
1 2326 THR n 
1 2327 LEU n 
1 2328 PRO n 
1 2329 ASN n 
1 2330 GLY n 
1 2331 GLU n 
1 2332 ARG n 
1 2333 LEU n 
1 2334 SER n 
1 2335 LEU n 
1 2336 PRO n 
1 2337 PRO n 
1 2338 ASN n 
1 2339 VAL n 
1 2340 ARG n 
1 2341 ILE n 
1 2342 MET n 
1 2343 PHE n 
1 2344 GLU n 
1 2345 VAL n 
1 2346 GLN n 
1 2347 ASP n 
1 2348 LEU n 
1 2349 LYS n 
1 2350 TYR n 
1 2351 ALA n 
1 2352 THR n 
1 2353 LEU n 
1 2354 ALA n 
1 2355 THR n 
1 2356 VAL n 
1 2357 SER n 
1 2358 ARG n 
1 2359 CYS n 
1 2360 GLY n 
1 2361 MET n 
1 2362 VAL n 
1 2363 TRP n 
1 2364 PHE n 
1 2365 SER n 
1 2366 GLU n 
1 2367 ASP n 
1 2368 VAL n 
1 2369 LEU n 
1 2370 SER n 
1 2371 THR n 
1 2372 ASP n 
1 2373 MET n 
1 2374 ILE n 
1 2375 PHE n 
1 2376 ASN n 
1 2377 ASN n 
1 2378 PHE n 
1 2379 LEU n 
1 2380 ALA n 
1 2381 ARG n 
1 2382 LEU n 
1 2383 ARG n 
1 2384 SER n 
1 2385 ILE n 
1 2386 PRO n 
1 2387 LEU n 
1 2388 ASP n 
1 2389 GLU n 
1 2390 GLY n 
1 2391 GLU n 
1 2392 ASP n 
1 2393 GLU n 
1 2394 ALA n 
1 2395 GLN n 
1 2396 ARG n 
1 2397 ARG n 
1 2398 ARG n 
1 2399 LYS n 
1 2400 GLY n 
1 2401 LYS n 
1 2402 GLU n 
1 2403 ASP n 
1 2404 GLU n 
1 2405 GLY n 
1 2406 GLU n 
1 2407 GLU n 
1 2408 ALA n 
1 2409 ALA n 
1 2410 SER n 
1 2411 PRO n 
1 2412 MET n 
1 2413 LEU n 
1 2414 GLN n 
1 2415 ILE n 
1 2416 GLN n 
1 2417 ARG n 
1 2418 ASP n 
1 2419 ALA n 
1 2420 ALA n 
1 2421 THR n 
1 2422 ILE n 
1 2423 MET n 
1 2424 GLN n 
1 2425 PRO n 
1 2426 TYR n 
1 2427 PHE n 
1 2428 THR n 
1 2429 SER n 
1 2430 ASN n 
1 2431 GLY n 
1 2432 LEU n 
1 2433 VAL n 
1 2434 THR n 
1 2435 LYS n 
1 2436 ALA n 
1 2437 LEU n 
1 2438 GLU n 
1 2439 HIS n 
1 2440 ALA n 
1 2441 PHE n 
1 2442 GLN n 
1 2443 LEU n 
1 2444 GLU n 
1 2445 HIS n 
1 2446 ILE n 
1 2447 MET n 
1 2448 ASP n 
1 2449 LEU n 
1 2450 THR n 
1 2451 ARG n 
1 2452 LEU n 
1 2453 ARG n 
1 2454 CYS n 
1 2455 LEU n 
1 2456 GLY n 
1 2457 SER n 
1 2458 LEU n 
1 2459 PHE n 
1 2460 SER n 
1 2461 MET n 
1 2462 LEU n 
1 2463 HIS n 
1 2464 GLN n 
1 2465 ALA n 
1 2466 CYS n 
1 2467 ARG n 
1 2468 ASN n 
1 2469 VAL n 
1 2470 ALA n 
1 2471 GLN n 
1 2472 TYR n 
1 2473 ASN n 
1 2474 ALA n 
1 2475 ASN n 
1 2476 HIS n 
1 2477 PRO n 
1 2478 ASP n 
1 2479 PHE n 
1 2480 PRO n 
1 2481 MET n 
1 2482 GLN n 
1 2483 ILE n 
1 2484 GLU n 
1 2485 GLN n 
1 2486 LEU n 
1 2487 GLU n 
1 2488 ARG n 
1 2489 TYR n 
1 2490 ILE n 
1 2491 GLN n 
1 2492 ARG n 
1 2493 TYR n 
1 2494 LEU n 
1 2495 VAL n 
1 2496 TYR n 
1 2497 ALA n 
1 2498 ILE n 
1 2499 LEU n 
1 2500 TRP n 
1 2501 SER n 
1 2502 LEU n 
1 2503 SER n 
1 2504 GLY n 
1 2505 ASP n 
1 2506 SER n 
1 2507 ARG n 
1 2508 LEU n 
1 2509 LYS n 
1 2510 MET n 
1 2511 ARG n 
1 2512 ALA n 
1 2513 GLU n 
1 2514 LEU n 
1 2515 GLY n 
1 2516 GLU n 
1 2517 TYR n 
1 2518 ILE n 
1 2519 ARG n 
1 2520 ARG n 
1 2521 ILE n 
1 2522 THR n 
1 2523 THR n 
1 2524 VAL n 
1 2525 PRO n 
1 2526 LEU n 
1 2527 PRO n 
1 2528 THR n 
1 2529 ALA n 
1 2530 PRO n 
1 2531 ASN n 
1 2532 ILE n 
1 2533 PRO n 
1 2534 ILE n 
1 2535 ILE n 
1 2536 ASP n 
1 2537 TYR n 
1 2538 GLU n 
1 2539 VAL n 
1 2540 SER n 
1 2541 ILE n 
1 2542 SER n 
1 2543 GLY n 
1 2544 GLU n 
1 2545 TRP n 
1 2546 SER n 
1 2547 PRO n 
1 2548 TRP n 
1 2549 GLN n 
1 2550 ALA n 
1 2551 LYS n 
1 2552 VAL n 
1 2553 PRO n 
1 2554 GLN n 
1 2555 ILE n 
1 2556 GLU n 
1 2557 VAL n 
1 2558 GLU n 
1 2559 THR n 
1 2560 HIS n 
1 2561 LYS n 
1 2562 VAL n 
1 2563 ALA n 
1 2564 ALA n 
1 2565 PRO n 
1 2566 ASP n 
1 2567 VAL n 
1 2568 VAL n 
1 2569 VAL n 
1 2570 PRO n 
1 2571 THR n 
1 2572 LEU n 
1 2573 ASP n 
1 2574 THR n 
1 2575 VAL n 
1 2576 ARG n 
1 2577 HIS n 
1 2578 GLU n 
1 2579 ALA n 
1 2580 LEU n 
1 2581 LEU n 
1 2582 TYR n 
1 2583 THR n 
1 2584 TRP n 
1 2585 LEU n 
1 2586 ALA n 
1 2587 GLU n 
1 2588 HIS n 
1 2589 LYS n 
1 2590 PRO n 
1 2591 LEU n 
1 2592 VAL n 
1 2593 LEU n 
1 2594 CYS n 
1 2595 GLY n 
1 2596 PRO n 
1 2597 PRO n 
1 2598 GLY n 
1 2599 SER n 
1 2600 GLY n 
1 2601 LYS n 
1 2602 THR n 
1 2603 MET n 
1 2604 THR n 
1 2605 LEU n 
1 2606 PHE n 
1 2607 SER n 
1 2608 ALA n 
1 2609 LEU n 
1 2610 ARG n 
1 2611 ALA n 
1 2612 LEU n 
1 2613 PRO n 
1 2614 ASP n 
1 2615 MET n 
1 2616 GLU n 
1 2617 VAL n 
1 2618 VAL n 
1 2619 GLY n 
1 2620 LEU n 
1 2621 ASN n 
1 2622 PHE n 
1 2623 SER n 
1 2624 SER n 
1 2625 ALA n 
1 2626 THR n 
1 2627 THR n 
1 2628 PRO n 
1 2629 GLU n 
1 2630 LEU n 
1 2631 LEU n 
1 2632 LEU n 
1 2633 LYS n 
1 2634 THR n 
1 2635 PHE n 
1 2636 ASP n 
1 2637 HIS n 
1 2638 TYR n 
1 2639 CYS n 
1 2640 GLU n 
1 2641 TYR n 
1 2642 ARG n 
1 2643 ARG n 
1 2644 THR n 
1 2645 PRO n 
1 2646 ASN n 
1 2647 GLY n 
1 2648 VAL n 
1 2649 VAL n 
1 2650 LEU n 
1 2651 ALA n 
1 2652 PRO n 
1 2653 VAL n 
1 2654 GLN n 
1 2655 LEU n 
1 2656 GLY n 
1 2657 LYS n 
1 2658 TRP n 
1 2659 LEU n 
1 2660 VAL n 
1 2661 LEU n 
1 2662 PHE n 
1 2663 CYS n 
1 2664 ASP n 
1 2665 GLU n 
1 2666 ILE n 
1 2667 ASN n 
1 2668 LEU n 
1 2669 PRO n 
1 2670 ASP n 
1 2671 MET n 
1 2672 ASP n 
1 2673 LYS n 
1 2674 TYR n 
1 2675 GLY n 
1 2676 THR n 
1 2677 GLN n 
1 2678 ARG n 
1 2679 VAL n 
1 2680 ILE n 
1 2681 SER n 
1 2682 PHE n 
1 2683 ILE n 
1 2684 ARG n 
1 2685 GLN n 
1 2686 MET n 
1 2687 VAL n 
1 2688 GLU n 
1 2689 HIS n 
1 2690 GLY n 
1 2691 GLY n 
1 2692 PHE n 
1 2693 TYR n 
1 2694 ARG n 
1 2695 THR n 
1 2696 SER n 
1 2697 ASP n 
1 2698 GLN n 
1 2699 THR n 
1 2700 TRP n 
1 2701 VAL n 
1 2702 LYS n 
1 2703 LEU n 
1 2704 GLU n 
1 2705 ARG n 
1 2706 ILE n 
1 2707 GLN n 
1 2708 PHE n 
1 2709 VAL n 
1 2710 GLY n 
1 2711 ALA n 
1 2712 CYS n 
1 2713 ASN n 
1 2714 PRO n 
1 2715 PRO n 
1 2716 THR n 
1 2717 ASP n 
1 2718 PRO n 
1 2719 GLY n 
1 2720 ARG n 
1 2721 LYS n 
1 2722 PRO n 
1 2723 LEU n 
1 2724 SER n 
1 2725 HIS n 
1 2726 ARG n 
1 2727 PHE n 
1 2728 LEU n 
1 2729 ARG n 
1 2730 HIS n 
1 2731 VAL n 
1 2732 PRO n 
1 2733 VAL n 
1 2734 VAL n 
1 2735 TYR n 
1 2736 VAL n 
1 2737 ASP n 
1 2738 TYR n 
1 2739 PRO n 
1 2740 GLY n 
1 2741 PRO n 
1 2742 ALA n 
1 2743 SER n 
1 2744 LEU n 
1 2745 THR n 
1 2746 GLN n 
1 2747 ILE n 
1 2748 TYR n 
1 2749 GLY n 
1 2750 THR n 
1 2751 PHE n 
1 2752 ASN n 
1 2753 ARG n 
1 2754 ALA n 
1 2755 MET n 
1 2756 LEU n 
1 2757 ARG n 
1 2758 LEU n 
1 2759 ILE n 
1 2760 PRO n 
1 2761 SER n 
1 2762 LEU n 
1 2763 ARG n 
1 2764 THR n 
1 2765 TYR n 
1 2766 ALA n 
1 2767 GLU n 
1 2768 PRO n 
1 2769 LEU n 
1 2770 THR n 
1 2771 ALA n 
1 2772 ALA n 
1 2773 MET n 
1 2774 VAL n 
1 2775 GLU n 
1 2776 PHE n 
1 2777 TYR n 
1 2778 THR n 
1 2779 MET n 
1 2780 SER n 
1 2781 GLN n 
1 2782 GLU n 
1 2783 ARG n 
1 2784 PHE n 
1 2785 THR n 
1 2786 GLN n 
1 2787 ASP n 
1 2788 THR n 
1 2789 GLN n 
1 2790 PRO n 
1 2791 HIS n 
1 2792 TYR n 
1 2793 ILE n 
1 2794 TYR n 
1 2795 SER n 
1 2796 PRO n 
1 2797 ARG n 
1 2798 GLU n 
1 2799 MET n 
1 2800 THR n 
1 2801 ARG n 
1 2802 TRP n 
1 2803 VAL n 
1 2804 ARG n 
1 2805 GLY n 
1 2806 ILE n 
1 2807 PHE n 
1 2808 GLU n 
1 2809 ALA n 
1 2810 LEU n 
1 2811 ARG n 
1 2812 PRO n 
1 2813 LEU n 
1 2814 GLU n 
1 2815 THR n 
1 2816 LEU n 
1 2817 PRO n 
1 2818 VAL n 
1 2819 GLU n 
1 2820 GLY n 
1 2821 LEU n 
1 2822 ILE n 
1 2823 ARG n 
1 2824 ILE n 
1 2825 TRP n 
1 2826 ALA n 
1 2827 HIS n 
1 2828 GLU n 
1 2829 ALA n 
1 2830 LEU n 
1 2831 ARG n 
1 2832 LEU n 
1 2833 PHE n 
1 2834 GLN n 
1 2835 ASP n 
1 2836 ARG n 
1 2837 LEU n 
1 2838 VAL n 
1 2839 GLU n 
1 2840 ASP n 
1 2841 GLU n 
1 2842 GLU n 
1 2843 ARG n 
1 2844 ARG n 
1 2845 TRP n 
1 2846 THR n 
1 2847 ASP n 
1 2848 GLU n 
1 2849 ASN n 
1 2850 ILE n 
1 2851 ASP n 
1 2852 THR n 
1 2853 VAL n 
1 2854 ALA n 
1 2855 LEU n 
1 2856 LYS n 
1 2857 HIS n 
1 2858 PHE n 
1 2859 PRO n 
1 2860 ASN n 
1 2861 ILE n 
1 2862 ASP n 
1 2863 ARG n 
1 2864 GLU n 
1 2865 LYS n 
1 2866 ALA n 
1 2867 MET n 
1 2868 SER n 
1 2869 ARG n 
1 2870 PRO n 
1 2871 ILE n 
1 2872 LEU n 
1 2873 TYR n 
1 2874 SER n 
1 2875 ASN n 
1 2876 TRP n 
1 2877 LEU n 
1 2878 SER n 
1 2879 LYS n 
1 2880 ASP n 
1 2881 TYR n 
1 2882 ILE n 
1 2883 PRO n 
1 2884 VAL n 
1 2885 ASP n 
1 2886 GLN n 
1 2887 GLU n 
1 2888 GLU n 
1 2889 LEU n 
1 2890 ARG n 
1 2891 ASP n 
1 2892 TYR n 
1 2893 VAL n 
1 2894 LYS n 
1 2895 ALA n 
1 2896 ARG n 
1 2897 LEU n 
1 2898 LYS n 
1 2899 VAL n 
1 2900 PHE n 
1 2901 TYR n 
1 2902 GLU n 
1 2903 GLU n 
1 2904 GLU n 
1 2905 LEU n 
1 2906 ASP n 
1 2907 VAL n 
1 2908 PRO n 
1 2909 LEU n 
1 2910 VAL n 
1 2911 LEU n 
1 2912 PHE n 
1 2913 ASN n 
1 2914 GLU n 
1 2915 VAL n 
1 2916 LEU n 
1 2917 ASP n 
1 2918 HIS n 
1 2919 VAL n 
1 2920 LEU n 
1 2921 ARG n 
1 2922 ILE n 
1 2923 ASP n 
1 2924 ARG n 
1 2925 ILE n 
1 2926 PHE n 
1 2927 ARG n 
1 2928 GLN n 
1 2929 PRO n 
1 2930 GLN n 
1 2931 GLY n 
1 2932 HIS n 
1 2933 LEU n 
1 2934 LEU n 
1 2935 LEU n 
1 2936 ILE n 
1 2937 GLY n 
1 2938 VAL n 
1 2939 SER n 
1 2940 GLY n 
1 2941 ALA n 
1 2942 GLY n 
1 2943 LYS n 
1 2944 THR n 
1 2945 THR n 
1 2946 LEU n 
1 2947 SER n 
1 2948 ARG n 
1 2949 PHE n 
1 2950 VAL n 
1 2951 ALA n 
1 2952 TRP n 
1 2953 MET n 
1 2954 ASN n 
1 2955 GLY n 
1 2956 LEU n 
1 2957 SER n 
1 2958 VAL n 
1 2959 TYR n 
1 2960 GLN n 
1 2961 ILE n 
1 2962 LYS n 
1 2963 VAL n 
1 2964 HIS n 
1 2965 ARG n 
1 2966 LYS n 
1 2967 TYR n 
1 2968 THR n 
1 2969 GLY n 
1 2970 GLU n 
1 2971 ASP n 
1 2972 PHE n 
1 2973 ASP n 
1 2974 GLU n 
1 2975 ASP n 
1 2976 LEU n 
1 2977 ARG n 
1 2978 THR n 
1 2979 VAL n 
1 2980 LEU n 
1 2981 ARG n 
1 2982 ARG n 
1 2983 SER n 
1 2984 GLY n 
1 2985 CYS n 
1 2986 LYS n 
1 2987 ASN n 
1 2988 GLU n 
1 2989 LYS n 
1 2990 ILE n 
1 2991 ALA n 
1 2992 PHE n 
1 2993 ILE n 
1 2994 MET n 
1 2995 ASP n 
1 2996 GLU n 
1 2997 SER n 
1 2998 ASN n 
1 2999 VAL n 
1 3000 LEU n 
1 3001 ASP n 
1 3002 SER n 
1 3003 GLY n 
1 3004 PHE n 
1 3005 LEU n 
1 3006 GLU n 
1 3007 ARG n 
1 3008 MET n 
1 3009 ASN n 
1 3010 THR n 
1 3011 LEU n 
1 3012 LEU n 
1 3013 ALA n 
1 3014 ASN n 
1 3015 GLY n 
1 3016 GLU n 
1 3017 VAL n 
1 3018 PRO n 
1 3019 GLY n 
1 3020 LEU n 
1 3021 PHE n 
1 3022 GLU n 
1 3023 GLY n 
1 3024 ASP n 
1 3025 GLU n 
1 3026 TYR n 
1 3027 ALA n 
1 3028 THR n 
1 3029 LEU n 
1 3030 MET n 
1 3031 THR n 
1 3032 GLN n 
1 3033 CYS n 
1 3034 LYS n 
1 3035 GLU n 
1 3036 GLY n 
1 3037 ALA n 
1 3038 GLN n 
1 3039 LYS n 
1 3040 GLU n 
1 3041 GLY n 
1 3042 LEU n 
1 3043 MET n 
1 3044 LEU n 
1 3045 ASP n 
1 3046 SER n 
1 3047 HIS n 
1 3048 GLU n 
1 3049 GLU n 
1 3050 LEU n 
1 3051 TYR n 
1 3052 LYS n 
1 3053 TRP n 
1 3054 PHE n 
1 3055 THR n 
1 3056 SER n 
1 3057 GLN n 
1 3058 VAL n 
1 3059 ILE n 
1 3060 ARG n 
1 3061 ASN n 
1 3062 LEU n 
1 3063 HIS n 
1 3064 VAL n 
1 3065 VAL n 
1 3066 PHE n 
1 3067 THR n 
1 3068 MET n 
1 3069 ASN n 
1 3070 PRO n 
1 3071 SER n 
1 3072 SER n 
1 3073 GLU n 
1 3074 GLY n 
1 3075 LEU n 
1 3076 LYS n 
1 3077 ASP n 
1 3078 ARG n 
1 3079 ALA n 
1 3080 ALA n 
1 3081 THR n 
1 3082 SER n 
1 3083 PRO n 
1 3084 ALA n 
1 3085 LEU n 
1 3086 PHE n 
1 3087 ASN n 
1 3088 ARG n 
1 3089 CYS n 
1 3090 VAL n 
1 3091 LEU n 
1 3092 ASN n 
1 3093 TRP n 
1 3094 PHE n 
1 3095 GLY n 
1 3096 ASP n 
1 3097 TRP n 
1 3098 SER n 
1 3099 THR n 
1 3100 GLU n 
1 3101 ALA n 
1 3102 LEU n 
1 3103 TYR n 
1 3104 GLN n 
1 3105 VAL n 
1 3106 GLY n 
1 3107 LYS n 
1 3108 GLU n 
1 3109 PHE n 
1 3110 THR n 
1 3111 SER n 
1 3112 LYS n 
1 3113 MET n 
1 3114 ASP n 
1 3115 LEU n 
1 3116 GLU n 
1 3117 LYS n 
1 3118 PRO n 
1 3119 ASN n 
1 3120 TYR n 
1 3121 ILE n 
1 3122 VAL n 
1 3123 PRO n 
1 3124 ASP n 
1 3125 TYR n 
1 3126 MET n 
1 3127 PRO n 
1 3128 VAL n 
1 3129 VAL n 
1 3130 TYR n 
1 3131 ASP n 
1 3132 LYS n 
1 3133 LEU n 
1 3134 PRO n 
1 3135 GLN n 
1 3136 PRO n 
1 3137 PRO n 
1 3138 SER n 
1 3139 HIS n 
1 3140 ARG n 
1 3141 GLU n 
1 3142 ALA n 
1 3143 ILE n 
1 3144 VAL n 
1 3145 ASN n 
1 3146 SER n 
1 3147 CYS n 
1 3148 VAL n 
1 3149 PHE n 
1 3150 VAL n 
1 3151 HIS n 
1 3152 GLN n 
1 3153 THR n 
1 3154 LEU n 
1 3155 HIS n 
1 3156 GLN n 
1 3157 ALA n 
1 3158 ASN n 
1 3159 ALA n 
1 3160 ARG n 
1 3161 LEU n 
1 3162 ALA n 
1 3163 LYS n 
1 3164 ARG n 
1 3165 GLY n 
1 3166 GLY n 
1 3167 ARG n 
1 3168 THR n 
1 3169 MET n 
1 3170 ALA n 
1 3171 ILE n 
1 3172 THR n 
1 3173 PRO n 
1 3174 ARG n 
1 3175 HIS n 
1 3176 TYR n 
1 3177 LEU n 
1 3178 ASP n 
1 3179 PHE n 
1 3180 ILE n 
1 3181 ASN n 
1 3182 HIS n 
1 3183 TYR n 
1 3184 ALA n 
1 3185 ASN n 
1 3186 LEU n 
1 3187 PHE n 
1 3188 HIS n 
1 3189 GLU n 
1 3190 LYS n 
1 3191 ARG n 
1 3192 SER n 
1 3193 GLU n 
1 3194 LEU n 
1 3195 GLU n 
1 3196 GLU n 
1 3197 GLN n 
1 3198 GLN n 
1 3199 MET n 
1 3200 HIS n 
1 3201 LEU n 
1 3202 ASN n 
1 3203 VAL n 
1 3204 GLY n 
1 3205 LEU n 
1 3206 ARG n 
1 3207 LYS n 
1 3208 ILE n 
1 3209 LYS n 
1 3210 GLU n 
1 3211 THR n 
1 3212 VAL n 
1 3213 ASP n 
1 3214 GLN n 
1 3215 VAL n 
1 3216 GLU n 
1 3217 GLU n 
1 3218 LEU n 
1 3219 ARG n 
1 3220 ARG n 
1 3221 ASP n 
1 3222 LEU n 
1 3223 ARG n 
1 3224 ILE n 
1 3225 LYS n 
1 3226 SER n 
1 3227 GLN n 
1 3228 GLU n 
1 3229 LEU n 
1 3230 GLU n 
1 3231 VAL n 
1 3232 LYS n 
1 3233 ASN n 
1 3234 ALA n 
1 3235 ALA n 
1 3236 ALA n 
1 3237 ASN n 
1 3238 ASP n 
1 3239 LYS n 
1 3240 LEU n 
1 3241 LYS n 
1 3242 LYS n 
1 3243 MET n 
1 3244 VAL n 
1 3245 LYS n 
1 3246 ASP n 
1 3247 GLN n 
1 3248 GLN n 
1 3249 GLU n 
1 3250 ALA n 
1 3251 GLU n 
1 3252 LYS n 
1 3253 LYS n 
1 3254 LYS n 
1 3255 VAL n 
1 3256 MET n 
1 3257 SER n 
1 3258 GLN n 
1 3259 GLU n 
1 3260 ILE n 
1 3261 GLN n 
1 3262 GLU n 
1 3263 GLN n 
1 3264 LEU n 
1 3265 HIS n 
1 3266 LYS n 
1 3267 GLN n 
1 3268 GLN n 
1 3269 GLU n 
1 3270 VAL n 
1 3271 ILE n 
1 3272 ALA n 
1 3273 ASP n 
1 3274 LYS n 
1 3275 GLN n 
1 3276 MET n 
1 3277 SER n 
1 3278 VAL n 
1 3279 LYS n 
1 3280 GLU n 
1 3281 ASP n 
1 3282 LEU n 
1 3283 ASP n 
1 3284 LYS n 
1 3285 VAL n 
1 3286 GLU n 
1 3287 PRO n 
1 3288 ALA n 
1 3289 VAL n 
1 3290 ILE n 
1 3291 GLU n 
1 3292 ALA n 
1 3293 GLN n 
1 3294 ASN n 
1 3295 ALA n 
1 3296 VAL n 
1 3297 LYS n 
1 3298 SER n 
1 3299 ILE n 
1 3300 LYS n 
1 3301 LYS n 
1 3302 GLN n 
1 3303 HIS n 
1 3304 LEU n 
1 3305 VAL n 
1 3306 GLU n 
1 3307 VAL n 
1 3308 ARG n 
1 3309 SER n 
1 3310 MET n 
1 3311 ALA n 
1 3312 ASN n 
1 3313 PRO n 
1 3314 PRO n 
1 3315 ALA n 
1 3316 ALA n 
1 3317 VAL n 
1 3318 LYS n 
1 3319 LEU n 
1 3320 ALA n 
1 3321 LEU n 
1 3322 GLU n 
1 3323 SER n 
1 3324 ILE n 
1 3325 CYS n 
1 3326 LEU n 
1 3327 LEU n 
1 3328 LEU n 
1 3329 GLY n 
1 3330 GLU n 
1 3331 SER n 
1 3332 THR n 
1 3333 THR n 
1 3334 ASP n 
1 3335 TRP n 
1 3336 LYS n 
1 3337 GLN n 
1 3338 ILE n 
1 3339 ARG n 
1 3340 SER n 
1 3341 ILE n 
1 3342 ILE n 
1 3343 MET n 
1 3344 ARG n 
1 3345 GLU n 
1 3346 ASN n 
1 3347 PHE n 
1 3348 ILE n 
1 3349 PRO n 
1 3350 THR n 
1 3351 ILE n 
1 3352 VAL n 
1 3353 ASN n 
1 3354 PHE n 
1 3355 SER n 
1 3356 ALA n 
1 3357 GLU n 
1 3358 GLU n 
1 3359 ILE n 
1 3360 SER n 
1 3361 ASP n 
1 3362 ALA n 
1 3363 ILE n 
1 3364 ARG n 
1 3365 GLU n 
1 3366 LYS n 
1 3367 MET n 
1 3368 LYS n 
1 3369 LYS n 
1 3370 ASN n 
1 3371 TYR n 
1 3372 MET n 
1 3373 SER n 
1 3374 ASN n 
1 3375 PRO n 
1 3376 SER n 
1 3377 TYR n 
1 3378 ASN n 
1 3379 TYR n 
1 3380 GLU n 
1 3381 ILE n 
1 3382 VAL n 
1 3383 ASN n 
1 3384 ARG n 
1 3385 ALA n 
1 3386 SER n 
1 3387 LEU n 
1 3388 ALA n 
1 3389 CYS n 
1 3390 GLY n 
1 3391 PRO n 
1 3392 MET n 
1 3393 VAL n 
1 3394 LYS n 
1 3395 TRP n 
1 3396 ALA n 
1 3397 ILE n 
1 3398 ALA n 
1 3399 GLN n 
1 3400 LEU n 
1 3401 ASN n 
1 3402 TYR n 
1 3403 ALA n 
1 3404 ASP n 
1 3405 MET n 
1 3406 LEU n 
1 3407 LYS n 
1 3408 ARG n 
1 3409 VAL n 
1 3410 GLU n 
1 3411 PRO n 
1 3412 LEU n 
1 3413 ARG n 
1 3414 ASN n 
1 3415 GLU n 
1 3416 LEU n 
1 3417 GLN n 
1 3418 LYS n 
1 3419 LEU n 
1 3420 GLU n 
1 3421 ASP n 
1 3422 ASP n 
1 3423 ALA n 
1 3424 LYS n 
1 3425 ASP n 
1 3426 ASN n 
1 3427 GLN n 
1 3428 GLN n 
1 3429 LYS n 
1 3430 ALA n 
1 3431 ASN n 
1 3432 GLU n 
1 3433 VAL n 
1 3434 GLU n 
1 3435 GLN n 
1 3436 MET n 
1 3437 ILE n 
1 3438 ARG n 
1 3439 ASP n 
1 3440 LEU n 
1 3441 GLU n 
1 3442 ALA n 
1 3443 SER n 
1 3444 ILE n 
1 3445 ALA n 
1 3446 ARG n 
1 3447 TYR n 
1 3448 LYS n 
1 3449 GLU n 
1 3450 GLU n 
1 3451 TYR n 
1 3452 ALA n 
1 3453 VAL n 
1 3454 LEU n 
1 3455 ILE n 
1 3456 SER n 
1 3457 GLU n 
1 3458 ALA n 
1 3459 GLN n 
1 3460 ALA n 
1 3461 ILE n 
1 3462 LYS n 
1 3463 ALA n 
1 3464 ASP n 
1 3465 LEU n 
1 3466 ALA n 
1 3467 ALA n 
1 3468 VAL n 
1 3469 GLU n 
1 3470 ALA n 
1 3471 LYS n 
1 3472 VAL n 
1 3473 ASN n 
1 3474 ARG n 
1 3475 SER n 
1 3476 THR n 
1 3477 ALA n 
1 3478 LEU n 
1 3479 LEU n 
1 3480 LYS n 
1 3481 SER n 
1 3482 LEU n 
1 3483 SER n 
1 3484 ALA n 
1 3485 GLU n 
1 3486 ARG n 
1 3487 GLU n 
1 3488 ARG n 
1 3489 TRP n 
1 3490 GLU n 
1 3491 LYS n 
1 3492 THR n 
1 3493 SER n 
1 3494 GLU n 
1 3495 THR n 
1 3496 PHE n 
1 3497 LYS n 
1 3498 ASN n 
1 3499 GLN n 
1 3500 MET n 
1 3501 SER n 
1 3502 THR n 
1 3503 ILE n 
1 3504 ALA n 
1 3505 GLY n 
1 3506 ASP n 
1 3507 CYS n 
1 3508 LEU n 
1 3509 LEU n 
1 3510 SER n 
1 3511 ALA n 
1 3512 ALA n 
1 3513 PHE n 
1 3514 ILE n 
1 3515 ALA n 
1 3516 TYR n 
1 3517 ALA n 
1 3518 GLY n 
1 3519 TYR n 
1 3520 PHE n 
1 3521 ASP n 
1 3522 GLN n 
1 3523 GLN n 
1 3524 MET n 
1 3525 ARG n 
1 3526 GLN n 
1 3527 ASN n 
1 3528 LEU n 
1 3529 PHE n 
1 3530 THR n 
1 3531 THR n 
1 3532 TRP n 
1 3533 SER n 
1 3534 HIS n 
1 3535 HIS n 
1 3536 LEU n 
1 3537 GLN n 
1 3538 GLN n 
1 3539 ALA n 
1 3540 ASN n 
1 3541 ILE n 
1 3542 GLN n 
1 3543 PHE n 
1 3544 ARG n 
1 3545 THR n 
1 3546 ASP n 
1 3547 ILE n 
1 3548 ALA n 
1 3549 ARG n 
1 3550 THR n 
1 3551 GLU n 
1 3552 TYR n 
1 3553 LEU n 
1 3554 SER n 
1 3555 ASN n 
1 3556 ALA n 
1 3557 ASP n 
1 3558 GLU n 
1 3559 ARG n 
1 3560 LEU n 
1 3561 ARG n 
1 3562 TRP n 
1 3563 GLN n 
1 3564 ALA n 
1 3565 SER n 
1 3566 SER n 
1 3567 LEU n 
1 3568 PRO n 
1 3569 ALA n 
1 3570 ASP n 
1 3571 ASP n 
1 3572 LEU n 
1 3573 CYS n 
1 3574 THR n 
1 3575 GLU n 
1 3576 ASN n 
1 3577 ALA n 
1 3578 ILE n 
1 3579 MET n 
1 3580 LEU n 
1 3581 LYS n 
1 3582 ARG n 
1 3583 PHE n 
1 3584 ASN n 
1 3585 ARG n 
1 3586 TYR n 
1 3587 PRO n 
1 3588 LEU n 
1 3589 ILE n 
1 3590 ILE n 
1 3591 ASP n 
1 3592 PRO n 
1 3593 SER n 
1 3594 GLY n 
1 3595 GLN n 
1 3596 ALA n 
1 3597 THR n 
1 3598 GLU n 
1 3599 PHE n 
1 3600 ILE n 
1 3601 MET n 
1 3602 ASN n 
1 3603 GLU n 
1 3604 TYR n 
1 3605 LYS n 
1 3606 ASP n 
1 3607 ARG n 
1 3608 LYS n 
1 3609 ILE n 
1 3610 THR n 
1 3611 ARG n 
1 3612 THR n 
1 3613 SER n 
1 3614 PHE n 
1 3615 LEU n 
1 3616 ASP n 
1 3617 ASP n 
1 3618 ALA n 
1 3619 PHE n 
1 3620 ARG n 
1 3621 LYS n 
1 3622 ASN n 
1 3623 LEU n 
1 3624 GLU n 
1 3625 SER n 
1 3626 ALA n 
1 3627 LEU n 
1 3628 ARG n 
1 3629 PHE n 
1 3630 GLY n 
1 3631 ASN n 
1 3632 PRO n 
1 3633 LEU n 
1 3634 LEU n 
1 3635 VAL n 
1 3636 GLN n 
1 3637 ASP n 
1 3638 VAL n 
1 3639 GLU n 
1 3640 SER n 
1 3641 TYR n 
1 3642 ASP n 
1 3643 PRO n 
1 3644 VAL n 
1 3645 LEU n 
1 3646 ASN n 
1 3647 PRO n 
1 3648 VAL n 
1 3649 LEU n 
1 3650 ASN n 
1 3651 ARG n 
1 3652 GLU n 
1 3653 VAL n 
1 3654 ARG n 
1 3655 ARG n 
1 3656 THR n 
1 3657 GLY n 
1 3658 GLY n 
1 3659 ARG n 
1 3660 VAL n 
1 3661 LEU n 
1 3662 ILE n 
1 3663 THR n 
1 3664 LEU n 
1 3665 GLY n 
1 3666 ASP n 
1 3667 GLN n 
1 3668 ASP n 
1 3669 ILE n 
1 3670 ASP n 
1 3671 LEU n 
1 3672 SER n 
1 3673 PRO n 
1 3674 SER n 
1 3675 PHE n 
1 3676 VAL n 
1 3677 ILE n 
1 3678 PHE n 
1 3679 LEU n 
1 3680 SER n 
1 3681 THR n 
1 3682 ARG n 
1 3683 ASP n 
1 3684 PRO n 
1 3685 THR n 
1 3686 VAL n 
1 3687 GLU n 
1 3688 PHE n 
1 3689 PRO n 
1 3690 PRO n 
1 3691 ASP n 
1 3692 LEU n 
1 3693 CYS n 
1 3694 SER n 
1 3695 ARG n 
1 3696 VAL n 
1 3697 THR n 
1 3698 PHE n 
1 3699 VAL n 
1 3700 ASN n 
1 3701 PHE n 
1 3702 THR n 
1 3703 VAL n 
1 3704 THR n 
1 3705 ARG n 
1 3706 SER n 
1 3707 SER n 
1 3708 LEU n 
1 3709 GLN n 
1 3710 SER n 
1 3711 GLN n 
1 3712 CYS n 
1 3713 LEU n 
1 3714 ASN n 
1 3715 GLU n 
1 3716 VAL n 
1 3717 LEU n 
1 3718 LYS n 
1 3719 ALA n 
1 3720 GLU n 
1 3721 ARG n 
1 3722 PRO n 
1 3723 ASP n 
1 3724 VAL n 
1 3725 ASP n 
1 3726 GLU n 
1 3727 LYS n 
1 3728 ARG n 
1 3729 SER n 
1 3730 ASP n 
1 3731 LEU n 
1 3732 LEU n 
1 3733 LYS n 
1 3734 LEU n 
1 3735 GLN n 
1 3736 GLY n 
1 3737 GLU n 
1 3738 PHE n 
1 3739 GLN n 
1 3740 LEU n 
1 3741 ARG n 
1 3742 LEU n 
1 3743 ARG n 
1 3744 GLN n 
1 3745 LEU n 
1 3746 GLU n 
1 3747 LYS n 
1 3748 SER n 
1 3749 LEU n 
1 3750 LEU n 
1 3751 GLN n 
1 3752 ALA n 
1 3753 LEU n 
1 3754 ASN n 
1 3755 GLU n 
1 3756 VAL n 
1 3757 LYS n 
1 3758 GLY n 
1 3759 ARG n 
1 3760 ILE n 
1 3761 LEU n 
1 3762 ASP n 
1 3763 ASP n 
1 3764 ASP n 
1 3765 THR n 
1 3766 ILE n 
1 3767 ILE n 
1 3768 THR n 
1 3769 THR n 
1 3770 LEU n 
1 3771 GLU n 
1 3772 ASN n 
1 3773 LEU n 
1 3774 LYS n 
1 3775 ARG n 
1 3776 GLU n 
1 3777 ALA n 
1 3778 ALA n 
1 3779 GLU n 
1 3780 VAL n 
1 3781 THR n 
1 3782 ARG n 
1 3783 LYS n 
1 3784 VAL n 
1 3785 GLU n 
1 3786 GLU n 
1 3787 THR n 
1 3788 ASP n 
1 3789 ILE n 
1 3790 VAL n 
1 3791 MET n 
1 3792 GLN n 
1 3793 GLU n 
1 3794 VAL n 
1 3795 GLU n 
1 3796 THR n 
1 3797 VAL n 
1 3798 SER n 
1 3799 GLN n 
1 3800 GLN n 
1 3801 TYR n 
1 3802 LEU n 
1 3803 PRO n 
1 3804 LEU n 
1 3805 SER n 
1 3806 THR n 
1 3807 ALA n 
1 3808 CYS n 
1 3809 SER n 
1 3810 SER n 
1 3811 ILE n 
1 3812 TYR n 
1 3813 PHE n 
1 3814 THR n 
1 3815 MET n 
1 3816 GLU n 
1 3817 SER n 
1 3818 LEU n 
1 3819 LYS n 
1 3820 GLN n 
1 3821 ILE n 
1 3822 HIS n 
1 3823 PHE n 
1 3824 LEU n 
1 3825 TYR n 
1 3826 GLN n 
1 3827 TYR n 
1 3828 SER n 
1 3829 LEU n 
1 3830 GLN n 
1 3831 PHE n 
1 3832 PHE n 
1 3833 LEU n 
1 3834 ASP n 
1 3835 ILE n 
1 3836 TYR n 
1 3837 HIS n 
1 3838 ASN n 
1 3839 VAL n 
1 3840 LEU n 
1 3841 TYR n 
1 3842 GLU n 
1 3843 ASN n 
1 3844 PRO n 
1 3845 ASN n 
1 3846 LEU n 
1 3847 LYS n 
1 3848 GLY n 
1 3849 VAL n 
1 3850 THR n 
1 3851 ASP n 
1 3852 HIS n 
1 3853 THR n 
1 3854 GLN n 
1 3855 ARG n 
1 3856 LEU n 
1 3857 SER n 
1 3858 ILE n 
1 3859 ILE n 
1 3860 THR n 
1 3861 LYS n 
1 3862 ASP n 
1 3863 LEU n 
1 3864 PHE n 
1 3865 GLN n 
1 3866 VAL n 
1 3867 ALA n 
1 3868 PHE n 
1 3869 ASN n 
1 3870 ARG n 
1 3871 VAL n 
1 3872 ALA n 
1 3873 ARG n 
1 3874 GLY n 
1 3875 MET n 
1 3876 LEU n 
1 3877 HIS n 
1 3878 GLN n 
1 3879 ASP n 
1 3880 HIS n 
1 3881 ILE n 
1 3882 THR n 
1 3883 PHE n 
1 3884 ALA n 
1 3885 MET n 
1 3886 LEU n 
1 3887 LEU n 
1 3888 ALA n 
1 3889 ARG n 
1 3890 ILE n 
1 3891 LYS n 
1 3892 LEU n 
1 3893 LYS n 
1 3894 GLY n 
1 3895 THR n 
1 3896 VAL n 
1 3897 GLY n 
1 3898 GLU n 
1 3899 PRO n 
1 3900 THR n 
1 3901 TYR n 
1 3902 ASP n 
1 3903 ALA n 
1 3904 GLU n 
1 3905 PHE n 
1 3906 GLN n 
1 3907 HIS n 
1 3908 PHE n 
1 3909 LEU n 
1 3910 ARG n 
1 3911 GLY n 
1 3912 ASN n 
1 3913 GLU n 
1 3914 ILE n 
1 3915 VAL n 
1 3916 LEU n 
1 3917 SER n 
1 3918 ALA n 
1 3919 GLY n 
1 3920 SER n 
1 3921 THR n 
1 3922 PRO n 
1 3923 ARG n 
1 3924 ILE n 
1 3925 GLN n 
1 3926 GLY n 
1 3927 LEU n 
1 3928 THR n 
1 3929 VAL n 
1 3930 GLU n 
1 3931 GLN n 
1 3932 ALA n 
1 3933 GLU n 
1 3934 ALA n 
1 3935 VAL n 
1 3936 VAL n 
1 3937 ARG n 
1 3938 LEU n 
1 3939 SER n 
1 3940 CYS n 
1 3941 LEU n 
1 3942 PRO n 
1 3943 ALA n 
1 3944 PHE n 
1 3945 LYS n 
1 3946 ASP n 
1 3947 LEU n 
1 3948 ILE n 
1 3949 ALA n 
1 3950 LYS n 
1 3951 VAL n 
1 3952 GLN n 
1 3953 ALA n 
1 3954 ASP n 
1 3955 GLU n 
1 3956 GLN n 
1 3957 PHE n 
1 3958 GLY n 
1 3959 ILE n 
1 3960 TRP n 
1 3961 LEU n 
1 3962 ASP n 
1 3963 SER n 
1 3964 SER n 
1 3965 SER n 
1 3966 PRO n 
1 3967 GLU n 
1 3968 GLN n 
1 3969 THR n 
1 3970 VAL n 
1 3971 PRO n 
1 3972 TYR n 
1 3973 LEU n 
1 3974 TRP n 
1 3975 SER n 
1 3976 GLU n 
1 3977 GLU n 
1 3978 THR n 
1 3979 PRO n 
1 3980 ALA n 
1 3981 THR n 
1 3982 PRO n 
1 3983 ILE n 
1 3984 GLY n 
1 3985 GLN n 
1 3986 ALA n 
1 3987 ILE n 
1 3988 HIS n 
1 3989 ARG n 
1 3990 LEU n 
1 3991 LEU n 
1 3992 LEU n 
1 3993 ILE n 
1 3994 GLN n 
1 3995 ALA n 
1 3996 PHE n 
1 3997 ARG n 
1 3998 PRO n 
1 3999 ASP n 
1 4000 ARG n 
1 4001 LEU n 
1 4002 LEU n 
1 4003 ALA n 
1 4004 MET n 
1 4005 ALA n 
1 4006 HIS n 
1 4007 MET n 
1 4008 PHE n 
1 4009 VAL n 
1 4010 SER n 
1 4011 THR n 
1 4012 ASN n 
1 4013 LEU n 
1 4014 GLY n 
1 4015 GLU n 
1 4016 SER n 
1 4017 PHE n 
1 4018 MET n 
1 4019 SER n 
1 4020 ILE n 
1 4021 MET n 
1 4022 GLU n 
1 4023 GLN n 
1 4024 PRO n 
1 4025 LEU n 
1 4026 ASP n 
1 4027 LEU n 
1 4028 THR n 
1 4029 HIS n 
1 4030 ILE n 
1 4031 VAL n 
1 4032 GLY n 
1 4033 THR n 
1 4034 GLU n 
1 4035 VAL n 
1 4036 LYS n 
1 4037 PRO n 
1 4038 ASN n 
1 4039 THR n 
1 4040 PRO n 
1 4041 VAL n 
1 4042 LEU n 
1 4043 MET n 
1 4044 CYS n 
1 4045 SER n 
1 4046 VAL n 
1 4047 PRO n 
1 4048 GLY n 
1 4049 TYR n 
1 4050 ASP n 
1 4051 ALA n 
1 4052 SER n 
1 4053 GLY n 
1 4054 HIS n 
1 4055 VAL n 
1 4056 GLU n 
1 4057 ASP n 
1 4058 LEU n 
1 4059 ALA n 
1 4060 ALA n 
1 4061 GLU n 
1 4062 GLN n 
1 4063 ASN n 
1 4064 THR n 
1 4065 GLN n 
1 4066 ILE n 
1 4067 THR n 
1 4068 SER n 
1 4069 ILE n 
1 4070 ALA n 
1 4071 ILE n 
1 4072 GLY n 
1 4073 SER n 
1 4074 ALA n 
1 4075 GLU n 
1 4076 GLY n 
1 4077 PHE n 
1 4078 ASN n 
1 4079 GLN n 
1 4080 ALA n 
1 4081 ASP n 
1 4082 LYS n 
1 4083 ALA n 
1 4084 ILE n 
1 4085 ASN n 
1 4086 THR n 
1 4087 ALA n 
1 4088 VAL n 
1 4089 LYS n 
1 4090 SER n 
1 4091 GLY n 
1 4092 ARG n 
1 4093 TRP n 
1 4094 VAL n 
1 4095 MET n 
1 4096 LEU n 
1 4097 LYS n 
1 4098 ASN n 
1 4099 VAL n 
1 4100 HIS n 
1 4101 LEU n 
1 4102 ALA n 
1 4103 PRO n 
1 4104 GLY n 
1 4105 TRP n 
1 4106 LEU n 
1 4107 MET n 
1 4108 GLN n 
1 4109 LEU n 
1 4110 GLU n 
1 4111 LYS n 
1 4112 LYS n 
1 4113 LEU n 
1 4114 HIS n 
1 4115 SER n 
1 4116 LEU n 
1 4117 GLN n 
1 4118 PRO n 
1 4119 HIS n 
1 4120 ALA n 
1 4121 CYS n 
1 4122 PHE n 
1 4123 ARG n 
1 4124 LEU n 
1 4125 PHE n 
1 4126 LEU n 
1 4127 THR n 
1 4128 MET n 
1 4129 GLU n 
1 4130 ILE n 
1 4131 ASN n 
1 4132 PRO n 
1 4133 LYS n 
1 4134 VAL n 
1 4135 PRO n 
1 4136 VAL n 
1 4137 ASN n 
1 4138 LEU n 
1 4139 LEU n 
1 4140 ARG n 
1 4141 ALA n 
1 4142 GLY n 
1 4143 ARG n 
1 4144 ILE n 
1 4145 PHE n 
1 4146 VAL n 
1 4147 PHE n 
1 4148 GLU n 
1 4149 PRO n 
1 4150 PRO n 
1 4151 PRO n 
1 4152 GLY n 
1 4153 VAL n 
1 4154 LYS n 
1 4155 ALA n 
1 4156 ASN n 
1 4157 MET n 
1 4158 LEU n 
1 4159 ARG n 
1 4160 THR n 
1 4161 PHE n 
1 4162 SER n 
1 4163 SER n 
1 4164 ILE n 
1 4165 PRO n 
1 4166 VAL n 
1 4167 SER n 
1 4168 ARG n 
1 4169 ILE n 
1 4170 CYS n 
1 4171 LYS n 
1 4172 SER n 
1 4173 PRO n 
1 4174 ASN n 
1 4175 GLU n 
1 4176 ARG n 
1 4177 ALA n 
1 4178 ARG n 
1 4179 LEU n 
1 4180 TYR n 
1 4181 PHE n 
1 4182 LEU n 
1 4183 LEU n 
1 4184 ALA n 
1 4185 TRP n 
1 4186 PHE n 
1 4187 HIS n 
1 4188 ALA n 
1 4189 ILE n 
1 4190 ILE n 
1 4191 GLN n 
1 4192 GLU n 
1 4193 ARG n 
1 4194 LEU n 
1 4195 ARG n 
1 4196 TYR n 
1 4197 ALA n 
1 4198 PRO n 
1 4199 LEU n 
1 4200 GLY n 
1 4201 TRP n 
1 4202 SER n 
1 4203 LYS n 
1 4204 LYS n 
1 4205 TYR n 
1 4206 GLU n 
1 4207 PHE n 
1 4208 GLY n 
1 4209 GLU n 
1 4210 SER n 
1 4211 ASP n 
1 4212 LEU n 
1 4213 ARG n 
1 4214 SER n 
1 4215 ALA n 
1 4216 CYS n 
1 4217 ASP n 
1 4218 THR n 
1 4219 VAL n 
1 4220 ASP n 
1 4221 THR n 
1 4222 TRP n 
1 4223 LEU n 
1 4224 ASP n 
1 4225 ASP n 
1 4226 THR n 
1 4227 ALA n 
1 4228 LYS n 
1 4229 GLY n 
1 4230 ARG n 
1 4231 GLN n 
1 4232 ASN n 
1 4233 ILE n 
1 4234 SER n 
1 4235 PRO n 
1 4236 ASP n 
1 4237 LYS n 
1 4238 ILE n 
1 4239 PRO n 
1 4240 TRP n 
1 4241 SER n 
1 4242 ALA n 
1 4243 LEU n 
1 4244 LYS n 
1 4245 THR n 
1 4246 LEU n 
1 4247 MET n 
1 4248 ALA n 
1 4249 GLN n 
1 4250 SER n 
1 4251 ILE n 
1 4252 TYR n 
1 4253 GLY n 
1 4254 GLY n 
1 4255 ARG n 
1 4256 VAL n 
1 4257 ASP n 
1 4258 ASN n 
1 4259 GLU n 
1 4260 PHE n 
1 4261 ASP n 
1 4262 GLN n 
1 4263 ARG n 
1 4264 LEU n 
1 4265 LEU n 
1 4266 ASN n 
1 4267 THR n 
1 4268 PHE n 
1 4269 LEU n 
1 4270 GLU n 
1 4271 ARG n 
1 4272 LEU n 
1 4273 PHE n 
1 4274 THR n 
1 4275 THR n 
1 4276 ARG n 
1 4277 SER n 
1 4278 PHE n 
1 4279 ASP n 
1 4280 SER n 
1 4281 GLU n 
1 4282 PHE n 
1 4283 LYS n 
1 4284 LEU n 
1 4285 ALA n 
1 4286 CYS n 
1 4287 LYS n 
1 4288 VAL n 
1 4289 ASP n 
1 4290 GLY n 
1 4291 HIS n 
1 4292 LYS n 
1 4293 ASP n 
1 4294 ILE n 
1 4295 GLN n 
1 4296 MET n 
1 4297 PRO n 
1 4298 ASP n 
1 4299 GLY n 
1 4300 ILE n 
1 4301 ARG n 
1 4302 ARG n 
1 4303 GLU n 
1 4304 GLU n 
1 4305 PHE n 
1 4306 VAL n 
1 4307 GLN n 
1 4308 TRP n 
1 4309 VAL n 
1 4310 GLU n 
1 4311 LEU n 
1 4312 LEU n 
1 4313 PRO n 
1 4314 ASP n 
1 4315 THR n 
1 4316 GLN n 
1 4317 THR n 
1 4318 PRO n 
1 4319 SER n 
1 4320 TRP n 
1 4321 LEU n 
1 4322 GLY n 
1 4323 LEU n 
1 4324 PRO n 
1 4325 ASN n 
1 4326 ASN n 
1 4327 ALA n 
1 4328 GLU n 
1 4329 ARG n 
1 4330 VAL n 
1 4331 LEU n 
1 4332 LEU n 
1 4333 THR n 
1 4334 THR n 
1 4335 GLN n 
1 4336 GLY n 
1 4337 VAL n 
1 4338 ASP n 
1 4339 MET n 
1 4340 ILE n 
1 4341 SER n 
1 4342 LYS n 
1 4343 MET n 
1 4344 LEU n 
1 4345 LYS n 
1 4346 MET n 
1 4347 GLN n 
1 4348 MET n 
1 4349 LEU n 
1 4350 GLU n 
1 4351 ASP n 
1 4352 GLU n 
1 4353 ASP n 
1 4354 ASP n 
1 4355 LEU n 
1 4356 ALA n 
1 4357 TYR n 
1 4358 ALA n 
1 4359 GLU n 
1 4360 THR n 
1 4361 GLU n 
1 4362 LYS n 
1 4363 LYS n 
1 4364 THR n 
1 4365 ARG n 
1 4366 THR n 
1 4367 ASP n 
1 4368 SER n 
1 4369 THR n 
1 4370 SER n 
1 4371 ASP n 
1 4372 GLY n 
1 4373 ARG n 
1 4374 PRO n 
1 4375 ALA n 
1 4376 TRP n 
1 4377 MET n 
1 4378 ARG n 
1 4379 THR n 
1 4380 LEU n 
1 4381 HIS n 
1 4382 THR n 
1 4383 THR n 
1 4384 ALA n 
1 4385 SER n 
1 4386 ASN n 
1 4387 TRP n 
1 4388 LEU n 
1 4389 HIS n 
1 4390 LEU n 
1 4391 ILE n 
1 4392 PRO n 
1 4393 GLN n 
1 4394 THR n 
1 4395 LEU n 
1 4396 SER n 
1 4397 HIS n 
1 4398 LEU n 
1 4399 LYS n 
1 4400 ARG n 
1 4401 THR n 
1 4402 VAL n 
1 4403 GLU n 
1 4404 ASN n 
1 4405 ILE n 
1 4406 LYS n 
1 4407 ASP n 
1 4408 PRO n 
1 4409 LEU n 
1 4410 PHE n 
1 4411 ARG n 
1 4412 PHE n 
1 4413 PHE n 
1 4414 GLU n 
1 4415 ARG n 
1 4416 GLU n 
1 4417 VAL n 
1 4418 LYS n 
1 4419 MET n 
1 4420 GLY n 
1 4421 ALA n 
1 4422 LYS n 
1 4423 LEU n 
1 4424 LEU n 
1 4425 GLN n 
1 4426 ASP n 
1 4427 VAL n 
1 4428 ARG n 
1 4429 GLN n 
1 4430 ASP n 
1 4431 LEU n 
1 4432 ALA n 
1 4433 ASP n 
1 4434 VAL n 
1 4435 VAL n 
1 4436 GLN n 
1 4437 VAL n 
1 4438 CYS n 
1 4439 GLU n 
1 4440 GLY n 
1 4441 LYS n 
1 4442 LYS n 
1 4443 LYS n 
1 4444 GLN n 
1 4445 THR n 
1 4446 ASN n 
1 4447 TYR n 
1 4448 LEU n 
1 4449 ARG n 
1 4450 THR n 
1 4451 LEU n 
1 4452 ILE n 
1 4453 ASN n 
1 4454 GLU n 
1 4455 LEU n 
1 4456 VAL n 
1 4457 LYS n 
1 4458 GLY n 
1 4459 ILE n 
1 4460 LEU n 
1 4461 PRO n 
1 4462 ARG n 
1 4463 SER n 
1 4464 TRP n 
1 4465 SER n 
1 4466 HIS n 
1 4467 TYR n 
1 4468 THR n 
1 4469 VAL n 
1 4470 PRO n 
1 4471 ALA n 
1 4472 GLY n 
1 4473 MET n 
1 4474 THR n 
1 4475 VAL n 
1 4476 ILE n 
1 4477 GLN n 
1 4478 TRP n 
1 4479 VAL n 
1 4480 SER n 
1 4481 ASP n 
1 4482 PHE n 
1 4483 SER n 
1 4484 GLU n 
1 4485 ARG n 
1 4486 ILE n 
1 4487 LYS n 
1 4488 GLN n 
1 4489 LEU n 
1 4490 GLN n 
1 4491 ASN n 
1 4492 ILE n 
1 4493 SER n 
1 4494 LEU n 
1 4495 ALA n 
1 4496 ALA n 
1 4497 ALA n 
1 4498 SER n 
1 4499 GLY n 
1 4500 GLY n 
1 4501 ALA n 
1 4502 LYS n 
1 4503 GLU n 
1 4504 LEU n 
1 4505 LYS n 
1 4506 ASN n 
1 4507 ILE n 
1 4508 HIS n 
1 4509 VAL n 
1 4510 CYS n 
1 4511 LEU n 
1 4512 GLY n 
1 4513 GLY n 
1 4514 LEU n 
1 4515 PHE n 
1 4516 VAL n 
1 4517 PRO n 
1 4518 GLU n 
1 4519 ALA n 
1 4520 TYR n 
1 4521 ILE n 
1 4522 THR n 
1 4523 ALA n 
1 4524 THR n 
1 4525 ARG n 
1 4526 GLN n 
1 4527 TYR n 
1 4528 VAL n 
1 4529 ALA n 
1 4530 GLN n 
1 4531 ALA n 
1 4532 ASN n 
1 4533 SER n 
1 4534 TRP n 
1 4535 SER n 
1 4536 LEU n 
1 4537 GLU n 
1 4538 GLU n 
1 4539 LEU n 
1 4540 CYS n 
1 4541 LEU n 
1 4542 GLU n 
1 4543 VAL n 
1 4544 ASN n 
1 4545 VAL n 
1 4546 THR n 
1 4547 THR n 
1 4548 SER n 
1 4549 GLN n 
1 4550 GLY n 
1 4551 ALA n 
1 4552 THR n 
1 4553 LEU n 
1 4554 ASP n 
1 4555 ALA n 
1 4556 CYS n 
1 4557 SER n 
1 4558 PHE n 
1 4559 GLY n 
1 4560 VAL n 
1 4561 THR n 
1 4562 GLY n 
1 4563 LEU n 
1 4564 LYS n 
1 4565 LEU n 
1 4566 GLN n 
1 4567 GLY n 
1 4568 ALA n 
1 4569 THR n 
1 4570 CYS n 
1 4571 ASN n 
1 4572 ASN n 
1 4573 ASN n 
1 4574 LYS n 
1 4575 LEU n 
1 4576 SER n 
1 4577 LEU n 
1 4578 SER n 
1 4579 ASN n 
1 4580 ALA n 
1 4581 ILE n 
1 4582 SER n 
1 4583 THR n 
1 4584 ALA n 
1 4585 LEU n 
1 4586 PRO n 
1 4587 LEU n 
1 4588 THR n 
1 4589 GLN n 
1 4590 LEU n 
1 4591 ARG n 
1 4592 TRP n 
1 4593 VAL n 
1 4594 LYS n 
1 4595 GLN n 
1 4596 THR n 
1 4597 ASN n 
1 4598 THR n 
1 4599 GLU n 
1 4600 LYS n 
1 4601 LYS n 
1 4602 ALA n 
1 4603 SER n 
1 4604 VAL n 
1 4605 VAL n 
1 4606 THR n 
1 4607 LEU n 
1 4608 PRO n 
1 4609 VAL n 
1 4610 TYR n 
1 4611 LEU n 
1 4612 ASN n 
1 4613 PHE n 
1 4614 THR n 
1 4615 ARG n 
1 4616 ALA n 
1 4617 ASP n 
1 4618 LEU n 
1 4619 ILE n 
1 4620 PHE n 
1 4621 THR n 
1 4622 VAL n 
1 4623 ASP n 
1 4624 PHE n 
1 4625 GLU n 
1 4626 ILE n 
1 4627 ALA n 
1 4628 THR n 
1 4629 LYS n 
1 4630 GLU n 
1 4631 ASP n 
1 4632 PRO n 
1 4633 ARG n 
1 4634 SER n 
1 4635 PHE n 
1 4636 TYR n 
1 4637 GLU n 
1 4638 ARG n 
1 4639 GLY n 
1 4640 VAL n 
1 4641 ALA n 
1 4642 VAL n 
1 4643 LEU n 
1 4644 CYS n 
1 4645 THR n 
1 4646 GLU n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   4646 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'DYNC1H1, DHC1, DNCH1, DNCL, DNECL, DYHC, KIAA0325' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               'fall armyworm' 
_entity_src_gen.pdbx_host_org_scientific_name      'Spodoptera frugiperda' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     7108 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ADP non-polymer         n "ADENOSINE-5'-DIPHOSPHATE"  ? 'C10 H15 N5 O10 P2' 427.201 
ALA 'L-peptide linking' y ALANINE                     ? 'C3 H7 N O2'        89.093  
ARG 'L-peptide linking' y ARGININE                    ? 'C6 H15 N4 O2 1'    175.209 
ASN 'L-peptide linking' y ASPARAGINE                  ? 'C4 H8 N2 O3'       132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'             ? 'C4 H7 N O4'        133.103 
ATP non-polymer         . "ADENOSINE-5'-TRIPHOSPHATE" ? 'C10 H16 N5 O13 P3' 507.181 
CYS 'L-peptide linking' y CYSTEINE                    ? 'C3 H7 N O2 S'      121.158 
GLN 'L-peptide linking' y GLUTAMINE                   ? 'C5 H10 N2 O3'      146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'             ? 'C5 H9 N O4'        147.129 
GLY 'peptide linking'   y GLYCINE                     ? 'C2 H5 N O2'        75.067  
HIS 'L-peptide linking' y HISTIDINE                   ? 'C6 H10 N3 O2 1'    156.162 
ILE 'L-peptide linking' y ISOLEUCINE                  ? 'C6 H13 N O2'       131.173 
LEU 'L-peptide linking' y LEUCINE                     ? 'C6 H13 N O2'       131.173 
LYS 'L-peptide linking' y LYSINE                      ? 'C6 H15 N2 O2 1'    147.195 
MET 'L-peptide linking' y METHIONINE                  ? 'C5 H11 N O2 S'     149.211 
MG  non-polymer         . 'MAGNESIUM ION'             ? 'Mg 2'              24.305  
PHE 'L-peptide linking' y PHENYLALANINE               ? 'C9 H11 N O2'       165.189 
PRO 'L-peptide linking' y PROLINE                     ? 'C5 H9 N O2'        115.130 
SER 'L-peptide linking' y SERINE                      ? 'C3 H7 N O3'        105.093 
THR 'L-peptide linking' y THREONINE                   ? 'C4 H9 N O3'        119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                  ? 'C11 H12 N2 O2'     204.225 
TYR 'L-peptide linking' y TYROSINE                    ? 'C9 H11 N O3'       181.189 
VAL 'L-peptide linking' y VALINE                      ? 'C5 H11 N O2'       117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1    MET 1    1    ?    ?   ?   A . n 
A 1 2    SER 2    2    ?    ?   ?   A . n 
A 1 3    GLU 3    3    ?    ?   ?   A . n 
A 1 4    PRO 4    4    ?    ?   ?   A . n 
A 1 5    GLY 5    5    ?    ?   ?   A . n 
A 1 6    GLY 6    6    ?    ?   ?   A . n 
A 1 7    GLY 7    7    ?    ?   ?   A . n 
A 1 8    GLY 8    8    ?    ?   ?   A . n 
A 1 9    GLY 9    9    ?    ?   ?   A . n 
A 1 10   GLU 10   10   ?    ?   ?   A . n 
A 1 11   ASP 11   11   ?    ?   ?   A . n 
A 1 12   GLY 12   12   ?    ?   ?   A . n 
A 1 13   SER 13   13   ?    ?   ?   A . n 
A 1 14   ALA 14   14   ?    ?   ?   A . n 
A 1 15   GLY 15   15   ?    ?   ?   A . n 
A 1 16   LEU 16   16   ?    ?   ?   A . n 
A 1 17   GLU 17   17   ?    ?   ?   A . n 
A 1 18   VAL 18   18   ?    ?   ?   A . n 
A 1 19   SER 19   19   ?    ?   ?   A . n 
A 1 20   ALA 20   20   ?    ?   ?   A . n 
A 1 21   VAL 21   21   ?    ?   ?   A . n 
A 1 22   GLN 22   22   ?    ?   ?   A . n 
A 1 23   ASN 23   23   ?    ?   ?   A . n 
A 1 24   VAL 24   24   ?    ?   ?   A . n 
A 1 25   ALA 25   25   ?    ?   ?   A . n 
A 1 26   ASP 26   26   ?    ?   ?   A . n 
A 1 27   VAL 27   27   ?    ?   ?   A . n 
A 1 28   SER 28   28   ?    ?   ?   A . n 
A 1 29   VAL 29   29   ?    ?   ?   A . n 
A 1 30   LEU 30   30   ?    ?   ?   A . n 
A 1 31   GLN 31   31   ?    ?   ?   A . n 
A 1 32   LYS 32   32   ?    ?   ?   A . n 
A 1 33   HIS 33   33   ?    ?   ?   A . n 
A 1 34   LEU 34   34   ?    ?   ?   A . n 
A 1 35   ARG 35   35   ?    ?   ?   A . n 
A 1 36   LYS 36   36   ?    ?   ?   A . n 
A 1 37   LEU 37   37   ?    ?   ?   A . n 
A 1 38   VAL 38   38   ?    ?   ?   A . n 
A 1 39   PRO 39   39   ?    ?   ?   A . n 
A 1 40   LEU 40   40   ?    ?   ?   A . n 
A 1 41   LEU 41   41   ?    ?   ?   A . n 
A 1 42   LEU 42   42   ?    ?   ?   A . n 
A 1 43   GLU 43   43   ?    ?   ?   A . n 
A 1 44   ASP 44   44   ?    ?   ?   A . n 
A 1 45   GLY 45   45   ?    ?   ?   A . n 
A 1 46   GLY 46   46   ?    ?   ?   A . n 
A 1 47   GLU 47   47   ?    ?   ?   A . n 
A 1 48   ALA 48   48   ?    ?   ?   A . n 
A 1 49   PRO 49   49   ?    ?   ?   A . n 
A 1 50   ALA 50   50   ?    ?   ?   A . n 
A 1 51   ALA 51   51   ?    ?   ?   A . n 
A 1 52   LEU 52   52   ?    ?   ?   A . n 
A 1 53   GLU 53   53   ?    ?   ?   A . n 
A 1 54   ALA 54   54   ?    ?   ?   A . n 
A 1 55   ALA 55   55   ?    ?   ?   A . n 
A 1 56   LEU 56   56   ?    ?   ?   A . n 
A 1 57   GLU 57   57   ?    ?   ?   A . n 
A 1 58   GLU 58   58   ?    ?   ?   A . n 
A 1 59   LYS 59   59   ?    ?   ?   A . n 
A 1 60   SER 60   60   ?    ?   ?   A . n 
A 1 61   ALA 61   61   ?    ?   ?   A . n 
A 1 62   LEU 62   62   ?    ?   ?   A . n 
A 1 63   GLU 63   63   ?    ?   ?   A . n 
A 1 64   GLN 64   64   ?    ?   ?   A . n 
A 1 65   MET 65   65   ?    ?   ?   A . n 
A 1 66   ARG 66   66   ?    ?   ?   A . n 
A 1 67   LYS 67   67   ?    ?   ?   A . n 
A 1 68   PHE 68   68   ?    ?   ?   A . n 
A 1 69   LEU 69   69   ?    ?   ?   A . n 
A 1 70   SER 70   70   ?    ?   ?   A . n 
A 1 71   ASP 71   71   ?    ?   ?   A . n 
A 1 72   PRO 72   72   ?    ?   ?   A . n 
A 1 73   GLN 73   73   ?    ?   ?   A . n 
A 1 74   VAL 74   74   ?    ?   ?   A . n 
A 1 75   HIS 75   75   ?    ?   ?   A . n 
A 1 76   THR 76   76   ?    ?   ?   A . n 
A 1 77   VAL 77   77   ?    ?   ?   A . n 
A 1 78   LEU 78   78   ?    ?   ?   A . n 
A 1 79   VAL 79   79   ?    ?   ?   A . n 
A 1 80   GLU 80   80   ?    ?   ?   A . n 
A 1 81   ARG 81   81   ?    ?   ?   A . n 
A 1 82   SER 82   82   ?    ?   ?   A . n 
A 1 83   THR 83   83   ?    ?   ?   A . n 
A 1 84   LEU 84   84   ?    ?   ?   A . n 
A 1 85   LYS 85   85   ?    ?   ?   A . n 
A 1 86   GLU 86   86   ?    ?   ?   A . n 
A 1 87   ASP 87   87   ?    ?   ?   A . n 
A 1 88   VAL 88   88   ?    ?   ?   A . n 
A 1 89   GLY 89   89   ?    ?   ?   A . n 
A 1 90   ASP 90   90   ?    ?   ?   A . n 
A 1 91   GLU 91   91   ?    ?   ?   A . n 
A 1 92   GLY 92   92   ?    ?   ?   A . n 
A 1 93   GLU 93   93   ?    ?   ?   A . n 
A 1 94   GLU 94   94   ?    ?   ?   A . n 
A 1 95   GLU 95   95   ?    ?   ?   A . n 
A 1 96   LYS 96   96   ?    ?   ?   A . n 
A 1 97   GLU 97   97   ?    ?   ?   A . n 
A 1 98   PHE 98   98   ?    ?   ?   A . n 
A 1 99   ILE 99   99   ?    ?   ?   A . n 
A 1 100  SER 100  100  ?    ?   ?   A . n 
A 1 101  TYR 101  101  ?    ?   ?   A . n 
A 1 102  ASN 102  102  ?    ?   ?   A . n 
A 1 103  ILE 103  103  ?    ?   ?   A . n 
A 1 104  ASN 104  104  ?    ?   ?   A . n 
A 1 105  ILE 105  105  ?    ?   ?   A . n 
A 1 106  ASP 106  106  ?    ?   ?   A . n 
A 1 107  ILE 107  107  ?    ?   ?   A . n 
A 1 108  HIS 108  108  ?    ?   ?   A . n 
A 1 109  TYR 109  109  ?    ?   ?   A . n 
A 1 110  GLY 110  110  ?    ?   ?   A . n 
A 1 111  VAL 111  111  ?    ?   ?   A . n 
A 1 112  LYS 112  112  ?    ?   ?   A . n 
A 1 113  SER 113  113  ?    ?   ?   A . n 
A 1 114  ASN 114  114  ?    ?   ?   A . n 
A 1 115  SER 115  115  ?    ?   ?   A . n 
A 1 116  LEU 116  116  ?    ?   ?   A . n 
A 1 117  ALA 117  117  ?    ?   ?   A . n 
A 1 118  PHE 118  118  ?    ?   ?   A . n 
A 1 119  ILE 119  119  ?    ?   ?   A . n 
A 1 120  LYS 120  120  ?    ?   ?   A . n 
A 1 121  ARG 121  121  ?    ?   ?   A . n 
A 1 122  THR 122  122  ?    ?   ?   A . n 
A 1 123  PRO 123  123  ?    ?   ?   A . n 
A 1 124  VAL 124  124  ?    ?   ?   A . n 
A 1 125  ILE 125  125  ?    ?   ?   A . n 
A 1 126  ASP 126  126  ?    ?   ?   A . n 
A 1 127  ALA 127  127  ?    ?   ?   A . n 
A 1 128  ASP 128  128  ?    ?   ?   A . n 
A 1 129  LYS 129  129  ?    ?   ?   A . n 
A 1 130  PRO 130  130  ?    ?   ?   A . n 
A 1 131  VAL 131  131  ?    ?   ?   A . n 
A 1 132  SER 132  132  ?    ?   ?   A . n 
A 1 133  SER 133  133  ?    ?   ?   A . n 
A 1 134  GLN 134  134  ?    ?   ?   A . n 
A 1 135  LEU 135  135  ?    ?   ?   A . n 
A 1 136  ARG 136  136  ?    ?   ?   A . n 
A 1 137  VAL 137  137  ?    ?   ?   A . n 
A 1 138  LEU 138  138  ?    ?   ?   A . n 
A 1 139  THR 139  139  ?    ?   ?   A . n 
A 1 140  LEU 140  140  ?    ?   ?   A . n 
A 1 141  SER 141  141  ?    ?   ?   A . n 
A 1 142  GLU 142  142  ?    ?   ?   A . n 
A 1 143  ASP 143  143  ?    ?   ?   A . n 
A 1 144  SER 144  144  ?    ?   ?   A . n 
A 1 145  PRO 145  145  ?    ?   ?   A . n 
A 1 146  TYR 146  146  ?    ?   ?   A . n 
A 1 147  GLU 147  147  ?    ?   ?   A . n 
A 1 148  THR 148  148  ?    ?   ?   A . n 
A 1 149  LEU 149  149  ?    ?   ?   A . n 
A 1 150  HIS 150  150  ?    ?   ?   A . n 
A 1 151  SER 151  151  ?    ?   ?   A . n 
A 1 152  PHE 152  152  ?    ?   ?   A . n 
A 1 153  ILE 153  153  ?    ?   ?   A . n 
A 1 154  SER 154  154  ?    ?   ?   A . n 
A 1 155  ASN 155  155  ?    ?   ?   A . n 
A 1 156  ALA 156  156  ?    ?   ?   A . n 
A 1 157  VAL 157  157  ?    ?   ?   A . n 
A 1 158  ALA 158  158  ?    ?   ?   A . n 
A 1 159  PRO 159  159  ?    ?   ?   A . n 
A 1 160  PHE 160  160  ?    ?   ?   A . n 
A 1 161  PHE 161  161  ?    ?   ?   A . n 
A 1 162  LYS 162  162  ?    ?   ?   A . n 
A 1 163  SER 163  163  ?    ?   ?   A . n 
A 1 164  TYR 164  164  ?    ?   ?   A . n 
A 1 165  ILE 165  165  ?    ?   ?   A . n 
A 1 166  ARG 166  166  ?    ?   ?   A . n 
A 1 167  GLU 167  167  ?    ?   ?   A . n 
A 1 168  SER 168  168  ?    ?   ?   A . n 
A 1 169  GLY 169  169  ?    ?   ?   A . n 
A 1 170  LYS 170  170  ?    ?   ?   A . n 
A 1 171  ALA 171  171  ?    ?   ?   A . n 
A 1 172  ASP 172  172  ?    ?   ?   A . n 
A 1 173  ARG 173  173  ?    ?   ?   A . n 
A 1 174  ASP 174  174  ?    ?   ?   A . n 
A 1 175  GLY 175  175  ?    ?   ?   A . n 
A 1 176  ASP 176  176  ?    ?   ?   A . n 
A 1 177  LYS 177  177  ?    ?   ?   A . n 
A 1 178  MET 178  178  ?    ?   ?   A . n 
A 1 179  ALA 179  179  ?    ?   ?   A . n 
A 1 180  PRO 180  180  ?    ?   ?   A . n 
A 1 181  SER 181  181  ?    ?   ?   A . n 
A 1 182  VAL 182  182  ?    ?   ?   A . n 
A 1 183  GLU 183  183  ?    ?   ?   A . n 
A 1 184  LYS 184  184  ?    ?   ?   A . n 
A 1 185  LYS 185  185  ?    ?   ?   A . n 
A 1 186  ILE 186  186  ?    ?   ?   A . n 
A 1 187  ALA 187  187  ?    ?   ?   A . n 
A 1 188  GLU 188  188  ?    ?   ?   A . n 
A 1 189  LEU 189  189  ?    ?   ?   A . n 
A 1 190  GLU 190  190  ?    ?   ?   A . n 
A 1 191  MET 191  191  ?    ?   ?   A . n 
A 1 192  GLY 192  192  ?    ?   ?   A . n 
A 1 193  LEU 193  193  ?    ?   ?   A . n 
A 1 194  LEU 194  194  ?    ?   ?   A . n 
A 1 195  HIS 195  195  ?    ?   ?   A . n 
A 1 196  LEU 196  196  ?    ?   ?   A . n 
A 1 197  GLN 197  197  ?    ?   ?   A . n 
A 1 198  GLN 198  198  ?    ?   ?   A . n 
A 1 199  ASN 199  199  ?    ?   ?   A . n 
A 1 200  ILE 200  200  ?    ?   ?   A . n 
A 1 201  GLU 201  201  ?    ?   ?   A . n 
A 1 202  ILE 202  202  ?    ?   ?   A . n 
A 1 203  PRO 203  203  ?    ?   ?   A . n 
A 1 204  GLU 204  204  ?    ?   ?   A . n 
A 1 205  ILE 205  205  ?    ?   ?   A . n 
A 1 206  SER 206  206  ?    ?   ?   A . n 
A 1 207  LEU 207  207  ?    ?   ?   A . n 
A 1 208  PRO 208  208  ?    ?   ?   A . n 
A 1 209  ILE 209  209  ?    ?   ?   A . n 
A 1 210  HIS 210  210  ?    ?   ?   A . n 
A 1 211  PRO 211  211  ?    ?   ?   A . n 
A 1 212  MET 212  212  ?    ?   ?   A . n 
A 1 213  ILE 213  213  ?    ?   ?   A . n 
A 1 214  THR 214  214  ?    ?   ?   A . n 
A 1 215  ASN 215  215  ?    ?   ?   A . n 
A 1 216  VAL 216  216  ?    ?   ?   A . n 
A 1 217  ALA 217  217  ?    ?   ?   A . n 
A 1 218  LYS 218  218  ?    ?   ?   A . n 
A 1 219  GLN 219  219  ?    ?   ?   A . n 
A 1 220  CYS 220  220  ?    ?   ?   A . n 
A 1 221  TYR 221  221  ?    ?   ?   A . n 
A 1 222  GLU 222  222  ?    ?   ?   A . n 
A 1 223  ARG 223  223  ?    ?   ?   A . n 
A 1 224  GLY 224  224  ?    ?   ?   A . n 
A 1 225  GLU 225  225  ?    ?   ?   A . n 
A 1 226  LYS 226  226  ?    ?   ?   A . n 
A 1 227  PRO 227  227  ?    ?   ?   A . n 
A 1 228  LYS 228  228  ?    ?   ?   A . n 
A 1 229  VAL 229  229  ?    ?   ?   A . n 
A 1 230  THR 230  230  ?    ?   ?   A . n 
A 1 231  ASP 231  231  ?    ?   ?   A . n 
A 1 232  PHE 232  232  ?    ?   ?   A . n 
A 1 233  GLY 233  233  ?    ?   ?   A . n 
A 1 234  ASP 234  234  ?    ?   ?   A . n 
A 1 235  LYS 235  235  ?    ?   ?   A . n 
A 1 236  VAL 236  236  ?    ?   ?   A . n 
A 1 237  GLU 237  237  ?    ?   ?   A . n 
A 1 238  ASP 238  238  ?    ?   ?   A . n 
A 1 239  PRO 239  239  ?    ?   ?   A . n 
A 1 240  THR 240  240  ?    ?   ?   A . n 
A 1 241  PHE 241  241  ?    ?   ?   A . n 
A 1 242  LEU 242  242  ?    ?   ?   A . n 
A 1 243  ASN 243  243  ?    ?   ?   A . n 
A 1 244  GLN 244  244  ?    ?   ?   A . n 
A 1 245  LEU 245  245  ?    ?   ?   A . n 
A 1 246  GLN 246  246  ?    ?   ?   A . n 
A 1 247  SER 247  247  ?    ?   ?   A . n 
A 1 248  GLY 248  248  ?    ?   ?   A . n 
A 1 249  VAL 249  249  ?    ?   ?   A . n 
A 1 250  ASN 250  250  ?    ?   ?   A . n 
A 1 251  ARG 251  251  ?    ?   ?   A . n 
A 1 252  TRP 252  252  ?    ?   ?   A . n 
A 1 253  ILE 253  253  ?    ?   ?   A . n 
A 1 254  ARG 254  254  ?    ?   ?   A . n 
A 1 255  GLU 255  255  ?    ?   ?   A . n 
A 1 256  ILE 256  256  ?    ?   ?   A . n 
A 1 257  GLN 257  257  ?    ?   ?   A . n 
A 1 258  LYS 258  258  ?    ?   ?   A . n 
A 1 259  VAL 259  259  ?    ?   ?   A . n 
A 1 260  THR 260  260  ?    ?   ?   A . n 
A 1 261  LYS 261  261  ?    ?   ?   A . n 
A 1 262  LEU 262  262  ?    ?   ?   A . n 
A 1 263  ASP 263  263  ?    ?   ?   A . n 
A 1 264  ARG 264  264  ?    ?   ?   A . n 
A 1 265  ASP 265  265  ?    ?   ?   A . n 
A 1 266  PRO 266  266  ?    ?   ?   A . n 
A 1 267  ALA 267  267  ?    ?   ?   A . n 
A 1 268  SER 268  268  ?    ?   ?   A . n 
A 1 269  GLY 269  269  ?    ?   ?   A . n 
A 1 270  THR 270  270  ?    ?   ?   A . n 
A 1 271  ALA 271  271  ?    ?   ?   A . n 
A 1 272  LEU 272  272  ?    ?   ?   A . n 
A 1 273  GLN 273  273  ?    ?   ?   A . n 
A 1 274  GLU 274  274  ?    ?   ?   A . n 
A 1 275  ILE 275  275  ?    ?   ?   A . n 
A 1 276  SER 276  276  ?    ?   ?   A . n 
A 1 277  PHE 277  277  ?    ?   ?   A . n 
A 1 278  TRP 278  278  ?    ?   ?   A . n 
A 1 279  LEU 279  279  ?    ?   ?   A . n 
A 1 280  ASN 280  280  ?    ?   ?   A . n 
A 1 281  LEU 281  281  ?    ?   ?   A . n 
A 1 282  GLU 282  282  ?    ?   ?   A . n 
A 1 283  ARG 283  283  ?    ?   ?   A . n 
A 1 284  ALA 284  284  ?    ?   ?   A . n 
A 1 285  LEU 285  285  ?    ?   ?   A . n 
A 1 286  TYR 286  286  ?    ?   ?   A . n 
A 1 287  ARG 287  287  ?    ?   ?   A . n 
A 1 288  ILE 288  288  ?    ?   ?   A . n 
A 1 289  GLN 289  289  ?    ?   ?   A . n 
A 1 290  GLU 290  290  ?    ?   ?   A . n 
A 1 291  LYS 291  291  ?    ?   ?   A . n 
A 1 292  ARG 292  292  ?    ?   ?   A . n 
A 1 293  GLU 293  293  ?    ?   ?   A . n 
A 1 294  SER 294  294  ?    ?   ?   A . n 
A 1 295  PRO 295  295  ?    ?   ?   A . n 
A 1 296  GLU 296  296  ?    ?   ?   A . n 
A 1 297  VAL 297  297  ?    ?   ?   A . n 
A 1 298  LEU 298  298  ?    ?   ?   A . n 
A 1 299  LEU 299  299  ?    ?   ?   A . n 
A 1 300  THR 300  300  ?    ?   ?   A . n 
A 1 301  LEU 301  301  ?    ?   ?   A . n 
A 1 302  ASP 302  302  ?    ?   ?   A . n 
A 1 303  ILE 303  303  ?    ?   ?   A . n 
A 1 304  LEU 304  304  ?    ?   ?   A . n 
A 1 305  LYS 305  305  ?    ?   ?   A . n 
A 1 306  HIS 306  306  ?    ?   ?   A . n 
A 1 307  GLY 307  307  ?    ?   ?   A . n 
A 1 308  LYS 308  308  ?    ?   ?   A . n 
A 1 309  ARG 309  309  ?    ?   ?   A . n 
A 1 310  PHE 310  310  ?    ?   ?   A . n 
A 1 311  HIS 311  311  ?    ?   ?   A . n 
A 1 312  ALA 312  312  ?    ?   ?   A . n 
A 1 313  THR 313  313  ?    ?   ?   A . n 
A 1 314  VAL 314  314  ?    ?   ?   A . n 
A 1 315  SER 315  315  ?    ?   ?   A . n 
A 1 316  PHE 316  316  ?    ?   ?   A . n 
A 1 317  ASP 317  317  ?    ?   ?   A . n 
A 1 318  THR 318  318  ?    ?   ?   A . n 
A 1 319  ASP 319  319  ?    ?   ?   A . n 
A 1 320  THR 320  320  ?    ?   ?   A . n 
A 1 321  GLY 321  321  ?    ?   ?   A . n 
A 1 322  LEU 322  322  ?    ?   ?   A . n 
A 1 323  LYS 323  323  ?    ?   ?   A . n 
A 1 324  GLN 324  324  ?    ?   ?   A . n 
A 1 325  ALA 325  325  ?    ?   ?   A . n 
A 1 326  LEU 326  326  ?    ?   ?   A . n 
A 1 327  GLU 327  327  ?    ?   ?   A . n 
A 1 328  THR 328  328  ?    ?   ?   A . n 
A 1 329  VAL 329  329  ?    ?   ?   A . n 
A 1 330  ASN 330  330  ?    ?   ?   A . n 
A 1 331  ASP 331  331  ?    ?   ?   A . n 
A 1 332  TYR 332  332  ?    ?   ?   A . n 
A 1 333  ASN 333  333  ?    ?   ?   A . n 
A 1 334  PRO 334  334  ?    ?   ?   A . n 
A 1 335  LEU 335  335  ?    ?   ?   A . n 
A 1 336  MET 336  336  ?    ?   ?   A . n 
A 1 337  LYS 337  337  ?    ?   ?   A . n 
A 1 338  ASP 338  338  ?    ?   ?   A . n 
A 1 339  PHE 339  339  ?    ?   ?   A . n 
A 1 340  PRO 340  340  ?    ?   ?   A . n 
A 1 341  LEU 341  341  ?    ?   ?   A . n 
A 1 342  ASN 342  342  ?    ?   ?   A . n 
A 1 343  ASP 343  343  ?    ?   ?   A . n 
A 1 344  LEU 344  344  ?    ?   ?   A . n 
A 1 345  LEU 345  345  ?    ?   ?   A . n 
A 1 346  SER 346  346  ?    ?   ?   A . n 
A 1 347  ALA 347  347  ?    ?   ?   A . n 
A 1 348  THR 348  348  ?    ?   ?   A . n 
A 1 349  GLU 349  349  ?    ?   ?   A . n 
A 1 350  LEU 350  350  ?    ?   ?   A . n 
A 1 351  ASP 351  351  ?    ?   ?   A . n 
A 1 352  LYS 352  352  ?    ?   ?   A . n 
A 1 353  ILE 353  353  ?    ?   ?   A . n 
A 1 354  ARG 354  354  ?    ?   ?   A . n 
A 1 355  GLN 355  355  ?    ?   ?   A . n 
A 1 356  ALA 356  356  ?    ?   ?   A . n 
A 1 357  LEU 357  357  ?    ?   ?   A . n 
A 1 358  VAL 358  358  ?    ?   ?   A . n 
A 1 359  ALA 359  359  ?    ?   ?   A . n 
A 1 360  ILE 360  360  ?    ?   ?   A . n 
A 1 361  PHE 361  361  ?    ?   ?   A . n 
A 1 362  THR 362  362  ?    ?   ?   A . n 
A 1 363  HIS 363  363  ?    ?   ?   A . n 
A 1 364  LEU 364  364  ?    ?   ?   A . n 
A 1 365  ARG 365  365  ?    ?   ?   A . n 
A 1 366  LYS 366  366  ?    ?   ?   A . n 
A 1 367  ILE 367  367  ?    ?   ?   A . n 
A 1 368  ARG 368  368  ?    ?   ?   A . n 
A 1 369  ASN 369  369  ?    ?   ?   A . n 
A 1 370  THR 370  370  ?    ?   ?   A . n 
A 1 371  LYS 371  371  ?    ?   ?   A . n 
A 1 372  TYR 372  372  ?    ?   ?   A . n 
A 1 373  PRO 373  373  ?    ?   ?   A . n 
A 1 374  ILE 374  374  ?    ?   ?   A . n 
A 1 375  GLN 375  375  ?    ?   ?   A . n 
A 1 376  ARG 376  376  ?    ?   ?   A . n 
A 1 377  ALA 377  377  ?    ?   ?   A . n 
A 1 378  LEU 378  378  ?    ?   ?   A . n 
A 1 379  ARG 379  379  ?    ?   ?   A . n 
A 1 380  LEU 380  380  ?    ?   ?   A . n 
A 1 381  VAL 381  381  ?    ?   ?   A . n 
A 1 382  GLU 382  382  ?    ?   ?   A . n 
A 1 383  ALA 383  383  ?    ?   ?   A . n 
A 1 384  ILE 384  384  ?    ?   ?   A . n 
A 1 385  SER 385  385  ?    ?   ?   A . n 
A 1 386  ARG 386  386  ?    ?   ?   A . n 
A 1 387  ASP 387  387  ?    ?   ?   A . n 
A 1 388  LEU 388  388  ?    ?   ?   A . n 
A 1 389  SER 389  389  ?    ?   ?   A . n 
A 1 390  SER 390  390  ?    ?   ?   A . n 
A 1 391  GLN 391  391  ?    ?   ?   A . n 
A 1 392  LEU 392  392  ?    ?   ?   A . n 
A 1 393  LEU 393  393  ?    ?   ?   A . n 
A 1 394  LYS 394  394  ?    ?   ?   A . n 
A 1 395  VAL 395  395  ?    ?   ?   A . n 
A 1 396  LEU 396  396  ?    ?   ?   A . n 
A 1 397  GLY 397  397  ?    ?   ?   A . n 
A 1 398  THR 398  398  ?    ?   ?   A . n 
A 1 399  ARG 399  399  ?    ?   ?   A . n 
A 1 400  LYS 400  400  ?    ?   ?   A . n 
A 1 401  LEU 401  401  ?    ?   ?   A . n 
A 1 402  MET 402  402  ?    ?   ?   A . n 
A 1 403  HIS 403  403  ?    ?   ?   A . n 
A 1 404  VAL 404  404  ?    ?   ?   A . n 
A 1 405  ALA 405  405  ?    ?   ?   A . n 
A 1 406  TYR 406  406  ?    ?   ?   A . n 
A 1 407  GLU 407  407  ?    ?   ?   A . n 
A 1 408  GLU 408  408  ?    ?   ?   A . n 
A 1 409  PHE 409  409  ?    ?   ?   A . n 
A 1 410  GLU 410  410  ?    ?   ?   A . n 
A 1 411  LYS 411  411  ?    ?   ?   A . n 
A 1 412  VAL 412  412  ?    ?   ?   A . n 
A 1 413  MET 413  413  ?    ?   ?   A . n 
A 1 414  VAL 414  414  ?    ?   ?   A . n 
A 1 415  ALA 415  415  ?    ?   ?   A . n 
A 1 416  CYS 416  416  ?    ?   ?   A . n 
A 1 417  PHE 417  417  ?    ?   ?   A . n 
A 1 418  GLU 418  418  ?    ?   ?   A . n 
A 1 419  VAL 419  419  ?    ?   ?   A . n 
A 1 420  PHE 420  420  ?    ?   ?   A . n 
A 1 421  GLN 421  421  ?    ?   ?   A . n 
A 1 422  THR 422  422  ?    ?   ?   A . n 
A 1 423  TRP 423  423  ?    ?   ?   A . n 
A 1 424  ASP 424  424  ?    ?   ?   A . n 
A 1 425  ASP 425  425  ?    ?   ?   A . n 
A 1 426  GLU 426  426  ?    ?   ?   A . n 
A 1 427  TYR 427  427  ?    ?   ?   A . n 
A 1 428  GLU 428  428  ?    ?   ?   A . n 
A 1 429  LYS 429  429  ?    ?   ?   A . n 
A 1 430  LEU 430  430  ?    ?   ?   A . n 
A 1 431  GLN 431  431  ?    ?   ?   A . n 
A 1 432  VAL 432  432  ?    ?   ?   A . n 
A 1 433  LEU 433  433  ?    ?   ?   A . n 
A 1 434  LEU 434  434  ?    ?   ?   A . n 
A 1 435  ARG 435  435  ?    ?   ?   A . n 
A 1 436  ASP 436  436  ?    ?   ?   A . n 
A 1 437  ILE 437  437  ?    ?   ?   A . n 
A 1 438  VAL 438  438  ?    ?   ?   A . n 
A 1 439  LYS 439  439  ?    ?   ?   A . n 
A 1 440  ARG 440  440  ?    ?   ?   A . n 
A 1 441  LYS 441  441  ?    ?   ?   A . n 
A 1 442  ARG 442  442  ?    ?   ?   A . n 
A 1 443  GLU 443  443  ?    ?   ?   A . n 
A 1 444  GLU 444  444  ?    ?   ?   A . n 
A 1 445  ASN 445  445  ?    ?   ?   A . n 
A 1 446  LEU 446  446  ?    ?   ?   A . n 
A 1 447  LYS 447  447  ?    ?   ?   A . n 
A 1 448  MET 448  448  ?    ?   ?   A . n 
A 1 449  VAL 449  449  ?    ?   ?   A . n 
A 1 450  TRP 450  450  ?    ?   ?   A . n 
A 1 451  ARG 451  451  ?    ?   ?   A . n 
A 1 452  ILE 452  452  ?    ?   ?   A . n 
A 1 453  ASN 453  453  ?    ?   ?   A . n 
A 1 454  PRO 454  454  ?    ?   ?   A . n 
A 1 455  ALA 455  455  ?    ?   ?   A . n 
A 1 456  HIS 456  456  ?    ?   ?   A . n 
A 1 457  ARG 457  457  ?    ?   ?   A . n 
A 1 458  LYS 458  458  ?    ?   ?   A . n 
A 1 459  LEU 459  459  ?    ?   ?   A . n 
A 1 460  GLN 460  460  ?    ?   ?   A . n 
A 1 461  ALA 461  461  ?    ?   ?   A . n 
A 1 462  ARG 462  462  ?    ?   ?   A . n 
A 1 463  LEU 463  463  ?    ?   ?   A . n 
A 1 464  ASP 464  464  ?    ?   ?   A . n 
A 1 465  GLN 465  465  ?    ?   ?   A . n 
A 1 466  MET 466  466  ?    ?   ?   A . n 
A 1 467  ARG 467  467  ?    ?   ?   A . n 
A 1 468  LYS 468  468  ?    ?   ?   A . n 
A 1 469  PHE 469  469  ?    ?   ?   A . n 
A 1 470  ARG 470  470  ?    ?   ?   A . n 
A 1 471  ARG 471  471  ?    ?   ?   A . n 
A 1 472  GLN 472  472  ?    ?   ?   A . n 
A 1 473  HIS 473  473  ?    ?   ?   A . n 
A 1 474  GLU 474  474  ?    ?   ?   A . n 
A 1 475  GLN 475  475  ?    ?   ?   A . n 
A 1 476  LEU 476  476  ?    ?   ?   A . n 
A 1 477  ARG 477  477  ?    ?   ?   A . n 
A 1 478  ALA 478  478  ?    ?   ?   A . n 
A 1 479  VAL 479  479  ?    ?   ?   A . n 
A 1 480  ILE 480  480  ?    ?   ?   A . n 
A 1 481  VAL 481  481  ?    ?   ?   A . n 
A 1 482  ARG 482  482  ?    ?   ?   A . n 
A 1 483  VAL 483  483  ?    ?   ?   A . n 
A 1 484  LEU 484  484  ?    ?   ?   A . n 
A 1 485  ARG 485  485  ?    ?   ?   A . n 
A 1 486  PRO 486  486  ?    ?   ?   A . n 
A 1 487  GLN 487  487  ?    ?   ?   A . n 
A 1 488  VAL 488  488  ?    ?   ?   A . n 
A 1 489  THR 489  489  ?    ?   ?   A . n 
A 1 490  ALA 490  490  ?    ?   ?   A . n 
A 1 491  VAL 491  491  ?    ?   ?   A . n 
A 1 492  ALA 492  492  ?    ?   ?   A . n 
A 1 493  GLN 493  493  ?    ?   ?   A . n 
A 1 494  GLN 494  494  ?    ?   ?   A . n 
A 1 495  ASN 495  495  ?    ?   ?   A . n 
A 1 496  GLN 496  496  ?    ?   ?   A . n 
A 1 497  GLY 497  497  ?    ?   ?   A . n 
A 1 498  GLU 498  498  ?    ?   ?   A . n 
A 1 499  VAL 499  499  ?    ?   ?   A . n 
A 1 500  PRO 500  500  ?    ?   ?   A . n 
A 1 501  GLU 501  501  ?    ?   ?   A . n 
A 1 502  PRO 502  502  ?    ?   ?   A . n 
A 1 503  GLN 503  503  ?    ?   ?   A . n 
A 1 504  ASP 504  504  ?    ?   ?   A . n 
A 1 505  MET 505  505  ?    ?   ?   A . n 
A 1 506  LYS 506  506  ?    ?   ?   A . n 
A 1 507  VAL 507  507  ?    ?   ?   A . n 
A 1 508  ALA 508  508  ?    ?   ?   A . n 
A 1 509  GLU 509  509  ?    ?   ?   A . n 
A 1 510  VAL 510  510  ?    ?   ?   A . n 
A 1 511  LEU 511  511  ?    ?   ?   A . n 
A 1 512  PHE 512  512  ?    ?   ?   A . n 
A 1 513  ASP 513  513  ?    ?   ?   A . n 
A 1 514  ALA 514  514  ?    ?   ?   A . n 
A 1 515  ALA 515  515  ?    ?   ?   A . n 
A 1 516  ASP 516  516  ?    ?   ?   A . n 
A 1 517  ALA 517  517  ?    ?   ?   A . n 
A 1 518  ASN 518  518  ?    ?   ?   A . n 
A 1 519  ALA 519  519  ?    ?   ?   A . n 
A 1 520  ILE 520  520  ?    ?   ?   A . n 
A 1 521  GLU 521  521  ?    ?   ?   A . n 
A 1 522  GLU 522  522  ?    ?   ?   A . n 
A 1 523  VAL 523  523  ?    ?   ?   A . n 
A 1 524  ASN 524  524  ?    ?   ?   A . n 
A 1 525  LEU 525  525  ?    ?   ?   A . n 
A 1 526  ALA 526  526  ?    ?   ?   A . n 
A 1 527  TYR 527  527  ?    ?   ?   A . n 
A 1 528  GLU 528  528  ?    ?   ?   A . n 
A 1 529  ASN 529  529  ?    ?   ?   A . n 
A 1 530  VAL 530  530  ?    ?   ?   A . n 
A 1 531  LYS 531  531  ?    ?   ?   A . n 
A 1 532  GLU 532  532  ?    ?   ?   A . n 
A 1 533  VAL 533  533  ?    ?   ?   A . n 
A 1 534  ASP 534  534  ?    ?   ?   A . n 
A 1 535  GLY 535  535  ?    ?   ?   A . n 
A 1 536  LEU 536  536  ?    ?   ?   A . n 
A 1 537  ASP 537  537  ?    ?   ?   A . n 
A 1 538  VAL 538  538  ?    ?   ?   A . n 
A 1 539  SER 539  539  ?    ?   ?   A . n 
A 1 540  LYS 540  540  ?    ?   ?   A . n 
A 1 541  GLU 541  541  ?    ?   ?   A . n 
A 1 542  GLY 542  542  ?    ?   ?   A . n 
A 1 543  THR 543  543  ?    ?   ?   A . n 
A 1 544  GLU 544  544  ?    ?   ?   A . n 
A 1 545  ALA 545  545  ?    ?   ?   A . n 
A 1 546  TRP 546  546  ?    ?   ?   A . n 
A 1 547  GLU 547  547  ?    ?   ?   A . n 
A 1 548  ALA 548  548  ?    ?   ?   A . n 
A 1 549  ALA 549  549  ?    ?   ?   A . n 
A 1 550  MET 550  550  ?    ?   ?   A . n 
A 1 551  LYS 551  551  ?    ?   ?   A . n 
A 1 552  ARG 552  552  ?    ?   ?   A . n 
A 1 553  TYR 553  553  ?    ?   ?   A . n 
A 1 554  ASP 554  554  ?    ?   ?   A . n 
A 1 555  GLU 555  555  ?    ?   ?   A . n 
A 1 556  ARG 556  556  ?    ?   ?   A . n 
A 1 557  ILE 557  557  ?    ?   ?   A . n 
A 1 558  ASP 558  558  ?    ?   ?   A . n 
A 1 559  ARG 559  559  ?    ?   ?   A . n 
A 1 560  VAL 560  560  ?    ?   ?   A . n 
A 1 561  GLU 561  561  ?    ?   ?   A . n 
A 1 562  THR 562  562  ?    ?   ?   A . n 
A 1 563  ARG 563  563  ?    ?   ?   A . n 
A 1 564  ILE 564  564  ?    ?   ?   A . n 
A 1 565  THR 565  565  ?    ?   ?   A . n 
A 1 566  ALA 566  566  ?    ?   ?   A . n 
A 1 567  ARG 567  567  ?    ?   ?   A . n 
A 1 568  LEU 568  568  ?    ?   ?   A . n 
A 1 569  ARG 569  569  ?    ?   ?   A . n 
A 1 570  ASP 570  570  ?    ?   ?   A . n 
A 1 571  GLN 571  571  ?    ?   ?   A . n 
A 1 572  LEU 572  572  ?    ?   ?   A . n 
A 1 573  GLY 573  573  ?    ?   ?   A . n 
A 1 574  THR 574  574  ?    ?   ?   A . n 
A 1 575  ALA 575  575  ?    ?   ?   A . n 
A 1 576  LYS 576  576  ?    ?   ?   A . n 
A 1 577  ASN 577  577  ?    ?   ?   A . n 
A 1 578  ALA 578  578  ?    ?   ?   A . n 
A 1 579  ASN 579  579  ?    ?   ?   A . n 
A 1 580  GLU 580  580  ?    ?   ?   A . n 
A 1 581  MET 581  581  ?    ?   ?   A . n 
A 1 582  PHE 582  582  ?    ?   ?   A . n 
A 1 583  ARG 583  583  ?    ?   ?   A . n 
A 1 584  ILE 584  584  ?    ?   ?   A . n 
A 1 585  PHE 585  585  ?    ?   ?   A . n 
A 1 586  SER 586  586  ?    ?   ?   A . n 
A 1 587  ARG 587  587  ?    ?   ?   A . n 
A 1 588  PHE 588  588  ?    ?   ?   A . n 
A 1 589  ASN 589  589  ?    ?   ?   A . n 
A 1 590  ALA 590  590  ?    ?   ?   A . n 
A 1 591  LEU 591  591  ?    ?   ?   A . n 
A 1 592  PHE 592  592  ?    ?   ?   A . n 
A 1 593  VAL 593  593  ?    ?   ?   A . n 
A 1 594  ARG 594  594  ?    ?   ?   A . n 
A 1 595  PRO 595  595  ?    ?   ?   A . n 
A 1 596  HIS 596  596  ?    ?   ?   A . n 
A 1 597  ILE 597  597  ?    ?   ?   A . n 
A 1 598  ARG 598  598  ?    ?   ?   A . n 
A 1 599  GLY 599  599  ?    ?   ?   A . n 
A 1 600  ALA 600  600  ?    ?   ?   A . n 
A 1 601  ILE 601  601  ?    ?   ?   A . n 
A 1 602  ARG 602  602  ?    ?   ?   A . n 
A 1 603  GLU 603  603  ?    ?   ?   A . n 
A 1 604  TYR 604  604  ?    ?   ?   A . n 
A 1 605  GLN 605  605  ?    ?   ?   A . n 
A 1 606  THR 606  606  ?    ?   ?   A . n 
A 1 607  GLN 607  607  ?    ?   ?   A . n 
A 1 608  LEU 608  608  ?    ?   ?   A . n 
A 1 609  ILE 609  609  ?    ?   ?   A . n 
A 1 610  GLN 610  610  ?    ?   ?   A . n 
A 1 611  ARG 611  611  ?    ?   ?   A . n 
A 1 612  VAL 612  612  ?    ?   ?   A . n 
A 1 613  LYS 613  613  ?    ?   ?   A . n 
A 1 614  ASP 614  614  ?    ?   ?   A . n 
A 1 615  ASP 615  615  ?    ?   ?   A . n 
A 1 616  ILE 616  616  ?    ?   ?   A . n 
A 1 617  GLU 617  617  ?    ?   ?   A . n 
A 1 618  SER 618  618  ?    ?   ?   A . n 
A 1 619  LEU 619  619  ?    ?   ?   A . n 
A 1 620  HIS 620  620  ?    ?   ?   A . n 
A 1 621  ASP 621  621  ?    ?   ?   A . n 
A 1 622  LYS 622  622  ?    ?   ?   A . n 
A 1 623  PHE 623  623  ?    ?   ?   A . n 
A 1 624  LYS 624  624  ?    ?   ?   A . n 
A 1 625  VAL 625  625  ?    ?   ?   A . n 
A 1 626  GLN 626  626  ?    ?   ?   A . n 
A 1 627  TYR 627  627  ?    ?   ?   A . n 
A 1 628  PRO 628  628  ?    ?   ?   A . n 
A 1 629  GLN 629  629  ?    ?   ?   A . n 
A 1 630  SER 630  630  ?    ?   ?   A . n 
A 1 631  GLN 631  631  ?    ?   ?   A . n 
A 1 632  ALA 632  632  ?    ?   ?   A . n 
A 1 633  CYS 633  633  ?    ?   ?   A . n 
A 1 634  LYS 634  634  ?    ?   ?   A . n 
A 1 635  MET 635  635  ?    ?   ?   A . n 
A 1 636  SER 636  636  ?    ?   ?   A . n 
A 1 637  HIS 637  637  ?    ?   ?   A . n 
A 1 638  VAL 638  638  ?    ?   ?   A . n 
A 1 639  ARG 639  639  ?    ?   ?   A . n 
A 1 640  ASP 640  640  ?    ?   ?   A . n 
A 1 641  LEU 641  641  ?    ?   ?   A . n 
A 1 642  PRO 642  642  ?    ?   ?   A . n 
A 1 643  PRO 643  643  ?    ?   ?   A . n 
A 1 644  VAL 644  644  ?    ?   ?   A . n 
A 1 645  SER 645  645  ?    ?   ?   A . n 
A 1 646  GLY 646  646  ?    ?   ?   A . n 
A 1 647  SER 647  647  ?    ?   ?   A . n 
A 1 648  ILE 648  648  ?    ?   ?   A . n 
A 1 649  ILE 649  649  ?    ?   ?   A . n 
A 1 650  TRP 650  650  ?    ?   ?   A . n 
A 1 651  ALA 651  651  ?    ?   ?   A . n 
A 1 652  LYS 652  652  ?    ?   ?   A . n 
A 1 653  GLN 653  653  ?    ?   ?   A . n 
A 1 654  ILE 654  654  ?    ?   ?   A . n 
A 1 655  ASP 655  655  ?    ?   ?   A . n 
A 1 656  ARG 656  656  ?    ?   ?   A . n 
A 1 657  GLN 657  657  ?    ?   ?   A . n 
A 1 658  LEU 658  658  ?    ?   ?   A . n 
A 1 659  THR 659  659  ?    ?   ?   A . n 
A 1 660  ALA 660  660  ?    ?   ?   A . n 
A 1 661  TYR 661  661  ?    ?   ?   A . n 
A 1 662  MET 662  662  ?    ?   ?   A . n 
A 1 663  LYS 663  663  ?    ?   ?   A . n 
A 1 664  ARG 664  664  ?    ?   ?   A . n 
A 1 665  VAL 665  665  ?    ?   ?   A . n 
A 1 666  GLU 666  666  ?    ?   ?   A . n 
A 1 667  ASP 667  667  ?    ?   ?   A . n 
A 1 668  VAL 668  668  ?    ?   ?   A . n 
A 1 669  LEU 669  669  ?    ?   ?   A . n 
A 1 670  GLY 670  670  ?    ?   ?   A . n 
A 1 671  LYS 671  671  ?    ?   ?   A . n 
A 1 672  GLY 672  672  ?    ?   ?   A . n 
A 1 673  TRP 673  673  ?    ?   ?   A . n 
A 1 674  GLU 674  674  ?    ?   ?   A . n 
A 1 675  ASN 675  675  ?    ?   ?   A . n 
A 1 676  HIS 676  676  ?    ?   ?   A . n 
A 1 677  VAL 677  677  ?    ?   ?   A . n 
A 1 678  GLU 678  678  ?    ?   ?   A . n 
A 1 679  GLY 679  679  ?    ?   ?   A . n 
A 1 680  GLN 680  680  ?    ?   ?   A . n 
A 1 681  LYS 681  681  ?    ?   ?   A . n 
A 1 682  LEU 682  682  ?    ?   ?   A . n 
A 1 683  LYS 683  683  ?    ?   ?   A . n 
A 1 684  GLN 684  684  ?    ?   ?   A . n 
A 1 685  ASP 685  685  ?    ?   ?   A . n 
A 1 686  GLY 686  686  ?    ?   ?   A . n 
A 1 687  ASP 687  687  ?    ?   ?   A . n 
A 1 688  SER 688  688  ?    ?   ?   A . n 
A 1 689  PHE 689  689  ?    ?   ?   A . n 
A 1 690  ARG 690  690  ?    ?   ?   A . n 
A 1 691  MET 691  691  ?    ?   ?   A . n 
A 1 692  LYS 692  692  ?    ?   ?   A . n 
A 1 693  LEU 693  693  ?    ?   ?   A . n 
A 1 694  ASN 694  694  ?    ?   ?   A . n 
A 1 695  THR 695  695  ?    ?   ?   A . n 
A 1 696  GLN 696  696  ?    ?   ?   A . n 
A 1 697  GLU 697  697  ?    ?   ?   A . n 
A 1 698  ILE 698  698  ?    ?   ?   A . n 
A 1 699  PHE 699  699  ?    ?   ?   A . n 
A 1 700  ASP 700  700  ?    ?   ?   A . n 
A 1 701  ASP 701  701  ?    ?   ?   A . n 
A 1 702  TRP 702  702  ?    ?   ?   A . n 
A 1 703  ALA 703  703  ?    ?   ?   A . n 
A 1 704  ARG 704  704  ?    ?   ?   A . n 
A 1 705  LYS 705  705  ?    ?   ?   A . n 
A 1 706  VAL 706  706  ?    ?   ?   A . n 
A 1 707  GLN 707  707  ?    ?   ?   A . n 
A 1 708  GLN 708  708  ?    ?   ?   A . n 
A 1 709  ARG 709  709  ?    ?   ?   A . n 
A 1 710  ASN 710  710  ?    ?   ?   A . n 
A 1 711  LEU 711  711  ?    ?   ?   A . n 
A 1 712  GLY 712  712  ?    ?   ?   A . n 
A 1 713  VAL 713  713  ?    ?   ?   A . n 
A 1 714  SER 714  714  ?    ?   ?   A . n 
A 1 715  GLY 715  715  ?    ?   ?   A . n 
A 1 716  ARG 716  716  ?    ?   ?   A . n 
A 1 717  ILE 717  717  ?    ?   ?   A . n 
A 1 718  PHE 718  718  ?    ?   ?   A . n 
A 1 719  THR 719  719  ?    ?   ?   A . n 
A 1 720  ILE 720  720  ?    ?   ?   A . n 
A 1 721  GLU 721  721  ?    ?   ?   A . n 
A 1 722  SER 722  722  ?    ?   ?   A . n 
A 1 723  THR 723  723  ?    ?   ?   A . n 
A 1 724  ARG 724  724  ?    ?   ?   A . n 
A 1 725  VAL 725  725  ?    ?   ?   A . n 
A 1 726  ARG 726  726  ?    ?   ?   A . n 
A 1 727  GLY 727  727  ?    ?   ?   A . n 
A 1 728  ARG 728  728  ?    ?   ?   A . n 
A 1 729  THR 729  729  ?    ?   ?   A . n 
A 1 730  GLY 730  730  ?    ?   ?   A . n 
A 1 731  ASN 731  731  ?    ?   ?   A . n 
A 1 732  VAL 732  732  ?    ?   ?   A . n 
A 1 733  LEU 733  733  ?    ?   ?   A . n 
A 1 734  LYS 734  734  ?    ?   ?   A . n 
A 1 735  LEU 735  735  ?    ?   ?   A . n 
A 1 736  LYS 736  736  ?    ?   ?   A . n 
A 1 737  VAL 737  737  ?    ?   ?   A . n 
A 1 738  ASN 738  738  ?    ?   ?   A . n 
A 1 739  PHE 739  739  ?    ?   ?   A . n 
A 1 740  LEU 740  740  ?    ?   ?   A . n 
A 1 741  PRO 741  741  ?    ?   ?   A . n 
A 1 742  GLU 742  742  ?    ?   ?   A . n 
A 1 743  ILE 743  743  ?    ?   ?   A . n 
A 1 744  ILE 744  744  ?    ?   ?   A . n 
A 1 745  THR 745  745  ?    ?   ?   A . n 
A 1 746  LEU 746  746  ?    ?   ?   A . n 
A 1 747  SER 747  747  ?    ?   ?   A . n 
A 1 748  LYS 748  748  ?    ?   ?   A . n 
A 1 749  GLU 749  749  ?    ?   ?   A . n 
A 1 750  VAL 750  750  ?    ?   ?   A . n 
A 1 751  ARG 751  751  ?    ?   ?   A . n 
A 1 752  ASN 752  752  ?    ?   ?   A . n 
A 1 753  LEU 753  753  ?    ?   ?   A . n 
A 1 754  LYS 754  754  ?    ?   ?   A . n 
A 1 755  TRP 755  755  ?    ?   ?   A . n 
A 1 756  LEU 756  756  ?    ?   ?   A . n 
A 1 757  GLY 757  757  ?    ?   ?   A . n 
A 1 758  PHE 758  758  ?    ?   ?   A . n 
A 1 759  ARG 759  759  ?    ?   ?   A . n 
A 1 760  VAL 760  760  ?    ?   ?   A . n 
A 1 761  PRO 761  761  ?    ?   ?   A . n 
A 1 762  LEU 762  762  ?    ?   ?   A . n 
A 1 763  ALA 763  763  ?    ?   ?   A . n 
A 1 764  ILE 764  764  ?    ?   ?   A . n 
A 1 765  VAL 765  765  ?    ?   ?   A . n 
A 1 766  ASN 766  766  ?    ?   ?   A . n 
A 1 767  LYS 767  767  ?    ?   ?   A . n 
A 1 768  ALA 768  768  ?    ?   ?   A . n 
A 1 769  HIS 769  769  ?    ?   ?   A . n 
A 1 770  GLN 770  770  ?    ?   ?   A . n 
A 1 771  ALA 771  771  ?    ?   ?   A . n 
A 1 772  ASN 772  772  ?    ?   ?   A . n 
A 1 773  GLN 773  773  ?    ?   ?   A . n 
A 1 774  LEU 774  774  ?    ?   ?   A . n 
A 1 775  TYR 775  775  ?    ?   ?   A . n 
A 1 776  PRO 776  776  ?    ?   ?   A . n 
A 1 777  PHE 777  777  ?    ?   ?   A . n 
A 1 778  ALA 778  778  ?    ?   ?   A . n 
A 1 779  ILE 779  779  ?    ?   ?   A . n 
A 1 780  SER 780  780  ?    ?   ?   A . n 
A 1 781  LEU 781  781  ?    ?   ?   A . n 
A 1 782  ILE 782  782  ?    ?   ?   A . n 
A 1 783  GLU 783  783  ?    ?   ?   A . n 
A 1 784  SER 784  784  ?    ?   ?   A . n 
A 1 785  VAL 785  785  ?    ?   ?   A . n 
A 1 786  ARG 786  786  ?    ?   ?   A . n 
A 1 787  THR 787  787  ?    ?   ?   A . n 
A 1 788  TYR 788  788  ?    ?   ?   A . n 
A 1 789  GLU 789  789  ?    ?   ?   A . n 
A 1 790  ARG 790  790  ?    ?   ?   A . n 
A 1 791  THR 791  791  ?    ?   ?   A . n 
A 1 792  CYS 792  792  ?    ?   ?   A . n 
A 1 793  GLU 793  793  ?    ?   ?   A . n 
A 1 794  LYS 794  794  ?    ?   ?   A . n 
A 1 795  VAL 795  795  ?    ?   ?   A . n 
A 1 796  GLU 796  796  ?    ?   ?   A . n 
A 1 797  GLU 797  797  ?    ?   ?   A . n 
A 1 798  ARG 798  798  ?    ?   ?   A . n 
A 1 799  ASN 799  799  ?    ?   ?   A . n 
A 1 800  THR 800  800  ?    ?   ?   A . n 
A 1 801  ILE 801  801  ?    ?   ?   A . n 
A 1 802  SER 802  802  ?    ?   ?   A . n 
A 1 803  LEU 803  803  ?    ?   ?   A . n 
A 1 804  LEU 804  804  ?    ?   ?   A . n 
A 1 805  VAL 805  805  ?    ?   ?   A . n 
A 1 806  ALA 806  806  ?    ?   ?   A . n 
A 1 807  GLY 807  807  ?    ?   ?   A . n 
A 1 808  LEU 808  808  ?    ?   ?   A . n 
A 1 809  LYS 809  809  ?    ?   ?   A . n 
A 1 810  LYS 810  810  ?    ?   ?   A . n 
A 1 811  GLU 811  811  ?    ?   ?   A . n 
A 1 812  VAL 812  812  ?    ?   ?   A . n 
A 1 813  GLN 813  813  ?    ?   ?   A . n 
A 1 814  ALA 814  814  ?    ?   ?   A . n 
A 1 815  LEU 815  815  ?    ?   ?   A . n 
A 1 816  ILE 816  816  ?    ?   ?   A . n 
A 1 817  ALA 817  817  ?    ?   ?   A . n 
A 1 818  GLU 818  818  ?    ?   ?   A . n 
A 1 819  GLY 819  819  ?    ?   ?   A . n 
A 1 820  ILE 820  820  ?    ?   ?   A . n 
A 1 821  ALA 821  821  ?    ?   ?   A . n 
A 1 822  LEU 822  822  ?    ?   ?   A . n 
A 1 823  VAL 823  823  ?    ?   ?   A . n 
A 1 824  TRP 824  824  ?    ?   ?   A . n 
A 1 825  GLU 825  825  ?    ?   ?   A . n 
A 1 826  SER 826  826  ?    ?   ?   A . n 
A 1 827  TYR 827  827  ?    ?   ?   A . n 
A 1 828  LYS 828  828  ?    ?   ?   A . n 
A 1 829  LEU 829  829  ?    ?   ?   A . n 
A 1 830  ASP 830  830  ?    ?   ?   A . n 
A 1 831  PRO 831  831  ?    ?   ?   A . n 
A 1 832  TYR 832  832  ?    ?   ?   A . n 
A 1 833  VAL 833  833  ?    ?   ?   A . n 
A 1 834  GLN 834  834  ?    ?   ?   A . n 
A 1 835  ARG 835  835  ?    ?   ?   A . n 
A 1 836  LEU 836  836  ?    ?   ?   A . n 
A 1 837  ALA 837  837  ?    ?   ?   A . n 
A 1 838  GLU 838  838  ?    ?   ?   A . n 
A 1 839  THR 839  839  ?    ?   ?   A . n 
A 1 840  VAL 840  840  ?    ?   ?   A . n 
A 1 841  PHE 841  841  ?    ?   ?   A . n 
A 1 842  ASN 842  842  ?    ?   ?   A . n 
A 1 843  PHE 843  843  ?    ?   ?   A . n 
A 1 844  GLN 844  844  ?    ?   ?   A . n 
A 1 845  GLU 845  845  ?    ?   ?   A . n 
A 1 846  LYS 846  846  ?    ?   ?   A . n 
A 1 847  VAL 847  847  ?    ?   ?   A . n 
A 1 848  ASP 848  848  ?    ?   ?   A . n 
A 1 849  ASP 849  849  ?    ?   ?   A . n 
A 1 850  LEU 850  850  ?    ?   ?   A . n 
A 1 851  LEU 851  851  ?    ?   ?   A . n 
A 1 852  ILE 852  852  ?    ?   ?   A . n 
A 1 853  ILE 853  853  ?    ?   ?   A . n 
A 1 854  GLU 854  854  ?    ?   ?   A . n 
A 1 855  GLU 855  855  ?    ?   ?   A . n 
A 1 856  LYS 856  856  ?    ?   ?   A . n 
A 1 857  ILE 857  857  ?    ?   ?   A . n 
A 1 858  ASP 858  858  ?    ?   ?   A . n 
A 1 859  LEU 859  859  ?    ?   ?   A . n 
A 1 860  GLU 860  860  ?    ?   ?   A . n 
A 1 861  VAL 861  861  ?    ?   ?   A . n 
A 1 862  ARG 862  862  ?    ?   ?   A . n 
A 1 863  SER 863  863  ?    ?   ?   A . n 
A 1 864  LEU 864  864  ?    ?   ?   A . n 
A 1 865  GLU 865  865  ?    ?   ?   A . n 
A 1 866  THR 866  866  ?    ?   ?   A . n 
A 1 867  CYS 867  867  ?    ?   ?   A . n 
A 1 868  MET 868  868  ?    ?   ?   A . n 
A 1 869  TYR 869  869  ?    ?   ?   A . n 
A 1 870  ASP 870  870  ?    ?   ?   A . n 
A 1 871  HIS 871  871  ?    ?   ?   A . n 
A 1 872  LYS 872  872  ?    ?   ?   A . n 
A 1 873  THR 873  873  ?    ?   ?   A . n 
A 1 874  PHE 874  874  ?    ?   ?   A . n 
A 1 875  SER 875  875  ?    ?   ?   A . n 
A 1 876  GLU 876  876  ?    ?   ?   A . n 
A 1 877  ILE 877  877  ?    ?   ?   A . n 
A 1 878  LEU 878  878  ?    ?   ?   A . n 
A 1 879  ASN 879  879  ?    ?   ?   A . n 
A 1 880  ARG 880  880  ?    ?   ?   A . n 
A 1 881  VAL 881  881  ?    ?   ?   A . n 
A 1 882  GLN 882  882  ?    ?   ?   A . n 
A 1 883  LYS 883  883  ?    ?   ?   A . n 
A 1 884  ALA 884  884  ?    ?   ?   A . n 
A 1 885  VAL 885  885  ?    ?   ?   A . n 
A 1 886  ASP 886  886  ?    ?   ?   A . n 
A 1 887  ASP 887  887  ?    ?   ?   A . n 
A 1 888  LEU 888  888  ?    ?   ?   A . n 
A 1 889  ASN 889  889  ?    ?   ?   A . n 
A 1 890  LEU 890  890  ?    ?   ?   A . n 
A 1 891  HIS 891  891  ?    ?   ?   A . n 
A 1 892  SER 892  892  ?    ?   ?   A . n 
A 1 893  TYR 893  893  ?    ?   ?   A . n 
A 1 894  SER 894  894  ?    ?   ?   A . n 
A 1 895  ASN 895  895  ?    ?   ?   A . n 
A 1 896  LEU 896  896  ?    ?   ?   A . n 
A 1 897  PRO 897  897  ?    ?   ?   A . n 
A 1 898  ILE 898  898  ?    ?   ?   A . n 
A 1 899  TRP 899  899  ?    ?   ?   A . n 
A 1 900  VAL 900  900  ?    ?   ?   A . n 
A 1 901  ASN 901  901  ?    ?   ?   A . n 
A 1 902  LYS 902  902  ?    ?   ?   A . n 
A 1 903  LEU 903  903  ?    ?   ?   A . n 
A 1 904  ASP 904  904  ?    ?   ?   A . n 
A 1 905  MET 905  905  ?    ?   ?   A . n 
A 1 906  GLU 906  906  ?    ?   ?   A . n 
A 1 907  ILE 907  907  ?    ?   ?   A . n 
A 1 908  GLU 908  908  ?    ?   ?   A . n 
A 1 909  ARG 909  909  ?    ?   ?   A . n 
A 1 910  ILE 910  910  ?    ?   ?   A . n 
A 1 911  LEU 911  911  ?    ?   ?   A . n 
A 1 912  GLY 912  912  ?    ?   ?   A . n 
A 1 913  VAL 913  913  ?    ?   ?   A . n 
A 1 914  ARG 914  914  ?    ?   ?   A . n 
A 1 915  LEU 915  915  ?    ?   ?   A . n 
A 1 916  GLN 916  916  ?    ?   ?   A . n 
A 1 917  ALA 917  917  ?    ?   ?   A . n 
A 1 918  GLY 918  918  ?    ?   ?   A . n 
A 1 919  LEU 919  919  ?    ?   ?   A . n 
A 1 920  ARG 920  920  ?    ?   ?   A . n 
A 1 921  ALA 921  921  ?    ?   ?   A . n 
A 1 922  TRP 922  922  ?    ?   ?   A . n 
A 1 923  THR 923  923  ?    ?   ?   A . n 
A 1 924  GLN 924  924  ?    ?   ?   A . n 
A 1 925  VAL 925  925  ?    ?   ?   A . n 
A 1 926  LEU 926  926  ?    ?   ?   A . n 
A 1 927  LEU 927  927  ?    ?   ?   A . n 
A 1 928  GLY 928  928  ?    ?   ?   A . n 
A 1 929  GLN 929  929  ?    ?   ?   A . n 
A 1 930  ALA 930  930  ?    ?   ?   A . n 
A 1 931  GLU 931  931  ?    ?   ?   A . n 
A 1 932  ASP 932  932  ?    ?   ?   A . n 
A 1 933  LYS 933  933  ?    ?   ?   A . n 
A 1 934  ALA 934  934  ?    ?   ?   A . n 
A 1 935  GLU 935  935  ?    ?   ?   A . n 
A 1 936  VAL 936  936  ?    ?   ?   A . n 
A 1 937  ASP 937  937  ?    ?   ?   A . n 
A 1 938  MET 938  938  ?    ?   ?   A . n 
A 1 939  ASP 939  939  ?    ?   ?   A . n 
A 1 940  THR 940  940  ?    ?   ?   A . n 
A 1 941  ASP 941  941  ?    ?   ?   A . n 
A 1 942  ALA 942  942  ?    ?   ?   A . n 
A 1 943  PRO 943  943  ?    ?   ?   A . n 
A 1 944  GLN 944  944  ?    ?   ?   A . n 
A 1 945  VAL 945  945  ?    ?   ?   A . n 
A 1 946  SER 946  946  ?    ?   ?   A . n 
A 1 947  HIS 947  947  ?    ?   ?   A . n 
A 1 948  LYS 948  948  ?    ?   ?   A . n 
A 1 949  PRO 949  949  ?    ?   ?   A . n 
A 1 950  GLY 950  950  ?    ?   ?   A . n 
A 1 951  GLY 951  951  ?    ?   ?   A . n 
A 1 952  GLU 952  952  ?    ?   ?   A . n 
A 1 953  PRO 953  953  ?    ?   ?   A . n 
A 1 954  LYS 954  954  ?    ?   ?   A . n 
A 1 955  ILE 955  955  ?    ?   ?   A . n 
A 1 956  LYS 956  956  ?    ?   ?   A . n 
A 1 957  ASN 957  957  ?    ?   ?   A . n 
A 1 958  VAL 958  958  ?    ?   ?   A . n 
A 1 959  VAL 959  959  ?    ?   ?   A . n 
A 1 960  HIS 960  960  ?    ?   ?   A . n 
A 1 961  GLU 961  961  ?    ?   ?   A . n 
A 1 962  LEU 962  962  ?    ?   ?   A . n 
A 1 963  ARG 963  963  ?    ?   ?   A . n 
A 1 964  ILE 964  964  ?    ?   ?   A . n 
A 1 965  THR 965  965  ?    ?   ?   A . n 
A 1 966  ASN 966  966  ?    ?   ?   A . n 
A 1 967  GLN 967  967  ?    ?   ?   A . n 
A 1 968  VAL 968  968  ?    ?   ?   A . n 
A 1 969  ILE 969  969  ?    ?   ?   A . n 
A 1 970  TYR 970  970  ?    ?   ?   A . n 
A 1 971  LEU 971  971  ?    ?   ?   A . n 
A 1 972  ASN 972  972  ?    ?   ?   A . n 
A 1 973  PRO 973  973  ?    ?   ?   A . n 
A 1 974  PRO 974  974  ?    ?   ?   A . n 
A 1 975  ILE 975  975  ?    ?   ?   A . n 
A 1 976  GLU 976  976  ?    ?   ?   A . n 
A 1 977  GLU 977  977  ?    ?   ?   A . n 
A 1 978  CYS 978  978  ?    ?   ?   A . n 
A 1 979  ARG 979  979  ?    ?   ?   A . n 
A 1 980  TYR 980  980  ?    ?   ?   A . n 
A 1 981  LYS 981  981  ?    ?   ?   A . n 
A 1 982  LEU 982  982  ?    ?   ?   A . n 
A 1 983  TYR 983  983  ?    ?   ?   A . n 
A 1 984  GLN 984  984  ?    ?   ?   A . n 
A 1 985  GLU 985  985  ?    ?   ?   A . n 
A 1 986  MET 986  986  ?    ?   ?   A . n 
A 1 987  PHE 987  987  ?    ?   ?   A . n 
A 1 988  ALA 988  988  ?    ?   ?   A . n 
A 1 989  TRP 989  989  ?    ?   ?   A . n 
A 1 990  LYS 990  990  ?    ?   ?   A . n 
A 1 991  MET 991  991  ?    ?   ?   A . n 
A 1 992  VAL 992  992  ?    ?   ?   A . n 
A 1 993  VAL 993  993  ?    ?   ?   A . n 
A 1 994  LEU 994  994  ?    ?   ?   A . n 
A 1 995  SER 995  995  ?    ?   ?   A . n 
A 1 996  LEU 996  996  ?    ?   ?   A . n 
A 1 997  PRO 997  997  ?    ?   ?   A . n 
A 1 998  ARG 998  998  ?    ?   ?   A . n 
A 1 999  ILE 999  999  ?    ?   ?   A . n 
A 1 1000 GLN 1000 1000 ?    ?   ?   A . n 
A 1 1001 SER 1001 1001 ?    ?   ?   A . n 
A 1 1002 GLN 1002 1002 ?    ?   ?   A . n 
A 1 1003 ARG 1003 1003 ?    ?   ?   A . n 
A 1 1004 TYR 1004 1004 ?    ?   ?   A . n 
A 1 1005 GLN 1005 1005 ?    ?   ?   A . n 
A 1 1006 VAL 1006 1006 ?    ?   ?   A . n 
A 1 1007 GLY 1007 1007 ?    ?   ?   A . n 
A 1 1008 VAL 1008 1008 ?    ?   ?   A . n 
A 1 1009 HIS 1009 1009 ?    ?   ?   A . n 
A 1 1010 TYR 1010 1010 ?    ?   ?   A . n 
A 1 1011 GLU 1011 1011 ?    ?   ?   A . n 
A 1 1012 LEU 1012 1012 ?    ?   ?   A . n 
A 1 1013 THR 1013 1013 ?    ?   ?   A . n 
A 1 1014 GLU 1014 1014 ?    ?   ?   A . n 
A 1 1015 GLU 1015 1015 ?    ?   ?   A . n 
A 1 1016 GLU 1016 1016 ?    ?   ?   A . n 
A 1 1017 LYS 1017 1017 ?    ?   ?   A . n 
A 1 1018 PHE 1018 1018 ?    ?   ?   A . n 
A 1 1019 TYR 1019 1019 ?    ?   ?   A . n 
A 1 1020 ARG 1020 1020 ?    ?   ?   A . n 
A 1 1021 ASN 1021 1021 ?    ?   ?   A . n 
A 1 1022 ALA 1022 1022 ?    ?   ?   A . n 
A 1 1023 LEU 1023 1023 ?    ?   ?   A . n 
A 1 1024 THR 1024 1024 ?    ?   ?   A . n 
A 1 1025 ARG 1025 1025 ?    ?   ?   A . n 
A 1 1026 MET 1026 1026 ?    ?   ?   A . n 
A 1 1027 PRO 1027 1027 ?    ?   ?   A . n 
A 1 1028 ASP 1028 1028 ?    ?   ?   A . n 
A 1 1029 GLY 1029 1029 ?    ?   ?   A . n 
A 1 1030 PRO 1030 1030 ?    ?   ?   A . n 
A 1 1031 VAL 1031 1031 ?    ?   ?   A . n 
A 1 1032 ALA 1032 1032 ?    ?   ?   A . n 
A 1 1033 LEU 1033 1033 ?    ?   ?   A . n 
A 1 1034 GLU 1034 1034 ?    ?   ?   A . n 
A 1 1035 GLU 1035 1035 ?    ?   ?   A . n 
A 1 1036 SER 1036 1036 ?    ?   ?   A . n 
A 1 1037 TYR 1037 1037 ?    ?   ?   A . n 
A 1 1038 SER 1038 1038 ?    ?   ?   A . n 
A 1 1039 ALA 1039 1039 ?    ?   ?   A . n 
A 1 1040 VAL 1040 1040 ?    ?   ?   A . n 
A 1 1041 MET 1041 1041 ?    ?   ?   A . n 
A 1 1042 GLY 1042 1042 ?    ?   ?   A . n 
A 1 1043 ILE 1043 1043 ?    ?   ?   A . n 
A 1 1044 VAL 1044 1044 ?    ?   ?   A . n 
A 1 1045 SER 1045 1045 ?    ?   ?   A . n 
A 1 1046 GLU 1046 1046 ?    ?   ?   A . n 
A 1 1047 VAL 1047 1047 ?    ?   ?   A . n 
A 1 1048 GLU 1048 1048 ?    ?   ?   A . n 
A 1 1049 GLN 1049 1049 ?    ?   ?   A . n 
A 1 1050 TYR 1050 1050 ?    ?   ?   A . n 
A 1 1051 VAL 1051 1051 ?    ?   ?   A . n 
A 1 1052 LYS 1052 1052 ?    ?   ?   A . n 
A 1 1053 VAL 1053 1053 ?    ?   ?   A . n 
A 1 1054 TRP 1054 1054 ?    ?   ?   A . n 
A 1 1055 LEU 1055 1055 ?    ?   ?   A . n 
A 1 1056 GLN 1056 1056 ?    ?   ?   A . n 
A 1 1057 TYR 1057 1057 ?    ?   ?   A . n 
A 1 1058 GLN 1058 1058 ?    ?   ?   A . n 
A 1 1059 CYS 1059 1059 ?    ?   ?   A . n 
A 1 1060 LEU 1060 1060 ?    ?   ?   A . n 
A 1 1061 TRP 1061 1061 ?    ?   ?   A . n 
A 1 1062 ASP 1062 1062 ?    ?   ?   A . n 
A 1 1063 MET 1063 1063 ?    ?   ?   A . n 
A 1 1064 GLN 1064 1064 ?    ?   ?   A . n 
A 1 1065 ALA 1065 1065 ?    ?   ?   A . n 
A 1 1066 GLU 1066 1066 ?    ?   ?   A . n 
A 1 1067 ASN 1067 1067 ?    ?   ?   A . n 
A 1 1068 ILE 1068 1068 ?    ?   ?   A . n 
A 1 1069 TYR 1069 1069 ?    ?   ?   A . n 
A 1 1070 ASN 1070 1070 ?    ?   ?   A . n 
A 1 1071 ARG 1071 1071 ?    ?   ?   A . n 
A 1 1072 LEU 1072 1072 ?    ?   ?   A . n 
A 1 1073 GLY 1073 1073 ?    ?   ?   A . n 
A 1 1074 GLU 1074 1074 ?    ?   ?   A . n 
A 1 1075 ASP 1075 1075 ?    ?   ?   A . n 
A 1 1076 LEU 1076 1076 ?    ?   ?   A . n 
A 1 1077 ASN 1077 1077 ?    ?   ?   A . n 
A 1 1078 LYS 1078 1078 ?    ?   ?   A . n 
A 1 1079 TRP 1079 1079 ?    ?   ?   A . n 
A 1 1080 GLN 1080 1080 ?    ?   ?   A . n 
A 1 1081 ALA 1081 1081 ?    ?   ?   A . n 
A 1 1082 LEU 1082 1082 ?    ?   ?   A . n 
A 1 1083 LEU 1083 1083 ?    ?   ?   A . n 
A 1 1084 VAL 1084 1084 ?    ?   ?   A . n 
A 1 1085 GLN 1085 1085 ?    ?   ?   A . n 
A 1 1086 ILE 1086 1086 ?    ?   ?   A . n 
A 1 1087 ARG 1087 1087 ?    ?   ?   A . n 
A 1 1088 LYS 1088 1088 ?    ?   ?   A . n 
A 1 1089 ALA 1089 1089 ?    ?   ?   A . n 
A 1 1090 ARG 1090 1090 ?    ?   ?   A . n 
A 1 1091 GLY 1091 1091 ?    ?   ?   A . n 
A 1 1092 THR 1092 1092 ?    ?   ?   A . n 
A 1 1093 PHE 1093 1093 ?    ?   ?   A . n 
A 1 1094 ASP 1094 1094 ?    ?   ?   A . n 
A 1 1095 ASN 1095 1095 ?    ?   ?   A . n 
A 1 1096 ALA 1096 1096 ?    ?   ?   A . n 
A 1 1097 GLU 1097 1097 ?    ?   ?   A . n 
A 1 1098 THR 1098 1098 ?    ?   ?   A . n 
A 1 1099 LYS 1099 1099 ?    ?   ?   A . n 
A 1 1100 LYS 1100 1100 ?    ?   ?   A . n 
A 1 1101 GLU 1101 1101 ?    ?   ?   A . n 
A 1 1102 PHE 1102 1102 ?    ?   ?   A . n 
A 1 1103 GLY 1103 1103 ?    ?   ?   A . n 
A 1 1104 PRO 1104 1104 ?    ?   ?   A . n 
A 1 1105 VAL 1105 1105 ?    ?   ?   A . n 
A 1 1106 VAL 1106 1106 ?    ?   ?   A . n 
A 1 1107 ILE 1107 1107 ?    ?   ?   A . n 
A 1 1108 ASP 1108 1108 ?    ?   ?   A . n 
A 1 1109 TYR 1109 1109 ?    ?   ?   A . n 
A 1 1110 GLY 1110 1110 ?    ?   ?   A . n 
A 1 1111 LYS 1111 1111 ?    ?   ?   A . n 
A 1 1112 VAL 1112 1112 ?    ?   ?   A . n 
A 1 1113 GLN 1113 1113 ?    ?   ?   A . n 
A 1 1114 SER 1114 1114 ?    ?   ?   A . n 
A 1 1115 LYS 1115 1115 ?    ?   ?   A . n 
A 1 1116 VAL 1116 1116 ?    ?   ?   A . n 
A 1 1117 ASN 1117 1117 ?    ?   ?   A . n 
A 1 1118 LEU 1118 1118 ?    ?   ?   A . n 
A 1 1119 LYS 1119 1119 ?    ?   ?   A . n 
A 1 1120 TYR 1120 1120 ?    ?   ?   A . n 
A 1 1121 ASP 1121 1121 ?    ?   ?   A . n 
A 1 1122 SER 1122 1122 ?    ?   ?   A . n 
A 1 1123 TRP 1123 1123 ?    ?   ?   A . n 
A 1 1124 HIS 1124 1124 ?    ?   ?   A . n 
A 1 1125 LYS 1125 1125 ?    ?   ?   A . n 
A 1 1126 GLU 1126 1126 ?    ?   ?   A . n 
A 1 1127 VAL 1127 1127 ?    ?   ?   A . n 
A 1 1128 LEU 1128 1128 ?    ?   ?   A . n 
A 1 1129 SER 1129 1129 ?    ?   ?   A . n 
A 1 1130 LYS 1130 1130 ?    ?   ?   A . n 
A 1 1131 PHE 1131 1131 ?    ?   ?   A . n 
A 1 1132 GLY 1132 1132 ?    ?   ?   A . n 
A 1 1133 GLN 1133 1133 ?    ?   ?   A . n 
A 1 1134 MET 1134 1134 ?    ?   ?   A . n 
A 1 1135 LEU 1135 1135 ?    ?   ?   A . n 
A 1 1136 GLY 1136 1136 ?    ?   ?   A . n 
A 1 1137 SER 1137 1137 ?    ?   ?   A . n 
A 1 1138 ASN 1138 1138 ?    ?   ?   A . n 
A 1 1139 MET 1139 1139 ?    ?   ?   A . n 
A 1 1140 THR 1140 1140 ?    ?   ?   A . n 
A 1 1141 GLU 1141 1141 ?    ?   ?   A . n 
A 1 1142 PHE 1142 1142 ?    ?   ?   A . n 
A 1 1143 HIS 1143 1143 ?    ?   ?   A . n 
A 1 1144 SER 1144 1144 ?    ?   ?   A . n 
A 1 1145 GLN 1145 1145 ?    ?   ?   A . n 
A 1 1146 ILE 1146 1146 ?    ?   ?   A . n 
A 1 1147 SER 1147 1147 ?    ?   ?   A . n 
A 1 1148 LYS 1148 1148 ?    ?   ?   A . n 
A 1 1149 SER 1149 1149 ?    ?   ?   A . n 
A 1 1150 ARG 1150 1150 ?    ?   ?   A . n 
A 1 1151 GLN 1151 1151 ?    ?   ?   A . n 
A 1 1152 GLU 1152 1152 ?    ?   ?   A . n 
A 1 1153 LEU 1153 1153 ?    ?   ?   A . n 
A 1 1154 GLU 1154 1154 ?    ?   ?   A . n 
A 1 1155 GLN 1155 1155 ?    ?   ?   A . n 
A 1 1156 HIS 1156 1156 ?    ?   ?   A . n 
A 1 1157 SER 1157 1157 ?    ?   ?   A . n 
A 1 1158 VAL 1158 1158 ?    ?   ?   A . n 
A 1 1159 ASP 1159 1159 ?    ?   ?   A . n 
A 1 1160 THR 1160 1160 ?    ?   ?   A . n 
A 1 1161 ALA 1161 1161 ?    ?   ?   A . n 
A 1 1162 SER 1162 1162 ?    ?   ?   A . n 
A 1 1163 THR 1163 1163 ?    ?   ?   A . n 
A 1 1164 SER 1164 1164 ?    ?   ?   A . n 
A 1 1165 ASP 1165 1165 ?    ?   ?   A . n 
A 1 1166 ALA 1166 1166 ?    ?   ?   A . n 
A 1 1167 VAL 1167 1167 ?    ?   ?   A . n 
A 1 1168 THR 1168 1168 ?    ?   ?   A . n 
A 1 1169 PHE 1169 1169 ?    ?   ?   A . n 
A 1 1170 ILE 1170 1170 ?    ?   ?   A . n 
A 1 1171 THR 1171 1171 ?    ?   ?   A . n 
A 1 1172 TYR 1172 1172 ?    ?   ?   A . n 
A 1 1173 VAL 1173 1173 ?    ?   ?   A . n 
A 1 1174 GLN 1174 1174 ?    ?   ?   A . n 
A 1 1175 SER 1175 1175 ?    ?   ?   A . n 
A 1 1176 LEU 1176 1176 ?    ?   ?   A . n 
A 1 1177 LYS 1177 1177 ?    ?   ?   A . n 
A 1 1178 ARG 1178 1178 ?    ?   ?   A . n 
A 1 1179 LYS 1179 1179 ?    ?   ?   A . n 
A 1 1180 ILE 1180 1180 ?    ?   ?   A . n 
A 1 1181 LYS 1181 1181 ?    ?   ?   A . n 
A 1 1182 GLN 1182 1182 ?    ?   ?   A . n 
A 1 1183 PHE 1183 1183 ?    ?   ?   A . n 
A 1 1184 GLU 1184 1184 ?    ?   ?   A . n 
A 1 1185 LYS 1185 1185 ?    ?   ?   A . n 
A 1 1186 GLN 1186 1186 ?    ?   ?   A . n 
A 1 1187 VAL 1187 1187 ?    ?   ?   A . n 
A 1 1188 GLU 1188 1188 ?    ?   ?   A . n 
A 1 1189 LEU 1189 1189 ?    ?   ?   A . n 
A 1 1190 TYR 1190 1190 ?    ?   ?   A . n 
A 1 1191 ARG 1191 1191 ?    ?   ?   A . n 
A 1 1192 ASN 1192 1192 ?    ?   ?   A . n 
A 1 1193 GLY 1193 1193 ?    ?   ?   A . n 
A 1 1194 GLN 1194 1194 ?    ?   ?   A . n 
A 1 1195 ARG 1195 1195 ?    ?   ?   A . n 
A 1 1196 LEU 1196 1196 ?    ?   ?   A . n 
A 1 1197 LEU 1197 1197 ?    ?   ?   A . n 
A 1 1198 GLU 1198 1198 ?    ?   ?   A . n 
A 1 1199 LYS 1199 1199 ?    ?   ?   A . n 
A 1 1200 GLN 1200 1200 ?    ?   ?   A . n 
A 1 1201 ARG 1201 1201 ?    ?   ?   A . n 
A 1 1202 PHE 1202 1202 ?    ?   ?   A . n 
A 1 1203 GLN 1203 1203 ?    ?   ?   A . n 
A 1 1204 PHE 1204 1204 ?    ?   ?   A . n 
A 1 1205 PRO 1205 1205 ?    ?   ?   A . n 
A 1 1206 PRO 1206 1206 ?    ?   ?   A . n 
A 1 1207 SER 1207 1207 ?    ?   ?   A . n 
A 1 1208 TRP 1208 1208 ?    ?   ?   A . n 
A 1 1209 LEU 1209 1209 ?    ?   ?   A . n 
A 1 1210 TYR 1210 1210 ?    ?   ?   A . n 
A 1 1211 ILE 1211 1211 ?    ?   ?   A . n 
A 1 1212 ASP 1212 1212 ?    ?   ?   A . n 
A 1 1213 ASN 1213 1213 ?    ?   ?   A . n 
A 1 1214 ILE 1214 1214 ?    ?   ?   A . n 
A 1 1215 GLU 1215 1215 ?    ?   ?   A . n 
A 1 1216 GLY 1216 1216 ?    ?   ?   A . n 
A 1 1217 GLU 1217 1217 ?    ?   ?   A . n 
A 1 1218 TRP 1218 1218 ?    ?   ?   A . n 
A 1 1219 GLY 1219 1219 ?    ?   ?   A . n 
A 1 1220 ALA 1220 1220 ?    ?   ?   A . n 
A 1 1221 PHE 1221 1221 ?    ?   ?   A . n 
A 1 1222 ASN 1222 1222 ?    ?   ?   A . n 
A 1 1223 ASP 1223 1223 ?    ?   ?   A . n 
A 1 1224 ILE 1224 1224 ?    ?   ?   A . n 
A 1 1225 MET 1225 1225 ?    ?   ?   A . n 
A 1 1226 ARG 1226 1226 ?    ?   ?   A . n 
A 1 1227 ARG 1227 1227 ?    ?   ?   A . n 
A 1 1228 LYS 1228 1228 ?    ?   ?   A . n 
A 1 1229 ASP 1229 1229 ?    ?   ?   A . n 
A 1 1230 SER 1230 1230 ?    ?   ?   A . n 
A 1 1231 ALA 1231 1231 ?    ?   ?   A . n 
A 1 1232 ILE 1232 1232 ?    ?   ?   A . n 
A 1 1233 GLN 1233 1233 ?    ?   ?   A . n 
A 1 1234 GLN 1234 1234 ?    ?   ?   A . n 
A 1 1235 GLN 1235 1235 ?    ?   ?   A . n 
A 1 1236 VAL 1236 1236 ?    ?   ?   A . n 
A 1 1237 ALA 1237 1237 ?    ?   ?   A . n 
A 1 1238 ASN 1238 1238 ?    ?   ?   A . n 
A 1 1239 LEU 1239 1239 ?    ?   ?   A . n 
A 1 1240 GLN 1240 1240 ?    ?   ?   A . n 
A 1 1241 MET 1241 1241 ?    ?   ?   A . n 
A 1 1242 LYS 1242 1242 ?    ?   ?   A . n 
A 1 1243 ILE 1243 1243 ?    ?   ?   A . n 
A 1 1244 VAL 1244 1244 ?    ?   ?   A . n 
A 1 1245 GLN 1245 1245 ?    ?   ?   A . n 
A 1 1246 GLU 1246 1246 ?    ?   ?   A . n 
A 1 1247 ASP 1247 1247 ?    ?   ?   A . n 
A 1 1248 ARG 1248 1248 ?    ?   ?   A . n 
A 1 1249 ALA 1249 1249 ?    ?   ?   A . n 
A 1 1250 VAL 1250 1250 ?    ?   ?   A . n 
A 1 1251 GLU 1251 1251 ?    ?   ?   A . n 
A 1 1252 SER 1252 1252 ?    ?   ?   A . n 
A 1 1253 ARG 1253 1253 ?    ?   ?   A . n 
A 1 1254 THR 1254 1254 ?    ?   ?   A . n 
A 1 1255 THR 1255 1255 ?    ?   ?   A . n 
A 1 1256 ASP 1256 1256 ?    ?   ?   A . n 
A 1 1257 LEU 1257 1257 ?    ?   ?   A . n 
A 1 1258 LEU 1258 1258 ?    ?   ?   A . n 
A 1 1259 THR 1259 1259 ?    ?   ?   A . n 
A 1 1260 ASP 1260 1260 ?    ?   ?   A . n 
A 1 1261 TRP 1261 1261 ?    ?   ?   A . n 
A 1 1262 GLU 1262 1262 ?    ?   ?   A . n 
A 1 1263 LYS 1263 1263 ?    ?   ?   A . n 
A 1 1264 THR 1264 1264 ?    ?   ?   A . n 
A 1 1265 LYS 1265 1265 ?    ?   ?   A . n 
A 1 1266 PRO 1266 1266 ?    ?   ?   A . n 
A 1 1267 VAL 1267 1267 ?    ?   ?   A . n 
A 1 1268 THR 1268 1268 ?    ?   ?   A . n 
A 1 1269 GLY 1269 1269 ?    ?   ?   A . n 
A 1 1270 ASN 1270 1270 ?    ?   ?   A . n 
A 1 1271 LEU 1271 1271 ?    ?   ?   A . n 
A 1 1272 ARG 1272 1272 ?    ?   ?   A . n 
A 1 1273 PRO 1273 1273 ?    ?   ?   A . n 
A 1 1274 GLU 1274 1274 ?    ?   ?   A . n 
A 1 1275 GLU 1275 1275 ?    ?   ?   A . n 
A 1 1276 ALA 1276 1276 ?    ?   ?   A . n 
A 1 1277 LEU 1277 1277 ?    ?   ?   A . n 
A 1 1278 GLN 1278 1278 ?    ?   ?   A . n 
A 1 1279 ALA 1279 1279 ?    ?   ?   A . n 
A 1 1280 LEU 1280 1280 ?    ?   ?   A . n 
A 1 1281 THR 1281 1281 ?    ?   ?   A . n 
A 1 1282 ILE 1282 1282 ?    ?   ?   A . n 
A 1 1283 TYR 1283 1283 ?    ?   ?   A . n 
A 1 1284 GLU 1284 1284 ?    ?   ?   A . n 
A 1 1285 GLY 1285 1285 ?    ?   ?   A . n 
A 1 1286 LYS 1286 1286 ?    ?   ?   A . n 
A 1 1287 PHE 1287 1287 ?    ?   ?   A . n 
A 1 1288 GLY 1288 1288 ?    ?   ?   A . n 
A 1 1289 ARG 1289 1289 ?    ?   ?   A . n 
A 1 1290 LEU 1290 1290 ?    ?   ?   A . n 
A 1 1291 LYS 1291 1291 ?    ?   ?   A . n 
A 1 1292 ASP 1292 1292 ?    ?   ?   A . n 
A 1 1293 ASP 1293 1293 ?    ?   ?   A . n 
A 1 1294 ARG 1294 1294 ?    ?   ?   A . n 
A 1 1295 GLU 1295 1295 ?    ?   ?   A . n 
A 1 1296 LYS 1296 1296 ?    ?   ?   A . n 
A 1 1297 CYS 1297 1297 ?    ?   ?   A . n 
A 1 1298 ALA 1298 1298 ?    ?   ?   A . n 
A 1 1299 LYS 1299 1299 ?    ?   ?   A . n 
A 1 1300 ALA 1300 1300 ?    ?   ?   A . n 
A 1 1301 LYS 1301 1301 ?    ?   ?   A . n 
A 1 1302 GLU 1302 1302 ?    ?   ?   A . n 
A 1 1303 ALA 1303 1303 ?    ?   ?   A . n 
A 1 1304 LEU 1304 1304 ?    ?   ?   A . n 
A 1 1305 GLU 1305 1305 ?    ?   ?   A . n 
A 1 1306 LEU 1306 1306 ?    ?   ?   A . n 
A 1 1307 THR 1307 1307 ?    ?   ?   A . n 
A 1 1308 ASP 1308 1308 ?    ?   ?   A . n 
A 1 1309 THR 1309 1309 ?    ?   ?   A . n 
A 1 1310 GLY 1310 1310 ?    ?   ?   A . n 
A 1 1311 LEU 1311 1311 ?    ?   ?   A . n 
A 1 1312 LEU 1312 1312 ?    ?   ?   A . n 
A 1 1313 SER 1313 1313 ?    ?   ?   A . n 
A 1 1314 GLY 1314 1314 ?    ?   ?   A . n 
A 1 1315 SER 1315 1315 ?    ?   ?   A . n 
A 1 1316 GLU 1316 1316 ?    ?   ?   A . n 
A 1 1317 GLU 1317 1317 ?    ?   ?   A . n 
A 1 1318 ARG 1318 1318 ?    ?   ?   A . n 
A 1 1319 VAL 1319 1319 ?    ?   ?   A . n 
A 1 1320 GLN 1320 1320 ?    ?   ?   A . n 
A 1 1321 VAL 1321 1321 ?    ?   ?   A . n 
A 1 1322 ALA 1322 1322 ?    ?   ?   A . n 
A 1 1323 LEU 1323 1323 ?    ?   ?   A . n 
A 1 1324 GLU 1324 1324 ?    ?   ?   A . n 
A 1 1325 GLU 1325 1325 ?    ?   ?   A . n 
A 1 1326 LEU 1326 1326 ?    ?   ?   A . n 
A 1 1327 GLN 1327 1327 ?    ?   ?   A . n 
A 1 1328 ASP 1328 1328 ?    ?   ?   A . n 
A 1 1329 LEU 1329 1329 ?    ?   ?   A . n 
A 1 1330 LYS 1330 1330 ?    ?   ?   A . n 
A 1 1331 GLY 1331 1331 ?    ?   ?   A . n 
A 1 1332 VAL 1332 1332 ?    ?   ?   A . n 
A 1 1333 TRP 1333 1333 ?    ?   ?   A . n 
A 1 1334 SER 1334 1334 ?    ?   ?   A . n 
A 1 1335 GLU 1335 1335 ?    ?   ?   A . n 
A 1 1336 LEU 1336 1336 ?    ?   ?   A . n 
A 1 1337 SER 1337 1337 ?    ?   ?   A . n 
A 1 1338 LYS 1338 1338 ?    ?   ?   A . n 
A 1 1339 VAL 1339 1339 ?    ?   ?   A . n 
A 1 1340 TRP 1340 1340 ?    ?   ?   A . n 
A 1 1341 GLU 1341 1341 ?    ?   ?   A . n 
A 1 1342 GLN 1342 1342 ?    ?   ?   A . n 
A 1 1343 ILE 1343 1343 ?    ?   ?   A . n 
A 1 1344 ASP 1344 1344 ?    ?   ?   A . n 
A 1 1345 GLN 1345 1345 ?    ?   ?   A . n 
A 1 1346 MET 1346 1346 ?    ?   ?   A . n 
A 1 1347 LYS 1347 1347 ?    ?   ?   A . n 
A 1 1348 GLU 1348 1348 ?    ?   ?   A . n 
A 1 1349 GLN 1349 1349 ?    ?   ?   A . n 
A 1 1350 PRO 1350 1350 ?    ?   ?   A . n 
A 1 1351 TRP 1351 1351 ?    ?   ?   A . n 
A 1 1352 VAL 1352 1352 ?    ?   ?   A . n 
A 1 1353 SER 1353 1353 ?    ?   ?   A . n 
A 1 1354 VAL 1354 1354 ?    ?   ?   A . n 
A 1 1355 GLN 1355 1355 ?    ?   ?   A . n 
A 1 1356 PRO 1356 1356 ?    ?   ?   A . n 
A 1 1357 ARG 1357 1357 ?    ?   ?   A . n 
A 1 1358 LYS 1358 1358 ?    ?   ?   A . n 
A 1 1359 LEU 1359 1359 ?    ?   ?   A . n 
A 1 1360 ARG 1360 1360 ?    ?   ?   A . n 
A 1 1361 GLN 1361 1361 ?    ?   ?   A . n 
A 1 1362 ASN 1362 1362 ?    ?   ?   A . n 
A 1 1363 LEU 1363 1363 ?    ?   ?   A . n 
A 1 1364 ASP 1364 1364 ?    ?   ?   A . n 
A 1 1365 ALA 1365 1365 ?    ?   ?   A . n 
A 1 1366 LEU 1366 1366 ?    ?   ?   A . n 
A 1 1367 LEU 1367 1367 ?    ?   ?   A . n 
A 1 1368 ASN 1368 1368 ?    ?   ?   A . n 
A 1 1369 GLN 1369 1369 ?    ?   ?   A . n 
A 1 1370 LEU 1370 1370 ?    ?   ?   A . n 
A 1 1371 LYS 1371 1371 ?    ?   ?   A . n 
A 1 1372 SER 1372 1372 ?    ?   ?   A . n 
A 1 1373 PHE 1373 1373 ?    ?   ?   A . n 
A 1 1374 PRO 1374 1374 ?    ?   ?   A . n 
A 1 1375 ALA 1375 1375 ?    ?   ?   A . n 
A 1 1376 ARG 1376 1376 ?    ?   ?   A . n 
A 1 1377 LEU 1377 1377 ?    ?   ?   A . n 
A 1 1378 ARG 1378 1378 ?    ?   ?   A . n 
A 1 1379 GLN 1379 1379 ?    ?   ?   A . n 
A 1 1380 TYR 1380 1380 ?    ?   ?   A . n 
A 1 1381 ALA 1381 1381 ?    ?   ?   A . n 
A 1 1382 SER 1382 1382 ?    ?   ?   A . n 
A 1 1383 TYR 1383 1383 ?    ?   ?   A . n 
A 1 1384 GLU 1384 1384 ?    ?   ?   A . n 
A 1 1385 PHE 1385 1385 ?    ?   ?   A . n 
A 1 1386 VAL 1386 1386 ?    ?   ?   A . n 
A 1 1387 GLN 1387 1387 ?    ?   ?   A . n 
A 1 1388 ARG 1388 1388 ?    ?   ?   A . n 
A 1 1389 LEU 1389 1389 ?    ?   ?   A . n 
A 1 1390 LEU 1390 1390 ?    ?   ?   A . n 
A 1 1391 LYS 1391 1391 ?    ?   ?   A . n 
A 1 1392 GLY 1392 1392 ?    ?   ?   A . n 
A 1 1393 TYR 1393 1393 ?    ?   ?   A . n 
A 1 1394 MET 1394 1394 ?    ?   ?   A . n 
A 1 1395 LYS 1395 1395 ?    ?   ?   A . n 
A 1 1396 ILE 1396 1396 ?    ?   ?   A . n 
A 1 1397 ASN 1397 1397 ?    ?   ?   A . n 
A 1 1398 MET 1398 1398 ?    ?   ?   A . n 
A 1 1399 LEU 1399 1399 ?    ?   ?   A . n 
A 1 1400 VAL 1400 1400 ?    ?   ?   A . n 
A 1 1401 ILE 1401 1401 ?    ?   ?   A . n 
A 1 1402 GLU 1402 1402 ?    ?   ?   A . n 
A 1 1403 LEU 1403 1403 ?    ?   ?   A . n 
A 1 1404 LYS 1404 1404 ?    ?   ?   A . n 
A 1 1405 SER 1405 1405 ?    ?   ?   A . n 
A 1 1406 GLU 1406 1406 ?    ?   ?   A . n 
A 1 1407 ALA 1407 1407 ?    ?   ?   A . n 
A 1 1408 LEU 1408 1408 ?    ?   ?   A . n 
A 1 1409 LYS 1409 1409 ?    ?   ?   A . n 
A 1 1410 ASP 1410 1410 ?    ?   ?   A . n 
A 1 1411 ARG 1411 1411 ?    ?   ?   A . n 
A 1 1412 HIS 1412 1412 ?    ?   ?   A . n 
A 1 1413 TRP 1413 1413 ?    ?   ?   A . n 
A 1 1414 LYS 1414 1414 ?    ?   ?   A . n 
A 1 1415 GLN 1415 1415 ?    ?   ?   A . n 
A 1 1416 LEU 1416 1416 ?    ?   ?   A . n 
A 1 1417 MET 1417 1417 ?    ?   ?   A . n 
A 1 1418 LYS 1418 1418 ?    ?   ?   A . n 
A 1 1419 ARG 1419 1419 ?    ?   ?   A . n 
A 1 1420 LEU 1420 1420 ?    ?   ?   A . n 
A 1 1421 HIS 1421 1421 ?    ?   ?   A . n 
A 1 1422 VAL 1422 1422 ?    ?   ?   A . n 
A 1 1423 ASN 1423 1423 ?    ?   ?   A . n 
A 1 1424 TRP 1424 1424 ?    ?   ?   A . n 
A 1 1425 VAL 1425 1425 ?    ?   ?   A . n 
A 1 1426 VAL 1426 1426 ?    ?   ?   A . n 
A 1 1427 SER 1427 1427 ?    ?   ?   A . n 
A 1 1428 GLU 1428 1428 ?    ?   ?   A . n 
A 1 1429 LEU 1429 1429 ?    ?   ?   A . n 
A 1 1430 THR 1430 1430 ?    ?   ?   A . n 
A 1 1431 LEU 1431 1431 ?    ?   ?   A . n 
A 1 1432 GLY 1432 1432 ?    ?   ?   A . n 
A 1 1433 GLN 1433 1433 ?    ?   ?   A . n 
A 1 1434 ILE 1434 1434 ?    ?   ?   A . n 
A 1 1435 TRP 1435 1435 ?    ?   ?   A . n 
A 1 1436 ASP 1436 1436 ?    ?   ?   A . n 
A 1 1437 VAL 1437 1437 ?    ?   ?   A . n 
A 1 1438 ASP 1438 1438 ?    ?   ?   A . n 
A 1 1439 LEU 1439 1439 ?    ?   ?   A . n 
A 1 1440 GLN 1440 1440 ?    ?   ?   A . n 
A 1 1441 LYS 1441 1441 ?    ?   ?   A . n 
A 1 1442 ASN 1442 1442 ?    ?   ?   A . n 
A 1 1443 GLU 1443 1443 ?    ?   ?   A . n 
A 1 1444 ALA 1444 1444 ?    ?   ?   A . n 
A 1 1445 ILE 1445 1445 ?    ?   ?   A . n 
A 1 1446 VAL 1446 1446 ?    ?   ?   A . n 
A 1 1447 LYS 1447 1447 ?    ?   ?   A . n 
A 1 1448 ASP 1448 1448 ?    ?   ?   A . n 
A 1 1449 VAL 1449 1449 ?    ?   ?   A . n 
A 1 1450 LEU 1450 1450 ?    ?   ?   A . n 
A 1 1451 LEU 1451 1451 ?    ?   ?   A . n 
A 1 1452 VAL 1452 1452 ?    ?   ?   A . n 
A 1 1453 ALA 1453 1453 ?    ?   ?   A . n 
A 1 1454 GLN 1454 1454 ?    ?   ?   A . n 
A 1 1455 GLY 1455 1455 ?    ?   ?   A . n 
A 1 1456 GLU 1456 1456 ?    ?   ?   A . n 
A 1 1457 MET 1457 1457 1457 MET MET A . n 
A 1 1458 ALA 1458 1458 1458 ALA ALA A . n 
A 1 1459 LEU 1459 1459 1459 LEU LEU A . n 
A 1 1460 GLU 1460 1460 1460 GLU GLU A . n 
A 1 1461 GLU 1461 1461 1461 GLU GLU A . n 
A 1 1462 PHE 1462 1462 1462 PHE PHE A . n 
A 1 1463 LEU 1463 1463 1463 LEU LEU A . n 
A 1 1464 LYS 1464 1464 1464 LYS LYS A . n 
A 1 1465 GLN 1465 1465 1465 GLN GLN A . n 
A 1 1466 ILE 1466 1466 1466 ILE ILE A . n 
A 1 1467 ARG 1467 1467 1467 ARG ARG A . n 
A 1 1468 GLU 1468 1468 1468 GLU GLU A . n 
A 1 1469 VAL 1469 1469 1469 VAL VAL A . n 
A 1 1470 TRP 1470 1470 1470 TRP TRP A . n 
A 1 1471 ASN 1471 1471 1471 ASN ASN A . n 
A 1 1472 THR 1472 1472 1472 THR THR A . n 
A 1 1473 TYR 1473 1473 1473 TYR TYR A . n 
A 1 1474 GLU 1474 1474 1474 GLU GLU A . n 
A 1 1475 LEU 1475 1475 1475 LEU LEU A . n 
A 1 1476 ASP 1476 1476 1476 ASP ASP A . n 
A 1 1477 LEU 1477 1477 1477 LEU LEU A . n 
A 1 1478 VAL 1478 1478 1478 VAL VAL A . n 
A 1 1479 ASN 1479 1479 1479 ASN ASN A . n 
A 1 1480 TYR 1480 1480 1480 TYR TYR A . n 
A 1 1481 GLN 1481 1481 1481 GLN GLN A . n 
A 1 1482 ASN 1482 1482 1482 ASN ASN A . n 
A 1 1483 LYS 1483 1483 1483 LYS LYS A . n 
A 1 1484 CYS 1484 1484 1484 CYS CYS A . n 
A 1 1485 ARG 1485 1485 1485 ARG ARG A . n 
A 1 1486 LEU 1486 1486 1486 LEU LEU A . n 
A 1 1487 ILE 1487 1487 1487 ILE ILE A . n 
A 1 1488 ARG 1488 1488 1488 ARG ARG A . n 
A 1 1489 GLY 1489 1489 1489 GLY GLY A . n 
A 1 1490 TRP 1490 1490 1490 TRP TRP A . n 
A 1 1491 ASP 1491 1491 1491 ASP ASP A . n 
A 1 1492 ASP 1492 1492 1492 ASP ASP A . n 
A 1 1493 LEU 1493 1493 1493 LEU LEU A . n 
A 1 1494 PHE 1494 1494 1494 PHE PHE A . n 
A 1 1495 ASN 1495 1495 1495 ASN ASN A . n 
A 1 1496 LYS 1496 1496 1496 LYS LYS A . n 
A 1 1497 VAL 1497 1497 1497 VAL VAL A . n 
A 1 1498 LYS 1498 1498 1498 LYS LYS A . n 
A 1 1499 GLU 1499 1499 1499 GLU GLU A . n 
A 1 1500 HIS 1500 1500 1500 HIS HIS A . n 
A 1 1501 ILE 1501 1501 1501 ILE ILE A . n 
A 1 1502 ASN 1502 1502 1502 ASN ASN A . n 
A 1 1503 SER 1503 1503 1503 SER SER A . n 
A 1 1504 VAL 1504 1504 1504 VAL VAL A . n 
A 1 1505 SER 1505 1505 1505 SER SER A . n 
A 1 1506 ALA 1506 1506 1506 ALA ALA A . n 
A 1 1507 MET 1507 1507 1507 MET MET A . n 
A 1 1508 LYS 1508 1508 1508 LYS LYS A . n 
A 1 1509 LEU 1509 1509 1509 LEU LEU A . n 
A 1 1510 SER 1510 1510 1510 SER SER A . n 
A 1 1511 PRO 1511 1511 1511 PRO PRO A . n 
A 1 1512 TYR 1512 1512 1512 TYR TYR A . n 
A 1 1513 TYR 1513 1513 1513 TYR TYR A . n 
A 1 1514 LYS 1514 1514 1514 LYS LYS A . n 
A 1 1515 VAL 1515 1515 1515 VAL VAL A . n 
A 1 1516 PHE 1516 1516 1516 PHE PHE A . n 
A 1 1517 GLU 1517 1517 1517 GLU GLU A . n 
A 1 1518 GLU 1518 1518 1518 GLU GLU A . n 
A 1 1519 ASP 1519 1519 1519 ASP ASP A . n 
A 1 1520 ALA 1520 1520 1520 ALA ALA A . n 
A 1 1521 LEU 1521 1521 1521 LEU LEU A . n 
A 1 1522 SER 1522 1522 1522 SER SER A . n 
A 1 1523 TRP 1523 1523 1523 TRP TRP A . n 
A 1 1524 GLU 1524 1524 1524 GLU GLU A . n 
A 1 1525 ASP 1525 1525 1525 ASP ASP A . n 
A 1 1526 LYS 1526 1526 1526 LYS LYS A . n 
A 1 1527 LEU 1527 1527 1527 LEU LEU A . n 
A 1 1528 ASN 1528 1528 1528 ASN ASN A . n 
A 1 1529 ARG 1529 1529 1529 ARG ARG A . n 
A 1 1530 ILE 1530 1530 1530 ILE ILE A . n 
A 1 1531 MET 1531 1531 1531 MET MET A . n 
A 1 1532 ALA 1532 1532 1532 ALA ALA A . n 
A 1 1533 LEU 1533 1533 1533 LEU LEU A . n 
A 1 1534 PHE 1534 1534 1534 PHE PHE A . n 
A 1 1535 ASP 1535 1535 1535 ASP ASP A . n 
A 1 1536 VAL 1536 1536 1536 VAL VAL A . n 
A 1 1537 TRP 1537 1537 1537 TRP TRP A . n 
A 1 1538 ILE 1538 1538 1538 ILE ILE A . n 
A 1 1539 ASP 1539 1539 1539 ASP ASP A . n 
A 1 1540 VAL 1540 1540 1540 VAL VAL A . n 
A 1 1541 GLN 1541 1541 1541 GLN GLN A . n 
A 1 1542 ARG 1542 1542 1542 ARG ARG A . n 
A 1 1543 ARG 1543 1543 1543 ARG ARG A . n 
A 1 1544 TRP 1544 1544 1544 TRP TRP A . n 
A 1 1545 VAL 1545 1545 1545 VAL VAL A . n 
A 1 1546 TYR 1546 1546 1546 TYR TYR A . n 
A 1 1547 LEU 1547 1547 1547 LEU LEU A . n 
A 1 1548 GLU 1548 1548 1548 GLU GLU A . n 
A 1 1549 GLY 1549 1549 1549 GLY GLY A . n 
A 1 1550 ILE 1550 1550 1550 ILE ILE A . n 
A 1 1551 PHE 1551 1551 1551 PHE PHE A . n 
A 1 1552 THR 1552 1552 1552 THR THR A . n 
A 1 1553 GLY 1553 1553 1553 GLY GLY A . n 
A 1 1554 SER 1554 1554 1554 SER SER A . n 
A 1 1555 ALA 1555 1555 1555 ALA ALA A . n 
A 1 1556 ASP 1556 1556 1556 ASP ASP A . n 
A 1 1557 ILE 1557 1557 1557 ILE ILE A . n 
A 1 1558 LYS 1558 1558 1558 LYS LYS A . n 
A 1 1559 HIS 1559 1559 1559 HIS HIS A . n 
A 1 1560 LEU 1560 1560 1560 LEU LEU A . n 
A 1 1561 LEU 1561 1561 1561 LEU LEU A . n 
A 1 1562 PRO 1562 1562 1562 PRO PRO A . n 
A 1 1563 VAL 1563 1563 1563 VAL VAL A . n 
A 1 1564 GLU 1564 1564 1564 GLU GLU A . n 
A 1 1565 THR 1565 1565 1565 THR THR A . n 
A 1 1566 GLN 1566 1566 1566 GLN GLN A . n 
A 1 1567 ARG 1567 1567 1567 ARG ARG A . n 
A 1 1568 PHE 1568 1568 1568 PHE PHE A . n 
A 1 1569 GLN 1569 1569 1569 GLN GLN A . n 
A 1 1570 SER 1570 1570 1570 SER SER A . n 
A 1 1571 ILE 1571 1571 1571 ILE ILE A . n 
A 1 1572 SER 1572 1572 1572 SER SER A . n 
A 1 1573 THR 1573 1573 1573 THR THR A . n 
A 1 1574 GLU 1574 1574 1574 GLU GLU A . n 
A 1 1575 PHE 1575 1575 1575 PHE PHE A . n 
A 1 1576 LEU 1576 1576 1576 LEU LEU A . n 
A 1 1577 ALA 1577 1577 1577 ALA ALA A . n 
A 1 1578 LEU 1578 1578 1578 LEU LEU A . n 
A 1 1579 MET 1579 1579 1579 MET MET A . n 
A 1 1580 LYS 1580 1580 1580 LYS LYS A . n 
A 1 1581 LYS 1581 1581 1581 LYS LYS A . n 
A 1 1582 VAL 1582 1582 1582 VAL VAL A . n 
A 1 1583 SER 1583 1583 1583 SER SER A . n 
A 1 1584 LYS 1584 1584 1584 LYS LYS A . n 
A 1 1585 SER 1585 1585 1585 SER SER A . n 
A 1 1586 PRO 1586 1586 1586 PRO PRO A . n 
A 1 1587 LEU 1587 1587 1587 LEU LEU A . n 
A 1 1588 VAL 1588 1588 1588 VAL VAL A . n 
A 1 1589 MET 1589 1589 1589 MET MET A . n 
A 1 1590 ASP 1590 1590 1590 ASP ASP A . n 
A 1 1591 VAL 1591 1591 1591 VAL VAL A . n 
A 1 1592 LEU 1592 1592 1592 LEU LEU A . n 
A 1 1593 ASN 1593 1593 1593 ASN ASN A . n 
A 1 1594 ILE 1594 1594 1594 ILE ILE A . n 
A 1 1595 GLN 1595 1595 1595 GLN GLN A . n 
A 1 1596 GLY 1596 1596 1596 GLY GLY A . n 
A 1 1597 VAL 1597 1597 1597 VAL VAL A . n 
A 1 1598 GLN 1598 1598 1598 GLN GLN A . n 
A 1 1599 ARG 1599 1599 1599 ARG ARG A . n 
A 1 1600 SER 1600 1600 1600 SER SER A . n 
A 1 1601 LEU 1601 1601 1601 LEU LEU A . n 
A 1 1602 GLU 1602 1602 1602 GLU GLU A . n 
A 1 1603 ARG 1603 1603 1603 ARG ARG A . n 
A 1 1604 LEU 1604 1604 1604 LEU LEU A . n 
A 1 1605 ALA 1605 1605 1605 ALA ALA A . n 
A 1 1606 ASP 1606 1606 1606 ASP ASP A . n 
A 1 1607 LEU 1607 1607 1607 LEU LEU A . n 
A 1 1608 LEU 1608 1608 1608 LEU LEU A . n 
A 1 1609 GLY 1609 1609 1609 GLY GLY A . n 
A 1 1610 LYS 1610 1610 1610 LYS LYS A . n 
A 1 1611 ILE 1611 1611 1611 ILE ILE A . n 
A 1 1612 GLN 1612 1612 1612 GLN GLN A . n 
A 1 1613 LYS 1613 1613 1613 LYS LYS A . n 
A 1 1614 ALA 1614 1614 1614 ALA ALA A . n 
A 1 1615 LEU 1615 1615 1615 LEU LEU A . n 
A 1 1616 GLY 1616 1616 1616 GLY GLY A . n 
A 1 1617 GLU 1617 1617 1617 GLU GLU A . n 
A 1 1618 TYR 1618 1618 1618 TYR TYR A . n 
A 1 1619 LEU 1619 1619 1619 LEU LEU A . n 
A 1 1620 GLU 1620 1620 1620 GLU GLU A . n 
A 1 1621 ARG 1621 1621 1621 ARG ARG A . n 
A 1 1622 GLU 1622 1622 1622 GLU GLU A . n 
A 1 1623 ARG 1623 1623 1623 ARG ARG A . n 
A 1 1624 SER 1624 1624 1624 SER SER A . n 
A 1 1625 SER 1625 1625 1625 SER SER A . n 
A 1 1626 PHE 1626 1626 1626 PHE PHE A . n 
A 1 1627 PRO 1627 1627 1627 PRO PRO A . n 
A 1 1628 ARG 1628 1628 1628 ARG ARG A . n 
A 1 1629 PHE 1629 1629 1629 PHE PHE A . n 
A 1 1630 TYR 1630 1630 1630 TYR TYR A . n 
A 1 1631 PHE 1631 1631 1631 PHE PHE A . n 
A 1 1632 VAL 1632 1632 1632 VAL VAL A . n 
A 1 1633 GLY 1633 1633 1633 GLY GLY A . n 
A 1 1634 ASP 1634 1634 1634 ASP ASP A . n 
A 1 1635 GLU 1635 1635 1635 GLU GLU A . n 
A 1 1636 ASP 1636 1636 1636 ASP ASP A . n 
A 1 1637 LEU 1637 1637 1637 LEU LEU A . n 
A 1 1638 LEU 1638 1638 1638 LEU LEU A . n 
A 1 1639 GLU 1639 1639 1639 GLU GLU A . n 
A 1 1640 ILE 1640 1640 1640 ILE ILE A . n 
A 1 1641 ILE 1641 1641 1641 ILE ILE A . n 
A 1 1642 GLY 1642 1642 1642 GLY GLY A . n 
A 1 1643 ASN 1643 1643 1643 ASN ASN A . n 
A 1 1644 SER 1644 1644 1644 SER SER A . n 
A 1 1645 LYS 1645 1645 1645 LYS LYS A . n 
A 1 1646 ASN 1646 1646 1646 ASN ASN A . n 
A 1 1647 VAL 1647 1647 1647 VAL VAL A . n 
A 1 1648 ALA 1648 1648 1648 ALA ALA A . n 
A 1 1649 LYS 1649 1649 1649 LYS LYS A . n 
A 1 1650 LEU 1650 1650 1650 LEU LEU A . n 
A 1 1651 GLN 1651 1651 1651 GLN GLN A . n 
A 1 1652 LYS 1652 1652 1652 LYS LYS A . n 
A 1 1653 HIS 1653 1653 1653 HIS HIS A . n 
A 1 1654 PHE 1654 1654 1654 PHE PHE A . n 
A 1 1655 LYS 1655 1655 1655 LYS LYS A . n 
A 1 1656 LYS 1656 1656 1656 LYS LYS A . n 
A 1 1657 MET 1657 1657 1657 MET MET A . n 
A 1 1658 PHE 1658 1658 1658 PHE PHE A . n 
A 1 1659 ALA 1659 1659 1659 ALA ALA A . n 
A 1 1660 GLY 1660 1660 1660 GLY GLY A . n 
A 1 1661 VAL 1661 1661 1661 VAL VAL A . n 
A 1 1662 SER 1662 1662 1662 SER SER A . n 
A 1 1663 SER 1663 1663 1663 SER SER A . n 
A 1 1664 ILE 1664 1664 1664 ILE ILE A . n 
A 1 1665 ILE 1665 1665 1665 ILE ILE A . n 
A 1 1666 LEU 1666 1666 1666 LEU LEU A . n 
A 1 1667 ASN 1667 1667 1667 ASN ASN A . n 
A 1 1668 GLU 1668 1668 1668 GLU GLU A . n 
A 1 1669 ASP 1669 1669 1669 ASP ASP A . n 
A 1 1670 ASN 1670 1670 1670 ASN ASN A . n 
A 1 1671 SER 1671 1671 1671 SER SER A . n 
A 1 1672 VAL 1672 1672 1672 VAL VAL A . n 
A 1 1673 VAL 1673 1673 1673 VAL VAL A . n 
A 1 1674 LEU 1674 1674 1674 LEU LEU A . n 
A 1 1675 GLY 1675 1675 1675 GLY GLY A . n 
A 1 1676 ILE 1676 1676 1676 ILE ILE A . n 
A 1 1677 SER 1677 1677 1677 SER SER A . n 
A 1 1678 SER 1678 1678 1678 SER SER A . n 
A 1 1679 ARG 1679 1679 1679 ARG ARG A . n 
A 1 1680 GLU 1680 1680 1680 GLU GLU A . n 
A 1 1681 GLY 1681 1681 1681 GLY GLY A . n 
A 1 1682 GLU 1682 1682 1682 GLU GLU A . n 
A 1 1683 GLU 1683 1683 1683 GLU GLU A . n 
A 1 1684 VAL 1684 1684 1684 VAL VAL A . n 
A 1 1685 MET 1685 1685 1685 MET MET A . n 
A 1 1686 PHE 1686 1686 1686 PHE PHE A . n 
A 1 1687 LYS 1687 1687 1687 LYS LYS A . n 
A 1 1688 THR 1688 1688 1688 THR THR A . n 
A 1 1689 PRO 1689 1689 1689 PRO PRO A . n 
A 1 1690 VAL 1690 1690 1690 VAL VAL A . n 
A 1 1691 SER 1691 1691 1691 SER SER A . n 
A 1 1692 ILE 1692 1692 1692 ILE ILE A . n 
A 1 1693 THR 1693 1693 1693 THR THR A . n 
A 1 1694 GLU 1694 1694 1694 GLU GLU A . n 
A 1 1695 HIS 1695 1695 1695 HIS HIS A . n 
A 1 1696 PRO 1696 1696 1696 PRO PRO A . n 
A 1 1697 LYS 1697 1697 1697 LYS LYS A . n 
A 1 1698 ILE 1698 1698 1698 ILE ILE A . n 
A 1 1699 ASN 1699 1699 1699 ASN ASN A . n 
A 1 1700 GLU 1700 1700 1700 GLU GLU A . n 
A 1 1701 TRP 1701 1701 1701 TRP TRP A . n 
A 1 1702 LEU 1702 1702 1702 LEU LEU A . n 
A 1 1703 THR 1703 1703 1703 THR THR A . n 
A 1 1704 LEU 1704 1704 1704 LEU LEU A . n 
A 1 1705 VAL 1705 1705 1705 VAL VAL A . n 
A 1 1706 GLU 1706 1706 1706 GLU GLU A . n 
A 1 1707 LYS 1707 1707 1707 LYS LYS A . n 
A 1 1708 GLU 1708 1708 1708 GLU GLU A . n 
A 1 1709 MET 1709 1709 1709 MET MET A . n 
A 1 1710 ARG 1710 1710 1710 ARG ARG A . n 
A 1 1711 VAL 1711 1711 1711 VAL VAL A . n 
A 1 1712 THR 1712 1712 1712 THR THR A . n 
A 1 1713 LEU 1713 1713 1713 LEU LEU A . n 
A 1 1714 ALA 1714 1714 1714 ALA ALA A . n 
A 1 1715 LYS 1715 1715 1715 LYS LYS A . n 
A 1 1716 LEU 1716 1716 1716 LEU LEU A . n 
A 1 1717 LEU 1717 1717 1717 LEU LEU A . n 
A 1 1718 ALA 1718 1718 1718 ALA ALA A . n 
A 1 1719 GLU 1719 1719 1719 GLU GLU A . n 
A 1 1720 SER 1720 1720 1720 SER SER A . n 
A 1 1721 VAL 1721 1721 1721 VAL VAL A . n 
A 1 1722 THR 1722 1722 1722 THR THR A . n 
A 1 1723 GLU 1723 1723 1723 GLU GLU A . n 
A 1 1724 VAL 1724 1724 1724 VAL VAL A . n 
A 1 1725 GLU 1725 1725 1725 GLU GLU A . n 
A 1 1726 ILE 1726 1726 1726 ILE ILE A . n 
A 1 1727 PHE 1727 1727 1727 PHE PHE A . n 
A 1 1728 GLY 1728 1728 1728 GLY GLY A . n 
A 1 1729 LYS 1729 1729 1729 LYS LYS A . n 
A 1 1730 ALA 1730 1730 1730 ALA ALA A . n 
A 1 1731 THR 1731 1731 1731 THR THR A . n 
A 1 1732 SER 1732 1732 1732 SER SER A . n 
A 1 1733 ILE 1733 1733 1733 ILE ILE A . n 
A 1 1734 ASP 1734 1734 1734 ASP ASP A . n 
A 1 1735 PRO 1735 1735 1735 PRO PRO A . n 
A 1 1736 ASN 1736 1736 1736 ASN ASN A . n 
A 1 1737 THR 1737 1737 1737 THR THR A . n 
A 1 1738 TYR 1738 1738 1738 TYR TYR A . n 
A 1 1739 ILE 1739 1739 1739 ILE ILE A . n 
A 1 1740 THR 1740 1740 1740 THR THR A . n 
A 1 1741 TRP 1741 1741 1741 TRP TRP A . n 
A 1 1742 ILE 1742 1742 1742 ILE ILE A . n 
A 1 1743 ASP 1743 1743 1743 ASP ASP A . n 
A 1 1744 LYS 1744 1744 1744 LYS LYS A . n 
A 1 1745 TYR 1745 1745 1745 TYR TYR A . n 
A 1 1746 GLN 1746 1746 1746 GLN GLN A . n 
A 1 1747 ALA 1747 1747 1747 ALA ALA A . n 
A 1 1748 GLN 1748 1748 1748 GLN GLN A . n 
A 1 1749 LEU 1749 1749 1749 LEU LEU A . n 
A 1 1750 VAL 1750 1750 1750 VAL VAL A . n 
A 1 1751 VAL 1751 1751 1751 VAL VAL A . n 
A 1 1752 LEU 1752 1752 1752 LEU LEU A . n 
A 1 1753 SER 1753 1753 1753 SER SER A . n 
A 1 1754 ALA 1754 1754 1754 ALA ALA A . n 
A 1 1755 GLN 1755 1755 1755 GLN GLN A . n 
A 1 1756 ILE 1756 1756 1756 ILE ILE A . n 
A 1 1757 ALA 1757 1757 1757 ALA ALA A . n 
A 1 1758 TRP 1758 1758 1758 TRP TRP A . n 
A 1 1759 SER 1759 1759 1759 SER SER A . n 
A 1 1760 GLU 1760 1760 1760 GLU GLU A . n 
A 1 1761 ASN 1761 1761 1761 ASN ASN A . n 
A 1 1762 VAL 1762 1762 1762 VAL VAL A . n 
A 1 1763 GLU 1763 1763 1763 GLU GLU A . n 
A 1 1764 THR 1764 1764 1764 THR THR A . n 
A 1 1765 ALA 1765 1765 1765 ALA ALA A . n 
A 1 1766 LEU 1766 1766 1766 LEU LEU A . n 
A 1 1767 SER 1767 1767 1767 SER SER A . n 
A 1 1768 SER 1768 1768 1768 SER SER A . n 
A 1 1769 MET 1769 1769 1769 MET MET A . n 
A 1 1770 GLY 1770 1770 1770 GLY GLY A . n 
A 1 1771 GLY 1771 1771 1771 GLY GLY A . n 
A 1 1772 GLY 1772 1772 1772 GLY GLY A . n 
A 1 1773 GLY 1773 1773 1773 GLY GLY A . n 
A 1 1774 ASP 1774 1774 1774 ASP ASP A . n 
A 1 1775 ALA 1775 1775 1775 ALA ALA A . n 
A 1 1776 ALA 1776 1776 1776 ALA ALA A . n 
A 1 1777 PRO 1777 1777 1777 PRO PRO A . n 
A 1 1778 LEU 1778 1778 1778 LEU LEU A . n 
A 1 1779 HIS 1779 1779 1779 HIS HIS A . n 
A 1 1780 SER 1780 1780 1780 SER SER A . n 
A 1 1781 VAL 1781 1781 1781 VAL VAL A . n 
A 1 1782 LEU 1782 1782 1782 LEU LEU A . n 
A 1 1783 SER 1783 1783 1783 SER SER A . n 
A 1 1784 ASN 1784 1784 1784 ASN ASN A . n 
A 1 1785 VAL 1785 1785 1785 VAL VAL A . n 
A 1 1786 GLU 1786 1786 1786 GLU GLU A . n 
A 1 1787 VAL 1787 1787 1787 VAL VAL A . n 
A 1 1788 THR 1788 1788 1788 THR THR A . n 
A 1 1789 LEU 1789 1789 1789 LEU LEU A . n 
A 1 1790 ASN 1790 1790 1790 ASN ASN A . n 
A 1 1791 VAL 1791 1791 1791 VAL VAL A . n 
A 1 1792 LEU 1792 1792 1792 LEU LEU A . n 
A 1 1793 ALA 1793 1793 1793 ALA ALA A . n 
A 1 1794 ASP 1794 1794 1794 ASP ASP A . n 
A 1 1795 SER 1795 1795 1795 SER SER A . n 
A 1 1796 VAL 1796 1796 1796 VAL VAL A . n 
A 1 1797 LEU 1797 1797 1797 LEU LEU A . n 
A 1 1798 MET 1798 1798 1798 MET MET A . n 
A 1 1799 GLU 1799 1799 1799 GLU GLU A . n 
A 1 1800 GLN 1800 1800 1800 GLN GLN A . n 
A 1 1801 PRO 1801 1801 1801 PRO PRO A . n 
A 1 1802 PRO 1802 1802 1802 PRO PRO A . n 
A 1 1803 LEU 1803 1803 1803 LEU LEU A . n 
A 1 1804 ARG 1804 1804 1804 ARG ARG A . n 
A 1 1805 ARG 1805 1805 1805 ARG ARG A . n 
A 1 1806 ARG 1806 1806 1806 ARG ARG A . n 
A 1 1807 LYS 1807 1807 1807 LYS LYS A . n 
A 1 1808 LEU 1808 1808 1808 LEU LEU A . n 
A 1 1809 GLU 1809 1809 1809 GLU GLU A . n 
A 1 1810 HIS 1810 1810 1810 HIS HIS A . n 
A 1 1811 LEU 1811 1811 1811 LEU LEU A . n 
A 1 1812 ILE 1812 1812 1812 ILE ILE A . n 
A 1 1813 THR 1813 1813 1813 THR THR A . n 
A 1 1814 GLU 1814 1814 1814 GLU GLU A . n 
A 1 1815 LEU 1815 1815 1815 LEU LEU A . n 
A 1 1816 VAL 1816 1816 1816 VAL VAL A . n 
A 1 1817 HIS 1817 1817 1817 HIS HIS A . n 
A 1 1818 GLN 1818 1818 1818 GLN GLN A . n 
A 1 1819 ARG 1819 1819 1819 ARG ARG A . n 
A 1 1820 ASP 1820 1820 1820 ASP ASP A . n 
A 1 1821 VAL 1821 1821 1821 VAL VAL A . n 
A 1 1822 THR 1822 1822 1822 THR THR A . n 
A 1 1823 ARG 1823 1823 1823 ARG ARG A . n 
A 1 1824 SER 1824 1824 1824 SER SER A . n 
A 1 1825 LEU 1825 1825 1825 LEU LEU A . n 
A 1 1826 ILE 1826 1826 1826 ILE ILE A . n 
A 1 1827 LYS 1827 1827 1827 LYS LYS A . n 
A 1 1828 SER 1828 1828 1828 SER SER A . n 
A 1 1829 LYS 1829 1829 1829 LYS LYS A . n 
A 1 1830 ILE 1830 1830 1830 ILE ILE A . n 
A 1 1831 ASP 1831 1831 1831 ASP ASP A . n 
A 1 1832 ASN 1832 1832 1832 ASN ASN A . n 
A 1 1833 ALA 1833 1833 1833 ALA ALA A . n 
A 1 1834 LYS 1834 1834 1834 LYS LYS A . n 
A 1 1835 SER 1835 1835 1835 SER SER A . n 
A 1 1836 PHE 1836 1836 1836 PHE PHE A . n 
A 1 1837 GLU 1837 1837 1837 GLU GLU A . n 
A 1 1838 TRP 1838 1838 1838 TRP TRP A . n 
A 1 1839 LEU 1839 1839 1839 LEU LEU A . n 
A 1 1840 SER 1840 1840 1840 SER SER A . n 
A 1 1841 GLN 1841 1841 1841 GLN GLN A . n 
A 1 1842 MET 1842 1842 1842 MET MET A . n 
A 1 1843 ARG 1843 1843 1843 ARG ARG A . n 
A 1 1844 PHE 1844 1844 1844 PHE PHE A . n 
A 1 1845 TYR 1845 1845 1845 TYR TYR A . n 
A 1 1846 PHE 1846 1846 1846 PHE PHE A . n 
A 1 1847 ASP 1847 1847 1847 ASP ASP A . n 
A 1 1848 PRO 1848 1848 1848 PRO PRO A . n 
A 1 1849 LYS 1849 1849 1849 LYS LYS A . n 
A 1 1850 GLN 1850 1850 1850 GLN GLN A . n 
A 1 1851 THR 1851 1851 1851 THR THR A . n 
A 1 1852 ASP 1852 1852 1852 ASP ASP A . n 
A 1 1853 VAL 1853 1853 1853 VAL VAL A . n 
A 1 1854 LEU 1854 1854 1854 LEU LEU A . n 
A 1 1855 GLN 1855 1855 1855 GLN GLN A . n 
A 1 1856 GLN 1856 1856 1856 GLN GLN A . n 
A 1 1857 LEU 1857 1857 1857 LEU LEU A . n 
A 1 1858 SER 1858 1858 1858 SER SER A . n 
A 1 1859 ILE 1859 1859 1859 ILE ILE A . n 
A 1 1860 GLN 1860 1860 1860 GLN GLN A . n 
A 1 1861 MET 1861 1861 1861 MET MET A . n 
A 1 1862 ALA 1862 1862 1862 ALA ALA A . n 
A 1 1863 ASN 1863 1863 1863 ASN ASN A . n 
A 1 1864 ALA 1864 1864 1864 ALA ALA A . n 
A 1 1865 LYS 1865 1865 1865 LYS LYS A . n 
A 1 1866 PHE 1866 1866 1866 PHE PHE A . n 
A 1 1867 ASN 1867 1867 1867 ASN ASN A . n 
A 1 1868 TYR 1868 1868 1868 TYR TYR A . n 
A 1 1869 GLY 1869 1869 1869 GLY GLY A . n 
A 1 1870 PHE 1870 1870 1870 PHE PHE A . n 
A 1 1871 GLU 1871 1871 1871 GLU GLU A . n 
A 1 1872 TYR 1872 1872 1872 TYR TYR A . n 
A 1 1873 LEU 1873 1873 1873 LEU LEU A . n 
A 1 1874 GLY 1874 1874 1874 GLY GLY A . n 
A 1 1875 VAL 1875 1875 1875 VAL VAL A . n 
A 1 1876 GLN 1876 1876 1876 GLN GLN A . n 
A 1 1877 ASP 1877 1877 1877 ASP ASP A . n 
A 1 1878 LYS 1878 1878 1878 LYS LYS A . n 
A 1 1879 LEU 1879 1879 1879 LEU LEU A . n 
A 1 1880 VAL 1880 1880 1880 VAL VAL A . n 
A 1 1881 GLN 1881 1881 1881 GLN GLN A . n 
A 1 1882 THR 1882 1882 1882 THR THR A . n 
A 1 1883 PRO 1883 1883 1883 PRO PRO A . n 
A 1 1884 LEU 1884 1884 1884 LEU LEU A . n 
A 1 1885 THR 1885 1885 1885 THR THR A . n 
A 1 1886 ASP 1886 1886 1886 ASP ASP A . n 
A 1 1887 ARG 1887 1887 1887 ARG ARG A . n 
A 1 1888 CYS 1888 1888 1888 CYS CYS A . n 
A 1 1889 TYR 1889 1889 1889 TYR TYR A . n 
A 1 1890 LEU 1890 1890 1890 LEU LEU A . n 
A 1 1891 THR 1891 1891 1891 THR THR A . n 
A 1 1892 MET 1892 1892 1892 MET MET A . n 
A 1 1893 THR 1893 1893 1893 THR THR A . n 
A 1 1894 GLN 1894 1894 1894 GLN GLN A . n 
A 1 1895 ALA 1895 1895 1895 ALA ALA A . n 
A 1 1896 LEU 1896 1896 1896 LEU LEU A . n 
A 1 1897 GLU 1897 1897 1897 GLU GLU A . n 
A 1 1898 ALA 1898 1898 1898 ALA ALA A . n 
A 1 1899 ARG 1899 1899 1899 ARG ARG A . n 
A 1 1900 LEU 1900 1900 1900 LEU LEU A . n 
A 1 1901 GLY 1901 1901 1901 GLY GLY A . n 
A 1 1902 GLY 1902 1902 1902 GLY GLY A . n 
A 1 1903 SER 1903 1903 1903 SER SER A . n 
A 1 1904 PRO 1904 1904 1904 PRO PRO A . n 
A 1 1905 PHE 1905 1905 1905 PHE PHE A . n 
A 1 1906 GLY 1906 1906 1906 GLY GLY A . n 
A 1 1907 PRO 1907 1907 1907 PRO PRO A . n 
A 1 1908 ALA 1908 1908 1908 ALA ALA A . n 
A 1 1909 GLY 1909 1909 1909 GLY GLY A . n 
A 1 1910 THR 1910 1910 1910 THR THR A . n 
A 1 1911 GLY 1911 1911 1911 GLY GLY A . n 
A 1 1912 LYS 1912 1912 1912 LYS LYS A . n 
A 1 1913 THR 1913 1913 1913 THR THR A . n 
A 1 1914 GLU 1914 1914 1914 GLU GLU A . n 
A 1 1915 SER 1915 1915 1915 SER SER A . n 
A 1 1916 VAL 1916 1916 1916 VAL VAL A . n 
A 1 1917 LYS 1917 1917 1917 LYS LYS A . n 
A 1 1918 ALA 1918 1918 1918 ALA ALA A . n 
A 1 1919 LEU 1919 1919 1919 LEU LEU A . n 
A 1 1920 GLY 1920 1920 1920 GLY GLY A . n 
A 1 1921 HIS 1921 1921 1921 HIS HIS A . n 
A 1 1922 GLN 1922 1922 1922 GLN GLN A . n 
A 1 1923 LEU 1923 1923 1923 LEU LEU A . n 
A 1 1924 GLY 1924 1924 1924 GLY GLY A . n 
A 1 1925 ARG 1925 1925 1925 ARG ARG A . n 
A 1 1926 PHE 1926 1926 1926 PHE PHE A . n 
A 1 1927 VAL 1927 1927 1927 VAL VAL A . n 
A 1 1928 LEU 1928 1928 1928 LEU LEU A . n 
A 1 1929 VAL 1929 1929 1929 VAL VAL A . n 
A 1 1930 PHE 1930 1930 1930 PHE PHE A . n 
A 1 1931 ASN 1931 1931 1931 ASN ASN A . n 
A 1 1932 CYS 1932 1932 1932 CYS CYS A . n 
A 1 1933 ASP 1933 1933 1933 ASP ASP A . n 
A 1 1934 GLU 1934 1934 1934 GLU GLU A . n 
A 1 1935 THR 1935 1935 1935 THR THR A . n 
A 1 1936 PHE 1936 1936 1936 PHE PHE A . n 
A 1 1937 ASP 1937 1937 1937 ASP ASP A . n 
A 1 1938 PHE 1938 1938 1938 PHE PHE A . n 
A 1 1939 GLN 1939 1939 1939 GLN GLN A . n 
A 1 1940 ALA 1940 1940 1940 ALA ALA A . n 
A 1 1941 MET 1941 1941 1941 MET MET A . n 
A 1 1942 GLY 1942 1942 1942 GLY GLY A . n 
A 1 1943 ARG 1943 1943 1943 ARG ARG A . n 
A 1 1944 ILE 1944 1944 1944 ILE ILE A . n 
A 1 1945 PHE 1945 1945 1945 PHE PHE A . n 
A 1 1946 VAL 1946 1946 1946 VAL VAL A . n 
A 1 1947 GLY 1947 1947 1947 GLY GLY A . n 
A 1 1948 LEU 1948 1948 1948 LEU LEU A . n 
A 1 1949 CYS 1949 1949 1949 CYS CYS A . n 
A 1 1950 GLN 1950 1950 1950 GLN GLN A . n 
A 1 1951 VAL 1951 1951 1951 VAL VAL A . n 
A 1 1952 GLY 1952 1952 1952 GLY GLY A . n 
A 1 1953 ALA 1953 1953 1953 ALA ALA A . n 
A 1 1954 TRP 1954 1954 1954 TRP TRP A . n 
A 1 1955 GLY 1955 1955 1955 GLY GLY A . n 
A 1 1956 CYS 1956 1956 1956 CYS CYS A . n 
A 1 1957 PHE 1957 1957 1957 PHE PHE A . n 
A 1 1958 ASP 1958 1958 1958 ASP ASP A . n 
A 1 1959 GLU 1959 1959 1959 GLU GLU A . n 
A 1 1960 PHE 1960 1960 1960 PHE PHE A . n 
A 1 1961 ASN 1961 1961 1961 ASN ASN A . n 
A 1 1962 ARG 1962 1962 1962 ARG ARG A . n 
A 1 1963 LEU 1963 1963 1963 LEU LEU A . n 
A 1 1964 GLU 1964 1964 1964 GLU GLU A . n 
A 1 1965 GLU 1965 1965 1965 GLU GLU A . n 
A 1 1966 ARG 1966 1966 1966 ARG ARG A . n 
A 1 1967 MET 1967 1967 1967 MET MET A . n 
A 1 1968 LEU 1968 1968 1968 LEU LEU A . n 
A 1 1969 SER 1969 1969 1969 SER SER A . n 
A 1 1970 ALA 1970 1970 1970 ALA ALA A . n 
A 1 1971 VAL 1971 1971 1971 VAL VAL A . n 
A 1 1972 SER 1972 1972 1972 SER SER A . n 
A 1 1973 GLN 1973 1973 1973 GLN GLN A . n 
A 1 1974 GLN 1974 1974 1974 GLN GLN A . n 
A 1 1975 VAL 1975 1975 1975 VAL VAL A . n 
A 1 1976 GLN 1976 1976 1976 GLN GLN A . n 
A 1 1977 CYS 1977 1977 1977 CYS CYS A . n 
A 1 1978 ILE 1978 1978 1978 ILE ILE A . n 
A 1 1979 GLN 1979 1979 1979 GLN GLN A . n 
A 1 1980 GLU 1980 1980 1980 GLU GLU A . n 
A 1 1981 ALA 1981 1981 1981 ALA ALA A . n 
A 1 1982 LEU 1982 1982 1982 LEU LEU A . n 
A 1 1983 ARG 1983 1983 1983 ARG ARG A . n 
A 1 1984 GLU 1984 1984 1984 GLU GLU A . n 
A 1 1985 HIS 1985 1985 1985 HIS HIS A . n 
A 1 1986 SER 1986 1986 1986 SER SER A . n 
A 1 1987 ASN 1987 1987 1987 ASN ASN A . n 
A 1 1988 PRO 1988 1988 1988 PRO PRO A . n 
A 1 1989 ASN 1989 1989 1989 ASN ASN A . n 
A 1 1990 TYR 1990 1990 1990 TYR TYR A . n 
A 1 1991 ASP 1991 1991 1991 ASP ASP A . n 
A 1 1992 LYS 1992 1992 1992 LYS LYS A . n 
A 1 1993 THR 1993 1993 1993 THR THR A . n 
A 1 1994 SER 1994 1994 1994 SER SER A . n 
A 1 1995 ALA 1995 1995 1995 ALA ALA A . n 
A 1 1996 PRO 1996 1996 1996 PRO PRO A . n 
A 1 1997 ILE 1997 1997 1997 ILE ILE A . n 
A 1 1998 THR 1998 1998 1998 THR THR A . n 
A 1 1999 CYS 1999 1999 1999 CYS CYS A . n 
A 1 2000 GLU 2000 2000 2000 GLU GLU A . n 
A 1 2001 LEU 2001 2001 2001 LEU LEU A . n 
A 1 2002 LEU 2002 2002 2002 LEU LEU A . n 
A 1 2003 ASN 2003 2003 2003 ASN ASN A . n 
A 1 2004 LYS 2004 2004 2004 LYS LYS A . n 
A 1 2005 GLN 2005 2005 2005 GLN GLN A . n 
A 1 2006 VAL 2006 2006 2006 VAL VAL A . n 
A 1 2007 LYS 2007 2007 2007 LYS LYS A . n 
A 1 2008 VAL 2008 2008 2008 VAL VAL A . n 
A 1 2009 SER 2009 2009 2009 SER SER A . n 
A 1 2010 PRO 2010 2010 2010 PRO PRO A . n 
A 1 2011 ASP 2011 2011 2011 ASP ASP A . n 
A 1 2012 MET 2012 2012 2012 MET MET A . n 
A 1 2013 ALA 2013 2013 2013 ALA ALA A . n 
A 1 2014 ILE 2014 2014 2014 ILE ILE A . n 
A 1 2015 PHE 2015 2015 2015 PHE PHE A . n 
A 1 2016 ILE 2016 2016 2016 ILE ILE A . n 
A 1 2017 THR 2017 2017 2017 THR THR A . n 
A 1 2018 MET 2018 2018 2018 MET MET A . n 
A 1 2019 ASN 2019 2019 2019 ASN ASN A . n 
A 1 2020 PRO 2020 2020 2020 PRO PRO A . n 
A 1 2021 GLY 2021 2021 2021 GLY GLY A . n 
A 1 2022 TYR 2022 2022 2022 TYR TYR A . n 
A 1 2023 ALA 2023 2023 2023 ALA ALA A . n 
A 1 2024 GLY 2024 2024 2024 GLY GLY A . n 
A 1 2025 ARG 2025 2025 2025 ARG ARG A . n 
A 1 2026 SER 2026 2026 2026 SER SER A . n 
A 1 2027 ASN 2027 2027 2027 ASN ASN A . n 
A 1 2028 LEU 2028 2028 2028 LEU LEU A . n 
A 1 2029 PRO 2029 2029 2029 PRO PRO A . n 
A 1 2030 ASP 2030 2030 2030 ASP ASP A . n 
A 1 2031 ASN 2031 2031 2031 ASN ASN A . n 
A 1 2032 LEU 2032 2032 2032 LEU LEU A . n 
A 1 2033 LYS 2033 2033 2033 LYS LYS A . n 
A 1 2034 LYS 2034 2034 2034 LYS LYS A . n 
A 1 2035 LEU 2035 2035 2035 LEU LEU A . n 
A 1 2036 PHE 2036 2036 2036 PHE PHE A . n 
A 1 2037 ARG 2037 2037 2037 ARG ARG A . n 
A 1 2038 SER 2038 2038 2038 SER SER A . n 
A 1 2039 LEU 2039 2039 2039 LEU LEU A . n 
A 1 2040 ALA 2040 2040 2040 ALA ALA A . n 
A 1 2041 MET 2041 2041 2041 MET MET A . n 
A 1 2042 THR 2042 2042 2042 THR THR A . n 
A 1 2043 LYS 2043 2043 2043 LYS LYS A . n 
A 1 2044 PRO 2044 2044 2044 PRO PRO A . n 
A 1 2045 ASP 2045 2045 2045 ASP ASP A . n 
A 1 2046 ARG 2046 2046 2046 ARG ARG A . n 
A 1 2047 GLN 2047 2047 2047 GLN GLN A . n 
A 1 2048 LEU 2048 2048 2048 LEU LEU A . n 
A 1 2049 ILE 2049 2049 2049 ILE ILE A . n 
A 1 2050 ALA 2050 2050 2050 ALA ALA A . n 
A 1 2051 GLN 2051 2051 2051 GLN GLN A . n 
A 1 2052 VAL 2052 2052 2052 VAL VAL A . n 
A 1 2053 MET 2053 2053 2053 MET MET A . n 
A 1 2054 LEU 2054 2054 2054 LEU LEU A . n 
A 1 2055 TYR 2055 2055 2055 TYR TYR A . n 
A 1 2056 SER 2056 2056 2056 SER SER A . n 
A 1 2057 GLN 2057 2057 2057 GLN GLN A . n 
A 1 2058 GLY 2058 2058 2058 GLY GLY A . n 
A 1 2059 PHE 2059 2059 2059 PHE PHE A . n 
A 1 2060 ARG 2060 2060 2060 ARG ARG A . n 
A 1 2061 THR 2061 2061 2061 THR THR A . n 
A 1 2062 ALA 2062 2062 2062 ALA ALA A . n 
A 1 2063 GLU 2063 2063 2063 GLU GLU A . n 
A 1 2064 VAL 2064 2064 2064 VAL VAL A . n 
A 1 2065 LEU 2065 2065 2065 LEU LEU A . n 
A 1 2066 ALA 2066 2066 2066 ALA ALA A . n 
A 1 2067 ASN 2067 2067 2067 ASN ASN A . n 
A 1 2068 LYS 2068 2068 2068 LYS LYS A . n 
A 1 2069 ILE 2069 2069 2069 ILE ILE A . n 
A 1 2070 VAL 2070 2070 2070 VAL VAL A . n 
A 1 2071 PRO 2071 2071 2071 PRO PRO A . n 
A 1 2072 PHE 2072 2072 2072 PHE PHE A . n 
A 1 2073 PHE 2073 2073 2073 PHE PHE A . n 
A 1 2074 LYS 2074 2074 2074 LYS LYS A . n 
A 1 2075 LEU 2075 2075 2075 LEU LEU A . n 
A 1 2076 CYS 2076 2076 2076 CYS CYS A . n 
A 1 2077 ASP 2077 2077 2077 ASP ASP A . n 
A 1 2078 GLU 2078 2078 2078 GLU GLU A . n 
A 1 2079 GLN 2079 2079 2079 GLN GLN A . n 
A 1 2080 LEU 2080 2080 2080 LEU LEU A . n 
A 1 2081 SER 2081 2081 2081 SER SER A . n 
A 1 2082 SER 2082 2082 2082 SER SER A . n 
A 1 2083 GLN 2083 2083 2083 GLN GLN A . n 
A 1 2084 SER 2084 2084 2084 SER SER A . n 
A 1 2085 HIS 2085 2085 2085 HIS HIS A . n 
A 1 2086 TYR 2086 2086 2086 TYR TYR A . n 
A 1 2087 ASP 2087 2087 2087 ASP ASP A . n 
A 1 2088 PHE 2088 2088 2088 PHE PHE A . n 
A 1 2089 GLY 2089 2089 2089 GLY GLY A . n 
A 1 2090 LEU 2090 2090 2090 LEU LEU A . n 
A 1 2091 ARG 2091 2091 2091 ARG ARG A . n 
A 1 2092 ALA 2092 2092 2092 ALA ALA A . n 
A 1 2093 LEU 2093 2093 2093 LEU LEU A . n 
A 1 2094 LYS 2094 2094 2094 LYS LYS A . n 
A 1 2095 SER 2095 2095 2095 SER SER A . n 
A 1 2096 VAL 2096 2096 2096 VAL VAL A . n 
A 1 2097 LEU 2097 2097 2097 LEU LEU A . n 
A 1 2098 VAL 2098 2098 2098 VAL VAL A . n 
A 1 2099 SER 2099 2099 2099 SER SER A . n 
A 1 2100 ALA 2100 2100 2100 ALA ALA A . n 
A 1 2101 GLY 2101 2101 2101 GLY GLY A . n 
A 1 2102 ASN 2102 2102 2102 ASN ASN A . n 
A 1 2103 VAL 2103 2103 2103 VAL VAL A . n 
A 1 2104 LYS 2104 2104 2104 LYS LYS A . n 
A 1 2105 ARG 2105 2105 2105 ARG ARG A . n 
A 1 2106 GLU 2106 2106 2106 GLU GLU A . n 
A 1 2107 ARG 2107 2107 2107 ARG ARG A . n 
A 1 2108 ILE 2108 2108 2108 ILE ILE A . n 
A 1 2109 GLN 2109 2109 2109 GLN GLN A . n 
A 1 2110 LYS 2110 2110 2110 LYS LYS A . n 
A 1 2111 ILE 2111 2111 2111 ILE ILE A . n 
A 1 2112 LYS 2112 2112 2112 LYS LYS A . n 
A 1 2113 ARG 2113 2113 2113 ARG ARG A . n 
A 1 2114 GLU 2114 2114 2114 GLU GLU A . n 
A 1 2115 LYS 2115 2115 2115 LYS LYS A . n 
A 1 2116 GLU 2116 2116 2116 GLU GLU A . n 
A 1 2117 GLU 2117 2117 2117 GLU GLU A . n 
A 1 2118 ARG 2118 2118 2118 ARG ARG A . n 
A 1 2119 GLY 2119 2119 2119 GLY GLY A . n 
A 1 2120 GLU 2120 2120 2120 GLU GLU A . n 
A 1 2121 ALA 2121 2121 2121 ALA ALA A . n 
A 1 2122 VAL 2122 2122 2122 VAL VAL A . n 
A 1 2123 ASP 2123 2123 2123 ASP ASP A . n 
A 1 2124 GLU 2124 2124 2124 GLU GLU A . n 
A 1 2125 GLY 2125 2125 2125 GLY GLY A . n 
A 1 2126 GLU 2126 2126 2126 GLU GLU A . n 
A 1 2127 ILE 2127 2127 2127 ILE ILE A . n 
A 1 2128 ALA 2128 2128 2128 ALA ALA A . n 
A 1 2129 GLU 2129 2129 2129 GLU GLU A . n 
A 1 2130 ASN 2130 2130 2130 ASN ASN A . n 
A 1 2131 LEU 2131 2131 2131 LEU LEU A . n 
A 1 2132 PRO 2132 2132 2132 PRO PRO A . n 
A 1 2133 GLU 2133 2133 2133 GLU GLU A . n 
A 1 2134 GLN 2134 2134 2134 GLN GLN A . n 
A 1 2135 GLU 2135 2135 2135 GLU GLU A . n 
A 1 2136 ILE 2136 2136 2136 ILE ILE A . n 
A 1 2137 LEU 2137 2137 2137 LEU LEU A . n 
A 1 2138 ILE 2138 2138 2138 ILE ILE A . n 
A 1 2139 GLN 2139 2139 2139 GLN GLN A . n 
A 1 2140 SER 2140 2140 2140 SER SER A . n 
A 1 2141 VAL 2141 2141 2141 VAL VAL A . n 
A 1 2142 CYS 2142 2142 2142 CYS CYS A . n 
A 1 2143 GLU 2143 2143 2143 GLU GLU A . n 
A 1 2144 THR 2144 2144 2144 THR THR A . n 
A 1 2145 MET 2145 2145 2145 MET MET A . n 
A 1 2146 VAL 2146 2146 2146 VAL VAL A . n 
A 1 2147 PRO 2147 2147 2147 PRO PRO A . n 
A 1 2148 LYS 2148 2148 2148 LYS LYS A . n 
A 1 2149 LEU 2149 2149 2149 LEU LEU A . n 
A 1 2150 VAL 2150 2150 2150 VAL VAL A . n 
A 1 2151 ALA 2151 2151 2151 ALA ALA A . n 
A 1 2152 GLU 2152 2152 2152 GLU GLU A . n 
A 1 2153 ASP 2153 2153 2153 ASP ASP A . n 
A 1 2154 ILE 2154 2154 2154 ILE ILE A . n 
A 1 2155 PRO 2155 2155 2155 PRO PRO A . n 
A 1 2156 LEU 2156 2156 2156 LEU LEU A . n 
A 1 2157 LEU 2157 2157 2157 LEU LEU A . n 
A 1 2158 PHE 2158 2158 2158 PHE PHE A . n 
A 1 2159 SER 2159 2159 2159 SER SER A . n 
A 1 2160 LEU 2160 2160 2160 LEU LEU A . n 
A 1 2161 LEU 2161 2161 2161 LEU LEU A . n 
A 1 2162 SER 2162 2162 2162 SER SER A . n 
A 1 2163 ASP 2163 2163 2163 ASP ASP A . n 
A 1 2164 VAL 2164 2164 2164 VAL VAL A . n 
A 1 2165 PHE 2165 2165 2165 PHE PHE A . n 
A 1 2166 PRO 2166 2166 2166 PRO PRO A . n 
A 1 2167 GLY 2167 2167 2167 GLY GLY A . n 
A 1 2168 VAL 2168 2168 2168 VAL VAL A . n 
A 1 2169 GLN 2169 2169 2169 GLN GLN A . n 
A 1 2170 TYR 2170 2170 2170 TYR TYR A . n 
A 1 2171 HIS 2171 2171 2171 HIS HIS A . n 
A 1 2172 ARG 2172 2172 2172 ARG ARG A . n 
A 1 2173 GLY 2173 2173 2173 GLY GLY A . n 
A 1 2174 GLU 2174 2174 2174 GLU GLU A . n 
A 1 2175 MET 2175 2175 2175 MET MET A . n 
A 1 2176 THR 2176 2176 2176 THR THR A . n 
A 1 2177 ALA 2177 2177 2177 ALA ALA A . n 
A 1 2178 LEU 2178 2178 2178 LEU LEU A . n 
A 1 2179 ARG 2179 2179 2179 ARG ARG A . n 
A 1 2180 GLU 2180 2180 2180 GLU GLU A . n 
A 1 2181 GLU 2181 2181 2181 GLU GLU A . n 
A 1 2182 LEU 2182 2182 2182 LEU LEU A . n 
A 1 2183 LYS 2183 2183 2183 LYS LYS A . n 
A 1 2184 LYS 2184 2184 2184 LYS LYS A . n 
A 1 2185 VAL 2185 2185 2185 VAL VAL A . n 
A 1 2186 CYS 2186 2186 2186 CYS CYS A . n 
A 1 2187 GLN 2187 2187 2187 GLN GLN A . n 
A 1 2188 GLU 2188 2188 2188 GLU GLU A . n 
A 1 2189 MET 2189 2189 2189 MET MET A . n 
A 1 2190 TYR 2190 2190 2190 TYR TYR A . n 
A 1 2191 LEU 2191 2191 2191 LEU LEU A . n 
A 1 2192 THR 2192 2192 2192 THR THR A . n 
A 1 2193 TYR 2193 2193 2193 TYR TYR A . n 
A 1 2194 GLY 2194 2194 2194 GLY GLY A . n 
A 1 2195 ASP 2195 2195 2195 ASP ASP A . n 
A 1 2196 GLY 2196 2196 2196 GLY GLY A . n 
A 1 2197 GLU 2197 2197 2197 GLU GLU A . n 
A 1 2198 GLU 2198 2198 2198 GLU GLU A . n 
A 1 2199 VAL 2199 2199 2199 VAL VAL A . n 
A 1 2200 GLY 2200 2200 2200 GLY GLY A . n 
A 1 2201 GLY 2201 2201 2201 GLY GLY A . n 
A 1 2202 MET 2202 2202 2202 MET MET A . n 
A 1 2203 TRP 2203 2203 2203 TRP TRP A . n 
A 1 2204 VAL 2204 2204 2204 VAL VAL A . n 
A 1 2205 GLU 2205 2205 2205 GLU GLU A . n 
A 1 2206 LYS 2206 2206 2206 LYS LYS A . n 
A 1 2207 VAL 2207 2207 2207 VAL VAL A . n 
A 1 2208 LEU 2208 2208 2208 LEU LEU A . n 
A 1 2209 GLN 2209 2209 2209 GLN GLN A . n 
A 1 2210 LEU 2210 2210 2210 LEU LEU A . n 
A 1 2211 TYR 2211 2211 2211 TYR TYR A . n 
A 1 2212 GLN 2212 2212 2212 GLN GLN A . n 
A 1 2213 ILE 2213 2213 2213 ILE ILE A . n 
A 1 2214 THR 2214 2214 2214 THR THR A . n 
A 1 2215 GLN 2215 2215 2215 GLN GLN A . n 
A 1 2216 ILE 2216 2216 2216 ILE ILE A . n 
A 1 2217 ASN 2217 2217 2217 ASN ASN A . n 
A 1 2218 HIS 2218 2218 2218 HIS HIS A . n 
A 1 2219 GLY 2219 2219 2219 GLY GLY A . n 
A 1 2220 LEU 2220 2220 2220 LEU LEU A . n 
A 1 2221 MET 2221 2221 2221 MET MET A . n 
A 1 2222 MET 2222 2222 2222 MET MET A . n 
A 1 2223 VAL 2223 2223 2223 VAL VAL A . n 
A 1 2224 GLY 2224 2224 2224 GLY GLY A . n 
A 1 2225 PRO 2225 2225 2225 PRO PRO A . n 
A 1 2226 SER 2226 2226 2226 SER SER A . n 
A 1 2227 GLY 2227 2227 2227 GLY GLY A . n 
A 1 2228 SER 2228 2228 2228 SER SER A . n 
A 1 2229 GLY 2229 2229 2229 GLY GLY A . n 
A 1 2230 LYS 2230 2230 2230 LYS LYS A . n 
A 1 2231 SER 2231 2231 2231 SER SER A . n 
A 1 2232 MET 2232 2232 2232 MET MET A . n 
A 1 2233 ALA 2233 2233 2233 ALA ALA A . n 
A 1 2234 TRP 2234 2234 2234 TRP TRP A . n 
A 1 2235 ARG 2235 2235 2235 ARG ARG A . n 
A 1 2236 VAL 2236 2236 2236 VAL VAL A . n 
A 1 2237 LEU 2237 2237 2237 LEU LEU A . n 
A 1 2238 LEU 2238 2238 2238 LEU LEU A . n 
A 1 2239 LYS 2239 2239 2239 LYS LYS A . n 
A 1 2240 ALA 2240 2240 2240 ALA ALA A . n 
A 1 2241 LEU 2241 2241 2241 LEU LEU A . n 
A 1 2242 GLU 2242 2242 2242 GLU GLU A . n 
A 1 2243 ARG 2243 2243 2243 ARG ARG A . n 
A 1 2244 LEU 2244 2244 2244 LEU LEU A . n 
A 1 2245 GLU 2245 2245 2245 GLU GLU A . n 
A 1 2246 GLY 2246 2246 2246 GLY GLY A . n 
A 1 2247 VAL 2247 2247 2247 VAL VAL A . n 
A 1 2248 GLU 2248 2248 2248 GLU GLU A . n 
A 1 2249 GLY 2249 2249 2249 GLY GLY A . n 
A 1 2250 VAL 2250 2250 2250 VAL VAL A . n 
A 1 2251 ALA 2251 2251 2251 ALA ALA A . n 
A 1 2252 HIS 2252 2252 2252 HIS HIS A . n 
A 1 2253 ILE 2253 2253 2253 ILE ILE A . n 
A 1 2254 ILE 2254 2254 2254 ILE ILE A . n 
A 1 2255 ASP 2255 2255 2255 ASP ASP A . n 
A 1 2256 PRO 2256 2256 2256 PRO PRO A . n 
A 1 2257 LYS 2257 2257 2257 LYS LYS A . n 
A 1 2258 ALA 2258 2258 2258 ALA ALA A . n 
A 1 2259 ILE 2259 2259 2259 ILE ILE A . n 
A 1 2260 SER 2260 2260 2260 SER SER A . n 
A 1 2261 LYS 2261 2261 2261 LYS LYS A . n 
A 1 2262 ASP 2262 2262 2262 ASP ASP A . n 
A 1 2263 HIS 2263 2263 2263 HIS HIS A . n 
A 1 2264 LEU 2264 2264 2264 LEU LEU A . n 
A 1 2265 TYR 2265 2265 2265 TYR TYR A . n 
A 1 2266 GLY 2266 2266 2266 GLY GLY A . n 
A 1 2267 THR 2267 2267 2267 THR THR A . n 
A 1 2268 LEU 2268 2268 2268 LEU LEU A . n 
A 1 2269 ASP 2269 2269 2269 ASP ASP A . n 
A 1 2270 PRO 2270 2270 2270 PRO PRO A . n 
A 1 2271 ASN 2271 2271 2271 ASN ASN A . n 
A 1 2272 THR 2272 2272 2272 THR THR A . n 
A 1 2273 ARG 2273 2273 2273 ARG ARG A . n 
A 1 2274 GLU 2274 2274 2274 GLU GLU A . n 
A 1 2275 TRP 2275 2275 2275 TRP TRP A . n 
A 1 2276 THR 2276 2276 2276 THR THR A . n 
A 1 2277 ASP 2277 2277 2277 ASP ASP A . n 
A 1 2278 GLY 2278 2278 2278 GLY GLY A . n 
A 1 2279 LEU 2279 2279 2279 LEU LEU A . n 
A 1 2280 PHE 2280 2280 2280 PHE PHE A . n 
A 1 2281 THR 2281 2281 2281 THR THR A . n 
A 1 2282 HIS 2282 2282 2282 HIS HIS A . n 
A 1 2283 VAL 2283 2283 2283 VAL VAL A . n 
A 1 2284 LEU 2284 2284 2284 LEU LEU A . n 
A 1 2285 ARG 2285 2285 2285 ARG ARG A . n 
A 1 2286 LYS 2286 2286 2286 LYS LYS A . n 
A 1 2287 ILE 2287 2287 2287 ILE ILE A . n 
A 1 2288 ILE 2288 2288 2288 ILE ILE A . n 
A 1 2289 ASP 2289 2289 2289 ASP ASP A . n 
A 1 2290 SER 2290 2290 2290 SER SER A . n 
A 1 2291 VAL 2291 2291 2291 VAL VAL A . n 
A 1 2292 ARG 2292 2292 2292 ARG ARG A . n 
A 1 2293 GLY 2293 2293 2293 GLY GLY A . n 
A 1 2294 GLU 2294 2294 2294 GLU GLU A . n 
A 1 2295 LEU 2295 2295 2295 LEU LEU A . n 
A 1 2296 GLN 2296 2296 2296 GLN GLN A . n 
A 1 2297 LYS 2297 2297 2297 LYS LYS A . n 
A 1 2298 ARG 2298 2298 2298 ARG ARG A . n 
A 1 2299 GLN 2299 2299 2299 GLN GLN A . n 
A 1 2300 TRP 2300 2300 2300 TRP TRP A . n 
A 1 2301 ILE 2301 2301 2301 ILE ILE A . n 
A 1 2302 VAL 2302 2302 2302 VAL VAL A . n 
A 1 2303 PHE 2303 2303 2303 PHE PHE A . n 
A 1 2304 ASP 2304 2304 2304 ASP ASP A . n 
A 1 2305 GLY 2305 2305 2305 GLY GLY A . n 
A 1 2306 ASP 2306 2306 2306 ASP ASP A . n 
A 1 2307 VAL 2307 2307 2307 VAL VAL A . n 
A 1 2308 ASP 2308 2308 2308 ASP ASP A . n 
A 1 2309 PRO 2309 2309 2309 PRO PRO A . n 
A 1 2310 GLU 2310 2310 2310 GLU GLU A . n 
A 1 2311 TRP 2311 2311 2311 TRP TRP A . n 
A 1 2312 VAL 2312 2312 2312 VAL VAL A . n 
A 1 2313 GLU 2313 2313 2313 GLU GLU A . n 
A 1 2314 ASN 2314 2314 2314 ASN ASN A . n 
A 1 2315 LEU 2315 2315 2315 LEU LEU A . n 
A 1 2316 ASN 2316 2316 2316 ASN ASN A . n 
A 1 2317 SER 2317 2317 2317 SER SER A . n 
A 1 2318 VAL 2318 2318 2318 VAL VAL A . n 
A 1 2319 LEU 2319 2319 2319 LEU LEU A . n 
A 1 2320 ASP 2320 2320 2320 ASP ASP A . n 
A 1 2321 ASP 2321 2321 2321 ASP ASP A . n 
A 1 2322 ASN 2322 2322 2322 ASN ASN A . n 
A 1 2323 LYS 2323 2323 2323 LYS LYS A . n 
A 1 2324 LEU 2324 2324 2324 LEU LEU A . n 
A 1 2325 LEU 2325 2325 2325 LEU LEU A . n 
A 1 2326 THR 2326 2326 2326 THR THR A . n 
A 1 2327 LEU 2327 2327 2327 LEU LEU A . n 
A 1 2328 PRO 2328 2328 2328 PRO PRO A . n 
A 1 2329 ASN 2329 2329 2329 ASN ASN A . n 
A 1 2330 GLY 2330 2330 2330 GLY GLY A . n 
A 1 2331 GLU 2331 2331 2331 GLU GLU A . n 
A 1 2332 ARG 2332 2332 2332 ARG ARG A . n 
A 1 2333 LEU 2333 2333 2333 LEU LEU A . n 
A 1 2334 SER 2334 2334 2334 SER SER A . n 
A 1 2335 LEU 2335 2335 2335 LEU LEU A . n 
A 1 2336 PRO 2336 2336 2336 PRO PRO A . n 
A 1 2337 PRO 2337 2337 2337 PRO PRO A . n 
A 1 2338 ASN 2338 2338 2338 ASN ASN A . n 
A 1 2339 VAL 2339 2339 2339 VAL VAL A . n 
A 1 2340 ARG 2340 2340 2340 ARG ARG A . n 
A 1 2341 ILE 2341 2341 2341 ILE ILE A . n 
A 1 2342 MET 2342 2342 2342 MET MET A . n 
A 1 2343 PHE 2343 2343 2343 PHE PHE A . n 
A 1 2344 GLU 2344 2344 2344 GLU GLU A . n 
A 1 2345 VAL 2345 2345 2345 VAL VAL A . n 
A 1 2346 GLN 2346 2346 2346 GLN GLN A . n 
A 1 2347 ASP 2347 2347 2347 ASP ASP A . n 
A 1 2348 LEU 2348 2348 2348 LEU LEU A . n 
A 1 2349 LYS 2349 2349 2349 LYS LYS A . n 
A 1 2350 TYR 2350 2350 2350 TYR TYR A . n 
A 1 2351 ALA 2351 2351 2351 ALA ALA A . n 
A 1 2352 THR 2352 2352 2352 THR THR A . n 
A 1 2353 LEU 2353 2353 2353 LEU LEU A . n 
A 1 2354 ALA 2354 2354 2354 ALA ALA A . n 
A 1 2355 THR 2355 2355 2355 THR THR A . n 
A 1 2356 VAL 2356 2356 2356 VAL VAL A . n 
A 1 2357 SER 2357 2357 2357 SER SER A . n 
A 1 2358 ARG 2358 2358 2358 ARG ARG A . n 
A 1 2359 CYS 2359 2359 2359 CYS CYS A . n 
A 1 2360 GLY 2360 2360 2360 GLY GLY A . n 
A 1 2361 MET 2361 2361 2361 MET MET A . n 
A 1 2362 VAL 2362 2362 2362 VAL VAL A . n 
A 1 2363 TRP 2363 2363 2363 TRP TRP A . n 
A 1 2364 PHE 2364 2364 2364 PHE PHE A . n 
A 1 2365 SER 2365 2365 2365 SER SER A . n 
A 1 2366 GLU 2366 2366 2366 GLU GLU A . n 
A 1 2367 ASP 2367 2367 2367 ASP ASP A . n 
A 1 2368 VAL 2368 2368 2368 VAL VAL A . n 
A 1 2369 LEU 2369 2369 2369 LEU LEU A . n 
A 1 2370 SER 2370 2370 2370 SER SER A . n 
A 1 2371 THR 2371 2371 2371 THR THR A . n 
A 1 2372 ASP 2372 2372 2372 ASP ASP A . n 
A 1 2373 MET 2373 2373 2373 MET MET A . n 
A 1 2374 ILE 2374 2374 2374 ILE ILE A . n 
A 1 2375 PHE 2375 2375 2375 PHE PHE A . n 
A 1 2376 ASN 2376 2376 2376 ASN ASN A . n 
A 1 2377 ASN 2377 2377 2377 ASN ASN A . n 
A 1 2378 PHE 2378 2378 2378 PHE PHE A . n 
A 1 2379 LEU 2379 2379 2379 LEU LEU A . n 
A 1 2380 ALA 2380 2380 2380 ALA ALA A . n 
A 1 2381 ARG 2381 2381 2381 ARG ARG A . n 
A 1 2382 LEU 2382 2382 2382 LEU LEU A . n 
A 1 2383 ARG 2383 2383 2383 ARG ARG A . n 
A 1 2384 SER 2384 2384 2384 SER SER A . n 
A 1 2385 ILE 2385 2385 2385 ILE ILE A . n 
A 1 2386 PRO 2386 2386 2386 PRO PRO A . n 
A 1 2387 LEU 2387 2387 2387 LEU LEU A . n 
A 1 2388 ASP 2388 2388 2388 ASP ASP A . n 
A 1 2389 GLU 2389 2389 2389 GLU GLU A . n 
A 1 2390 GLY 2390 2390 ?    ?   ?   A . n 
A 1 2391 GLU 2391 2391 ?    ?   ?   A . n 
A 1 2392 ASP 2392 2392 ?    ?   ?   A . n 
A 1 2393 GLU 2393 2393 ?    ?   ?   A . n 
A 1 2394 ALA 2394 2394 ?    ?   ?   A . n 
A 1 2395 GLN 2395 2395 ?    ?   ?   A . n 
A 1 2396 ARG 2396 2396 ?    ?   ?   A . n 
A 1 2397 ARG 2397 2397 ?    ?   ?   A . n 
A 1 2398 ARG 2398 2398 ?    ?   ?   A . n 
A 1 2399 LYS 2399 2399 ?    ?   ?   A . n 
A 1 2400 GLY 2400 2400 ?    ?   ?   A . n 
A 1 2401 LYS 2401 2401 ?    ?   ?   A . n 
A 1 2402 GLU 2402 2402 ?    ?   ?   A . n 
A 1 2403 ASP 2403 2403 ?    ?   ?   A . n 
A 1 2404 GLU 2404 2404 ?    ?   ?   A . n 
A 1 2405 GLY 2405 2405 ?    ?   ?   A . n 
A 1 2406 GLU 2406 2406 ?    ?   ?   A . n 
A 1 2407 GLU 2407 2407 ?    ?   ?   A . n 
A 1 2408 ALA 2408 2408 ?    ?   ?   A . n 
A 1 2409 ALA 2409 2409 ?    ?   ?   A . n 
A 1 2410 SER 2410 2410 2410 SER SER A . n 
A 1 2411 PRO 2411 2411 2411 PRO PRO A . n 
A 1 2412 MET 2412 2412 2412 MET MET A . n 
A 1 2413 LEU 2413 2413 2413 LEU LEU A . n 
A 1 2414 GLN 2414 2414 2414 GLN GLN A . n 
A 1 2415 ILE 2415 2415 2415 ILE ILE A . n 
A 1 2416 GLN 2416 2416 2416 GLN GLN A . n 
A 1 2417 ARG 2417 2417 2417 ARG ARG A . n 
A 1 2418 ASP 2418 2418 2418 ASP ASP A . n 
A 1 2419 ALA 2419 2419 2419 ALA ALA A . n 
A 1 2420 ALA 2420 2420 2420 ALA ALA A . n 
A 1 2421 THR 2421 2421 2421 THR THR A . n 
A 1 2422 ILE 2422 2422 2422 ILE ILE A . n 
A 1 2423 MET 2423 2423 2423 MET MET A . n 
A 1 2424 GLN 2424 2424 2424 GLN GLN A . n 
A 1 2425 PRO 2425 2425 2425 PRO PRO A . n 
A 1 2426 TYR 2426 2426 2426 TYR TYR A . n 
A 1 2427 PHE 2427 2427 2427 PHE PHE A . n 
A 1 2428 THR 2428 2428 2428 THR THR A . n 
A 1 2429 SER 2429 2429 2429 SER SER A . n 
A 1 2430 ASN 2430 2430 2430 ASN ASN A . n 
A 1 2431 GLY 2431 2431 2431 GLY GLY A . n 
A 1 2432 LEU 2432 2432 2432 LEU LEU A . n 
A 1 2433 VAL 2433 2433 2433 VAL VAL A . n 
A 1 2434 THR 2434 2434 2434 THR THR A . n 
A 1 2435 LYS 2435 2435 2435 LYS LYS A . n 
A 1 2436 ALA 2436 2436 2436 ALA ALA A . n 
A 1 2437 LEU 2437 2437 2437 LEU LEU A . n 
A 1 2438 GLU 2438 2438 2438 GLU GLU A . n 
A 1 2439 HIS 2439 2439 2439 HIS HIS A . n 
A 1 2440 ALA 2440 2440 2440 ALA ALA A . n 
A 1 2441 PHE 2441 2441 2441 PHE PHE A . n 
A 1 2442 GLN 2442 2442 2442 GLN GLN A . n 
A 1 2443 LEU 2443 2443 2443 LEU LEU A . n 
A 1 2444 GLU 2444 2444 2444 GLU GLU A . n 
A 1 2445 HIS 2445 2445 2445 HIS HIS A . n 
A 1 2446 ILE 2446 2446 2446 ILE ILE A . n 
A 1 2447 MET 2447 2447 2447 MET MET A . n 
A 1 2448 ASP 2448 2448 2448 ASP ASP A . n 
A 1 2449 LEU 2449 2449 2449 LEU LEU A . n 
A 1 2450 THR 2450 2450 2450 THR THR A . n 
A 1 2451 ARG 2451 2451 2451 ARG ARG A . n 
A 1 2452 LEU 2452 2452 2452 LEU LEU A . n 
A 1 2453 ARG 2453 2453 2453 ARG ARG A . n 
A 1 2454 CYS 2454 2454 2454 CYS CYS A . n 
A 1 2455 LEU 2455 2455 2455 LEU LEU A . n 
A 1 2456 GLY 2456 2456 2456 GLY GLY A . n 
A 1 2457 SER 2457 2457 2457 SER SER A . n 
A 1 2458 LEU 2458 2458 2458 LEU LEU A . n 
A 1 2459 PHE 2459 2459 2459 PHE PHE A . n 
A 1 2460 SER 2460 2460 2460 SER SER A . n 
A 1 2461 MET 2461 2461 2461 MET MET A . n 
A 1 2462 LEU 2462 2462 2462 LEU LEU A . n 
A 1 2463 HIS 2463 2463 2463 HIS HIS A . n 
A 1 2464 GLN 2464 2464 2464 GLN GLN A . n 
A 1 2465 ALA 2465 2465 2465 ALA ALA A . n 
A 1 2466 CYS 2466 2466 2466 CYS CYS A . n 
A 1 2467 ARG 2467 2467 2467 ARG ARG A . n 
A 1 2468 ASN 2468 2468 2468 ASN ASN A . n 
A 1 2469 VAL 2469 2469 2469 VAL VAL A . n 
A 1 2470 ALA 2470 2470 2470 ALA ALA A . n 
A 1 2471 GLN 2471 2471 2471 GLN GLN A . n 
A 1 2472 TYR 2472 2472 2472 TYR TYR A . n 
A 1 2473 ASN 2473 2473 2473 ASN ASN A . n 
A 1 2474 ALA 2474 2474 2474 ALA ALA A . n 
A 1 2475 ASN 2475 2475 2475 ASN ASN A . n 
A 1 2476 HIS 2476 2476 2476 HIS HIS A . n 
A 1 2477 PRO 2477 2477 2477 PRO PRO A . n 
A 1 2478 ASP 2478 2478 2478 ASP ASP A . n 
A 1 2479 PHE 2479 2479 2479 PHE PHE A . n 
A 1 2480 PRO 2480 2480 2480 PRO PRO A . n 
A 1 2481 MET 2481 2481 2481 MET MET A . n 
A 1 2482 GLN 2482 2482 2482 GLN GLN A . n 
A 1 2483 ILE 2483 2483 2483 ILE ILE A . n 
A 1 2484 GLU 2484 2484 2484 GLU GLU A . n 
A 1 2485 GLN 2485 2485 2485 GLN GLN A . n 
A 1 2486 LEU 2486 2486 2486 LEU LEU A . n 
A 1 2487 GLU 2487 2487 2487 GLU GLU A . n 
A 1 2488 ARG 2488 2488 2488 ARG ARG A . n 
A 1 2489 TYR 2489 2489 2489 TYR TYR A . n 
A 1 2490 ILE 2490 2490 2490 ILE ILE A . n 
A 1 2491 GLN 2491 2491 2491 GLN GLN A . n 
A 1 2492 ARG 2492 2492 2492 ARG ARG A . n 
A 1 2493 TYR 2493 2493 2493 TYR TYR A . n 
A 1 2494 LEU 2494 2494 2494 LEU LEU A . n 
A 1 2495 VAL 2495 2495 2495 VAL VAL A . n 
A 1 2496 TYR 2496 2496 2496 TYR TYR A . n 
A 1 2497 ALA 2497 2497 2497 ALA ALA A . n 
A 1 2498 ILE 2498 2498 2498 ILE ILE A . n 
A 1 2499 LEU 2499 2499 2499 LEU LEU A . n 
A 1 2500 TRP 2500 2500 2500 TRP TRP A . n 
A 1 2501 SER 2501 2501 2501 SER SER A . n 
A 1 2502 LEU 2502 2502 2502 LEU LEU A . n 
A 1 2503 SER 2503 2503 2503 SER SER A . n 
A 1 2504 GLY 2504 2504 2504 GLY GLY A . n 
A 1 2505 ASP 2505 2505 2505 ASP ASP A . n 
A 1 2506 SER 2506 2506 2506 SER SER A . n 
A 1 2507 ARG 2507 2507 2507 ARG ARG A . n 
A 1 2508 LEU 2508 2508 2508 LEU LEU A . n 
A 1 2509 LYS 2509 2509 2509 LYS LYS A . n 
A 1 2510 MET 2510 2510 2510 MET MET A . n 
A 1 2511 ARG 2511 2511 2511 ARG ARG A . n 
A 1 2512 ALA 2512 2512 2512 ALA ALA A . n 
A 1 2513 GLU 2513 2513 2513 GLU GLU A . n 
A 1 2514 LEU 2514 2514 2514 LEU LEU A . n 
A 1 2515 GLY 2515 2515 2515 GLY GLY A . n 
A 1 2516 GLU 2516 2516 2516 GLU GLU A . n 
A 1 2517 TYR 2517 2517 2517 TYR TYR A . n 
A 1 2518 ILE 2518 2518 2518 ILE ILE A . n 
A 1 2519 ARG 2519 2519 2519 ARG ARG A . n 
A 1 2520 ARG 2520 2520 2520 ARG ARG A . n 
A 1 2521 ILE 2521 2521 2521 ILE ILE A . n 
A 1 2522 THR 2522 2522 2522 THR THR A . n 
A 1 2523 THR 2523 2523 2523 THR THR A . n 
A 1 2524 VAL 2524 2524 2524 VAL VAL A . n 
A 1 2525 PRO 2525 2525 2525 PRO PRO A . n 
A 1 2526 LEU 2526 2526 2526 LEU LEU A . n 
A 1 2527 PRO 2527 2527 2527 PRO PRO A . n 
A 1 2528 THR 2528 2528 2528 THR THR A . n 
A 1 2529 ALA 2529 2529 2529 ALA ALA A . n 
A 1 2530 PRO 2530 2530 2530 PRO PRO A . n 
A 1 2531 ASN 2531 2531 2531 ASN ASN A . n 
A 1 2532 ILE 2532 2532 2532 ILE ILE A . n 
A 1 2533 PRO 2533 2533 2533 PRO PRO A . n 
A 1 2534 ILE 2534 2534 2534 ILE ILE A . n 
A 1 2535 ILE 2535 2535 2535 ILE ILE A . n 
A 1 2536 ASP 2536 2536 2536 ASP ASP A . n 
A 1 2537 TYR 2537 2537 2537 TYR TYR A . n 
A 1 2538 GLU 2538 2538 2538 GLU GLU A . n 
A 1 2539 VAL 2539 2539 2539 VAL VAL A . n 
A 1 2540 SER 2540 2540 2540 SER SER A . n 
A 1 2541 ILE 2541 2541 2541 ILE ILE A . n 
A 1 2542 SER 2542 2542 2542 SER SER A . n 
A 1 2543 GLY 2543 2543 2543 GLY GLY A . n 
A 1 2544 GLU 2544 2544 2544 GLU GLU A . n 
A 1 2545 TRP 2545 2545 2545 TRP TRP A . n 
A 1 2546 SER 2546 2546 2546 SER SER A . n 
A 1 2547 PRO 2547 2547 2547 PRO PRO A . n 
A 1 2548 TRP 2548 2548 2548 TRP TRP A . n 
A 1 2549 GLN 2549 2549 2549 GLN GLN A . n 
A 1 2550 ALA 2550 2550 2550 ALA ALA A . n 
A 1 2551 LYS 2551 2551 2551 LYS LYS A . n 
A 1 2552 VAL 2552 2552 2552 VAL VAL A . n 
A 1 2553 PRO 2553 2553 2553 PRO PRO A . n 
A 1 2554 GLN 2554 2554 2554 GLN GLN A . n 
A 1 2555 ILE 2555 2555 2555 ILE ILE A . n 
A 1 2556 GLU 2556 2556 2556 GLU GLU A . n 
A 1 2557 VAL 2557 2557 2557 VAL VAL A . n 
A 1 2558 GLU 2558 2558 2558 GLU GLU A . n 
A 1 2559 THR 2559 2559 2559 THR THR A . n 
A 1 2560 HIS 2560 2560 2560 HIS HIS A . n 
A 1 2561 LYS 2561 2561 2561 LYS LYS A . n 
A 1 2562 VAL 2562 2562 2562 VAL VAL A . n 
A 1 2563 ALA 2563 2563 2563 ALA ALA A . n 
A 1 2564 ALA 2564 2564 2564 ALA ALA A . n 
A 1 2565 PRO 2565 2565 2565 PRO PRO A . n 
A 1 2566 ASP 2566 2566 2566 ASP ASP A . n 
A 1 2567 VAL 2567 2567 2567 VAL VAL A . n 
A 1 2568 VAL 2568 2568 2568 VAL VAL A . n 
A 1 2569 VAL 2569 2569 2569 VAL VAL A . n 
A 1 2570 PRO 2570 2570 2570 PRO PRO A . n 
A 1 2571 THR 2571 2571 2571 THR THR A . n 
A 1 2572 LEU 2572 2572 2572 LEU LEU A . n 
A 1 2573 ASP 2573 2573 2573 ASP ASP A . n 
A 1 2574 THR 2574 2574 2574 THR THR A . n 
A 1 2575 VAL 2575 2575 2575 VAL VAL A . n 
A 1 2576 ARG 2576 2576 2576 ARG ARG A . n 
A 1 2577 HIS 2577 2577 2577 HIS HIS A . n 
A 1 2578 GLU 2578 2578 2578 GLU GLU A . n 
A 1 2579 ALA 2579 2579 2579 ALA ALA A . n 
A 1 2580 LEU 2580 2580 2580 LEU LEU A . n 
A 1 2581 LEU 2581 2581 2581 LEU LEU A . n 
A 1 2582 TYR 2582 2582 2582 TYR TYR A . n 
A 1 2583 THR 2583 2583 2583 THR THR A . n 
A 1 2584 TRP 2584 2584 2584 TRP TRP A . n 
A 1 2585 LEU 2585 2585 2585 LEU LEU A . n 
A 1 2586 ALA 2586 2586 2586 ALA ALA A . n 
A 1 2587 GLU 2587 2587 2587 GLU GLU A . n 
A 1 2588 HIS 2588 2588 2588 HIS HIS A . n 
A 1 2589 LYS 2589 2589 2589 LYS LYS A . n 
A 1 2590 PRO 2590 2590 2590 PRO PRO A . n 
A 1 2591 LEU 2591 2591 2591 LEU LEU A . n 
A 1 2592 VAL 2592 2592 2592 VAL VAL A . n 
A 1 2593 LEU 2593 2593 2593 LEU LEU A . n 
A 1 2594 CYS 2594 2594 2594 CYS CYS A . n 
A 1 2595 GLY 2595 2595 2595 GLY GLY A . n 
A 1 2596 PRO 2596 2596 2596 PRO PRO A . n 
A 1 2597 PRO 2597 2597 2597 PRO PRO A . n 
A 1 2598 GLY 2598 2598 2598 GLY GLY A . n 
A 1 2599 SER 2599 2599 2599 SER SER A . n 
A 1 2600 GLY 2600 2600 2600 GLY GLY A . n 
A 1 2601 LYS 2601 2601 2601 LYS LYS A . n 
A 1 2602 THR 2602 2602 2602 THR THR A . n 
A 1 2603 MET 2603 2603 2603 MET MET A . n 
A 1 2604 THR 2604 2604 2604 THR THR A . n 
A 1 2605 LEU 2605 2605 2605 LEU LEU A . n 
A 1 2606 PHE 2606 2606 2606 PHE PHE A . n 
A 1 2607 SER 2607 2607 2607 SER SER A . n 
A 1 2608 ALA 2608 2608 2608 ALA ALA A . n 
A 1 2609 LEU 2609 2609 2609 LEU LEU A . n 
A 1 2610 ARG 2610 2610 2610 ARG ARG A . n 
A 1 2611 ALA 2611 2611 2611 ALA ALA A . n 
A 1 2612 LEU 2612 2612 2612 LEU LEU A . n 
A 1 2613 PRO 2613 2613 2613 PRO PRO A . n 
A 1 2614 ASP 2614 2614 2614 ASP ASP A . n 
A 1 2615 MET 2615 2615 2615 MET MET A . n 
A 1 2616 GLU 2616 2616 2616 GLU GLU A . n 
A 1 2617 VAL 2617 2617 2617 VAL VAL A . n 
A 1 2618 VAL 2618 2618 2618 VAL VAL A . n 
A 1 2619 GLY 2619 2619 2619 GLY GLY A . n 
A 1 2620 LEU 2620 2620 2620 LEU LEU A . n 
A 1 2621 ASN 2621 2621 2621 ASN ASN A . n 
A 1 2622 PHE 2622 2622 2622 PHE PHE A . n 
A 1 2623 SER 2623 2623 2623 SER SER A . n 
A 1 2624 SER 2624 2624 2624 SER SER A . n 
A 1 2625 ALA 2625 2625 2625 ALA ALA A . n 
A 1 2626 THR 2626 2626 2626 THR THR A . n 
A 1 2627 THR 2627 2627 2627 THR THR A . n 
A 1 2628 PRO 2628 2628 2628 PRO PRO A . n 
A 1 2629 GLU 2629 2629 2629 GLU GLU A . n 
A 1 2630 LEU 2630 2630 2630 LEU LEU A . n 
A 1 2631 LEU 2631 2631 2631 LEU LEU A . n 
A 1 2632 LEU 2632 2632 2632 LEU LEU A . n 
A 1 2633 LYS 2633 2633 2633 LYS LYS A . n 
A 1 2634 THR 2634 2634 2634 THR THR A . n 
A 1 2635 PHE 2635 2635 2635 PHE PHE A . n 
A 1 2636 ASP 2636 2636 2636 ASP ASP A . n 
A 1 2637 HIS 2637 2637 2637 HIS HIS A . n 
A 1 2638 TYR 2638 2638 2638 TYR TYR A . n 
A 1 2639 CYS 2639 2639 2639 CYS CYS A . n 
A 1 2640 GLU 2640 2640 2640 GLU GLU A . n 
A 1 2641 TYR 2641 2641 2641 TYR TYR A . n 
A 1 2642 ARG 2642 2642 2642 ARG ARG A . n 
A 1 2643 ARG 2643 2643 2643 ARG ARG A . n 
A 1 2644 THR 2644 2644 2644 THR THR A . n 
A 1 2645 PRO 2645 2645 2645 PRO PRO A . n 
A 1 2646 ASN 2646 2646 2646 ASN ASN A . n 
A 1 2647 GLY 2647 2647 2647 GLY GLY A . n 
A 1 2648 VAL 2648 2648 2648 VAL VAL A . n 
A 1 2649 VAL 2649 2649 2649 VAL VAL A . n 
A 1 2650 LEU 2650 2650 2650 LEU LEU A . n 
A 1 2651 ALA 2651 2651 2651 ALA ALA A . n 
A 1 2652 PRO 2652 2652 2652 PRO PRO A . n 
A 1 2653 VAL 2653 2653 2653 VAL VAL A . n 
A 1 2654 GLN 2654 2654 2654 GLN GLN A . n 
A 1 2655 LEU 2655 2655 2655 LEU LEU A . n 
A 1 2656 GLY 2656 2656 2656 GLY GLY A . n 
A 1 2657 LYS 2657 2657 2657 LYS LYS A . n 
A 1 2658 TRP 2658 2658 2658 TRP TRP A . n 
A 1 2659 LEU 2659 2659 2659 LEU LEU A . n 
A 1 2660 VAL 2660 2660 2660 VAL VAL A . n 
A 1 2661 LEU 2661 2661 2661 LEU LEU A . n 
A 1 2662 PHE 2662 2662 2662 PHE PHE A . n 
A 1 2663 CYS 2663 2663 2663 CYS CYS A . n 
A 1 2664 ASP 2664 2664 2664 ASP ASP A . n 
A 1 2665 GLU 2665 2665 2665 GLU GLU A . n 
A 1 2666 ILE 2666 2666 2666 ILE ILE A . n 
A 1 2667 ASN 2667 2667 2667 ASN ASN A . n 
A 1 2668 LEU 2668 2668 2668 LEU LEU A . n 
A 1 2669 PRO 2669 2669 2669 PRO PRO A . n 
A 1 2670 ASP 2670 2670 2670 ASP ASP A . n 
A 1 2671 MET 2671 2671 2671 MET MET A . n 
A 1 2672 ASP 2672 2672 2672 ASP ASP A . n 
A 1 2673 LYS 2673 2673 2673 LYS LYS A . n 
A 1 2674 TYR 2674 2674 2674 TYR TYR A . n 
A 1 2675 GLY 2675 2675 2675 GLY GLY A . n 
A 1 2676 THR 2676 2676 2676 THR THR A . n 
A 1 2677 GLN 2677 2677 2677 GLN GLN A . n 
A 1 2678 ARG 2678 2678 2678 ARG ARG A . n 
A 1 2679 VAL 2679 2679 2679 VAL VAL A . n 
A 1 2680 ILE 2680 2680 2680 ILE ILE A . n 
A 1 2681 SER 2681 2681 2681 SER SER A . n 
A 1 2682 PHE 2682 2682 2682 PHE PHE A . n 
A 1 2683 ILE 2683 2683 2683 ILE ILE A . n 
A 1 2684 ARG 2684 2684 2684 ARG ARG A . n 
A 1 2685 GLN 2685 2685 2685 GLN GLN A . n 
A 1 2686 MET 2686 2686 2686 MET MET A . n 
A 1 2687 VAL 2687 2687 2687 VAL VAL A . n 
A 1 2688 GLU 2688 2688 2688 GLU GLU A . n 
A 1 2689 HIS 2689 2689 2689 HIS HIS A . n 
A 1 2690 GLY 2690 2690 2690 GLY GLY A . n 
A 1 2691 GLY 2691 2691 2691 GLY GLY A . n 
A 1 2692 PHE 2692 2692 2692 PHE PHE A . n 
A 1 2693 TYR 2693 2693 2693 TYR TYR A . n 
A 1 2694 ARG 2694 2694 2694 ARG ARG A . n 
A 1 2695 THR 2695 2695 2695 THR THR A . n 
A 1 2696 SER 2696 2696 2696 SER SER A . n 
A 1 2697 ASP 2697 2697 2697 ASP ASP A . n 
A 1 2698 GLN 2698 2698 2698 GLN GLN A . n 
A 1 2699 THR 2699 2699 2699 THR THR A . n 
A 1 2700 TRP 2700 2700 2700 TRP TRP A . n 
A 1 2701 VAL 2701 2701 2701 VAL VAL A . n 
A 1 2702 LYS 2702 2702 2702 LYS LYS A . n 
A 1 2703 LEU 2703 2703 2703 LEU LEU A . n 
A 1 2704 GLU 2704 2704 2704 GLU GLU A . n 
A 1 2705 ARG 2705 2705 2705 ARG ARG A . n 
A 1 2706 ILE 2706 2706 2706 ILE ILE A . n 
A 1 2707 GLN 2707 2707 2707 GLN GLN A . n 
A 1 2708 PHE 2708 2708 2708 PHE PHE A . n 
A 1 2709 VAL 2709 2709 2709 VAL VAL A . n 
A 1 2710 GLY 2710 2710 2710 GLY GLY A . n 
A 1 2711 ALA 2711 2711 2711 ALA ALA A . n 
A 1 2712 CYS 2712 2712 2712 CYS CYS A . n 
A 1 2713 ASN 2713 2713 2713 ASN ASN A . n 
A 1 2714 PRO 2714 2714 2714 PRO PRO A . n 
A 1 2715 PRO 2715 2715 2715 PRO PRO A . n 
A 1 2716 THR 2716 2716 2716 THR THR A . n 
A 1 2717 ASP 2717 2717 2717 ASP ASP A . n 
A 1 2718 PRO 2718 2718 2718 PRO PRO A . n 
A 1 2719 GLY 2719 2719 2719 GLY GLY A . n 
A 1 2720 ARG 2720 2720 2720 ARG ARG A . n 
A 1 2721 LYS 2721 2721 2721 LYS LYS A . n 
A 1 2722 PRO 2722 2722 2722 PRO PRO A . n 
A 1 2723 LEU 2723 2723 2723 LEU LEU A . n 
A 1 2724 SER 2724 2724 2724 SER SER A . n 
A 1 2725 HIS 2725 2725 2725 HIS HIS A . n 
A 1 2726 ARG 2726 2726 2726 ARG ARG A . n 
A 1 2727 PHE 2727 2727 2727 PHE PHE A . n 
A 1 2728 LEU 2728 2728 2728 LEU LEU A . n 
A 1 2729 ARG 2729 2729 2729 ARG ARG A . n 
A 1 2730 HIS 2730 2730 2730 HIS HIS A . n 
A 1 2731 VAL 2731 2731 2731 VAL VAL A . n 
A 1 2732 PRO 2732 2732 2732 PRO PRO A . n 
A 1 2733 VAL 2733 2733 2733 VAL VAL A . n 
A 1 2734 VAL 2734 2734 2734 VAL VAL A . n 
A 1 2735 TYR 2735 2735 2735 TYR TYR A . n 
A 1 2736 VAL 2736 2736 2736 VAL VAL A . n 
A 1 2737 ASP 2737 2737 2737 ASP ASP A . n 
A 1 2738 TYR 2738 2738 2738 TYR TYR A . n 
A 1 2739 PRO 2739 2739 2739 PRO PRO A . n 
A 1 2740 GLY 2740 2740 2740 GLY GLY A . n 
A 1 2741 PRO 2741 2741 2741 PRO PRO A . n 
A 1 2742 ALA 2742 2742 2742 ALA ALA A . n 
A 1 2743 SER 2743 2743 2743 SER SER A . n 
A 1 2744 LEU 2744 2744 2744 LEU LEU A . n 
A 1 2745 THR 2745 2745 2745 THR THR A . n 
A 1 2746 GLN 2746 2746 2746 GLN GLN A . n 
A 1 2747 ILE 2747 2747 2747 ILE ILE A . n 
A 1 2748 TYR 2748 2748 2748 TYR TYR A . n 
A 1 2749 GLY 2749 2749 2749 GLY GLY A . n 
A 1 2750 THR 2750 2750 2750 THR THR A . n 
A 1 2751 PHE 2751 2751 2751 PHE PHE A . n 
A 1 2752 ASN 2752 2752 2752 ASN ASN A . n 
A 1 2753 ARG 2753 2753 2753 ARG ARG A . n 
A 1 2754 ALA 2754 2754 2754 ALA ALA A . n 
A 1 2755 MET 2755 2755 2755 MET MET A . n 
A 1 2756 LEU 2756 2756 2756 LEU LEU A . n 
A 1 2757 ARG 2757 2757 2757 ARG ARG A . n 
A 1 2758 LEU 2758 2758 2758 LEU LEU A . n 
A 1 2759 ILE 2759 2759 2759 ILE ILE A . n 
A 1 2760 PRO 2760 2760 2760 PRO PRO A . n 
A 1 2761 SER 2761 2761 2761 SER SER A . n 
A 1 2762 LEU 2762 2762 2762 LEU LEU A . n 
A 1 2763 ARG 2763 2763 2763 ARG ARG A . n 
A 1 2764 THR 2764 2764 2764 THR THR A . n 
A 1 2765 TYR 2765 2765 2765 TYR TYR A . n 
A 1 2766 ALA 2766 2766 2766 ALA ALA A . n 
A 1 2767 GLU 2767 2767 2767 GLU GLU A . n 
A 1 2768 PRO 2768 2768 2768 PRO PRO A . n 
A 1 2769 LEU 2769 2769 2769 LEU LEU A . n 
A 1 2770 THR 2770 2770 2770 THR THR A . n 
A 1 2771 ALA 2771 2771 2771 ALA ALA A . n 
A 1 2772 ALA 2772 2772 2772 ALA ALA A . n 
A 1 2773 MET 2773 2773 2773 MET MET A . n 
A 1 2774 VAL 2774 2774 2774 VAL VAL A . n 
A 1 2775 GLU 2775 2775 2775 GLU GLU A . n 
A 1 2776 PHE 2776 2776 2776 PHE PHE A . n 
A 1 2777 TYR 2777 2777 2777 TYR TYR A . n 
A 1 2778 THR 2778 2778 2778 THR THR A . n 
A 1 2779 MET 2779 2779 2779 MET MET A . n 
A 1 2780 SER 2780 2780 2780 SER SER A . n 
A 1 2781 GLN 2781 2781 2781 GLN GLN A . n 
A 1 2782 GLU 2782 2782 2782 GLU GLU A . n 
A 1 2783 ARG 2783 2783 2783 ARG ARG A . n 
A 1 2784 PHE 2784 2784 2784 PHE PHE A . n 
A 1 2785 THR 2785 2785 2785 THR THR A . n 
A 1 2786 GLN 2786 2786 2786 GLN GLN A . n 
A 1 2787 ASP 2787 2787 2787 ASP ASP A . n 
A 1 2788 THR 2788 2788 2788 THR THR A . n 
A 1 2789 GLN 2789 2789 2789 GLN GLN A . n 
A 1 2790 PRO 2790 2790 2790 PRO PRO A . n 
A 1 2791 HIS 2791 2791 2791 HIS HIS A . n 
A 1 2792 TYR 2792 2792 2792 TYR TYR A . n 
A 1 2793 ILE 2793 2793 2793 ILE ILE A . n 
A 1 2794 TYR 2794 2794 2794 TYR TYR A . n 
A 1 2795 SER 2795 2795 2795 SER SER A . n 
A 1 2796 PRO 2796 2796 2796 PRO PRO A . n 
A 1 2797 ARG 2797 2797 2797 ARG ARG A . n 
A 1 2798 GLU 2798 2798 2798 GLU GLU A . n 
A 1 2799 MET 2799 2799 2799 MET MET A . n 
A 1 2800 THR 2800 2800 2800 THR THR A . n 
A 1 2801 ARG 2801 2801 2801 ARG ARG A . n 
A 1 2802 TRP 2802 2802 2802 TRP TRP A . n 
A 1 2803 VAL 2803 2803 2803 VAL VAL A . n 
A 1 2804 ARG 2804 2804 2804 ARG ARG A . n 
A 1 2805 GLY 2805 2805 2805 GLY GLY A . n 
A 1 2806 ILE 2806 2806 2806 ILE ILE A . n 
A 1 2807 PHE 2807 2807 2807 PHE PHE A . n 
A 1 2808 GLU 2808 2808 2808 GLU GLU A . n 
A 1 2809 ALA 2809 2809 2809 ALA ALA A . n 
A 1 2810 LEU 2810 2810 2810 LEU LEU A . n 
A 1 2811 ARG 2811 2811 2811 ARG ARG A . n 
A 1 2812 PRO 2812 2812 2812 PRO PRO A . n 
A 1 2813 LEU 2813 2813 2813 LEU LEU A . n 
A 1 2814 GLU 2814 2814 2814 GLU GLU A . n 
A 1 2815 THR 2815 2815 2815 THR THR A . n 
A 1 2816 LEU 2816 2816 2816 LEU LEU A . n 
A 1 2817 PRO 2817 2817 2817 PRO PRO A . n 
A 1 2818 VAL 2818 2818 2818 VAL VAL A . n 
A 1 2819 GLU 2819 2819 2819 GLU GLU A . n 
A 1 2820 GLY 2820 2820 2820 GLY GLY A . n 
A 1 2821 LEU 2821 2821 2821 LEU LEU A . n 
A 1 2822 ILE 2822 2822 2822 ILE ILE A . n 
A 1 2823 ARG 2823 2823 2823 ARG ARG A . n 
A 1 2824 ILE 2824 2824 2824 ILE ILE A . n 
A 1 2825 TRP 2825 2825 2825 TRP TRP A . n 
A 1 2826 ALA 2826 2826 2826 ALA ALA A . n 
A 1 2827 HIS 2827 2827 2827 HIS HIS A . n 
A 1 2828 GLU 2828 2828 2828 GLU GLU A . n 
A 1 2829 ALA 2829 2829 2829 ALA ALA A . n 
A 1 2830 LEU 2830 2830 2830 LEU LEU A . n 
A 1 2831 ARG 2831 2831 2831 ARG ARG A . n 
A 1 2832 LEU 2832 2832 2832 LEU LEU A . n 
A 1 2833 PHE 2833 2833 2833 PHE PHE A . n 
A 1 2834 GLN 2834 2834 2834 GLN GLN A . n 
A 1 2835 ASP 2835 2835 2835 ASP ASP A . n 
A 1 2836 ARG 2836 2836 2836 ARG ARG A . n 
A 1 2837 LEU 2837 2837 2837 LEU LEU A . n 
A 1 2838 VAL 2838 2838 2838 VAL VAL A . n 
A 1 2839 GLU 2839 2839 2839 GLU GLU A . n 
A 1 2840 ASP 2840 2840 2840 ASP ASP A . n 
A 1 2841 GLU 2841 2841 2841 GLU GLU A . n 
A 1 2842 GLU 2842 2842 2842 GLU GLU A . n 
A 1 2843 ARG 2843 2843 2843 ARG ARG A . n 
A 1 2844 ARG 2844 2844 2844 ARG ARG A . n 
A 1 2845 TRP 2845 2845 2845 TRP TRP A . n 
A 1 2846 THR 2846 2846 2846 THR THR A . n 
A 1 2847 ASP 2847 2847 2847 ASP ASP A . n 
A 1 2848 GLU 2848 2848 2848 GLU GLU A . n 
A 1 2849 ASN 2849 2849 2849 ASN ASN A . n 
A 1 2850 ILE 2850 2850 2850 ILE ILE A . n 
A 1 2851 ASP 2851 2851 2851 ASP ASP A . n 
A 1 2852 THR 2852 2852 2852 THR THR A . n 
A 1 2853 VAL 2853 2853 2853 VAL VAL A . n 
A 1 2854 ALA 2854 2854 2854 ALA ALA A . n 
A 1 2855 LEU 2855 2855 2855 LEU LEU A . n 
A 1 2856 LYS 2856 2856 2856 LYS LYS A . n 
A 1 2857 HIS 2857 2857 2857 HIS HIS A . n 
A 1 2858 PHE 2858 2858 2858 PHE PHE A . n 
A 1 2859 PRO 2859 2859 2859 PRO PRO A . n 
A 1 2860 ASN 2860 2860 2860 ASN ASN A . n 
A 1 2861 ILE 2861 2861 2861 ILE ILE A . n 
A 1 2862 ASP 2862 2862 2862 ASP ASP A . n 
A 1 2863 ARG 2863 2863 2863 ARG ARG A . n 
A 1 2864 GLU 2864 2864 2864 GLU GLU A . n 
A 1 2865 LYS 2865 2865 2865 LYS LYS A . n 
A 1 2866 ALA 2866 2866 2866 ALA ALA A . n 
A 1 2867 MET 2867 2867 2867 MET MET A . n 
A 1 2868 SER 2868 2868 2868 SER SER A . n 
A 1 2869 ARG 2869 2869 2869 ARG ARG A . n 
A 1 2870 PRO 2870 2870 2870 PRO PRO A . n 
A 1 2871 ILE 2871 2871 2871 ILE ILE A . n 
A 1 2872 LEU 2872 2872 2872 LEU LEU A . n 
A 1 2873 TYR 2873 2873 2873 TYR TYR A . n 
A 1 2874 SER 2874 2874 2874 SER SER A . n 
A 1 2875 ASN 2875 2875 2875 ASN ASN A . n 
A 1 2876 TRP 2876 2876 2876 TRP TRP A . n 
A 1 2877 LEU 2877 2877 2877 LEU LEU A . n 
A 1 2878 SER 2878 2878 2878 SER SER A . n 
A 1 2879 LYS 2879 2879 2879 LYS LYS A . n 
A 1 2880 ASP 2880 2880 2880 ASP ASP A . n 
A 1 2881 TYR 2881 2881 2881 TYR TYR A . n 
A 1 2882 ILE 2882 2882 2882 ILE ILE A . n 
A 1 2883 PRO 2883 2883 2883 PRO PRO A . n 
A 1 2884 VAL 2884 2884 2884 VAL VAL A . n 
A 1 2885 ASP 2885 2885 2885 ASP ASP A . n 
A 1 2886 GLN 2886 2886 2886 GLN GLN A . n 
A 1 2887 GLU 2887 2887 2887 GLU GLU A . n 
A 1 2888 GLU 2888 2888 2888 GLU GLU A . n 
A 1 2889 LEU 2889 2889 2889 LEU LEU A . n 
A 1 2890 ARG 2890 2890 2890 ARG ARG A . n 
A 1 2891 ASP 2891 2891 2891 ASP ASP A . n 
A 1 2892 TYR 2892 2892 2892 TYR TYR A . n 
A 1 2893 VAL 2893 2893 2893 VAL VAL A . n 
A 1 2894 LYS 2894 2894 2894 LYS LYS A . n 
A 1 2895 ALA 2895 2895 2895 ALA ALA A . n 
A 1 2896 ARG 2896 2896 2896 ARG ARG A . n 
A 1 2897 LEU 2897 2897 2897 LEU LEU A . n 
A 1 2898 LYS 2898 2898 2898 LYS LYS A . n 
A 1 2899 VAL 2899 2899 2899 VAL VAL A . n 
A 1 2900 PHE 2900 2900 2900 PHE PHE A . n 
A 1 2901 TYR 2901 2901 2901 TYR TYR A . n 
A 1 2902 GLU 2902 2902 2902 GLU GLU A . n 
A 1 2903 GLU 2903 2903 2903 GLU GLU A . n 
A 1 2904 GLU 2904 2904 2904 GLU GLU A . n 
A 1 2905 LEU 2905 2905 2905 LEU LEU A . n 
A 1 2906 ASP 2906 2906 2906 ASP ASP A . n 
A 1 2907 VAL 2907 2907 2907 VAL VAL A . n 
A 1 2908 PRO 2908 2908 2908 PRO PRO A . n 
A 1 2909 LEU 2909 2909 2909 LEU LEU A . n 
A 1 2910 VAL 2910 2910 2910 VAL VAL A . n 
A 1 2911 LEU 2911 2911 2911 LEU LEU A . n 
A 1 2912 PHE 2912 2912 2912 PHE PHE A . n 
A 1 2913 ASN 2913 2913 2913 ASN ASN A . n 
A 1 2914 GLU 2914 2914 2914 GLU GLU A . n 
A 1 2915 VAL 2915 2915 2915 VAL VAL A . n 
A 1 2916 LEU 2916 2916 2916 LEU LEU A . n 
A 1 2917 ASP 2917 2917 2917 ASP ASP A . n 
A 1 2918 HIS 2918 2918 2918 HIS HIS A . n 
A 1 2919 VAL 2919 2919 2919 VAL VAL A . n 
A 1 2920 LEU 2920 2920 2920 LEU LEU A . n 
A 1 2921 ARG 2921 2921 2921 ARG ARG A . n 
A 1 2922 ILE 2922 2922 2922 ILE ILE A . n 
A 1 2923 ASP 2923 2923 2923 ASP ASP A . n 
A 1 2924 ARG 2924 2924 2924 ARG ARG A . n 
A 1 2925 ILE 2925 2925 2925 ILE ILE A . n 
A 1 2926 PHE 2926 2926 2926 PHE PHE A . n 
A 1 2927 ARG 2927 2927 2927 ARG ARG A . n 
A 1 2928 GLN 2928 2928 2928 GLN GLN A . n 
A 1 2929 PRO 2929 2929 2929 PRO PRO A . n 
A 1 2930 GLN 2930 2930 2930 GLN GLN A . n 
A 1 2931 GLY 2931 2931 2931 GLY GLY A . n 
A 1 2932 HIS 2932 2932 2932 HIS HIS A . n 
A 1 2933 LEU 2933 2933 2933 LEU LEU A . n 
A 1 2934 LEU 2934 2934 2934 LEU LEU A . n 
A 1 2935 LEU 2935 2935 2935 LEU LEU A . n 
A 1 2936 ILE 2936 2936 2936 ILE ILE A . n 
A 1 2937 GLY 2937 2937 2937 GLY GLY A . n 
A 1 2938 VAL 2938 2938 2938 VAL VAL A . n 
A 1 2939 SER 2939 2939 2939 SER SER A . n 
A 1 2940 GLY 2940 2940 2940 GLY GLY A . n 
A 1 2941 ALA 2941 2941 2941 ALA ALA A . n 
A 1 2942 GLY 2942 2942 2942 GLY GLY A . n 
A 1 2943 LYS 2943 2943 2943 LYS LYS A . n 
A 1 2944 THR 2944 2944 2944 THR THR A . n 
A 1 2945 THR 2945 2945 2945 THR THR A . n 
A 1 2946 LEU 2946 2946 2946 LEU LEU A . n 
A 1 2947 SER 2947 2947 2947 SER SER A . n 
A 1 2948 ARG 2948 2948 2948 ARG ARG A . n 
A 1 2949 PHE 2949 2949 2949 PHE PHE A . n 
A 1 2950 VAL 2950 2950 2950 VAL VAL A . n 
A 1 2951 ALA 2951 2951 2951 ALA ALA A . n 
A 1 2952 TRP 2952 2952 2952 TRP TRP A . n 
A 1 2953 MET 2953 2953 2953 MET MET A . n 
A 1 2954 ASN 2954 2954 2954 ASN ASN A . n 
A 1 2955 GLY 2955 2955 2955 GLY GLY A . n 
A 1 2956 LEU 2956 2956 2956 LEU LEU A . n 
A 1 2957 SER 2957 2957 2957 SER SER A . n 
A 1 2958 VAL 2958 2958 2958 VAL VAL A . n 
A 1 2959 TYR 2959 2959 2959 TYR TYR A . n 
A 1 2960 GLN 2960 2960 2960 GLN GLN A . n 
A 1 2961 ILE 2961 2961 2961 ILE ILE A . n 
A 1 2962 LYS 2962 2962 2962 LYS LYS A . n 
A 1 2963 VAL 2963 2963 2963 VAL VAL A . n 
A 1 2964 HIS 2964 2964 2964 HIS HIS A . n 
A 1 2965 ARG 2965 2965 2965 ARG ARG A . n 
A 1 2966 LYS 2966 2966 2966 LYS LYS A . n 
A 1 2967 TYR 2967 2967 2967 TYR TYR A . n 
A 1 2968 THR 2968 2968 2968 THR THR A . n 
A 1 2969 GLY 2969 2969 2969 GLY GLY A . n 
A 1 2970 GLU 2970 2970 2970 GLU GLU A . n 
A 1 2971 ASP 2971 2971 2971 ASP ASP A . n 
A 1 2972 PHE 2972 2972 2972 PHE PHE A . n 
A 1 2973 ASP 2973 2973 2973 ASP ASP A . n 
A 1 2974 GLU 2974 2974 2974 GLU GLU A . n 
A 1 2975 ASP 2975 2975 2975 ASP ASP A . n 
A 1 2976 LEU 2976 2976 2976 LEU LEU A . n 
A 1 2977 ARG 2977 2977 2977 ARG ARG A . n 
A 1 2978 THR 2978 2978 2978 THR THR A . n 
A 1 2979 VAL 2979 2979 2979 VAL VAL A . n 
A 1 2980 LEU 2980 2980 2980 LEU LEU A . n 
A 1 2981 ARG 2981 2981 2981 ARG ARG A . n 
A 1 2982 ARG 2982 2982 2982 ARG ARG A . n 
A 1 2983 SER 2983 2983 2983 SER SER A . n 
A 1 2984 GLY 2984 2984 2984 GLY GLY A . n 
A 1 2985 CYS 2985 2985 2985 CYS CYS A . n 
A 1 2986 LYS 2986 2986 2986 LYS LYS A . n 
A 1 2987 ASN 2987 2987 2987 ASN ASN A . n 
A 1 2988 GLU 2988 2988 2988 GLU GLU A . n 
A 1 2989 LYS 2989 2989 2989 LYS LYS A . n 
A 1 2990 ILE 2990 2990 2990 ILE ILE A . n 
A 1 2991 ALA 2991 2991 2991 ALA ALA A . n 
A 1 2992 PHE 2992 2992 2992 PHE PHE A . n 
A 1 2993 ILE 2993 2993 2993 ILE ILE A . n 
A 1 2994 MET 2994 2994 2994 MET MET A . n 
A 1 2995 ASP 2995 2995 2995 ASP ASP A . n 
A 1 2996 GLU 2996 2996 2996 GLU GLU A . n 
A 1 2997 SER 2997 2997 2997 SER SER A . n 
A 1 2998 ASN 2998 2998 2998 ASN ASN A . n 
A 1 2999 VAL 2999 2999 2999 VAL VAL A . n 
A 1 3000 LEU 3000 3000 3000 LEU LEU A . n 
A 1 3001 ASP 3001 3001 3001 ASP ASP A . n 
A 1 3002 SER 3002 3002 3002 SER SER A . n 
A 1 3003 GLY 3003 3003 3003 GLY GLY A . n 
A 1 3004 PHE 3004 3004 3004 PHE PHE A . n 
A 1 3005 LEU 3005 3005 3005 LEU LEU A . n 
A 1 3006 GLU 3006 3006 3006 GLU GLU A . n 
A 1 3007 ARG 3007 3007 3007 ARG ARG A . n 
A 1 3008 MET 3008 3008 3008 MET MET A . n 
A 1 3009 ASN 3009 3009 3009 ASN ASN A . n 
A 1 3010 THR 3010 3010 3010 THR THR A . n 
A 1 3011 LEU 3011 3011 3011 LEU LEU A . n 
A 1 3012 LEU 3012 3012 3012 LEU LEU A . n 
A 1 3013 ALA 3013 3013 3013 ALA ALA A . n 
A 1 3014 ASN 3014 3014 3014 ASN ASN A . n 
A 1 3015 GLY 3015 3015 3015 GLY GLY A . n 
A 1 3016 GLU 3016 3016 3016 GLU GLU A . n 
A 1 3017 VAL 3017 3017 3017 VAL VAL A . n 
A 1 3018 PRO 3018 3018 3018 PRO PRO A . n 
A 1 3019 GLY 3019 3019 3019 GLY GLY A . n 
A 1 3020 LEU 3020 3020 3020 LEU LEU A . n 
A 1 3021 PHE 3021 3021 3021 PHE PHE A . n 
A 1 3022 GLU 3022 3022 3022 GLU GLU A . n 
A 1 3023 GLY 3023 3023 3023 GLY GLY A . n 
A 1 3024 ASP 3024 3024 3024 ASP ASP A . n 
A 1 3025 GLU 3025 3025 3025 GLU GLU A . n 
A 1 3026 TYR 3026 3026 3026 TYR TYR A . n 
A 1 3027 ALA 3027 3027 3027 ALA ALA A . n 
A 1 3028 THR 3028 3028 3028 THR THR A . n 
A 1 3029 LEU 3029 3029 3029 LEU LEU A . n 
A 1 3030 MET 3030 3030 3030 MET MET A . n 
A 1 3031 THR 3031 3031 3031 THR THR A . n 
A 1 3032 GLN 3032 3032 3032 GLN GLN A . n 
A 1 3033 CYS 3033 3033 3033 CYS CYS A . n 
A 1 3034 LYS 3034 3034 3034 LYS LYS A . n 
A 1 3035 GLU 3035 3035 3035 GLU GLU A . n 
A 1 3036 GLY 3036 3036 3036 GLY GLY A . n 
A 1 3037 ALA 3037 3037 3037 ALA ALA A . n 
A 1 3038 GLN 3038 3038 3038 GLN GLN A . n 
A 1 3039 LYS 3039 3039 3039 LYS LYS A . n 
A 1 3040 GLU 3040 3040 3040 GLU GLU A . n 
A 1 3041 GLY 3041 3041 3041 GLY GLY A . n 
A 1 3042 LEU 3042 3042 3042 LEU LEU A . n 
A 1 3043 MET 3043 3043 3043 MET MET A . n 
A 1 3044 LEU 3044 3044 3044 LEU LEU A . n 
A 1 3045 ASP 3045 3045 3045 ASP ASP A . n 
A 1 3046 SER 3046 3046 3046 SER SER A . n 
A 1 3047 HIS 3047 3047 3047 HIS HIS A . n 
A 1 3048 GLU 3048 3048 3048 GLU GLU A . n 
A 1 3049 GLU 3049 3049 3049 GLU GLU A . n 
A 1 3050 LEU 3050 3050 3050 LEU LEU A . n 
A 1 3051 TYR 3051 3051 3051 TYR TYR A . n 
A 1 3052 LYS 3052 3052 3052 LYS LYS A . n 
A 1 3053 TRP 3053 3053 3053 TRP TRP A . n 
A 1 3054 PHE 3054 3054 3054 PHE PHE A . n 
A 1 3055 THR 3055 3055 3055 THR THR A . n 
A 1 3056 SER 3056 3056 3056 SER SER A . n 
A 1 3057 GLN 3057 3057 3057 GLN GLN A . n 
A 1 3058 VAL 3058 3058 3058 VAL VAL A . n 
A 1 3059 ILE 3059 3059 3059 ILE ILE A . n 
A 1 3060 ARG 3060 3060 3060 ARG ARG A . n 
A 1 3061 ASN 3061 3061 3061 ASN ASN A . n 
A 1 3062 LEU 3062 3062 3062 LEU LEU A . n 
A 1 3063 HIS 3063 3063 3063 HIS HIS A . n 
A 1 3064 VAL 3064 3064 3064 VAL VAL A . n 
A 1 3065 VAL 3065 3065 3065 VAL VAL A . n 
A 1 3066 PHE 3066 3066 3066 PHE PHE A . n 
A 1 3067 THR 3067 3067 3067 THR THR A . n 
A 1 3068 MET 3068 3068 3068 MET MET A . n 
A 1 3069 ASN 3069 3069 3069 ASN ASN A . n 
A 1 3070 PRO 3070 3070 3070 PRO PRO A . n 
A 1 3071 SER 3071 3071 3071 SER SER A . n 
A 1 3072 SER 3072 3072 3072 SER SER A . n 
A 1 3073 GLU 3073 3073 3073 GLU GLU A . n 
A 1 3074 GLY 3074 3074 3074 GLY GLY A . n 
A 1 3075 LEU 3075 3075 3075 LEU LEU A . n 
A 1 3076 LYS 3076 3076 3076 LYS LYS A . n 
A 1 3077 ASP 3077 3077 3077 ASP ASP A . n 
A 1 3078 ARG 3078 3078 3078 ARG ARG A . n 
A 1 3079 ALA 3079 3079 3079 ALA ALA A . n 
A 1 3080 ALA 3080 3080 3080 ALA ALA A . n 
A 1 3081 THR 3081 3081 3081 THR THR A . n 
A 1 3082 SER 3082 3082 3082 SER SER A . n 
A 1 3083 PRO 3083 3083 3083 PRO PRO A . n 
A 1 3084 ALA 3084 3084 3084 ALA ALA A . n 
A 1 3085 LEU 3085 3085 3085 LEU LEU A . n 
A 1 3086 PHE 3086 3086 3086 PHE PHE A . n 
A 1 3087 ASN 3087 3087 3087 ASN ASN A . n 
A 1 3088 ARG 3088 3088 3088 ARG ARG A . n 
A 1 3089 CYS 3089 3089 3089 CYS CYS A . n 
A 1 3090 VAL 3090 3090 3090 VAL VAL A . n 
A 1 3091 LEU 3091 3091 3091 LEU LEU A . n 
A 1 3092 ASN 3092 3092 3092 ASN ASN A . n 
A 1 3093 TRP 3093 3093 3093 TRP TRP A . n 
A 1 3094 PHE 3094 3094 3094 PHE PHE A . n 
A 1 3095 GLY 3095 3095 3095 GLY GLY A . n 
A 1 3096 ASP 3096 3096 3096 ASP ASP A . n 
A 1 3097 TRP 3097 3097 3097 TRP TRP A . n 
A 1 3098 SER 3098 3098 3098 SER SER A . n 
A 1 3099 THR 3099 3099 3099 THR THR A . n 
A 1 3100 GLU 3100 3100 3100 GLU GLU A . n 
A 1 3101 ALA 3101 3101 3101 ALA ALA A . n 
A 1 3102 LEU 3102 3102 3102 LEU LEU A . n 
A 1 3103 TYR 3103 3103 3103 TYR TYR A . n 
A 1 3104 GLN 3104 3104 3104 GLN GLN A . n 
A 1 3105 VAL 3105 3105 3105 VAL VAL A . n 
A 1 3106 GLY 3106 3106 3106 GLY GLY A . n 
A 1 3107 LYS 3107 3107 3107 LYS LYS A . n 
A 1 3108 GLU 3108 3108 3108 GLU GLU A . n 
A 1 3109 PHE 3109 3109 3109 PHE PHE A . n 
A 1 3110 THR 3110 3110 3110 THR THR A . n 
A 1 3111 SER 3111 3111 3111 SER SER A . n 
A 1 3112 LYS 3112 3112 3112 LYS LYS A . n 
A 1 3113 MET 3113 3113 3113 MET MET A . n 
A 1 3114 ASP 3114 3114 3114 ASP ASP A . n 
A 1 3115 LEU 3115 3115 3115 LEU LEU A . n 
A 1 3116 GLU 3116 3116 3116 GLU GLU A . n 
A 1 3117 LYS 3117 3117 3117 LYS LYS A . n 
A 1 3118 PRO 3118 3118 3118 PRO PRO A . n 
A 1 3119 ASN 3119 3119 3119 ASN ASN A . n 
A 1 3120 TYR 3120 3120 3120 TYR TYR A . n 
A 1 3121 ILE 3121 3121 3121 ILE ILE A . n 
A 1 3122 VAL 3122 3122 3122 VAL VAL A . n 
A 1 3123 PRO 3123 3123 3123 PRO PRO A . n 
A 1 3124 ASP 3124 3124 3124 ASP ASP A . n 
A 1 3125 TYR 3125 3125 3125 TYR TYR A . n 
A 1 3126 MET 3126 3126 3126 MET MET A . n 
A 1 3127 PRO 3127 3127 3127 PRO PRO A . n 
A 1 3128 VAL 3128 3128 3128 VAL VAL A . n 
A 1 3129 VAL 3129 3129 3129 VAL VAL A . n 
A 1 3130 TYR 3130 3130 3130 TYR TYR A . n 
A 1 3131 ASP 3131 3131 3131 ASP ASP A . n 
A 1 3132 LYS 3132 3132 3132 LYS LYS A . n 
A 1 3133 LEU 3133 3133 3133 LEU LEU A . n 
A 1 3134 PRO 3134 3134 3134 PRO PRO A . n 
A 1 3135 GLN 3135 3135 3135 GLN GLN A . n 
A 1 3136 PRO 3136 3136 3136 PRO PRO A . n 
A 1 3137 PRO 3137 3137 3137 PRO PRO A . n 
A 1 3138 SER 3138 3138 3138 SER SER A . n 
A 1 3139 HIS 3139 3139 3139 HIS HIS A . n 
A 1 3140 ARG 3140 3140 3140 ARG ARG A . n 
A 1 3141 GLU 3141 3141 3141 GLU GLU A . n 
A 1 3142 ALA 3142 3142 3142 ALA ALA A . n 
A 1 3143 ILE 3143 3143 3143 ILE ILE A . n 
A 1 3144 VAL 3144 3144 3144 VAL VAL A . n 
A 1 3145 ASN 3145 3145 3145 ASN ASN A . n 
A 1 3146 SER 3146 3146 3146 SER SER A . n 
A 1 3147 CYS 3147 3147 3147 CYS CYS A . n 
A 1 3148 VAL 3148 3148 3148 VAL VAL A . n 
A 1 3149 PHE 3149 3149 3149 PHE PHE A . n 
A 1 3150 VAL 3150 3150 3150 VAL VAL A . n 
A 1 3151 HIS 3151 3151 3151 HIS HIS A . n 
A 1 3152 GLN 3152 3152 3152 GLN GLN A . n 
A 1 3153 THR 3153 3153 3153 THR THR A . n 
A 1 3154 LEU 3154 3154 3154 LEU LEU A . n 
A 1 3155 HIS 3155 3155 3155 HIS HIS A . n 
A 1 3156 GLN 3156 3156 3156 GLN GLN A . n 
A 1 3157 ALA 3157 3157 3157 ALA ALA A . n 
A 1 3158 ASN 3158 3158 3158 ASN ASN A . n 
A 1 3159 ALA 3159 3159 3159 ALA ALA A . n 
A 1 3160 ARG 3160 3160 3160 ARG ARG A . n 
A 1 3161 LEU 3161 3161 3161 LEU LEU A . n 
A 1 3162 ALA 3162 3162 3162 ALA ALA A . n 
A 1 3163 LYS 3163 3163 3163 LYS LYS A . n 
A 1 3164 ARG 3164 3164 3164 ARG ARG A . n 
A 1 3165 GLY 3165 3165 3165 GLY GLY A . n 
A 1 3166 GLY 3166 3166 3166 GLY GLY A . n 
A 1 3167 ARG 3167 3167 3167 ARG ARG A . n 
A 1 3168 THR 3168 3168 3168 THR THR A . n 
A 1 3169 MET 3169 3169 3169 MET MET A . n 
A 1 3170 ALA 3170 3170 3170 ALA ALA A . n 
A 1 3171 ILE 3171 3171 3171 ILE ILE A . n 
A 1 3172 THR 3172 3172 3172 THR THR A . n 
A 1 3173 PRO 3173 3173 3173 PRO PRO A . n 
A 1 3174 ARG 3174 3174 3174 ARG ARG A . n 
A 1 3175 HIS 3175 3175 3175 HIS HIS A . n 
A 1 3176 TYR 3176 3176 3176 TYR TYR A . n 
A 1 3177 LEU 3177 3177 3177 LEU LEU A . n 
A 1 3178 ASP 3178 3178 3178 ASP ASP A . n 
A 1 3179 PHE 3179 3179 3179 PHE PHE A . n 
A 1 3180 ILE 3180 3180 3180 ILE ILE A . n 
A 1 3181 ASN 3181 3181 3181 ASN ASN A . n 
A 1 3182 HIS 3182 3182 3182 HIS HIS A . n 
A 1 3183 TYR 3183 3183 3183 TYR TYR A . n 
A 1 3184 ALA 3184 3184 3184 ALA ALA A . n 
A 1 3185 ASN 3185 3185 3185 ASN ASN A . n 
A 1 3186 LEU 3186 3186 3186 LEU LEU A . n 
A 1 3187 PHE 3187 3187 3187 PHE PHE A . n 
A 1 3188 HIS 3188 3188 3188 HIS HIS A . n 
A 1 3189 GLU 3189 3189 3189 GLU GLU A . n 
A 1 3190 LYS 3190 3190 3190 LYS LYS A . n 
A 1 3191 ARG 3191 3191 3191 ARG ARG A . n 
A 1 3192 SER 3192 3192 3192 SER SER A . n 
A 1 3193 GLU 3193 3193 3193 GLU GLU A . n 
A 1 3194 LEU 3194 3194 3194 LEU LEU A . n 
A 1 3195 GLU 3195 3195 3195 GLU GLU A . n 
A 1 3196 GLU 3196 3196 3196 GLU GLU A . n 
A 1 3197 GLN 3197 3197 3197 GLN GLN A . n 
A 1 3198 GLN 3198 3198 3198 GLN GLN A . n 
A 1 3199 MET 3199 3199 3199 MET MET A . n 
A 1 3200 HIS 3200 3200 3200 HIS HIS A . n 
A 1 3201 LEU 3201 3201 3201 LEU LEU A . n 
A 1 3202 ASN 3202 3202 3202 ASN ASN A . n 
A 1 3203 VAL 3203 3203 3203 VAL VAL A . n 
A 1 3204 GLY 3204 3204 3204 GLY GLY A . n 
A 1 3205 LEU 3205 3205 3205 LEU LEU A . n 
A 1 3206 ARG 3206 3206 3206 ARG ARG A . n 
A 1 3207 LYS 3207 3207 3207 LYS LYS A . n 
A 1 3208 ILE 3208 3208 3208 ILE ILE A . n 
A 1 3209 LYS 3209 3209 3209 LYS LYS A . n 
A 1 3210 GLU 3210 3210 3210 GLU GLU A . n 
A 1 3211 THR 3211 3211 3211 THR THR A . n 
A 1 3212 VAL 3212 3212 3212 VAL VAL A . n 
A 1 3213 ASP 3213 3213 3213 ASP ASP A . n 
A 1 3214 GLN 3214 3214 3214 GLN GLN A . n 
A 1 3215 VAL 3215 3215 3215 VAL VAL A . n 
A 1 3216 GLU 3216 3216 3216 GLU GLU A . n 
A 1 3217 GLU 3217 3217 3217 GLU GLU A . n 
A 1 3218 LEU 3218 3218 3218 LEU LEU A . n 
A 1 3219 ARG 3219 3219 3219 ARG ARG A . n 
A 1 3220 ARG 3220 3220 3220 ARG ARG A . n 
A 1 3221 ASP 3221 3221 3221 ASP ASP A . n 
A 1 3222 LEU 3222 3222 3222 LEU LEU A . n 
A 1 3223 ARG 3223 3223 3223 ARG ARG A . n 
A 1 3224 ILE 3224 3224 3224 ILE ILE A . n 
A 1 3225 LYS 3225 3225 3225 LYS LYS A . n 
A 1 3226 SER 3226 3226 3226 SER SER A . n 
A 1 3227 GLN 3227 3227 3227 GLN GLN A . n 
A 1 3228 GLU 3228 3228 3228 GLU GLU A . n 
A 1 3229 LEU 3229 3229 3229 LEU LEU A . n 
A 1 3230 GLU 3230 3230 3230 GLU GLU A . n 
A 1 3231 VAL 3231 3231 3231 VAL VAL A . n 
A 1 3232 LYS 3232 3232 3232 LYS LYS A . n 
A 1 3233 ASN 3233 3233 3233 ASN ASN A . n 
A 1 3234 ALA 3234 3234 3234 ALA ALA A . n 
A 1 3235 ALA 3235 3235 3235 ALA ALA A . n 
A 1 3236 ALA 3236 3236 3236 ALA ALA A . n 
A 1 3237 ASN 3237 3237 3237 ASN ASN A . n 
A 1 3238 ASP 3238 3238 3238 ASP ASP A . n 
A 1 3239 LYS 3239 3239 3239 LYS LYS A . n 
A 1 3240 LEU 3240 3240 3240 LEU LEU A . n 
A 1 3241 LYS 3241 3241 3241 LYS LYS A . n 
A 1 3242 LYS 3242 3242 3242 LYS LYS A . n 
A 1 3243 MET 3243 3243 ?    ?   ?   A . n 
A 1 3244 VAL 3244 3244 ?    ?   ?   A . n 
A 1 3245 LYS 3245 3245 ?    ?   ?   A . n 
A 1 3246 ASP 3246 3246 ?    ?   ?   A . n 
A 1 3247 GLN 3247 3247 ?    ?   ?   A . n 
A 1 3248 GLN 3248 3248 ?    ?   ?   A . n 
A 1 3249 GLU 3249 3249 ?    ?   ?   A . n 
A 1 3250 ALA 3250 3250 ?    ?   ?   A . n 
A 1 3251 GLU 3251 3251 ?    ?   ?   A . n 
A 1 3252 LYS 3252 3252 ?    ?   ?   A . n 
A 1 3253 LYS 3253 3253 ?    ?   ?   A . n 
A 1 3254 LYS 3254 3254 ?    ?   ?   A . n 
A 1 3255 VAL 3255 3255 ?    ?   ?   A . n 
A 1 3256 MET 3256 3256 ?    ?   ?   A . n 
A 1 3257 SER 3257 3257 ?    ?   ?   A . n 
A 1 3258 GLN 3258 3258 ?    ?   ?   A . n 
A 1 3259 GLU 3259 3259 ?    ?   ?   A . n 
A 1 3260 ILE 3260 3260 ?    ?   ?   A . n 
A 1 3261 GLN 3261 3261 ?    ?   ?   A . n 
A 1 3262 GLU 3262 3262 ?    ?   ?   A . n 
A 1 3263 GLN 3263 3263 ?    ?   ?   A . n 
A 1 3264 LEU 3264 3264 ?    ?   ?   A . n 
A 1 3265 HIS 3265 3265 ?    ?   ?   A . n 
A 1 3266 LYS 3266 3266 ?    ?   ?   A . n 
A 1 3267 GLN 3267 3267 ?    ?   ?   A . n 
A 1 3268 GLN 3268 3268 ?    ?   ?   A . n 
A 1 3269 GLU 3269 3269 ?    ?   ?   A . n 
A 1 3270 VAL 3270 3270 ?    ?   ?   A . n 
A 1 3271 ILE 3271 3271 ?    ?   ?   A . n 
A 1 3272 ALA 3272 3272 ?    ?   ?   A . n 
A 1 3273 ASP 3273 3273 ?    ?   ?   A . n 
A 1 3274 LYS 3274 3274 ?    ?   ?   A . n 
A 1 3275 GLN 3275 3275 ?    ?   ?   A . n 
A 1 3276 MET 3276 3276 ?    ?   ?   A . n 
A 1 3277 SER 3277 3277 ?    ?   ?   A . n 
A 1 3278 VAL 3278 3278 ?    ?   ?   A . n 
A 1 3279 LYS 3279 3279 ?    ?   ?   A . n 
A 1 3280 GLU 3280 3280 ?    ?   ?   A . n 
A 1 3281 ASP 3281 3281 ?    ?   ?   A . n 
A 1 3282 LEU 3282 3282 ?    ?   ?   A . n 
A 1 3283 ASP 3283 3283 ?    ?   ?   A . n 
A 1 3284 LYS 3284 3284 ?    ?   ?   A . n 
A 1 3285 VAL 3285 3285 ?    ?   ?   A . n 
A 1 3286 GLU 3286 3286 ?    ?   ?   A . n 
A 1 3287 PRO 3287 3287 ?    ?   ?   A . n 
A 1 3288 ALA 3288 3288 ?    ?   ?   A . n 
A 1 3289 VAL 3289 3289 ?    ?   ?   A . n 
A 1 3290 ILE 3290 3290 ?    ?   ?   A . n 
A 1 3291 GLU 3291 3291 ?    ?   ?   A . n 
A 1 3292 ALA 3292 3292 ?    ?   ?   A . n 
A 1 3293 GLN 3293 3293 ?    ?   ?   A . n 
A 1 3294 ASN 3294 3294 ?    ?   ?   A . n 
A 1 3295 ALA 3295 3295 ?    ?   ?   A . n 
A 1 3296 VAL 3296 3296 ?    ?   ?   A . n 
A 1 3297 LYS 3297 3297 ?    ?   ?   A . n 
A 1 3298 SER 3298 3298 ?    ?   ?   A . n 
A 1 3299 ILE 3299 3299 ?    ?   ?   A . n 
A 1 3300 LYS 3300 3300 ?    ?   ?   A . n 
A 1 3301 LYS 3301 3301 ?    ?   ?   A . n 
A 1 3302 GLN 3302 3302 ?    ?   ?   A . n 
A 1 3303 HIS 3303 3303 ?    ?   ?   A . n 
A 1 3304 LEU 3304 3304 ?    ?   ?   A . n 
A 1 3305 VAL 3305 3305 ?    ?   ?   A . n 
A 1 3306 GLU 3306 3306 ?    ?   ?   A . n 
A 1 3307 VAL 3307 3307 ?    ?   ?   A . n 
A 1 3308 ARG 3308 3308 ?    ?   ?   A . n 
A 1 3309 SER 3309 3309 ?    ?   ?   A . n 
A 1 3310 MET 3310 3310 ?    ?   ?   A . n 
A 1 3311 ALA 3311 3311 ?    ?   ?   A . n 
A 1 3312 ASN 3312 3312 ?    ?   ?   A . n 
A 1 3313 PRO 3313 3313 ?    ?   ?   A . n 
A 1 3314 PRO 3314 3314 ?    ?   ?   A . n 
A 1 3315 ALA 3315 3315 ?    ?   ?   A . n 
A 1 3316 ALA 3316 3316 ?    ?   ?   A . n 
A 1 3317 VAL 3317 3317 ?    ?   ?   A . n 
A 1 3318 LYS 3318 3318 ?    ?   ?   A . n 
A 1 3319 LEU 3319 3319 ?    ?   ?   A . n 
A 1 3320 ALA 3320 3320 ?    ?   ?   A . n 
A 1 3321 LEU 3321 3321 ?    ?   ?   A . n 
A 1 3322 GLU 3322 3322 ?    ?   ?   A . n 
A 1 3323 SER 3323 3323 ?    ?   ?   A . n 
A 1 3324 ILE 3324 3324 ?    ?   ?   A . n 
A 1 3325 CYS 3325 3325 ?    ?   ?   A . n 
A 1 3326 LEU 3326 3326 ?    ?   ?   A . n 
A 1 3327 LEU 3327 3327 ?    ?   ?   A . n 
A 1 3328 LEU 3328 3328 ?    ?   ?   A . n 
A 1 3329 GLY 3329 3329 ?    ?   ?   A . n 
A 1 3330 GLU 3330 3330 ?    ?   ?   A . n 
A 1 3331 SER 3331 3331 ?    ?   ?   A . n 
A 1 3332 THR 3332 3332 ?    ?   ?   A . n 
A 1 3333 THR 3333 3333 ?    ?   ?   A . n 
A 1 3334 ASP 3334 3334 ?    ?   ?   A . n 
A 1 3335 TRP 3335 3335 ?    ?   ?   A . n 
A 1 3336 LYS 3336 3336 ?    ?   ?   A . n 
A 1 3337 GLN 3337 3337 ?    ?   ?   A . n 
A 1 3338 ILE 3338 3338 ?    ?   ?   A . n 
A 1 3339 ARG 3339 3339 ?    ?   ?   A . n 
A 1 3340 SER 3340 3340 ?    ?   ?   A . n 
A 1 3341 ILE 3341 3341 ?    ?   ?   A . n 
A 1 3342 ILE 3342 3342 ?    ?   ?   A . n 
A 1 3343 MET 3343 3343 ?    ?   ?   A . n 
A 1 3344 ARG 3344 3344 ?    ?   ?   A . n 
A 1 3345 GLU 3345 3345 ?    ?   ?   A . n 
A 1 3346 ASN 3346 3346 ?    ?   ?   A . n 
A 1 3347 PHE 3347 3347 ?    ?   ?   A . n 
A 1 3348 ILE 3348 3348 ?    ?   ?   A . n 
A 1 3349 PRO 3349 3349 ?    ?   ?   A . n 
A 1 3350 THR 3350 3350 ?    ?   ?   A . n 
A 1 3351 ILE 3351 3351 ?    ?   ?   A . n 
A 1 3352 VAL 3352 3352 ?    ?   ?   A . n 
A 1 3353 ASN 3353 3353 ?    ?   ?   A . n 
A 1 3354 PHE 3354 3354 ?    ?   ?   A . n 
A 1 3355 SER 3355 3355 ?    ?   ?   A . n 
A 1 3356 ALA 3356 3356 ?    ?   ?   A . n 
A 1 3357 GLU 3357 3357 ?    ?   ?   A . n 
A 1 3358 GLU 3358 3358 ?    ?   ?   A . n 
A 1 3359 ILE 3359 3359 ?    ?   ?   A . n 
A 1 3360 SER 3360 3360 ?    ?   ?   A . n 
A 1 3361 ASP 3361 3361 ?    ?   ?   A . n 
A 1 3362 ALA 3362 3362 ?    ?   ?   A . n 
A 1 3363 ILE 3363 3363 ?    ?   ?   A . n 
A 1 3364 ARG 3364 3364 ?    ?   ?   A . n 
A 1 3365 GLU 3365 3365 ?    ?   ?   A . n 
A 1 3366 LYS 3366 3366 ?    ?   ?   A . n 
A 1 3367 MET 3367 3367 ?    ?   ?   A . n 
A 1 3368 LYS 3368 3368 ?    ?   ?   A . n 
A 1 3369 LYS 3369 3369 ?    ?   ?   A . n 
A 1 3370 ASN 3370 3370 ?    ?   ?   A . n 
A 1 3371 TYR 3371 3371 ?    ?   ?   A . n 
A 1 3372 MET 3372 3372 ?    ?   ?   A . n 
A 1 3373 SER 3373 3373 ?    ?   ?   A . n 
A 1 3374 ASN 3374 3374 ?    ?   ?   A . n 
A 1 3375 PRO 3375 3375 ?    ?   ?   A . n 
A 1 3376 SER 3376 3376 ?    ?   ?   A . n 
A 1 3377 TYR 3377 3377 ?    ?   ?   A . n 
A 1 3378 ASN 3378 3378 ?    ?   ?   A . n 
A 1 3379 TYR 3379 3379 ?    ?   ?   A . n 
A 1 3380 GLU 3380 3380 ?    ?   ?   A . n 
A 1 3381 ILE 3381 3381 ?    ?   ?   A . n 
A 1 3382 VAL 3382 3382 ?    ?   ?   A . n 
A 1 3383 ASN 3383 3383 ?    ?   ?   A . n 
A 1 3384 ARG 3384 3384 ?    ?   ?   A . n 
A 1 3385 ALA 3385 3385 ?    ?   ?   A . n 
A 1 3386 SER 3386 3386 ?    ?   ?   A . n 
A 1 3387 LEU 3387 3387 ?    ?   ?   A . n 
A 1 3388 ALA 3388 3388 ?    ?   ?   A . n 
A 1 3389 CYS 3389 3389 ?    ?   ?   A . n 
A 1 3390 GLY 3390 3390 ?    ?   ?   A . n 
A 1 3391 PRO 3391 3391 ?    ?   ?   A . n 
A 1 3392 MET 3392 3392 ?    ?   ?   A . n 
A 1 3393 VAL 3393 3393 ?    ?   ?   A . n 
A 1 3394 LYS 3394 3394 ?    ?   ?   A . n 
A 1 3395 TRP 3395 3395 ?    ?   ?   A . n 
A 1 3396 ALA 3396 3396 ?    ?   ?   A . n 
A 1 3397 ILE 3397 3397 ?    ?   ?   A . n 
A 1 3398 ALA 3398 3398 ?    ?   ?   A . n 
A 1 3399 GLN 3399 3399 ?    ?   ?   A . n 
A 1 3400 LEU 3400 3400 ?    ?   ?   A . n 
A 1 3401 ASN 3401 3401 ?    ?   ?   A . n 
A 1 3402 TYR 3402 3402 ?    ?   ?   A . n 
A 1 3403 ALA 3403 3403 ?    ?   ?   A . n 
A 1 3404 ASP 3404 3404 ?    ?   ?   A . n 
A 1 3405 MET 3405 3405 ?    ?   ?   A . n 
A 1 3406 LEU 3406 3406 ?    ?   ?   A . n 
A 1 3407 LYS 3407 3407 ?    ?   ?   A . n 
A 1 3408 ARG 3408 3408 ?    ?   ?   A . n 
A 1 3409 VAL 3409 3409 ?    ?   ?   A . n 
A 1 3410 GLU 3410 3410 ?    ?   ?   A . n 
A 1 3411 PRO 3411 3411 ?    ?   ?   A . n 
A 1 3412 LEU 3412 3412 ?    ?   ?   A . n 
A 1 3413 ARG 3413 3413 ?    ?   ?   A . n 
A 1 3414 ASN 3414 3414 ?    ?   ?   A . n 
A 1 3415 GLU 3415 3415 ?    ?   ?   A . n 
A 1 3416 LEU 3416 3416 ?    ?   ?   A . n 
A 1 3417 GLN 3417 3417 ?    ?   ?   A . n 
A 1 3418 LYS 3418 3418 ?    ?   ?   A . n 
A 1 3419 LEU 3419 3419 ?    ?   ?   A . n 
A 1 3420 GLU 3420 3420 ?    ?   ?   A . n 
A 1 3421 ASP 3421 3421 ?    ?   ?   A . n 
A 1 3422 ASP 3422 3422 ?    ?   ?   A . n 
A 1 3423 ALA 3423 3423 ?    ?   ?   A . n 
A 1 3424 LYS 3424 3424 ?    ?   ?   A . n 
A 1 3425 ASP 3425 3425 ?    ?   ?   A . n 
A 1 3426 ASN 3426 3426 ?    ?   ?   A . n 
A 1 3427 GLN 3427 3427 ?    ?   ?   A . n 
A 1 3428 GLN 3428 3428 ?    ?   ?   A . n 
A 1 3429 LYS 3429 3429 ?    ?   ?   A . n 
A 1 3430 ALA 3430 3430 ?    ?   ?   A . n 
A 1 3431 ASN 3431 3431 ?    ?   ?   A . n 
A 1 3432 GLU 3432 3432 ?    ?   ?   A . n 
A 1 3433 VAL 3433 3433 ?    ?   ?   A . n 
A 1 3434 GLU 3434 3434 ?    ?   ?   A . n 
A 1 3435 GLN 3435 3435 ?    ?   ?   A . n 
A 1 3436 MET 3436 3436 ?    ?   ?   A . n 
A 1 3437 ILE 3437 3437 ?    ?   ?   A . n 
A 1 3438 ARG 3438 3438 ?    ?   ?   A . n 
A 1 3439 ASP 3439 3439 ?    ?   ?   A . n 
A 1 3440 LEU 3440 3440 ?    ?   ?   A . n 
A 1 3441 GLU 3441 3441 ?    ?   ?   A . n 
A 1 3442 ALA 3442 3442 ?    ?   ?   A . n 
A 1 3443 SER 3443 3443 ?    ?   ?   A . n 
A 1 3444 ILE 3444 3444 ?    ?   ?   A . n 
A 1 3445 ALA 3445 3445 ?    ?   ?   A . n 
A 1 3446 ARG 3446 3446 ?    ?   ?   A . n 
A 1 3447 TYR 3447 3447 ?    ?   ?   A . n 
A 1 3448 LYS 3448 3448 ?    ?   ?   A . n 
A 1 3449 GLU 3449 3449 3449 GLU GLU A . n 
A 1 3450 GLU 3450 3450 3450 GLU GLU A . n 
A 1 3451 TYR 3451 3451 3451 TYR TYR A . n 
A 1 3452 ALA 3452 3452 3452 ALA ALA A . n 
A 1 3453 VAL 3453 3453 3453 VAL VAL A . n 
A 1 3454 LEU 3454 3454 3454 LEU LEU A . n 
A 1 3455 ILE 3455 3455 3455 ILE ILE A . n 
A 1 3456 SER 3456 3456 3456 SER SER A . n 
A 1 3457 GLU 3457 3457 3457 GLU GLU A . n 
A 1 3458 ALA 3458 3458 3458 ALA ALA A . n 
A 1 3459 GLN 3459 3459 3459 GLN GLN A . n 
A 1 3460 ALA 3460 3460 3460 ALA ALA A . n 
A 1 3461 ILE 3461 3461 3461 ILE ILE A . n 
A 1 3462 LYS 3462 3462 3462 LYS LYS A . n 
A 1 3463 ALA 3463 3463 3463 ALA ALA A . n 
A 1 3464 ASP 3464 3464 3464 ASP ASP A . n 
A 1 3465 LEU 3465 3465 3465 LEU LEU A . n 
A 1 3466 ALA 3466 3466 3466 ALA ALA A . n 
A 1 3467 ALA 3467 3467 3467 ALA ALA A . n 
A 1 3468 VAL 3468 3468 3468 VAL VAL A . n 
A 1 3469 GLU 3469 3469 3469 GLU GLU A . n 
A 1 3470 ALA 3470 3470 3470 ALA ALA A . n 
A 1 3471 LYS 3471 3471 3471 LYS LYS A . n 
A 1 3472 VAL 3472 3472 3472 VAL VAL A . n 
A 1 3473 ASN 3473 3473 3473 ASN ASN A . n 
A 1 3474 ARG 3474 3474 3474 ARG ARG A . n 
A 1 3475 SER 3475 3475 3475 SER SER A . n 
A 1 3476 THR 3476 3476 3476 THR THR A . n 
A 1 3477 ALA 3477 3477 3477 ALA ALA A . n 
A 1 3478 LEU 3478 3478 3478 LEU LEU A . n 
A 1 3479 LEU 3479 3479 3479 LEU LEU A . n 
A 1 3480 LYS 3480 3480 3480 LYS LYS A . n 
A 1 3481 SER 3481 3481 3481 SER SER A . n 
A 1 3482 LEU 3482 3482 3482 LEU LEU A . n 
A 1 3483 SER 3483 3483 3483 SER SER A . n 
A 1 3484 ALA 3484 3484 3484 ALA ALA A . n 
A 1 3485 GLU 3485 3485 3485 GLU GLU A . n 
A 1 3486 ARG 3486 3486 3486 ARG ARG A . n 
A 1 3487 GLU 3487 3487 3487 GLU GLU A . n 
A 1 3488 ARG 3488 3488 3488 ARG ARG A . n 
A 1 3489 TRP 3489 3489 3489 TRP TRP A . n 
A 1 3490 GLU 3490 3490 3490 GLU GLU A . n 
A 1 3491 LYS 3491 3491 3491 LYS LYS A . n 
A 1 3492 THR 3492 3492 3492 THR THR A . n 
A 1 3493 SER 3493 3493 3493 SER SER A . n 
A 1 3494 GLU 3494 3494 3494 GLU GLU A . n 
A 1 3495 THR 3495 3495 3495 THR THR A . n 
A 1 3496 PHE 3496 3496 3496 PHE PHE A . n 
A 1 3497 LYS 3497 3497 3497 LYS LYS A . n 
A 1 3498 ASN 3498 3498 3498 ASN ASN A . n 
A 1 3499 GLN 3499 3499 3499 GLN GLN A . n 
A 1 3500 MET 3500 3500 3500 MET MET A . n 
A 1 3501 SER 3501 3501 3501 SER SER A . n 
A 1 3502 THR 3502 3502 3502 THR THR A . n 
A 1 3503 ILE 3503 3503 3503 ILE ILE A . n 
A 1 3504 ALA 3504 3504 3504 ALA ALA A . n 
A 1 3505 GLY 3505 3505 3505 GLY GLY A . n 
A 1 3506 ASP 3506 3506 3506 ASP ASP A . n 
A 1 3507 CYS 3507 3507 3507 CYS CYS A . n 
A 1 3508 LEU 3508 3508 3508 LEU LEU A . n 
A 1 3509 LEU 3509 3509 3509 LEU LEU A . n 
A 1 3510 SER 3510 3510 3510 SER SER A . n 
A 1 3511 ALA 3511 3511 3511 ALA ALA A . n 
A 1 3512 ALA 3512 3512 3512 ALA ALA A . n 
A 1 3513 PHE 3513 3513 3513 PHE PHE A . n 
A 1 3514 ILE 3514 3514 3514 ILE ILE A . n 
A 1 3515 ALA 3515 3515 3515 ALA ALA A . n 
A 1 3516 TYR 3516 3516 3516 TYR TYR A . n 
A 1 3517 ALA 3517 3517 3517 ALA ALA A . n 
A 1 3518 GLY 3518 3518 3518 GLY GLY A . n 
A 1 3519 TYR 3519 3519 3519 TYR TYR A . n 
A 1 3520 PHE 3520 3520 3520 PHE PHE A . n 
A 1 3521 ASP 3521 3521 3521 ASP ASP A . n 
A 1 3522 GLN 3522 3522 3522 GLN GLN A . n 
A 1 3523 GLN 3523 3523 3523 GLN GLN A . n 
A 1 3524 MET 3524 3524 3524 MET MET A . n 
A 1 3525 ARG 3525 3525 3525 ARG ARG A . n 
A 1 3526 GLN 3526 3526 3526 GLN GLN A . n 
A 1 3527 ASN 3527 3527 3527 ASN ASN A . n 
A 1 3528 LEU 3528 3528 3528 LEU LEU A . n 
A 1 3529 PHE 3529 3529 3529 PHE PHE A . n 
A 1 3530 THR 3530 3530 3530 THR THR A . n 
A 1 3531 THR 3531 3531 3531 THR THR A . n 
A 1 3532 TRP 3532 3532 3532 TRP TRP A . n 
A 1 3533 SER 3533 3533 3533 SER SER A . n 
A 1 3534 HIS 3534 3534 3534 HIS HIS A . n 
A 1 3535 HIS 3535 3535 3535 HIS HIS A . n 
A 1 3536 LEU 3536 3536 3536 LEU LEU A . n 
A 1 3537 GLN 3537 3537 3537 GLN GLN A . n 
A 1 3538 GLN 3538 3538 3538 GLN GLN A . n 
A 1 3539 ALA 3539 3539 3539 ALA ALA A . n 
A 1 3540 ASN 3540 3540 3540 ASN ASN A . n 
A 1 3541 ILE 3541 3541 3541 ILE ILE A . n 
A 1 3542 GLN 3542 3542 3542 GLN GLN A . n 
A 1 3543 PHE 3543 3543 3543 PHE PHE A . n 
A 1 3544 ARG 3544 3544 3544 ARG ARG A . n 
A 1 3545 THR 3545 3545 3545 THR THR A . n 
A 1 3546 ASP 3546 3546 3546 ASP ASP A . n 
A 1 3547 ILE 3547 3547 3547 ILE ILE A . n 
A 1 3548 ALA 3548 3548 3548 ALA ALA A . n 
A 1 3549 ARG 3549 3549 3549 ARG ARG A . n 
A 1 3550 THR 3550 3550 3550 THR THR A . n 
A 1 3551 GLU 3551 3551 3551 GLU GLU A . n 
A 1 3552 TYR 3552 3552 3552 TYR TYR A . n 
A 1 3553 LEU 3553 3553 3553 LEU LEU A . n 
A 1 3554 SER 3554 3554 3554 SER SER A . n 
A 1 3555 ASN 3555 3555 3555 ASN ASN A . n 
A 1 3556 ALA 3556 3556 3556 ALA ALA A . n 
A 1 3557 ASP 3557 3557 3557 ASP ASP A . n 
A 1 3558 GLU 3558 3558 3558 GLU GLU A . n 
A 1 3559 ARG 3559 3559 3559 ARG ARG A . n 
A 1 3560 LEU 3560 3560 3560 LEU LEU A . n 
A 1 3561 ARG 3561 3561 3561 ARG ARG A . n 
A 1 3562 TRP 3562 3562 3562 TRP TRP A . n 
A 1 3563 GLN 3563 3563 3563 GLN GLN A . n 
A 1 3564 ALA 3564 3564 3564 ALA ALA A . n 
A 1 3565 SER 3565 3565 3565 SER SER A . n 
A 1 3566 SER 3566 3566 3566 SER SER A . n 
A 1 3567 LEU 3567 3567 3567 LEU LEU A . n 
A 1 3568 PRO 3568 3568 3568 PRO PRO A . n 
A 1 3569 ALA 3569 3569 3569 ALA ALA A . n 
A 1 3570 ASP 3570 3570 3570 ASP ASP A . n 
A 1 3571 ASP 3571 3571 3571 ASP ASP A . n 
A 1 3572 LEU 3572 3572 3572 LEU LEU A . n 
A 1 3573 CYS 3573 3573 3573 CYS CYS A . n 
A 1 3574 THR 3574 3574 3574 THR THR A . n 
A 1 3575 GLU 3575 3575 3575 GLU GLU A . n 
A 1 3576 ASN 3576 3576 3576 ASN ASN A . n 
A 1 3577 ALA 3577 3577 3577 ALA ALA A . n 
A 1 3578 ILE 3578 3578 3578 ILE ILE A . n 
A 1 3579 MET 3579 3579 3579 MET MET A . n 
A 1 3580 LEU 3580 3580 3580 LEU LEU A . n 
A 1 3581 LYS 3581 3581 3581 LYS LYS A . n 
A 1 3582 ARG 3582 3582 3582 ARG ARG A . n 
A 1 3583 PHE 3583 3583 3583 PHE PHE A . n 
A 1 3584 ASN 3584 3584 3584 ASN ASN A . n 
A 1 3585 ARG 3585 3585 3585 ARG ARG A . n 
A 1 3586 TYR 3586 3586 3586 TYR TYR A . n 
A 1 3587 PRO 3587 3587 3587 PRO PRO A . n 
A 1 3588 LEU 3588 3588 3588 LEU LEU A . n 
A 1 3589 ILE 3589 3589 3589 ILE ILE A . n 
A 1 3590 ILE 3590 3590 3590 ILE ILE A . n 
A 1 3591 ASP 3591 3591 3591 ASP ASP A . n 
A 1 3592 PRO 3592 3592 3592 PRO PRO A . n 
A 1 3593 SER 3593 3593 3593 SER SER A . n 
A 1 3594 GLY 3594 3594 3594 GLY GLY A . n 
A 1 3595 GLN 3595 3595 3595 GLN GLN A . n 
A 1 3596 ALA 3596 3596 3596 ALA ALA A . n 
A 1 3597 THR 3597 3597 3597 THR THR A . n 
A 1 3598 GLU 3598 3598 3598 GLU GLU A . n 
A 1 3599 PHE 3599 3599 3599 PHE PHE A . n 
A 1 3600 ILE 3600 3600 3600 ILE ILE A . n 
A 1 3601 MET 3601 3601 3601 MET MET A . n 
A 1 3602 ASN 3602 3602 3602 ASN ASN A . n 
A 1 3603 GLU 3603 3603 3603 GLU GLU A . n 
A 1 3604 TYR 3604 3604 3604 TYR TYR A . n 
A 1 3605 LYS 3605 3605 3605 LYS LYS A . n 
A 1 3606 ASP 3606 3606 3606 ASP ASP A . n 
A 1 3607 ARG 3607 3607 3607 ARG ARG A . n 
A 1 3608 LYS 3608 3608 3608 LYS LYS A . n 
A 1 3609 ILE 3609 3609 3609 ILE ILE A . n 
A 1 3610 THR 3610 3610 3610 THR THR A . n 
A 1 3611 ARG 3611 3611 3611 ARG ARG A . n 
A 1 3612 THR 3612 3612 3612 THR THR A . n 
A 1 3613 SER 3613 3613 3613 SER SER A . n 
A 1 3614 PHE 3614 3614 3614 PHE PHE A . n 
A 1 3615 LEU 3615 3615 3615 LEU LEU A . n 
A 1 3616 ASP 3616 3616 3616 ASP ASP A . n 
A 1 3617 ASP 3617 3617 3617 ASP ASP A . n 
A 1 3618 ALA 3618 3618 3618 ALA ALA A . n 
A 1 3619 PHE 3619 3619 3619 PHE PHE A . n 
A 1 3620 ARG 3620 3620 3620 ARG ARG A . n 
A 1 3621 LYS 3621 3621 3621 LYS LYS A . n 
A 1 3622 ASN 3622 3622 3622 ASN ASN A . n 
A 1 3623 LEU 3623 3623 3623 LEU LEU A . n 
A 1 3624 GLU 3624 3624 3624 GLU GLU A . n 
A 1 3625 SER 3625 3625 3625 SER SER A . n 
A 1 3626 ALA 3626 3626 3626 ALA ALA A . n 
A 1 3627 LEU 3627 3627 3627 LEU LEU A . n 
A 1 3628 ARG 3628 3628 3628 ARG ARG A . n 
A 1 3629 PHE 3629 3629 3629 PHE PHE A . n 
A 1 3630 GLY 3630 3630 3630 GLY GLY A . n 
A 1 3631 ASN 3631 3631 3631 ASN ASN A . n 
A 1 3632 PRO 3632 3632 3632 PRO PRO A . n 
A 1 3633 LEU 3633 3633 3633 LEU LEU A . n 
A 1 3634 LEU 3634 3634 3634 LEU LEU A . n 
A 1 3635 VAL 3635 3635 3635 VAL VAL A . n 
A 1 3636 GLN 3636 3636 3636 GLN GLN A . n 
A 1 3637 ASP 3637 3637 3637 ASP ASP A . n 
A 1 3638 VAL 3638 3638 3638 VAL VAL A . n 
A 1 3639 GLU 3639 3639 3639 GLU GLU A . n 
A 1 3640 SER 3640 3640 3640 SER SER A . n 
A 1 3641 TYR 3641 3641 3641 TYR TYR A . n 
A 1 3642 ASP 3642 3642 3642 ASP ASP A . n 
A 1 3643 PRO 3643 3643 3643 PRO PRO A . n 
A 1 3644 VAL 3644 3644 3644 VAL VAL A . n 
A 1 3645 LEU 3645 3645 3645 LEU LEU A . n 
A 1 3646 ASN 3646 3646 3646 ASN ASN A . n 
A 1 3647 PRO 3647 3647 3647 PRO PRO A . n 
A 1 3648 VAL 3648 3648 3648 VAL VAL A . n 
A 1 3649 LEU 3649 3649 3649 LEU LEU A . n 
A 1 3650 ASN 3650 3650 3650 ASN ASN A . n 
A 1 3651 ARG 3651 3651 3651 ARG ARG A . n 
A 1 3652 GLU 3652 3652 3652 GLU GLU A . n 
A 1 3653 VAL 3653 3653 3653 VAL VAL A . n 
A 1 3654 ARG 3654 3654 3654 ARG ARG A . n 
A 1 3655 ARG 3655 3655 3655 ARG ARG A . n 
A 1 3656 THR 3656 3656 3656 THR THR A . n 
A 1 3657 GLY 3657 3657 3657 GLY GLY A . n 
A 1 3658 GLY 3658 3658 3658 GLY GLY A . n 
A 1 3659 ARG 3659 3659 3659 ARG ARG A . n 
A 1 3660 VAL 3660 3660 3660 VAL VAL A . n 
A 1 3661 LEU 3661 3661 3661 LEU LEU A . n 
A 1 3662 ILE 3662 3662 3662 ILE ILE A . n 
A 1 3663 THR 3663 3663 3663 THR THR A . n 
A 1 3664 LEU 3664 3664 3664 LEU LEU A . n 
A 1 3665 GLY 3665 3665 3665 GLY GLY A . n 
A 1 3666 ASP 3666 3666 3666 ASP ASP A . n 
A 1 3667 GLN 3667 3667 3667 GLN GLN A . n 
A 1 3668 ASP 3668 3668 3668 ASP ASP A . n 
A 1 3669 ILE 3669 3669 3669 ILE ILE A . n 
A 1 3670 ASP 3670 3670 3670 ASP ASP A . n 
A 1 3671 LEU 3671 3671 3671 LEU LEU A . n 
A 1 3672 SER 3672 3672 3672 SER SER A . n 
A 1 3673 PRO 3673 3673 3673 PRO PRO A . n 
A 1 3674 SER 3674 3674 3674 SER SER A . n 
A 1 3675 PHE 3675 3675 3675 PHE PHE A . n 
A 1 3676 VAL 3676 3676 3676 VAL VAL A . n 
A 1 3677 ILE 3677 3677 3677 ILE ILE A . n 
A 1 3678 PHE 3678 3678 3678 PHE PHE A . n 
A 1 3679 LEU 3679 3679 3679 LEU LEU A . n 
A 1 3680 SER 3680 3680 3680 SER SER A . n 
A 1 3681 THR 3681 3681 3681 THR THR A . n 
A 1 3682 ARG 3682 3682 3682 ARG ARG A . n 
A 1 3683 ASP 3683 3683 3683 ASP ASP A . n 
A 1 3684 PRO 3684 3684 3684 PRO PRO A . n 
A 1 3685 THR 3685 3685 3685 THR THR A . n 
A 1 3686 VAL 3686 3686 3686 VAL VAL A . n 
A 1 3687 GLU 3687 3687 3687 GLU GLU A . n 
A 1 3688 PHE 3688 3688 3688 PHE PHE A . n 
A 1 3689 PRO 3689 3689 3689 PRO PRO A . n 
A 1 3690 PRO 3690 3690 3690 PRO PRO A . n 
A 1 3691 ASP 3691 3691 3691 ASP ASP A . n 
A 1 3692 LEU 3692 3692 3692 LEU LEU A . n 
A 1 3693 CYS 3693 3693 3693 CYS CYS A . n 
A 1 3694 SER 3694 3694 3694 SER SER A . n 
A 1 3695 ARG 3695 3695 3695 ARG ARG A . n 
A 1 3696 VAL 3696 3696 3696 VAL VAL A . n 
A 1 3697 THR 3697 3697 3697 THR THR A . n 
A 1 3698 PHE 3698 3698 3698 PHE PHE A . n 
A 1 3699 VAL 3699 3699 3699 VAL VAL A . n 
A 1 3700 ASN 3700 3700 3700 ASN ASN A . n 
A 1 3701 PHE 3701 3701 3701 PHE PHE A . n 
A 1 3702 THR 3702 3702 3702 THR THR A . n 
A 1 3703 VAL 3703 3703 3703 VAL VAL A . n 
A 1 3704 THR 3704 3704 3704 THR THR A . n 
A 1 3705 ARG 3705 3705 3705 ARG ARG A . n 
A 1 3706 SER 3706 3706 3706 SER SER A . n 
A 1 3707 SER 3707 3707 3707 SER SER A . n 
A 1 3708 LEU 3708 3708 3708 LEU LEU A . n 
A 1 3709 GLN 3709 3709 3709 GLN GLN A . n 
A 1 3710 SER 3710 3710 3710 SER SER A . n 
A 1 3711 GLN 3711 3711 3711 GLN GLN A . n 
A 1 3712 CYS 3712 3712 3712 CYS CYS A . n 
A 1 3713 LEU 3713 3713 3713 LEU LEU A . n 
A 1 3714 ASN 3714 3714 3714 ASN ASN A . n 
A 1 3715 GLU 3715 3715 3715 GLU GLU A . n 
A 1 3716 VAL 3716 3716 3716 VAL VAL A . n 
A 1 3717 LEU 3717 3717 3717 LEU LEU A . n 
A 1 3718 LYS 3718 3718 3718 LYS LYS A . n 
A 1 3719 ALA 3719 3719 3719 ALA ALA A . n 
A 1 3720 GLU 3720 3720 3720 GLU GLU A . n 
A 1 3721 ARG 3721 3721 3721 ARG ARG A . n 
A 1 3722 PRO 3722 3722 3722 PRO PRO A . n 
A 1 3723 ASP 3723 3723 3723 ASP ASP A . n 
A 1 3724 VAL 3724 3724 3724 VAL VAL A . n 
A 1 3725 ASP 3725 3725 3725 ASP ASP A . n 
A 1 3726 GLU 3726 3726 3726 GLU GLU A . n 
A 1 3727 LYS 3727 3727 3727 LYS LYS A . n 
A 1 3728 ARG 3728 3728 3728 ARG ARG A . n 
A 1 3729 SER 3729 3729 3729 SER SER A . n 
A 1 3730 ASP 3730 3730 3730 ASP ASP A . n 
A 1 3731 LEU 3731 3731 3731 LEU LEU A . n 
A 1 3732 LEU 3732 3732 3732 LEU LEU A . n 
A 1 3733 LYS 3733 3733 3733 LYS LYS A . n 
A 1 3734 LEU 3734 3734 3734 LEU LEU A . n 
A 1 3735 GLN 3735 3735 3735 GLN GLN A . n 
A 1 3736 GLY 3736 3736 3736 GLY GLY A . n 
A 1 3737 GLU 3737 3737 3737 GLU GLU A . n 
A 1 3738 PHE 3738 3738 3738 PHE PHE A . n 
A 1 3739 GLN 3739 3739 3739 GLN GLN A . n 
A 1 3740 LEU 3740 3740 3740 LEU LEU A . n 
A 1 3741 ARG 3741 3741 3741 ARG ARG A . n 
A 1 3742 LEU 3742 3742 3742 LEU LEU A . n 
A 1 3743 ARG 3743 3743 3743 ARG ARG A . n 
A 1 3744 GLN 3744 3744 3744 GLN GLN A . n 
A 1 3745 LEU 3745 3745 3745 LEU LEU A . n 
A 1 3746 GLU 3746 3746 3746 GLU GLU A . n 
A 1 3747 LYS 3747 3747 3747 LYS LYS A . n 
A 1 3748 SER 3748 3748 3748 SER SER A . n 
A 1 3749 LEU 3749 3749 3749 LEU LEU A . n 
A 1 3750 LEU 3750 3750 3750 LEU LEU A . n 
A 1 3751 GLN 3751 3751 3751 GLN GLN A . n 
A 1 3752 ALA 3752 3752 3752 ALA ALA A . n 
A 1 3753 LEU 3753 3753 3753 LEU LEU A . n 
A 1 3754 ASN 3754 3754 3754 ASN ASN A . n 
A 1 3755 GLU 3755 3755 3755 GLU GLU A . n 
A 1 3756 VAL 3756 3756 3756 VAL VAL A . n 
A 1 3757 LYS 3757 3757 3757 LYS LYS A . n 
A 1 3758 GLY 3758 3758 3758 GLY GLY A . n 
A 1 3759 ARG 3759 3759 3759 ARG ARG A . n 
A 1 3760 ILE 3760 3760 3760 ILE ILE A . n 
A 1 3761 LEU 3761 3761 3761 LEU LEU A . n 
A 1 3762 ASP 3762 3762 3762 ASP ASP A . n 
A 1 3763 ASP 3763 3763 3763 ASP ASP A . n 
A 1 3764 ASP 3764 3764 3764 ASP ASP A . n 
A 1 3765 THR 3765 3765 3765 THR THR A . n 
A 1 3766 ILE 3766 3766 3766 ILE ILE A . n 
A 1 3767 ILE 3767 3767 3767 ILE ILE A . n 
A 1 3768 THR 3768 3768 3768 THR THR A . n 
A 1 3769 THR 3769 3769 3769 THR THR A . n 
A 1 3770 LEU 3770 3770 3770 LEU LEU A . n 
A 1 3771 GLU 3771 3771 3771 GLU GLU A . n 
A 1 3772 ASN 3772 3772 3772 ASN ASN A . n 
A 1 3773 LEU 3773 3773 3773 LEU LEU A . n 
A 1 3774 LYS 3774 3774 3774 LYS LYS A . n 
A 1 3775 ARG 3775 3775 3775 ARG ARG A . n 
A 1 3776 GLU 3776 3776 3776 GLU GLU A . n 
A 1 3777 ALA 3777 3777 3777 ALA ALA A . n 
A 1 3778 ALA 3778 3778 3778 ALA ALA A . n 
A 1 3779 GLU 3779 3779 3779 GLU GLU A . n 
A 1 3780 VAL 3780 3780 3780 VAL VAL A . n 
A 1 3781 THR 3781 3781 3781 THR THR A . n 
A 1 3782 ARG 3782 3782 3782 ARG ARG A . n 
A 1 3783 LYS 3783 3783 3783 LYS LYS A . n 
A 1 3784 VAL 3784 3784 3784 VAL VAL A . n 
A 1 3785 GLU 3785 3785 3785 GLU GLU A . n 
A 1 3786 GLU 3786 3786 3786 GLU GLU A . n 
A 1 3787 THR 3787 3787 3787 THR THR A . n 
A 1 3788 ASP 3788 3788 3788 ASP ASP A . n 
A 1 3789 ILE 3789 3789 3789 ILE ILE A . n 
A 1 3790 VAL 3790 3790 3790 VAL VAL A . n 
A 1 3791 MET 3791 3791 3791 MET MET A . n 
A 1 3792 GLN 3792 3792 3792 GLN GLN A . n 
A 1 3793 GLU 3793 3793 3793 GLU GLU A . n 
A 1 3794 VAL 3794 3794 3794 VAL VAL A . n 
A 1 3795 GLU 3795 3795 3795 GLU GLU A . n 
A 1 3796 THR 3796 3796 3796 THR THR A . n 
A 1 3797 VAL 3797 3797 3797 VAL VAL A . n 
A 1 3798 SER 3798 3798 3798 SER SER A . n 
A 1 3799 GLN 3799 3799 3799 GLN GLN A . n 
A 1 3800 GLN 3800 3800 3800 GLN GLN A . n 
A 1 3801 TYR 3801 3801 3801 TYR TYR A . n 
A 1 3802 LEU 3802 3802 3802 LEU LEU A . n 
A 1 3803 PRO 3803 3803 3803 PRO PRO A . n 
A 1 3804 LEU 3804 3804 3804 LEU LEU A . n 
A 1 3805 SER 3805 3805 3805 SER SER A . n 
A 1 3806 THR 3806 3806 3806 THR THR A . n 
A 1 3807 ALA 3807 3807 3807 ALA ALA A . n 
A 1 3808 CYS 3808 3808 3808 CYS CYS A . n 
A 1 3809 SER 3809 3809 3809 SER SER A . n 
A 1 3810 SER 3810 3810 3810 SER SER A . n 
A 1 3811 ILE 3811 3811 3811 ILE ILE A . n 
A 1 3812 TYR 3812 3812 3812 TYR TYR A . n 
A 1 3813 PHE 3813 3813 3813 PHE PHE A . n 
A 1 3814 THR 3814 3814 3814 THR THR A . n 
A 1 3815 MET 3815 3815 3815 MET MET A . n 
A 1 3816 GLU 3816 3816 3816 GLU GLU A . n 
A 1 3817 SER 3817 3817 3817 SER SER A . n 
A 1 3818 LEU 3818 3818 3818 LEU LEU A . n 
A 1 3819 LYS 3819 3819 3819 LYS LYS A . n 
A 1 3820 GLN 3820 3820 3820 GLN GLN A . n 
A 1 3821 ILE 3821 3821 3821 ILE ILE A . n 
A 1 3822 HIS 3822 3822 3822 HIS HIS A . n 
A 1 3823 PHE 3823 3823 3823 PHE PHE A . n 
A 1 3824 LEU 3824 3824 3824 LEU LEU A . n 
A 1 3825 TYR 3825 3825 3825 TYR TYR A . n 
A 1 3826 GLN 3826 3826 3826 GLN GLN A . n 
A 1 3827 TYR 3827 3827 3827 TYR TYR A . n 
A 1 3828 SER 3828 3828 3828 SER SER A . n 
A 1 3829 LEU 3829 3829 3829 LEU LEU A . n 
A 1 3830 GLN 3830 3830 3830 GLN GLN A . n 
A 1 3831 PHE 3831 3831 3831 PHE PHE A . n 
A 1 3832 PHE 3832 3832 3832 PHE PHE A . n 
A 1 3833 LEU 3833 3833 3833 LEU LEU A . n 
A 1 3834 ASP 3834 3834 3834 ASP ASP A . n 
A 1 3835 ILE 3835 3835 3835 ILE ILE A . n 
A 1 3836 TYR 3836 3836 3836 TYR TYR A . n 
A 1 3837 HIS 3837 3837 3837 HIS HIS A . n 
A 1 3838 ASN 3838 3838 3838 ASN ASN A . n 
A 1 3839 VAL 3839 3839 3839 VAL VAL A . n 
A 1 3840 LEU 3840 3840 3840 LEU LEU A . n 
A 1 3841 TYR 3841 3841 3841 TYR TYR A . n 
A 1 3842 GLU 3842 3842 3842 GLU GLU A . n 
A 1 3843 ASN 3843 3843 3843 ASN ASN A . n 
A 1 3844 PRO 3844 3844 3844 PRO PRO A . n 
A 1 3845 ASN 3845 3845 3845 ASN ASN A . n 
A 1 3846 LEU 3846 3846 3846 LEU LEU A . n 
A 1 3847 LYS 3847 3847 3847 LYS LYS A . n 
A 1 3848 GLY 3848 3848 3848 GLY GLY A . n 
A 1 3849 VAL 3849 3849 3849 VAL VAL A . n 
A 1 3850 THR 3850 3850 3850 THR THR A . n 
A 1 3851 ASP 3851 3851 3851 ASP ASP A . n 
A 1 3852 HIS 3852 3852 3852 HIS HIS A . n 
A 1 3853 THR 3853 3853 3853 THR THR A . n 
A 1 3854 GLN 3854 3854 3854 GLN GLN A . n 
A 1 3855 ARG 3855 3855 3855 ARG ARG A . n 
A 1 3856 LEU 3856 3856 3856 LEU LEU A . n 
A 1 3857 SER 3857 3857 3857 SER SER A . n 
A 1 3858 ILE 3858 3858 3858 ILE ILE A . n 
A 1 3859 ILE 3859 3859 3859 ILE ILE A . n 
A 1 3860 THR 3860 3860 3860 THR THR A . n 
A 1 3861 LYS 3861 3861 3861 LYS LYS A . n 
A 1 3862 ASP 3862 3862 3862 ASP ASP A . n 
A 1 3863 LEU 3863 3863 3863 LEU LEU A . n 
A 1 3864 PHE 3864 3864 3864 PHE PHE A . n 
A 1 3865 GLN 3865 3865 3865 GLN GLN A . n 
A 1 3866 VAL 3866 3866 3866 VAL VAL A . n 
A 1 3867 ALA 3867 3867 3867 ALA ALA A . n 
A 1 3868 PHE 3868 3868 3868 PHE PHE A . n 
A 1 3869 ASN 3869 3869 3869 ASN ASN A . n 
A 1 3870 ARG 3870 3870 3870 ARG ARG A . n 
A 1 3871 VAL 3871 3871 3871 VAL VAL A . n 
A 1 3872 ALA 3872 3872 3872 ALA ALA A . n 
A 1 3873 ARG 3873 3873 3873 ARG ARG A . n 
A 1 3874 GLY 3874 3874 3874 GLY GLY A . n 
A 1 3875 MET 3875 3875 3875 MET MET A . n 
A 1 3876 LEU 3876 3876 3876 LEU LEU A . n 
A 1 3877 HIS 3877 3877 3877 HIS HIS A . n 
A 1 3878 GLN 3878 3878 3878 GLN GLN A . n 
A 1 3879 ASP 3879 3879 3879 ASP ASP A . n 
A 1 3880 HIS 3880 3880 3880 HIS HIS A . n 
A 1 3881 ILE 3881 3881 3881 ILE ILE A . n 
A 1 3882 THR 3882 3882 3882 THR THR A . n 
A 1 3883 PHE 3883 3883 3883 PHE PHE A . n 
A 1 3884 ALA 3884 3884 3884 ALA ALA A . n 
A 1 3885 MET 3885 3885 3885 MET MET A . n 
A 1 3886 LEU 3886 3886 3886 LEU LEU A . n 
A 1 3887 LEU 3887 3887 3887 LEU LEU A . n 
A 1 3888 ALA 3888 3888 3888 ALA ALA A . n 
A 1 3889 ARG 3889 3889 3889 ARG ARG A . n 
A 1 3890 ILE 3890 3890 3890 ILE ILE A . n 
A 1 3891 LYS 3891 3891 3891 LYS LYS A . n 
A 1 3892 LEU 3892 3892 3892 LEU LEU A . n 
A 1 3893 LYS 3893 3893 3893 LYS LYS A . n 
A 1 3894 GLY 3894 3894 3894 GLY GLY A . n 
A 1 3895 THR 3895 3895 3895 THR THR A . n 
A 1 3896 VAL 3896 3896 3896 VAL VAL A . n 
A 1 3897 GLY 3897 3897 3897 GLY GLY A . n 
A 1 3898 GLU 3898 3898 3898 GLU GLU A . n 
A 1 3899 PRO 3899 3899 3899 PRO PRO A . n 
A 1 3900 THR 3900 3900 3900 THR THR A . n 
A 1 3901 TYR 3901 3901 3901 TYR TYR A . n 
A 1 3902 ASP 3902 3902 3902 ASP ASP A . n 
A 1 3903 ALA 3903 3903 3903 ALA ALA A . n 
A 1 3904 GLU 3904 3904 3904 GLU GLU A . n 
A 1 3905 PHE 3905 3905 3905 PHE PHE A . n 
A 1 3906 GLN 3906 3906 3906 GLN GLN A . n 
A 1 3907 HIS 3907 3907 3907 HIS HIS A . n 
A 1 3908 PHE 3908 3908 3908 PHE PHE A . n 
A 1 3909 LEU 3909 3909 3909 LEU LEU A . n 
A 1 3910 ARG 3910 3910 3910 ARG ARG A . n 
A 1 3911 GLY 3911 3911 3911 GLY GLY A . n 
A 1 3912 ASN 3912 3912 3912 ASN ASN A . n 
A 1 3913 GLU 3913 3913 3913 GLU GLU A . n 
A 1 3914 ILE 3914 3914 3914 ILE ILE A . n 
A 1 3915 VAL 3915 3915 3915 VAL VAL A . n 
A 1 3916 LEU 3916 3916 3916 LEU LEU A . n 
A 1 3917 SER 3917 3917 3917 SER SER A . n 
A 1 3918 ALA 3918 3918 3918 ALA ALA A . n 
A 1 3919 GLY 3919 3919 3919 GLY GLY A . n 
A 1 3920 SER 3920 3920 3920 SER SER A . n 
A 1 3921 THR 3921 3921 3921 THR THR A . n 
A 1 3922 PRO 3922 3922 3922 PRO PRO A . n 
A 1 3923 ARG 3923 3923 3923 ARG ARG A . n 
A 1 3924 ILE 3924 3924 3924 ILE ILE A . n 
A 1 3925 GLN 3925 3925 3925 GLN GLN A . n 
A 1 3926 GLY 3926 3926 3926 GLY GLY A . n 
A 1 3927 LEU 3927 3927 3927 LEU LEU A . n 
A 1 3928 THR 3928 3928 3928 THR THR A . n 
A 1 3929 VAL 3929 3929 3929 VAL VAL A . n 
A 1 3930 GLU 3930 3930 3930 GLU GLU A . n 
A 1 3931 GLN 3931 3931 3931 GLN GLN A . n 
A 1 3932 ALA 3932 3932 3932 ALA ALA A . n 
A 1 3933 GLU 3933 3933 3933 GLU GLU A . n 
A 1 3934 ALA 3934 3934 3934 ALA ALA A . n 
A 1 3935 VAL 3935 3935 3935 VAL VAL A . n 
A 1 3936 VAL 3936 3936 3936 VAL VAL A . n 
A 1 3937 ARG 3937 3937 3937 ARG ARG A . n 
A 1 3938 LEU 3938 3938 3938 LEU LEU A . n 
A 1 3939 SER 3939 3939 3939 SER SER A . n 
A 1 3940 CYS 3940 3940 3940 CYS CYS A . n 
A 1 3941 LEU 3941 3941 3941 LEU LEU A . n 
A 1 3942 PRO 3942 3942 3942 PRO PRO A . n 
A 1 3943 ALA 3943 3943 3943 ALA ALA A . n 
A 1 3944 PHE 3944 3944 3944 PHE PHE A . n 
A 1 3945 LYS 3945 3945 3945 LYS LYS A . n 
A 1 3946 ASP 3946 3946 3946 ASP ASP A . n 
A 1 3947 LEU 3947 3947 3947 LEU LEU A . n 
A 1 3948 ILE 3948 3948 3948 ILE ILE A . n 
A 1 3949 ALA 3949 3949 3949 ALA ALA A . n 
A 1 3950 LYS 3950 3950 3950 LYS LYS A . n 
A 1 3951 VAL 3951 3951 3951 VAL VAL A . n 
A 1 3952 GLN 3952 3952 3952 GLN GLN A . n 
A 1 3953 ALA 3953 3953 3953 ALA ALA A . n 
A 1 3954 ASP 3954 3954 3954 ASP ASP A . n 
A 1 3955 GLU 3955 3955 3955 GLU GLU A . n 
A 1 3956 GLN 3956 3956 3956 GLN GLN A . n 
A 1 3957 PHE 3957 3957 3957 PHE PHE A . n 
A 1 3958 GLY 3958 3958 3958 GLY GLY A . n 
A 1 3959 ILE 3959 3959 3959 ILE ILE A . n 
A 1 3960 TRP 3960 3960 3960 TRP TRP A . n 
A 1 3961 LEU 3961 3961 3961 LEU LEU A . n 
A 1 3962 ASP 3962 3962 3962 ASP ASP A . n 
A 1 3963 SER 3963 3963 3963 SER SER A . n 
A 1 3964 SER 3964 3964 3964 SER SER A . n 
A 1 3965 SER 3965 3965 3965 SER SER A . n 
A 1 3966 PRO 3966 3966 3966 PRO PRO A . n 
A 1 3967 GLU 3967 3967 3967 GLU GLU A . n 
A 1 3968 GLN 3968 3968 3968 GLN GLN A . n 
A 1 3969 THR 3969 3969 3969 THR THR A . n 
A 1 3970 VAL 3970 3970 3970 VAL VAL A . n 
A 1 3971 PRO 3971 3971 3971 PRO PRO A . n 
A 1 3972 TYR 3972 3972 3972 TYR TYR A . n 
A 1 3973 LEU 3973 3973 3973 LEU LEU A . n 
A 1 3974 TRP 3974 3974 3974 TRP TRP A . n 
A 1 3975 SER 3975 3975 3975 SER SER A . n 
A 1 3976 GLU 3976 3976 3976 GLU GLU A . n 
A 1 3977 GLU 3977 3977 3977 GLU GLU A . n 
A 1 3978 THR 3978 3978 3978 THR THR A . n 
A 1 3979 PRO 3979 3979 3979 PRO PRO A . n 
A 1 3980 ALA 3980 3980 3980 ALA ALA A . n 
A 1 3981 THR 3981 3981 3981 THR THR A . n 
A 1 3982 PRO 3982 3982 3982 PRO PRO A . n 
A 1 3983 ILE 3983 3983 3983 ILE ILE A . n 
A 1 3984 GLY 3984 3984 3984 GLY GLY A . n 
A 1 3985 GLN 3985 3985 3985 GLN GLN A . n 
A 1 3986 ALA 3986 3986 3986 ALA ALA A . n 
A 1 3987 ILE 3987 3987 3987 ILE ILE A . n 
A 1 3988 HIS 3988 3988 3988 HIS HIS A . n 
A 1 3989 ARG 3989 3989 3989 ARG ARG A . n 
A 1 3990 LEU 3990 3990 3990 LEU LEU A . n 
A 1 3991 LEU 3991 3991 3991 LEU LEU A . n 
A 1 3992 LEU 3992 3992 3992 LEU LEU A . n 
A 1 3993 ILE 3993 3993 3993 ILE ILE A . n 
A 1 3994 GLN 3994 3994 3994 GLN GLN A . n 
A 1 3995 ALA 3995 3995 3995 ALA ALA A . n 
A 1 3996 PHE 3996 3996 3996 PHE PHE A . n 
A 1 3997 ARG 3997 3997 3997 ARG ARG A . n 
A 1 3998 PRO 3998 3998 3998 PRO PRO A . n 
A 1 3999 ASP 3999 3999 3999 ASP ASP A . n 
A 1 4000 ARG 4000 4000 4000 ARG ARG A . n 
A 1 4001 LEU 4001 4001 4001 LEU LEU A . n 
A 1 4002 LEU 4002 4002 4002 LEU LEU A . n 
A 1 4003 ALA 4003 4003 4003 ALA ALA A . n 
A 1 4004 MET 4004 4004 4004 MET MET A . n 
A 1 4005 ALA 4005 4005 4005 ALA ALA A . n 
A 1 4006 HIS 4006 4006 4006 HIS HIS A . n 
A 1 4007 MET 4007 4007 4007 MET MET A . n 
A 1 4008 PHE 4008 4008 4008 PHE PHE A . n 
A 1 4009 VAL 4009 4009 4009 VAL VAL A . n 
A 1 4010 SER 4010 4010 4010 SER SER A . n 
A 1 4011 THR 4011 4011 4011 THR THR A . n 
A 1 4012 ASN 4012 4012 4012 ASN ASN A . n 
A 1 4013 LEU 4013 4013 4013 LEU LEU A . n 
A 1 4014 GLY 4014 4014 4014 GLY GLY A . n 
A 1 4015 GLU 4015 4015 4015 GLU GLU A . n 
A 1 4016 SER 4016 4016 4016 SER SER A . n 
A 1 4017 PHE 4017 4017 4017 PHE PHE A . n 
A 1 4018 MET 4018 4018 4018 MET MET A . n 
A 1 4019 SER 4019 4019 4019 SER SER A . n 
A 1 4020 ILE 4020 4020 4020 ILE ILE A . n 
A 1 4021 MET 4021 4021 4021 MET MET A . n 
A 1 4022 GLU 4022 4022 4022 GLU GLU A . n 
A 1 4023 GLN 4023 4023 4023 GLN GLN A . n 
A 1 4024 PRO 4024 4024 4024 PRO PRO A . n 
A 1 4025 LEU 4025 4025 4025 LEU LEU A . n 
A 1 4026 ASP 4026 4026 4026 ASP ASP A . n 
A 1 4027 LEU 4027 4027 4027 LEU LEU A . n 
A 1 4028 THR 4028 4028 4028 THR THR A . n 
A 1 4029 HIS 4029 4029 4029 HIS HIS A . n 
A 1 4030 ILE 4030 4030 4030 ILE ILE A . n 
A 1 4031 VAL 4031 4031 4031 VAL VAL A . n 
A 1 4032 GLY 4032 4032 4032 GLY GLY A . n 
A 1 4033 THR 4033 4033 4033 THR THR A . n 
A 1 4034 GLU 4034 4034 4034 GLU GLU A . n 
A 1 4035 VAL 4035 4035 4035 VAL VAL A . n 
A 1 4036 LYS 4036 4036 4036 LYS LYS A . n 
A 1 4037 PRO 4037 4037 4037 PRO PRO A . n 
A 1 4038 ASN 4038 4038 4038 ASN ASN A . n 
A 1 4039 THR 4039 4039 4039 THR THR A . n 
A 1 4040 PRO 4040 4040 4040 PRO PRO A . n 
A 1 4041 VAL 4041 4041 4041 VAL VAL A . n 
A 1 4042 LEU 4042 4042 4042 LEU LEU A . n 
A 1 4043 MET 4043 4043 4043 MET MET A . n 
A 1 4044 CYS 4044 4044 4044 CYS CYS A . n 
A 1 4045 SER 4045 4045 4045 SER SER A . n 
A 1 4046 VAL 4046 4046 4046 VAL VAL A . n 
A 1 4047 PRO 4047 4047 4047 PRO PRO A . n 
A 1 4048 GLY 4048 4048 4048 GLY GLY A . n 
A 1 4049 TYR 4049 4049 4049 TYR TYR A . n 
A 1 4050 ASP 4050 4050 4050 ASP ASP A . n 
A 1 4051 ALA 4051 4051 4051 ALA ALA A . n 
A 1 4052 SER 4052 4052 4052 SER SER A . n 
A 1 4053 GLY 4053 4053 4053 GLY GLY A . n 
A 1 4054 HIS 4054 4054 4054 HIS HIS A . n 
A 1 4055 VAL 4055 4055 4055 VAL VAL A . n 
A 1 4056 GLU 4056 4056 4056 GLU GLU A . n 
A 1 4057 ASP 4057 4057 4057 ASP ASP A . n 
A 1 4058 LEU 4058 4058 4058 LEU LEU A . n 
A 1 4059 ALA 4059 4059 4059 ALA ALA A . n 
A 1 4060 ALA 4060 4060 4060 ALA ALA A . n 
A 1 4061 GLU 4061 4061 4061 GLU GLU A . n 
A 1 4062 GLN 4062 4062 4062 GLN GLN A . n 
A 1 4063 ASN 4063 4063 4063 ASN ASN A . n 
A 1 4064 THR 4064 4064 4064 THR THR A . n 
A 1 4065 GLN 4065 4065 4065 GLN GLN A . n 
A 1 4066 ILE 4066 4066 4066 ILE ILE A . n 
A 1 4067 THR 4067 4067 4067 THR THR A . n 
A 1 4068 SER 4068 4068 4068 SER SER A . n 
A 1 4069 ILE 4069 4069 4069 ILE ILE A . n 
A 1 4070 ALA 4070 4070 4070 ALA ALA A . n 
A 1 4071 ILE 4071 4071 4071 ILE ILE A . n 
A 1 4072 GLY 4072 4072 4072 GLY GLY A . n 
A 1 4073 SER 4073 4073 4073 SER SER A . n 
A 1 4074 ALA 4074 4074 4074 ALA ALA A . n 
A 1 4075 GLU 4075 4075 4075 GLU GLU A . n 
A 1 4076 GLY 4076 4076 4076 GLY GLY A . n 
A 1 4077 PHE 4077 4077 4077 PHE PHE A . n 
A 1 4078 ASN 4078 4078 4078 ASN ASN A . n 
A 1 4079 GLN 4079 4079 4079 GLN GLN A . n 
A 1 4080 ALA 4080 4080 4080 ALA ALA A . n 
A 1 4081 ASP 4081 4081 4081 ASP ASP A . n 
A 1 4082 LYS 4082 4082 4082 LYS LYS A . n 
A 1 4083 ALA 4083 4083 4083 ALA ALA A . n 
A 1 4084 ILE 4084 4084 4084 ILE ILE A . n 
A 1 4085 ASN 4085 4085 4085 ASN ASN A . n 
A 1 4086 THR 4086 4086 4086 THR THR A . n 
A 1 4087 ALA 4087 4087 4087 ALA ALA A . n 
A 1 4088 VAL 4088 4088 4088 VAL VAL A . n 
A 1 4089 LYS 4089 4089 4089 LYS LYS A . n 
A 1 4090 SER 4090 4090 4090 SER SER A . n 
A 1 4091 GLY 4091 4091 4091 GLY GLY A . n 
A 1 4092 ARG 4092 4092 4092 ARG ARG A . n 
A 1 4093 TRP 4093 4093 4093 TRP TRP A . n 
A 1 4094 VAL 4094 4094 4094 VAL VAL A . n 
A 1 4095 MET 4095 4095 4095 MET MET A . n 
A 1 4096 LEU 4096 4096 4096 LEU LEU A . n 
A 1 4097 LYS 4097 4097 4097 LYS LYS A . n 
A 1 4098 ASN 4098 4098 4098 ASN ASN A . n 
A 1 4099 VAL 4099 4099 4099 VAL VAL A . n 
A 1 4100 HIS 4100 4100 4100 HIS HIS A . n 
A 1 4101 LEU 4101 4101 4101 LEU LEU A . n 
A 1 4102 ALA 4102 4102 4102 ALA ALA A . n 
A 1 4103 PRO 4103 4103 4103 PRO PRO A . n 
A 1 4104 GLY 4104 4104 4104 GLY GLY A . n 
A 1 4105 TRP 4105 4105 4105 TRP TRP A . n 
A 1 4106 LEU 4106 4106 4106 LEU LEU A . n 
A 1 4107 MET 4107 4107 4107 MET MET A . n 
A 1 4108 GLN 4108 4108 4108 GLN GLN A . n 
A 1 4109 LEU 4109 4109 4109 LEU LEU A . n 
A 1 4110 GLU 4110 4110 4110 GLU GLU A . n 
A 1 4111 LYS 4111 4111 4111 LYS LYS A . n 
A 1 4112 LYS 4112 4112 4112 LYS LYS A . n 
A 1 4113 LEU 4113 4113 4113 LEU LEU A . n 
A 1 4114 HIS 4114 4114 4114 HIS HIS A . n 
A 1 4115 SER 4115 4115 4115 SER SER A . n 
A 1 4116 LEU 4116 4116 4116 LEU LEU A . n 
A 1 4117 GLN 4117 4117 4117 GLN GLN A . n 
A 1 4118 PRO 4118 4118 4118 PRO PRO A . n 
A 1 4119 HIS 4119 4119 4119 HIS HIS A . n 
A 1 4120 ALA 4120 4120 4120 ALA ALA A . n 
A 1 4121 CYS 4121 4121 4121 CYS CYS A . n 
A 1 4122 PHE 4122 4122 4122 PHE PHE A . n 
A 1 4123 ARG 4123 4123 4123 ARG ARG A . n 
A 1 4124 LEU 4124 4124 4124 LEU LEU A . n 
A 1 4125 PHE 4125 4125 4125 PHE PHE A . n 
A 1 4126 LEU 4126 4126 4126 LEU LEU A . n 
A 1 4127 THR 4127 4127 4127 THR THR A . n 
A 1 4128 MET 4128 4128 4128 MET MET A . n 
A 1 4129 GLU 4129 4129 4129 GLU GLU A . n 
A 1 4130 ILE 4130 4130 4130 ILE ILE A . n 
A 1 4131 ASN 4131 4131 4131 ASN ASN A . n 
A 1 4132 PRO 4132 4132 4132 PRO PRO A . n 
A 1 4133 LYS 4133 4133 4133 LYS LYS A . n 
A 1 4134 VAL 4134 4134 4134 VAL VAL A . n 
A 1 4135 PRO 4135 4135 4135 PRO PRO A . n 
A 1 4136 VAL 4136 4136 4136 VAL VAL A . n 
A 1 4137 ASN 4137 4137 4137 ASN ASN A . n 
A 1 4138 LEU 4138 4138 4138 LEU LEU A . n 
A 1 4139 LEU 4139 4139 4139 LEU LEU A . n 
A 1 4140 ARG 4140 4140 4140 ARG ARG A . n 
A 1 4141 ALA 4141 4141 4141 ALA ALA A . n 
A 1 4142 GLY 4142 4142 4142 GLY GLY A . n 
A 1 4143 ARG 4143 4143 4143 ARG ARG A . n 
A 1 4144 ILE 4144 4144 4144 ILE ILE A . n 
A 1 4145 PHE 4145 4145 4145 PHE PHE A . n 
A 1 4146 VAL 4146 4146 4146 VAL VAL A . n 
A 1 4147 PHE 4147 4147 4147 PHE PHE A . n 
A 1 4148 GLU 4148 4148 4148 GLU GLU A . n 
A 1 4149 PRO 4149 4149 4149 PRO PRO A . n 
A 1 4150 PRO 4150 4150 4150 PRO PRO A . n 
A 1 4151 PRO 4151 4151 4151 PRO PRO A . n 
A 1 4152 GLY 4152 4152 4152 GLY GLY A . n 
A 1 4153 VAL 4153 4153 4153 VAL VAL A . n 
A 1 4154 LYS 4154 4154 4154 LYS LYS A . n 
A 1 4155 ALA 4155 4155 4155 ALA ALA A . n 
A 1 4156 ASN 4156 4156 4156 ASN ASN A . n 
A 1 4157 MET 4157 4157 4157 MET MET A . n 
A 1 4158 LEU 4158 4158 4158 LEU LEU A . n 
A 1 4159 ARG 4159 4159 4159 ARG ARG A . n 
A 1 4160 THR 4160 4160 4160 THR THR A . n 
A 1 4161 PHE 4161 4161 4161 PHE PHE A . n 
A 1 4162 SER 4162 4162 4162 SER SER A . n 
A 1 4163 SER 4163 4163 4163 SER SER A . n 
A 1 4164 ILE 4164 4164 4164 ILE ILE A . n 
A 1 4165 PRO 4165 4165 4165 PRO PRO A . n 
A 1 4166 VAL 4166 4166 4166 VAL VAL A . n 
A 1 4167 SER 4167 4167 4167 SER SER A . n 
A 1 4168 ARG 4168 4168 4168 ARG ARG A . n 
A 1 4169 ILE 4169 4169 4169 ILE ILE A . n 
A 1 4170 CYS 4170 4170 4170 CYS CYS A . n 
A 1 4171 LYS 4171 4171 4171 LYS LYS A . n 
A 1 4172 SER 4172 4172 4172 SER SER A . n 
A 1 4173 PRO 4173 4173 4173 PRO PRO A . n 
A 1 4174 ASN 4174 4174 4174 ASN ASN A . n 
A 1 4175 GLU 4175 4175 4175 GLU GLU A . n 
A 1 4176 ARG 4176 4176 4176 ARG ARG A . n 
A 1 4177 ALA 4177 4177 4177 ALA ALA A . n 
A 1 4178 ARG 4178 4178 4178 ARG ARG A . n 
A 1 4179 LEU 4179 4179 4179 LEU LEU A . n 
A 1 4180 TYR 4180 4180 4180 TYR TYR A . n 
A 1 4181 PHE 4181 4181 4181 PHE PHE A . n 
A 1 4182 LEU 4182 4182 4182 LEU LEU A . n 
A 1 4183 LEU 4183 4183 4183 LEU LEU A . n 
A 1 4184 ALA 4184 4184 4184 ALA ALA A . n 
A 1 4185 TRP 4185 4185 4185 TRP TRP A . n 
A 1 4186 PHE 4186 4186 4186 PHE PHE A . n 
A 1 4187 HIS 4187 4187 4187 HIS HIS A . n 
A 1 4188 ALA 4188 4188 4188 ALA ALA A . n 
A 1 4189 ILE 4189 4189 4189 ILE ILE A . n 
A 1 4190 ILE 4190 4190 4190 ILE ILE A . n 
A 1 4191 GLN 4191 4191 4191 GLN GLN A . n 
A 1 4192 GLU 4192 4192 4192 GLU GLU A . n 
A 1 4193 ARG 4193 4193 4193 ARG ARG A . n 
A 1 4194 LEU 4194 4194 4194 LEU LEU A . n 
A 1 4195 ARG 4195 4195 4195 ARG ARG A . n 
A 1 4196 TYR 4196 4196 4196 TYR TYR A . n 
A 1 4197 ALA 4197 4197 4197 ALA ALA A . n 
A 1 4198 PRO 4198 4198 4198 PRO PRO A . n 
A 1 4199 LEU 4199 4199 4199 LEU LEU A . n 
A 1 4200 GLY 4200 4200 4200 GLY GLY A . n 
A 1 4201 TRP 4201 4201 4201 TRP TRP A . n 
A 1 4202 SER 4202 4202 4202 SER SER A . n 
A 1 4203 LYS 4203 4203 4203 LYS LYS A . n 
A 1 4204 LYS 4204 4204 4204 LYS LYS A . n 
A 1 4205 TYR 4205 4205 4205 TYR TYR A . n 
A 1 4206 GLU 4206 4206 4206 GLU GLU A . n 
A 1 4207 PHE 4207 4207 4207 PHE PHE A . n 
A 1 4208 GLY 4208 4208 4208 GLY GLY A . n 
A 1 4209 GLU 4209 4209 4209 GLU GLU A . n 
A 1 4210 SER 4210 4210 4210 SER SER A . n 
A 1 4211 ASP 4211 4211 4211 ASP ASP A . n 
A 1 4212 LEU 4212 4212 4212 LEU LEU A . n 
A 1 4213 ARG 4213 4213 4213 ARG ARG A . n 
A 1 4214 SER 4214 4214 4214 SER SER A . n 
A 1 4215 ALA 4215 4215 4215 ALA ALA A . n 
A 1 4216 CYS 4216 4216 4216 CYS CYS A . n 
A 1 4217 ASP 4217 4217 4217 ASP ASP A . n 
A 1 4218 THR 4218 4218 4218 THR THR A . n 
A 1 4219 VAL 4219 4219 4219 VAL VAL A . n 
A 1 4220 ASP 4220 4220 4220 ASP ASP A . n 
A 1 4221 THR 4221 4221 4221 THR THR A . n 
A 1 4222 TRP 4222 4222 4222 TRP TRP A . n 
A 1 4223 LEU 4223 4223 4223 LEU LEU A . n 
A 1 4224 ASP 4224 4224 4224 ASP ASP A . n 
A 1 4225 ASP 4225 4225 4225 ASP ASP A . n 
A 1 4226 THR 4226 4226 4226 THR THR A . n 
A 1 4227 ALA 4227 4227 4227 ALA ALA A . n 
A 1 4228 LYS 4228 4228 4228 LYS LYS A . n 
A 1 4229 GLY 4229 4229 4229 GLY GLY A . n 
A 1 4230 ARG 4230 4230 4230 ARG ARG A . n 
A 1 4231 GLN 4231 4231 4231 GLN GLN A . n 
A 1 4232 ASN 4232 4232 4232 ASN ASN A . n 
A 1 4233 ILE 4233 4233 4233 ILE ILE A . n 
A 1 4234 SER 4234 4234 4234 SER SER A . n 
A 1 4235 PRO 4235 4235 4235 PRO PRO A . n 
A 1 4236 ASP 4236 4236 4236 ASP ASP A . n 
A 1 4237 LYS 4237 4237 4237 LYS LYS A . n 
A 1 4238 ILE 4238 4238 4238 ILE ILE A . n 
A 1 4239 PRO 4239 4239 4239 PRO PRO A . n 
A 1 4240 TRP 4240 4240 4240 TRP TRP A . n 
A 1 4241 SER 4241 4241 4241 SER SER A . n 
A 1 4242 ALA 4242 4242 4242 ALA ALA A . n 
A 1 4243 LEU 4243 4243 4243 LEU LEU A . n 
A 1 4244 LYS 4244 4244 4244 LYS LYS A . n 
A 1 4245 THR 4245 4245 4245 THR THR A . n 
A 1 4246 LEU 4246 4246 4246 LEU LEU A . n 
A 1 4247 MET 4247 4247 4247 MET MET A . n 
A 1 4248 ALA 4248 4248 4248 ALA ALA A . n 
A 1 4249 GLN 4249 4249 4249 GLN GLN A . n 
A 1 4250 SER 4250 4250 4250 SER SER A . n 
A 1 4251 ILE 4251 4251 4251 ILE ILE A . n 
A 1 4252 TYR 4252 4252 4252 TYR TYR A . n 
A 1 4253 GLY 4253 4253 4253 GLY GLY A . n 
A 1 4254 GLY 4254 4254 4254 GLY GLY A . n 
A 1 4255 ARG 4255 4255 4255 ARG ARG A . n 
A 1 4256 VAL 4256 4256 4256 VAL VAL A . n 
A 1 4257 ASP 4257 4257 4257 ASP ASP A . n 
A 1 4258 ASN 4258 4258 4258 ASN ASN A . n 
A 1 4259 GLU 4259 4259 4259 GLU GLU A . n 
A 1 4260 PHE 4260 4260 4260 PHE PHE A . n 
A 1 4261 ASP 4261 4261 4261 ASP ASP A . n 
A 1 4262 GLN 4262 4262 4262 GLN GLN A . n 
A 1 4263 ARG 4263 4263 4263 ARG ARG A . n 
A 1 4264 LEU 4264 4264 4264 LEU LEU A . n 
A 1 4265 LEU 4265 4265 4265 LEU LEU A . n 
A 1 4266 ASN 4266 4266 4266 ASN ASN A . n 
A 1 4267 THR 4267 4267 4267 THR THR A . n 
A 1 4268 PHE 4268 4268 4268 PHE PHE A . n 
A 1 4269 LEU 4269 4269 4269 LEU LEU A . n 
A 1 4270 GLU 4270 4270 4270 GLU GLU A . n 
A 1 4271 ARG 4271 4271 4271 ARG ARG A . n 
A 1 4272 LEU 4272 4272 4272 LEU LEU A . n 
A 1 4273 PHE 4273 4273 4273 PHE PHE A . n 
A 1 4274 THR 4274 4274 4274 THR THR A . n 
A 1 4275 THR 4275 4275 4275 THR THR A . n 
A 1 4276 ARG 4276 4276 4276 ARG ARG A . n 
A 1 4277 SER 4277 4277 4277 SER SER A . n 
A 1 4278 PHE 4278 4278 4278 PHE PHE A . n 
A 1 4279 ASP 4279 4279 4279 ASP ASP A . n 
A 1 4280 SER 4280 4280 4280 SER SER A . n 
A 1 4281 GLU 4281 4281 4281 GLU GLU A . n 
A 1 4282 PHE 4282 4282 4282 PHE PHE A . n 
A 1 4283 LYS 4283 4283 4283 LYS LYS A . n 
A 1 4284 LEU 4284 4284 4284 LEU LEU A . n 
A 1 4285 ALA 4285 4285 4285 ALA ALA A . n 
A 1 4286 CYS 4286 4286 4286 CYS CYS A . n 
A 1 4287 LYS 4287 4287 4287 LYS LYS A . n 
A 1 4288 VAL 4288 4288 4288 VAL VAL A . n 
A 1 4289 ASP 4289 4289 4289 ASP ASP A . n 
A 1 4290 GLY 4290 4290 4290 GLY GLY A . n 
A 1 4291 HIS 4291 4291 4291 HIS HIS A . n 
A 1 4292 LYS 4292 4292 4292 LYS LYS A . n 
A 1 4293 ASP 4293 4293 4293 ASP ASP A . n 
A 1 4294 ILE 4294 4294 4294 ILE ILE A . n 
A 1 4295 GLN 4295 4295 4295 GLN GLN A . n 
A 1 4296 MET 4296 4296 4296 MET MET A . n 
A 1 4297 PRO 4297 4297 4297 PRO PRO A . n 
A 1 4298 ASP 4298 4298 4298 ASP ASP A . n 
A 1 4299 GLY 4299 4299 4299 GLY GLY A . n 
A 1 4300 ILE 4300 4300 4300 ILE ILE A . n 
A 1 4301 ARG 4301 4301 4301 ARG ARG A . n 
A 1 4302 ARG 4302 4302 4302 ARG ARG A . n 
A 1 4303 GLU 4303 4303 4303 GLU GLU A . n 
A 1 4304 GLU 4304 4304 4304 GLU GLU A . n 
A 1 4305 PHE 4305 4305 4305 PHE PHE A . n 
A 1 4306 VAL 4306 4306 4306 VAL VAL A . n 
A 1 4307 GLN 4307 4307 4307 GLN GLN A . n 
A 1 4308 TRP 4308 4308 4308 TRP TRP A . n 
A 1 4309 VAL 4309 4309 4309 VAL VAL A . n 
A 1 4310 GLU 4310 4310 4310 GLU GLU A . n 
A 1 4311 LEU 4311 4311 4311 LEU LEU A . n 
A 1 4312 LEU 4312 4312 4312 LEU LEU A . n 
A 1 4313 PRO 4313 4313 4313 PRO PRO A . n 
A 1 4314 ASP 4314 4314 4314 ASP ASP A . n 
A 1 4315 THR 4315 4315 4315 THR THR A . n 
A 1 4316 GLN 4316 4316 4316 GLN GLN A . n 
A 1 4317 THR 4317 4317 4317 THR THR A . n 
A 1 4318 PRO 4318 4318 4318 PRO PRO A . n 
A 1 4319 SER 4319 4319 4319 SER SER A . n 
A 1 4320 TRP 4320 4320 4320 TRP TRP A . n 
A 1 4321 LEU 4321 4321 4321 LEU LEU A . n 
A 1 4322 GLY 4322 4322 4322 GLY GLY A . n 
A 1 4323 LEU 4323 4323 4323 LEU LEU A . n 
A 1 4324 PRO 4324 4324 4324 PRO PRO A . n 
A 1 4325 ASN 4325 4325 4325 ASN ASN A . n 
A 1 4326 ASN 4326 4326 4326 ASN ASN A . n 
A 1 4327 ALA 4327 4327 4327 ALA ALA A . n 
A 1 4328 GLU 4328 4328 4328 GLU GLU A . n 
A 1 4329 ARG 4329 4329 4329 ARG ARG A . n 
A 1 4330 VAL 4330 4330 4330 VAL VAL A . n 
A 1 4331 LEU 4331 4331 4331 LEU LEU A . n 
A 1 4332 LEU 4332 4332 4332 LEU LEU A . n 
A 1 4333 THR 4333 4333 4333 THR THR A . n 
A 1 4334 THR 4334 4334 4334 THR THR A . n 
A 1 4335 GLN 4335 4335 4335 GLN GLN A . n 
A 1 4336 GLY 4336 4336 4336 GLY GLY A . n 
A 1 4337 VAL 4337 4337 4337 VAL VAL A . n 
A 1 4338 ASP 4338 4338 4338 ASP ASP A . n 
A 1 4339 MET 4339 4339 4339 MET MET A . n 
A 1 4340 ILE 4340 4340 4340 ILE ILE A . n 
A 1 4341 SER 4341 4341 4341 SER SER A . n 
A 1 4342 LYS 4342 4342 4342 LYS LYS A . n 
A 1 4343 MET 4343 4343 4343 MET MET A . n 
A 1 4344 LEU 4344 4344 4344 LEU LEU A . n 
A 1 4345 LYS 4345 4345 4345 LYS LYS A . n 
A 1 4346 MET 4346 4346 4346 MET MET A . n 
A 1 4347 GLN 4347 4347 4347 GLN GLN A . n 
A 1 4348 MET 4348 4348 ?    ?   ?   A . n 
A 1 4349 LEU 4349 4349 ?    ?   ?   A . n 
A 1 4350 GLU 4350 4350 ?    ?   ?   A . n 
A 1 4351 ASP 4351 4351 ?    ?   ?   A . n 
A 1 4352 GLU 4352 4352 ?    ?   ?   A . n 
A 1 4353 ASP 4353 4353 ?    ?   ?   A . n 
A 1 4354 ASP 4354 4354 ?    ?   ?   A . n 
A 1 4355 LEU 4355 4355 ?    ?   ?   A . n 
A 1 4356 ALA 4356 4356 ?    ?   ?   A . n 
A 1 4357 TYR 4357 4357 ?    ?   ?   A . n 
A 1 4358 ALA 4358 4358 ?    ?   ?   A . n 
A 1 4359 GLU 4359 4359 ?    ?   ?   A . n 
A 1 4360 THR 4360 4360 ?    ?   ?   A . n 
A 1 4361 GLU 4361 4361 ?    ?   ?   A . n 
A 1 4362 LYS 4362 4362 ?    ?   ?   A . n 
A 1 4363 LYS 4363 4363 ?    ?   ?   A . n 
A 1 4364 THR 4364 4364 ?    ?   ?   A . n 
A 1 4365 ARG 4365 4365 ?    ?   ?   A . n 
A 1 4366 THR 4366 4366 ?    ?   ?   A . n 
A 1 4367 ASP 4367 4367 ?    ?   ?   A . n 
A 1 4368 SER 4368 4368 ?    ?   ?   A . n 
A 1 4369 THR 4369 4369 ?    ?   ?   A . n 
A 1 4370 SER 4370 4370 ?    ?   ?   A . n 
A 1 4371 ASP 4371 4371 ?    ?   ?   A . n 
A 1 4372 GLY 4372 4372 ?    ?   ?   A . n 
A 1 4373 ARG 4373 4373 ?    ?   ?   A . n 
A 1 4374 PRO 4374 4374 4374 PRO PRO A . n 
A 1 4375 ALA 4375 4375 4375 ALA ALA A . n 
A 1 4376 TRP 4376 4376 4376 TRP TRP A . n 
A 1 4377 MET 4377 4377 4377 MET MET A . n 
A 1 4378 ARG 4378 4378 4378 ARG ARG A . n 
A 1 4379 THR 4379 4379 4379 THR THR A . n 
A 1 4380 LEU 4380 4380 4380 LEU LEU A . n 
A 1 4381 HIS 4381 4381 4381 HIS HIS A . n 
A 1 4382 THR 4382 4382 4382 THR THR A . n 
A 1 4383 THR 4383 4383 4383 THR THR A . n 
A 1 4384 ALA 4384 4384 4384 ALA ALA A . n 
A 1 4385 SER 4385 4385 4385 SER SER A . n 
A 1 4386 ASN 4386 4386 4386 ASN ASN A . n 
A 1 4387 TRP 4387 4387 4387 TRP TRP A . n 
A 1 4388 LEU 4388 4388 4388 LEU LEU A . n 
A 1 4389 HIS 4389 4389 4389 HIS HIS A . n 
A 1 4390 LEU 4390 4390 4390 LEU LEU A . n 
A 1 4391 ILE 4391 4391 4391 ILE ILE A . n 
A 1 4392 PRO 4392 4392 4392 PRO PRO A . n 
A 1 4393 GLN 4393 4393 4393 GLN GLN A . n 
A 1 4394 THR 4394 4394 4394 THR THR A . n 
A 1 4395 LEU 4395 4395 4395 LEU LEU A . n 
A 1 4396 SER 4396 4396 4396 SER SER A . n 
A 1 4397 HIS 4397 4397 4397 HIS HIS A . n 
A 1 4398 LEU 4398 4398 4398 LEU LEU A . n 
A 1 4399 LYS 4399 4399 4399 LYS LYS A . n 
A 1 4400 ARG 4400 4400 4400 ARG ARG A . n 
A 1 4401 THR 4401 4401 4401 THR THR A . n 
A 1 4402 VAL 4402 4402 4402 VAL VAL A . n 
A 1 4403 GLU 4403 4403 4403 GLU GLU A . n 
A 1 4404 ASN 4404 4404 4404 ASN ASN A . n 
A 1 4405 ILE 4405 4405 4405 ILE ILE A . n 
A 1 4406 LYS 4406 4406 4406 LYS LYS A . n 
A 1 4407 ASP 4407 4407 4407 ASP ASP A . n 
A 1 4408 PRO 4408 4408 4408 PRO PRO A . n 
A 1 4409 LEU 4409 4409 4409 LEU LEU A . n 
A 1 4410 PHE 4410 4410 4410 PHE PHE A . n 
A 1 4411 ARG 4411 4411 4411 ARG ARG A . n 
A 1 4412 PHE 4412 4412 4412 PHE PHE A . n 
A 1 4413 PHE 4413 4413 4413 PHE PHE A . n 
A 1 4414 GLU 4414 4414 4414 GLU GLU A . n 
A 1 4415 ARG 4415 4415 4415 ARG ARG A . n 
A 1 4416 GLU 4416 4416 4416 GLU GLU A . n 
A 1 4417 VAL 4417 4417 4417 VAL VAL A . n 
A 1 4418 LYS 4418 4418 4418 LYS LYS A . n 
A 1 4419 MET 4419 4419 4419 MET MET A . n 
A 1 4420 GLY 4420 4420 4420 GLY GLY A . n 
A 1 4421 ALA 4421 4421 4421 ALA ALA A . n 
A 1 4422 LYS 4422 4422 4422 LYS LYS A . n 
A 1 4423 LEU 4423 4423 4423 LEU LEU A . n 
A 1 4424 LEU 4424 4424 4424 LEU LEU A . n 
A 1 4425 GLN 4425 4425 4425 GLN GLN A . n 
A 1 4426 ASP 4426 4426 4426 ASP ASP A . n 
A 1 4427 VAL 4427 4427 4427 VAL VAL A . n 
A 1 4428 ARG 4428 4428 4428 ARG ARG A . n 
A 1 4429 GLN 4429 4429 4429 GLN GLN A . n 
A 1 4430 ASP 4430 4430 4430 ASP ASP A . n 
A 1 4431 LEU 4431 4431 4431 LEU LEU A . n 
A 1 4432 ALA 4432 4432 4432 ALA ALA A . n 
A 1 4433 ASP 4433 4433 4433 ASP ASP A . n 
A 1 4434 VAL 4434 4434 4434 VAL VAL A . n 
A 1 4435 VAL 4435 4435 4435 VAL VAL A . n 
A 1 4436 GLN 4436 4436 4436 GLN GLN A . n 
A 1 4437 VAL 4437 4437 4437 VAL VAL A . n 
A 1 4438 CYS 4438 4438 4438 CYS CYS A . n 
A 1 4439 GLU 4439 4439 4439 GLU GLU A . n 
A 1 4440 GLY 4440 4440 4440 GLY GLY A . n 
A 1 4441 LYS 4441 4441 4441 LYS LYS A . n 
A 1 4442 LYS 4442 4442 4442 LYS LYS A . n 
A 1 4443 LYS 4443 4443 4443 LYS LYS A . n 
A 1 4444 GLN 4444 4444 4444 GLN GLN A . n 
A 1 4445 THR 4445 4445 4445 THR THR A . n 
A 1 4446 ASN 4446 4446 4446 ASN ASN A . n 
A 1 4447 TYR 4447 4447 4447 TYR TYR A . n 
A 1 4448 LEU 4448 4448 4448 LEU LEU A . n 
A 1 4449 ARG 4449 4449 4449 ARG ARG A . n 
A 1 4450 THR 4450 4450 4450 THR THR A . n 
A 1 4451 LEU 4451 4451 4451 LEU LEU A . n 
A 1 4452 ILE 4452 4452 4452 ILE ILE A . n 
A 1 4453 ASN 4453 4453 4453 ASN ASN A . n 
A 1 4454 GLU 4454 4454 4454 GLU GLU A . n 
A 1 4455 LEU 4455 4455 4455 LEU LEU A . n 
A 1 4456 VAL 4456 4456 4456 VAL VAL A . n 
A 1 4457 LYS 4457 4457 4457 LYS LYS A . n 
A 1 4458 GLY 4458 4458 4458 GLY GLY A . n 
A 1 4459 ILE 4459 4459 4459 ILE ILE A . n 
A 1 4460 LEU 4460 4460 4460 LEU LEU A . n 
A 1 4461 PRO 4461 4461 4461 PRO PRO A . n 
A 1 4462 ARG 4462 4462 4462 ARG ARG A . n 
A 1 4463 SER 4463 4463 4463 SER SER A . n 
A 1 4464 TRP 4464 4464 4464 TRP TRP A . n 
A 1 4465 SER 4465 4465 4465 SER SER A . n 
A 1 4466 HIS 4466 4466 4466 HIS HIS A . n 
A 1 4467 TYR 4467 4467 4467 TYR TYR A . n 
A 1 4468 THR 4468 4468 4468 THR THR A . n 
A 1 4469 VAL 4469 4469 4469 VAL VAL A . n 
A 1 4470 PRO 4470 4470 4470 PRO PRO A . n 
A 1 4471 ALA 4471 4471 4471 ALA ALA A . n 
A 1 4472 GLY 4472 4472 4472 GLY GLY A . n 
A 1 4473 MET 4473 4473 4473 MET MET A . n 
A 1 4474 THR 4474 4474 4474 THR THR A . n 
A 1 4475 VAL 4475 4475 4475 VAL VAL A . n 
A 1 4476 ILE 4476 4476 4476 ILE ILE A . n 
A 1 4477 GLN 4477 4477 4477 GLN GLN A . n 
A 1 4478 TRP 4478 4478 4478 TRP TRP A . n 
A 1 4479 VAL 4479 4479 4479 VAL VAL A . n 
A 1 4480 SER 4480 4480 4480 SER SER A . n 
A 1 4481 ASP 4481 4481 4481 ASP ASP A . n 
A 1 4482 PHE 4482 4482 4482 PHE PHE A . n 
A 1 4483 SER 4483 4483 4483 SER SER A . n 
A 1 4484 GLU 4484 4484 4484 GLU GLU A . n 
A 1 4485 ARG 4485 4485 4485 ARG ARG A . n 
A 1 4486 ILE 4486 4486 4486 ILE ILE A . n 
A 1 4487 LYS 4487 4487 4487 LYS LYS A . n 
A 1 4488 GLN 4488 4488 4488 GLN GLN A . n 
A 1 4489 LEU 4489 4489 4489 LEU LEU A . n 
A 1 4490 GLN 4490 4490 4490 GLN GLN A . n 
A 1 4491 ASN 4491 4491 4491 ASN ASN A . n 
A 1 4492 ILE 4492 4492 4492 ILE ILE A . n 
A 1 4493 SER 4493 4493 4493 SER SER A . n 
A 1 4494 LEU 4494 4494 4494 LEU LEU A . n 
A 1 4495 ALA 4495 4495 4495 ALA ALA A . n 
A 1 4496 ALA 4496 4496 4496 ALA ALA A . n 
A 1 4497 ALA 4497 4497 4497 ALA ALA A . n 
A 1 4498 SER 4498 4498 4498 SER SER A . n 
A 1 4499 GLY 4499 4499 4499 GLY GLY A . n 
A 1 4500 GLY 4500 4500 4500 GLY GLY A . n 
A 1 4501 ALA 4501 4501 4501 ALA ALA A . n 
A 1 4502 LYS 4502 4502 4502 LYS LYS A . n 
A 1 4503 GLU 4503 4503 4503 GLU GLU A . n 
A 1 4504 LEU 4504 4504 4504 LEU LEU A . n 
A 1 4505 LYS 4505 4505 4505 LYS LYS A . n 
A 1 4506 ASN 4506 4506 4506 ASN ASN A . n 
A 1 4507 ILE 4507 4507 4507 ILE ILE A . n 
A 1 4508 HIS 4508 4508 4508 HIS HIS A . n 
A 1 4509 VAL 4509 4509 4509 VAL VAL A . n 
A 1 4510 CYS 4510 4510 4510 CYS CYS A . n 
A 1 4511 LEU 4511 4511 4511 LEU LEU A . n 
A 1 4512 GLY 4512 4512 4512 GLY GLY A . n 
A 1 4513 GLY 4513 4513 4513 GLY GLY A . n 
A 1 4514 LEU 4514 4514 4514 LEU LEU A . n 
A 1 4515 PHE 4515 4515 4515 PHE PHE A . n 
A 1 4516 VAL 4516 4516 4516 VAL VAL A . n 
A 1 4517 PRO 4517 4517 4517 PRO PRO A . n 
A 1 4518 GLU 4518 4518 4518 GLU GLU A . n 
A 1 4519 ALA 4519 4519 4519 ALA ALA A . n 
A 1 4520 TYR 4520 4520 4520 TYR TYR A . n 
A 1 4521 ILE 4521 4521 4521 ILE ILE A . n 
A 1 4522 THR 4522 4522 4522 THR THR A . n 
A 1 4523 ALA 4523 4523 4523 ALA ALA A . n 
A 1 4524 THR 4524 4524 4524 THR THR A . n 
A 1 4525 ARG 4525 4525 4525 ARG ARG A . n 
A 1 4526 GLN 4526 4526 4526 GLN GLN A . n 
A 1 4527 TYR 4527 4527 4527 TYR TYR A . n 
A 1 4528 VAL 4528 4528 4528 VAL VAL A . n 
A 1 4529 ALA 4529 4529 4529 ALA ALA A . n 
A 1 4530 GLN 4530 4530 4530 GLN GLN A . n 
A 1 4531 ALA 4531 4531 4531 ALA ALA A . n 
A 1 4532 ASN 4532 4532 4532 ASN ASN A . n 
A 1 4533 SER 4533 4533 4533 SER SER A . n 
A 1 4534 TRP 4534 4534 4534 TRP TRP A . n 
A 1 4535 SER 4535 4535 4535 SER SER A . n 
A 1 4536 LEU 4536 4536 4536 LEU LEU A . n 
A 1 4537 GLU 4537 4537 4537 GLU GLU A . n 
A 1 4538 GLU 4538 4538 4538 GLU GLU A . n 
A 1 4539 LEU 4539 4539 4539 LEU LEU A . n 
A 1 4540 CYS 4540 4540 4540 CYS CYS A . n 
A 1 4541 LEU 4541 4541 4541 LEU LEU A . n 
A 1 4542 GLU 4542 4542 4542 GLU GLU A . n 
A 1 4543 VAL 4543 4543 4543 VAL VAL A . n 
A 1 4544 ASN 4544 4544 4544 ASN ASN A . n 
A 1 4545 VAL 4545 4545 4545 VAL VAL A . n 
A 1 4546 THR 4546 4546 4546 THR THR A . n 
A 1 4547 THR 4547 4547 4547 THR THR A . n 
A 1 4548 SER 4548 4548 4548 SER SER A . n 
A 1 4549 GLN 4549 4549 4549 GLN GLN A . n 
A 1 4550 GLY 4550 4550 4550 GLY GLY A . n 
A 1 4551 ALA 4551 4551 4551 ALA ALA A . n 
A 1 4552 THR 4552 4552 4552 THR THR A . n 
A 1 4553 LEU 4553 4553 4553 LEU LEU A . n 
A 1 4554 ASP 4554 4554 4554 ASP ASP A . n 
A 1 4555 ALA 4555 4555 4555 ALA ALA A . n 
A 1 4556 CYS 4556 4556 4556 CYS CYS A . n 
A 1 4557 SER 4557 4557 4557 SER SER A . n 
A 1 4558 PHE 4558 4558 4558 PHE PHE A . n 
A 1 4559 GLY 4559 4559 4559 GLY GLY A . n 
A 1 4560 VAL 4560 4560 4560 VAL VAL A . n 
A 1 4561 THR 4561 4561 4561 THR THR A . n 
A 1 4562 GLY 4562 4562 4562 GLY GLY A . n 
A 1 4563 LEU 4563 4563 4563 LEU LEU A . n 
A 1 4564 LYS 4564 4564 4564 LYS LYS A . n 
A 1 4565 LEU 4565 4565 4565 LEU LEU A . n 
A 1 4566 GLN 4566 4566 4566 GLN GLN A . n 
A 1 4567 GLY 4567 4567 4567 GLY GLY A . n 
A 1 4568 ALA 4568 4568 4568 ALA ALA A . n 
A 1 4569 THR 4569 4569 4569 THR THR A . n 
A 1 4570 CYS 4570 4570 4570 CYS CYS A . n 
A 1 4571 ASN 4571 4571 4571 ASN ASN A . n 
A 1 4572 ASN 4572 4572 4572 ASN ASN A . n 
A 1 4573 ASN 4573 4573 4573 ASN ASN A . n 
A 1 4574 LYS 4574 4574 4574 LYS LYS A . n 
A 1 4575 LEU 4575 4575 4575 LEU LEU A . n 
A 1 4576 SER 4576 4576 4576 SER SER A . n 
A 1 4577 LEU 4577 4577 4577 LEU LEU A . n 
A 1 4578 SER 4578 4578 4578 SER SER A . n 
A 1 4579 ASN 4579 4579 4579 ASN ASN A . n 
A 1 4580 ALA 4580 4580 4580 ALA ALA A . n 
A 1 4581 ILE 4581 4581 4581 ILE ILE A . n 
A 1 4582 SER 4582 4582 4582 SER SER A . n 
A 1 4583 THR 4583 4583 4583 THR THR A . n 
A 1 4584 ALA 4584 4584 4584 ALA ALA A . n 
A 1 4585 LEU 4585 4585 4585 LEU LEU A . n 
A 1 4586 PRO 4586 4586 4586 PRO PRO A . n 
A 1 4587 LEU 4587 4587 4587 LEU LEU A . n 
A 1 4588 THR 4588 4588 4588 THR THR A . n 
A 1 4589 GLN 4589 4589 4589 GLN GLN A . n 
A 1 4590 LEU 4590 4590 4590 LEU LEU A . n 
A 1 4591 ARG 4591 4591 4591 ARG ARG A . n 
A 1 4592 TRP 4592 4592 4592 TRP TRP A . n 
A 1 4593 VAL 4593 4593 4593 VAL VAL A . n 
A 1 4594 LYS 4594 4594 4594 LYS LYS A . n 
A 1 4595 GLN 4595 4595 4595 GLN GLN A . n 
A 1 4596 THR 4596 4596 4596 THR THR A . n 
A 1 4597 ASN 4597 4597 4597 ASN ASN A . n 
A 1 4598 THR 4598 4598 4598 THR THR A . n 
A 1 4599 GLU 4599 4599 4599 GLU GLU A . n 
A 1 4600 LYS 4600 4600 4600 LYS LYS A . n 
A 1 4601 LYS 4601 4601 4601 LYS LYS A . n 
A 1 4602 ALA 4602 4602 4602 ALA ALA A . n 
A 1 4603 SER 4603 4603 4603 SER SER A . n 
A 1 4604 VAL 4604 4604 4604 VAL VAL A . n 
A 1 4605 VAL 4605 4605 4605 VAL VAL A . n 
A 1 4606 THR 4606 4606 4606 THR THR A . n 
A 1 4607 LEU 4607 4607 4607 LEU LEU A . n 
A 1 4608 PRO 4608 4608 4608 PRO PRO A . n 
A 1 4609 VAL 4609 4609 4609 VAL VAL A . n 
A 1 4610 TYR 4610 4610 4610 TYR TYR A . n 
A 1 4611 LEU 4611 4611 4611 LEU LEU A . n 
A 1 4612 ASN 4612 4612 4612 ASN ASN A . n 
A 1 4613 PHE 4613 4613 4613 PHE PHE A . n 
A 1 4614 THR 4614 4614 4614 THR THR A . n 
A 1 4615 ARG 4615 4615 4615 ARG ARG A . n 
A 1 4616 ALA 4616 4616 4616 ALA ALA A . n 
A 1 4617 ASP 4617 4617 4617 ASP ASP A . n 
A 1 4618 LEU 4618 4618 4618 LEU LEU A . n 
A 1 4619 ILE 4619 4619 4619 ILE ILE A . n 
A 1 4620 PHE 4620 4620 4620 PHE PHE A . n 
A 1 4621 THR 4621 4621 4621 THR THR A . n 
A 1 4622 VAL 4622 4622 4622 VAL VAL A . n 
A 1 4623 ASP 4623 4623 4623 ASP ASP A . n 
A 1 4624 PHE 4624 4624 4624 PHE PHE A . n 
A 1 4625 GLU 4625 4625 4625 GLU GLU A . n 
A 1 4626 ILE 4626 4626 4626 ILE ILE A . n 
A 1 4627 ALA 4627 4627 4627 ALA ALA A . n 
A 1 4628 THR 4628 4628 4628 THR THR A . n 
A 1 4629 LYS 4629 4629 4629 LYS LYS A . n 
A 1 4630 GLU 4630 4630 4630 GLU GLU A . n 
A 1 4631 ASP 4631 4631 4631 ASP ASP A . n 
A 1 4632 PRO 4632 4632 4632 PRO PRO A . n 
A 1 4633 ARG 4633 4633 4633 ARG ARG A . n 
A 1 4634 SER 4634 4634 4634 SER SER A . n 
A 1 4635 PHE 4635 4635 4635 PHE PHE A . n 
A 1 4636 TYR 4636 4636 4636 TYR TYR A . n 
A 1 4637 GLU 4637 4637 4637 GLU GLU A . n 
A 1 4638 ARG 4638 4638 4638 ARG ARG A . n 
A 1 4639 GLY 4639 4639 4639 GLY GLY A . n 
A 1 4640 VAL 4640 4640 4640 VAL VAL A . n 
A 1 4641 ALA 4641 4641 4641 ALA ALA A . n 
A 1 4642 VAL 4642 4642 4642 VAL VAL A . n 
A 1 4643 LEU 4643 4643 4643 LEU LEU A . n 
A 1 4644 CYS 4644 4644 4644 CYS CYS A . n 
A 1 4645 THR 4645 4645 4645 THR THR A . n 
A 1 4646 GLU 4646 4646 ?    ?   ?   A . n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 ADP ? ? ADP ? ? 'SUBJECT OF INVESTIGATION' ? 
2 ATP ? ? ATP ? ? 'SUBJECT OF INVESTIGATION' ? 
3 MG  ? ? MG  ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 ADP 1 4701 4701 ADP ADP A . 
C 3 ATP 1 4702 4702 ATP ATP A . 
D 2 ADP 1 4703 4703 ADP ADP A . 
E 2 ADP 1 4704 4704 ADP ADP A . 
F 4 MG  1 4705 4705 MG  MG  A . 
G 4 MG  1 4706 4706 MG  MG  A . 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9BMY 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_struct.entry_id                     9BMY 
_struct.title                        'State-1 of motor domain from full-length human dynein-1 in apo condition' 
_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        9BMY 
_struct_keywords.text            'dynein-1, MOTOR PROTEIN' 
_struct_keywords.pdbx_keywords   'MOTOR PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 2 ? 
E N N 2 ? 
F N N 4 ? 
G N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    DYHC1_HUMAN 
_struct_ref.pdbx_db_accession          Q14204 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MSEPGGGGGEDGSAGLEVSAVQNVADVSVLQKHLRKLVPLLLEDGGEAPAALEAALEEKSALEQMRKFLSDPQVHTVLVE
RSTLKEDVGDEGEEEKEFISYNINIDIHYGVKSNSLAFIKRTPVIDADKPVSSQLRVLTLSEDSPYETLHSFISNAVAPF
FKSYIRESGKADRDGDKMAPSVEKKIAELEMGLLHLQQNIEIPEISLPIHPMITNVAKQCYERGEKPKVTDFGDKVEDPT
FLNQLQSGVNRWIREIQKVTKLDRDPASGTALQEISFWLNLERALYRIQEKRESPEVLLTLDILKHGKRFHATVSFDTDT
GLKQALETVNDYNPLMKDFPLNDLLSATELDKIRQALVAIFTHLRKIRNTKYPIQRALRLVEAISRDLSSQLLKVLGTRK
LMHVAYEEFEKVMVACFEVFQTWDDEYEKLQVLLRDIVKRKREENLKMVWRINPAHRKLQARLDQMRKFRRQHEQLRAVI
VRVLRPQVTAVAQQNQGEVPEPQDMKVAEVLFDAADANAIEEVNLAYENVKEVDGLDVSKEGTEAWEAAMKRYDERIDRV
ETRITARLRDQLGTAKNANEMFRIFSRFNALFVRPHIRGAIREYQTQLIQRVKDDIESLHDKFKVQYPQSQACKMSHVRD
LPPVSGSIIWAKQIDRQLTAYMKRVEDVLGKGWENHVEGQKLKQDGDSFRMKLNTQEIFDDWARKVQQRNLGVSGRIFTI
ESTRVRGRTGNVLKLKVNFLPEIITLSKEVRNLKWLGFRVPLAIVNKAHQANQLYPFAISLIESVRTYERTCEKVEERNT
ISLLVAGLKKEVQALIAEGIALVWESYKLDPYVQRLAETVFNFQEKVDDLLIIEEKIDLEVRSLETCMYDHKTFSEILNR
VQKAVDDLNLHSYSNLPIWVNKLDMEIERILGVRLQAGLRAWTQVLLGQAEDKAEVDMDTDAPQVSHKPGGEPKIKNVVH
ELRITNQVIYLNPPIEECRYKLYQEMFAWKMVVLSLPRIQSQRYQVGVHYELTEEEKFYRNALTRMPDGPVALEESYSAV
MGIVSEVEQYVKVWLQYQCLWDMQAENIYNRLGEDLNKWQALLVQIRKARGTFDNAETKKEFGPVVIDYGKVQSKVNLKY
DSWHKEVLSKFGQMLGSNMTEFHSQISKSRQELEQHSVDTASTSDAVTFITYVQSLKRKIKQFEKQVELYRNGQRLLEKQ
RFQFPPSWLYIDNIEGEWGAFNDIMRRKDSAIQQQVANLQMKIVQEDRAVESRTTDLLTDWEKTKPVTGNLRPEEALQAL
TIYEGKFGRLKDDREKCAKAKEALELTDTGLLSGSEERVQVALEELQDLKGVWSELSKVWEQIDQMKEQPWVSVQPRKLR
QNLDALLNQLKSFPARLRQYASYEFVQRLLKGYMKINMLVIELKSEALKDRHWKQLMKRLHVNWVVSELTLGQIWDVDLQ
KNEAIVKDVLLVAQGEMALEEFLKQIREVWNTYELDLVNYQNKCRLIRGWDDLFNKVKEHINSVSAMKLSPYYKVFEEDA
LSWEDKLNRIMALFDVWIDVQRRWVYLEGIFTGSADIKHLLPVETQRFQSISTEFLALMKKVSKSPLVMDVLNIQGVQRS
LERLADLLGKIQKALGEYLERERSSFPRFYFVGDEDLLEIIGNSKNVAKLQKHFKKMFAGVSSIILNEDNSVVLGISSRE
GEEVMFKTPVSITEHPKINEWLTLVEKEMRVTLAKLLAESVTEVEIFGKATSIDPNTYITWIDKYQAQLVVLSAQIAWSE
NVETALSSMGGGGDAAPLHSVLSNVEVTLNVLADSVLMEQPPLRRRKLEHLITELVHQRDVTRSLIKSKIDNAKSFEWLS
QMRFYFDPKQTDVLQQLSIQMANAKFNYGFEYLGVQDKLVQTPLTDRCYLTMTQALEARLGGSPFGPAGTGKTESVKALG
HQLGRFVLVFNCDETFDFQAMGRIFVGLCQVGAWGCFDEFNRLEERMLSAVSQQVQCIQEALREHSNPNYDKTSAPITCE
LLNKQVKVSPDMAIFITMNPGYAGRSNLPDNLKKLFRSLAMTKPDRQLIAQVMLYSQGFRTAEVLANKIVPFFKLCDEQL
SSQSHYDFGLRALKSVLVSAGNVKRERIQKIKREKEERGEAVDEGEIAENLPEQEILIQSVCETMVPKLVAEDIPLLFSL
LSDVFPGVQYHRGEMTALREELKKVCQEMYLTYGDGEEVGGMWVEKVLQLYQITQINHGLMMVGPSGSGKSMAWRVLLKA
LERLEGVEGVAHIIDPKAISKDHLYGTLDPNTREWTDGLFTHVLRKIIDSVRGELQKRQWIVFDGDVDPEWVENLNSVLD
DNKLLTLPNGERLSLPPNVRIMFEVQDLKYATLATVSRCGMVWFSEDVLSTDMIFNNFLARLRSIPLDEGEDEAQRRRKG
KEDEGEEAASPMLQIQRDAATIMQPYFTSNGLVTKALEHAFQLEHIMDLTRLRCLGSLFSMLHQACRNVAQYNANHPDFP
MQIEQLERYIQRYLVYAILWSLSGDSRLKMRAELGEYIRRITTVPLPTAPNIPIIDYEVSISGEWSPWQAKVPQIEVETH
KVAAPDVVVPTLDTVRHEALLYTWLAEHKPLVLCGPPGSGKTMTLFSALRALPDMEVVGLNFSSATTPELLLKTFDHYCE
YRRTPNGVVLAPVQLGKWLVLFCDEINLPDMDKYGTQRVISFIRQMVEHGGFYRTSDQTWVKLERIQFVGACNPPTDPGR
KPLSHRFLRHVPVVYVDYPGPASLTQIYGTFNRAMLRLIPSLRTYAEPLTAAMVEFYTMSQERFTQDTQPHYIYSPREMT
RWVRGIFEALRPLETLPVEGLIRIWAHEALRLFQDRLVEDEERRWTDENIDTVALKHFPNIDREKAMSRPILYSNWLSKD
YIPVDQEELRDYVKARLKVFYEEELDVPLVLFNEVLDHVLRIDRIFRQPQGHLLLIGVSGAGKTTLSRFVAWMNGLSVYQ
IKVHRKYTGEDFDEDLRTVLRRSGCKNEKIAFIMDESNVLDSGFLERMNTLLANGEVPGLFEGDEYATLMTQCKEGAQKE
GLMLDSHEELYKWFTSQVIRNLHVVFTMNPSSEGLKDRAATSPALFNRCVLNWFGDWSTEALYQVGKEFTSKMDLEKPNY
IVPDYMPVVYDKLPQPPSHREAIVNSCVFVHQTLHQANARLAKRGGRTMAITPRHYLDFINHYANLFHEKRSELEEQQMH
LNVGLRKIKETVDQVEELRRDLRIKSQELEVKNAAANDKLKKMVKDQQEAEKKKVMSQEIQEQLHKQQEVIADKQMSVKE
DLDKVEPAVIEAQNAVKSIKKQHLVEVRSMANPPAAVKLALESICLLLGESTTDWKQIRSIIMRENFIPTIVNFSAEEIS
DAIREKMKKNYMSNPSYNYEIVNRASLACGPMVKWAIAQLNYADMLKRVEPLRNELQKLEDDAKDNQQKANEVEQMIRDL
EASIARYKEEYAVLISEAQAIKADLAAVEAKVNRSTALLKSLSAERERWEKTSETFKNQMSTIAGDCLLSAAFIAYAGYF
DQQMRQNLFTTWSHHLQQANIQFRTDIARTEYLSNADERLRWQASSLPADDLCTENAIMLKRFNRYPLIIDPSGQATEFI
MNEYKDRKITRTSFLDDAFRKNLESALRFGNPLLVQDVESYDPVLNPVLNREVRRTGGRVLITLGDQDIDLSPSFVIFLS
TRDPTVEFPPDLCSRVTFVNFTVTRSSLQSQCLNEVLKAERPDVDEKRSDLLKLQGEFQLRLRQLEKSLLQALNEVKGRI
LDDDTIITTLENLKREAAEVTRKVEETDIVMQEVETVSQQYLPLSTACSSIYFTMESLKQIHFLYQYSLQFFLDIYHNVL
YENPNLKGVTDHTQRLSIITKDLFQVAFNRVARGMLHQDHITFAMLLARIKLKGTVGEPTYDAEFQHFLRGNEIVLSAGS
TPRIQGLTVEQAEAVVRLSCLPAFKDLIAKVQADEQFGIWLDSSSPEQTVPYLWSEETPATPIGQAIHRLLLIQAFRPDR
LLAMAHMFVSTNLGESFMSIMEQPLDLTHIVGTEVKPNTPVLMCSVPGYDASGHVEDLAAEQNTQITSIAIGSAEGFNQA
DKAINTAVKSGRWVMLKNVHLAPGWLMQLEKKLHSLQPHACFRLFLTMEINPKVPVNLLRAGRIFVFEPPPGVKANMLRT
FSSIPVSRICKSPNERARLYFLLAWFHAIIQERLRYAPLGWSKKYEFGESDLRSACDTVDTWLDDTAKGRQNISPDKIPW
SALKTLMAQSIYGGRVDNEFDQRLLNTFLERLFTTRSFDSEFKLACKVDGHKDIQMPDGIRREEFVQWVELLPDTQTPSW
LGLPNNAERVLLTTQGVDMISKMLKMQMLEDEDDLAYAETEKKTRTDSTSDGRPAWMRTLHTTASNWLHLIPQTLSHLKR
TVENIKDPLFRFFEREVKMGAKLLQDVRQDLADVVQVCEGKKKQTNYLRTLINELVKGILPRSWSHYTVPAGMTVIQWVS
DFSERIKQLQNISLAAASGGAKELKNIHVCLGGLFVPEAYITATRQYVAQANSWSLEELCLEVNVTTSQGATLDACSFGV
TGLKLQGATCNNNKLSLSNAISTALPLTQLRWVKQTNTEKKASVVTLPVYLNFTRADLIFTVDFEIATKEDPRSFYERGV
AVLCTE
;
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9BMY 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 4646 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q14204 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  4646 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       4646 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'electron microscopy' 
_pdbx_struct_assembly_auth_evidence.details                'not applicable' 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   ? 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1   AA1 MET A 1457 ? ASN A 1471 ? MET A 1457 ASN A 1471 1 ? 15 
HELX_P HELX_P2   AA2 GLY A 1489 ? LEU A 1509 ? GLY A 1489 LEU A 1509 1 ? 21 
HELX_P HELX_P3   AA3 SER A 1510 ? LYS A 1514 ? SER A 1510 LYS A 1514 5 ? 5  
HELX_P HELX_P4   AA4 PHE A 1516 ? SER A 1554 ? PHE A 1516 SER A 1554 1 ? 39 
HELX_P HELX_P5   AA5 ALA A 1555 ? LEU A 1561 ? ALA A 1555 LEU A 1561 1 ? 7  
HELX_P HELX_P6   AA6 LEU A 1561 ? SER A 1585 ? LEU A 1561 SER A 1585 1 ? 25 
HELX_P HELX_P7   AA7 LEU A 1587 ? ASN A 1593 ? LEU A 1587 ASN A 1593 1 ? 7  
HELX_P HELX_P8   AA8 GLY A 1596 ? ALA A 1614 ? GLY A 1596 ALA A 1614 1 ? 19 
HELX_P HELX_P9   AA9 LEU A 1615 ? PHE A 1626 ? LEU A 1615 PHE A 1626 1 ? 12 
HELX_P HELX_P10  AB1 PRO A 1627 ? VAL A 1632 ? PRO A 1627 VAL A 1632 5 ? 6  
HELX_P HELX_P11  AB2 GLY A 1633 ? ASN A 1643 ? GLY A 1633 ASN A 1643 1 ? 11 
HELX_P HELX_P12  AB3 ASN A 1646 ? LYS A 1652 ? ASN A 1646 LYS A 1652 5 ? 7  
HELX_P HELX_P13  AB4 HIS A 1653 ? PHE A 1658 ? HIS A 1653 PHE A 1658 1 ? 6  
HELX_P HELX_P14  AB5 LYS A 1697 ? GLY A 1728 ? LYS A 1697 GLY A 1728 1 ? 32 
HELX_P HELX_P15  AB6 ASP A 1734 ? TYR A 1745 ? ASP A 1734 TYR A 1745 1 ? 12 
HELX_P HELX_P16  AB7 GLN A 1746 ? MET A 1769 ? GLN A 1746 MET A 1769 1 ? 24 
HELX_P HELX_P17  AB8 GLY A 1770 ? GLY A 1772 ? GLY A 1770 GLY A 1772 5 ? 3  
HELX_P HELX_P18  AB9 PRO A 1777 ? LEU A 1797 ? PRO A 1777 LEU A 1797 1 ? 21 
HELX_P HELX_P19  AC1 PRO A 1801 ? SER A 1828 ? PRO A 1801 SER A 1828 1 ? 28 
HELX_P HELX_P20  AC2 SER A 1835 ? SER A 1840 ? SER A 1835 SER A 1840 1 ? 6  
HELX_P HELX_P21  AC3 ASP A 1852 ? GLN A 1855 ? ASP A 1852 GLN A 1855 5 ? 4  
HELX_P HELX_P22  AC4 THR A 1882 ? ALA A 1898 ? THR A 1882 ALA A 1898 1 ? 17 
HELX_P HELX_P23  AC5 GLY A 1911 ? LEU A 1923 ? GLY A 1911 LEU A 1923 1 ? 13 
HELX_P HELX_P24  AC6 ASP A 1937 ? GLY A 1952 ? ASP A 1937 GLY A 1952 1 ? 16 
HELX_P HELX_P25  AC7 PHE A 1960 ? LEU A 1963 ? PHE A 1960 LEU A 1963 5 ? 4  
HELX_P HELX_P26  AC8 GLU A 1964 ? ASN A 1987 ? GLU A 1964 ASN A 1987 1 ? 24 
HELX_P HELX_P27  AC9 PRO A 2029 ? LYS A 2034 ? PRO A 2029 LYS A 2034 1 ? 6  
HELX_P HELX_P28  AD1 ASP A 2045 ? GLY A 2058 ? ASP A 2045 GLY A 2058 1 ? 14 
HELX_P HELX_P29  AD2 THR A 2061 ? LEU A 2080 ? THR A 2061 LEU A 2080 1 ? 20 
HELX_P HELX_P30  AD3 GLY A 2089 ? GLU A 2117 ? GLY A 2089 GLU A 2117 1 ? 29 
HELX_P HELX_P31  AD4 ASP A 2123 ? ASN A 2130 ? ASP A 2123 ASN A 2130 1 ? 8  
HELX_P HELX_P32  AD5 PRO A 2132 ? VAL A 2146 ? PRO A 2132 VAL A 2146 1 ? 15 
HELX_P HELX_P33  AD6 PRO A 2147 ? LEU A 2149 ? PRO A 2147 LEU A 2149 5 ? 3  
HELX_P HELX_P34  AD7 VAL A 2150 ? GLU A 2152 ? VAL A 2150 GLU A 2152 5 ? 3  
HELX_P HELX_P35  AD8 ASP A 2153 ? PHE A 2165 ? ASP A 2153 PHE A 2165 1 ? 13 
HELX_P HELX_P36  AD9 MET A 2175 ? MET A 2189 ? MET A 2175 MET A 2189 1 ? 15 
HELX_P HELX_P37  AE1 GLY A 2200 ? GLN A 2215 ? GLY A 2200 GLN A 2215 1 ? 16 
HELX_P HELX_P38  AE2 GLY A 2229 ? GLY A 2246 ? GLY A 2229 GLY A 2246 1 ? 18 
HELX_P HELX_P39  AE3 ASP A 2255 ? ILE A 2259 ? ASP A 2255 ILE A 2259 5 ? 5  
HELX_P HELX_P40  AE4 SER A 2260 ? TYR A 2265 ? SER A 2260 TYR A 2265 1 ? 6  
HELX_P HELX_P41  AE5 GLY A 2278 ? SER A 2290 ? GLY A 2278 SER A 2290 1 ? 13 
HELX_P HELX_P42  AE6 GLY A 2293 ? LYS A 2297 ? GLY A 2293 LYS A 2297 5 ? 5  
HELX_P HELX_P43  AE7 ASP A 2308 ? GLU A 2313 ? ASP A 2308 GLU A 2313 1 ? 6  
HELX_P HELX_P44  AE8 LEU A 2315 ? ASP A 2320 ? LEU A 2315 ASP A 2320 1 ? 6  
HELX_P HELX_P45  AE9 THR A 2352 ? ARG A 2358 ? THR A 2352 ARG A 2358 1 ? 7  
HELX_P HELX_P46  AF1 SER A 2370 ? ILE A 2385 ? SER A 2370 ILE A 2385 1 ? 16 
HELX_P HELX_P47  AF2 PRO A 2411 ? GLN A 2424 ? PRO A 2411 GLN A 2424 1 ? 14 
HELX_P HELX_P48  AF3 PRO A 2425 ? THR A 2428 ? PRO A 2425 THR A 2428 5 ? 4  
HELX_P HELX_P49  AF4 GLY A 2431 ? LEU A 2443 ? GLY A 2431 LEU A 2443 1 ? 13 
HELX_P HELX_P50  AF5 THR A 2450 ? HIS A 2476 ? THR A 2450 HIS A 2476 1 ? 27 
HELX_P HELX_P51  AF6 GLN A 2482 ? GLY A 2504 ? GLN A 2482 GLY A 2504 1 ? 23 
HELX_P HELX_P52  AF7 ARG A 2507 ? THR A 2522 ? ARG A 2507 THR A 2522 1 ? 16 
HELX_P HELX_P53  AF8 PRO A 2533 ? ILE A 2535 ? PRO A 2533 ILE A 2535 5 ? 3  
HELX_P HELX_P54  AF9 GLN A 2549 ? VAL A 2552 ? GLN A 2549 VAL A 2552 5 ? 4  
HELX_P HELX_P55  AG1 GLU A 2558 ? VAL A 2562 ? GLU A 2558 VAL A 2562 5 ? 5  
HELX_P HELX_P56  AG2 THR A 2571 ? GLU A 2587 ? THR A 2571 GLU A 2587 1 ? 17 
HELX_P HELX_P57  AG3 GLY A 2600 ? ALA A 2611 ? GLY A 2600 ALA A 2611 1 ? 12 
HELX_P HELX_P58  AG4 THR A 2627 ? TYR A 2638 ? THR A 2627 TYR A 2638 1 ? 12 
HELX_P HELX_P59  AG5 GLN A 2677 ? HIS A 2689 ? GLN A 2677 HIS A 2689 1 ? 13 
HELX_P HELX_P60  AG6 SER A 2724 ? ARG A 2729 ? SER A 2724 ARG A 2729 1 ? 6  
HELX_P HELX_P61  AG7 GLY A 2740 ? LEU A 2756 ? GLY A 2740 LEU A 2756 1 ? 17 
HELX_P HELX_P62  AG8 ARG A 2757 ? LEU A 2758 ? ARG A 2757 LEU A 2758 5 ? 2  
HELX_P HELX_P63  AG9 ILE A 2759 ? THR A 2764 ? ILE A 2759 THR A 2764 5 ? 6  
HELX_P HELX_P64  AH1 TYR A 2765 ? PHE A 2784 ? TYR A 2765 PHE A 2784 1 ? 20 
HELX_P HELX_P65  AH2 SER A 2795 ? ALA A 2809 ? SER A 2795 ALA A 2809 1 ? 15 
HELX_P HELX_P66  AH3 PRO A 2817 ? GLN A 2834 ? PRO A 2817 GLN A 2834 1 ? 18 
HELX_P HELX_P67  AH4 GLU A 2839 ? PHE A 2858 ? GLU A 2839 PHE A 2858 1 ? 20 
HELX_P HELX_P68  AH5 ASP A 2862 ? SER A 2868 ? ASP A 2862 SER A 2868 1 ? 7  
HELX_P HELX_P69  AH6 ASP A 2885 ? GLU A 2904 ? ASP A 2885 GLU A 2904 1 ? 20 
HELX_P HELX_P70  AH7 PHE A 2912 ? ARG A 2927 ? PHE A 2912 ARG A 2927 1 ? 16 
HELX_P HELX_P71  AH8 GLY A 2942 ? ASN A 2954 ? GLY A 2942 ASN A 2954 1 ? 13 
HELX_P HELX_P72  AH9 THR A 2968 ? CYS A 2985 ? THR A 2968 CYS A 2985 1 ? 18 
HELX_P HELX_P73  AI1 SER A 2997 ? VAL A 2999 ? SER A 2997 VAL A 2999 5 ? 3  
HELX_P HELX_P74  AI2 ASP A 3001 ? GLY A 3015 ? ASP A 3001 GLY A 3015 1 ? 15 
HELX_P HELX_P75  AI3 GLY A 3023 ? GLU A 3040 ? GLY A 3023 GLU A 3040 1 ? 18 
HELX_P HELX_P76  AI4 SER A 3046 ? ASN A 3061 ? SER A 3046 ASN A 3061 1 ? 16 
HELX_P HELX_P77  AI5 SER A 3071 ? SER A 3082 ? SER A 3071 SER A 3082 1 ? 12 
HELX_P HELX_P78  AI6 PRO A 3083 ? ARG A 3088 ? PRO A 3083 ARG A 3088 1 ? 6  
HELX_P HELX_P79  AI7 SER A 3098 ? THR A 3110 ? SER A 3098 THR A 3110 1 ? 13 
HELX_P HELX_P80  AI8 SER A 3138 ? ARG A 3164 ? SER A 3138 ARG A 3164 1 ? 27 
HELX_P HELX_P81  AI9 THR A 3172 ? LYS A 3242 ? THR A 3172 LYS A 3242 1 ? 71 
HELX_P HELX_P82  AJ1 GLU A 3450 ? LEU A 3482 ? GLU A 3450 LEU A 3482 1 ? 33 
HELX_P HELX_P83  AJ2 LEU A 3482 ? THR A 3495 ? LEU A 3482 THR A 3495 1 ? 14 
HELX_P HELX_P84  AJ3 THR A 3495 ? ALA A 3517 ? THR A 3495 ALA A 3517 1 ? 23 
HELX_P HELX_P85  AJ4 GLY A 3518 ? PHE A 3520 ? GLY A 3518 PHE A 3520 5 ? 3  
HELX_P HELX_P86  AJ5 ASP A 3521 ? ALA A 3539 ? ASP A 3521 ALA A 3539 1 ? 19 
HELX_P HELX_P87  AJ6 ALA A 3548 ? LEU A 3553 ? ALA A 3548 LEU A 3553 1 ? 6  
HELX_P HELX_P88  AJ7 ASN A 3555 ? SER A 3565 ? ASN A 3555 SER A 3565 1 ? 11 
HELX_P HELX_P89  AJ8 ASP A 3570 ? PHE A 3583 ? ASP A 3570 PHE A 3583 1 ? 14 
HELX_P HELX_P90  AJ9 GLY A 3594 ? TYR A 3604 ? GLY A 3594 TYR A 3604 1 ? 11 
HELX_P HELX_P91  AK1 ALA A 3618 ? GLY A 3630 ? ALA A 3618 GLY A 3630 1 ? 13 
HELX_P HELX_P92  AK2 ASP A 3637 ? TYR A 3641 ? ASP A 3637 TYR A 3641 5 ? 5  
HELX_P HELX_P93  AK3 ASP A 3642 ? VAL A 3644 ? ASP A 3642 VAL A 3644 5 ? 3  
HELX_P HELX_P94  AK4 LEU A 3645 ? ASN A 3650 ? LEU A 3645 ASN A 3650 1 ? 6  
HELX_P HELX_P95  AK5 PRO A 3689 ? ARG A 3695 ? PRO A 3689 ARG A 3695 1 ? 7  
HELX_P HELX_P96  AK6 THR A 3704 ? ARG A 3721 ? THR A 3704 ARG A 3721 1 ? 18 
HELX_P HELX_P97  AK7 ARG A 3721 ? VAL A 3756 ? ARG A 3721 VAL A 3756 1 ? 36 
HELX_P HELX_P98  AK8 ASP A 3763 ? GLN A 3799 ? ASP A 3763 GLN A 3799 1 ? 37 
HELX_P HELX_P99  AK9 TYR A 3801 ? SER A 3817 ? TYR A 3801 SER A 3817 1 ? 17 
HELX_P HELX_P100 AL1 LEU A 3818 ? ILE A 3821 ? LEU A 3818 ILE A 3821 5 ? 4  
HELX_P HELX_P101 AL2 SER A 3828 ? GLU A 3842 ? SER A 3828 GLU A 3842 1 ? 15 
HELX_P HELX_P102 AL3 ASN A 3843 ? LYS A 3847 ? ASN A 3843 LYS A 3847 5 ? 5  
HELX_P HELX_P103 AL4 ASP A 3851 ? ARG A 3873 ? ASP A 3851 ARG A 3873 1 ? 23 
HELX_P HELX_P104 AL5 GLY A 3874 ? MET A 3875 ? GLY A 3874 MET A 3875 5 ? 2  
HELX_P HELX_P105 AL6 LEU A 3876 ? GLN A 3878 ? LEU A 3876 GLN A 3878 5 ? 3  
HELX_P HELX_P106 AL7 ASP A 3879 ? THR A 3895 ? ASP A 3879 THR A 3895 1 ? 17 
HELX_P HELX_P107 AL8 TYR A 3901 ? LEU A 3909 ? TYR A 3901 LEU A 3909 1 ? 9  
HELX_P HELX_P108 AL9 THR A 3928 ? SER A 3939 ? THR A 3928 SER A 3939 1 ? 12 
HELX_P HELX_P109 AM1 ASP A 3946 ? ASP A 3954 ? ASP A 3946 ASP A 3954 1 ? 9  
HELX_P HELX_P110 AM2 GLN A 3956 ? ASP A 3962 ? GLN A 3956 ASP A 3962 1 ? 7  
HELX_P HELX_P111 AM3 SER A 3965 ? THR A 3969 ? SER A 3965 THR A 3969 5 ? 5  
HELX_P HELX_P112 AM4 THR A 3981 ? ARG A 3997 ? THR A 3981 ARG A 3997 1 ? 17 
HELX_P HELX_P113 AM5 ARG A 4000 ? GLY A 4014 ? ARG A 4000 GLY A 4014 1 ? 15 
HELX_P HELX_P114 AM6 MET A 4018 ? GLN A 4023 ? MET A 4018 GLN A 4023 5 ? 6  
HELX_P HELX_P115 AM7 ASP A 4026 ? GLU A 4034 ? ASP A 4026 GLU A 4034 1 ? 9  
HELX_P HELX_P116 AM8 ALA A 4051 ? ASN A 4063 ? ALA A 4051 ASN A 4063 1 ? 13 
HELX_P HELX_P117 AM9 SER A 4073 ? VAL A 4088 ? SER A 4073 VAL A 4088 1 ? 16 
HELX_P HELX_P118 AN1 ASN A 4098 ? LEU A 4101 ? ASN A 4098 LEU A 4101 5 ? 4  
HELX_P HELX_P119 AN2 ALA A 4102 ? SER A 4115 ? ALA A 4102 SER A 4115 1 ? 14 
HELX_P HELX_P120 AN3 PRO A 4135 ? GLY A 4142 ? PRO A 4135 GLY A 4142 1 ? 8  
HELX_P HELX_P121 AN4 GLY A 4152 ? ILE A 4164 ? GLY A 4152 ILE A 4164 1 ? 13 
HELX_P HELX_P122 AN5 PRO A 4165 ? CYS A 4170 ? PRO A 4165 CYS A 4170 1 ? 6  
HELX_P HELX_P123 AN6 GLU A 4175 ? LEU A 4194 ? GLU A 4175 LEU A 4194 1 ? 20 
HELX_P HELX_P124 AN7 TYR A 4196 ? TRP A 4201 ? TYR A 4196 TRP A 4201 1 ? 6  
HELX_P HELX_P125 AN8 GLY A 4208 ? ALA A 4227 ? GLY A 4208 ALA A 4227 1 ? 20 
HELX_P HELX_P126 AN9 SER A 4234 ? ILE A 4238 ? SER A 4234 ILE A 4238 5 ? 5  
HELX_P HELX_P127 AO1 PRO A 4239 ? SER A 4250 ? PRO A 4239 SER A 4250 1 ? 12 
HELX_P HELX_P128 AO2 ASN A 4258 ? PHE A 4273 ? ASN A 4258 PHE A 4273 1 ? 16 
HELX_P HELX_P129 AO3 THR A 4274 ? ASP A 4279 ? THR A 4274 ASP A 4279 5 ? 6  
HELX_P HELX_P130 AO4 ARG A 4301 ? LEU A 4311 ? ARG A 4301 LEU A 4311 1 ? 11 
HELX_P HELX_P131 AO5 THR A 4317 ? GLY A 4322 ? THR A 4317 GLY A 4322 5 ? 6  
HELX_P HELX_P132 AO6 PRO A 4324 ? ALA A 4327 ? PRO A 4324 ALA A 4327 5 ? 4  
HELX_P HELX_P133 AO7 GLU A 4328 ? GLN A 4347 ? GLU A 4328 GLN A 4347 1 ? 20 
HELX_P HELX_P134 AO8 ALA A 4375 ? ILE A 4391 ? ALA A 4375 ILE A 4391 1 ? 17 
HELX_P HELX_P135 AO9 THR A 4401 ? LYS A 4406 ? THR A 4401 LYS A 4406 1 ? 6  
HELX_P HELX_P136 AP1 ASP A 4407 ? GLU A 4439 ? ASP A 4407 GLU A 4439 1 ? 33 
HELX_P HELX_P137 AP2 THR A 4445 ? GLY A 4458 ? THR A 4445 GLY A 4458 1 ? 14 
HELX_P HELX_P138 AP3 THR A 4474 ? SER A 4498 ? THR A 4474 SER A 4498 1 ? 25 
HELX_P HELX_P139 AP4 GLY A 4500 ? LYS A 4505 ? GLY A 4500 LYS A 4505 5 ? 6  
HELX_P HELX_P140 AP5 VAL A 4516 ? ASN A 4532 ? VAL A 4516 ASN A 4532 1 ? 17 
HELX_P HELX_P141 AP6 SER A 4535 ? GLU A 4537 ? SER A 4535 GLU A 4537 5 ? 3  
HELX_P HELX_P142 AP7 ASP A 4631 ? ARG A 4638 ? ASP A 4631 ARG A 4638 1 ? 8  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A THR 1913 OG1 ? ? ? 1_555 F MG . MG ? ? A THR 1913 A MG 4705 1_555 ? ? ? ? ? ? ? 2.095 ? ? 
metalc2 metalc ? ? A SER 2231 OG  ? ? ? 1_555 G MG . MG ? ? A SER 2231 A MG 4706 1_555 ? ? ? ? ? ? ? 1.959 ? ? 
metalc3 metalc ? ? A GLU 2344 OE2 ? ? ? 1_555 G MG . MG ? ? A GLU 2344 A MG 4706 1_555 ? ? ? ? ? ? ? 1.745 ? ? 
metalc4 metalc ? ? B ADP .    O3B ? ? ? 1_555 F MG . MG ? ? A ADP 4701 A MG 4705 1_555 ? ? ? ? ? ? ? 2.102 ? ? 
metalc5 metalc ? ? C ATP .    O2G ? ? ? 1_555 G MG . MG ? ? A ATP 4702 A MG 4706 1_555 ? ? ? ? ? ? ? 2.072 ? ? 
metalc6 metalc ? ? C ATP .    O2B ? ? ? 1_555 G MG . MG ? ? A ATP 4702 A MG 4706 1_555 ? ? ? ? ? ? ? 2.138 ? ? 
metalc7 metalc ? ? C ATP .    O3B ? ? ? 1_555 G MG . MG ? ? A ATP 4702 A MG 4706 1_555 ? ? ? ? ? ? ? 2.957 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  OG1 ? A THR 1913 ? A THR 1913 ? 1_555 MG ? F MG . ? A MG 4705 ? 1_555 O3B ? B ADP .    ? A ADP 4701 ? 1_555 91.0  ? 
2  OG  ? A SER 2231 ? A SER 2231 ? 1_555 MG ? G MG . ? A MG 4706 ? 1_555 OE2 ? A GLU 2344 ? A GLU 2344 ? 1_555 89.2  ? 
3  OG  ? A SER 2231 ? A SER 2231 ? 1_555 MG ? G MG . ? A MG 4706 ? 1_555 O2G ? C ATP .    ? A ATP 4702 ? 1_555 169.2 ? 
4  OE2 ? A GLU 2344 ? A GLU 2344 ? 1_555 MG ? G MG . ? A MG 4706 ? 1_555 O2G ? C ATP .    ? A ATP 4702 ? 1_555 89.0  ? 
5  OG  ? A SER 2231 ? A SER 2231 ? 1_555 MG ? G MG . ? A MG 4706 ? 1_555 O2B ? C ATP .    ? A ATP 4702 ? 1_555 89.1  ? 
6  OE2 ? A GLU 2344 ? A GLU 2344 ? 1_555 MG ? G MG . ? A MG 4706 ? 1_555 O2B ? C ATP .    ? A ATP 4702 ? 1_555 101.3 ? 
7  O2G ? C ATP .    ? A ATP 4702 ? 1_555 MG ? G MG . ? A MG 4706 ? 1_555 O2B ? C ATP .    ? A ATP 4702 ? 1_555 101.6 ? 
8  OG  ? A SER 2231 ? A SER 2231 ? 1_555 MG ? G MG . ? A MG 4706 ? 1_555 O3B ? C ATP .    ? A ATP 4702 ? 1_555 132.3 ? 
9  OE2 ? A GLU 2344 ? A GLU 2344 ? 1_555 MG ? G MG . ? A MG 4706 ? 1_555 O3B ? C ATP .    ? A ATP 4702 ? 1_555 126.0 ? 
10 O2G ? C ATP .    ? A ATP 4702 ? 1_555 MG ? G MG . ? A MG 4706 ? 1_555 O3B ? C ATP .    ? A ATP 4702 ? 1_555 56.1  ? 
11 O2B ? C ATP .    ? A ATP 4702 ? 1_555 MG ? G MG . ? A MG 4706 ? 1_555 O3B ? C ATP .    ? A ATP 4702 ? 1_555 56.2  ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2 ? 
AA2 ? 3 ? 
AA3 ? 3 ? 
AA4 ? 2 ? 
AA5 ? 3 ? 
AA6 ? 2 ? 
AA7 ? 5 ? 
AA8 ? 2 ? 
AA9 ? 2 ? 
AB1 ? 2 ? 
AB2 ? 5 ? 
AB3 ? 4 ? 
AB4 ? 2 ? 
AB5 ? 5 ? 
AB6 ? 5 ? 
AB7 ? 3 ? 
AB8 ? 5 ? 
AB9 ? 2 ? 
AC1 ? 4 ? 
AC2 ? 6 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA4 1 2 ? parallel      
AA5 1 2 ? parallel      
AA5 2 3 ? parallel      
AA6 1 2 ? anti-parallel 
AA7 1 2 ? parallel      
AA7 2 3 ? parallel      
AA7 3 4 ? parallel      
AA7 4 5 ? parallel      
AA8 1 2 ? anti-parallel 
AA9 1 2 ? anti-parallel 
AB1 1 2 ? anti-parallel 
AB2 1 2 ? parallel      
AB2 2 3 ? parallel      
AB2 3 4 ? parallel      
AB2 4 5 ? parallel      
AB3 1 2 ? anti-parallel 
AB3 2 3 ? parallel      
AB3 3 4 ? anti-parallel 
AB4 1 2 ? anti-parallel 
AB5 1 2 ? parallel      
AB5 2 3 ? parallel      
AB5 3 4 ? parallel      
AB5 4 5 ? parallel      
AB6 1 2 ? parallel      
AB6 2 3 ? parallel      
AB6 3 4 ? parallel      
AB6 4 5 ? parallel      
AB7 1 2 ? anti-parallel 
AB7 2 3 ? anti-parallel 
AB8 1 2 ? parallel      
AB8 2 3 ? parallel      
AB8 3 4 ? parallel      
AB8 4 5 ? parallel      
AB9 1 2 ? anti-parallel 
AC1 1 2 ? parallel      
AC1 2 3 ? anti-parallel 
AC1 3 4 ? anti-parallel 
AC2 1 2 ? anti-parallel 
AC2 2 3 ? parallel      
AC2 3 4 ? anti-parallel 
AC2 4 5 ? parallel      
AC2 5 6 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 1477 ? TYR A 1480 ? LEU A 1477 TYR A 1480 
AA1 2 CYS A 1484 ? ILE A 1487 ? CYS A 1484 ILE A 1487 
AA2 1 SER A 1663 ? LEU A 1666 ? SER A 1663 LEU A 1666 
AA2 2 VAL A 1672 ? SER A 1677 ? VAL A 1672 SER A 1677 
AA2 3 GLU A 1683 ? SER A 1691 ? GLU A 1683 SER A 1691 
AA3 1 MET A 1842 ? PHE A 1846 ? MET A 1842 PHE A 1846 
AA3 2 LEU A 1857 ? MET A 1861 ? LEU A 1857 MET A 1861 
AA3 3 ALA A 1864 ? ASN A 1867 ? ALA A 1864 ASN A 1867 
AA4 1 GLY A 1901 ? PHE A 1905 ? GLY A 1901 PHE A 1905 
AA4 2 PHE A 2036 ? ALA A 2040 ? PHE A 2036 ALA A 2040 
AA5 1 VAL A 1927 ? ASN A 1931 ? VAL A 1927 ASN A 1931 
AA5 2 TRP A 1954 ? ASP A 1958 ? TRP A 1954 ASP A 1958 
AA5 3 ALA A 2013 ? THR A 2017 ? ALA A 2013 THR A 2017 
AA6 1 THR A 1998 ? LEU A 2001 ? THR A 1998 LEU A 2001 
AA6 2 LYS A 2004 ? LYS A 2007 ? LYS A 2004 LYS A 2007 
AA7 1 GLY A 2249 ? ILE A 2254 ? GLY A 2249 ILE A 2254 
AA7 2 ARG A 2298 ? ASP A 2304 ? ARG A 2298 ASP A 2304 
AA7 3 VAL A 2339 ? VAL A 2345 ? VAL A 2339 VAL A 2345 
AA7 4 GLY A 2219 ? VAL A 2223 ? GLY A 2219 VAL A 2223 
AA7 5 GLY A 2360 ? TRP A 2363 ? GLY A 2360 TRP A 2363 
AA8 1 GLY A 2266 ? LEU A 2268 ? GLY A 2266 LEU A 2268 
AA8 2 TRP A 2275 ? ASP A 2277 ? TRP A 2275 ASP A 2277 
AA9 1 LEU A 2324 ? THR A 2326 ? LEU A 2324 THR A 2326 
AA9 2 ARG A 2332 ? SER A 2334 ? ARG A 2332 SER A 2334 
AB1 1 TYR A 2537 ? VAL A 2539 ? TYR A 2537 VAL A 2539 
AB1 2 TRP A 2545 ? PRO A 2547 ? TRP A 2545 PRO A 2547 
AB2 1 MET A 2615 ? LEU A 2620 ? MET A 2615 LEU A 2620 
AB2 2 TRP A 2658 ? CYS A 2663 ? TRP A 2658 CYS A 2663 
AB2 3 ILE A 2706 ? CYS A 2712 ? ILE A 2706 CYS A 2712 
AB2 4 LEU A 2591 ? CYS A 2594 ? LEU A 2591 CYS A 2594 
AB2 5 VAL A 2733 ? TYR A 2735 ? VAL A 2733 TYR A 2735 
AB3 1 CYS A 2639 ? THR A 2644 ? CYS A 2639 THR A 2644 
AB3 2 GLY A 2647 ? PRO A 2652 ? GLY A 2647 PRO A 2652 
AB3 3 THR A 2699 ? LEU A 2703 ? THR A 2699 LEU A 2703 
AB3 4 GLY A 2691 ? ARG A 2694 ? GLY A 2691 ARG A 2694 
AB4 1 TYR A 2873 ? SER A 2874 ? TYR A 2873 SER A 2874 
AB4 2 ILE A 2882 ? PRO A 2883 ? ILE A 2882 PRO A 2883 
AB5 1 SER A 2957 ? TYR A 2959 ? SER A 2957 TYR A 2959 
AB5 2 ILE A 2990 ? ASP A 2995 ? ILE A 2990 ASP A 2995 
AB5 3 LEU A 3062 ? MET A 3068 ? LEU A 3062 MET A 3068 
AB5 4 HIS A 2932 ? GLY A 2937 ? HIS A 2932 GLY A 2937 
AB5 5 CYS A 3089 ? GLY A 3095 ? CYS A 3089 GLY A 3095 
AB6 1 THR A 3610 ? SER A 3613 ? THR A 3610 SER A 3613 
AB6 2 PRO A 3632 ? GLN A 3636 ? PRO A 3632 GLN A 3636 
AB6 3 VAL A 3676 ? THR A 3681 ? VAL A 3676 THR A 3681 
AB6 4 TYR A 3586 ? ILE A 3590 ? TYR A 3586 ILE A 3590 
AB6 5 VAL A 3696 ? ASN A 3700 ? VAL A 3696 ASN A 3700 
AB7 1 VAL A 3653 ? THR A 3656 ? VAL A 3653 THR A 3656 
AB7 2 ARG A 3659 ? LEU A 3664 ? ARG A 3659 LEU A 3664 
AB7 3 GLN A 3667 ? ASP A 3670 ? GLN A 3667 ASP A 3670 
AB8 1 ILE A 4066 ? ALA A 4070 ? ILE A 4066 ALA A 4070 
AB8 2 TRP A 4093 ? LYS A 4097 ? TRP A 4093 LYS A 4097 
AB8 3 ARG A 4123 ? GLU A 4129 ? ARG A 4123 GLU A 4129 
AB8 4 VAL A 4041 ? SER A 4045 ? VAL A 4041 SER A 4045 
AB8 5 ARG A 4143 ? PHE A 4147 ? ARG A 4143 PHE A 4147 
AB9 1 LYS A 4283 ? ALA A 4285 ? LYS A 4283 ALA A 4285 
AB9 2 ILE A 4294 ? GLN A 4295 ? ILE A 4294 GLN A 4295 
AC1 1 VAL A 4509 ? CYS A 4510 ? VAL A 4509 CYS A 4510 
AC1 2 SER A 4557 ? THR A 4561 ? SER A 4557 THR A 4561 
AC1 3 LEU A 4587 ? LYS A 4594 ? LEU A 4587 LYS A 4594 
AC1 4 LEU A 4539 ? THR A 4546 ? LEU A 4539 THR A 4546 
AC2 1 LYS A 4564 ? ASN A 4571 ? LYS A 4564 ASN A 4571 
AC2 2 LYS A 4574 ? ALA A 4584 ? LYS A 4574 ALA A 4584 
AC2 3 LEU A 4618 ? ILE A 4626 ? LEU A 4618 ILE A 4626 
AC2 4 VAL A 4604 ? TYR A 4610 ? VAL A 4604 TYR A 4610 
AC2 5 ALA A 4641 ? LEU A 4643 ? ALA A 4641 LEU A 4643 
AC2 6 LYS A 4564 ? ASN A 4571 ? LYS A 4564 ASN A 4571 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N VAL A 1478 ? N VAL A 1478 O LEU A 1486 ? O LEU A 1486 
AA2 1 2 N SER A 1663 ? N SER A 1663 O SER A 1677 ? O SER A 1677 
AA2 2 3 N VAL A 1673 ? N VAL A 1673 O VAL A 1690 ? O VAL A 1690 
AA3 1 2 N ARG A 1843 ? N ARG A 1843 O GLN A 1860 ? O GLN A 1860 
AA3 2 3 N ILE A 1859 ? N ILE A 1859 O PHE A 1866 ? O PHE A 1866 
AA4 1 2 N GLY A 1901 ? N GLY A 1901 O ARG A 2037 ? O ARG A 2037 
AA5 1 2 N LEU A 1928 ? N LEU A 1928 O CYS A 1956 ? O CYS A 1956 
AA5 2 3 N PHE A 1957 ? N PHE A 1957 O PHE A 2015 ? O PHE A 2015 
AA6 1 2 N CYS A 1999 ? N CYS A 1999 O VAL A 2006 ? O VAL A 2006 
AA7 1 2 N ILE A 2254 ? N ILE A 2254 O VAL A 2302 ? O VAL A 2302 
AA7 2 3 N PHE A 2303 ? N PHE A 2303 O MET A 2342 ? O MET A 2342 
AA7 3 4 O PHE A 2343 ? O PHE A 2343 N MET A 2222 ? N MET A 2222 
AA7 4 5 N MET A 2221 ? N MET A 2221 O GLY A 2360 ? O GLY A 2360 
AA8 1 2 N THR A 2267 ? N THR A 2267 O THR A 2276 ? O THR A 2276 
AA9 1 2 N LEU A 2325 ? N LEU A 2325 O LEU A 2333 ? O LEU A 2333 
AB1 1 2 N GLU A 2538 ? N GLU A 2538 O SER A 2546 ? O SER A 2546 
AB2 1 2 N LEU A 2620 ? N LEU A 2620 O PHE A 2662 ? O PHE A 2662 
AB2 2 3 N CYS A 2663 ? N CYS A 2663 O ALA A 2711 ? O ALA A 2711 
AB2 3 4 O GLY A 2710 ? O GLY A 2710 N LEU A 2591 ? N LEU A 2591 
AB2 4 5 N CYS A 2594 ? N CYS A 2594 O VAL A 2734 ? O VAL A 2734 
AB3 1 2 N GLU A 2640 ? N GLU A 2640 O ALA A 2651 ? O ALA A 2651 
AB3 2 3 N LEU A 2650 ? N LEU A 2650 O LYS A 2702 ? O LYS A 2702 
AB3 3 4 O VAL A 2701 ? O VAL A 2701 N PHE A 2692 ? N PHE A 2692 
AB4 1 2 N SER A 2874 ? N SER A 2874 O ILE A 2882 ? O ILE A 2882 
AB5 1 2 N SER A 2957 ? N SER A 2957 O ALA A 2991 ? O ALA A 2991 
AB5 2 3 N PHE A 2992 ? N PHE A 2992 O HIS A 3063 ? O HIS A 3063 
AB5 3 4 O PHE A 3066 ? O PHE A 3066 N LEU A 2933 ? N LEU A 2933 
AB5 4 5 N HIS A 2932 ? N HIS A 2932 O VAL A 3090 ? O VAL A 3090 
AB6 1 2 N THR A 3612 ? N THR A 3612 O LEU A 3634 ? O LEU A 3634 
AB6 2 3 N VAL A 3635 ? N VAL A 3635 O PHE A 3678 ? O PHE A 3678 
AB6 3 4 O LEU A 3679 ? O LEU A 3679 N ILE A 3589 ? N ILE A 3589 
AB6 4 5 N LEU A 3588 ? N LEU A 3588 O THR A 3697 ? O THR A 3697 
AB7 1 2 N ARG A 3654 ? N ARG A 3654 O LEU A 3661 ? O LEU A 3661 
AB7 2 3 N ILE A 3662 ? N ILE A 3662 O ILE A 3669 ? O ILE A 3669 
AB8 1 2 N THR A 4067 ? N THR A 4067 O MET A 4095 ? O MET A 4095 
AB8 2 3 N LEU A 4096 ? N LEU A 4096 O THR A 4127 ? O THR A 4127 
AB8 3 4 O LEU A 4126 ? O LEU A 4126 N MET A 4043 ? N MET A 4043 
AB8 4 5 N CYS A 4044 ? N CYS A 4044 O PHE A 4147 ? O PHE A 4147 
AB9 1 2 N ALA A 4285 ? N ALA A 4285 O ILE A 4294 ? O ILE A 4294 
AC1 1 2 N VAL A 4509 ? N VAL A 4509 O THR A 4561 ? O THR A 4561 
AC1 2 3 N PHE A 4558 ? N PHE A 4558 O LEU A 4590 ? O LEU A 4590 
AC1 3 4 O GLN A 4589 ? O GLN A 4589 N ASN A 4544 ? N ASN A 4544 
AC2 1 2 N LEU A 4565 ? N LEU A 4565 O THR A 4583 ? O THR A 4583 
AC2 2 3 N LEU A 4575 ? N LEU A 4575 O GLU A 4625 ? O GLU A 4625 
AC2 3 4 O ILE A 4619 ? O ILE A 4619 N VAL A 4609 ? N VAL A 4609 
AC2 4 5 N TYR A 4610 ? N TYR A 4610 O VAL A 4642 ? O VAL A 4642 
AC2 5 6 O ALA A 4641 ? O ALA A 4641 N GLN A 4566 ? N GLN A 4566 
# 
_pdbx_entry_details.entry_id                   9BMY 
_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 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   OE2 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   GLU 
_pdbx_validate_close_contact.auth_seq_id_1    2629 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   NZ 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   LYS 
_pdbx_validate_close_contact.auth_seq_id_2    2633 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.12 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ASN A 1643 ? ? -99.38  32.64   
2  1 ASN A 1670 ? ? 71.09   33.17   
3  1 ALA A 1862 ? ? 58.16   -121.44 
4  1 THR A 2061 ? ? -99.09  38.31   
5  1 ALA A 2121 ? ? -98.93  36.97   
6  1 ASN A 2130 ? ? -101.13 75.71   
7  1 PRO A 2796 ? ? -59.74  -9.13   
8  1 SER A 3640 ? ? -103.11 40.34   
9  1 PRO A 3643 ? ? -66.58  2.23    
10 1 ARG A 3910 ? ? 52.81   -98.40  
11 1 ASP A 3946 ? ? -95.54  53.22   
12 1 GLU A 3977 ? ? -95.07  -60.65  
13 1 CYS A 4170 ? ? -90.33  30.19   
14 1 ALA A 4197 ? ? -20.74  -67.77  
15 1 GLU A 4206 ? ? -95.69  59.27   
16 1 TYR A 4252 ? ? 75.05   -9.69   
17 1 ASP A 4298 ? ? -92.24  48.98   
18 1 ASP A 4314 ? ? -90.61  31.06   
19 1 ASN A 4597 ? ? 35.08   47.87   
20 1 GLU A 4599 ? ? 59.33   -162.51 
21 1 ALA A 4602 ? ? 65.32   -0.66   
22 1 THR A 4628 ? ? 52.04   -142.80 
# 
_pdbx_validate_planes.id              1 
_pdbx_validate_planes.PDB_model_num   1 
_pdbx_validate_planes.auth_comp_id    ARG 
_pdbx_validate_planes.auth_asym_id    A 
_pdbx_validate_planes.auth_seq_id     4195 
_pdbx_validate_planes.PDB_ins_code    ? 
_pdbx_validate_planes.label_alt_id    ? 
_pdbx_validate_planes.rmsd            0.118 
_pdbx_validate_planes.type            'SIDE CHAIN' 
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          9BMY 
_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                    9BMY 
_em_3d_reconstruction.id                          1 
_em_3d_reconstruction.method                      ? 
_em_3d_reconstruction.algorithm                   ? 
_em_3d_reconstruction.citation_id                 ? 
_em_3d_reconstruction.details                     ? 
_em_3d_reconstruction.resolution                  2.86 
_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               136324 
_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' 
_em_buffer.pH            7.2 
# 
_em_entity_assembly.id                   1 
_em_entity_assembly.parent_id            0 
_em_entity_assembly.source               RECOMBINANT 
_em_entity_assembly.type                 COMPLEX 
_em_entity_assembly.name                 'State-1 of motor domain from full-length human dynein-1 in apo condition' 
_em_entity_assembly.details              ? 
_em_entity_assembly.synonym              ? 
_em_entity_assembly.oligomeric_details   ? 
_em_entity_assembly.entity_id_list       1 
# 
_em_imaging.entry_id                        9BMY 
_em_imaging.id                              1 
_em_imaging.astigmatism                     ? 
_em_imaging.electron_beam_tilt_params       ? 
_em_imaging.residual_tilt                   ? 
_em_imaging.microscope_model                'FEI TITAN KRIOS' 
_em_imaging.specimen_holder_type            ? 
_em_imaging.specimen_holder_model           'FEI TITAN KRIOS AUTOGRID HOLDER' 
_em_imaging.details                         ? 
_em_imaging.date                            ? 
_em_imaging.accelerating_voltage            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              9BMY 
_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                9BMY 
_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           9BMY 
_em_admin.last_update        2025-04-30 
_em_admin.map_release_date   2025-04-23 
_em_admin.title              'State-1 of motor domain from full-length human dynein-1 in apo condition' 
# 
_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 ? ? 
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 ? ? ? ? 
CLASSIFICATION             ? 12 1 ? ? ? ? 
RECONSTRUCTION             ? 13 1 ? ? ? ? 
# 
_em_specimen.concentration           2 
_em_specimen.details                 7.2 
_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                    9BMY 
_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 ? 215.081 210.683 146.023 1.00 36.31 ? 1457 MET A N     1 
ATOM   2     C  CA    . MET A 1 1457 ? 214.963 212.084 146.414 1.00 36.14 ? 1457 MET A CA    1 
ATOM   3     C  C     . MET A 1 1457 ? 213.620 212.353 147.084 1.00 36.56 ? 1457 MET A C     1 
ATOM   4     O  O     . MET A 1 1457 ? 213.301 213.495 147.414 1.00 37.52 ? 1457 MET A O     1 
ATOM   5     C  CB    . MET A 1 1457 ? 215.136 212.997 145.200 1.00 34.60 ? 1457 MET A CB    1 
ATOM   6     C  CG    . MET A 1 1457 ? 213.954 212.984 144.246 1.00 36.04 ? 1457 MET A CG    1 
ATOM   7     S  SD    . MET A 1 1457 ? 213.783 211.411 143.383 1.00 62.27 ? 1457 MET A SD    1 
ATOM   8     C  CE    . MET A 1 1457 ? 215.225 211.447 142.321 1.00 40.38 ? 1457 MET A CE    1 
ATOM   9     N  N     . ALA A 1 1458 ? 212.836 211.291 147.283 1.00 31.23 ? 1458 ALA A N     1 
ATOM   10    C  CA    . ALA A 1 1458 ? 211.561 211.438 147.975 1.00 31.23 ? 1458 ALA A CA    1 
ATOM   11    C  C     . ALA A 1 1458 ? 211.756 211.922 149.403 1.00 35.75 ? 1458 ALA A C     1 
ATOM   12    O  O     . ALA A 1 1458 ? 210.927 212.681 149.921 1.00 38.19 ? 1458 ALA A O     1 
ATOM   13    C  CB    . ALA A 1 1458 ? 210.798 210.113 147.960 1.00 30.17 ? 1458 ALA A CB    1 
ATOM   14    N  N     . LEU A 1 1459 ? 212.837 211.492 150.057 1.00 36.57 ? 1459 LEU A N     1 
ATOM   15    C  CA    . LEU A 1 1459 ? 213.160 212.012 151.380 1.00 32.87 ? 1459 LEU A CA    1 
ATOM   16    C  C     . LEU A 1 1459 ? 213.447 213.508 151.325 1.00 32.47 ? 1459 LEU A C     1 
ATOM   17    O  O     . LEU A 1 1459 ? 213.027 214.260 152.212 1.00 34.96 ? 1459 LEU A O     1 
ATOM   18    C  CB    . LEU A 1 1459 ? 214.355 211.261 151.965 1.00 25.11 ? 1459 LEU A CB    1 
ATOM   19    C  CG    . LEU A 1 1459 ? 214.178 209.783 152.318 1.00 32.15 ? 1459 LEU A CG    1 
ATOM   20    C  CD1   . LEU A 1 1459 ? 214.459 208.891 151.118 1.00 34.96 ? 1459 LEU A CD1   1 
ATOM   21    C  CD2   . LEU A 1 1459 ? 215.077 209.413 153.483 1.00 30.79 ? 1459 LEU A CD2   1 
ATOM   22    N  N     . GLU A 1 1460 ? 214.162 213.956 150.290 1.00 26.08 ? 1460 GLU A N     1 
ATOM   23    C  CA    . GLU A 1 1460 ? 214.458 215.379 150.160 1.00 30.66 ? 1460 GLU A CA    1 
ATOM   24    C  C     . GLU A 1 1460 ? 213.180 216.193 149.998 1.00 36.05 ? 1460 GLU A C     1 
ATOM   25    O  O     . GLU A 1 1460 ? 213.089 217.324 150.490 1.00 36.11 ? 1460 GLU A O     1 
ATOM   26    C  CB    . GLU A 1 1460 ? 215.404 215.614 148.981 1.00 30.79 ? 1460 GLU A CB    1 
ATOM   27    C  CG    . GLU A 1 1460 ? 215.727 217.076 148.720 1.00 31.46 ? 1460 GLU A CG    1 
ATOM   28    C  CD    . GLU A 1 1460 ? 216.602 217.273 147.497 1.00 42.28 ? 1460 GLU A CD    1 
ATOM   29    O  OE1   . GLU A 1 1460 ? 216.167 216.903 146.385 1.00 41.21 ? 1460 GLU A OE1   1 
ATOM   30    O  OE2   . GLU A 1 1460 ? 217.726 217.795 147.647 1.00 37.94 ? 1460 GLU A OE2   1 
ATOM   31    N  N     . GLU A 1 1461 ? 212.181 215.634 149.310 1.00 32.87 ? 1461 GLU A N     1 
ATOM   32    C  CA    . GLU A 1 1461 ? 210.908 216.332 149.158 1.00 29.66 ? 1461 GLU A CA    1 
ATOM   33    C  C     . GLU A 1 1461 ? 210.221 216.530 150.502 1.00 32.21 ? 1461 GLU A C     1 
ATOM   34    O  O     . GLU A 1 1461 ? 209.656 217.598 150.766 1.00 33.07 ? 1461 GLU A O     1 
ATOM   35    C  CB    . GLU A 1 1461 ? 210.000 215.566 148.197 1.00 27.72 ? 1461 GLU A CB    1 
ATOM   36    C  CG    . GLU A 1 1461 ? 210.655 215.221 146.871 1.00 33.58 ? 1461 GLU A CG    1 
ATOM   37    C  CD    . GLU A 1 1461 ? 211.457 216.375 146.302 1.00 40.13 ? 1461 GLU A CD    1 
ATOM   38    O  OE1   . GLU A 1 1461 ? 210.857 217.428 146.002 1.00 38.93 ? 1461 GLU A OE1   1 
ATOM   39    O  OE2   . GLU A 1 1461 ? 212.688 216.228 146.155 1.00 43.02 ? 1461 GLU A OE2   1 
ATOM   40    N  N     . PHE A 1 1462 ? 210.256 215.513 151.366 1.00 30.68 ? 1462 PHE A N     1 
ATOM   41    C  CA    . PHE A 1 1462 ? 209.635 215.639 152.680 1.00 26.41 ? 1462 PHE A CA    1 
ATOM   42    C  C     . PHE A 1 1462 ? 210.307 216.728 153.503 1.00 29.82 ? 1462 PHE A C     1 
ATOM   43    O  O     . PHE A 1 1462 ? 209.627 217.525 154.162 1.00 30.78 ? 1462 PHE A O     1 
ATOM   44    C  CB    . PHE A 1 1462 ? 209.674 214.301 153.416 1.00 27.55 ? 1462 PHE A CB    1 
ATOM   45    C  CG    . PHE A 1 1462 ? 208.838 213.227 152.774 1.00 37.74 ? 1462 PHE A CG    1 
ATOM   46    C  CD1   . PHE A 1 1462 ? 207.850 213.554 151.858 1.00 34.98 ? 1462 PHE A CD1   1 
ATOM   47    C  CD2   . PHE A 1 1462 ? 209.040 211.894 153.086 1.00 33.74 ? 1462 PHE A CD2   1 
ATOM   48    C  CE1   . PHE A 1 1462 ? 207.082 212.570 151.266 1.00 36.34 ? 1462 PHE A CE1   1 
ATOM   49    C  CE2   . PHE A 1 1462 ? 208.274 210.905 152.497 1.00 35.25 ? 1462 PHE A CE2   1 
ATOM   50    C  CZ    . PHE A 1 1462 ? 207.294 211.243 151.586 1.00 36.89 ? 1462 PHE A CZ    1 
ATOM   51    N  N     . LEU A 1 1463 ? 211.640 216.788 153.475 1.00 28.25 ? 1463 LEU A N     1 
ATOM   52    C  CA    . LEU A 1 1463 ? 212.340 217.856 154.181 1.00 25.26 ? 1463 LEU A CA    1 
ATOM   53    C  C     . LEU A 1 1463 ? 211.982 219.221 153.610 1.00 27.82 ? 1463 LEU A C     1 
ATOM   54    O  O     . LEU A 1 1463 ? 211.801 220.186 154.361 1.00 31.14 ? 1463 LEU A O     1 
ATOM   55    C  CB    . LEU A 1 1463 ? 213.853 217.638 154.127 1.00 28.03 ? 1463 LEU A CB    1 
ATOM   56    C  CG    . LEU A 1 1463 ? 214.503 216.704 155.151 1.00 28.14 ? 1463 LEU A CG    1 
ATOM   57    C  CD1   . LEU A 1 1463 ? 214.335 217.254 156.562 1.00 26.85 ? 1463 LEU A CD1   1 
ATOM   58    C  CD2   . LEU A 1 1463 ? 213.979 215.283 155.060 1.00 27.00 ? 1463 LEU A CD2   1 
ATOM   59    N  N     . LYS A 1 1464 ? 211.882 219.324 152.282 1.00 28.08 ? 1464 LYS A N     1 
ATOM   60    C  CA    . LYS A 1 1464 ? 211.500 220.589 151.665 1.00 25.69 ? 1464 LYS A CA    1 
ATOM   61    C  C     . LYS A 1 1464 ? 210.075 220.976 152.044 1.00 27.93 ? 1464 LYS A C     1 
ATOM   62    O  O     . LYS A 1 1464 ? 209.796 222.148 152.320 1.00 31.40 ? 1464 LYS A O     1 
ATOM   63    C  CB    . LYS A 1 1464 ? 211.652 220.497 150.147 1.00 27.40 ? 1464 LYS A CB    1 
ATOM   64    C  CG    . LYS A 1 1464 ? 211.390 221.799 149.410 1.00 24.34 ? 1464 LYS A CG    1 
ATOM   65    C  CD    . LYS A 1 1464 ? 212.490 222.816 149.674 1.00 28.00 ? 1464 LYS A CD    1 
ATOM   66    C  CE    . LYS A 1 1464 ? 212.285 224.078 148.852 1.00 32.94 ? 1464 LYS A CE    1 
ATOM   67    N  NZ    . LYS A 1 1464 ? 213.331 225.104 149.126 1.00 35.89 ? 1464 LYS A NZ    1 
ATOM   68    N  N     . GLN A 1 1465 ? 209.160 220.004 152.059 1.00 27.27 ? 1465 GLN A N     1 
ATOM   69    C  CA    . GLN A 1 1465 ? 207.788 220.286 152.468 1.00 23.93 ? 1465 GLN A CA    1 
ATOM   70    C  C     . GLN A 1 1465 ? 207.723 220.698 153.933 1.00 28.94 ? 1465 GLN A C     1 
ATOM   71    O  O     . GLN A 1 1465 ? 207.001 221.635 154.290 1.00 31.08 ? 1465 GLN A O     1 
ATOM   72    C  CB    . GLN A 1 1465 ? 206.899 219.069 152.214 1.00 24.02 ? 1465 GLN A CB    1 
ATOM   73    C  CG    . GLN A 1 1465 ? 206.656 218.770 150.747 1.00 27.05 ? 1465 GLN A CG    1 
ATOM   74    C  CD    . GLN A 1 1465 ? 206.175 217.352 150.513 1.00 33.71 ? 1465 GLN A CD    1 
ATOM   75    O  OE1   . GLN A 1 1465 ? 206.787 216.593 149.760 1.00 35.17 ? 1465 GLN A OE1   1 
ATOM   76    N  NE2   . GLN A 1 1465 ? 205.073 216.987 151.158 1.00 35.58 ? 1465 GLN A NE2   1 
ATOM   77    N  N     . ILE A 1 1466 ? 208.469 220.005 154.798 1.00 26.70 ? 1466 ILE A N     1 
ATOM   78    C  CA    . ILE A 1 1466 ? 208.510 220.377 156.208 1.00 23.10 ? 1466 ILE A CA    1 
ATOM   79    C  C     . ILE A 1 1466 ? 209.107 221.768 156.371 1.00 22.25 ? 1466 ILE A C     1 
ATOM   80    O  O     . ILE A 1 1466 ? 208.601 222.594 157.142 1.00 23.76 ? 1466 ILE A O     1 
ATOM   81    C  CB    . ILE A 1 1466 ? 209.292 219.326 157.017 1.00 18.36 ? 1466 ILE A CB    1 
ATOM   82    C  CG1   . ILE A 1 1466 ? 208.538 217.996 157.025 1.00 22.46 ? 1466 ILE A CG1   1 
ATOM   83    C  CG2   . ILE A 1 1466 ? 209.515 219.807 158.439 1.00 20.44 ? 1466 ILE A CG2   1 
ATOM   84    C  CD1   . ILE A 1 1466 ? 209.137 216.951 157.934 1.00 24.28 ? 1466 ILE A CD1   1 
ATOM   85    N  N     . ARG A 1 1467 ? 210.187 222.052 155.641 1.00 21.83 ? 1467 ARG A N     1 
ATOM   86    C  CA    . ARG A 1 1467 ? 210.810 223.370 155.704 1.00 25.61 ? 1467 ARG A CA    1 
ATOM   87    C  C     . ARG A 1 1467 ? 209.868 224.459 155.207 1.00 27.28 ? 1467 ARG A C     1 
ATOM   88    O  O     . ARG A 1 1467 ? 209.802 225.540 155.801 1.00 29.24 ? 1467 ARG A O     1 
ATOM   89    C  CB    . ARG A 1 1467 ? 212.108 223.365 154.894 1.00 26.41 ? 1467 ARG A CB    1 
ATOM   90    C  CG    . ARG A 1 1467 ? 212.731 224.732 154.666 1.00 29.22 ? 1467 ARG A CG    1 
ATOM   91    C  CD    . ARG A 1 1467 ? 213.300 225.301 155.953 1.00 25.69 ? 1467 ARG A CD    1 
ATOM   92    N  NE    . ARG A 1 1467 ? 214.277 224.412 156.570 1.00 26.52 ? 1467 ARG A NE    1 
ATOM   93    C  CZ    . ARG A 1 1467 ? 215.478 224.143 156.076 1.00 29.41 ? 1467 ARG A CZ    1 
ATOM   94    N  NH1   . ARG A 1 1467 ? 215.912 224.708 154.961 1.00 30.53 ? 1467 ARG A NH1   1 
ATOM   95    N  NH2   . ARG A 1 1467 ? 216.269 223.292 156.724 1.00 31.35 ? 1467 ARG A NH2   1 
ATOM   96    N  N     . GLU A 1 1468 ? 209.125 224.191 154.131 1.00 25.01 ? 1468 GLU A N     1 
ATOM   97    C  CA    . GLU A 1 1468 ? 208.218 225.190 153.576 1.00 25.54 ? 1468 GLU A CA    1 
ATOM   98    C  C     . GLU A 1 1468 ? 207.001 225.433 154.460 1.00 29.12 ? 1468 GLU A C     1 
ATOM   99    O  O     . GLU A 1 1468 ? 206.500 226.562 154.517 1.00 29.86 ? 1468 GLU A O     1 
ATOM   100   C  CB    . GLU A 1 1468 ? 207.767 224.771 152.175 1.00 23.03 ? 1468 GLU A CB    1 
ATOM   101   C  CG    . GLU A 1 1468 ? 208.804 225.010 151.088 1.00 29.41 ? 1468 GLU A CG    1 
ATOM   102   C  CD    . GLU A 1 1468 ? 208.957 226.477 150.724 1.00 38.60 ? 1468 GLU A CD    1 
ATOM   103   O  OE1   . GLU A 1 1468 ? 208.171 227.308 151.226 1.00 40.72 ? 1468 GLU A OE1   1 
ATOM   104   O  OE2   . GLU A 1 1468 ? 209.869 226.800 149.934 1.00 35.18 ? 1468 GLU A OE2   1 
ATOM   105   N  N     . VAL A 1 1469 ? 206.506 224.400 155.143 1.00 25.64 ? 1469 VAL A N     1 
ATOM   106   C  CA    . VAL A 1 1469 ? 205.342 224.569 156.006 1.00 19.91 ? 1469 VAL A CA    1 
ATOM   107   C  C     . VAL A 1 1469 ? 205.659 225.512 157.160 1.00 22.49 ? 1469 VAL A C     1 
ATOM   108   O  O     . VAL A 1 1469 ? 204.861 226.396 157.494 1.00 27.60 ? 1469 VAL A O     1 
ATOM   109   C  CB    . VAL A 1 1469 ? 204.847 223.201 156.511 1.00 19.91 ? 1469 VAL A CB    1 
ATOM   110   C  CG1   . VAL A 1 1469 ? 203.952 223.366 157.731 1.00 23.60 ? 1469 VAL A CG1   1 
ATOM   111   C  CG2   . VAL A 1 1469 ? 204.104 222.472 155.409 1.00 19.91 ? 1469 VAL A CG2   1 
ATOM   112   N  N     . TRP A 1 1470 ? 206.827 225.356 157.773 1.00 20.71 ? 1470 TRP A N     1 
ATOM   113   C  CA    . TRP A 1 1470 ? 207.187 226.107 158.968 1.00 20.44 ? 1470 TRP A CA    1 
ATOM   114   C  C     . TRP A 1 1470 ? 207.867 227.436 158.669 1.00 25.51 ? 1470 TRP A C     1 
ATOM   115   O  O     . TRP A 1 1470 ? 208.149 228.193 159.604 1.00 30.06 ? 1470 TRP A O     1 
ATOM   116   C  CB    . TRP A 1 1470 ? 208.077 225.249 159.870 1.00 18.98 ? 1470 TRP A CB    1 
ATOM   117   C  CG    . TRP A 1 1470 ? 207.344 224.065 160.406 1.00 16.07 ? 1470 TRP A CG    1 
ATOM   118   C  CD1   . TRP A 1 1470 ? 207.559 222.756 160.099 1.00 17.35 ? 1470 TRP A CD1   1 
ATOM   119   C  CD2   . TRP A 1 1470 ? 206.256 224.087 161.334 1.00 16.33 ? 1470 TRP A CD2   1 
ATOM   120   N  NE1   . TRP A 1 1470 ? 206.676 221.957 160.785 1.00 19.10 ? 1470 TRP A NE1   1 
ATOM   121   C  CE2   . TRP A 1 1470 ? 205.864 222.752 161.551 1.00 17.33 ? 1470 TRP A CE2   1 
ATOM   122   C  CE3   . TRP A 1 1470 ? 205.577 225.106 162.006 1.00 15.28 ? 1470 TRP A CE3   1 
ATOM   123   C  CZ2   . TRP A 1 1470 ? 204.826 222.411 162.412 1.00 14.09 ? 1470 TRP A CZ2   1 
ATOM   124   C  CZ3   . TRP A 1 1470 ? 204.548 224.765 162.859 1.00 16.23 ? 1470 TRP A CZ3   1 
ATOM   125   C  CH2   . TRP A 1 1470 ? 204.182 223.429 163.055 1.00 12.50 ? 1470 TRP A CH2   1 
ATOM   126   N  N     . ASN A 1 1471 ? 208.138 227.741 157.405 1.00 28.35 ? 1471 ASN A N     1 
ATOM   127   C  CA    . ASN A 1 1471 ? 208.641 229.055 157.038 1.00 25.48 ? 1471 ASN A CA    1 
ATOM   128   C  C     . ASN A 1 1471 ? 207.527 230.071 156.826 1.00 27.41 ? 1471 ASN A C     1 
ATOM   129   O  O     . ASN A 1 1471 ? 207.816 231.263 156.677 1.00 30.88 ? 1471 ASN A O     1 
ATOM   130   C  CB    . ASN A 1 1471 ? 209.496 228.960 155.770 1.00 23.08 ? 1471 ASN A CB    1 
ATOM   131   C  CG    . ASN A 1 1471 ? 210.852 228.335 156.028 1.00 32.94 ? 1471 ASN A CG    1 
ATOM   132   O  OD1   . ASN A 1 1471 ? 211.167 227.953 157.155 1.00 32.58 ? 1471 ASN A OD1   1 
ATOM   133   N  ND2   . ASN A 1 1471 ? 211.663 228.227 154.982 1.00 31.67 ? 1471 ASN A ND2   1 
ATOM   134   N  N     . THR A 1 1472 ? 206.269 229.630 156.810 1.00 22.40 ? 1472 THR A N     1 
ATOM   135   C  CA    . THR A 1 1472 ? 205.134 230.513 156.571 1.00 24.54 ? 1472 THR A CA    1 
ATOM   136   C  C     . THR A 1 1472 ? 204.018 230.389 157.596 1.00 30.25 ? 1472 THR A C     1 
ATOM   137   O  O     . THR A 1 1472 ? 203.230 231.333 157.730 1.00 31.66 ? 1472 THR A O     1 
ATOM   138   C  CB    . THR A 1 1472 ? 204.534 230.256 155.181 1.00 28.01 ? 1472 THR A CB    1 
ATOM   139   O  OG1   . THR A 1 1472 ? 204.034 228.915 155.118 1.00 27.75 ? 1472 THR A OG1   1 
ATOM   140   C  CG2   . THR A 1 1472 ? 205.580 230.455 154.093 1.00 28.19 ? 1472 THR A CG2   1 
ATOM   141   N  N     . TYR A 1 1473 ? 203.919 229.274 158.316 1.00 25.03 ? 1473 TYR A N     1 
ATOM   142   C  CA    . TYR A 1 1473 ? 202.783 229.043 159.198 1.00 21.26 ? 1473 TYR A CA    1 
ATOM   143   C  C     . TYR A 1 1473 ? 202.866 229.980 160.398 1.00 27.43 ? 1473 TYR A C     1 
ATOM   144   O  O     . TYR A 1 1473 ? 203.836 229.938 161.162 1.00 23.70 ? 1473 TYR A O     1 
ATOM   145   C  CB    . TYR A 1 1473 ? 202.763 227.587 159.650 1.00 18.63 ? 1473 TYR A CB    1 
ATOM   146   C  CG    . TYR A 1 1473 ? 201.591 227.226 160.532 1.00 23.06 ? 1473 TYR A CG    1 
ATOM   147   C  CD1   . TYR A 1 1473 ? 200.324 227.045 159.992 1.00 30.47 ? 1473 TYR A CD1   1 
ATOM   148   C  CD2   . TYR A 1 1473 ? 201.746 227.083 161.900 1.00 21.08 ? 1473 TYR A CD2   1 
ATOM   149   C  CE1   . TYR A 1 1473 ? 199.247 226.713 160.794 1.00 26.11 ? 1473 TYR A CE1   1 
ATOM   150   C  CE2   . TYR A 1 1473 ? 200.676 226.758 162.706 1.00 22.07 ? 1473 TYR A CE2   1 
ATOM   151   C  CZ    . TYR A 1 1473 ? 199.431 226.571 162.152 1.00 26.74 ? 1473 TYR A CZ    1 
ATOM   152   O  OH    . TYR A 1 1473 ? 198.368 226.247 162.961 1.00 23.25 ? 1473 TYR A OH    1 
ATOM   153   N  N     . GLU A 1 1474 ? 201.851 230.821 160.564 1.00 21.77 ? 1474 GLU A N     1 
ATOM   154   C  CA    . GLU A 1 1474 ? 201.820 231.821 161.619 1.00 19.81 ? 1474 GLU A CA    1 
ATOM   155   C  C     . GLU A 1 1474 ? 200.770 231.457 162.659 1.00 24.32 ? 1474 GLU A C     1 
ATOM   156   O  O     . GLU A 1 1474 ? 199.719 230.899 162.327 1.00 28.49 ? 1474 GLU A O     1 
ATOM   157   C  CB    . GLU A 1 1474 ? 201.521 233.212 161.050 1.00 20.98 ? 1474 GLU A CB    1 
ATOM   158   C  CG    . GLU A 1 1474 ? 202.671 233.828 160.275 1.00 22.04 ? 1474 GLU A CG    1 
ATOM   159   C  CD    . GLU A 1 1474 ? 202.416 235.275 159.905 1.00 30.16 ? 1474 GLU A CD    1 
ATOM   160   O  OE1   . GLU A 1 1474 ? 201.312 235.779 160.198 1.00 31.43 ? 1474 GLU A OE1   1 
ATOM   161   O  OE2   . GLU A 1 1474 ? 203.320 235.910 159.323 1.00 33.85 ? 1474 GLU A OE2   1 
ATOM   162   N  N     . LEU A 1 1475 ? 201.064 231.771 163.918 1.00 21.43 ? 1475 LEU A N     1 
ATOM   163   C  CA    . LEU A 1 1475 ? 200.091 231.590 164.986 1.00 17.40 ? 1475 LEU A CA    1 
ATOM   164   C  C     . LEU A 1 1475 ? 198.857 232.437 164.712 1.00 22.30 ? 1475 LEU A C     1 
ATOM   165   O  O     . LEU A 1 1475 ? 198.937 233.669 164.663 1.00 22.47 ? 1475 LEU A O     1 
ATOM   166   C  CB    . LEU A 1 1475 ? 200.710 231.962 166.331 1.00 12.85 ? 1475 LEU A CB    1 
ATOM   167   C  CG    . LEU A 1 1475 ? 201.788 231.011 166.851 1.00 16.69 ? 1475 LEU A CG    1 
ATOM   168   C  CD1   . LEU A 1 1475 ? 202.460 231.583 168.084 1.00 12.76 ? 1475 LEU A CD1   1 
ATOM   169   C  CD2   . LEU A 1 1475 ? 201.193 229.643 167.145 1.00 12.07 ? 1475 LEU A CD2   1 
ATOM   170   N  N     . ASP A 1 1476 ? 197.719 231.774 164.529 1.00 19.94 ? 1476 ASP A N     1 
ATOM   171   C  CA    . ASP A 1 1476 ? 196.477 232.468 164.216 1.00 17.67 ? 1476 ASP A CA    1 
ATOM   172   C  C     . ASP A 1 1476 ? 196.018 233.259 165.436 1.00 24.36 ? 1476 ASP A C     1 
ATOM   173   O  O     . ASP A 1 1476 ? 195.677 232.679 166.471 1.00 27.76 ? 1476 ASP A O     1 
ATOM   174   C  CB    . ASP A 1 1476 ? 195.418 231.460 163.779 1.00 26.96 ? 1476 ASP A CB    1 
ATOM   175   C  CG    . ASP A 1 1476 ? 194.160 232.117 163.252 1.00 36.95 ? 1476 ASP A CG    1 
ATOM   176   O  OD1   . ASP A 1 1476 ? 194.122 233.362 163.156 1.00 37.99 ? 1476 ASP A OD1   1 
ATOM   177   O  OD2   . ASP A 1 1476 ? 193.215 231.379 162.909 1.00 35.38 ? 1476 ASP A OD2   1 
ATOM   178   N  N     . LEU A 1 1477 ? 196.010 234.583 165.314 1.00 24.71 ? 1477 LEU A N     1 
ATOM   179   C  CA    . LEU A 1 1477 ? 195.762 235.470 166.440 1.00 17.60 ? 1477 LEU A CA    1 
ATOM   180   C  C     . LEU A 1 1477 ? 194.339 236.010 166.399 1.00 22.82 ? 1477 LEU A C     1 
ATOM   181   O  O     . LEU A 1 1477 ? 193.781 236.244 165.322 1.00 30.25 ? 1477 LEU A O     1 
ATOM   182   C  CB    . LEU A 1 1477 ? 196.755 236.632 166.452 1.00 18.09 ? 1477 LEU A CB    1 
ATOM   183   C  CG    . LEU A 1 1477 ? 198.204 236.273 166.784 1.00 19.44 ? 1477 LEU A CG    1 
ATOM   184   C  CD1   . LEU A 1 1477 ? 199.049 237.526 166.912 1.00 21.81 ? 1477 LEU A CD1   1 
ATOM   185   C  CD2   . LEU A 1 1477 ? 198.282 235.437 168.046 1.00 11.65 ? 1477 LEU A CD2   1 
ATOM   186   N  N     . VAL A 1 1478 ? 193.758 236.194 167.582 1.00 26.98 ? 1478 VAL A N     1 
ATOM   187   C  CA    . VAL A 1 1478 ? 192.445 236.803 167.748 1.00 21.35 ? 1478 VAL A CA    1 
ATOM   188   C  C     . VAL A 1 1478 ? 192.506 237.808 168.889 1.00 18.19 ? 1478 VAL A C     1 
ATOM   189   O  O     . VAL A 1 1478 ? 193.098 237.539 169.940 1.00 19.05 ? 1478 VAL A O     1 
ATOM   190   C  CB    . VAL A 1 1478 ? 191.345 235.748 168.003 1.00 22.35 ? 1478 VAL A CB    1 
ATOM   191   C  CG1   . VAL A 1 1478 ? 191.584 235.010 169.310 1.00 16.40 ? 1478 VAL A CG1   1 
ATOM   192   C  CG2   . VAL A 1 1478 ? 189.986 236.427 168.046 1.00 20.91 ? 1478 VAL A CG2   1 
ATOM   193   N  N     . ASN A 1 1479 ? 191.910 238.976 168.672 1.00 18.76 ? 1479 ASN A N     1 
ATOM   194   C  CA    . ASN A 1 1479 ? 191.807 239.966 169.733 1.00 18.15 ? 1479 ASN A CA    1 
ATOM   195   C  C     . ASN A 1 1479 ? 190.851 239.482 170.816 1.00 21.20 ? 1479 ASN A C     1 
ATOM   196   O  O     . ASN A 1 1479 ? 189.805 238.895 170.526 1.00 20.85 ? 1479 ASN A O     1 
ATOM   197   C  CB    . ASN A 1 1479 ? 191.333 241.303 169.172 1.00 19.14 ? 1479 ASN A CB    1 
ATOM   198   C  CG    . ASN A 1 1479 ? 191.061 242.323 170.255 1.00 18.96 ? 1479 ASN A CG    1 
ATOM   199   O  OD1   . ASN A 1 1479 ? 191.943 242.651 171.048 1.00 22.84 ? 1479 ASN A OD1   1 
ATOM   200   N  ND2   . ASN A 1 1479 ? 189.836 242.829 170.296 1.00 20.72 ? 1479 ASN A ND2   1 
ATOM   201   N  N     . TYR A 1 1480 ? 191.215 239.731 172.071 1.00 17.89 ? 1480 TYR A N     1 
ATOM   202   C  CA    . TYR A 1 1480 ? 190.413 239.321 173.220 1.00 20.18 ? 1480 TYR A CA    1 
ATOM   203   C  C     . TYR A 1 1480 ? 190.124 240.562 174.060 1.00 20.59 ? 1480 TYR A C     1 
ATOM   204   O  O     . TYR A 1 1480 ? 190.963 240.988 174.860 1.00 19.26 ? 1480 TYR A O     1 
ATOM   205   C  CB    . TYR A 1 1480 ? 191.130 238.238 174.025 1.00 16.84 ? 1480 TYR A CB    1 
ATOM   206   C  CG    . TYR A 1 1480 ? 190.465 237.888 175.338 1.00 13.44 ? 1480 TYR A CG    1 
ATOM   207   C  CD1   . TYR A 1 1480 ? 189.377 237.025 175.377 1.00 16.30 ? 1480 TYR A CD1   1 
ATOM   208   C  CD2   . TYR A 1 1480 ? 190.934 238.402 176.539 1.00 13.40 ? 1480 TYR A CD2   1 
ATOM   209   C  CE1   . TYR A 1 1480 ? 188.766 236.695 176.573 1.00 14.28 ? 1480 TYR A CE1   1 
ATOM   210   C  CE2   . TYR A 1 1480 ? 190.328 238.078 177.741 1.00 15.34 ? 1480 TYR A CE2   1 
ATOM   211   C  CZ    . TYR A 1 1480 ? 189.246 237.224 177.750 1.00 16.43 ? 1480 TYR A CZ    1 
ATOM   212   O  OH    . TYR A 1 1480 ? 188.641 236.895 178.941 1.00 20.91 ? 1480 TYR A OH    1 
ATOM   213   N  N     . GLN A 1 1481 ? 188.939 241.143 173.861 1.00 18.23 ? 1481 GLN A N     1 
ATOM   214   C  CA    . GLN A 1 1481 ? 188.460 242.289 174.639 1.00 19.36 ? 1481 GLN A CA    1 
ATOM   215   C  C     . GLN A 1 1481 ? 189.420 243.475 174.580 1.00 19.60 ? 1481 GLN A C     1 
ATOM   216   O  O     . GLN A 1 1481 ? 189.574 244.206 175.561 1.00 26.47 ? 1481 GLN A O     1 
ATOM   217   C  CB    . GLN A 1 1481 ? 188.195 241.898 176.096 1.00 22.87 ? 1481 GLN A CB    1 
ATOM   218   C  CG    . GLN A 1 1481 ? 187.376 240.633 176.264 1.00 17.83 ? 1481 GLN A CG    1 
ATOM   219   C  CD    . GLN A 1 1481 ? 187.361 240.145 177.695 1.00 18.21 ? 1481 GLN A CD    1 
ATOM   220   O  OE1   . GLN A 1 1481 ? 187.979 240.745 178.571 1.00 23.08 ? 1481 GLN A OE1   1 
ATOM   221   N  NE2   . GLN A 1 1481 ? 186.651 239.050 177.942 1.00 24.98 ? 1481 GLN A NE2   1 
ATOM   222   N  N     . ASN A 1 1482 ? 190.069 243.671 173.430 1.00 15.25 ? 1482 ASN A N     1 
ATOM   223   C  CA    . ASN A 1 1482 ? 190.989 244.791 173.211 1.00 17.77 ? 1482 ASN A CA    1 
ATOM   224   C  C     . ASN A 1 1482 ? 192.112 244.820 174.244 1.00 19.71 ? 1482 ASN A C     1 
ATOM   225   O  O     . ASN A 1 1482 ? 192.604 245.889 174.612 1.00 25.71 ? 1482 ASN A O     1 
ATOM   226   C  CB    . ASN A 1 1482 ? 190.244 246.129 173.195 1.00 20.52 ? 1482 ASN A CB    1 
ATOM   227   C  CG    . ASN A 1 1482 ? 189.254 246.232 172.052 1.00 29.09 ? 1482 ASN A CG    1 
ATOM   228   O  OD1   . ASN A 1 1482 ? 189.182 245.350 171.195 1.00 24.92 ? 1482 ASN A OD1   1 
ATOM   229   N  ND2   . ASN A 1 1482 ? 188.482 247.311 172.034 1.00 27.57 ? 1482 ASN A ND2   1 
ATOM   230   N  N     . LYS A 1 1483 ? 192.529 243.647 174.718 1.00 18.97 ? 1483 LYS A N     1 
ATOM   231   C  CA    . LYS A 1 1483 ? 193.621 243.539 175.673 1.00 18.04 ? 1483 LYS A CA    1 
ATOM   232   C  C     . LYS A 1 1483 ? 194.858 242.862 175.106 1.00 25.05 ? 1483 LYS A C     1 
ATOM   233   O  O     . LYS A 1 1483 ? 195.973 243.247 175.464 1.00 24.52 ? 1483 LYS A O     1 
ATOM   234   C  CB    . LYS A 1 1483 ? 193.171 242.766 176.919 1.00 17.46 ? 1483 LYS A CB    1 
ATOM   235   C  CG    . LYS A 1 1483 ? 191.950 243.336 177.623 1.00 24.86 ? 1483 LYS A CG    1 
ATOM   236   C  CD    . LYS A 1 1483 ? 191.259 242.270 178.466 1.00 25.37 ? 1483 LYS A CD    1 
ATOM   237   C  CE    . LYS A 1 1483 ? 190.254 242.878 179.431 1.00 24.38 ? 1483 LYS A CE    1 
ATOM   238   N  NZ    . LYS A 1 1483 ? 190.912 243.461 180.632 1.00 22.19 ? 1483 LYS A NZ    1 
ATOM   239   N  N     . CYS A 1 1484 ? 194.692 241.876 174.237 1.00 19.73 ? 1484 CYS A N     1 
ATOM   240   C  CA    . CYS A 1 1484 ? 195.803 241.094 173.705 1.00 16.99 ? 1484 CYS A CA    1 
ATOM   241   C  C     . CYS A 1 1484 ? 195.310 240.371 172.457 1.00 20.13 ? 1484 CYS A C     1 
ATOM   242   O  O     . CYS A 1 1484 ? 194.197 240.616 171.976 1.00 21.43 ? 1484 CYS A O     1 
ATOM   243   C  CB    . CYS A 1 1484 ? 196.349 240.128 174.757 1.00 14.22 ? 1484 CYS A CB    1 
ATOM   244   S  SG    . CYS A 1 1484 ? 195.199 238.823 175.225 1.00 42.47 ? 1484 CYS A SG    1 
ATOM   245   N  N     . ARG A 1 1485 ? 196.142 239.477 171.928 1.00 21.25 ? 1485 ARG A N     1 
ATOM   246   C  CA    . ARG A 1 1485 ? 195.821 238.718 170.723 1.00 17.36 ? 1485 ARG A CA    1 
ATOM   247   C  C     . ARG A 1 1485 ? 196.073 237.241 170.993 1.00 20.94 ? 1485 ARG A C     1 
ATOM   248   O  O     . ARG A 1 1485 ? 197.176 236.743 170.749 1.00 35.19 ? 1485 ARG A O     1 
ATOM   249   C  CB    . ARG A 1 1485 ? 196.643 239.202 169.529 1.00 17.47 ? 1485 ARG A CB    1 
ATOM   250   C  CG    . ARG A 1 1485 ? 196.458 240.672 169.206 1.00 20.08 ? 1485 ARG A CG    1 
ATOM   251   C  CD    . ARG A 1 1485 ? 195.389 240.866 168.143 1.00 21.80 ? 1485 ARG A CD    1 
ATOM   252   N  NE    . ARG A 1 1485 ? 195.665 240.106 166.931 1.00 17.82 ? 1485 ARG A NE    1 
ATOM   253   C  CZ    . ARG A 1 1485 ? 196.633 240.388 166.068 1.00 24.37 ? 1485 ARG A CZ    1 
ATOM   254   N  NH1   . ARG A 1 1485 ? 197.437 241.425 166.243 1.00 28.82 ? 1485 ARG A NH1   1 
ATOM   255   N  NH2   . ARG A 1 1485 ? 196.795 239.615 164.999 1.00 21.81 ? 1485 ARG A NH2   1 
ATOM   256   N  N     . LEU A 1 1486 ? 195.046 236.542 171.469 1.00 16.90 ? 1486 LEU A N     1 
ATOM   257   C  CA    . LEU A 1 1486 ? 195.153 235.138 171.834 1.00 14.60 ? 1486 LEU A CA    1 
ATOM   258   C  C     . LEU A 1 1486 ? 195.403 234.274 170.598 1.00 12.77 ? 1486 LEU A C     1 
ATOM   259   O  O     . LEU A 1 1486 ? 195.381 234.744 169.460 1.00 17.09 ? 1486 LEU A O     1 
ATOM   260   C  CB    . LEU A 1 1486 ? 193.886 234.679 172.549 1.00 13.15 ? 1486 LEU A CB    1 
ATOM   261   C  CG    . LEU A 1 1486 ? 193.638 235.211 173.959 1.00 9.95  ? 1486 LEU A CG    1 
ATOM   262   C  CD1   . LEU A 1 1486 ? 192.594 234.365 174.650 1.00 10.93 ? 1486 LEU A CD1   1 
ATOM   263   C  CD2   . LEU A 1 1486 ? 194.917 235.258 174.771 1.00 11.64 ? 1486 LEU A CD2   1 
ATOM   264   N  N     . ILE A 1 1487 ? 195.633 232.986 170.836 1.00 11.25 ? 1487 ILE A N     1 
ATOM   265   C  CA    . ILE A 1 1487 ? 195.955 232.025 169.785 1.00 13.94 ? 1487 ILE A CA    1 
ATOM   266   C  C     . ILE A 1 1487 ? 194.832 231.002 169.686 1.00 11.65 ? 1487 ILE A C     1 
ATOM   267   O  O     . ILE A 1 1487 ? 194.535 230.297 170.658 1.00 18.06 ? 1487 ILE A O     1 
ATOM   268   C  CB    . ILE A 1 1487 ? 197.303 231.336 170.050 1.00 12.50 ? 1487 ILE A CB    1 
ATOM   269   C  CG1   . ILE A 1 1487 ? 198.448 232.333 169.890 1.00 12.93 ? 1487 ILE A CG1   1 
ATOM   270   C  CG2   . ILE A 1 1487 ? 197.489 230.130 169.144 1.00 10.71 ? 1487 ILE A CG2   1 
ATOM   271   C  CD1   . ILE A 1 1487 ? 199.772 231.808 170.345 1.00 11.49 ? 1487 ILE A CD1   1 
ATOM   272   N  N     . ARG A 1 1488 ? 194.211 230.916 168.511 1.00 12.34 ? 1488 ARG A N     1 
ATOM   273   C  CA    . ARG A 1 1488 ? 193.281 229.843 168.204 1.00 14.96 ? 1488 ARG A CA    1 
ATOM   274   C  C     . ARG A 1 1488 ? 194.004 228.750 167.417 1.00 16.31 ? 1488 ARG A C     1 
ATOM   275   O  O     . ARG A 1 1488 ? 195.231 228.755 167.280 1.00 15.51 ? 1488 ARG A O     1 
ATOM   276   C  CB    . ARG A 1 1488 ? 192.064 230.341 167.418 1.00 15.81 ? 1488 ARG A CB    1 
ATOM   277   C  CG    . ARG A 1 1488 ? 192.393 230.812 166.011 1.00 27.26 ? 1488 ARG A CG    1 
ATOM   278   C  CD    . ARG A 1 1488 ? 191.186 231.383 165.272 1.00 28.09 ? 1488 ARG A CD    1 
ATOM   279   N  NE    . ARG A 1 1488 ? 190.663 232.641 165.782 1.00 28.35 ? 1488 ARG A NE    1 
ATOM   280   C  CZ    . ARG A 1 1488 ? 189.537 233.191 165.347 1.00 33.21 ? 1488 ARG A CZ    1 
ATOM   281   N  NH1   . ARG A 1 1488 ? 188.805 232.618 164.405 1.00 30.49 ? 1488 ARG A NH1   1 
ATOM   282   N  NH2   . ARG A 1 1488 ? 189.134 234.344 165.868 1.00 33.14 ? 1488 ARG A NH2   1 
ATOM   283   N  N     . GLY A 1 1489 ? 193.234 227.806 166.884 1.00 14.90 ? 1489 GLY A N     1 
ATOM   284   C  CA    . GLY A 1 1489 ? 193.784 226.781 166.011 1.00 15.69 ? 1489 GLY A CA    1 
ATOM   285   C  C     . GLY A 1 1489 ? 194.711 225.804 166.695 1.00 14.63 ? 1489 GLY A C     1 
ATOM   286   O  O     . GLY A 1 1489 ? 195.695 225.367 166.089 1.00 18.63 ? 1489 GLY A O     1 
ATOM   287   N  N     . TRP A 1 1490 ? 194.416 225.439 167.942 1.00 11.14 ? 1490 TRP A N     1 
ATOM   288   C  CA    . TRP A 1 1490 ? 195.247 224.469 168.647 1.00 11.84 ? 1490 TRP A CA    1 
ATOM   289   C  C     . TRP A 1 1490 ? 195.194 223.100 167.987 1.00 19.18 ? 1490 TRP A C     1 
ATOM   290   O  O     . TRP A 1 1490 ? 196.207 222.394 167.925 1.00 18.71 ? 1490 TRP A O     1 
ATOM   291   C  CB    . TRP A 1 1490 ? 194.821 224.382 170.107 1.00 11.07 ? 1490 TRP A CB    1 
ATOM   292   C  CG    . TRP A 1 1490 ? 195.085 225.637 170.831 1.00 11.13 ? 1490 TRP A CG    1 
ATOM   293   C  CD1   . TRP A 1 1490 ? 194.187 226.600 171.178 1.00 9.47  ? 1490 TRP A CD1   1 
ATOM   294   C  CD2   . TRP A 1 1490 ? 196.359 226.094 171.268 1.00 14.35 ? 1490 TRP A CD2   1 
ATOM   295   N  NE1   . TRP A 1 1490 ? 194.829 227.624 171.832 1.00 6.58  ? 1490 TRP A NE1   1 
ATOM   296   C  CE2   . TRP A 1 1490 ? 196.166 227.336 171.895 1.00 7.68  ? 1490 TRP A CE2   1 
ATOM   297   C  CE3   . TRP A 1 1490 ? 197.650 225.564 171.199 1.00 11.85 ? 1490 TRP A CE3   1 
ATOM   298   C  CZ2   . TRP A 1 1490 ? 197.213 228.053 172.448 1.00 8.25  ? 1490 TRP A CZ2   1 
ATOM   299   C  CZ3   . TRP A 1 1490 ? 198.682 226.276 171.744 1.00 10.92 ? 1490 TRP A CZ3   1 
ATOM   300   C  CH2   . TRP A 1 1490 ? 198.461 227.504 172.361 1.00 6.49  ? 1490 TRP A CH2   1 
ATOM   301   N  N     . ASP A 1 1491 ? 194.018 222.698 167.502 1.00 15.33 ? 1491 ASP A N     1 
ATOM   302   C  CA    . ASP A 1 1491 ? 193.923 221.429 166.792 1.00 15.57 ? 1491 ASP A CA    1 
ATOM   303   C  C     . ASP A 1 1491 ? 194.772 221.447 165.527 1.00 18.30 ? 1491 ASP A C     1 
ATOM   304   O  O     . ASP A 1 1491 ? 195.466 220.471 165.225 1.00 19.96 ? 1491 ASP A O     1 
ATOM   305   C  CB    . ASP A 1 1491 ? 192.462 221.120 166.466 1.00 18.07 ? 1491 ASP A CB    1 
ATOM   306   C  CG    . ASP A 1 1491 ? 191.738 220.457 167.621 1.00 27.14 ? 1491 ASP A CG    1 
ATOM   307   O  OD1   . ASP A 1 1491 ? 192.177 219.372 168.056 1.00 31.16 ? 1491 ASP A OD1   1 
ATOM   308   O  OD2   . ASP A 1 1491 ? 190.730 221.021 168.096 1.00 31.37 ? 1491 ASP A OD2   1 
ATOM   309   N  N     . ASP A 1 1492 ? 194.739 222.554 164.781 1.00 18.80 ? 1492 ASP A N     1 
ATOM   310   C  CA    . ASP A 1 1492 ? 195.557 222.653 163.576 1.00 17.93 ? 1492 ASP A CA    1 
ATOM   311   C  C     . ASP A 1 1492 ? 197.043 222.624 163.911 1.00 20.36 ? 1492 ASP A C     1 
ATOM   312   O  O     . ASP A 1 1492 ? 197.828 221.964 163.221 1.00 21.47 ? 1492 ASP A O     1 
ATOM   313   C  CB    . ASP A 1 1492 ? 195.205 223.927 162.807 1.00 17.72 ? 1492 ASP A CB    1 
ATOM   314   C  CG    . ASP A 1 1492 ? 193.770 223.938 162.329 1.00 26.87 ? 1492 ASP A CG    1 
ATOM   315   O  OD1   . ASP A 1 1492 ? 193.389 223.025 161.568 1.00 28.56 ? 1492 ASP A OD1   1 
ATOM   316   O  OD2   . ASP A 1 1492 ? 193.022 224.862 162.711 1.00 32.01 ? 1492 ASP A OD2   1 
ATOM   317   N  N     . LEU A 1 1493 ? 197.447 223.339 164.963 1.00 21.33 ? 1493 LEU A N     1 
ATOM   318   C  CA    . LEU A 1 1493 ? 198.850 223.355 165.369 1.00 13.89 ? 1493 LEU A CA    1 
ATOM   319   C  C     . LEU A 1 1493 ? 199.322 221.974 165.806 1.00 14.54 ? 1493 LEU A C     1 
ATOM   320   O  O     . LEU A 1 1493 ? 200.394 221.513 165.400 1.00 18.27 ? 1493 LEU A O     1 
ATOM   321   C  CB    . LEU A 1 1493 ? 199.050 224.369 166.496 1.00 16.99 ? 1493 LEU A CB    1 
ATOM   322   C  CG    . LEU A 1 1493 ? 200.473 224.758 166.905 1.00 13.36 ? 1493 LEU A CG    1 
ATOM   323   C  CD1   . LEU A 1 1493 ? 201.194 225.511 165.815 1.00 16.59 ? 1493 LEU A CD1   1 
ATOM   324   C  CD2   . LEU A 1 1493 ? 200.427 225.582 168.178 1.00 11.50 ? 1493 LEU A CD2   1 
ATOM   325   N  N     . PHE A 1 1494 ? 198.530 221.296 166.637 1.00 16.05 ? 1494 PHE A N     1 
ATOM   326   C  CA    . PHE A 1 1494 ? 198.988 220.043 167.229 1.00 15.92 ? 1494 PHE A CA    1 
ATOM   327   C  C     . PHE A 1 1494 ? 199.017 218.914 166.206 1.00 19.11 ? 1494 PHE A C     1 
ATOM   328   O  O     . PHE A 1 1494 ? 199.978 218.138 166.163 1.00 18.39 ? 1494 PHE A O     1 
ATOM   329   C  CB    . PHE A 1 1494 ? 198.108 219.680 168.422 1.00 14.24 ? 1494 PHE A CB    1 
ATOM   330   C  CG    . PHE A 1 1494 ? 198.377 220.512 169.641 1.00 13.35 ? 1494 PHE A CG    1 
ATOM   331   C  CD1   . PHE A 1 1494 ? 199.644 221.013 169.882 1.00 15.80 ? 1494 PHE A CD1   1 
ATOM   332   C  CD2   . PHE A 1 1494 ? 197.367 220.801 170.538 1.00 15.51 ? 1494 PHE A CD2   1 
ATOM   333   C  CE1   . PHE A 1 1494 ? 199.900 221.783 170.998 1.00 9.72  ? 1494 PHE A CE1   1 
ATOM   334   C  CE2   . PHE A 1 1494 ? 197.618 221.571 171.658 1.00 16.67 ? 1494 PHE A CE2   1 
ATOM   335   C  CZ    . PHE A 1 1494 ? 198.886 222.060 171.887 1.00 11.99 ? 1494 PHE A CZ    1 
ATOM   336   N  N     . ASN A 1 1495 ? 197.975 218.800 165.379 1.00 17.86 ? 1495 ASN A N     1 
ATOM   337   C  CA    . ASN A 1 1495 ? 197.967 217.758 164.356 1.00 19.36 ? 1495 ASN A CA    1 
ATOM   338   C  C     . ASN A 1 1495 ? 199.064 217.984 163.325 1.00 15.26 ? 1495 ASN A C     1 
ATOM   339   O  O     . ASN A 1 1495 ? 199.698 217.026 162.868 1.00 17.04 ? 1495 ASN A O     1 
ATOM   340   C  CB    . ASN A 1 1495 ? 196.600 217.680 163.679 1.00 15.38 ? 1495 ASN A CB    1 
ATOM   341   C  CG    . ASN A 1 1495 ? 195.461 217.630 164.671 1.00 19.26 ? 1495 ASN A CG    1 
ATOM   342   O  OD1   . ASN A 1 1495 ? 195.628 217.178 165.803 1.00 26.86 ? 1495 ASN A OD1   1 
ATOM   343   N  ND2   . ASN A 1 1495 ? 194.291 218.094 164.253 1.00 21.14 ? 1495 ASN A ND2   1 
ATOM   344   N  N     . LYS A 1 1496 ? 199.300 219.240 162.939 1.00 17.34 ? 1496 LYS A N     1 
ATOM   345   C  CA    . LYS A 1 1496 ? 200.362 219.522 161.978 1.00 15.65 ? 1496 LYS A CA    1 
ATOM   346   C  C     . LYS A 1 1496 ? 201.721 219.113 162.528 1.00 18.71 ? 1496 LYS A C     1 
ATOM   347   O  O     . LYS A 1 1496 ? 202.524 218.497 161.819 1.00 21.95 ? 1496 LYS A O     1 
ATOM   348   C  CB    . LYS A 1 1496 ? 200.360 221.004 161.606 1.00 18.19 ? 1496 LYS A CB    1 
ATOM   349   C  CG    . LYS A 1 1496 ? 201.402 221.387 160.568 1.00 19.28 ? 1496 LYS A CG    1 
ATOM   350   C  CD    . LYS A 1 1496 ? 201.165 220.674 159.246 1.00 21.64 ? 1496 LYS A CD    1 
ATOM   351   C  CE    . LYS A 1 1496 ? 199.867 221.117 158.599 1.00 23.20 ? 1496 LYS A CE    1 
ATOM   352   N  NZ    . LYS A 1 1496 ? 199.934 222.533 158.146 1.00 23.95 ? 1496 LYS A NZ    1 
ATOM   353   N  N     . VAL A 1 1497 ? 201.992 219.436 163.795 1.00 20.93 ? 1497 VAL A N     1 
ATOM   354   C  CA    . VAL A 1 1497 ? 203.261 219.048 164.403 1.00 14.33 ? 1497 VAL A CA    1 
ATOM   355   C  C     . VAL A 1 1497 ? 203.364 217.530 164.495 1.00 13.41 ? 1497 VAL A C     1 
ATOM   356   O  O     . VAL A 1 1497 ? 204.399 216.944 164.160 1.00 14.73 ? 1497 VAL A O     1 
ATOM   357   C  CB    . VAL A 1 1497 ? 203.422 219.712 165.784 1.00 15.55 ? 1497 VAL A CB    1 
ATOM   358   C  CG1   . VAL A 1 1497 ? 204.562 219.074 166.551 1.00 13.01 ? 1497 VAL A CG1   1 
ATOM   359   C  CG2   . VAL A 1 1497 ? 203.658 221.199 165.632 1.00 15.54 ? 1497 VAL A CG2   1 
ATOM   360   N  N     . LYS A 1 1498 ? 202.288 216.868 164.935 1.00 13.88 ? 1498 LYS A N     1 
ATOM   361   C  CA    . LYS A 1 1498 ? 202.307 215.411 165.037 1.00 15.82 ? 1498 LYS A CA    1 
ATOM   362   C  C     . LYS A 1 1498 ? 202.537 214.764 163.678 1.00 15.72 ? 1498 LYS A C     1 
ATOM   363   O  O     . LYS A 1 1498 ? 203.270 213.776 163.570 1.00 16.61 ? 1498 LYS A O     1 
ATOM   364   C  CB    . LYS A 1 1498 ? 201.003 214.894 165.647 1.00 16.07 ? 1498 LYS A CB    1 
ATOM   365   C  CG    . LYS A 1 1498 ? 200.794 215.204 167.119 1.00 16.84 ? 1498 LYS A CG    1 
ATOM   366   C  CD    . LYS A 1 1498 ? 199.404 214.753 167.554 1.00 23.95 ? 1498 LYS A CD    1 
ATOM   367   C  CE    . LYS A 1 1498 ? 198.756 215.716 168.536 1.00 18.30 ? 1498 LYS A CE    1 
ATOM   368   N  NZ    . LYS A 1 1498 ? 199.741 216.389 169.417 1.00 22.93 ? 1498 LYS A NZ    1 
ATOM   369   N  N     . GLU A 1 1499 ? 201.915 215.309 162.630 1.00 16.65 ? 1499 GLU A N     1 
ATOM   370   C  CA    . GLU A 1 1499 ? 202.061 214.729 161.299 1.00 16.38 ? 1499 GLU A CA    1 
ATOM   371   C  C     . GLU A 1 1499 ? 203.511 214.770 160.831 1.00 20.77 ? 1499 GLU A C     1 
ATOM   372   O  O     . GLU A 1 1499 ? 204.022 213.779 160.296 1.00 27.50 ? 1499 GLU A O     1 
ATOM   373   C  CB    . GLU A 1 1499 ? 201.147 215.456 160.314 1.00 15.68 ? 1499 GLU A CB    1 
ATOM   374   C  CG    . GLU A 1 1499 ? 201.008 214.789 158.954 1.00 26.35 ? 1499 GLU A CG    1 
ATOM   375   C  CD    . GLU A 1 1499 ? 202.128 215.151 157.999 1.00 33.58 ? 1499 GLU A CD    1 
ATOM   376   O  OE1   . GLU A 1 1499 ? 202.682 216.262 158.130 1.00 32.69 ? 1499 GLU A OE1   1 
ATOM   377   O  OE2   . GLU A 1 1499 ? 202.449 214.328 157.118 1.00 39.69 ? 1499 GLU A OE2   1 
ATOM   378   N  N     . HIS A 1 1500 ? 204.193 215.900 161.029 1.00 17.29 ? 1500 HIS A N     1 
ATOM   379   C  CA    . HIS A 1 1500 ? 205.597 215.976 160.646 1.00 16.37 ? 1500 HIS A CA    1 
ATOM   380   C  C     . HIS A 1 1500 ? 206.476 215.123 161.553 1.00 19.42 ? 1500 HIS A C     1 
ATOM   381   O  O     . HIS A 1 1500 ? 207.475 214.562 161.091 1.00 18.13 ? 1500 HIS A O     1 
ATOM   382   C  CB    . HIS A 1 1500 ? 206.077 217.428 160.657 1.00 15.95 ? 1500 HIS A CB    1 
ATOM   383   C  CG    . HIS A 1 1500 ? 205.400 218.295 159.642 1.00 21.08 ? 1500 HIS A CG    1 
ATOM   384   N  ND1   . HIS A 1 1500 ? 205.693 218.233 158.298 1.00 24.39 ? 1500 HIS A ND1   1 
ATOM   385   C  CD2   . HIS A 1 1500 ? 204.465 219.264 159.777 1.00 22.83 ? 1500 HIS A CD2   1 
ATOM   386   C  CE1   . HIS A 1 1500 ? 204.958 219.114 157.646 1.00 26.63 ? 1500 HIS A CE1   1 
ATOM   387   N  NE2   . HIS A 1 1500 ? 204.204 219.754 158.521 1.00 23.87 ? 1500 HIS A NE2   1 
ATOM   388   N  N     . ILE A 1 1501 ? 206.128 215.020 162.838 1.00 22.01 ? 1501 ILE A N     1 
ATOM   389   C  CA    . ILE A 1 1501 ? 206.903 214.190 163.756 1.00 16.17 ? 1501 ILE A CA    1 
ATOM   390   C  C     . ILE A 1 1501 ? 206.825 212.726 163.341 1.00 21.88 ? 1501 ILE A C     1 
ATOM   391   O  O     . ILE A 1 1501 ? 207.833 212.008 163.348 1.00 25.84 ? 1501 ILE A O     1 
ATOM   392   C  CB    . ILE A 1 1501 ? 206.425 214.404 165.204 1.00 17.81 ? 1501 ILE A CB    1 
ATOM   393   C  CG1   . ILE A 1 1501 ? 206.883 215.771 165.715 1.00 17.75 ? 1501 ILE A CG1   1 
ATOM   394   C  CG2   . ILE A 1 1501 ? 206.947 213.307 166.119 1.00 15.45 ? 1501 ILE A CG2   1 
ATOM   395   C  CD1   . ILE A 1 1501 ? 206.512 216.047 167.152 1.00 13.37 ? 1501 ILE A CD1   1 
ATOM   396   N  N     . ASN A 1 1502 ? 205.630 212.260 162.972 1.00 23.37 ? 1502 ASN A N     1 
ATOM   397   C  CA    . ASN A 1 1502 ? 205.494 210.895 162.477 1.00 21.43 ? 1502 ASN A CA    1 
ATOM   398   C  C     . ASN A 1 1502 ? 206.263 210.698 161.176 1.00 24.02 ? 1502 ASN A C     1 
ATOM   399   O  O     . ASN A 1 1502 ? 206.947 209.683 161.000 1.00 27.03 ? 1502 ASN A O     1 
ATOM   400   C  CB    . ASN A 1 1502 ? 204.017 210.548 162.281 1.00 18.68 ? 1502 ASN A CB    1 
ATOM   401   C  CG    . ASN A 1 1502 ? 203.202 210.752 163.539 1.00 24.55 ? 1502 ASN A CG    1 
ATOM   402   O  OD1   . ASN A 1 1502 ? 203.701 210.583 164.650 1.00 25.26 ? 1502 ASN A OD1   1 
ATOM   403   N  ND2   . ASN A 1 1502 ? 201.936 211.119 163.370 1.00 22.56 ? 1502 ASN A ND2   1 
ATOM   404   N  N     . SER A 1 1503 ? 206.166 211.660 160.253 1.00 19.19 ? 1503 SER A N     1 
ATOM   405   C  CA    . SER A 1 1503 ? 206.852 211.527 158.971 1.00 20.11 ? 1503 SER A CA    1 
ATOM   406   C  C     . SER A 1 1503 ? 208.364 211.487 159.155 1.00 26.76 ? 1503 SER A C     1 
ATOM   407   O  O     . SER A 1 1503 ? 209.057 210.707 158.490 1.00 33.17 ? 1503 SER A O     1 
ATOM   408   C  CB    . SER A 1 1503 ? 206.456 212.669 158.037 1.00 19.62 ? 1503 SER A CB    1 
ATOM   409   O  OG    . SER A 1 1503 ? 206.967 213.906 158.496 1.00 28.75 ? 1503 SER A OG    1 
ATOM   410   N  N     . VAL A 1 1504 ? 208.895 212.323 160.049 1.00 26.60 ? 1504 VAL A N     1 
ATOM   411   C  CA    . VAL A 1 1504 ? 210.322 212.274 160.355 1.00 26.03 ? 1504 VAL A CA    1 
ATOM   412   C  C     . VAL A 1 1504 ? 210.686 210.932 160.976 1.00 26.05 ? 1504 VAL A C     1 
ATOM   413   O  O     . VAL A 1 1504 ? 211.711 210.331 160.637 1.00 30.49 ? 1504 VAL A O     1 
ATOM   414   C  CB    . VAL A 1 1504 ? 210.714 213.451 161.269 1.00 22.86 ? 1504 VAL A CB    1 
ATOM   415   C  CG1   . VAL A 1 1504 ? 212.062 213.198 161.923 1.00 24.11 ? 1504 VAL A CG1   1 
ATOM   416   C  CG2   . VAL A 1 1504 ? 210.743 214.746 160.479 1.00 20.23 ? 1504 VAL A CG2   1 
ATOM   417   N  N     . SER A 1 1505 ? 209.858 210.443 161.901 1.00 24.67 ? 1505 SER A N     1 
ATOM   418   C  CA    . SER A 1 1505 ? 210.113 209.139 162.504 1.00 27.10 ? 1505 SER A CA    1 
ATOM   419   C  C     . SER A 1 1505 ? 209.999 208.022 161.473 1.00 26.74 ? 1505 SER A C     1 
ATOM   420   O  O     . SER A 1 1505 ? 210.823 207.101 161.445 1.00 32.01 ? 1505 SER A O     1 
ATOM   421   C  CB    . SER A 1 1505 ? 209.149 208.900 163.666 1.00 20.19 ? 1505 SER A CB    1 
ATOM   422   O  OG    . SER A 1 1505 ? 209.413 209.791 164.733 1.00 29.75 ? 1505 SER A OG    1 
ATOM   423   N  N     . ALA A 1 1506 ? 208.981 208.091 160.612 1.00 27.60 ? 1506 ALA A N     1 
ATOM   424   C  CA    . ALA A 1 1506 ? 208.773 207.046 159.616 1.00 27.27 ? 1506 ALA A CA    1 
ATOM   425   C  C     . ALA A 1 1506 ? 209.881 207.003 158.576 1.00 27.89 ? 1506 ALA A C     1 
ATOM   426   O  O     . ALA A 1 1506 ? 210.235 205.916 158.110 1.00 35.10 ? 1506 ALA A O     1 
ATOM   427   C  CB    . ALA A 1 1506 ? 207.424 207.237 158.921 1.00 24.23 ? 1506 ALA A CB    1 
ATOM   428   N  N     . MET A 1 1507 ? 210.435 208.158 158.203 1.00 27.58 ? 1507 MET A N     1 
ATOM   429   C  CA    . MET A 1 1507 ? 211.459 208.188 157.165 1.00 30.16 ? 1507 MET A CA    1 
ATOM   430   C  C     . MET A 1 1507 ? 212.793 207.644 157.663 1.00 33.07 ? 1507 MET A C     1 
ATOM   431   O  O     . MET A 1 1507 ? 213.697 207.402 156.858 1.00 34.13 ? 1507 MET A O     1 
ATOM   432   C  CB    . MET A 1 1507 ? 211.615 209.612 156.632 1.00 27.29 ? 1507 MET A CB    1 
ATOM   433   C  CG    . MET A 1 1507 ? 212.252 210.574 157.610 1.00 25.56 ? 1507 MET A CG    1 
ATOM   434   S  SD    . MET A 1 1507 ? 213.031 211.992 156.823 1.00 53.56 ? 1507 MET A SD    1 
ATOM   435   C  CE    . MET A 1 1507 ? 211.663 213.150 156.843 1.00 30.51 ? 1507 MET A CE    1 
ATOM   436   N  N     . LYS A 1 1508 ? 212.942 207.451 158.977 1.00 28.53 ? 1508 LYS A N     1 
ATOM   437   C  CA    . LYS A 1 1508 ? 214.140 206.784 159.482 1.00 28.50 ? 1508 LYS A CA    1 
ATOM   438   C  C     . LYS A 1 1508 ? 214.183 205.322 159.054 1.00 32.57 ? 1508 LYS A C     1 
ATOM   439   O  O     . LYS A 1 1508 ? 215.269 204.763 158.860 1.00 32.96 ? 1508 LYS A O     1 
ATOM   440   C  CB    . LYS A 1 1508 ? 214.216 206.894 161.004 1.00 29.08 ? 1508 LYS A CB    1 
ATOM   441   C  CG    . LYS A 1 1508 ? 214.054 208.304 161.536 1.00 30.77 ? 1508 LYS A CG    1 
ATOM   442   C  CD    . LYS A 1 1508 ? 213.922 208.313 163.049 1.00 28.69 ? 1508 LYS A CD    1 
ATOM   443   C  CE    . LYS A 1 1508 ? 213.648 209.714 163.568 1.00 31.74 ? 1508 LYS A CE    1 
ATOM   444   N  NZ    . LYS A 1 1508 ? 213.445 209.728 165.043 1.00 35.82 ? 1508 LYS A NZ    1 
ATOM   445   N  N     . LEU A 1 1509 ? 213.016 204.690 158.905 1.00 33.25 ? 1509 LEU A N     1 
ATOM   446   C  CA    . LEU A 1 1509 ? 212.969 203.298 158.472 1.00 34.76 ? 1509 LEU A CA    1 
ATOM   447   C  C     . LEU A 1 1509 ? 213.472 203.136 157.044 1.00 35.22 ? 1509 LEU A C     1 
ATOM   448   O  O     . LEU A 1 1509 ? 213.978 202.066 156.686 1.00 35.53 ? 1509 LEU A O     1 
ATOM   449   C  CB    . LEU A 1 1509 ? 211.544 202.761 158.593 1.00 27.17 ? 1509 LEU A CB    1 
ATOM   450   C  CG    . LEU A 1 1509 ? 210.806 203.074 159.896 1.00 34.56 ? 1509 LEU A CG    1 
ATOM   451   C  CD1   . LEU A 1 1509 ? 209.390 202.526 159.852 1.00 30.97 ? 1509 LEU A CD1   1 
ATOM   452   C  CD2   . LEU A 1 1509 ? 211.561 202.514 161.092 1.00 32.16 ? 1509 LEU A CD2   1 
ATOM   453   N  N     . SER A 1 1510 ? 213.334 204.168 156.222 1.00 33.88 ? 1510 SER A N     1 
ATOM   454   C  CA    . SER A 1 1510 ? 213.784 204.085 154.842 1.00 33.58 ? 1510 SER A CA    1 
ATOM   455   C  C     . SER A 1 1510 ? 215.301 203.923 154.795 1.00 36.02 ? 1510 SER A C     1 
ATOM   456   O  O     . SER A 1 1510 ? 216.020 204.563 155.574 1.00 35.85 ? 1510 SER A O     1 
ATOM   457   C  CB    . SER A 1 1510 ? 213.361 205.333 154.066 1.00 32.28 ? 1510 SER A CB    1 
ATOM   458   O  OG    . SER A 1 1510 ? 214.015 206.486 154.566 1.00 37.12 ? 1510 SER A OG    1 
ATOM   459   N  N     . PRO A 1 1511 ? 215.822 203.068 153.912 1.00 39.57 ? 1511 PRO A N     1 
ATOM   460   C  CA    . PRO A 1 1511 ? 217.281 202.887 153.843 1.00 33.73 ? 1511 PRO A CA    1 
ATOM   461   C  C     . PRO A 1 1511 ? 218.036 204.141 153.437 1.00 33.71 ? 1511 PRO A C     1 
ATOM   462   O  O     . PRO A 1 1511 ? 219.212 204.285 153.789 1.00 34.27 ? 1511 PRO A O     1 
ATOM   463   C  CB    . PRO A 1 1511 ? 217.443 201.766 152.808 1.00 33.68 ? 1511 PRO A CB    1 
ATOM   464   C  CG    . PRO A 1 1511 ? 216.209 201.848 151.973 1.00 35.73 ? 1511 PRO A CG    1 
ATOM   465   C  CD    . PRO A 1 1511 ? 215.115 202.239 152.922 1.00 35.16 ? 1511 PRO A CD    1 
ATOM   466   N  N     . TYR A 1 1512 ? 217.398 205.058 152.710 1.00 31.33 ? 1512 TYR A N     1 
ATOM   467   C  CA    . TYR A 1 1512 ? 218.055 206.271 152.237 1.00 31.89 ? 1512 TYR A CA    1 
ATOM   468   C  C     . TYR A 1 1512 ? 218.072 207.383 153.281 1.00 33.39 ? 1512 TYR A C     1 
ATOM   469   O  O     . TYR A 1 1512 ? 218.266 208.552 152.926 1.00 34.01 ? 1512 TYR A O     1 
ATOM   470   C  CB    . TYR A 1 1512 ? 217.383 206.769 150.956 1.00 33.09 ? 1512 TYR A CB    1 
ATOM   471   C  CG    . TYR A 1 1512 ? 217.206 205.703 149.895 1.00 32.65 ? 1512 TYR A CG    1 
ATOM   472   C  CD1   . TYR A 1 1512 ? 218.180 204.733 149.685 1.00 37.51 ? 1512 TYR A CD1   1 
ATOM   473   C  CD2   . TYR A 1 1512 ? 216.064 205.666 149.106 1.00 33.98 ? 1512 TYR A CD2   1 
ATOM   474   C  CE1   . TYR A 1 1512 ? 218.020 203.760 148.719 1.00 36.98 ? 1512 TYR A CE1   1 
ATOM   475   C  CE2   . TYR A 1 1512 ? 215.896 204.697 148.137 1.00 34.76 ? 1512 TYR A CE2   1 
ATOM   476   C  CZ    . TYR A 1 1512 ? 216.877 203.746 147.948 1.00 37.63 ? 1512 TYR A CZ    1 
ATOM   477   O  OH    . TYR A 1 1512 ? 216.713 202.778 146.984 1.00 41.90 ? 1512 TYR A OH    1 
ATOM   478   N  N     . TYR A 1 1513 ? 217.875 207.041 154.554 1.00 33.29 ? 1513 TYR A N     1 
ATOM   479   C  CA    . TYR A 1 1513 ? 217.815 208.033 155.618 1.00 28.07 ? 1513 TYR A CA    1 
ATOM   480   C  C     . TYR A 1 1513 ? 219.192 208.542 156.031 1.00 32.72 ? 1513 TYR A C     1 
ATOM   481   O  O     . TYR A 1 1513 ? 219.280 209.584 156.690 1.00 36.18 ? 1513 TYR A O     1 
ATOM   482   C  CB    . TYR A 1 1513 ? 217.085 207.435 156.826 1.00 27.16 ? 1513 TYR A CB    1 
ATOM   483   C  CG    . TYR A 1 1513 ? 217.021 208.328 158.045 1.00 31.72 ? 1513 TYR A CG    1 
ATOM   484   C  CD1   . TYR A 1 1513 ? 216.098 209.362 158.121 1.00 31.47 ? 1513 TYR A CD1   1 
ATOM   485   C  CD2   . TYR A 1 1513 ? 217.875 208.129 159.121 1.00 28.99 ? 1513 TYR A CD2   1 
ATOM   486   C  CE1   . TYR A 1 1513 ? 216.032 210.178 159.233 1.00 32.58 ? 1513 TYR A CE1   1 
ATOM   487   C  CE2   . TYR A 1 1513 ? 217.817 208.940 160.237 1.00 33.34 ? 1513 TYR A CE2   1 
ATOM   488   C  CZ    . TYR A 1 1513 ? 216.895 209.963 160.288 1.00 36.05 ? 1513 TYR A CZ    1 
ATOM   489   O  OH    . TYR A 1 1513 ? 216.833 210.772 161.396 1.00 36.12 ? 1513 TYR A OH    1 
ATOM   490   N  N     . LYS A 1 1514 ? 220.264 207.847 155.644 1.00 33.24 ? 1514 LYS A N     1 
ATOM   491   C  CA    . LYS A 1 1514 ? 221.599 208.217 156.107 1.00 30.67 ? 1514 LYS A CA    1 
ATOM   492   C  C     . LYS A 1 1514 ? 222.035 209.571 155.556 1.00 31.38 ? 1514 LYS A C     1 
ATOM   493   O  O     . LYS A 1 1514 ? 222.671 210.357 156.267 1.00 31.15 ? 1514 LYS A O     1 
ATOM   494   C  CB    . LYS A 1 1514 ? 222.605 207.133 155.721 1.00 26.75 ? 1514 LYS A CB    1 
ATOM   495   C  CG    . LYS A 1 1514 ? 224.003 207.360 156.274 1.00 29.41 ? 1514 LYS A CG    1 
ATOM   496   C  CD    . LYS A 1 1514 ? 223.976 207.565 157.781 1.00 32.02 ? 1514 LYS A CD    1 
ATOM   497   C  CE    . LYS A 1 1514 ? 225.365 207.872 158.318 1.00 33.10 ? 1514 LYS A CE    1 
ATOM   498   N  NZ    . LYS A 1 1514 ? 225.358 208.087 159.792 1.00 29.50 ? 1514 LYS A NZ    1 
ATOM   499   N  N     . VAL A 1 1515 ? 221.711 209.859 154.294 1.00 28.70 ? 1515 VAL A N     1 
ATOM   500   C  CA    . VAL A 1 1515 ? 222.184 211.094 153.673 1.00 29.08 ? 1515 VAL A CA    1 
ATOM   501   C  C     . VAL A 1 1515 ? 221.534 212.310 154.323 1.00 32.56 ? 1515 VAL A C     1 
ATOM   502   O  O     . VAL A 1 1515 ? 222.169 213.359 154.481 1.00 30.88 ? 1515 VAL A O     1 
ATOM   503   C  CB    . VAL A 1 1515 ? 221.940 211.055 152.152 1.00 30.50 ? 1515 VAL A CB    1 
ATOM   504   C  CG1   . VAL A 1 1515 ? 220.459 210.869 151.840 1.00 28.55 ? 1515 VAL A CG1   1 
ATOM   505   C  CG2   . VAL A 1 1515 ? 222.479 212.313 151.490 1.00 27.41 ? 1515 VAL A CG2   1 
ATOM   506   N  N     . PHE A 1 1516 ? 220.266 212.190 154.718 1.00 31.47 ? 1516 PHE A N     1 
ATOM   507   C  CA    . PHE A 1 1516 ? 219.518 213.292 155.309 1.00 26.65 ? 1516 PHE A CA    1 
ATOM   508   C  C     . PHE A 1 1516 ? 219.307 213.109 156.807 1.00 30.22 ? 1516 PHE A C     1 
ATOM   509   O  O     . PHE A 1 1516 ? 218.377 213.692 157.375 1.00 29.82 ? 1516 PHE A O     1 
ATOM   510   C  CB    . PHE A 1 1516 ? 218.172 213.450 154.602 1.00 28.61 ? 1516 PHE A CB    1 
ATOM   511   C  CG    . PHE A 1 1516 ? 218.283 213.593 153.112 1.00 29.63 ? 1516 PHE A CG    1 
ATOM   512   C  CD1   . PHE A 1 1516 ? 219.235 214.429 152.554 1.00 27.99 ? 1516 PHE A CD1   1 
ATOM   513   C  CD2   . PHE A 1 1516 ? 217.439 212.887 152.271 1.00 28.11 ? 1516 PHE A CD2   1 
ATOM   514   C  CE1   . PHE A 1 1516 ? 219.339 214.562 151.182 1.00 31.24 ? 1516 PHE A CE1   1 
ATOM   515   C  CE2   . PHE A 1 1516 ? 217.539 213.015 150.901 1.00 30.37 ? 1516 PHE A CE2   1 
ATOM   516   C  CZ    . PHE A 1 1516 ? 218.491 213.854 150.355 1.00 33.57 ? 1516 PHE A CZ    1 
ATOM   517   N  N     . GLU A 1 1517 ? 220.152 212.306 157.457 1.00 33.74 ? 1517 GLU A N     1 
ATOM   518   C  CA    . GLU A 1 1517 ? 219.957 212.006 158.872 1.00 30.12 ? 1517 GLU A CA    1 
ATOM   519   C  C     . GLU A 1 1517 ? 220.093 213.256 159.731 1.00 22.85 ? 1517 GLU A C     1 
ATOM   520   O  O     . GLU A 1 1517 ? 219.262 213.511 160.609 1.00 27.06 ? 1517 GLU A O     1 
ATOM   521   C  CB    . GLU A 1 1517 ? 220.951 210.935 159.320 1.00 30.75 ? 1517 GLU A CB    1 
ATOM   522   C  CG    . GLU A 1 1517 ? 220.890 210.609 160.802 1.00 36.80 ? 1517 GLU A CG    1 
ATOM   523   C  CD    . GLU A 1 1517 ? 221.733 209.405 161.168 1.00 42.87 ? 1517 GLU A CD    1 
ATOM   524   O  OE1   . GLU A 1 1517 ? 222.953 209.428 160.897 1.00 40.14 ? 1517 GLU A OE1   1 
ATOM   525   O  OE2   . GLU A 1 1517 ? 221.178 208.437 161.729 1.00 41.55 ? 1517 GLU A OE2   1 
ATOM   526   N  N     . GLU A 1 1518 ? 221.136 214.054 159.489 1.00 25.47 ? 1518 GLU A N     1 
ATOM   527   C  CA    . GLU A 1 1518 ? 221.370 215.229 160.323 1.00 28.74 ? 1518 GLU A CA    1 
ATOM   528   C  C     . GLU A 1 1518 ? 220.250 216.251 160.171 1.00 27.18 ? 1518 GLU A C     1 
ATOM   529   O  O     . GLU A 1 1518 ? 219.782 216.823 161.163 1.00 27.18 ? 1518 GLU A O     1 
ATOM   530   C  CB    . GLU A 1 1518 ? 222.721 215.857 159.981 1.00 21.77 ? 1518 GLU A CB    1 
ATOM   531   C  CG    . GLU A 1 1518 ? 223.063 217.082 160.816 1.00 26.03 ? 1518 GLU A CG    1 
ATOM   532   C  CD    . GLU A 1 1518 ? 224.204 217.889 160.229 1.00 37.53 ? 1518 GLU A CD    1 
ATOM   533   O  OE1   . GLU A 1 1518 ? 224.079 218.348 159.075 1.00 33.74 ? 1518 GLU A OE1   1 
ATOM   534   O  OE2   . GLU A 1 1518 ? 225.228 218.064 160.923 1.00 41.61 ? 1518 GLU A OE2   1 
ATOM   535   N  N     . ASP A 1 1519 ? 219.807 216.495 158.937 1.00 28.61 ? 1519 ASP A N     1 
ATOM   536   C  CA    . ASP A 1 1519 ? 218.737 217.462 158.714 1.00 23.74 ? 1519 ASP A CA    1 
ATOM   537   C  C     . ASP A 1 1519 ? 217.423 216.983 159.322 1.00 24.84 ? 1519 ASP A C     1 
ATOM   538   O  O     . ASP A 1 1519 ? 216.679 217.777 159.909 1.00 26.92 ? 1519 ASP A O     1 
ATOM   539   C  CB    . ASP A 1 1519 ? 218.584 217.732 157.219 1.00 19.53 ? 1519 ASP A CB    1 
ATOM   540   C  CG    . ASP A 1 1519 ? 217.807 219.002 156.933 1.00 33.87 ? 1519 ASP A CG    1 
ATOM   541   O  OD1   . ASP A 1 1519 ? 218.092 220.033 157.576 1.00 35.01 ? 1519 ASP A OD1   1 
ATOM   542   O  OD2   . ASP A 1 1519 ? 216.925 218.976 156.050 1.00 35.81 ? 1519 ASP A OD2   1 
ATOM   543   N  N     . ALA A 1 1520 ? 217.119 215.691 159.187 1.00 24.82 ? 1520 ALA A N     1 
ATOM   544   C  CA    . ALA A 1 1520 ? 215.918 215.149 159.812 1.00 21.70 ? 1520 ALA A CA    1 
ATOM   545   C  C     . ALA A 1 1520 ? 216.003 215.218 161.333 1.00 22.71 ? 1520 ALA A C     1 
ATOM   546   O  O     . ALA A 1 1520 ? 215.017 215.546 162.000 1.00 24.86 ? 1520 ALA A O     1 
ATOM   547   C  CB    . ALA A 1 1520 ? 215.688 213.711 159.350 1.00 18.51 ? 1520 ALA A CB    1 
ATOM   548   N  N     . LEU A 1 1521 ? 217.173 214.907 161.898 1.00 24.74 ? 1521 LEU A N     1 
ATOM   549   C  CA    . LEU A 1 1521 ? 217.342 215.004 163.344 1.00 21.46 ? 1521 LEU A CA    1 
ATOM   550   C  C     . LEU A 1 1521 ? 217.230 216.443 163.826 1.00 20.52 ? 1521 LEU A C     1 
ATOM   551   O  O     . LEU A 1 1521 ? 216.760 216.687 164.942 1.00 22.09 ? 1521 LEU A O     1 
ATOM   552   C  CB    . LEU A 1 1521 ? 218.685 214.410 163.764 1.00 22.69 ? 1521 LEU A CB    1 
ATOM   553   C  CG    . LEU A 1 1521 ? 218.787 212.886 163.757 1.00 23.11 ? 1521 LEU A CG    1 
ATOM   554   C  CD1   . LEU A 1 1521 ? 220.183 212.447 164.164 1.00 21.57 ? 1521 LEU A CD1   1 
ATOM   555   C  CD2   . LEU A 1 1521 ? 217.739 212.275 164.671 1.00 20.95 ? 1521 LEU A CD2   1 
ATOM   556   N  N     . SER A 1 1522 ? 217.666 217.402 163.008 1.00 17.37 ? 1522 SER A N     1 
ATOM   557   C  CA    . SER A 1 1522 ? 217.467 218.805 163.348 1.00 20.82 ? 1522 SER A CA    1 
ATOM   558   C  C     . SER A 1 1522 ? 215.983 219.145 163.412 1.00 19.94 ? 1522 SER A C     1 
ATOM   559   O  O     . SER A 1 1522 ? 215.544 219.876 164.306 1.00 18.55 ? 1522 SER A O     1 
ATOM   560   C  CB    . SER A 1 1522 ? 218.179 219.697 162.332 1.00 21.00 ? 1522 SER A CB    1 
ATOM   561   O  OG    . SER A 1 1522 ? 217.337 219.982 161.229 1.00 25.19 ? 1522 SER A OG    1 
ATOM   562   N  N     . TRP A 1 1523 ? 215.197 218.621 162.469 1.00 17.48 ? 1523 TRP A N     1 
ATOM   563   C  CA    . TRP A 1 1523 ? 213.766 218.899 162.466 1.00 18.82 ? 1523 TRP A CA    1 
ATOM   564   C  C     . TRP A 1 1523 ? 213.046 218.162 163.586 1.00 20.59 ? 1523 TRP A C     1 
ATOM   565   O  O     . TRP A 1 1523 ? 212.069 218.683 164.136 1.00 23.36 ? 1523 TRP A O     1 
ATOM   566   C  CB    . TRP A 1 1523 ? 213.165 218.542 161.108 1.00 15.19 ? 1523 TRP A CB    1 
ATOM   567   C  CG    . TRP A 1 1523 ? 213.297 219.654 160.130 1.00 21.84 ? 1523 TRP A CG    1 
ATOM   568   C  CD1   . TRP A 1 1523 ? 214.174 219.731 159.090 1.00 23.91 ? 1523 TRP A CD1   1 
ATOM   569   C  CD2   . TRP A 1 1523 ? 212.548 220.873 160.117 1.00 24.20 ? 1523 TRP A CD2   1 
ATOM   570   N  NE1   . TRP A 1 1523 ? 214.009 220.916 158.420 1.00 27.31 ? 1523 TRP A NE1   1 
ATOM   571   C  CE2   . TRP A 1 1523 ? 213.016 221.637 159.031 1.00 24.98 ? 1523 TRP A CE2   1 
ATOM   572   C  CE3   . TRP A 1 1523 ? 211.522 221.389 160.914 1.00 18.74 ? 1523 TRP A CE3   1 
ATOM   573   C  CZ2   . TRP A 1 1523 ? 212.495 222.888 158.722 1.00 22.52 ? 1523 TRP A CZ2   1 
ATOM   574   C  CZ3   . TRP A 1 1523 ? 211.006 222.630 160.605 1.00 18.94 ? 1523 TRP A CZ3   1 
ATOM   575   C  CH2   . TRP A 1 1523 ? 211.493 223.366 159.518 1.00 20.00 ? 1523 TRP A CH2   1 
ATOM   576   N  N     . GLU A 1 1524 ? 213.509 216.961 163.940 1.00 18.31 ? 1524 GLU A N     1 
ATOM   577   C  CA    . GLU A 1 1524 ? 212.928 216.254 165.076 1.00 15.60 ? 1524 GLU A CA    1 
ATOM   578   C  C     . GLU A 1 1524 ? 213.091 217.062 166.357 1.00 13.24 ? 1524 GLU A C     1 
ATOM   579   O  O     . GLU A 1 1524 ? 212.172 217.127 167.180 1.00 14.44 ? 1524 GLU A O     1 
ATOM   580   C  CB    . GLU A 1 1524 ? 213.574 214.877 165.223 1.00 19.96 ? 1524 GLU A CB    1 
ATOM   581   C  CG    . GLU A 1 1524 ? 213.175 214.133 166.488 1.00 21.81 ? 1524 GLU A CG    1 
ATOM   582   C  CD    . GLU A 1 1524 ? 214.108 212.983 166.804 1.00 28.07 ? 1524 GLU A CD    1 
ATOM   583   O  OE1   . GLU A 1 1524 ? 214.869 213.085 167.789 1.00 25.76 ? 1524 GLU A OE1   1 
ATOM   584   O  OE2   . GLU A 1 1524 ? 214.081 211.975 166.066 1.00 25.71 ? 1524 GLU A OE2   1 
ATOM   585   N  N     . ASP A 1 1525 ? 214.257 217.684 166.541 1.00 17.36 ? 1525 ASP A N     1 
ATOM   586   C  CA    . ASP A 1 1525 ? 214.463 218.545 167.698 1.00 14.17 ? 1525 ASP A CA    1 
ATOM   587   C  C     . ASP A 1 1525 ? 213.545 219.762 167.659 1.00 16.55 ? 1525 ASP A C     1 
ATOM   588   O  O     . ASP A 1 1525 ? 212.936 220.120 168.673 1.00 16.46 ? 1525 ASP A O     1 
ATOM   589   C  CB    . ASP A 1 1525 ? 215.925 218.977 167.771 1.00 16.01 ? 1525 ASP A CB    1 
ATOM   590   C  CG    . ASP A 1 1525 ? 216.238 219.759 169.025 1.00 24.99 ? 1525 ASP A CG    1 
ATOM   591   O  OD1   . ASP A 1 1525 ? 216.319 219.140 170.109 1.00 28.25 ? 1525 ASP A OD1   1 
ATOM   592   O  OD2   . ASP A 1 1525 ? 216.409 220.991 168.930 1.00 26.79 ? 1525 ASP A OD2   1 
ATOM   593   N  N     . LYS A 1 1526 ? 213.435 220.411 166.498 1.00 15.25 ? 1526 LYS A N     1 
ATOM   594   C  CA    . LYS A 1 1526 ? 212.597 221.603 166.395 1.00 11.45 ? 1526 LYS A CA    1 
ATOM   595   C  C     . LYS A 1 1526 ? 211.125 221.265 166.592 1.00 14.18 ? 1526 LYS A C     1 
ATOM   596   O  O     . LYS A 1 1526 ? 210.414 221.958 167.329 1.00 18.24 ? 1526 LYS A O     1 
ATOM   597   C  CB    . LYS A 1 1526 ? 212.819 222.291 165.045 1.00 14.52 ? 1526 LYS A CB    1 
ATOM   598   C  CG    . LYS A 1 1526 ? 214.204 222.887 164.878 1.00 15.76 ? 1526 LYS A CG    1 
ATOM   599   C  CD    . LYS A 1 1526 ? 214.321 223.695 163.598 1.00 14.10 ? 1526 LYS A CD    1 
ATOM   600   C  CE    . LYS A 1 1526 ? 214.385 222.796 162.379 1.00 21.22 ? 1526 LYS A CE    1 
ATOM   601   N  NZ    . LYS A 1 1526 ? 214.611 223.566 161.126 1.00 25.79 ? 1526 LYS A NZ    1 
ATOM   602   N  N     . LEU A 1 1527 ? 210.650 220.195 165.950 1.00 10.40 ? 1527 LEU A N     1 
ATOM   603   C  CA    . LEU A 1 1527 ? 209.250 219.811 166.100 1.00 10.88 ? 1527 LEU A CA    1 
ATOM   604   C  C     . LEU A 1 1527 ? 208.940 219.405 167.534 1.00 12.44 ? 1527 LEU A C     1 
ATOM   605   O  O     . LEU A 1 1527 ? 207.861 219.712 168.054 1.00 12.50 ? 1527 LEU A O     1 
ATOM   606   C  CB    . LEU A 1 1527 ? 208.909 218.677 165.135 1.00 13.84 ? 1527 LEU A CB    1 
ATOM   607   C  CG    . LEU A 1 1527 ? 208.908 219.014 163.644 1.00 11.76 ? 1527 LEU A CG    1 
ATOM   608   C  CD1   . LEU A 1 1527 ? 209.166 217.763 162.817 1.00 17.59 ? 1527 LEU A CD1   1 
ATOM   609   C  CD2   . LEU A 1 1527 ? 207.602 219.668 163.239 1.00 14.74 ? 1527 LEU A CD2   1 
ATOM   610   N  N     . ASN A 1 1528 ? 209.870 218.707 168.187 1.00 14.13 ? 1528 ASN A N     1 
ATOM   611   C  CA    . ASN A 1 1528 ? 209.675 218.351 169.589 1.00 9.47  ? 1528 ASN A CA    1 
ATOM   612   C  C     . ASN A 1 1528 ? 209.640 219.588 170.477 1.00 10.44 ? 1528 ASN A C     1 
ATOM   613   O  O     . ASN A 1 1528 ? 208.893 219.621 171.462 1.00 10.79 ? 1528 ASN A O     1 
ATOM   614   C  CB    . ASN A 1 1528 ? 210.775 217.401 170.050 1.00 11.99 ? 1528 ASN A CB    1 
ATOM   615   C  CG    . ASN A 1 1528 ? 210.481 215.959 169.701 1.00 10.33 ? 1528 ASN A CG    1 
ATOM   616   O  OD1   . ASN A 1 1528 ? 209.335 215.519 169.744 1.00 17.74 ? 1528 ASN A OD1   1 
ATOM   617   N  ND2   . ASN A 1 1528 ? 211.520 215.213 169.351 1.00 12.43 ? 1528 ASN A ND2   1 
ATOM   618   N  N     . ARG A 1 1529 ? 210.440 220.603 170.149 1.00 10.26 ? 1529 ARG A N     1 
ATOM   619   C  CA    . ARG A 1 1529 ? 210.431 221.839 170.925 1.00 8.91  ? 1529 ARG A CA    1 
ATOM   620   C  C     . ARG A 1 1529 ? 209.135 222.613 170.719 1.00 9.16  ? 1529 ARG A C     1 
ATOM   621   O  O     . ARG A 1 1529 ? 208.635 223.253 171.650 1.00 12.26 ? 1529 ARG A O     1 
ATOM   622   C  CB    . ARG A 1 1529 ? 211.643 222.693 170.555 1.00 10.19 ? 1529 ARG A CB    1 
ATOM   623   C  CG    . ARG A 1 1529 ? 212.921 222.257 171.244 1.00 10.35 ? 1529 ARG A CG    1 
ATOM   624   C  CD    . ARG A 1 1529 ? 214.160 222.792 170.547 1.00 12.03 ? 1529 ARG A CD    1 
ATOM   625   N  NE    . ARG A 1 1529 ? 214.091 224.230 170.318 1.00 14.92 ? 1529 ARG A NE    1 
ATOM   626   C  CZ    . ARG A 1 1529 ? 214.299 224.812 169.145 1.00 16.49 ? 1529 ARG A CZ    1 
ATOM   627   N  NH1   . ARG A 1 1529 ? 214.590 224.105 168.065 1.00 13.39 ? 1529 ARG A NH1   1 
ATOM   628   N  NH2   . ARG A 1 1529 ? 214.216 226.135 169.054 1.00 19.26 ? 1529 ARG A NH2   1 
ATOM   629   N  N     . ILE A 1 1530 ? 208.579 222.568 169.506 1.00 10.81 ? 1530 ILE A N     1 
ATOM   630   C  CA    . ILE A 1 1530 ? 207.286 223.198 169.253 1.00 7.03  ? 1530 ILE A CA    1 
ATOM   631   C  C     . ILE A 1 1530 ? 206.197 222.525 170.079 1.00 10.18 ? 1530 ILE A C     1 
ATOM   632   O  O     . ILE A 1 1530 ? 205.325 223.194 170.645 1.00 16.30 ? 1530 ILE A O     1 
ATOM   633   C  CB    . ILE A 1 1530 ? 206.957 223.166 167.748 1.00 10.65 ? 1530 ILE A CB    1 
ATOM   634   C  CG1   . ILE A 1 1530 ? 208.018 223.921 166.949 1.00 13.21 ? 1530 ILE A CG1   1 
ATOM   635   C  CG2   . ILE A 1 1530 ? 205.583 223.761 167.486 1.00 10.42 ? 1530 ILE A CG2   1 
ATOM   636   C  CD1   . ILE A 1 1530 ? 207.778 223.913 165.456 1.00 12.56 ? 1530 ILE A CD1   1 
ATOM   637   N  N     . MET A 1 1531 ? 206.228 221.192 170.156 1.00 9.69  ? 1531 MET A N     1 
ATOM   638   C  CA    . MET A 1 1531 ? 205.254 220.476 170.974 1.00 7.52  ? 1531 MET A CA    1 
ATOM   639   C  C     . MET A 1 1531 ? 205.373 220.851 172.445 1.00 8.87  ? 1531 MET A C     1 
ATOM   640   O  O     . MET A 1 1531 ? 204.363 221.095 173.112 1.00 16.22 ? 1531 MET A O     1 
ATOM   641   C  CB    . MET A 1 1531 ? 205.425 218.967 170.797 1.00 7.85  ? 1531 MET A CB    1 
ATOM   642   C  CG    . MET A 1 1531 ? 204.298 218.140 171.396 1.00 12.99 ? 1531 MET A CG    1 
ATOM   643   S  SD    . MET A 1 1531 ? 202.690 218.424 170.639 1.00 28.89 ? 1531 MET A SD    1 
ATOM   644   C  CE    . MET A 1 1531 ? 202.830 217.401 169.180 1.00 14.22 ? 1531 MET A CE    1 
ATOM   645   N  N     . ALA A 1 1532 ? 206.600 220.910 172.967 1.00 8.14  ? 1532 ALA A N     1 
ATOM   646   C  CA    . ALA A 1 1532 ? 206.781 221.165 174.391 1.00 6.82  ? 1532 ALA A CA    1 
ATOM   647   C  C     . ALA A 1 1532 ? 206.380 222.584 174.773 1.00 9.18  ? 1532 ALA A C     1 
ATOM   648   O  O     . ALA A 1 1532 ? 206.004 222.828 175.925 1.00 17.27 ? 1532 ALA A O     1 
ATOM   649   C  CB    . ALA A 1 1532 ? 208.231 220.894 174.791 1.00 9.67  ? 1532 ALA A CB    1 
ATOM   650   N  N     . LEU A 1 1533 ? 206.445 223.526 173.833 1.00 5.75  ? 1533 LEU A N     1 
ATOM   651   C  CA    . LEU A 1 1533 ? 206.114 224.911 174.149 1.00 8.03  ? 1533 LEU A CA    1 
ATOM   652   C  C     . LEU A 1 1533 ? 204.609 225.146 174.140 1.00 9.11  ? 1533 LEU A C     1 
ATOM   653   O  O     . LEU A 1 1533 ? 204.040 225.610 175.134 1.00 11.78 ? 1533 LEU A O     1 
ATOM   654   C  CB    . LEU A 1 1533 ? 206.807 225.856 173.165 1.00 9.61  ? 1533 LEU A CB    1 
ATOM   655   C  CG    . LEU A 1 1533 ? 206.511 227.347 173.345 1.00 9.12  ? 1533 LEU A CG    1 
ATOM   656   C  CD1   . LEU A 1 1533 ? 207.075 227.863 174.661 1.00 5.85  ? 1533 LEU A CD1   1 
ATOM   657   C  CD2   . LEU A 1 1533 ? 207.058 228.147 172.176 1.00 8.62  ? 1533 LEU A CD2   1 
ATOM   658   N  N     . PHE A 1 1534 ? 203.949 224.828 173.028 1.00 8.39  ? 1534 PHE A N     1 
ATOM   659   C  CA    . PHE A 1 1534 ? 202.533 225.131 172.876 1.00 9.54  ? 1534 PHE A CA    1 
ATOM   660   C  C     . PHE A 1 1534 ? 201.629 224.158 173.616 1.00 9.22  ? 1534 PHE A C     1 
ATOM   661   O  O     . PHE A 1 1534 ? 200.435 224.438 173.755 1.00 12.56 ? 1534 PHE A O     1 
ATOM   662   C  CB    . PHE A 1 1534 ? 202.176 225.173 171.390 1.00 8.13  ? 1534 PHE A CB    1 
ATOM   663   C  CG    . PHE A 1 1534 ? 202.902 226.247 170.640 1.00 7.93  ? 1534 PHE A CG    1 
ATOM   664   C  CD1   . PHE A 1 1534 ? 202.784 227.572 171.023 1.00 11.05 ? 1534 PHE A CD1   1 
ATOM   665   C  CD2   . PHE A 1 1534 ? 203.724 225.934 169.575 1.00 8.42  ? 1534 PHE A CD2   1 
ATOM   666   C  CE1   . PHE A 1 1534 ? 203.458 228.566 170.346 1.00 11.27 ? 1534 PHE A CE1   1 
ATOM   667   C  CE2   . PHE A 1 1534 ? 204.402 226.924 168.894 1.00 13.97 ? 1534 PHE A CE2   1 
ATOM   668   C  CZ    . PHE A 1 1534 ? 204.268 228.243 169.280 1.00 17.38 ? 1534 PHE A CZ    1 
ATOM   669   N  N     . ASP A 1 1535 ? 202.159 223.030 174.095 1.00 8.05  ? 1535 ASP A N     1 
ATOM   670   C  CA    . ASP A 1 1535 ? 201.396 222.220 175.037 1.00 9.38  ? 1535 ASP A CA    1 
ATOM   671   C  C     . ASP A 1 1535 ? 201.327 222.888 176.403 1.00 6.65  ? 1535 ASP A C     1 
ATOM   672   O  O     . ASP A 1 1535 ? 200.409 222.612 177.183 1.00 10.19 ? 1535 ASP A O     1 
ATOM   673   C  CB    . ASP A 1 1535 ? 202.003 220.823 175.157 1.00 7.98  ? 1535 ASP A CB    1 
ATOM   674   C  CG    . ASP A 1 1535 ? 201.007 219.799 175.655 1.00 11.73 ? 1535 ASP A CG    1 
ATOM   675   O  OD1   . ASP A 1 1535 ? 200.031 219.521 174.929 1.00 6.79  ? 1535 ASP A OD1   1 
ATOM   676   O  OD2   . ASP A 1 1535 ? 201.199 219.273 176.771 1.00 13.46 ? 1535 ASP A OD2   1 
ATOM   677   N  N     . VAL A 1 1536 ? 202.285 223.762 176.711 1.00 5.67  ? 1536 VAL A N     1 
ATOM   678   C  CA    . VAL A 1 1536 ? 202.212 224.549 177.936 1.00 6.78  ? 1536 VAL A CA    1 
ATOM   679   C  C     . VAL A 1 1536 ? 201.492 225.867 177.681 1.00 7.45  ? 1536 VAL A C     1 
ATOM   680   O  O     . VAL A 1 1536 ? 200.721 226.337 178.524 1.00 10.14 ? 1536 VAL A O     1 
ATOM   681   C  CB    . VAL A 1 1536 ? 203.623 224.774 178.512 1.00 7.01  ? 1536 VAL A CB    1 
ATOM   682   C  CG1   . VAL A 1 1536 ? 203.554 225.597 179.788 1.00 8.32  ? 1536 VAL A CG1   1 
ATOM   683   C  CG2   . VAL A 1 1536 ? 204.314 223.447 178.771 1.00 6.12  ? 1536 VAL A CG2   1 
ATOM   684   N  N     . TRP A 1 1537 ? 201.719 226.470 176.510 1.00 7.24  ? 1537 TRP A N     1 
ATOM   685   C  CA    . TRP A 1 1537 ? 201.096 227.751 176.187 1.00 5.40  ? 1537 TRP A CA    1 
ATOM   686   C  C     . TRP A 1 1537 ? 199.577 227.650 176.248 1.00 6.91  ? 1537 TRP A C     1 
ATOM   687   O  O     . TRP A 1 1537 ? 198.905 228.567 176.735 1.00 8.14  ? 1537 TRP A O     1 
ATOM   688   C  CB    . TRP A 1 1537 ? 201.527 228.208 174.794 1.00 7.43  ? 1537 TRP A CB    1 
ATOM   689   C  CG    . TRP A 1 1537 ? 201.003 229.564 174.386 1.00 11.98 ? 1537 TRP A CG    1 
ATOM   690   C  CD1   . TRP A 1 1537 ? 199.959 229.811 173.557 1.00 25.31 ? 1537 TRP A CD1   1 
ATOM   691   C  CD2   . TRP A 1 1537 ? 201.585 230.840 174.673 1.00 9.70  ? 1537 TRP A CD2   1 
ATOM   692   N  NE1   . TRP A 1 1537 ? 199.793 231.157 173.380 1.00 24.62 ? 1537 TRP A NE1   1 
ATOM   693   C  CE2   . TRP A 1 1537 ? 200.792 231.812 174.043 1.00 22.14 ? 1537 TRP A CE2   1 
ATOM   694   C  CE3   . TRP A 1 1537 ? 202.682 231.256 175.421 1.00 27.35 ? 1537 TRP A CE3   1 
ATOM   695   C  CZ2   . TRP A 1 1537 ? 201.061 233.168 174.137 1.00 28.08 ? 1537 TRP A CZ2   1 
ATOM   696   C  CZ3   . TRP A 1 1537 ? 202.941 232.603 175.523 1.00 28.15 ? 1537 TRP A CZ3   1 
ATOM   697   C  CH2   . TRP A 1 1537 ? 202.138 233.545 174.884 1.00 24.73 ? 1537 TRP A CH2   1 
ATOM   698   N  N     . ILE A 1 1538 ? 199.020 226.543 175.748 1.00 5.87  ? 1538 ILE A N     1 
ATOM   699   C  CA    . ILE A 1 1538 ? 197.569 226.388 175.688 1.00 5.92  ? 1538 ILE A CA    1 
ATOM   700   C  C     . ILE A 1 1538 ? 196.968 226.371 177.088 1.00 6.79  ? 1538 ILE A C     1 
ATOM   701   O  O     . ILE A 1 1538 ? 195.918 226.977 177.336 1.00 5.50  ? 1538 ILE A O     1 
ATOM   702   C  CB    . ILE A 1 1538 ? 197.194 225.130 174.878 1.00 7.65  ? 1538 ILE A CB    1 
ATOM   703   C  CG1   . ILE A 1 1538 ? 195.675 225.030 174.721 1.00 5.36  ? 1538 ILE A CG1   1 
ATOM   704   C  CG2   . ILE A 1 1538 ? 197.769 223.865 175.509 1.00 4.85  ? 1538 ILE A CG2   1 
ATOM   705   C  CD1   . ILE A 1 1538 ? 195.223 223.897 173.840 1.00 4.01  ? 1538 ILE A CD1   1 
ATOM   706   N  N     . ASP A 1 1539 ? 197.618 225.681 178.027 1.00 6.54  ? 1539 ASP A N     1 
ATOM   707   C  CA    . ASP A 1 1539 ? 197.138 225.671 179.403 1.00 4.82  ? 1539 ASP A CA    1 
ATOM   708   C  C     . ASP A 1 1539 ? 197.343 227.017 180.084 1.00 5.02  ? 1539 ASP A C     1 
ATOM   709   O  O     . ASP A 1 1539 ? 196.532 227.406 180.931 1.00 9.97  ? 1539 ASP A O     1 
ATOM   710   C  CB    . ASP A 1 1539 ? 197.835 224.567 180.197 1.00 5.60  ? 1539 ASP A CB    1 
ATOM   711   C  CG    . ASP A 1 1539 ? 197.216 223.204 179.965 1.00 8.94  ? 1539 ASP A CG    1 
ATOM   712   O  OD1   . ASP A 1 1539 ? 195.999 223.136 179.704 1.00 10.86 ? 1539 ASP A OD1   1 
ATOM   713   O  OD2   . ASP A 1 1539 ? 197.948 222.196 180.049 1.00 20.78 ? 1539 ASP A OD2   1 
ATOM   714   N  N     . VAL A 1 1540 ? 198.411 227.734 179.732 1.00 3.82  ? 1540 VAL A N     1 
ATOM   715   C  CA    . VAL A 1 1540 ? 198.660 229.045 180.322 1.00 2.70  ? 1540 VAL A CA    1 
ATOM   716   C  C     . VAL A 1 1540 ? 197.639 230.059 179.821 1.00 2.14  ? 1540 VAL A C     1 
ATOM   717   O  O     . VAL A 1 1540 ? 197.086 230.844 180.598 1.00 1.22  ? 1540 VAL A O     1 
ATOM   718   C  CB    . VAL A 1 1540 ? 200.103 229.496 180.028 1.00 3.42  ? 1540 VAL A CB    1 
ATOM   719   C  CG1   . VAL A 1 1540 ? 200.291 230.967 180.361 1.00 2.60  ? 1540 VAL A CG1   1 
ATOM   720   C  CG2   . VAL A 1 1540 ? 201.085 228.643 180.808 1.00 4.07  ? 1540 VAL A CG2   1 
ATOM   721   N  N     . GLN A 1 1541 ? 197.374 230.057 178.512 1.00 2.90  ? 1541 GLN A N     1 
ATOM   722   C  CA    . GLN A 1 1541 ? 196.390 230.982 177.957 1.00 1.92  ? 1541 GLN A CA    1 
ATOM   723   C  C     . GLN A 1 1541 ? 194.994 230.689 178.493 1.00 2.22  ? 1541 GLN A C     1 
ATOM   724   O  O     . GLN A 1 1541 ? 194.237 231.612 178.808 1.00 2.48  ? 1541 GLN A O     1 
ATOM   725   C  CB    . GLN A 1 1541 ? 196.407 230.917 176.431 1.00 1.93  ? 1541 GLN A CB    1 
ATOM   726   C  CG    . GLN A 1 1541 ? 195.322 231.744 175.765 1.00 3.18  ? 1541 GLN A CG    1 
ATOM   727   C  CD    . GLN A 1 1541 ? 195.509 231.861 174.269 1.00 6.88  ? 1541 GLN A CD    1 
ATOM   728   O  OE1   . GLN A 1 1541 ? 196.469 232.467 173.798 1.00 17.40 ? 1541 GLN A OE1   1 
ATOM   729   N  NE2   . GLN A 1 1541 ? 194.589 231.281 173.512 1.00 8.89  ? 1541 GLN A NE2   1 
ATOM   730   N  N     . ARG A 1 1542 ? 194.638 229.409 178.604 1.00 3.46  ? 1542 ARG A N     1 
ATOM   731   C  CA    . ARG A 1 1542 ? 193.328 229.043 179.133 1.00 3.22  ? 1542 ARG A CA    1 
ATOM   732   C  C     . ARG A 1 1542 ? 193.157 229.526 180.567 1.00 2.96  ? 1542 ARG A C     1 
ATOM   733   O  O     . ARG A 1 1542 ? 192.122 230.096 180.925 1.00 3.24  ? 1542 ARG A O     1 
ATOM   734   C  CB    . ARG A 1 1542 ? 193.142 227.529 179.047 1.00 2.97  ? 1542 ARG A CB    1 
ATOM   735   C  CG    . ARG A 1 1542 ? 191.927 227.000 179.777 1.00 3.75  ? 1542 ARG A CG    1 
ATOM   736   C  CD    . ARG A 1 1542 ? 191.763 225.512 179.528 1.00 4.12  ? 1542 ARG A CD    1 
ATOM   737   N  NE    . ARG A 1 1542 ? 192.837 224.739 180.139 1.00 5.72  ? 1542 ARG A NE    1 
ATOM   738   C  CZ    . ARG A 1 1542 ? 192.942 224.495 181.438 1.00 13.20 ? 1542 ARG A CZ    1 
ATOM   739   N  NH1   . ARG A 1 1542 ? 192.032 224.920 182.298 1.00 13.10 ? 1542 ARG A NH1   1 
ATOM   740   N  NH2   . ARG A 1 1542 ? 193.986 223.802 181.884 1.00 11.49 ? 1542 ARG A NH2   1 
ATOM   741   N  N     . ARG A 1 1543 ? 194.175 229.314 181.404 1.00 3.00  ? 1543 ARG A N     1 
ATOM   742   C  CA    . ARG A 1 1543 ? 194.075 229.706 182.806 1.00 2.97  ? 1543 ARG A CA    1 
ATOM   743   C  C     . ARG A 1 1543 ? 194.080 231.219 182.962 1.00 2.81  ? 1543 ARG A C     1 
ATOM   744   O  O     . ARG A 1 1543 ? 193.380 231.761 183.827 1.00 8.39  ? 1543 ARG A O     1 
ATOM   745   C  CB    . ARG A 1 1543 ? 195.208 229.074 183.609 1.00 2.67  ? 1543 ARG A CB    1 
ATOM   746   C  CG    . ARG A 1 1543 ? 194.969 227.614 183.926 1.00 6.13  ? 1543 ARG A CG    1 
ATOM   747   C  CD    . ARG A 1 1543 ? 196.145 226.991 184.641 1.00 7.52  ? 1543 ARG A CD    1 
ATOM   748   N  NE    . ARG A 1 1543 ? 196.224 225.561 184.378 1.00 15.67 ? 1543 ARG A NE    1 
ATOM   749   C  CZ    . ARG A 1 1543 ? 195.919 224.621 185.262 1.00 17.21 ? 1543 ARG A CZ    1 
ATOM   750   N  NH1   . ARG A 1 1543 ? 195.509 224.927 186.482 1.00 15.55 ? 1543 ARG A NH1   1 
ATOM   751   N  NH2   . ARG A 1 1543 ? 196.029 223.343 184.913 1.00 18.32 ? 1543 ARG A NH2   1 
ATOM   752   N  N     . TRP A 1 1544 ? 194.858 231.920 182.136 1.00 1.86  ? 1544 TRP A N     1 
ATOM   753   C  CA    . TRP A 1 1544 ? 194.892 233.374 182.217 1.00 1.67  ? 1544 TRP A CA    1 
ATOM   754   C  C     . TRP A 1 1544 ? 193.557 233.994 181.829 1.00 3.10  ? 1544 TRP A C     1 
ATOM   755   O  O     . TRP A 1 1544 ? 193.194 235.049 182.357 1.00 4.05  ? 1544 TRP A O     1 
ATOM   756   C  CB    . TRP A 1 1544 ? 196.004 233.933 181.330 1.00 2.52  ? 1544 TRP A CB    1 
ATOM   757   C  CG    . TRP A 1 1544 ? 196.106 235.426 181.391 1.00 2.02  ? 1544 TRP A CG    1 
ATOM   758   C  CD1   . TRP A 1 1544 ? 196.812 236.162 182.293 1.00 3.76  ? 1544 TRP A CD1   1 
ATOM   759   C  CD2   . TRP A 1 1544 ? 195.461 236.365 180.524 1.00 1.86  ? 1544 TRP A CD2   1 
ATOM   760   N  NE1   . TRP A 1 1544 ? 196.657 237.501 182.039 1.00 3.38  ? 1544 TRP A NE1   1 
ATOM   761   C  CE2   . TRP A 1 1544 ? 195.831 237.653 180.957 1.00 2.57  ? 1544 TRP A CE2   1 
ATOM   762   C  CE3   . TRP A 1 1544 ? 194.609 236.243 179.423 1.00 2.25  ? 1544 TRP A CE3   1 
ATOM   763   C  CZ2   . TRP A 1 1544 ? 195.381 238.808 180.326 1.00 3.63  ? 1544 TRP A CZ2   1 
ATOM   764   C  CZ3   . TRP A 1 1544 ? 194.165 237.389 178.800 1.00 2.54  ? 1544 TRP A CZ3   1 
ATOM   765   C  CH2   . TRP A 1 1544 ? 194.550 238.656 179.253 1.00 4.28  ? 1544 TRP A CH2   1 
ATOM   766   N  N     . VAL A 1 1545 ? 192.815 233.363 180.917 1.00 2.59  ? 1545 VAL A N     1 
ATOM   767   C  CA    . VAL A 1 1545 ? 191.562 233.949 180.449 1.00 3.50  ? 1545 VAL A CA    1 
ATOM   768   C  C     . VAL A 1 1545 ? 190.553 234.051 181.588 1.00 4.76  ? 1545 VAL A C     1 
ATOM   769   O  O     . VAL A 1 1545 ? 189.951 235.108 181.811 1.00 5.89  ? 1545 VAL A O     1 
ATOM   770   C  CB    . VAL A 1 1545 ? 191.001 233.145 179.262 1.00 2.80  ? 1545 VAL A CB    1 
ATOM   771   C  CG1   . VAL A 1 1545 ? 189.529 233.448 179.062 1.00 4.63  ? 1545 VAL A CG1   1 
ATOM   772   C  CG2   . VAL A 1 1545 ? 191.775 233.476 178.005 1.00 2.88  ? 1545 VAL A CG2   1 
ATOM   773   N  N     . TYR A 1 1546 ? 190.352 232.961 182.331 1.00 3.17  ? 1546 TYR A N     1 
ATOM   774   C  CA    . TYR A 1 1546 ? 189.342 233.001 183.381 1.00 3.90  ? 1546 TYR A CA    1 
ATOM   775   C  C     . TYR A 1 1546 ? 189.860 233.615 184.677 1.00 4.74  ? 1546 TYR A C     1 
ATOM   776   O  O     . TYR A 1 1546 ? 189.058 234.133 185.459 1.00 5.21  ? 1546 TYR A O     1 
ATOM   777   C  CB    . TYR A 1 1546 ? 188.756 231.603 183.632 1.00 3.64  ? 1546 TYR A CB    1 
ATOM   778   C  CG    . TYR A 1 1546 ? 189.694 230.540 184.165 1.00 2.81  ? 1546 TYR A CG    1 
ATOM   779   C  CD1   . TYR A 1 1546 ? 190.155 230.576 185.476 1.00 3.36  ? 1546 TYR A CD1   1 
ATOM   780   C  CD2   . TYR A 1 1546 ? 190.082 229.471 183.369 1.00 3.14  ? 1546 TYR A CD2   1 
ATOM   781   C  CE1   . TYR A 1 1546 ? 190.994 229.604 185.964 1.00 3.57  ? 1546 TYR A CE1   1 
ATOM   782   C  CE2   . TYR A 1 1546 ? 190.921 228.490 183.852 1.00 3.71  ? 1546 TYR A CE2   1 
ATOM   783   C  CZ    . TYR A 1 1546 ? 191.375 228.561 185.151 1.00 5.57  ? 1546 TYR A CZ    1 
ATOM   784   O  OH    . TYR A 1 1546 ? 192.210 227.586 185.644 1.00 6.15  ? 1546 TYR A OH    1 
ATOM   785   N  N     . LEU A 1 1547 ? 191.170 233.577 184.925 1.00 3.39  ? 1547 LEU A N     1 
ATOM   786   C  CA    . LEU A 1 1547 ? 191.706 234.311 186.066 1.00 3.42  ? 1547 LEU A CA    1 
ATOM   787   C  C     . LEU A 1 1547 ? 191.653 235.813 185.825 1.00 3.45  ? 1547 LEU A C     1 
ATOM   788   O  O     . LEU A 1 1547 ? 191.379 236.586 186.749 1.00 5.90  ? 1547 LEU A O     1 
ATOM   789   C  CB    . LEU A 1 1547 ? 193.135 233.865 186.369 1.00 3.30  ? 1547 LEU A CB    1 
ATOM   790   C  CG    . LEU A 1 1547 ? 193.280 232.535 187.105 1.00 4.25  ? 1547 LEU A CG    1 
ATOM   791   C  CD1   . LEU A 1 1547 ? 194.743 232.173 187.271 1.00 3.46  ? 1547 LEU A CD1   1 
ATOM   792   C  CD2   . LEU A 1 1547 ? 192.576 232.592 188.451 1.00 3.50  ? 1547 LEU A CD2   1 
ATOM   793   N  N     . GLU A 1 1548 ? 191.909 236.245 184.589 1.00 3.86  ? 1548 GLU A N     1 
ATOM   794   C  CA    . GLU A 1 1548 ? 191.814 237.664 184.264 1.00 8.25  ? 1548 GLU A CA    1 
ATOM   795   C  C     . GLU A 1 1548 ? 190.378 238.155 184.397 1.00 8.23  ? 1548 GLU A C     1 
ATOM   796   O  O     . GLU A 1 1548 ? 190.141 239.286 184.835 1.00 15.14 ? 1548 GLU A O     1 
ATOM   797   C  CB    . GLU A 1 1548 ? 192.352 237.913 182.854 1.00 6.33  ? 1548 GLU A CB    1 
ATOM   798   C  CG    . GLU A 1 1548 ? 192.659 239.362 182.509 1.00 8.34  ? 1548 GLU A CG    1 
ATOM   799   C  CD    . GLU A 1 1548 ? 191.417 240.175 182.207 1.00 18.95 ? 1548 GLU A CD    1 
ATOM   800   O  OE1   . GLU A 1 1548 ? 190.571 239.700 181.420 1.00 20.52 ? 1548 GLU A OE1   1 
ATOM   801   O  OE2   . GLU A 1 1548 ? 191.294 241.291 182.750 1.00 19.04 ? 1548 GLU A OE2   1 
ATOM   802   N  N     . GLY A 1 1549 ? 189.407 237.321 184.024 1.00 5.09  ? 1549 GLY A N     1 
ATOM   803   C  CA    . GLY A 1 1549 ? 188.015 237.706 184.182 1.00 7.58  ? 1549 GLY A CA    1 
ATOM   804   C  C     . GLY A 1 1549 ? 187.614 237.881 185.635 1.00 9.60  ? 1549 GLY A C     1 
ATOM   805   O  O     . GLY A 1 1549 ? 186.858 238.793 185.975 1.00 18.95 ? 1549 GLY A O     1 
ATOM   806   N  N     . ILE A 1 1550 ? 188.108 237.004 186.509 1.00 7.75  ? 1550 ILE A N     1 
ATOM   807   C  CA    . ILE A 1 1550 ? 187.783 237.105 187.928 1.00 8.58  ? 1550 ILE A CA    1 
ATOM   808   C  C     . ILE A 1 1550 ? 188.466 238.312 188.560 1.00 9.62  ? 1550 ILE A C     1 
ATOM   809   O  O     . ILE A 1 1550 ? 187.852 239.051 189.338 1.00 16.79 ? 1550 ILE A O     1 
ATOM   810   C  CB    . ILE A 1 1550 ? 188.146 235.797 188.652 1.00 7.60  ? 1550 ILE A CB    1 
ATOM   811   C  CG1   . ILE A 1 1550 ? 187.294 234.652 188.108 1.00 6.54  ? 1550 ILE A CG1   1 
ATOM   812   C  CG2   . ILE A 1 1550 ? 187.960 235.943 190.150 1.00 12.98 ? 1550 ILE A CG2   1 
ATOM   813   C  CD1   . ILE A 1 1550 ? 187.738 233.289 188.553 1.00 5.28  ? 1550 ILE A CD1   1 
ATOM   814   N  N     . PHE A 1 1551 ? 189.736 238.541 188.235 1.00 13.36 ? 1551 PHE A N     1 
ATOM   815   C  CA    . PHE A 1 1551 ? 190.490 239.631 188.844 1.00 11.02 ? 1551 PHE A CA    1 
ATOM   816   C  C     . PHE A 1 1551 ? 190.234 240.975 188.176 1.00 12.72 ? 1551 PHE A C     1 
ATOM   817   O  O     . PHE A 1 1551 ? 190.927 241.948 188.492 1.00 18.87 ? 1551 PHE A O     1 
ATOM   818   C  CB    . PHE A 1 1551 ? 191.988 239.317 188.824 1.00 5.47  ? 1551 PHE A CB    1 
ATOM   819   C  CG    . PHE A 1 1551 ? 192.411 238.328 189.870 1.00 6.44  ? 1551 PHE A CG    1 
ATOM   820   C  CD1   . PHE A 1 1551 ? 192.472 238.694 191.203 1.00 6.07  ? 1551 PHE A CD1   1 
ATOM   821   C  CD2   . PHE A 1 1551 ? 192.759 237.036 189.519 1.00 6.46  ? 1551 PHE A CD2   1 
ATOM   822   C  CE1   . PHE A 1 1551 ? 192.861 237.788 192.168 1.00 6.45  ? 1551 PHE A CE1   1 
ATOM   823   C  CE2   . PHE A 1 1551 ? 193.150 236.124 190.478 1.00 4.85  ? 1551 PHE A CE2   1 
ATOM   824   C  CZ    . PHE A 1 1551 ? 193.201 236.501 191.805 1.00 8.68  ? 1551 PHE A CZ    1 
ATOM   825   N  N     . THR A 1 1552 ? 189.275 241.050 187.261 1.00 10.81 ? 1552 THR A N     1 
ATOM   826   C  CA    . THR A 1 1552 ? 188.858 242.302 186.645 1.00 13.88 ? 1552 THR A CA    1 
ATOM   827   C  C     . THR A 1 1552 ? 187.387 242.612 186.871 1.00 22.61 ? 1552 THR A C     1 
ATOM   828   O  O     . THR A 1 1552 ? 187.039 243.759 187.164 1.00 25.35 ? 1552 THR A O     1 
ATOM   829   C  CB    . THR A 1 1552 ? 189.152 242.273 185.134 1.00 16.46 ? 1552 THR A CB    1 
ATOM   830   O  OG1   . THR A 1 1552 ? 190.569 242.302 184.922 1.00 20.13 ? 1552 THR A OG1   1 
ATOM   831   C  CG2   . THR A 1 1552 ? 188.519 243.461 184.431 1.00 16.02 ? 1552 THR A CG2   1 
ATOM   832   N  N     . GLY A 1 1553 ? 186.515 241.614 186.768 1.00 17.83 ? 1553 GLY A N     1 
ATOM   833   C  CA    . GLY A 1 1553 ? 185.087 241.793 186.911 1.00 21.23 ? 1553 GLY A CA    1 
ATOM   834   C  C     . GLY A 1 1553 ? 184.553 241.770 188.326 1.00 22.63 ? 1553 GLY A C     1 
ATOM   835   O  O     . GLY A 1 1553 ? 183.338 241.898 188.511 1.00 23.45 ? 1553 GLY A O     1 
ATOM   836   N  N     . SER A 1 1554 ? 185.411 241.613 189.336 1.00 22.22 ? 1554 SER A N     1 
ATOM   837   C  CA    . SER A 1 1554 ? 184.974 241.581 190.735 1.00 25.16 ? 1554 SER A CA    1 
ATOM   838   C  C     . SER A 1 1554 ? 185.976 242.391 191.557 1.00 21.72 ? 1554 SER A C     1 
ATOM   839   O  O     . SER A 1 1554 ? 187.016 241.875 191.971 1.00 27.12 ? 1554 SER A O     1 
ATOM   840   C  CB    . SER A 1 1554 ? 184.849 240.152 191.248 1.00 28.25 ? 1554 SER A CB    1 
ATOM   841   O  OG    . SER A 1 1554 ? 186.106 239.497 191.255 1.00 26.49 ? 1554 SER A OG    1 
ATOM   842   N  N     . ALA A 1 1555 ? 185.647 243.662 191.795 1.00 24.61 ? 1555 ALA A N     1 
ATOM   843   C  CA    . ALA A 1 1555 ? 186.540 244.526 192.561 1.00 27.79 ? 1555 ALA A CA    1 
ATOM   844   C  C     . ALA A 1 1555 ? 186.615 244.110 194.024 1.00 29.02 ? 1555 ALA A C     1 
ATOM   845   O  O     . ALA A 1 1555 ? 187.541 244.513 194.737 1.00 31.36 ? 1555 ALA A O     1 
ATOM   846   C  CB    . ALA A 1 1555 ? 186.088 245.982 192.446 1.00 24.79 ? 1555 ALA A CB    1 
ATOM   847   N  N     . ASP A 1 1556 ? 185.654 243.308 194.488 1.00 23.59 ? 1556 ASP A N     1 
ATOM   848   C  CA    . ASP A 1 1556 ? 185.655 242.878 195.884 1.00 26.60 ? 1556 ASP A CA    1 
ATOM   849   C  C     . ASP A 1 1556 ? 186.814 241.936 196.181 1.00 29.03 ? 1556 ASP A C     1 
ATOM   850   O  O     . ASP A 1 1556 ? 187.283 241.858 197.323 1.00 30.48 ? 1556 ASP A O     1 
ATOM   851   C  CB    . ASP A 1 1556 ? 184.324 242.205 196.222 1.00 23.24 ? 1556 ASP A CB    1 
ATOM   852   C  CG    . ASP A 1 1556 ? 183.902 241.195 195.175 1.00 30.49 ? 1556 ASP A CG    1 
ATOM   853   O  OD1   . ASP A 1 1556 ? 183.686 241.597 194.014 1.00 33.07 ? 1556 ASP A OD1   1 
ATOM   854   O  OD2   . ASP A 1 1556 ? 183.788 239.999 195.515 1.00 30.35 ? 1556 ASP A OD2   1 
ATOM   855   N  N     . ILE A 1 1557 ? 187.283 241.201 195.170 1.00 21.40 ? 1557 ILE A N     1 
ATOM   856   C  CA    . ILE A 1 1557 ? 188.329 240.208 195.400 1.00 19.12 ? 1557 ILE A CA    1 
ATOM   857   C  C     . ILE A 1 1557 ? 189.657 240.888 195.712 1.00 20.58 ? 1557 ILE A C     1 
ATOM   858   O  O     . ILE A 1 1557 ? 190.521 240.314 196.387 1.00 20.94 ? 1557 ILE A O     1 
ATOM   859   C  CB    . ILE A 1 1557 ? 188.439 239.253 194.194 1.00 18.46 ? 1557 ILE A CB    1 
ATOM   860   C  CG1   . ILE A 1 1557 ? 189.085 237.932 194.613 1.00 17.15 ? 1557 ILE A CG1   1 
ATOM   861   C  CG2   . ILE A 1 1557 ? 189.238 239.881 193.064 1.00 16.78 ? 1557 ILE A CG2   1 
ATOM   862   C  CD1   . ILE A 1 1557 ? 189.148 236.909 193.504 1.00 11.64 ? 1557 ILE A CD1   1 
ATOM   863   N  N     . LYS A 1 1558 ? 189.839 242.120 195.232 1.00 19.87 ? 1558 LYS A N     1 
ATOM   864   C  CA    . LYS A 1 1558 ? 191.080 242.842 195.494 1.00 17.94 ? 1558 LYS A CA    1 
ATOM   865   C  C     . LYS A 1 1558 ? 191.253 243.106 196.985 1.00 21.88 ? 1558 LYS A C     1 
ATOM   866   O  O     . LYS A 1 1558 ? 192.357 242.986 197.527 1.00 22.64 ? 1558 LYS A O     1 
ATOM   867   C  CB    . LYS A 1 1558 ? 191.098 244.151 194.706 1.00 17.70 ? 1558 LYS A CB    1 
ATOM   868   C  CG    . LYS A 1 1558 ? 192.359 244.975 194.899 1.00 21.23 ? 1558 LYS A CG    1 
ATOM   869   C  CD    . LYS A 1 1558 ? 192.338 246.224 194.036 1.00 27.20 ? 1558 LYS A CD    1 
ATOM   870   C  CE    . LYS A 1 1558 ? 193.638 247.000 194.159 1.00 29.05 ? 1558 LYS A CE    1 
ATOM   871   N  NZ    . LYS A 1 1558 ? 194.814 246.180 193.756 1.00 29.64 ? 1558 LYS A NZ    1 
ATOM   872   N  N     . HIS A 1 1559 ? 190.166 243.472 197.665 1.00 25.89 ? 1559 HIS A N     1 
ATOM   873   C  CA    . HIS A 1 1559 ? 190.228 243.657 199.110 1.00 26.69 ? 1559 HIS A CA    1 
ATOM   874   C  C     . HIS A 1 1559 ? 190.265 242.320 199.838 1.00 22.90 ? 1559 HIS A C     1 
ATOM   875   O  O     . HIS A 1 1559 ? 190.972 242.172 200.841 1.00 27.09 ? 1559 HIS A O     1 
ATOM   876   C  CB    . HIS A 1 1559 ? 189.037 244.488 199.581 1.00 25.11 ? 1559 HIS A CB    1 
ATOM   877   C  CG    . HIS A 1 1559 ? 189.041 245.894 199.066 1.00 31.11 ? 1559 HIS A CG    1 
ATOM   878   N  ND1   . HIS A 1 1559 ? 188.466 246.248 197.865 1.00 32.94 ? 1559 HIS A ND1   1 
ATOM   879   C  CD2   . HIS A 1 1559 ? 189.555 247.033 199.586 1.00 31.60 ? 1559 HIS A CD2   1 
ATOM   880   C  CE1   . HIS A 1 1559 ? 188.622 247.545 197.669 1.00 32.83 ? 1559 HIS A CE1   1 
ATOM   881   N  NE2   . HIS A 1 1559 ? 189.280 248.045 198.700 1.00 30.53 ? 1559 HIS A NE2   1 
ATOM   882   N  N     . LEU A 1 1560 ? 189.504 241.338 199.350 1.00 20.32 ? 1560 LEU A N     1 
ATOM   883   C  CA    . LEU A 1 1560 ? 189.437 240.044 200.024 1.00 18.85 ? 1560 LEU A CA    1 
ATOM   884   C  C     . LEU A 1 1560 ? 190.786 239.335 199.993 1.00 21.92 ? 1560 LEU A C     1 
ATOM   885   O  O     . LEU A 1 1560 ? 191.220 238.760 200.998 1.00 23.19 ? 1560 LEU A O     1 
ATOM   886   C  CB    . LEU A 1 1560 ? 188.353 239.181 199.379 1.00 20.91 ? 1560 LEU A CB    1 
ATOM   887   C  CG    . LEU A 1 1560 ? 188.256 237.726 199.838 1.00 24.67 ? 1560 LEU A CG    1 
ATOM   888   C  CD1   . LEU A 1 1560 ? 187.998 237.646 201.334 1.00 23.84 ? 1560 LEU A CD1   1 
ATOM   889   C  CD2   . LEU A 1 1560 ? 187.169 236.993 199.065 1.00 20.75 ? 1560 LEU A CD2   1 
ATOM   890   N  N     . LEU A 1 1561 ? 191.463 239.363 198.847 1.00 20.82 ? 1561 LEU A N     1 
ATOM   891   C  CA    . LEU A 1 1561 ? 192.763 238.718 198.667 1.00 19.12 ? 1561 LEU A CA    1 
ATOM   892   C  C     . LEU A 1 1561 ? 193.737 239.701 198.031 1.00 20.73 ? 1561 LEU A C     1 
ATOM   893   O  O     . LEU A 1 1561 ? 194.028 239.622 196.832 1.00 20.36 ? 1561 LEU A O     1 
ATOM   894   C  CB    . LEU A 1 1561 ? 192.631 237.450 197.825 1.00 19.66 ? 1561 LEU A CB    1 
ATOM   895   C  CG    . LEU A 1 1561 ? 191.637 236.424 198.358 1.00 19.74 ? 1561 LEU A CG    1 
ATOM   896   C  CD1   . LEU A 1 1561 ? 191.471 235.272 197.389 1.00 20.94 ? 1561 LEU A CD1   1 
ATOM   897   C  CD2   . LEU A 1 1561 ? 192.133 235.920 199.704 1.00 21.58 ? 1561 LEU A CD2   1 
ATOM   898   N  N     . PRO A 1 1562 ? 194.253 240.655 198.812 1.00 21.62 ? 1562 PRO A N     1 
ATOM   899   C  CA    . PRO A 1 1562 ? 195.196 241.631 198.236 1.00 18.01 ? 1562 PRO A CA    1 
ATOM   900   C  C     . PRO A 1 1562 ? 196.477 241.002 197.714 1.00 18.40 ? 1562 PRO A C     1 
ATOM   901   O  O     . PRO A 1 1562 ? 196.983 241.416 196.664 1.00 15.29 ? 1562 PRO A O     1 
ATOM   902   C  CB    . PRO A 1 1562 ? 195.459 242.586 199.409 1.00 15.95 ? 1562 PRO A CB    1 
ATOM   903   C  CG    . PRO A 1 1562 ? 194.299 242.389 200.335 1.00 18.51 ? 1562 PRO A CG    1 
ATOM   904   C  CD    . PRO A 1 1562 ? 193.969 240.937 200.228 1.00 13.87 ? 1562 PRO A CD    1 
ATOM   905   N  N     . VAL A 1 1563 ? 197.017 240.007 198.422 1.00 19.08 ? 1563 VAL A N     1 
ATOM   906   C  CA    . VAL A 1 1563 ? 198.281 239.401 198.008 1.00 15.54 ? 1563 VAL A CA    1 
ATOM   907   C  C     . VAL A 1 1563 ? 198.114 238.691 196.673 1.00 18.31 ? 1563 VAL A C     1 
ATOM   908   O  O     . VAL A 1 1563 ? 198.908 238.881 195.743 1.00 21.23 ? 1563 VAL A O     1 
ATOM   909   C  CB    . VAL A 1 1563 ? 198.800 238.442 199.095 1.00 22.66 ? 1563 VAL A CB    1 
ATOM   910   C  CG1   . VAL A 1 1563 ? 200.055 237.734 198.619 1.00 20.90 ? 1563 VAL A CG1   1 
ATOM   911   C  CG2   . VAL A 1 1563 ? 199.069 239.198 200.383 1.00 17.92 ? 1563 VAL A CG2   1 
ATOM   912   N  N     . GLU A 1 1564 ? 197.068 237.873 196.552 1.00 18.15 ? 1564 GLU A N     1 
ATOM   913   C  CA    . GLU A 1 1564 ? 196.817 237.163 195.303 1.00 15.43 ? 1564 GLU A CA    1 
ATOM   914   C  C     . GLU A 1 1564 ? 196.531 238.133 194.164 1.00 14.94 ? 1564 GLU A C     1 
ATOM   915   O  O     . GLU A 1 1564 ? 196.982 237.927 193.032 1.00 18.90 ? 1564 GLU A O     1 
ATOM   916   C  CB    . GLU A 1 1564 ? 195.659 236.180 195.484 1.00 13.11 ? 1564 GLU A CB    1 
ATOM   917   C  CG    . GLU A 1 1564 ? 195.930 235.045 196.470 1.00 15.93 ? 1564 GLU A CG    1 
ATOM   918   C  CD    . GLU A 1 1564 ? 195.903 235.476 197.928 1.00 29.21 ? 1564 GLU A CD    1 
ATOM   919   O  OE1   . GLU A 1 1564 ? 195.672 236.672 198.203 1.00 32.26 ? 1564 GLU A OE1   1 
ATOM   920   O  OE2   . GLU A 1 1564 ? 196.111 234.611 198.804 1.00 32.54 ? 1564 GLU A OE2   1 
ATOM   921   N  N     . THR A 1 1565 ? 195.777 239.197 194.447 1.00 12.02 ? 1565 THR A N     1 
ATOM   922   C  CA    . THR A 1 1565 ? 195.437 240.159 193.403 1.00 11.39 ? 1565 THR A CA    1 
ATOM   923   C  C     . THR A 1 1565 ? 196.680 240.861 192.868 1.00 16.98 ? 1565 THR A C     1 
ATOM   924   O  O     . THR A 1 1565 ? 196.823 241.044 191.653 1.00 14.75 ? 1565 THR A O     1 
ATOM   925   C  CB    . THR A 1 1565 ? 194.432 241.177 193.938 1.00 11.29 ? 1565 THR A CB    1 
ATOM   926   O  OG1   . THR A 1 1565 ? 193.254 240.493 194.379 1.00 20.80 ? 1565 THR A OG1   1 
ATOM   927   C  CG2   . THR A 1 1565 ? 194.056 242.171 192.854 1.00 8.58  ? 1565 THR A CG2   1 
ATOM   928   N  N     . GLN A 1 1566 ? 197.591 241.264 193.757 1.00 17.17 ? 1566 GLN A N     1 
ATOM   929   C  CA    . GLN A 1 1566 ? 198.833 241.882 193.299 1.00 17.29 ? 1566 GLN A CA    1 
ATOM   930   C  C     . GLN A 1 1566 ? 199.736 240.865 192.614 1.00 16.96 ? 1566 GLN A C     1 
ATOM   931   O  O     . GLN A 1 1566 ? 200.381 241.178 191.606 1.00 14.73 ? 1566 GLN A O     1 
ATOM   932   C  CB    . GLN A 1 1566 ? 199.556 242.558 194.466 1.00 19.36 ? 1566 GLN A CB    1 
ATOM   933   C  CG    . GLN A 1 1566 ? 198.753 243.616 195.235 1.00 27.13 ? 1566 GLN A CG    1 
ATOM   934   C  CD    . GLN A 1 1566 ? 198.156 244.709 194.353 1.00 32.83 ? 1566 GLN A CD    1 
ATOM   935   O  OE1   . GLN A 1 1566 ? 197.285 244.460 193.519 1.00 29.53 ? 1566 GLN A OE1   1 
ATOM   936   N  NE2   . GLN A 1 1566 ? 198.636 245.935 194.537 1.00 25.49 ? 1566 GLN A NE2   1 
ATOM   937   N  N     . ARG A 1 1567 ? 199.799 239.641 193.144 1.00 18.56 ? 1567 ARG A N     1 
ATOM   938   C  CA    . ARG A 1 1567 ? 200.605 238.612 192.492 1.00 11.63 ? 1567 ARG A CA    1 
ATOM   939   C  C     . ARG A 1 1567 ? 200.085 238.307 191.097 1.00 14.70 ? 1567 ARG A C     1 
ATOM   940   O  O     . ARG A 1 1567 ? 200.872 238.143 190.160 1.00 17.82 ? 1567 ARG A O     1 
ATOM   941   C  CB    . ARG A 1 1567 ? 200.658 237.341 193.340 1.00 9.54  ? 1567 ARG A CB    1 
ATOM   942   C  CG    . ARG A 1 1567 ? 201.426 237.500 194.638 1.00 23.84 ? 1567 ARG A CG    1 
ATOM   943   C  CD    . ARG A 1 1567 ? 201.426 236.222 195.462 1.00 27.89 ? 1567 ARG A CD    1 
ATOM   944   N  NE    . ARG A 1 1567 ? 202.157 235.139 194.817 1.00 25.24 ? 1567 ARG A NE    1 
ATOM   945   C  CZ    . ARG A 1 1567 ? 202.177 233.886 195.253 1.00 32.08 ? 1567 ARG A CZ    1 
ATOM   946   N  NH1   . ARG A 1 1567 ? 201.530 233.526 196.349 1.00 27.40 ? 1567 ARG A NH1   1 
ATOM   947   N  NH2   . ARG A 1 1567 ? 202.870 232.974 194.579 1.00 34.02 ? 1567 ARG A NH2   1 
ATOM   948   N  N     . PHE A 1 1568 ? 198.762 238.244 190.928 1.00 14.72 ? 1568 PHE A N     1 
ATOM   949   C  CA    . PHE A 1 1568 ? 198.221 238.011 189.595 1.00 8.90  ? 1568 PHE A CA    1 
ATOM   950   C  C     . PHE A 1 1568 ? 198.520 239.168 188.655 1.00 9.03  ? 1568 PHE A C     1 
ATOM   951   O  O     . PHE A 1 1568 ? 198.711 238.952 187.455 1.00 10.37 ? 1568 PHE A O     1 
ATOM   952   C  CB    . PHE A 1 1568 ? 196.713 237.769 189.643 1.00 11.30 ? 1568 PHE A CB    1 
ATOM   953   C  CG    . PHE A 1 1568 ? 196.092 237.648 188.284 1.00 9.49  ? 1568 PHE A CG    1 
ATOM   954   C  CD1   . PHE A 1 1568 ? 196.222 236.478 187.553 1.00 5.71  ? 1568 PHE A CD1   1 
ATOM   955   C  CD2   . PHE A 1 1568 ? 195.414 238.713 187.717 1.00 4.59  ? 1568 PHE A CD2   1 
ATOM   956   C  CE1   . PHE A 1 1568 ? 195.669 236.368 186.295 1.00 3.49  ? 1568 PHE A CE1   1 
ATOM   957   C  CE2   . PHE A 1 1568 ? 194.864 238.606 186.460 1.00 5.01  ? 1568 PHE A CE2   1 
ATOM   958   C  CZ    . PHE A 1 1568 ? 194.992 237.433 185.749 1.00 4.22  ? 1568 PHE A CZ    1 
ATOM   959   N  N     . GLN A 1 1569 ? 198.550 240.395 189.175 1.00 16.62 ? 1569 GLN A N     1 
ATOM   960   C  CA    . GLN A 1 1569 ? 198.851 241.545 188.329 1.00 15.79 ? 1569 GLN A CA    1 
ATOM   961   C  C     . GLN A 1 1569 ? 200.255 241.444 187.746 1.00 16.35 ? 1569 GLN A C     1 
ATOM   962   O  O     . GLN A 1 1569 ? 200.472 241.757 186.570 1.00 16.30 ? 1569 GLN A O     1 
ATOM   963   C  CB    . GLN A 1 1569 ? 198.692 242.837 189.128 1.00 17.71 ? 1569 GLN A CB    1 
ATOM   964   C  CG    . GLN A 1 1569 ? 198.912 244.090 188.306 1.00 20.36 ? 1569 GLN A CG    1 
ATOM   965   C  CD    . GLN A 1 1569 ? 197.902 244.218 187.184 1.00 27.04 ? 1569 GLN A CD    1 
ATOM   966   O  OE1   . GLN A 1 1569 ? 198.218 243.981 186.020 1.00 27.79 ? 1569 GLN A OE1   1 
ATOM   967   N  NE2   . GLN A 1 1569 ? 196.679 244.601 187.531 1.00 27.03 ? 1569 GLN A NE2   1 
ATOM   968   N  N     . SER A 1 1570 ? 201.222 241.012 188.559 1.00 15.62 ? 1570 SER A N     1 
ATOM   969   C  CA    . SER A 1 1570 ? 202.595 240.869 188.085 1.00 14.84 ? 1570 SER A CA    1 
ATOM   970   C  C     . SER A 1 1570 ? 202.701 239.793 187.010 1.00 18.37 ? 1570 SER A C     1 
ATOM   971   O  O     . SER A 1 1570 ? 203.364 239.986 185.985 1.00 24.02 ? 1570 SER A O     1 
ATOM   972   C  CB    . SER A 1 1570 ? 203.517 240.546 189.262 1.00 18.73 ? 1570 SER A CB    1 
ATOM   973   O  OG    . SER A 1 1570 ? 203.324 241.462 190.328 1.00 21.35 ? 1570 SER A OG    1 
ATOM   974   N  N     . ILE A 1 1571 ? 202.055 238.648 187.230 1.00 16.59 ? 1571 ILE A N     1 
ATOM   975   C  CA    . ILE A 1 1571 ? 202.070 237.582 186.234 1.00 11.82 ? 1571 ILE A CA    1 
ATOM   976   C  C     . ILE A 1 1571 ? 201.284 237.991 184.997 1.00 14.38 ? 1571 ILE A C     1 
ATOM   977   O  O     . ILE A 1 1571 ? 201.677 237.680 183.866 1.00 15.63 ? 1571 ILE A O     1 
ATOM   978   C  CB    . ILE A 1 1571 ? 201.535 236.277 186.848 1.00 10.56 ? 1571 ILE A CB    1 
ATOM   979   C  CG1   . ILE A 1 1571 ? 202.061 236.125 188.273 1.00 14.81 ? 1571 ILE A CG1   1 
ATOM   980   C  CG2   . ILE A 1 1571 ? 201.914 235.085 186.001 1.00 13.00 ? 1571 ILE A CG2   1 
ATOM   981   C  CD1   . ILE A 1 1571 ? 201.677 234.845 188.928 1.00 15.44 ? 1571 ILE A CD1   1 
ATOM   982   N  N     . SER A 1 1572 ? 200.166 238.692 185.188 1.00 11.55 ? 1572 SER A N     1 
ATOM   983   C  CA    . SER A 1 1572 ? 199.390 239.169 184.049 1.00 10.47 ? 1572 SER A CA    1 
ATOM   984   C  C     . SER A 1 1572 ? 200.178 240.176 183.223 1.00 14.57 ? 1572 SER A C     1 
ATOM   985   O  O     . SER A 1 1572 ? 199.902 240.350 182.031 1.00 15.68 ? 1572 SER A O     1 
ATOM   986   C  CB    . SER A 1 1572 ? 198.076 239.782 184.532 1.00 9.59  ? 1572 SER A CB    1 
ATOM   987   O  OG    . SER A 1 1572 ? 197.246 240.152 183.449 1.00 16.28 ? 1572 SER A OG    1 
ATOM   988   N  N     . THR A 1 1573 ? 201.152 240.854 183.834 1.00 18.01 ? 1573 THR A N     1 
ATOM   989   C  CA    . THR A 1 1573 ? 201.992 241.777 183.078 1.00 16.69 ? 1573 THR A CA    1 
ATOM   990   C  C     . THR A 1 1573 ? 202.976 241.028 182.187 1.00 15.79 ? 1573 THR A C     1 
ATOM   991   O  O     . THR A 1 1573 ? 203.136 241.367 181.010 1.00 15.68 ? 1573 THR A O     1 
ATOM   992   C  CB    . THR A 1 1573 ? 202.735 242.715 184.029 1.00 16.79 ? 1573 THR A CB    1 
ATOM   993   O  OG1   . THR A 1 1573 ? 201.795 243.351 184.902 1.00 23.67 ? 1573 THR A OG1   1 
ATOM   994   C  CG2   . THR A 1 1573 ? 203.477 243.782 183.245 1.00 12.10 ? 1573 THR A CG2   1 
ATOM   995   N  N     . GLU A 1 1574 ? 203.636 240.000 182.728 1.00 15.04 ? 1574 GLU A N     1 
ATOM   996   C  CA    . GLU A 1 1574 ? 204.599 239.244 181.934 1.00 12.26 ? 1574 GLU A CA    1 
ATOM   997   C  C     . GLU A 1 1574 ? 203.905 238.468 180.822 1.00 16.44 ? 1574 GLU A C     1 
ATOM   998   O  O     . GLU A 1 1574 ? 204.462 238.299 179.731 1.00 17.63 ? 1574 GLU A O     1 
ATOM   999   C  CB    . GLU A 1 1574 ? 205.405 238.305 182.833 1.00 12.79 ? 1574 GLU A CB    1 
ATOM   1000  C  CG    . GLU A 1 1574 ? 206.317 237.329 182.090 1.00 14.67 ? 1574 GLU A CG    1 
ATOM   1001  C  CD    . GLU A 1 1574 ? 207.251 238.006 181.094 1.00 23.49 ? 1574 GLU A CD    1 
ATOM   1002  O  OE1   . GLU A 1 1574 ? 207.673 239.157 181.340 1.00 27.07 ? 1574 GLU A OE1   1 
ATOM   1003  O  OE2   . GLU A 1 1574 ? 207.563 237.383 180.057 1.00 19.21 ? 1574 GLU A OE2   1 
ATOM   1004  N  N     . PHE A 1 1575 ? 202.688 237.984 181.080 1.00 12.44 ? 1575 PHE A N     1 
ATOM   1005  C  CA    . PHE A 1 1575 ? 201.931 237.301 180.037 1.00 11.32 ? 1575 PHE A CA    1 
ATOM   1006  C  C     . PHE A 1 1575 ? 201.617 238.246 178.884 1.00 10.68 ? 1575 PHE A C     1 
ATOM   1007  O  O     . PHE A 1 1575 ? 201.860 237.920 177.718 1.00 8.84  ? 1575 PHE A O     1 
ATOM   1008  C  CB    . PHE A 1 1575 ? 200.646 236.707 180.618 1.00 11.44 ? 1575 PHE A CB    1 
ATOM   1009  C  CG    . PHE A 1 1575 ? 199.712 236.153 179.581 1.00 8.88  ? 1575 PHE A CG    1 
ATOM   1010  C  CD1   . PHE A 1 1575 ? 199.898 234.876 179.076 1.00 9.87  ? 1575 PHE A CD1   1 
ATOM   1011  C  CD2   . PHE A 1 1575 ? 198.645 236.902 179.115 1.00 7.40  ? 1575 PHE A CD2   1 
ATOM   1012  C  CE1   . PHE A 1 1575 ? 199.043 234.362 178.123 1.00 7.42  ? 1575 PHE A CE1   1 
ATOM   1013  C  CE2   . PHE A 1 1575 ? 197.790 236.393 178.162 1.00 6.80  ? 1575 PHE A CE2   1 
ATOM   1014  C  CZ    . PHE A 1 1575 ? 197.987 235.120 177.668 1.00 6.24  ? 1575 PHE A CZ    1 
ATOM   1015  N  N     . LEU A 1 1576 ? 201.092 239.435 179.196 1.00 17.90 ? 1576 LEU A N     1 
ATOM   1016  C  CA    . LEU A 1 1576 ? 200.757 240.400 178.153 1.00 15.98 ? 1576 LEU A CA    1 
ATOM   1017  C  C     . LEU A 1 1576 ? 201.992 240.874 177.399 1.00 14.28 ? 1576 LEU A C     1 
ATOM   1018  O  O     . LEU A 1 1576 ? 201.922 241.112 176.188 1.00 16.74 ? 1576 LEU A O     1 
ATOM   1019  C  CB    . LEU A 1 1576 ? 200.013 241.593 178.755 1.00 14.71 ? 1576 LEU A CB    1 
ATOM   1020  C  CG    . LEU A 1 1576 ? 198.582 241.350 179.241 1.00 16.38 ? 1576 LEU A CG    1 
ATOM   1021  C  CD1   . LEU A 1 1576 ? 197.999 242.609 179.860 1.00 20.16 ? 1576 LEU A CD1   1 
ATOM   1022  C  CD2   . LEU A 1 1576 ? 197.703 240.869 178.101 1.00 18.87 ? 1576 LEU A CD2   1 
ATOM   1023  N  N     . ALA A 1 1577 ? 203.123 241.031 178.091 1.00 12.99 ? 1577 ALA A N     1 
ATOM   1024  C  CA    . ALA A 1 1577 ? 204.356 241.408 177.410 1.00 15.29 ? 1577 ALA A CA    1 
ATOM   1025  C  C     . ALA A 1 1577 ? 204.771 240.344 176.400 1.00 16.86 ? 1577 ALA A C     1 
ATOM   1026  O  O     . ALA A 1 1577 ? 205.181 240.664 175.279 1.00 17.89 ? 1577 ALA A O     1 
ATOM   1027  C  CB    . ALA A 1 1577 ? 205.468 241.645 178.429 1.00 11.88 ? 1577 ALA A CB    1 
ATOM   1028  N  N     . LEU A 1 1578 ? 204.659 239.071 176.780 1.00 12.69 ? 1578 LEU A N     1 
ATOM   1029  C  CA    . LEU A 1 1578 ? 204.984 237.993 175.855 1.00 14.46 ? 1578 LEU A CA    1 
ATOM   1030  C  C     . LEU A 1 1578 ? 203.945 237.885 174.746 1.00 14.39 ? 1578 LEU A C     1 
ATOM   1031  O  O     . LEU A 1 1578 ? 204.262 237.458 173.631 1.00 15.57 ? 1578 LEU A O     1 
ATOM   1032  C  CB    . LEU A 1 1578 ? 205.119 236.682 176.626 1.00 12.35 ? 1578 LEU A CB    1 
ATOM   1033  C  CG    . LEU A 1 1578 ? 205.518 235.409 175.891 1.00 12.57 ? 1578 LEU A CG    1 
ATOM   1034  C  CD1   . LEU A 1 1578 ? 206.898 235.541 175.282 1.00 16.56 ? 1578 LEU A CD1   1 
ATOM   1035  C  CD2   . LEU A 1 1578 ? 205.511 234.282 176.891 1.00 13.40 ? 1578 LEU A CD2   1 
ATOM   1036  N  N     . MET A 1 1579 ? 202.698 238.273 175.030 1.00 15.47 ? 1579 MET A N     1 
ATOM   1037  C  CA    . MET A 1 1579 ? 201.677 238.321 173.987 1.00 11.02 ? 1579 MET A CA    1 
ATOM   1038  C  C     . MET A 1 1579 ? 202.012 239.354 172.921 1.00 13.54 ? 1579 MET A C     1 
ATOM   1039  O  O     . MET A 1 1579 ? 201.807 239.101 171.728 1.00 16.69 ? 1579 MET A O     1 
ATOM   1040  C  CB    . MET A 1 1579 ? 200.311 238.636 174.596 1.00 14.90 ? 1579 MET A CB    1 
ATOM   1041  C  CG    . MET A 1 1579 ? 199.775 237.568 175.518 1.00 16.72 ? 1579 MET A CG    1 
ATOM   1042  S  SD    . MET A 1 1579 ? 199.533 235.991 174.699 1.00 33.42 ? 1579 MET A SD    1 
ATOM   1043  C  CE    . MET A 1 1579 ? 198.159 236.395 173.634 1.00 29.41 ? 1579 MET A CE    1 
ATOM   1044  N  N     . LYS A 1 1580 ? 202.513 240.522 173.330 1.00 14.74 ? 1580 LYS A N     1 
ATOM   1045  C  CA    . LYS A 1 1580 ? 202.825 241.576 172.370 1.00 18.01 ? 1580 LYS A CA    1 
ATOM   1046  C  C     . LYS A 1 1580 ? 203.947 241.153 171.430 1.00 19.21 ? 1580 LYS A C     1 
ATOM   1047  O  O     . LYS A 1 1580 ? 203.930 241.492 170.241 1.00 22.13 ? 1580 LYS A O     1 
ATOM   1048  C  CB    . LYS A 1 1580 ? 203.190 242.864 173.110 1.00 18.13 ? 1580 LYS A CB    1 
ATOM   1049  C  CG    . LYS A 1 1580 ? 203.394 244.066 172.203 1.00 24.69 ? 1580 LYS A CG    1 
ATOM   1050  C  CD    . LYS A 1 1580 ? 203.747 245.310 173.002 1.00 24.94 ? 1580 LYS A CD    1 
ATOM   1051  C  CE    . LYS A 1 1580 ? 202.551 245.820 173.788 1.00 25.59 ? 1580 LYS A CE    1 
ATOM   1052  N  NZ    . LYS A 1 1580 ? 201.476 246.332 172.894 1.00 31.76 ? 1580 LYS A NZ    1 
ATOM   1053  N  N     . LYS A 1 1581 ? 204.934 240.415 171.945 1.00 17.42 ? 1581 LYS A N     1 
ATOM   1054  C  CA    . LYS A 1 1581 ? 205.991 239.893 171.083 1.00 15.33 ? 1581 LYS A CA    1 
ATOM   1055  C  C     . LYS A 1 1581 ? 205.429 238.937 170.039 1.00 17.11 ? 1581 LYS A C     1 
ATOM   1056  O  O     . LYS A 1 1581 ? 205.841 238.968 168.874 1.00 21.18 ? 1581 LYS A O     1 
ATOM   1057  C  CB    . LYS A 1 1581 ? 207.061 239.192 171.919 1.00 13.19 ? 1581 LYS A CB    1 
ATOM   1058  C  CG    . LYS A 1 1581 ? 208.017 240.130 172.629 1.00 14.77 ? 1581 LYS A CG    1 
ATOM   1059  C  CD    . LYS A 1 1581 ? 209.016 239.356 173.470 1.00 14.64 ? 1581 LYS A CD    1 
ATOM   1060  C  CE    . LYS A 1 1581 ? 208.397 238.892 174.774 1.00 15.90 ? 1581 LYS A CE    1 
ATOM   1061  N  NZ    . LYS A 1 1581 ? 209.217 239.291 175.951 1.00 18.54 ? 1581 LYS A NZ    1 
ATOM   1062  N  N     . VAL A 1 1582 ? 204.490 238.079 170.441 1.00 13.57 ? 1582 VAL A N     1 
ATOM   1063  C  CA    . VAL A 1 1582 ? 203.869 237.150 169.502 1.00 12.49 ? 1582 VAL A CA    1 
ATOM   1064  C  C     . VAL A 1 1582 ? 203.121 237.915 168.419 1.00 16.49 ? 1582 VAL A C     1 
ATOM   1065  O  O     . VAL A 1 1582 ? 203.101 237.509 167.250 1.00 19.46 ? 1582 VAL A O     1 
ATOM   1066  C  CB    . VAL A 1 1582 ? 202.946 236.171 170.252 1.00 13.56 ? 1582 VAL A CB    1 
ATOM   1067  C  CG1   . VAL A 1 1582 ? 202.196 235.276 169.275 1.00 8.75  ? 1582 VAL A CG1   1 
ATOM   1068  C  CG2   . VAL A 1 1582 ? 203.748 235.336 171.238 1.00 10.43 ? 1582 VAL A CG2   1 
ATOM   1069  N  N     . SER A 1 1583 ? 202.495 239.036 168.787 1.00 19.90 ? 1583 SER A N     1 
ATOM   1070  C  CA    . SER A 1 1583 ? 201.769 239.836 167.806 1.00 18.38 ? 1583 SER A CA    1 
ATOM   1071  C  C     . SER A 1 1583 ? 202.708 240.391 166.739 1.00 25.58 ? 1583 SER A C     1 
ATOM   1072  O  O     . SER A 1 1583 ? 202.360 240.418 165.552 1.00 30.74 ? 1583 SER A O     1 
ATOM   1073  C  CB    . SER A 1 1583 ? 201.018 240.966 168.505 1.00 22.32 ? 1583 SER A CB    1 
ATOM   1074  O  OG    . SER A 1 1583 ? 200.178 241.656 167.596 1.00 32.97 ? 1583 SER A OG    1 
ATOM   1075  N  N     . LYS A 1 1584 ? 203.893 240.849 167.143 1.00 16.72 ? 1584 LYS A N     1 
ATOM   1076  C  CA    . LYS A 1 1584 ? 204.853 241.375 166.177 1.00 20.25 ? 1584 LYS A CA    1 
ATOM   1077  C  C     . LYS A 1 1584 ? 205.326 240.287 165.220 1.00 26.24 ? 1584 LYS A C     1 
ATOM   1078  O  O     . LYS A 1 1584 ? 205.393 240.497 164.004 1.00 23.81 ? 1584 LYS A O     1 
ATOM   1079  C  CB    . LYS A 1 1584 ? 206.043 242.003 166.905 1.00 20.52 ? 1584 LYS A CB    1 
ATOM   1080  C  CG    . LYS A 1 1584 ? 205.662 242.998 167.980 1.00 22.30 ? 1584 LYS A CG    1 
ATOM   1081  C  CD    . LYS A 1 1584 ? 204.877 244.162 167.399 1.00 27.61 ? 1584 LYS A CD    1 
ATOM   1082  C  CE    . LYS A 1 1584 ? 204.523 245.176 168.471 1.00 28.44 ? 1584 LYS A CE    1 
ATOM   1083  N  NZ    . LYS A 1 1584 ? 205.735 245.689 169.167 1.00 29.68 ? 1584 LYS A NZ    1 
ATOM   1084  N  N     . SER A 1 1585 ? 205.651 239.108 165.754 1.00 21.71 ? 1585 SER A N     1 
ATOM   1085  C  CA    . SER A 1 1585 ? 206.158 237.985 164.967 1.00 20.62 ? 1585 SER A CA    1 
ATOM   1086  C  C     . SER A 1 1585 ? 205.277 236.771 165.229 1.00 19.91 ? 1585 SER A C     1 
ATOM   1087  O  O     . SER A 1 1585 ? 205.606 235.923 166.072 1.00 21.97 ? 1585 SER A O     1 
ATOM   1088  C  CB    . SER A 1 1585 ? 207.616 237.688 165.309 1.00 23.16 ? 1585 SER A CB    1 
ATOM   1089  O  OG    . SER A 1 1585 ? 207.743 237.257 166.654 1.00 33.13 ? 1585 SER A OG    1 
ATOM   1090  N  N     . PRO A 1 1586 ? 204.148 236.644 164.529 1.00 18.84 ? 1586 PRO A N     1 
ATOM   1091  C  CA    . PRO A 1 1586 ? 203.273 235.486 164.742 1.00 19.19 ? 1586 PRO A CA    1 
ATOM   1092  C  C     . PRO A 1 1586 ? 203.789 234.200 164.118 1.00 22.49 ? 1586 PRO A C     1 
ATOM   1093  O  O     . PRO A 1 1586 ? 203.147 233.155 164.286 1.00 21.51 ? 1586 PRO A O     1 
ATOM   1094  C  CB    . PRO A 1 1586 ? 201.955 235.926 164.097 1.00 18.31 ? 1586 PRO A CB    1 
ATOM   1095  C  CG    . PRO A 1 1586 ? 202.362 236.880 163.025 1.00 16.40 ? 1586 PRO A CG    1 
ATOM   1096  C  CD    . PRO A 1 1586 ? 203.690 237.489 163.412 1.00 19.16 ? 1586 PRO A CD    1 
ATOM   1097  N  N     . LEU A 1 1587 ? 204.915 234.246 163.408 1.00 22.55 ? 1587 LEU A N     1 
ATOM   1098  C  CA    . LEU A 1 1587 ? 205.511 233.037 162.861 1.00 19.54 ? 1587 LEU A CA    1 
ATOM   1099  C  C     . LEU A 1 1587 ? 205.943 232.112 163.993 1.00 16.41 ? 1587 LEU A C     1 
ATOM   1100  O  O     . LEU A 1 1587 ? 206.513 232.556 164.993 1.00 18.74 ? 1587 LEU A O     1 
ATOM   1101  C  CB    . LEU A 1 1587 ? 206.709 233.395 161.979 1.00 20.35 ? 1587 LEU A CB    1 
ATOM   1102  C  CG    . LEU A 1 1587 ? 207.415 232.254 161.247 1.00 19.85 ? 1587 LEU A CG    1 
ATOM   1103  C  CD1   . LEU A 1 1587 ? 206.464 231.600 160.259 1.00 25.31 ? 1587 LEU A CD1   1 
ATOM   1104  C  CD2   . LEU A 1 1587 ? 208.668 232.751 160.543 1.00 23.70 ? 1587 LEU A CD2   1 
ATOM   1105  N  N     . VAL A 1 1588 ? 205.668 230.817 163.828 1.00 16.51 ? 1588 VAL A N     1 
ATOM   1106  C  CA    . VAL A 1 1588 ? 205.918 229.858 164.901 1.00 17.19 ? 1588 VAL A CA    1 
ATOM   1107  C  C     . VAL A 1 1588 ? 207.406 229.776 165.219 1.00 17.11 ? 1588 VAL A C     1 
ATOM   1108  O  O     . VAL A 1 1588 ? 207.803 229.727 166.390 1.00 19.31 ? 1588 VAL A O     1 
ATOM   1109  C  CB    . VAL A 1 1588 ? 205.337 228.480 164.532 1.00 14.66 ? 1588 VAL A CB    1 
ATOM   1110  C  CG1   . VAL A 1 1588 ? 205.749 227.436 165.555 1.00 10.48 ? 1588 VAL A CG1   1 
ATOM   1111  C  CG2   . VAL A 1 1588 ? 203.825 228.558 164.429 1.00 17.54 ? 1588 VAL A CG2   1 
ATOM   1112  N  N     . MET A 1 1589 ? 208.253 229.762 164.188 1.00 21.59 ? 1589 MET A N     1 
ATOM   1113  C  CA    . MET A 1 1589 ? 209.692 229.665 164.414 1.00 18.42 ? 1589 MET A CA    1 
ATOM   1114  C  C     . MET A 1 1589 ? 210.216 230.872 165.184 1.00 19.30 ? 1589 MET A C     1 
ATOM   1115  O  O     . MET A 1 1589 ? 211.068 230.729 166.068 1.00 19.82 ? 1589 MET A O     1 
ATOM   1116  C  CB    . MET A 1 1589 ? 210.422 229.513 163.081 1.00 14.14 ? 1589 MET A CB    1 
ATOM   1117  C  CG    . MET A 1 1589 ? 210.285 228.133 162.455 1.00 19.41 ? 1589 MET A CG    1 
ATOM   1118  S  SD    . MET A 1 1589 ? 210.312 226.798 163.668 1.00 39.80 ? 1589 MET A SD    1 
ATOM   1119  C  CE    . MET A 1 1589 ? 212.070 226.621 163.944 1.00 20.09 ? 1589 MET A CE    1 
ATOM   1120  N  N     . ASP A 1 1590 ? 209.718 232.069 164.863 1.00 20.15 ? 1590 ASP A N     1 
ATOM   1121  C  CA    . ASP A 1 1590 ? 210.125 233.258 165.606 1.00 17.25 ? 1590 ASP A CA    1 
ATOM   1122  C  C     . ASP A 1 1590 ? 209.708 233.168 167.068 1.00 17.46 ? 1590 ASP A C     1 
ATOM   1123  O  O     . ASP A 1 1590 ? 210.474 233.540 167.965 1.00 21.31 ? 1590 ASP A O     1 
ATOM   1124  C  CB    . ASP A 1 1590 ? 209.539 234.510 164.956 1.00 20.10 ? 1590 ASP A CB    1 
ATOM   1125  C  CG    . ASP A 1 1590 ? 210.153 234.807 163.603 1.00 32.95 ? 1590 ASP A CG    1 
ATOM   1126  O  OD1   . ASP A 1 1590 ? 211.332 234.450 163.393 1.00 35.20 ? 1590 ASP A OD1   1 
ATOM   1127  O  OD2   . ASP A 1 1590 ? 209.459 235.398 162.751 1.00 38.73 ? 1590 ASP A OD2   1 
ATOM   1128  N  N     . VAL A 1 1591 ? 208.492 232.681 167.329 1.00 12.12 ? 1591 VAL A N     1 
ATOM   1129  C  CA    . VAL A 1 1591 ? 208.056 232.482 168.707 1.00 12.26 ? 1591 VAL A CA    1 
ATOM   1130  C  C     . VAL A 1 1591 ? 208.906 231.415 169.383 1.00 14.88 ? 1591 VAL A C     1 
ATOM   1131  O  O     . VAL A 1 1591 ? 209.293 231.553 170.550 1.00 20.39 ? 1591 VAL A O     1 
ATOM   1132  C  CB    . VAL A 1 1591 ? 206.557 232.126 168.748 1.00 13.93 ? 1591 VAL A CB    1 
ATOM   1133  C  CG1   . VAL A 1 1591 ? 206.112 231.864 170.176 1.00 9.37  ? 1591 VAL A CG1   1 
ATOM   1134  C  CG2   . VAL A 1 1591 ? 205.731 233.242 168.133 1.00 13.86 ? 1591 VAL A CG2   1 
ATOM   1135  N  N     . LEU A 1 1592 ? 209.216 230.336 168.661 1.00 14.12 ? 1592 LEU A N     1 
ATOM   1136  C  CA    . LEU A 1 1592 ? 210.026 229.261 169.222 1.00 16.61 ? 1592 LEU A CA    1 
ATOM   1137  C  C     . LEU A 1 1592 ? 211.440 229.715 169.562 1.00 13.96 ? 1592 LEU A C     1 
ATOM   1138  O  O     . LEU A 1 1592 ? 212.074 229.122 170.441 1.00 15.26 ? 1592 LEU A O     1 
ATOM   1139  C  CB    . LEU A 1 1592 ? 210.073 228.081 168.246 1.00 19.30 ? 1592 LEU A CB    1 
ATOM   1140  C  CG    . LEU A 1 1592 ? 210.842 226.830 168.676 1.00 16.60 ? 1592 LEU A CG    1 
ATOM   1141  C  CD1   . LEU A 1 1592 ? 210.106 226.105 169.791 1.00 10.13 ? 1592 LEU A CD1   1 
ATOM   1142  C  CD2   . LEU A 1 1592 ? 211.084 225.908 167.494 1.00 15.51 ? 1592 LEU A CD2   1 
ATOM   1143  N  N     . ASN A 1 1593 ? 211.942 230.753 168.898 1.00 18.56 ? 1593 ASN A N     1 
ATOM   1144  C  CA    . ASN A 1 1593 ? 213.287 231.261 169.132 1.00 17.46 ? 1593 ASN A CA    1 
ATOM   1145  C  C     . ASN A 1 1593 ? 213.333 232.398 170.147 1.00 18.78 ? 1593 ASN A C     1 
ATOM   1146  O  O     . ASN A 1 1593 ? 214.412 232.945 170.391 1.00 22.36 ? 1593 ASN A O     1 
ATOM   1147  C  CB    . ASN A 1 1593 ? 213.908 231.728 167.812 1.00 17.85 ? 1593 ASN A CB    1 
ATOM   1148  C  CG    . ASN A 1 1593 ? 214.051 230.603 166.806 1.00 26.08 ? 1593 ASN A CG    1 
ATOM   1149  O  OD1   . ASN A 1 1593 ? 213.716 229.454 167.090 1.00 23.67 ? 1593 ASN A OD1   1 
ATOM   1150  N  ND2   . ASN A 1 1593 ? 214.545 230.930 165.618 1.00 24.55 ? 1593 ASN A ND2   1 
ATOM   1151  N  N     . ILE A 1 1594 ? 212.196 232.770 170.739 1.00 19.26 ? 1594 ILE A N     1 
ATOM   1152  C  CA    . ILE A 1 1594 ? 212.205 233.790 171.780 1.00 17.05 ? 1594 ILE A CA    1 
ATOM   1153  C  C     . ILE A 1 1594 ? 212.992 233.275 172.973 1.00 16.27 ? 1594 ILE A C     1 
ATOM   1154  O  O     . ILE A 1 1594 ? 212.808 232.133 173.409 1.00 21.73 ? 1594 ILE A O     1 
ATOM   1155  C  CB    . ILE A 1 1594 ? 210.765 234.176 172.164 1.00 14.12 ? 1594 ILE A CB    1 
ATOM   1156  C  CG1   . ILE A 1 1594 ? 210.041 234.782 170.961 1.00 12.79 ? 1594 ILE A CG1   1 
ATOM   1157  C  CG2   . ILE A 1 1594 ? 210.764 235.145 173.334 1.00 11.99 ? 1594 ILE A CG2   1 
ATOM   1158  C  CD1   . ILE A 1 1594 ? 208.618 235.193 171.241 1.00 10.90 ? 1594 ILE A CD1   1 
ATOM   1159  N  N     . GLN A 1 1595 ? 213.883 234.115 173.497 1.00 18.61 ? 1595 GLN A N     1 
ATOM   1160  C  CA    . GLN A 1 1595 ? 214.819 233.677 174.523 1.00 19.11 ? 1595 GLN A CA    1 
ATOM   1161  C  C     . GLN A 1 1595 ? 214.085 233.242 175.785 1.00 14.90 ? 1595 GLN A C     1 
ATOM   1162  O  O     . GLN A 1 1595 ? 213.319 234.011 176.372 1.00 13.42 ? 1595 GLN A O     1 
ATOM   1163  C  CB    . GLN A 1 1595 ? 215.804 234.799 174.847 1.00 17.32 ? 1595 GLN A CB    1 
ATOM   1164  C  CG    . GLN A 1 1595 ? 216.864 234.419 175.863 1.00 17.62 ? 1595 GLN A CG    1 
ATOM   1165  C  CD    . GLN A 1 1595 ? 217.827 235.554 176.149 1.00 30.99 ? 1595 GLN A CD    1 
ATOM   1166  O  OE1   . GLN A 1 1595 ? 217.705 236.645 175.590 1.00 31.14 ? 1595 GLN A OE1   1 
ATOM   1167  N  NE2   . GLN A 1 1595 ? 218.795 235.304 177.023 1.00 28.97 ? 1595 GLN A NE2   1 
ATOM   1168  N  N     . GLY A 1 1596 ? 214.326 231.999 176.196 1.00 18.89 ? 1596 GLY A N     1 
ATOM   1169  C  CA    . GLY A 1 1596 ? 213.732 231.470 177.409 1.00 15.15 ? 1596 GLY A CA    1 
ATOM   1170  C  C     . GLY A 1 1596 ? 212.230 231.336 177.371 1.00 17.14 ? 1596 GLY A C     1 
ATOM   1171  O  O     . GLY A 1 1596 ? 211.595 231.304 178.427 1.00 20.06 ? 1596 GLY A O     1 
ATOM   1172  N  N     . VAL A 1 1597 ? 211.639 231.251 176.178 1.00 17.81 ? 1597 VAL A N     1 
ATOM   1173  C  CA    . VAL A 1 1597 ? 210.184 231.183 176.077 1.00 12.72 ? 1597 VAL A CA    1 
ATOM   1174  C  C     . VAL A 1 1597 ? 209.663 229.891 176.696 1.00 12.64 ? 1597 VAL A C     1 
ATOM   1175  O  O     . VAL A 1 1597 ? 208.581 229.866 177.294 1.00 18.03 ? 1597 VAL A O     1 
ATOM   1176  C  CB    . VAL A 1 1597 ? 209.735 231.356 174.611 1.00 13.98 ? 1597 VAL A CB    1 
ATOM   1177  C  CG1   . VAL A 1 1597 ? 209.987 230.098 173.795 1.00 14.34 ? 1597 VAL A CG1   1 
ATOM   1178  C  CG2   . VAL A 1 1597 ? 208.267 231.750 174.551 1.00 16.70 ? 1597 VAL A CG2   1 
ATOM   1179  N  N     . GLN A 1 1598 ? 210.422 228.800 176.571 1.00 9.79  ? 1598 GLN A N     1 
ATOM   1180  C  CA    . GLN A 1 1598 ? 210.030 227.545 177.202 1.00 7.98  ? 1598 GLN A CA    1 
ATOM   1181  C  C     . GLN A 1 1598 ? 209.995 227.683 178.718 1.00 11.44 ? 1598 GLN A C     1 
ATOM   1182  O  O     . GLN A 1 1598 ? 209.044 227.245 179.375 1.00 14.46 ? 1598 GLN A O     1 
ATOM   1183  C  CB    . GLN A 1 1598 ? 210.984 226.429 176.785 1.00 9.93  ? 1598 GLN A CB    1 
ATOM   1184  C  CG    . GLN A 1 1598 ? 210.549 225.047 177.230 1.00 7.23  ? 1598 GLN A CG    1 
ATOM   1185  C  CD    . GLN A 1 1598 ? 209.190 224.665 176.692 1.00 9.60  ? 1598 GLN A CD    1 
ATOM   1186  O  OE1   . GLN A 1 1598 ? 208.984 224.621 175.482 1.00 18.28 ? 1598 GLN A OE1   1 
ATOM   1187  N  NE2   . GLN A 1 1598 ? 208.258 224.370 177.588 1.00 4.80  ? 1598 GLN A NE2   1 
ATOM   1188  N  N     . ARG A 1 1599 ? 211.030 228.297 179.292 1.00 16.93 ? 1599 ARG A N     1 
ATOM   1189  C  CA    . ARG A 1 1599 ? 211.076 228.449 180.741 1.00 14.36 ? 1599 ARG A CA    1 
ATOM   1190  C  C     . ARG A 1 1599 ? 210.098 229.517 181.213 1.00 13.39 ? 1599 ARG A C     1 
ATOM   1191  O  O     . ARG A 1 1599 ? 209.597 229.444 182.341 1.00 14.43 ? 1599 ARG A O     1 
ATOM   1192  C  CB    . ARG A 1 1599 ? 212.510 228.764 181.179 1.00 11.98 ? 1599 ARG A CB    1 
ATOM   1193  C  CG    . ARG A 1 1599 ? 212.756 228.763 182.686 1.00 17.19 ? 1599 ARG A CG    1 
ATOM   1194  C  CD    . ARG A 1 1599 ? 212.541 230.134 183.305 1.00 20.86 ? 1599 ARG A CD    1 
ATOM   1195  N  NE    . ARG A 1 1599 ? 213.454 231.130 182.760 1.00 26.89 ? 1599 ARG A NE    1 
ATOM   1196  C  CZ    . ARG A 1 1599 ? 213.292 232.440 182.884 1.00 35.27 ? 1599 ARG A CZ    1 
ATOM   1197  N  NH1   . ARG A 1 1599 ? 212.236 232.949 183.499 1.00 25.34 ? 1599 ARG A NH1   1 
ATOM   1198  N  NH2   . ARG A 1 1599 ? 214.206 233.259 182.373 1.00 24.13 ? 1599 ARG A NH2   1 
ATOM   1199  N  N     . SER A 1 1600 ? 209.806 230.507 180.366 1.00 11.11 ? 1600 SER A N     1 
ATOM   1200  C  CA    . SER A 1 1600 ? 208.826 231.526 180.729 1.00 10.83 ? 1600 SER A CA    1 
ATOM   1201  C  C     . SER A 1 1600 ? 207.440 230.918 180.897 1.00 17.03 ? 1600 SER A C     1 
ATOM   1202  O  O     . SER A 1 1600 ? 206.735 231.207 181.871 1.00 15.75 ? 1600 SER A O     1 
ATOM   1203  C  CB    . SER A 1 1600 ? 208.803 232.632 179.674 1.00 9.55  ? 1600 SER A CB    1 
ATOM   1204  O  OG    . SER A 1 1600 ? 210.041 233.317 179.622 1.00 16.20 ? 1600 SER A OG    1 
ATOM   1205  N  N     . LEU A 1 1601 ? 207.032 230.062 179.956 1.00 9.31  ? 1601 LEU A N     1 
ATOM   1206  C  CA    . LEU A 1 1601 ? 205.735 229.406 180.073 1.00 8.10  ? 1601 LEU A CA    1 
ATOM   1207  C  C     . LEU A 1 1601 ? 205.705 228.431 181.237 1.00 10.65 ? 1601 LEU A C     1 
ATOM   1208  O  O     . LEU A 1 1601 ? 204.681 228.302 181.917 1.00 16.00 ? 1601 LEU A O     1 
ATOM   1209  C  CB    . LEU A 1 1601 ? 205.367 228.682 178.777 1.00 11.69 ? 1601 LEU A CB    1 
ATOM   1210  C  CG    . LEU A 1 1601 ? 204.678 229.546 177.729 1.00 6.55  ? 1601 LEU A CG    1 
ATOM   1211  C  CD1   . LEU A 1 1601 ? 203.374 230.009 178.351 1.00 9.73  ? 1601 LEU A CD1   1 
ATOM   1212  C  CD2   . LEU A 1 1601 ? 205.516 230.716 177.267 1.00 11.63 ? 1601 LEU A CD2   1 
ATOM   1213  N  N     . GLU A 1 1602 ? 206.811 227.726 181.473 1.00 11.33 ? 1602 GLU A N     1 
ATOM   1214  C  CA    . GLU A 1 1602 ? 206.858 226.802 182.599 1.00 12.01 ? 1602 GLU A CA    1 
ATOM   1215  C  C     . GLU A 1 1602 ? 206.650 227.543 183.913 1.00 9.43  ? 1602 GLU A C     1 
ATOM   1216  O  O     . GLU A 1 1602 ? 205.949 227.054 184.806 1.00 7.47  ? 1602 GLU A O     1 
ATOM   1217  C  CB    . GLU A 1 1602 ? 208.185 226.046 182.600 1.00 14.88 ? 1602 GLU A CB    1 
ATOM   1218  C  CG    . GLU A 1 1602 ? 208.303 224.996 183.692 1.00 19.14 ? 1602 GLU A CG    1 
ATOM   1219  C  CD    . GLU A 1 1602 ? 209.611 224.233 183.630 1.00 28.04 ? 1602 GLU A CD    1 
ATOM   1220  O  OE1   . GLU A 1 1602 ? 210.440 224.538 182.745 1.00 31.37 ? 1602 GLU A OE1   1 
ATOM   1221  O  OE2   . GLU A 1 1602 ? 209.808 223.324 184.463 1.00 26.19 ? 1602 GLU A OE2   1 
ATOM   1222  N  N     . ARG A 1 1603 ? 207.238 228.734 184.042 1.00 6.55  ? 1603 ARG A N     1 
ATOM   1223  C  CA    . ARG A 1 1603 ? 207.018 229.536 185.239 1.00 10.71 ? 1603 ARG A CA    1 
ATOM   1224  C  C     . ARG A 1 1603 ? 205.606 230.110 185.266 1.00 11.16 ? 1603 ARG A C     1 
ATOM   1225  O  O     . ARG A 1 1603 ? 204.974 230.166 186.327 1.00 12.27 ? 1603 ARG A O     1 
ATOM   1226  C  CB    . ARG A 1 1603 ? 208.052 230.659 185.321 1.00 11.13 ? 1603 ARG A CB    1 
ATOM   1227  C  CG    . ARG A 1 1603 ? 207.875 231.548 186.536 1.00 12.89 ? 1603 ARG A CG    1 
ATOM   1228  C  CD    . ARG A 1 1603 ? 209.054 232.475 186.734 1.00 14.15 ? 1603 ARG A CD    1 
ATOM   1229  N  NE    . ARG A 1 1603 ? 208.621 233.824 187.080 1.00 20.57 ? 1603 ARG A NE    1 
ATOM   1230  C  CZ    . ARG A 1 1603 ? 208.358 234.778 186.199 1.00 16.67 ? 1603 ARG A CZ    1 
ATOM   1231  N  NH1   . ARG A 1 1603 ? 208.459 234.566 184.897 1.00 13.24 ? 1603 ARG A NH1   1 
ATOM   1232  N  NH2   . ARG A 1 1603 ? 207.984 235.977 186.635 1.00 16.85 ? 1603 ARG A NH2   1 
ATOM   1233  N  N     . LEU A 1 1604 ? 205.096 230.540 184.108 1.00 8.80  ? 1604 LEU A N     1 
ATOM   1234  C  CA    . LEU A 1 1604 ? 203.736 231.066 184.048 1.00 8.05  ? 1604 LEU A CA    1 
ATOM   1235  C  C     . LEU A 1 1604 ? 202.718 230.003 184.438 1.00 7.46  ? 1604 LEU A C     1 
ATOM   1236  O  O     . LEU A 1 1604 ? 201.758 230.289 185.162 1.00 10.07 ? 1604 LEU A O     1 
ATOM   1237  C  CB    . LEU A 1 1604 ? 203.435 231.601 182.648 1.00 7.90  ? 1604 LEU A CB    1 
ATOM   1238  C  CG    . LEU A 1 1604 ? 204.083 232.920 182.221 1.00 6.14  ? 1604 LEU A CG    1 
ATOM   1239  C  CD1   . LEU A 1 1604 ? 203.645 233.307 180.821 1.00 6.44  ? 1604 LEU A CD1   1 
ATOM   1240  C  CD2   . LEU A 1 1604 ? 203.777 234.030 183.201 1.00 8.77  ? 1604 LEU A CD2   1 
ATOM   1241  N  N     . ALA A 1 1605 ? 202.907 228.771 183.963 1.00 7.02  ? 1605 ALA A N     1 
ATOM   1242  C  CA    . ALA A 1 1605 ? 201.985 227.693 184.309 1.00 4.96  ? 1605 ALA A CA    1 
ATOM   1243  C  C     . ALA A 1 1605 ? 201.997 227.416 185.807 1.00 9.01  ? 1605 ALA A C     1 
ATOM   1244  O  O     . ALA A 1 1605 ? 200.940 227.284 186.434 1.00 11.78 ? 1605 ALA A O     1 
ATOM   1245  C  CB    . ALA A 1 1605 ? 202.340 226.430 183.524 1.00 3.33  ? 1605 ALA A CB    1 
ATOM   1246  N  N     . ASP A 1 1606 ? 203.191 227.329 186.398 1.00 9.93  ? 1606 ASP A N     1 
ATOM   1247  C  CA    . ASP A 1 1606 ? 203.286 227.067 187.830 1.00 8.31  ? 1606 ASP A CA    1 
ATOM   1248  C  C     . ASP A 1 1606 ? 202.724 228.225 188.646 1.00 10.08 ? 1606 ASP A C     1 
ATOM   1249  O  O     . ASP A 1 1606 ? 201.986 228.012 189.615 1.00 8.68  ? 1606 ASP A O     1 
ATOM   1250  C  CB    . ASP A 1 1606 ? 204.740 226.795 188.214 1.00 14.13 ? 1606 ASP A CB    1 
ATOM   1251  C  CG    . ASP A 1 1606 ? 204.938 226.705 189.714 1.00 26.68 ? 1606 ASP A CG    1 
ATOM   1252  O  OD1   . ASP A 1 1606 ? 204.383 225.773 190.333 1.00 20.89 ? 1606 ASP A OD1   1 
ATOM   1253  O  OD2   . ASP A 1 1606 ? 205.644 227.570 190.273 1.00 27.39 ? 1606 ASP A OD2   1 
ATOM   1254  N  N     . LEU A 1 1607 ? 203.063 229.458 188.265 1.00 9.15  ? 1607 LEU A N     1 
ATOM   1255  C  CA    . LEU A 1 1607 ? 202.603 230.620 189.016 1.00 6.26  ? 1607 LEU A CA    1 
ATOM   1256  C  C     . LEU A 1 1607 ? 201.090 230.784 188.930 1.00 8.87  ? 1607 LEU A C     1 
ATOM   1257  O  O     . LEU A 1 1607 ? 200.437 231.098 189.932 1.00 14.20 ? 1607 LEU A O     1 
ATOM   1258  C  CB    . LEU A 1 1607 ? 203.310 231.876 188.515 1.00 9.42  ? 1607 LEU A CB    1 
ATOM   1259  C  CG    . LEU A 1 1607 ? 204.763 232.105 188.931 1.00 13.56 ? 1607 LEU A CG    1 
ATOM   1260  C  CD1   . LEU A 1 1607 ? 205.208 233.493 188.503 1.00 11.09 ? 1607 LEU A CD1   1 
ATOM   1261  C  CD2   . LEU A 1 1607 ? 204.942 231.914 190.430 1.00 7.28  ? 1607 LEU A CD2   1 
ATOM   1262  N  N     . LEU A 1 1608 ? 200.514 230.587 187.740 1.00 8.79  ? 1608 LEU A N     1 
ATOM   1263  C  CA    . LEU A 1 1608 ? 199.065 230.697 187.599 1.00 5.20  ? 1608 LEU A CA    1 
ATOM   1264  C  C     . LEU A 1 1608 ? 198.344 229.604 188.375 1.00 7.48  ? 1608 LEU A C     1 
ATOM   1265  O  O     . LEU A 1 1608 ? 197.225 229.818 188.855 1.00 10.05 ? 1608 LEU A O     1 
ATOM   1266  C  CB    . LEU A 1 1608 ? 198.672 230.646 186.123 1.00 4.50  ? 1608 LEU A CB    1 
ATOM   1267  C  CG    . LEU A 1 1608 ? 198.898 231.914 185.298 1.00 4.15  ? 1608 LEU A CG    1 
ATOM   1268  C  CD1   . LEU A 1 1608 ? 198.781 231.611 183.812 1.00 2.84  ? 1608 LEU A CD1   1 
ATOM   1269  C  CD2   . LEU A 1 1608 ? 197.935 233.015 185.702 1.00 2.23  ? 1608 LEU A CD2   1 
ATOM   1270  N  N     . GLY A 1 1609 ? 198.962 228.430 188.506 1.00 6.18  ? 1609 GLY A N     1 
ATOM   1271  C  CA    . GLY A 1 1609 ? 198.375 227.379 189.317 1.00 6.39  ? 1609 GLY A CA    1 
ATOM   1272  C  C     . GLY A 1 1609 ? 198.308 227.731 190.788 1.00 12.73 ? 1609 GLY A C     1 
ATOM   1273  O  O     . GLY A 1 1609 ? 197.349 227.366 191.473 1.00 14.08 ? 1609 GLY A O     1 
ATOM   1274  N  N     . LYS A 1 1610 ? 199.321 228.434 191.297 1.00 13.97 ? 1610 LYS A N     1 
ATOM   1275  C  CA    . LYS A 1 1610 ? 199.306 228.853 192.695 1.00 11.36 ? 1610 LYS A CA    1 
ATOM   1276  C  C     . LYS A 1 1610 ? 198.184 229.847 192.963 1.00 11.53 ? 1610 LYS A C     1 
ATOM   1277  O  O     . LYS A 1 1610 ? 197.513 229.770 193.998 1.00 17.33 ? 1610 LYS A O     1 
ATOM   1278  C  CB    . LYS A 1 1610 ? 200.659 229.451 193.077 1.00 12.18 ? 1610 LYS A CB    1 
ATOM   1279  C  CG    . LYS A 1 1610 ? 201.825 228.493 192.927 1.00 12.37 ? 1610 LYS A CG    1 
ATOM   1280  C  CD    . LYS A 1 1610 ? 201.708 227.336 193.902 1.00 21.43 ? 1610 LYS A CD    1 
ATOM   1281  C  CE    . LYS A 1 1610 ? 202.952 226.464 193.878 1.00 26.49 ? 1610 LYS A CE    1 
ATOM   1282  N  NZ    . LYS A 1 1610 ? 203.080 225.715 192.600 1.00 25.01 ? 1610 LYS A NZ    1 
ATOM   1283  N  N     . ILE A 1 1611 ? 197.969 230.790 192.043 1.00 10.18 ? 1611 ILE A N     1 
ATOM   1284  C  CA    . ILE A 1 1611 ? 196.852 231.722 192.175 1.00 10.40 ? 1611 ILE A CA    1 
ATOM   1285  C  C     . ILE A 1 1611 ? 195.530 230.971 192.156 1.00 9.35  ? 1611 ILE A C     1 
ATOM   1286  O  O     . ILE A 1 1611 ? 194.601 231.297 192.905 1.00 16.46 ? 1611 ILE A O     1 
ATOM   1287  C  CB    . ILE A 1 1611 ? 196.912 232.785 191.064 1.00 8.32  ? 1611 ILE A CB    1 
ATOM   1288  C  CG1   . ILE A 1 1611 ? 198.180 233.619 191.199 1.00 8.55  ? 1611 ILE A CG1   1 
ATOM   1289  C  CG2   . ILE A 1 1611 ? 195.679 233.667 191.091 1.00 6.36  ? 1611 ILE A CG2   1 
ATOM   1290  C  CD1   . ILE A 1 1611 ? 198.424 234.489 190.015 1.00 11.94 ? 1611 ILE A CD1   1 
ATOM   1291  N  N     . GLN A 1 1612 ? 195.424 229.959 191.296 1.00 10.68 ? 1612 GLN A N     1 
ATOM   1292  C  CA    . GLN A 1 1612 ? 194.203 229.166 191.218 1.00 9.77  ? 1612 GLN A CA    1 
ATOM   1293  C  C     . GLN A 1 1612 ? 193.898 228.478 192.544 1.00 11.40 ? 1612 GLN A C     1 
ATOM   1294  O  O     . GLN A 1 1612 ? 192.750 228.474 192.999 1.00 15.52 ? 1612 GLN A O     1 
ATOM   1295  C  CB    . GLN A 1 1612 ? 194.334 228.144 190.094 1.00 9.54  ? 1612 GLN A CB    1 
ATOM   1296  C  CG    . GLN A 1 1612 ? 193.103 227.315 189.853 1.00 8.53  ? 1612 GLN A CG    1 
ATOM   1297  C  CD    . GLN A 1 1612 ? 193.277 226.366 188.695 1.00 9.42  ? 1612 GLN A CD    1 
ATOM   1298  O  OE1   . GLN A 1 1612 ? 194.342 226.302 188.084 1.00 14.71 ? 1612 GLN A OE1   1 
ATOM   1299  N  NE2   . GLN A 1 1612 ? 192.234 225.612 188.390 1.00 14.91 ? 1612 GLN A NE2   1 
ATOM   1300  N  N     . LYS A 1 1613 ? 194.916 227.901 193.182 1.00 11.65 ? 1613 LYS A N     1 
ATOM   1301  C  CA    . LYS A 1 1613 ? 194.719 227.210 194.450 1.00 9.94  ? 1613 LYS A CA    1 
ATOM   1302  C  C     . LYS A 1 1613 ? 194.511 228.162 195.618 1.00 12.63 ? 1613 LYS A C     1 
ATOM   1303  O  O     . LYS A 1 1613 ? 194.134 227.710 196.704 1.00 16.66 ? 1613 LYS A O     1 
ATOM   1304  C  CB    . LYS A 1 1613 ? 195.912 226.296 194.738 1.00 13.07 ? 1613 LYS A CB    1 
ATOM   1305  C  CG    . LYS A 1 1613 ? 196.219 225.312 193.623 1.00 14.05 ? 1613 LYS A CG    1 
ATOM   1306  C  CD    . LYS A 1 1613 ? 195.282 224.119 193.649 1.00 16.40 ? 1613 LYS A CD    1 
ATOM   1307  C  CE    . LYS A 1 1613 ? 195.589 223.157 192.511 1.00 17.64 ? 1613 LYS A CE    1 
ATOM   1308  N  NZ    . LYS A 1 1613 ? 196.206 223.852 191.345 1.00 15.29 ? 1613 LYS A NZ    1 
ATOM   1309  N  N     . ALA A 1 1614 ? 194.748 229.457 195.425 1.00 12.94 ? 1614 ALA A N     1 
ATOM   1310  C  CA    . ALA A 1 1614 ? 194.579 230.451 196.474 1.00 10.97 ? 1614 ALA A CA    1 
ATOM   1311  C  C     . ALA A 1 1614 ? 193.222 231.139 196.433 1.00 12.36 ? 1614 ALA A C     1 
ATOM   1312  O  O     . ALA A 1 1614 ? 192.958 232.005 197.272 1.00 13.63 ? 1614 ALA A O     1 
ATOM   1313  C  CB    . ALA A 1 1614 ? 195.692 231.497 196.386 1.00 12.92 ? 1614 ALA A CB    1 
ATOM   1314  N  N     . LEU A 1 1615 ? 192.359 230.778 195.486 1.00 11.34 ? 1615 LEU A N     1 
ATOM   1315  C  CA    . LEU A 1 1615 ? 191.034 231.369 195.364 1.00 8.71  ? 1615 LEU A CA    1 
ATOM   1316  C  C     . LEU A 1 1615 ? 189.943 230.490 195.962 1.00 8.65  ? 1615 LEU A C     1 
ATOM   1317  O  O     . LEU A 1 1615 ? 188.760 230.732 195.708 1.00 9.68  ? 1615 LEU A O     1 
ATOM   1318  C  CB    . LEU A 1 1615 ? 190.718 231.659 193.895 1.00 9.02  ? 1615 LEU A CB    1 
ATOM   1319  C  CG    . LEU A 1 1615 ? 191.617 232.660 193.166 1.00 9.65  ? 1615 LEU A CG    1 
ATOM   1320  C  CD1   . LEU A 1 1615 ? 190.938 233.179 191.911 1.00 8.91  ? 1615 LEU A CD1   1 
ATOM   1321  C  CD2   . LEU A 1 1615 ? 192.000 233.811 194.079 1.00 11.47 ? 1615 LEU A CD2   1 
ATOM   1322  N  N     . GLY A 1 1616 ? 190.316 229.478 196.748 1.00 11.00 ? 1616 GLY A N     1 
ATOM   1323  C  CA    . GLY A 1 1616 ? 189.329 228.541 197.255 1.00 6.14  ? 1616 GLY A CA    1 
ATOM   1324  C  C     . GLY A 1 1616 ? 188.285 229.189 198.144 1.00 11.83 ? 1616 GLY A C     1 
ATOM   1325  O  O     . GLY A 1 1616 ? 187.091 228.906 198.021 1.00 13.80 ? 1616 GLY A O     1 
ATOM   1326  N  N     . GLU A 1 1617 ? 188.716 230.066 199.054 1.00 9.88  ? 1617 GLU A N     1 
ATOM   1327  C  CA    . GLU A 1 1617 ? 187.755 230.705 199.950 1.00 12.16 ? 1617 GLU A CA    1 
ATOM   1328  C  C     . GLU A 1 1617 ? 186.882 231.699 199.195 1.00 10.40 ? 1617 GLU A C     1 
ATOM   1329  O  O     . GLU A 1 1617 ? 185.717 231.903 199.551 1.00 12.97 ? 1617 GLU A O     1 
ATOM   1330  C  CB    . GLU A 1 1617 ? 188.479 231.379 201.118 1.00 11.19 ? 1617 GLU A CB    1 
ATOM   1331  C  CG    . GLU A 1 1617 ? 189.440 232.483 200.726 1.00 23.65 ? 1617 GLU A CG    1 
ATOM   1332  C  CD    . GLU A 1 1617 ? 188.749 233.823 200.579 1.00 28.80 ? 1617 GLU A CD    1 
ATOM   1333  O  OE1   . GLU A 1 1617 ? 187.638 233.987 201.126 1.00 22.01 ? 1617 GLU A OE1   1 
ATOM   1334  O  OE2   . GLU A 1 1617 ? 189.303 234.704 199.897 1.00 30.63 ? 1617 GLU A OE2   1 
ATOM   1335  N  N     . TYR A 1 1618 ? 187.431 232.335 198.158 1.00 8.73  ? 1618 TYR A N     1 
ATOM   1336  C  CA    . TYR A 1 1618 ? 186.620 233.210 197.320 1.00 11.14 ? 1618 TYR A CA    1 
ATOM   1337  C  C     . TYR A 1 1618 ? 185.555 232.415 196.575 1.00 9.37  ? 1618 TYR A C     1 
ATOM   1338  O  O     . TYR A 1 1618 ? 184.425 232.887 196.402 1.00 9.99  ? 1618 TYR A O     1 
ATOM   1339  C  CB    . TYR A 1 1618 ? 187.511 233.974 196.338 1.00 6.90  ? 1618 TYR A CB    1 
ATOM   1340  C  CG    . TYR A 1 1618 ? 186.751 234.725 195.269 1.00 7.05  ? 1618 TYR A CG    1 
ATOM   1341  C  CD1   . TYR A 1 1618 ? 186.221 235.982 195.523 1.00 9.53  ? 1618 TYR A CD1   1 
ATOM   1342  C  CD2   . TYR A 1 1618 ? 186.567 234.180 194.005 1.00 8.56  ? 1618 TYR A CD2   1 
ATOM   1343  C  CE1   . TYR A 1 1618 ? 185.526 236.675 194.554 1.00 11.98 ? 1618 TYR A CE1   1 
ATOM   1344  C  CE2   . TYR A 1 1618 ? 185.872 234.865 193.027 1.00 10.95 ? 1618 TYR A CE2   1 
ATOM   1345  C  CZ    . TYR A 1 1618 ? 185.354 236.112 193.308 1.00 17.69 ? 1618 TYR A CZ    1 
ATOM   1346  O  OH    . TYR A 1 1618 ? 184.661 236.800 192.337 1.00 20.47 ? 1618 TYR A OH    1 
ATOM   1347  N  N     . LEU A 1 1619 ? 185.900 231.208 196.124 1.00 7.26  ? 1619 LEU A N     1 
ATOM   1348  C  CA    . LEU A 1 1619 ? 184.934 230.366 195.428 1.00 5.39  ? 1619 LEU A CA    1 
ATOM   1349  C  C     . LEU A 1 1619 ? 183.822 229.907 196.365 1.00 8.59  ? 1619 LEU A C     1 
ATOM   1350  O  O     . LEU A 1 1619 ? 182.661 229.808 195.954 1.00 12.23 ? 1619 LEU A O     1 
ATOM   1351  C  CB    . LEU A 1 1619 ? 185.642 229.167 194.805 1.00 5.37  ? 1619 LEU A CB    1 
ATOM   1352  C  CG    . LEU A 1 1619 ? 186.547 229.496 193.620 1.00 5.41  ? 1619 LEU A CG    1 
ATOM   1353  C  CD1   . LEU A 1 1619 ? 187.209 228.241 193.093 1.00 7.85  ? 1619 LEU A CD1   1 
ATOM   1354  C  CD2   . LEU A 1 1619 ? 185.765 230.199 192.524 1.00 3.74  ? 1619 LEU A CD2   1 
ATOM   1355  N  N     . GLU A 1 1620 ? 184.159 229.616 197.624 1.00 10.66 ? 1620 GLU A N     1 
ATOM   1356  C  CA    . GLU A 1 1620 ? 183.135 229.221 198.585 1.00 8.20  ? 1620 GLU A CA    1 
ATOM   1357  C  C     . GLU A 1 1620 ? 182.157 230.354 198.861 1.00 9.37  ? 1620 GLU A C     1 
ATOM   1358  O  O     . GLU A 1 1620 ? 181.001 230.104 199.217 1.00 17.73 ? 1620 GLU A O     1 
ATOM   1359  C  CB    . GLU A 1 1620 ? 183.788 228.751 199.886 1.00 8.22  ? 1620 GLU A CB    1 
ATOM   1360  C  CG    . GLU A 1 1620 ? 184.189 227.284 199.883 1.00 11.08 ? 1620 GLU A CG    1 
ATOM   1361  C  CD    . GLU A 1 1620 ? 183.001 226.348 199.748 1.00 16.73 ? 1620 GLU A CD    1 
ATOM   1362  O  OE1   . GLU A 1 1620 ? 182.207 226.246 200.704 1.00 14.17 ? 1620 GLU A OE1   1 
ATOM   1363  O  OE2   . GLU A 1 1620 ? 182.862 225.717 198.681 1.00 13.99 ? 1620 GLU A OE2   1 
ATOM   1364  N  N     . ARG A 1 1621 ? 182.598 231.603 198.703 1.00 5.92  ? 1621 ARG A N     1 
ATOM   1365  C  CA    . ARG A 1 1621 ? 181.696 232.732 198.894 1.00 7.99  ? 1621 ARG A CA    1 
ATOM   1366  C  C     . ARG A 1 1621 ? 180.739 232.883 197.718 1.00 10.96 ? 1621 ARG A C     1 
ATOM   1367  O  O     . ARG A 1 1621 ? 179.568 233.234 197.905 1.00 12.07 ? 1621 ARG A O     1 
ATOM   1368  C  CB    . ARG A 1 1621 ? 182.498 234.013 199.101 1.00 10.86 ? 1621 ARG A CB    1 
ATOM   1369  C  CG    . ARG A 1 1621 ? 181.716 235.136 199.757 1.00 12.45 ? 1621 ARG A CG    1 
ATOM   1370  C  CD    . ARG A 1 1621 ? 182.615 236.321 200.056 1.00 17.54 ? 1621 ARG A CD    1 
ATOM   1371  N  NE    . ARG A 1 1621 ? 183.306 236.789 198.861 1.00 19.51 ? 1621 ARG A NE    1 
ATOM   1372  C  CZ    . ARG A 1 1621 ? 182.844 237.729 198.048 1.00 28.20 ? 1621 ARG A CZ    1 
ATOM   1373  N  NH1   . ARG A 1 1621 ? 181.687 238.329 198.274 1.00 29.75 ? 1621 ARG A NH1   1 
ATOM   1374  N  NH2   . ARG A 1 1621 ? 183.560 238.076 196.983 1.00 24.97 ? 1621 ARG A NH2   1 
ATOM   1375  N  N     . GLU A 1 1622 ? 181.216 232.628 196.499 1.00 9.42  ? 1622 GLU A N     1 
ATOM   1376  C  CA    . GLU A 1 1622 ? 180.359 232.737 195.327 1.00 7.94  ? 1622 GLU A CA    1 
ATOM   1377  C  C     . GLU A 1 1622 ? 179.349 231.602 195.245 1.00 7.08  ? 1622 GLU A C     1 
ATOM   1378  O  O     . GLU A 1 1622 ? 178.290 231.776 194.632 1.00 8.88  ? 1622 GLU A O     1 
ATOM   1379  C  CB    . GLU A 1 1622 ? 181.208 232.772 194.054 1.00 9.64  ? 1622 GLU A CB    1 
ATOM   1380  C  CG    . GLU A 1 1622 ? 182.301 233.825 194.067 1.00 12.86 ? 1622 GLU A CG    1 
ATOM   1381  C  CD    . GLU A 1 1622 ? 181.809 235.184 193.609 1.00 21.05 ? 1622 GLU A CD    1 
ATOM   1382  O  OE1   . GLU A 1 1622 ? 181.358 235.297 192.450 1.00 23.33 ? 1622 GLU A OE1   1 
ATOM   1383  O  OE2   . GLU A 1 1622 ? 181.877 236.140 194.408 1.00 24.10 ? 1622 GLU A OE2   1 
ATOM   1384  N  N     . ARG A 1 1623 ? 179.650 230.450 195.849 1.00 5.47  ? 1623 ARG A N     1 
ATOM   1385  C  CA    . ARG A 1 1623 ? 178.726 229.323 195.800 1.00 4.57  ? 1623 ARG A CA    1 
ATOM   1386  C  C     . ARG A 1 1623 ? 177.419 229.635 196.519 1.00 7.04  ? 1623 ARG A C     1 
ATOM   1387  O  O     . ARG A 1 1623 ? 176.375 229.075 196.171 1.00 13.77 ? 1623 ARG A O     1 
ATOM   1388  C  CB    . ARG A 1 1623 ? 179.386 228.080 196.397 1.00 2.81  ? 1623 ARG A CB    1 
ATOM   1389  C  CG    . ARG A 1 1623 ? 180.321 227.356 195.439 1.00 2.95  ? 1623 ARG A CG    1 
ATOM   1390  C  CD    . ARG A 1 1623 ? 180.803 226.044 196.024 1.00 2.76  ? 1623 ARG A CD    1 
ATOM   1391  N  NE    . ARG A 1 1623 ? 182.202 225.771 195.707 1.00 7.80  ? 1623 ARG A NE    1 
ATOM   1392  C  CZ    . ARG A 1 1623 ? 182.634 225.286 194.552 1.00 5.90  ? 1623 ARG A CZ    1 
ATOM   1393  N  NH1   . ARG A 1 1623 ? 181.799 225.002 193.566 1.00 8.75  ? 1623 ARG A NH1   1 
ATOM   1394  N  NH2   . ARG A 1 1623 ? 183.934 225.070 194.384 1.00 3.39  ? 1623 ARG A NH2   1 
ATOM   1395  N  N     . SER A 1 1624 ? 177.456 230.518 197.516 1.00 5.92  ? 1624 SER A N     1 
ATOM   1396  C  CA    . SER A 1 1624 ? 176.227 230.919 198.195 1.00 6.62  ? 1624 SER A CA    1 
ATOM   1397  C  C     . SER A 1 1624 ? 175.314 231.714 197.271 1.00 8.39  ? 1624 SER A C     1 
ATOM   1398  O  O     . SER A 1 1624 ? 174.091 231.539 197.295 1.00 15.32 ? 1624 SER A O     1 
ATOM   1399  C  CB    . SER A 1 1624 ? 176.565 231.731 199.443 1.00 8.80  ? 1624 SER A CB    1 
ATOM   1400  O  OG    . SER A 1 1624 ? 177.276 230.945 200.382 1.00 20.17 ? 1624 SER A OG    1 
ATOM   1401  N  N     . SER A 1 1625 ? 175.890 232.590 196.444 1.00 8.23  ? 1625 SER A N     1 
ATOM   1402  C  CA    . SER A 1 1625 ? 175.089 233.451 195.581 1.00 7.20  ? 1625 SER A CA    1 
ATOM   1403  C  C     . SER A 1 1625 ? 174.344 232.673 194.505 1.00 9.41  ? 1625 SER A C     1 
ATOM   1404  O  O     . SER A 1 1625 ? 173.353 233.178 193.965 1.00 16.02 ? 1625 SER A O     1 
ATOM   1405  C  CB    . SER A 1 1625 ? 175.984 234.514 194.941 1.00 9.74  ? 1625 SER A CB    1 
ATOM   1406  O  OG    . SER A 1 1625 ? 176.859 233.937 193.988 1.00 16.69 ? 1625 SER A OG    1 
ATOM   1407  N  N     . PHE A 1 1626 ? 174.800 231.466 194.173 1.00 9.20  ? 1626 PHE A N     1 
ATOM   1408  C  CA    . PHE A 1 1626 ? 174.092 230.575 193.255 1.00 4.97  ? 1626 PHE A CA    1 
ATOM   1409  C  C     . PHE A 1 1626 ? 174.350 229.153 193.730 1.00 3.67  ? 1626 PHE A C     1 
ATOM   1410  O  O     . PHE A 1 1626 ? 175.340 228.522 193.341 1.00 2.61  ? 1626 PHE A O     1 
ATOM   1411  C  CB    . PHE A 1 1626 ? 174.545 230.779 191.809 1.00 2.87  ? 1626 PHE A CB    1 
ATOM   1412  C  CG    . PHE A 1 1626 ? 173.700 230.058 190.798 1.00 3.00  ? 1626 PHE A CG    1 
ATOM   1413  C  CD1   . PHE A 1 1626 ? 172.407 230.475 190.532 1.00 3.14  ? 1626 PHE A CD1   1 
ATOM   1414  C  CD2   . PHE A 1 1626 ? 174.205 228.972 190.103 1.00 3.57  ? 1626 PHE A CD2   1 
ATOM   1415  C  CE1   . PHE A 1 1626 ? 171.629 229.814 189.600 1.00 3.05  ? 1626 PHE A CE1   1 
ATOM   1416  C  CE2   . PHE A 1 1626 ? 173.434 228.308 189.169 1.00 2.72  ? 1626 PHE A CE2   1 
ATOM   1417  C  CZ    . PHE A 1 1626 ? 172.143 228.731 188.916 1.00 3.35  ? 1626 PHE A CZ    1 
ATOM   1418  N  N     . PRO A 1 1627 ? 173.470 228.613 194.579 1.00 4.42  ? 1627 PRO A N     1 
ATOM   1419  C  CA    . PRO A 1 1627 ? 173.799 227.367 195.295 1.00 3.28  ? 1627 PRO A CA    1 
ATOM   1420  C  C     . PRO A 1 1627 ? 174.015 226.156 194.404 1.00 2.11  ? 1627 PRO A C     1 
ATOM   1421  O  O     . PRO A 1 1627 ? 174.589 225.166 194.874 1.00 1.91  ? 1627 PRO A O     1 
ATOM   1422  C  CB    . PRO A 1 1627 ? 172.596 227.173 196.229 1.00 2.11  ? 1627 PRO A CB    1 
ATOM   1423  C  CG    . PRO A 1 1627 ? 171.507 228.006 195.645 1.00 3.67  ? 1627 PRO A CG    1 
ATOM   1424  C  CD    . PRO A 1 1627 ? 172.182 229.176 195.015 1.00 4.99  ? 1627 PRO A CD    1 
ATOM   1425  N  N     . ARG A 1 1628 ? 173.582 226.185 193.143 1.00 1.19  ? 1628 ARG A N     1 
ATOM   1426  C  CA    . ARG A 1 1628 ? 173.925 225.087 192.250 1.00 1.83  ? 1628 ARG A CA    1 
ATOM   1427  C  C     . ARG A 1 1628 ? 175.418 225.028 191.948 1.00 2.27  ? 1628 ARG A C     1 
ATOM   1428  O  O     . ARG A 1 1628 ? 175.882 224.016 191.415 1.00 1.78  ? 1628 ARG A O     1 
ATOM   1429  C  CB    . ARG A 1 1628 ? 173.124 225.186 190.951 1.00 1.99  ? 1628 ARG A CB    1 
ATOM   1430  C  CG    . ARG A 1 1628 ? 171.622 225.124 191.162 1.00 1.40  ? 1628 ARG A CG    1 
ATOM   1431  C  CD    . ARG A 1 1628 ? 170.861 225.224 189.858 1.00 1.88  ? 1628 ARG A CD    1 
ATOM   1432  N  NE    . ARG A 1 1628 ? 169.419 225.168 190.069 1.00 3.61  ? 1628 ARG A NE    1 
ATOM   1433  C  CZ    . ARG A 1 1628 ? 168.650 224.138 189.743 1.00 1.60  ? 1628 ARG A CZ    1 
ATOM   1434  N  NH1   . ARG A 1 1628 ? 169.156 223.043 189.199 1.00 2.65  ? 1628 ARG A NH1   1 
ATOM   1435  N  NH2   . ARG A 1 1628 ? 167.344 224.208 189.969 1.00 1.60  ? 1628 ARG A NH2   1 
ATOM   1436  N  N     . PHE A 1 1629 ? 176.173 226.079 192.281 1.00 2.35  ? 1629 PHE A N     1 
ATOM   1437  C  CA    . PHE A 1 1629 ? 177.626 226.027 192.184 1.00 1.76  ? 1629 PHE A CA    1 
ATOM   1438  C  C     . PHE A 1 1629 ? 178.241 225.085 193.209 1.00 1.09  ? 1629 PHE A C     1 
ATOM   1439  O  O     . PHE A 1 1629 ? 179.401 224.693 193.053 1.00 2.27  ? 1629 PHE A O     1 
ATOM   1440  C  CB    . PHE A 1 1629 ? 178.223 227.424 192.358 1.00 1.42  ? 1629 PHE A CB    1 
ATOM   1441  C  CG    . PHE A 1 1629 ? 178.022 228.324 191.176 1.00 0.84  ? 1629 PHE A CG    1 
ATOM   1442  C  CD1   . PHE A 1 1629 ? 177.820 227.798 189.911 1.00 1.09  ? 1629 PHE A CD1   1 
ATOM   1443  C  CD2   . PHE A 1 1629 ? 178.041 229.699 191.330 1.00 0.76  ? 1629 PHE A CD2   1 
ATOM   1444  C  CE1   . PHE A 1 1629 ? 177.637 228.630 188.825 1.00 1.43  ? 1629 PHE A CE1   1 
ATOM   1445  C  CE2   . PHE A 1 1629 ? 177.858 230.531 190.250 1.00 0.61  ? 1629 PHE A CE2   1 
ATOM   1446  C  CZ    . PHE A 1 1629 ? 177.657 229.999 188.996 1.00 1.63  ? 1629 PHE A CZ    1 
ATOM   1447  N  N     . TYR A 1 1630 ? 177.493 224.716 194.253 1.00 1.36  ? 1630 TYR A N     1 
ATOM   1448  C  CA    . TYR A 1 1630 ? 178.005 223.781 195.248 1.00 1.38  ? 1630 TYR A CA    1 
ATOM   1449  C  C     . TYR A 1 1630 ? 178.287 222.410 194.652 1.00 0.91  ? 1630 TYR A C     1 
ATOM   1450  O  O     . TYR A 1 1630 ? 179.023 221.622 195.254 1.00 0.89  ? 1630 TYR A O     1 
ATOM   1451  C  CB    . TYR A 1 1630 ? 177.021 223.645 196.410 1.00 0.68  ? 1630 TYR A CB    1 
ATOM   1452  C  CG    . TYR A 1 1630 ? 177.155 224.718 197.464 1.00 2.80  ? 1630 TYR A CG    1 
ATOM   1453  C  CD1   . TYR A 1 1630 ? 178.182 224.678 198.397 1.00 2.97  ? 1630 TYR A CD1   1 
ATOM   1454  C  CD2   . TYR A 1 1630 ? 176.252 225.769 197.530 1.00 4.03  ? 1630 TYR A CD2   1 
ATOM   1455  C  CE1   . TYR A 1 1630 ? 178.307 225.659 199.362 1.00 2.41  ? 1630 TYR A CE1   1 
ATOM   1456  C  CE2   . TYR A 1 1630 ? 176.369 226.753 198.487 1.00 3.27  ? 1630 TYR A CE2   1 
ATOM   1457  C  CZ    . TYR A 1 1630 ? 177.399 226.694 199.401 1.00 3.33  ? 1630 TYR A CZ    1 
ATOM   1458  O  OH    . TYR A 1 1630 ? 177.515 227.673 200.357 1.00 11.13 ? 1630 TYR A OH    1 
ATOM   1459  N  N     . PHE A 1 1631 ? 177.718 222.110 193.489 1.00 1.56  ? 1631 PHE A N     1 
ATOM   1460  C  CA    . PHE A 1 1631 ? 177.913 220.836 192.818 1.00 1.47  ? 1631 PHE A CA    1 
ATOM   1461  C  C     . PHE A 1 1631 ? 178.898 220.944 191.661 1.00 1.52  ? 1631 PHE A C     1 
ATOM   1462  O  O     . PHE A 1 1631 ? 178.901 220.091 190.770 1.00 5.97  ? 1631 PHE A O     1 
ATOM   1463  C  CB    . PHE A 1 1631 ? 176.565 220.296 192.347 1.00 2.03  ? 1631 PHE A CB    1 
ATOM   1464  C  CG    . PHE A 1 1631 ? 175.528 220.267 193.431 1.00 1.20  ? 1631 PHE A CG    1 
ATOM   1465  C  CD1   . PHE A 1 1631 ? 175.810 219.691 194.659 1.00 0.82  ? 1631 PHE A CD1   1 
ATOM   1466  C  CD2   . PHE A 1 1631 ? 174.285 220.842 193.236 1.00 1.70  ? 1631 PHE A CD2   1 
ATOM   1467  C  CE1   . PHE A 1 1631 ? 174.866 219.672 195.666 1.00 0.65  ? 1631 PHE A CE1   1 
ATOM   1468  C  CE2   . PHE A 1 1631 ? 173.335 220.828 194.239 1.00 1.45  ? 1631 PHE A CE2   1 
ATOM   1469  C  CZ    . PHE A 1 1631 ? 173.626 220.243 195.455 1.00 1.09  ? 1631 PHE A CZ    1 
ATOM   1470  N  N     . VAL A 1 1632 ? 179.735 221.976 191.670 1.00 1.98  ? 1632 VAL A N     1 
ATOM   1471  C  CA    . VAL A 1 1632 ? 180.739 222.218 190.643 1.00 2.31  ? 1632 VAL A CA    1 
ATOM   1472  C  C     . VAL A 1 1632 ? 182.102 222.278 191.316 1.00 1.71  ? 1632 VAL A C     1 
ATOM   1473  O  O     . VAL A 1 1632 ? 182.245 222.857 192.396 1.00 1.90  ? 1632 VAL A O     1 
ATOM   1474  C  CB    . VAL A 1 1632 ? 180.452 223.523 189.870 1.00 1.65  ? 1632 VAL A CB    1 
ATOM   1475  C  CG1   . VAL A 1 1632 ? 181.450 223.713 188.754 1.00 1.02  ? 1632 VAL A CG1   1 
ATOM   1476  C  CG2   . VAL A 1 1632 ? 179.037 223.521 189.324 1.00 1.59  ? 1632 VAL A CG2   1 
ATOM   1477  N  N     . GLY A 1 1633 ? 183.100 221.670 190.679 1.00 3.57  ? 1633 GLY A N     1 
ATOM   1478  C  CA    . GLY A 1 1633 ? 184.447 221.729 191.204 1.00 5.45  ? 1633 GLY A CA    1 
ATOM   1479  C  C     . GLY A 1 1633 ? 185.027 223.128 191.144 1.00 2.30  ? 1633 GLY A C     1 
ATOM   1480  O  O     . GLY A 1 1633 ? 184.516 224.022 190.468 1.00 1.39  ? 1633 GLY A O     1 
ATOM   1481  N  N     . ASP A 1 1634 ? 186.125 223.315 191.878 1.00 3.65  ? 1634 ASP A N     1 
ATOM   1482  C  CA    . ASP A 1 1634 ? 186.733 224.638 191.988 1.00 3.37  ? 1634 ASP A CA    1 
ATOM   1483  C  C     . ASP A 1 1634 ? 187.224 225.143 190.635 1.00 4.69  ? 1634 ASP A C     1 
ATOM   1484  O  O     . ASP A 1 1634 ? 186.990 226.300 190.273 1.00 3.87  ? 1634 ASP A O     1 
ATOM   1485  C  CB    . ASP A 1 1634 ? 187.879 224.607 192.998 1.00 3.64  ? 1634 ASP A CB    1 
ATOM   1486  C  CG    . ASP A 1 1634 ? 187.398 224.750 194.424 1.00 11.18 ? 1634 ASP A CG    1 
ATOM   1487  O  OD1   . ASP A 1 1634 ? 186.422 225.491 194.645 1.00 15.70 ? 1634 ASP A OD1   1 
ATOM   1488  O  OD2   . ASP A 1 1634 ? 187.996 224.124 195.324 1.00 18.07 ? 1634 ASP A OD2   1 
ATOM   1489  N  N     . GLU A 1 1635 ? 187.908 224.286 189.874 1.00 3.18  ? 1635 GLU A N     1 
ATOM   1490  C  CA    . GLU A 1 1635 ? 188.447 224.717 188.587 1.00 5.96  ? 1635 GLU A CA    1 
ATOM   1491  C  C     . GLU A 1 1635 ? 187.334 225.040 187.600 1.00 5.22  ? 1635 GLU A C     1 
ATOM   1492  O  O     . GLU A 1 1635 ? 187.409 226.038 186.874 1.00 7.73  ? 1635 GLU A O     1 
ATOM   1493  C  CB    . GLU A 1 1635 ? 189.380 223.650 188.016 1.00 14.55 ? 1635 GLU A CB    1 
ATOM   1494  C  CG    . GLU A 1 1635 ? 190.049 224.058 186.712 1.00 13.84 ? 1635 GLU A CG    1 
ATOM   1495  C  CD    . GLU A 1 1635 ? 191.009 223.007 186.191 1.00 25.41 ? 1635 GLU A CD    1 
ATOM   1496  O  OE1   . GLU A 1 1635 ? 191.141 221.945 186.835 1.00 32.31 ? 1635 GLU A OE1   1 
ATOM   1497  O  OE2   . GLU A 1 1635 ? 191.645 223.252 185.144 1.00 25.20 ? 1635 GLU A OE2   1 
ATOM   1498  N  N     . ASP A 1 1636 ? 186.294 224.208 187.559 1.00 5.40  ? 1636 ASP A N     1 
ATOM   1499  C  CA    . ASP A 1 1636 ? 185.172 224.478 186.667 1.00 5.52  ? 1636 ASP A CA    1 
ATOM   1500  C  C     . ASP A 1 1636 ? 184.436 225.746 187.077 1.00 3.14  ? 1636 ASP A C     1 
ATOM   1501  O  O     . ASP A 1 1636 ? 183.948 226.491 186.218 1.00 2.07  ? 1636 ASP A O     1 
ATOM   1502  C  CB    . ASP A 1 1636 ? 184.219 223.284 186.647 1.00 5.73  ? 1636 ASP A CB    1 
ATOM   1503  C  CG    . ASP A 1 1636 ? 184.819 222.071 185.974 1.00 13.75 ? 1636 ASP A CG    1 
ATOM   1504  O  OD1   . ASP A 1 1636 ? 185.667 222.243 185.074 1.00 18.09 ? 1636 ASP A OD1   1 
ATOM   1505  O  OD2   . ASP A 1 1636 ? 184.432 220.943 186.337 1.00 17.31 ? 1636 ASP A OD2   1 
ATOM   1506  N  N     . LEU A 1 1637 ? 184.332 225.999 188.384 1.00 2.06  ? 1637 LEU A N     1 
ATOM   1507  C  CA    . LEU A 1 1637 ? 183.685 227.219 188.854 1.00 1.98  ? 1637 LEU A CA    1 
ATOM   1508  C  C     . LEU A 1 1637 ? 184.466 228.459 188.434 1.00 2.75  ? 1637 LEU A C     1 
ATOM   1509  O  O     . LEU A 1 1637 ? 183.873 229.469 188.043 1.00 1.70  ? 1637 LEU A O     1 
ATOM   1510  C  CB    . LEU A 1 1637 ? 183.516 227.174 190.373 1.00 4.17  ? 1637 LEU A CB    1 
ATOM   1511  C  CG    . LEU A 1 1637 ? 182.768 228.352 191.004 1.00 1.77  ? 1637 LEU A CG    1 
ATOM   1512  C  CD1   . LEU A 1 1637 ? 181.436 228.584 190.312 1.00 0.61  ? 1637 LEU A CD1   1 
ATOM   1513  C  CD2   . LEU A 1 1637 ? 182.573 228.133 192.494 1.00 1.72  ? 1637 LEU A CD2   1 
ATOM   1514  N  N     . LEU A 1 1638 ? 185.799 228.401 188.510 1.00 4.51  ? 1638 LEU A N     1 
ATOM   1515  C  CA    . LEU A 1 1638 ? 186.616 229.516 188.038 1.00 2.73  ? 1638 LEU A CA    1 
ATOM   1516  C  C     . LEU A 1 1638 ? 186.402 229.758 186.551 1.00 2.75  ? 1638 LEU A C     1 
ATOM   1517  O  O     . LEU A 1 1638 ? 186.359 230.908 186.100 1.00 5.09  ? 1638 LEU A O     1 
ATOM   1518  C  CB    . LEU A 1 1638 ? 188.093 229.253 188.324 1.00 3.36  ? 1638 LEU A CB    1 
ATOM   1519  C  CG    . LEU A 1 1638 ? 188.526 229.134 189.784 1.00 4.20  ? 1638 LEU A CG    1 
ATOM   1520  C  CD1   . LEU A 1 1638 ? 189.658 228.140 189.905 1.00 4.72  ? 1638 LEU A CD1   1 
ATOM   1521  C  CD2   . LEU A 1 1638 ? 188.937 230.477 190.345 1.00 4.11  ? 1638 LEU A CD2   1 
ATOM   1522  N  N     . GLU A 1 1639 ? 186.272 228.683 185.772 1.00 2.13  ? 1639 GLU A N     1 
ATOM   1523  C  CA    . GLU A 1 1639 ? 185.954 228.831 184.358 1.00 3.25  ? 1639 GLU A CA    1 
ATOM   1524  C  C     . GLU A 1 1639 ? 184.588 229.480 184.169 1.00 4.68  ? 1639 GLU A C     1 
ATOM   1525  O  O     . GLU A 1 1639 ? 184.411 230.318 183.280 1.00 11.54 ? 1639 GLU A O     1 
ATOM   1526  C  CB    . GLU A 1 1639 ? 186.009 227.470 183.665 1.00 4.78  ? 1639 GLU A CB    1 
ATOM   1527  C  CG    . GLU A 1 1639 ? 185.768 227.522 182.167 1.00 12.64 ? 1639 GLU A CG    1 
ATOM   1528  C  CD    . GLU A 1 1639 ? 185.880 226.162 181.510 1.00 19.57 ? 1639 GLU A CD    1 
ATOM   1529  O  OE1   . GLU A 1 1639 ? 186.127 225.171 182.229 1.00 18.20 ? 1639 GLU A OE1   1 
ATOM   1530  O  OE2   . GLU A 1 1639 ? 185.714 226.083 180.276 1.00 18.93 ? 1639 GLU A OE2   1 
ATOM   1531  N  N     . ILE A 1 1640 ? 183.610 229.109 185.001 1.00 3.72  ? 1640 ILE A N     1 
ATOM   1532  C  CA    . ILE A 1 1640 ? 182.280 229.707 184.911 1.00 3.65  ? 1640 ILE A CA    1 
ATOM   1533  C  C     . ILE A 1 1640 ? 182.325 231.184 185.284 1.00 3.97  ? 1640 ILE A C     1 
ATOM   1534  O  O     . ILE A 1 1640 ? 181.791 232.036 184.566 1.00 5.97  ? 1640 ILE A O     1 
ATOM   1535  C  CB    . ILE A 1 1640 ? 181.284 228.928 185.791 1.00 5.39  ? 1640 ILE A CB    1 
ATOM   1536  C  CG1   . ILE A 1 1640 ? 181.054 227.522 185.232 1.00 2.93  ? 1640 ILE A CG1   1 
ATOM   1537  C  CG2   . ILE A 1 1640 ? 179.978 229.698 185.957 1.00 1.90  ? 1640 ILE A CG2   1 
ATOM   1538  C  CD1   . ILE A 1 1640 ? 180.572 226.523 186.261 1.00 1.08  ? 1640 ILE A CD1   1 
ATOM   1539  N  N     . ILE A 1 1641 ? 182.960 231.510 186.411 1.00 3.51  ? 1641 ILE A N     1 
ATOM   1540  C  CA    . ILE A 1 1641 ? 182.996 232.896 186.871 1.00 2.54  ? 1641 ILE A CA    1 
ATOM   1541  C  C     . ILE A 1 1641 ? 183.845 233.748 185.934 1.00 5.13  ? 1641 ILE A C     1 
ATOM   1542  O  O     . ILE A 1 1641 ? 183.441 234.845 185.528 1.00 3.33  ? 1641 ILE A O     1 
ATOM   1543  C  CB    . ILE A 1 1641 ? 183.515 232.971 188.319 1.00 4.04  ? 1641 ILE A CB    1 
ATOM   1544  C  CG1   . ILE A 1 1641 ? 182.674 232.094 189.249 1.00 3.74  ? 1641 ILE A CG1   1 
ATOM   1545  C  CG2   . ILE A 1 1641 ? 183.534 234.411 188.808 1.00 4.88  ? 1641 ILE A CG2   1 
ATOM   1546  C  CD1   . ILE A 1 1641 ? 181.208 232.410 189.236 1.00 4.94  ? 1641 ILE A CD1   1 
ATOM   1547  N  N     . GLY A 1 1642 ? 185.031 233.255 185.577 1.00 7.67  ? 1642 GLY A N     1 
ATOM   1548  C  CA    . GLY A 1 1642 ? 185.958 234.055 184.798 1.00 3.62  ? 1642 GLY A CA    1 
ATOM   1549  C  C     . GLY A 1 1642 ? 185.535 234.261 183.359 1.00 7.85  ? 1642 GLY A C     1 
ATOM   1550  O  O     . GLY A 1 1642 ? 185.895 235.269 182.744 1.00 12.58 ? 1642 GLY A O     1 
ATOM   1551  N  N     . ASN A 1 1643 ? 184.775 233.323 182.800 1.00 6.65  ? 1643 ASN A N     1 
ATOM   1552  C  CA    . ASN A 1 1643 ? 184.296 233.420 181.424 1.00 9.79  ? 1643 ASN A CA    1 
ATOM   1553  C  C     . ASN A 1 1643 ? 182.862 233.916 181.359 1.00 10.55 ? 1643 ASN A C     1 
ATOM   1554  O  O     . ASN A 1 1643 ? 182.107 233.542 180.459 1.00 13.27 ? 1643 ASN A O     1 
ATOM   1555  C  CB    . ASN A 1 1643 ? 184.430 232.074 180.719 1.00 12.12 ? 1643 ASN A CB    1 
ATOM   1556  C  CG    . ASN A 1 1643 ? 185.833 231.821 180.213 1.00 10.98 ? 1643 ASN A CG    1 
ATOM   1557  O  OD1   . ASN A 1 1643 ? 186.533 230.936 180.702 1.00 12.44 ? 1643 ASN A OD1   1 
ATOM   1558  N  ND2   . ASN A 1 1643 ? 186.250 232.598 179.222 1.00 18.29 ? 1643 ASN A ND2   1 
ATOM   1559  N  N     . SER A 1 1644 ? 182.468 234.779 182.299 1.00 14.82 ? 1644 SER A N     1 
ATOM   1560  C  CA    . SER A 1 1644 ? 181.089 235.248 182.357 1.00 12.05 ? 1644 SER A CA    1 
ATOM   1561  C  C     . SER A 1 1644 ? 180.687 236.027 181.112 1.00 16.26 ? 1644 SER A C     1 
ATOM   1562  O  O     . SER A 1 1644 ? 179.488 236.178 180.851 1.00 21.91 ? 1644 SER A O     1 
ATOM   1563  C  CB    . SER A 1 1644 ? 180.880 236.103 183.607 1.00 12.01 ? 1644 SER A CB    1 
ATOM   1564  O  OG    . SER A 1 1644 ? 181.497 237.371 183.468 1.00 19.22 ? 1644 SER A OG    1 
ATOM   1565  N  N     . LYS A 1 1645 ? 181.653 236.525 180.340 1.00 14.40 ? 1645 LYS A N     1 
ATOM   1566  C  CA    . LYS A 1 1645 ? 181.357 237.187 179.075 1.00 14.27 ? 1645 LYS A CA    1 
ATOM   1567  C  C     . LYS A 1 1645 ? 181.381 236.216 177.898 1.00 22.83 ? 1645 LYS A C     1 
ATOM   1568  O  O     . LYS A 1 1645 ? 180.602 236.372 176.951 1.00 29.58 ? 1645 LYS A O     1 
ATOM   1569  C  CB    . LYS A 1 1645 ? 182.346 238.327 178.835 1.00 19.21 ? 1645 LYS A CB    1 
ATOM   1570  C  CG    . LYS A 1 1645 ? 182.317 239.405 179.909 1.00 20.33 ? 1645 LYS A CG    1 
ATOM   1571  C  CD    . LYS A 1 1645 ? 183.503 240.346 179.791 1.00 17.79 ? 1645 LYS A CD    1 
ATOM   1572  C  CE    . LYS A 1 1645 ? 183.628 240.901 178.383 1.00 25.61 ? 1645 LYS A CE    1 
ATOM   1573  N  NZ    . LYS A 1 1645 ? 184.742 241.882 178.266 1.00 29.00 ? 1645 LYS A NZ    1 
ATOM   1574  N  N     . ASN A 1 1646 ? 182.258 235.214 177.938 1.00 19.73 ? 1646 ASN A N     1 
ATOM   1575  C  CA    . ASN A 1 1646 ? 182.326 234.187 176.898 1.00 15.10 ? 1646 ASN A CA    1 
ATOM   1576  C  C     . ASN A 1 1646 ? 181.343 233.083 177.265 1.00 17.60 ? 1646 ASN A C     1 
ATOM   1577  O  O     . ASN A 1 1646 ? 181.698 232.084 177.890 1.00 20.75 ? 1646 ASN A O     1 
ATOM   1578  C  CB    . ASN A 1 1646 ? 183.747 233.655 176.757 1.00 21.20 ? 1646 ASN A CB    1 
ATOM   1579  C  CG    . ASN A 1 1646 ? 184.755 234.752 176.485 1.00 27.11 ? 1646 ASN A CG    1 
ATOM   1580  O  OD1   . ASN A 1 1646 ? 185.610 235.048 177.321 1.00 25.19 ? 1646 ASN A OD1   1 
ATOM   1581  N  ND2   . ASN A 1 1646 ? 184.662 235.364 175.309 1.00 26.94 ? 1646 ASN A ND2   1 
ATOM   1582  N  N     . VAL A 1 1647 ? 180.084 233.270 176.863 1.00 19.86 ? 1647 VAL A N     1 
ATOM   1583  C  CA    . VAL A 1 1647 ? 179.019 232.356 177.264 1.00 13.13 ? 1647 VAL A CA    1 
ATOM   1584  C  C     . VAL A 1 1647 ? 179.165 230.990 176.604 1.00 13.07 ? 1647 VAL A C     1 
ATOM   1585  O  O     . VAL A 1 1647 ? 178.715 229.979 177.157 1.00 15.31 ? 1647 VAL A O     1 
ATOM   1586  C  CB    . VAL A 1 1647 ? 177.650 232.982 176.954 1.00 11.75 ? 1647 VAL A CB    1 
ATOM   1587  C  CG1   . VAL A 1 1647 ? 177.409 234.191 177.840 1.00 12.19 ? 1647 VAL A CG1   1 
ATOM   1588  C  CG2   . VAL A 1 1647 ? 177.597 233.385 175.497 1.00 15.93 ? 1647 VAL A CG2   1 
ATOM   1589  N  N     . ALA A 1 1648 ? 179.774 230.928 175.416 1.00 11.60 ? 1648 ALA A N     1 
ATOM   1590  C  CA    . ALA A 1 1648 ? 179.901 229.650 174.721 1.00 12.94 ? 1648 ALA A CA    1 
ATOM   1591  C  C     . ALA A 1 1648 ? 180.709 228.644 175.530 1.00 16.00 ? 1648 ALA A C     1 
ATOM   1592  O  O     . ALA A 1 1648 ? 180.505 227.432 175.396 1.00 19.00 ? 1648 ALA A O     1 
ATOM   1593  C  CB    . ALA A 1 1648 ? 180.535 229.856 173.346 1.00 13.52 ? 1648 ALA A CB    1 
ATOM   1594  N  N     . LYS A 1 1649 ? 181.625 229.119 176.372 1.00 13.41 ? 1649 LYS A N     1 
ATOM   1595  C  CA    . LYS A 1 1649 ? 182.397 228.234 177.231 1.00 13.88 ? 1649 LYS A CA    1 
ATOM   1596  C  C     . LYS A 1 1649 ? 181.610 227.751 178.442 1.00 10.71 ? 1649 LYS A C     1 
ATOM   1597  O  O     . LYS A 1 1649 ? 182.067 226.832 179.131 1.00 11.86 ? 1649 LYS A O     1 
ATOM   1598  C  CB    . LYS A 1 1649 ? 183.676 228.939 177.686 1.00 13.62 ? 1649 LYS A CB    1 
ATOM   1599  C  CG    . LYS A 1 1649 ? 184.623 229.258 176.546 1.00 14.38 ? 1649 LYS A CG    1 
ATOM   1600  C  CD    . LYS A 1 1649 ? 185.785 230.115 177.001 1.00 16.17 ? 1649 LYS A CD    1 
ATOM   1601  C  CE    . LYS A 1 1649 ? 186.431 230.812 175.819 1.00 25.68 ? 1649 LYS A CE    1 
ATOM   1602  N  NZ    . LYS A 1 1649 ? 185.408 231.430 174.929 1.00 27.12 ? 1649 LYS A NZ    1 
ATOM   1603  N  N     . LEU A 1 1650 ? 180.446 228.336 178.709 1.00 10.51 ? 1650 LEU A N     1 
ATOM   1604  C  CA    . LEU A 1 1650 ? 179.604 227.933 179.826 1.00 6.58  ? 1650 LEU A CA    1 
ATOM   1605  C  C     . LEU A 1 1650 ? 178.766 226.704 179.528 1.00 8.48  ? 1650 LEU A C     1 
ATOM   1606  O  O     . LEU A 1 1650 ? 178.223 226.104 180.462 1.00 8.19  ? 1650 LEU A O     1 
ATOM   1607  C  CB    . LEU A 1 1650 ? 178.670 229.079 180.234 1.00 6.59  ? 1650 LEU A CB    1 
ATOM   1608  C  CG    . LEU A 1 1650 ? 179.195 230.170 181.165 1.00 7.91  ? 1650 LEU A CG    1 
ATOM   1609  C  CD1   . LEU A 1 1650 ? 179.530 229.551 182.498 1.00 6.09  ? 1650 LEU A CD1   1 
ATOM   1610  C  CD2   . LEU A 1 1650 ? 180.404 230.878 180.593 1.00 14.10 ? 1650 LEU A CD2   1 
ATOM   1611  N  N     . GLN A 1 1651 ? 178.661 226.307 178.257 1.00 7.64  ? 1651 GLN A N     1 
ATOM   1612  C  CA    . GLN A 1 1651 ? 177.699 225.280 177.875 1.00 6.14  ? 1651 GLN A CA    1 
ATOM   1613  C  C     . GLN A 1 1651 ? 178.031 223.935 178.510 1.00 6.91  ? 1651 GLN A C     1 
ATOM   1614  O  O     . GLN A 1 1651 ? 177.131 223.212 178.948 1.00 10.76 ? 1651 GLN A O     1 
ATOM   1615  C  CB    . GLN A 1 1651 ? 177.646 225.161 176.351 1.00 7.16  ? 1651 GLN A CB    1 
ATOM   1616  C  CG    . GLN A 1 1651 ? 177.176 226.423 175.625 1.00 6.59  ? 1651 GLN A CG    1 
ATOM   1617  C  CD    . GLN A 1 1651 ? 175.692 226.713 175.790 1.00 5.74  ? 1651 GLN A CD    1 
ATOM   1618  O  OE1   . GLN A 1 1651 ? 175.024 226.149 176.652 1.00 13.69 ? 1651 GLN A OE1   1 
ATOM   1619  N  NE2   . GLN A 1 1651 ? 175.170 227.597 174.951 1.00 5.31  ? 1651 GLN A NE2   1 
ATOM   1620  N  N     . LYS A 1 1652 ? 179.318 223.589 178.583 1.00 6.78  ? 1652 LYS A N     1 
ATOM   1621  C  CA    . LYS A 1 1652 ? 179.718 222.281 179.087 1.00 7.13  ? 1652 LYS A CA    1 
ATOM   1622  C  C     . LYS A 1 1652 ? 179.447 222.099 180.575 1.00 5.35  ? 1652 LYS A C     1 
ATOM   1623  O  O     . LYS A 1 1652 ? 179.518 220.966 181.061 1.00 6.97  ? 1652 LYS A O     1 
ATOM   1624  C  CB    . LYS A 1 1652 ? 181.206 222.042 178.818 1.00 6.19  ? 1652 LYS A CB    1 
ATOM   1625  C  CG    . LYS A 1 1652 ? 182.131 222.988 179.564 1.00 8.77  ? 1652 LYS A CG    1 
ATOM   1626  C  CD    . LYS A 1 1652 ? 183.592 222.686 179.280 1.00 11.74 ? 1652 LYS A CD    1 
ATOM   1627  C  CE    . LYS A 1 1652 ? 183.993 223.115 177.883 1.00 20.05 ? 1652 LYS A CE    1 
ATOM   1628  N  NZ    . LYS A 1 1652 ? 185.453 222.939 177.655 1.00 18.11 ? 1652 LYS A NZ    1 
ATOM   1629  N  N     . HIS A 1 1653 ? 179.147 223.169 181.310 1.00 5.13  ? 1653 HIS A N     1 
ATOM   1630  C  CA    . HIS A 1 1653 ? 178.991 223.085 182.756 1.00 4.34  ? 1653 HIS A CA    1 
ATOM   1631  C  C     . HIS A 1 1653 ? 177.543 222.992 183.216 1.00 3.56  ? 1653 HIS A C     1 
ATOM   1632  O  O     . HIS A 1 1653 ? 177.308 222.748 184.404 1.00 3.80  ? 1653 HIS A O     1 
ATOM   1633  C  CB    . HIS A 1 1653 ? 179.650 224.293 183.430 1.00 4.91  ? 1653 HIS A CB    1 
ATOM   1634  C  CG    . HIS A 1 1653 ? 181.096 224.461 183.088 1.00 4.92  ? 1653 HIS A CG    1 
ATOM   1635  N  ND1   . HIS A 1 1653 ? 182.062 223.563 183.485 1.00 6.02  ? 1653 HIS A ND1   1 
ATOM   1636  C  CD2   . HIS A 1 1653 ? 181.741 225.424 182.392 1.00 5.71  ? 1653 HIS A CD2   1 
ATOM   1637  C  CE1   . HIS A 1 1653 ? 183.240 223.965 183.046 1.00 5.35  ? 1653 HIS A CE1   1 
ATOM   1638  N  NE2   . HIS A 1 1653 ? 183.074 225.092 182.379 1.00 8.73  ? 1653 HIS A NE2   1 
ATOM   1639  N  N     . PHE A 1 1654 ? 176.572 223.172 182.318 1.00 4.04  ? 1654 PHE A N     1 
ATOM   1640  C  CA    . PHE A 1 1654 ? 175.176 223.184 182.743 1.00 2.77  ? 1654 PHE A CA    1 
ATOM   1641  C  C     . PHE A 1 1654 ? 174.701 221.809 183.195 1.00 3.66  ? 1654 PHE A C     1 
ATOM   1642  O  O     . PHE A 1 1654 ? 173.818 221.718 184.054 1.00 8.33  ? 1654 PHE A O     1 
ATOM   1643  C  CB    . PHE A 1 1654 ? 174.283 223.713 181.622 1.00 3.46  ? 1654 PHE A CB    1 
ATOM   1644  C  CG    . PHE A 1 1654 ? 174.413 225.190 181.395 1.00 3.61  ? 1654 PHE A CG    1 
ATOM   1645  C  CD1   . PHE A 1 1654 ? 173.872 226.092 182.295 1.00 3.00  ? 1654 PHE A CD1   1 
ATOM   1646  C  CD2   . PHE A 1 1654 ? 175.077 225.678 180.283 1.00 4.30  ? 1654 PHE A CD2   1 
ATOM   1647  C  CE1   . PHE A 1 1654 ? 173.992 227.450 182.091 1.00 2.45  ? 1654 PHE A CE1   1 
ATOM   1648  C  CE2   . PHE A 1 1654 ? 175.198 227.038 180.074 1.00 3.39  ? 1654 PHE A CE2   1 
ATOM   1649  C  CZ    . PHE A 1 1654 ? 174.656 227.925 180.980 1.00 2.44  ? 1654 PHE A CZ    1 
ATOM   1650  N  N     . LYS A 1 1655 ? 175.266 220.732 182.640 1.00 3.52  ? 1655 LYS A N     1 
ATOM   1651  C  CA    . LYS A 1 1655 ? 174.853 219.397 183.056 1.00 2.95  ? 1655 LYS A CA    1 
ATOM   1652  C  C     . LYS A 1 1655 ? 175.205 219.115 184.509 1.00 2.52  ? 1655 LYS A C     1 
ATOM   1653  O  O     . LYS A 1 1655 ? 174.607 218.224 185.120 1.00 5.09  ? 1655 LYS A O     1 
ATOM   1654  C  CB    . LYS A 1 1655 ? 175.483 218.328 182.158 1.00 3.81  ? 1655 LYS A CB    1 
ATOM   1655  C  CG    . LYS A 1 1655 ? 176.998 218.241 182.250 1.00 8.87  ? 1655 LYS A CG    1 
ATOM   1656  C  CD    . LYS A 1 1655 ? 177.553 217.142 181.352 1.00 5.37  ? 1655 LYS A CD    1 
ATOM   1657  C  CE    . LYS A 1 1655 ? 177.487 217.527 179.888 1.00 11.01 ? 1655 LYS A CE    1 
ATOM   1658  N  NZ    . LYS A 1 1655 ? 178.146 216.514 179.018 1.00 18.02 ? 1655 LYS A NZ    1 
ATOM   1659  N  N     . LYS A 1 1656 ? 176.163 219.847 185.072 1.00 3.17  ? 1656 LYS A N     1 
ATOM   1660  C  CA    . LYS A 1 1656 ? 176.540 219.670 186.466 1.00 4.11  ? 1656 LYS A CA    1 
ATOM   1661  C  C     . LYS A 1 1656 ? 175.634 220.432 187.422 1.00 4.18  ? 1656 LYS A C     1 
ATOM   1662  O  O     . LYS A 1 1656 ? 175.477 220.016 188.575 1.00 9.50  ? 1656 LYS A O     1 
ATOM   1663  C  CB    . LYS A 1 1656 ? 177.991 220.110 186.675 1.00 5.14  ? 1656 LYS A CB    1 
ATOM   1664  C  CG    . LYS A 1 1656 ? 178.917 219.697 185.550 1.00 4.47  ? 1656 LYS A CG    1 
ATOM   1665  C  CD    . LYS A 1 1656 ? 180.305 220.286 185.714 1.00 4.07  ? 1656 LYS A CD    1 
ATOM   1666  C  CE    . LYS A 1 1656 ? 181.086 220.177 184.418 1.00 7.82  ? 1656 LYS A CE    1 
ATOM   1667  N  NZ    . LYS A 1 1656 ? 182.437 220.775 184.523 1.00 10.03 ? 1656 LYS A NZ    1 
ATOM   1668  N  N     . MET A 1 1657 ? 175.031 221.531 186.972 1.00 2.62  ? 1657 MET A N     1 
ATOM   1669  C  CA    . MET A 1 1657 ? 174.192 222.360 187.826 1.00 2.57  ? 1657 MET A CA    1 
ATOM   1670  C  C     . MET A 1 1657 ? 172.704 222.080 187.669 1.00 1.89  ? 1657 MET A C     1 
ATOM   1671  O  O     . MET A 1 1657 ? 171.912 222.575 188.476 1.00 2.24  ? 1657 MET A O     1 
ATOM   1672  C  CB    . MET A 1 1657 ? 174.447 223.846 187.543 1.00 3.82  ? 1657 MET A CB    1 
ATOM   1673  C  CG    . MET A 1 1657 ? 175.891 224.278 187.684 1.00 2.17  ? 1657 MET A CG    1 
ATOM   1674  S  SD    . MET A 1 1657 ? 176.143 225.978 187.148 1.00 12.66 ? 1657 MET A SD    1 
ATOM   1675  C  CE    . MET A 1 1657 ? 176.210 225.777 185.371 1.00 3.20  ? 1657 MET A CE    1 
ATOM   1676  N  N     . PHE A 1 1658 ? 172.303 221.309 186.665 1.00 2.95  ? 1658 PHE A N     1 
ATOM   1677  C  CA    . PHE A 1 1658 ? 170.896 221.093 186.373 1.00 2.74  ? 1658 PHE A CA    1 
ATOM   1678  C  C     . PHE A 1 1658 ? 170.640 219.614 186.118 1.00 4.08  ? 1658 PHE A C     1 
ATOM   1679  O  O     . PHE A 1 1658 ? 171.539 218.862 185.737 1.00 4.20  ? 1658 PHE A O     1 
ATOM   1680  C  CB    . PHE A 1 1658 ? 170.442 221.922 185.167 1.00 1.06  ? 1658 PHE A CB    1 
ATOM   1681  C  CG    . PHE A 1 1658 ? 170.350 223.395 185.439 1.00 1.49  ? 1658 PHE A CG    1 
ATOM   1682  C  CD1   . PHE A 1 1658 ? 171.465 224.209 185.313 1.00 2.11  ? 1658 PHE A CD1   1 
ATOM   1683  C  CD2   . PHE A 1 1658 ? 169.148 223.971 185.813 1.00 1.88  ? 1658 PHE A CD2   1 
ATOM   1684  C  CE1   . PHE A 1 1658 ? 171.383 225.566 185.560 1.00 2.12  ? 1658 PHE A CE1   1 
ATOM   1685  C  CE2   . PHE A 1 1658 ? 169.059 225.327 186.060 1.00 1.85  ? 1658 PHE A CE2   1 
ATOM   1686  C  CZ    . PHE A 1 1658 ? 170.179 226.127 185.934 1.00 2.21  ? 1658 PHE A CZ    1 
ATOM   1687  N  N     . ALA A 1 1659 ? 169.390 219.208 186.343 1.00 2.81  ? 1659 ALA A N     1 
ATOM   1688  C  CA    . ALA A 1 1659 ? 169.009 217.816 186.127 1.00 2.01  ? 1659 ALA A CA    1 
ATOM   1689  C  C     . ALA A 1 1659 ? 168.996 217.468 184.644 1.00 3.28  ? 1659 ALA A C     1 
ATOM   1690  O  O     . ALA A 1 1659 ? 169.537 216.435 184.235 1.00 8.38  ? 1659 ALA A O     1 
ATOM   1691  C  CB    . ALA A 1 1659 ? 167.642 217.544 186.753 1.00 1.97  ? 1659 ALA A CB    1 
ATOM   1692  N  N     . GLY A 1 1660 ? 168.388 218.319 183.822 1.00 1.99  ? 1660 GLY A N     1 
ATOM   1693  C  CA    . GLY A 1 1660 ? 168.234 218.011 182.416 1.00 2.02  ? 1660 GLY A CA    1 
ATOM   1694  C  C     . GLY A 1 1660 ? 168.559 219.147 181.469 1.00 2.48  ? 1660 GLY A C     1 
ATOM   1695  O  O     . GLY A 1 1660 ? 168.251 219.069 180.277 1.00 4.22  ? 1660 GLY A O     1 
ATOM   1696  N  N     . VAL A 1 1661 ? 169.178 220.208 181.974 1.00 2.50  ? 1661 VAL A N     1 
ATOM   1697  C  CA    . VAL A 1 1661 ? 169.606 221.321 181.138 1.00 2.39  ? 1661 VAL A CA    1 
ATOM   1698  C  C     . VAL A 1 1661 ? 171.047 221.058 180.720 1.00 4.28  ? 1661 VAL A C     1 
ATOM   1699  O  O     . VAL A 1 1661 ? 171.964 221.127 181.541 1.00 7.25  ? 1661 VAL A O     1 
ATOM   1700  C  CB    . VAL A 1 1661 ? 169.475 222.666 181.862 1.00 1.58  ? 1661 VAL A CB    1 
ATOM   1701  C  CG1   . VAL A 1 1661 ? 170.050 223.781 181.008 1.00 1.99  ? 1661 VAL A CG1   1 
ATOM   1702  C  CG2   . VAL A 1 1661 ? 168.025 222.943 182.216 1.00 1.37  ? 1661 VAL A CG2   1 
ATOM   1703  N  N     . SER A 1 1662 ? 171.246 220.746 179.443 1.00 4.88  ? 1662 SER A N     1 
ATOM   1704  C  CA    . SER A 1 1662 ? 172.588 220.527 178.925 1.00 5.43  ? 1662 SER A CA    1 
ATOM   1705  C  C     . SER A 1 1662 ? 173.175 221.777 178.285 1.00 4.98  ? 1662 SER A C     1 
ATOM   1706  O  O     . SER A 1 1662 ? 174.398 221.947 178.284 1.00 8.38  ? 1662 SER A O     1 
ATOM   1707  C  CB    . SER A 1 1662 ? 172.581 219.379 177.912 1.00 6.89  ? 1662 SER A CB    1 
ATOM   1708  O  OG    . SER A 1 1662 ? 173.871 219.164 177.374 1.00 17.85 ? 1662 SER A OG    1 
ATOM   1709  N  N     . SER A 1 1663 ? 172.331 222.655 177.752 1.00 4.24  ? 1663 SER A N     1 
ATOM   1710  C  CA    . SER A 1 1663 ? 172.792 223.888 177.134 1.00 3.36  ? 1663 SER A CA    1 
ATOM   1711  C  C     . SER A 1 1663 ? 171.656 224.898 177.149 1.00 5.02  ? 1663 SER A C     1 
ATOM   1712  O  O     . SER A 1 1663 ? 170.494 224.550 177.376 1.00 6.35  ? 1663 SER A O     1 
ATOM   1713  C  CB    . SER A 1 1663 ? 173.287 223.654 175.701 1.00 3.86  ? 1663 SER A CB    1 
ATOM   1714  O  OG    . SER A 1 1663 ? 172.224 223.280 174.844 1.00 6.12  ? 1663 SER A OG    1 
ATOM   1715  N  N     . ILE A 1 1664 ? 172.010 226.153 176.905 1.00 4.27  ? 1664 ILE A N     1 
ATOM   1716  C  CA    . ILE A 1 1664 ? 171.048 227.244 176.814 1.00 4.20  ? 1664 ILE A CA    1 
ATOM   1717  C  C     . ILE A 1 1664 ? 171.028 227.761 175.383 1.00 5.29  ? 1664 ILE A C     1 
ATOM   1718  O  O     . ILE A 1 1664 ? 172.026 227.677 174.658 1.00 8.38  ? 1664 ILE A O     1 
ATOM   1719  C  CB    . ILE A 1 1664 ? 171.378 228.378 177.809 1.00 5.62  ? 1664 ILE A CB    1 
ATOM   1720  C  CG1   . ILE A 1 1664 ? 172.802 228.889 177.583 1.00 6.31  ? 1664 ILE A CG1   1 
ATOM   1721  C  CG2   . ILE A 1 1664 ? 171.200 227.906 179.240 1.00 3.25  ? 1664 ILE A CG2   1 
ATOM   1722  C  CD1   . ILE A 1 1664 ? 173.173 230.059 178.455 1.00 3.56  ? 1664 ILE A CD1   1 
ATOM   1723  N  N     . ILE A 1 1665 ? 169.877 228.286 174.971 1.00 7.10  ? 1665 ILE A N     1 
ATOM   1724  C  CA    . ILE A 1 1665 ? 169.709 228.884 173.650 1.00 6.47  ? 1665 ILE A CA    1 
ATOM   1725  C  C     . ILE A 1 1665 ? 169.931 230.384 173.765 1.00 8.59  ? 1665 ILE A C     1 
ATOM   1726  O  O     . ILE A 1 1665 ? 169.372 231.041 174.652 1.00 10.07 ? 1665 ILE A O     1 
ATOM   1727  C  CB    . ILE A 1 1665 ? 168.326 228.577 173.047 1.00 5.59  ? 1665 ILE A CB    1 
ATOM   1728  C  CG1   . ILE A 1 1665 ? 168.156 227.080 172.790 1.00 6.45  ? 1665 ILE A CG1   1 
ATOM   1729  C  CG2   . ILE A 1 1665 ? 168.116 229.350 171.758 1.00 9.06  ? 1665 ILE A CG2   1 
ATOM   1730  C  CD1   . ILE A 1 1665 ? 167.581 226.322 173.933 1.00 6.63  ? 1665 ILE A CD1   1 
ATOM   1731  N  N     . LEU A 1 1666 ? 170.741 230.923 172.860 1.00 7.17  ? 1666 LEU A N     1 
ATOM   1732  C  CA    . LEU A 1 1666 ? 171.141 232.318 172.880 1.00 8.27  ? 1666 LEU A CA    1 
ATOM   1733  C  C     . LEU A 1 1666 ? 170.839 232.945 171.528 1.00 14.85 ? 1666 LEU A C     1 
ATOM   1734  O  O     . LEU A 1 1666 ? 170.786 232.261 170.503 1.00 22.13 ? 1666 LEU A O     1 
ATOM   1735  C  CB    . LEU A 1 1666 ? 172.632 232.441 173.207 1.00 11.27 ? 1666 LEU A CB    1 
ATOM   1736  C  CG    . LEU A 1 1666 ? 173.001 231.979 174.614 1.00 9.42  ? 1666 LEU A CG    1 
ATOM   1737  C  CD1   . LEU A 1 1666 ? 174.493 231.959 174.793 1.00 8.96  ? 1666 LEU A CD1   1 
ATOM   1738  C  CD2   . LEU A 1 1666 ? 172.372 232.913 175.626 1.00 10.33 ? 1666 LEU A CD2   1 
ATOM   1739  N  N     . ASN A 1 1667 ? 170.641 234.258 171.533 1.00 16.81 ? 1667 ASN A N     1 
ATOM   1740  C  CA    . ASN A 1 1667 ? 170.434 234.995 170.294 1.00 15.35 ? 1667 ASN A CA    1 
ATOM   1741  C  C     . ASN A 1 1667 ? 171.767 235.108 169.555 1.00 19.91 ? 1667 ASN A C     1 
ATOM   1742  O  O     . ASN A 1 1667 ? 172.791 234.556 169.969 1.00 26.20 ? 1667 ASN A O     1 
ATOM   1743  C  CB    . ASN A 1 1667 ? 169.813 236.361 170.575 1.00 9.73  ? 1667 ASN A CB    1 
ATOM   1744  C  CG    . ASN A 1 1667 ? 170.536 237.122 171.668 1.00 17.40 ? 1667 ASN A CG    1 
ATOM   1745  O  OD1   . ASN A 1 1667 ? 171.608 236.720 172.121 1.00 22.22 ? 1667 ASN A OD1   1 
ATOM   1746  N  ND2   . ASN A 1 1667 ? 169.960 238.242 172.084 1.00 14.38 ? 1667 ASN A ND2   1 
ATOM   1747  N  N     . GLU A 1 1668 ? 171.766 235.835 168.435 1.00 23.05 ? 1668 GLU A N     1 
ATOM   1748  C  CA    . GLU A 1 1668 ? 172.996 235.990 167.663 1.00 19.99 ? 1668 GLU A CA    1 
ATOM   1749  C  C     . GLU A 1 1668 ? 174.047 236.777 168.432 1.00 21.47 ? 1668 GLU A C     1 
ATOM   1750  O  O     . GLU A 1 1668 ? 175.248 236.557 168.242 1.00 25.89 ? 1668 GLU A O     1 
ATOM   1751  C  CB    . GLU A 1 1668 ? 172.691 236.662 166.319 1.00 24.72 ? 1668 GLU A CB    1 
ATOM   1752  C  CG    . GLU A 1 1668 ? 172.711 238.193 166.323 1.00 28.33 ? 1668 GLU A CG    1 
ATOM   1753  C  CD    . GLU A 1 1668 ? 171.612 238.822 167.168 1.00 31.91 ? 1668 GLU A CD    1 
ATOM   1754  O  OE1   . GLU A 1 1668 ? 170.738 238.091 167.679 1.00 26.16 ? 1668 GLU A OE1   1 
ATOM   1755  O  OE2   . GLU A 1 1668 ? 171.628 240.061 167.325 1.00 35.99 ? 1668 GLU A OE2   1 
ATOM   1756  N  N     . ASP A 1 1669 ? 173.619 237.690 169.305 1.00 21.81 ? 1669 ASP A N     1 
ATOM   1757  C  CA    . ASP A 1 1669 ? 174.562 238.499 170.069 1.00 19.95 ? 1669 ASP A CA    1 
ATOM   1758  C  C     . ASP A 1 1669 ? 175.156 237.687 171.217 1.00 19.83 ? 1669 ASP A C     1 
ATOM   1759  O  O     . ASP A 1 1669 ? 176.313 237.905 171.591 1.00 26.01 ? 1669 ASP A O     1 
ATOM   1760  C  CB    . ASP A 1 1669 ? 173.826 239.770 170.537 1.00 20.16 ? 1669 ASP A CB    1 
ATOM   1761  C  CG    . ASP A 1 1669 ? 174.613 240.642 171.528 1.00 27.55 ? 1669 ASP A CG    1 
ATOM   1762  O  OD1   . ASP A 1 1669 ? 174.218 241.819 171.652 1.00 34.17 ? 1669 ASP A OD1   1 
ATOM   1763  O  OD2   . ASP A 1 1669 ? 175.593 240.225 172.173 1.00 32.20 ? 1669 ASP A OD2   1 
ATOM   1764  N  N     . ASN A 1 1670 ? 174.409 236.695 171.720 1.00 21.18 ? 1670 ASN A N     1 
ATOM   1765  C  CA    . ASN A 1 1670 ? 174.717 235.967 172.955 1.00 18.64 ? 1670 ASN A CA    1 
ATOM   1766  C  C     . ASN A 1 1670 ? 174.499 236.841 174.185 1.00 18.00 ? 1670 ASN A C     1 
ATOM   1767  O  O     . ASN A 1 1670 ? 175.204 236.709 175.187 1.00 19.58 ? 1670 ASN A O     1 
ATOM   1768  C  CB    . ASN A 1 1670 ? 176.139 235.388 172.962 1.00 13.76 ? 1670 ASN A CB    1 
ATOM   1769  C  CG    . ASN A 1 1670 ? 176.353 234.349 171.884 1.00 21.67 ? 1670 ASN A CG    1 
ATOM   1770  O  OD1   . ASN A 1 1670 ? 175.745 233.278 171.905 1.00 23.09 ? 1670 ASN A OD1   1 
ATOM   1771  N  ND2   . ASN A 1 1670 ? 177.225 234.655 170.933 1.00 27.55 ? 1670 ASN A ND2   1 
ATOM   1772  N  N     . SER A 1 1671 ? 173.514 237.735 174.112 1.00 20.74 ? 1671 SER A N     1 
ATOM   1773  C  CA    . SER A 1 1671 ? 173.182 238.643 175.198 1.00 14.74 ? 1671 SER A CA    1 
ATOM   1774  C  C     . SER A 1 1671 ? 171.850 238.338 175.863 1.00 17.11 ? 1671 SER A C     1 
ATOM   1775  O  O     . SER A 1 1671 ? 171.585 238.866 176.946 1.00 17.35 ? 1671 SER A O     1 
ATOM   1776  C  CB    . SER A 1 1671 ? 173.156 240.089 174.686 1.00 15.89 ? 1671 SER A CB    1 
ATOM   1777  O  OG    . SER A 1 1671 ? 172.284 240.214 173.579 1.00 19.81 ? 1671 SER A OG    1 
ATOM   1778  N  N     . VAL A 1 1672 ? 171.004 237.523 175.241 1.00 15.80 ? 1672 VAL A N     1 
ATOM   1779  C  CA    . VAL A 1 1672 ? 169.711 237.150 175.798 1.00 11.13 ? 1672 VAL A CA    1 
ATOM   1780  C  C     . VAL A 1 1672 ? 169.604 235.632 175.778 1.00 9.86  ? 1672 VAL A C     1 
ATOM   1781  O  O     . VAL A 1 1672 ? 169.853 235.004 174.742 1.00 12.59 ? 1672 VAL A O     1 
ATOM   1782  C  CB    . VAL A 1 1672 ? 168.544 237.787 175.019 1.00 9.95  ? 1672 VAL A CB    1 
ATOM   1783  C  CG1   . VAL A 1 1672 ? 167.220 237.365 175.615 1.00 9.26  ? 1672 VAL A CG1   1 
ATOM   1784  C  CG2   . VAL A 1 1672 ? 168.669 239.300 175.013 1.00 8.61  ? 1672 VAL A CG2   1 
ATOM   1785  N  N     . VAL A 1 1673 ? 169.243 235.047 176.915 1.00 11.99 ? 1673 VAL A N     1 
ATOM   1786  C  CA    . VAL A 1 1673 ? 169.017 233.610 177.013 1.00 8.34  ? 1673 VAL A CA    1 
ATOM   1787  C  C     . VAL A 1 1673 ? 167.585 233.343 176.564 1.00 5.34  ? 1673 VAL A C     1 
ATOM   1788  O  O     . VAL A 1 1673 ? 166.631 233.672 177.273 1.00 8.78  ? 1673 VAL A O     1 
ATOM   1789  C  CB    . VAL A 1 1673 ? 169.261 233.094 178.436 1.00 7.74  ? 1673 VAL A CB    1 
ATOM   1790  C  CG1   . VAL A 1 1673 ? 168.811 231.644 178.562 1.00 7.30  ? 1673 VAL A CG1   1 
ATOM   1791  C  CG2   . VAL A 1 1673 ? 170.721 233.241 178.812 1.00 3.99  ? 1673 VAL A CG2   1 
ATOM   1792  N  N     . LEU A 1 1674 ? 167.435 232.765 175.372 1.00 6.54  ? 1674 LEU A N     1 
ATOM   1793  C  CA    . LEU A 1 1674 ? 166.107 232.489 174.837 1.00 6.78  ? 1674 LEU A CA    1 
ATOM   1794  C  C     . LEU A 1 1674 ? 165.464 231.264 175.476 1.00 4.74  ? 1674 LEU A C     1 
ATOM   1795  O  O     . LEU A 1 1674 ? 164.239 231.226 175.628 1.00 5.57  ? 1674 LEU A O     1 
ATOM   1796  C  CB    . LEU A 1 1674 ? 166.179 232.313 173.320 1.00 9.83  ? 1674 LEU A CB    1 
ATOM   1797  C  CG    . LEU A 1 1674 ? 166.412 233.592 172.517 1.00 6.70  ? 1674 LEU A CG    1 
ATOM   1798  C  CD1   . LEU A 1 1674 ? 166.325 233.316 171.029 1.00 12.02 ? 1674 LEU A CD1   1 
ATOM   1799  C  CD2   . LEU A 1 1674 ? 165.421 234.669 172.925 1.00 7.10  ? 1674 LEU A CD2   1 
ATOM   1800  N  N     . GLY A 1 1675 ? 166.253 230.262 175.846 1.00 5.55  ? 1675 GLY A N     1 
ATOM   1801  C  CA    . GLY A 1 1675 ? 165.686 229.065 176.431 1.00 3.25  ? 1675 GLY A CA    1 
ATOM   1802  C  C     . GLY A 1 1675 ? 166.765 228.090 176.847 1.00 4.30  ? 1675 GLY A C     1 
ATOM   1803  O  O     . GLY A 1 1675 ? 167.948 228.428 176.906 1.00 6.22  ? 1675 GLY A O     1 
ATOM   1804  N  N     . ILE A 1 1676 ? 166.332 226.862 177.137 1.00 3.43  ? 1676 ILE A N     1 
ATOM   1805  C  CA    . ILE A 1 1676 ? 167.216 225.792 177.572 1.00 3.56  ? 1676 ILE A CA    1 
ATOM   1806  C  C     . ILE A 1 1676 ? 166.989 224.575 176.687 1.00 2.91  ? 1676 ILE A C     1 
ATOM   1807  O  O     . ILE A 1 1676 ? 165.942 224.419 176.057 1.00 4.45  ? 1676 ILE A O     1 
ATOM   1808  C  CB    . ILE A 1 1676 ? 167.003 225.419 179.055 1.00 6.21  ? 1676 ILE A CB    1 
ATOM   1809  C  CG1   . ILE A 1 1676 ? 165.528 225.100 179.314 1.00 1.92  ? 1676 ILE A CG1   1 
ATOM   1810  C  CG2   . ILE A 1 1676 ? 167.502 226.533 179.963 1.00 1.09  ? 1676 ILE A CG2   1 
ATOM   1811  C  CD1   . ILE A 1 1676 ? 165.204 224.819 180.754 1.00 2.17  ? 1676 ILE A CD1   1 
ATOM   1812  N  N     . SER A 1 1677 ? 167.999 223.711 176.639 1.00 3.02  ? 1677 SER A N     1 
ATOM   1813  C  CA    . SER A 1 1677 ? 167.953 222.508 175.822 1.00 3.54  ? 1677 SER A CA    1 
ATOM   1814  C  C     . SER A 1 1677 ? 168.517 221.335 176.613 1.00 5.00  ? 1677 SER A C     1 
ATOM   1815  O  O     . SER A 1 1677 ? 169.315 221.506 177.537 1.00 4.97  ? 1677 SER A O     1 
ATOM   1816  C  CB    . SER A 1 1677 ? 168.727 222.690 174.511 1.00 4.60  ? 1677 SER A CB    1 
ATOM   1817  O  OG    . SER A 1 1677 ? 168.854 221.463 173.815 1.00 13.24 ? 1677 SER A OG    1 
ATOM   1818  N  N     . SER A 1 1678 ? 168.086 220.136 176.237 1.00 3.57  ? 1678 SER A N     1 
ATOM   1819  C  CA    . SER A 1 1678 ? 168.554 218.905 176.853 1.00 5.40  ? 1678 SER A CA    1 
ATOM   1820  C  C     . SER A 1 1678 ? 169.673 218.284 176.023 1.00 7.52  ? 1678 SER A C     1 
ATOM   1821  O  O     . SER A 1 1678 ? 169.993 218.734 174.921 1.00 7.15  ? 1678 SER A O     1 
ATOM   1822  C  CB    . SER A 1 1678 ? 167.400 217.912 177.015 1.00 5.51  ? 1678 SER A CB    1 
ATOM   1823  O  OG    . SER A 1 1678 ? 166.754 217.679 175.778 1.00 6.12  ? 1678 SER A OG    1 
ATOM   1824  N  N     . ARG A 1 1679 ? 170.268 217.225 176.572 1.00 8.18  ? 1679 ARG A N     1 
ATOM   1825  C  CA    . ARG A 1 1679 ? 171.340 216.527 175.871 1.00 6.56  ? 1679 ARG A CA    1 
ATOM   1826  C  C     . ARG A 1 1679 ? 170.842 215.791 174.633 1.00 9.23  ? 1679 ARG A C     1 
ATOM   1827  O  O     . ARG A 1 1679 ? 171.647 215.481 173.750 1.00 18.41 ? 1679 ARG A O     1 
ATOM   1828  C  CB    . ARG A 1 1679 ? 172.035 215.548 176.817 1.00 7.69  ? 1679 ARG A CB    1 
ATOM   1829  C  CG    . ARG A 1 1679 ? 171.163 214.392 177.269 1.00 12.11 ? 1679 ARG A CG    1 
ATOM   1830  C  CD    . ARG A 1 1679 ? 171.954 213.406 178.105 1.00 12.89 ? 1679 ARG A CD    1 
ATOM   1831  N  NE    . ARG A 1 1679 ? 172.586 214.054 179.249 1.00 20.97 ? 1679 ARG A NE    1 
ATOM   1832  C  CZ    . ARG A 1 1679 ? 173.437 213.457 180.073 1.00 25.86 ? 1679 ARG A CZ    1 
ATOM   1833  N  NH1   . ARG A 1 1679 ? 173.789 212.194 179.906 1.00 26.34 ? 1679 ARG A NH1   1 
ATOM   1834  N  NH2   . ARG A 1 1679 ? 173.948 214.147 181.089 1.00 20.13 ? 1679 ARG A NH2   1 
ATOM   1835  N  N     . GLU A 1 1680 ? 169.543 215.510 174.546 1.00 12.32 ? 1680 GLU A N     1 
ATOM   1836  C  CA    . GLU A 1 1680 ? 168.960 214.851 173.386 1.00 8.69  ? 1680 GLU A CA    1 
ATOM   1837  C  C     . GLU A 1 1680 ? 168.424 215.830 172.351 1.00 8.82  ? 1680 GLU A C     1 
ATOM   1838  O  O     . GLU A 1 1680 ? 167.872 215.397 171.336 1.00 18.63 ? 1680 GLU A O     1 
ATOM   1839  C  CB    . GLU A 1 1680 ? 167.836 213.903 173.819 1.00 9.22  ? 1680 GLU A CB    1 
ATOM   1840  C  CG    . GLU A 1 1680 ? 168.295 212.735 174.669 1.00 10.77 ? 1680 GLU A CG    1 
ATOM   1841  C  CD    . GLU A 1 1680 ? 167.968 212.915 176.135 1.00 17.15 ? 1680 GLU A CD    1 
ATOM   1842  O  OE1   . GLU A 1 1680 ? 168.172 211.958 176.912 1.00 20.03 ? 1680 GLU A OE1   1 
ATOM   1843  O  OE2   . GLU A 1 1680 ? 167.499 214.011 176.509 1.00 12.15 ? 1680 GLU A OE2   1 
ATOM   1844  N  N     . GLY A 1 1681 ? 168.564 217.132 172.583 1.00 7.06  ? 1681 GLY A N     1 
ATOM   1845  C  CA    . GLY A 1 1681 ? 168.138 218.138 171.635 1.00 6.50  ? 1681 GLY A CA    1 
ATOM   1846  C  C     . GLY A 1 1681 ? 166.792 218.769 171.919 1.00 10.26 ? 1681 GLY A C     1 
ATOM   1847  O  O     . GLY A 1 1681 ? 166.438 219.747 171.249 1.00 9.67  ? 1681 GLY A O     1 
ATOM   1848  N  N     . GLU A 1 1682 ? 166.032 218.245 172.878 1.00 8.82  ? 1682 GLU A N     1 
ATOM   1849  C  CA    . GLU A 1 1682 ? 164.739 218.829 173.206 1.00 8.50  ? 1682 GLU A CA    1 
ATOM   1850  C  C     . GLU A 1 1682 ? 164.927 220.222 173.795 1.00 6.39  ? 1682 GLU A C     1 
ATOM   1851  O  O     . GLU A 1 1682 ? 165.754 220.424 174.689 1.00 7.54  ? 1682 GLU A O     1 
ATOM   1852  C  CB    . GLU A 1 1682 ? 163.980 217.934 174.180 1.00 7.58  ? 1682 GLU A CB    1 
ATOM   1853  C  CG    . GLU A 1 1682 ? 162.561 218.394 174.460 1.00 5.61  ? 1682 GLU A CG    1 
ATOM   1854  C  CD    . GLU A 1 1682 ? 161.908 217.620 175.586 1.00 4.66  ? 1682 GLU A CD    1 
ATOM   1855  O  OE1   . GLU A 1 1682 ? 162.318 217.799 176.749 1.00 4.11  ? 1682 GLU A OE1   1 
ATOM   1856  O  OE2   . GLU A 1 1682 ? 160.985 216.829 175.306 1.00 8.20  ? 1682 GLU A OE2   1 
ATOM   1857  N  N     . GLU A 1 1683 ? 164.150 221.181 173.300 1.00 6.17  ? 1683 GLU A N     1 
ATOM   1858  C  CA    . GLU A 1 1683 ? 164.309 222.583 173.651 1.00 4.16  ? 1683 GLU A CA    1 
ATOM   1859  C  C     . GLU A 1 1683 ? 163.088 223.089 174.403 1.00 5.73  ? 1683 GLU A C     1 
ATOM   1860  O  O     . GLU A 1 1683 ? 161.954 222.711 174.094 1.00 9.60  ? 1683 GLU A O     1 
ATOM   1861  C  CB    . GLU A 1 1683 ? 164.528 223.443 172.404 1.00 5.09  ? 1683 GLU A CB    1 
ATOM   1862  C  CG    . GLU A 1 1683 ? 165.848 223.203 171.698 1.00 14.87 ? 1683 GLU A CG    1 
ATOM   1863  C  CD    . GLU A 1 1683 ? 166.064 224.156 170.539 1.00 21.56 ? 1683 GLU A CD    1 
ATOM   1864  O  OE1   . GLU A 1 1683 ? 165.177 224.999 170.289 1.00 21.86 ? 1683 GLU A OE1   1 
ATOM   1865  O  OE2   . GLU A 1 1683 ? 167.119 224.064 169.879 1.00 27.32 ? 1683 GLU A OE2   1 
ATOM   1866  N  N     . VAL A 1 1684 ? 163.329 223.944 175.390 1.00 2.80  ? 1684 VAL A N     1 
ATOM   1867  C  CA    . VAL A 1 1684 ? 162.281 224.689 176.076 1.00 2.91  ? 1684 VAL A CA    1 
ATOM   1868  C  C     . VAL A 1 1684 ? 162.529 226.165 175.807 1.00 4.25  ? 1684 VAL A C     1 
ATOM   1869  O  O     . VAL A 1 1684 ? 163.587 226.696 176.165 1.00 9.51  ? 1684 VAL A O     1 
ATOM   1870  C  CB    . VAL A 1 1684 ? 162.263 224.405 177.586 1.00 2.59  ? 1684 VAL A CB    1 
ATOM   1871  C  CG1   . VAL A 1 1684 ? 161.076 225.095 178.235 1.00 1.81  ? 1684 VAL A CG1   1 
ATOM   1872  C  CG2   . VAL A 1 1684 ? 162.234 222.909 177.853 1.00 2.41  ? 1684 VAL A CG2   1 
ATOM   1873  N  N     . MET A 1 1685 ? 161.563 226.825 175.179 1.00 2.97  ? 1685 MET A N     1 
ATOM   1874  C  CA    . MET A 1 1685 ? 161.667 228.242 174.855 1.00 3.82  ? 1685 MET A CA    1 
ATOM   1875  C  C     . MET A 1 1685 ? 160.989 229.049 175.954 1.00 5.34  ? 1685 MET A C     1 
ATOM   1876  O  O     . MET A 1 1685 ? 159.800 228.856 176.226 1.00 9.08  ? 1685 MET A O     1 
ATOM   1877  C  CB    . MET A 1 1685 ? 161.036 228.543 173.497 1.00 3.63  ? 1685 MET A CB    1 
ATOM   1878  C  CG    . MET A 1 1685 ? 161.882 228.117 172.310 1.00 8.21  ? 1685 MET A CG    1 
ATOM   1879  S  SD    . MET A 1 1685 ? 163.623 228.557 172.481 1.00 22.81 ? 1685 MET A SD    1 
ATOM   1880  C  CE    . MET A 1 1685 ? 163.650 230.141 171.648 1.00 7.18  ? 1685 MET A CE    1 
ATOM   1881  N  N     . PHE A 1 1686 ? 161.744 229.950 176.576 1.00 4.96  ? 1686 PHE A N     1 
ATOM   1882  C  CA    . PHE A 1 1686 ? 161.209 230.754 177.664 1.00 3.93  ? 1686 PHE A CA    1 
ATOM   1883  C  C     . PHE A 1 1686 ? 160.103 231.671 177.161 1.00 8.39  ? 1686 PHE A C     1 
ATOM   1884  O  O     . PHE A 1 1686 ? 160.173 232.209 176.053 1.00 14.47 ? 1686 PHE A O     1 
ATOM   1885  C  CB    . PHE A 1 1686 ? 162.315 231.587 178.310 1.00 3.42  ? 1686 PHE A CB    1 
ATOM   1886  C  CG    . PHE A 1 1686 ? 163.351 230.774 179.027 1.00 4.52  ? 1686 PHE A CG    1 
ATOM   1887  C  CD1   . PHE A 1 1686 ? 163.065 229.494 179.472 1.00 4.43  ? 1686 PHE A CD1   1 
ATOM   1888  C  CD2   . PHE A 1 1686 ? 164.612 231.296 179.264 1.00 2.76  ? 1686 PHE A CD2   1 
ATOM   1889  C  CE1   . PHE A 1 1686 ? 164.021 228.748 180.133 1.00 4.14  ? 1686 PHE A CE1   1 
ATOM   1890  C  CE2   . PHE A 1 1686 ? 165.569 230.556 179.925 1.00 2.47  ? 1686 PHE A CE2   1 
ATOM   1891  C  CZ    . PHE A 1 1686 ? 165.272 229.279 180.360 1.00 4.09  ? 1686 PHE A CZ    1 
ATOM   1892  N  N     . LYS A 1 1687 ? 159.064 231.838 177.980 1.00 7.07  ? 1687 LYS A N     1 
ATOM   1893  C  CA    . LYS A 1 1687 ? 158.010 232.786 177.636 1.00 11.41 ? 1687 LYS A CA    1 
ATOM   1894  C  C     . LYS A 1 1687 ? 158.515 234.219 177.743 1.00 12.19 ? 1687 LYS A C     1 
ATOM   1895  O  O     . LYS A 1 1687 ? 158.198 235.061 176.896 1.00 17.53 ? 1687 LYS A O     1 
ATOM   1896  C  CB    . LYS A 1 1687 ? 156.791 232.567 178.532 1.00 8.00  ? 1687 LYS A CB    1 
ATOM   1897  C  CG    . LYS A 1 1687 ? 156.611 231.130 178.989 1.00 9.26  ? 1687 LYS A CG    1 
ATOM   1898  C  CD    . LYS A 1 1687 ? 156.224 230.214 177.834 1.00 11.37 ? 1687 LYS A CD    1 
ATOM   1899  C  CE    . LYS A 1 1687 ? 154.732 230.243 177.562 1.00 12.80 ? 1687 LYS A CE    1 
ATOM   1900  N  NZ    . LYS A 1 1687 ? 154.395 229.558 176.285 1.00 8.20  ? 1687 LYS A NZ    1 
ATOM   1901  N  N     . THR A 1 1688 ? 159.301 234.511 178.772 1.00 11.10 ? 1688 THR A N     1 
ATOM   1902  C  CA    . THR A 1 1688 ? 159.956 235.808 178.928 1.00 11.02 ? 1688 THR A CA    1 
ATOM   1903  C  C     . THR A 1 1688 ? 161.465 235.604 178.899 1.00 9.88  ? 1688 THR A C     1 
ATOM   1904  O  O     . THR A 1 1688 ? 162.034 235.080 179.875 1.00 9.15  ? 1688 THR A O     1 
ATOM   1905  C  CB    . THR A 1 1688 ? 159.531 236.483 180.232 1.00 16.59 ? 1688 THR A CB    1 
ATOM   1906  O  OG1   . THR A 1 1688 ? 158.125 236.756 180.193 1.00 19.54 ? 1688 THR A OG1   1 
ATOM   1907  C  CG2   . THR A 1 1688 ? 160.279 237.788 180.424 1.00 16.74 ? 1688 THR A CG2   1 
ATOM   1908  N  N     . PRO A 1 1689 ? 162.149 235.980 177.819 1.00 14.05 ? 1689 PRO A N     1 
ATOM   1909  C  CA    . PRO A 1 1689 ? 163.591 235.725 177.729 1.00 11.88 ? 1689 PRO A CA    1 
ATOM   1910  C  C     . PRO A 1 1689 ? 164.386 236.510 178.763 1.00 7.01  ? 1689 PRO A C     1 
ATOM   1911  O  O     . PRO A 1 1689 ? 163.980 237.582 179.216 1.00 11.53 ? 1689 PRO A O     1 
ATOM   1912  C  CB    . PRO A 1 1689 ? 163.942 236.170 176.303 1.00 9.42  ? 1689 PRO A CB    1 
ATOM   1913  C  CG    . PRO A 1 1689 ? 162.638 236.182 175.571 1.00 12.52 ? 1689 PRO A CG    1 
ATOM   1914  C  CD    . PRO A 1 1689 ? 161.619 236.577 176.584 1.00 9.22  ? 1689 PRO A CD    1 
ATOM   1915  N  N     . VAL A 1 1690 ? 165.538 235.955 179.129 1.00 7.67  ? 1690 VAL A N     1 
ATOM   1916  C  CA    . VAL A 1 1690 ? 166.412 236.522 180.151 1.00 6.68  ? 1690 VAL A CA    1 
ATOM   1917  C  C     . VAL A 1 1690 ? 167.533 237.286 179.458 1.00 9.94  ? 1690 VAL A C     1 
ATOM   1918  O  O     . VAL A 1 1690 ? 168.284 236.714 178.661 1.00 10.26 ? 1690 VAL A O     1 
ATOM   1919  C  CB    . VAL A 1 1690 ? 166.981 235.428 181.067 1.00 6.18  ? 1690 VAL A CB    1 
ATOM   1920  C  CG1   . VAL A 1 1690 ? 168.000 236.013 182.029 1.00 5.15  ? 1690 VAL A CG1   1 
ATOM   1921  C  CG2   . VAL A 1 1690 ? 165.868 234.734 181.817 1.00 5.13  ? 1690 VAL A CG2   1 
ATOM   1922  N  N     . SER A 1 1691 ? 167.659 238.572 179.776 1.00 11.19 ? 1691 SER A N     1 
ATOM   1923  C  CA    . SER A 1 1691 ? 168.681 239.419 179.177 1.00 11.66 ? 1691 SER A CA    1 
ATOM   1924  C  C     . SER A 1 1691 ? 169.929 239.428 180.050 1.00 16.01 ? 1691 SER A C     1 
ATOM   1925  O  O     . SER A 1 1691 ? 169.859 239.750 181.239 1.00 9.06  ? 1691 SER A O     1 
ATOM   1926  C  CB    . SER A 1 1691 ? 168.159 240.844 178.988 1.00 15.36 ? 1691 SER A CB    1 
ATOM   1927  O  OG    . SER A 1 1691 ? 169.225 241.760 178.829 1.00 15.76 ? 1691 SER A OG    1 
ATOM   1928  N  N     . ILE A 1 1692 ? 171.067 239.073 179.453 1.00 14.01 ? 1692 ILE A N     1 
ATOM   1929  C  CA    . ILE A 1 1692 ? 172.319 239.082 180.196 1.00 13.05 ? 1692 ILE A CA    1 
ATOM   1930  C  C     . ILE A 1 1692 ? 172.871 240.500 180.317 1.00 17.20 ? 1692 ILE A C     1 
ATOM   1931  O  O     . ILE A 1 1692 ? 173.545 240.822 181.300 1.00 17.10 ? 1692 ILE A O     1 
ATOM   1932  C  CB    . ILE A 1 1692 ? 173.332 238.124 179.544 1.00 13.74 ? 1692 ILE A CB    1 
ATOM   1933  C  CG1   . ILE A 1 1692 ? 172.783 236.697 179.545 1.00 7.60  ? 1692 ILE A CG1   1 
ATOM   1934  C  CG2   . ILE A 1 1692 ? 174.672 238.165 180.263 1.00 10.10 ? 1692 ILE A CG2   1 
ATOM   1935  C  CD1   . ILE A 1 1692 ? 173.772 235.657 179.074 1.00 5.35  ? 1692 ILE A CD1   1 
ATOM   1936  N  N     . THR A 1 1693 ? 172.586 241.372 179.346 1.00 15.39 ? 1693 THR A N     1 
ATOM   1937  C  CA    . THR A 1 1693 ? 173.076 242.745 179.425 1.00 13.73 ? 1693 THR A CA    1 
ATOM   1938  C  C     . THR A 1 1693 ? 172.480 243.482 180.617 1.00 11.95 ? 1693 THR A C     1 
ATOM   1939  O  O     . THR A 1 1693 ? 173.184 244.228 181.308 1.00 16.07 ? 1693 THR A O     1 
ATOM   1940  C  CB    . THR A 1 1693 ? 172.769 243.501 178.132 1.00 17.18 ? 1693 THR A CB    1 
ATOM   1941  O  OG1   . THR A 1 1693 ? 171.350 243.595 177.955 1.00 16.12 ? 1693 THR A OG1   1 
ATOM   1942  C  CG2   . THR A 1 1693 ? 173.387 242.796 176.943 1.00 13.25 ? 1693 THR A CG2   1 
ATOM   1943  N  N     . GLU A 1 1694 ? 171.185 243.290 180.873 1.00 11.52 ? 1694 GLU A N     1 
ATOM   1944  C  CA    . GLU A 1 1694 ? 170.536 244.026 181.954 1.00 12.18 ? 1694 GLU A CA    1 
ATOM   1945  C  C     . GLU A 1 1694 ? 170.856 243.418 183.313 1.00 12.27 ? 1694 GLU A C     1 
ATOM   1946  O  O     . GLU A 1 1694 ? 170.678 244.070 184.348 1.00 10.23 ? 1694 GLU A O     1 
ATOM   1947  C  CB    . GLU A 1 1694 ? 169.028 244.077 181.717 1.00 12.49 ? 1694 GLU A CB    1 
ATOM   1948  C  CG    . GLU A 1 1694 ? 168.637 244.905 180.503 1.00 19.66 ? 1694 GLU A CG    1 
ATOM   1949  C  CD    . GLU A 1 1694 ? 167.141 244.934 180.265 1.00 29.82 ? 1694 GLU A CD    1 
ATOM   1950  O  OE1   . GLU A 1 1694 ? 166.410 244.209 180.969 1.00 32.02 ? 1694 GLU A OE1   1 
ATOM   1951  O  OE2   . GLU A 1 1694 ? 166.697 245.686 179.371 1.00 24.67 ? 1694 GLU A OE2   1 
ATOM   1952  N  N     . HIS A 1 1695 ? 171.324 242.169 183.333 1.00 16.72 ? 1695 HIS A N     1 
ATOM   1953  C  CA    . HIS A 1 1695 ? 171.783 241.498 184.546 1.00 12.77 ? 1695 HIS A CA    1 
ATOM   1954  C  C     . HIS A 1 1695 ? 173.143 240.882 184.258 1.00 13.44 ? 1695 HIS A C     1 
ATOM   1955  O  O     . HIS A 1 1695 ? 173.249 239.664 184.046 1.00 12.95 ? 1695 HIS A O     1 
ATOM   1956  C  CB    . HIS A 1 1695 ? 170.782 240.435 185.001 1.00 10.70 ? 1695 HIS A CB    1 
ATOM   1957  C  CG    . HIS A 1 1695 ? 169.381 240.945 185.129 1.00 13.46 ? 1695 HIS A CG    1 
ATOM   1958  N  ND1   . HIS A 1 1695 ? 168.879 241.452 186.307 1.00 10.90 ? 1695 HIS A ND1   1 
ATOM   1959  C  CD2   . HIS A 1 1695 ? 168.377 241.031 184.224 1.00 9.56  ? 1695 HIS A CD2   1 
ATOM   1960  C  CE1   . HIS A 1 1695 ? 167.625 241.826 186.125 1.00 15.86 ? 1695 HIS A CE1   1 
ATOM   1961  N  NE2   . HIS A 1 1695 ? 167.297 241.582 184.869 1.00 12.73 ? 1695 HIS A NE2   1 
ATOM   1962  N  N     . PRO A 1 1696 ? 174.217 241.677 184.237 1.00 12.94 ? 1696 PRO A N     1 
ATOM   1963  C  CA    . PRO A 1 1696 ? 175.491 241.168 183.702 1.00 9.45  ? 1696 PRO A CA    1 
ATOM   1964  C  C     . PRO A 1 1696 ? 176.133 240.088 184.549 1.00 9.46  ? 1696 PRO A C     1 
ATOM   1965  O  O     . PRO A 1 1696 ? 176.707 239.142 183.999 1.00 13.72 ? 1696 PRO A O     1 
ATOM   1966  C  CB    . PRO A 1 1696 ? 176.363 242.430 183.636 1.00 10.79 ? 1696 PRO A CB    1 
ATOM   1967  C  CG    . PRO A 1 1696 ? 175.387 243.572 183.671 1.00 12.59 ? 1696 PRO A CG    1 
ATOM   1968  C  CD    . PRO A 1 1696 ? 174.307 243.103 184.580 1.00 8.76  ? 1696 PRO A CD    1 
ATOM   1969  N  N     . LYS A 1 1697 ? 176.062 240.199 185.871 1.00 10.52 ? 1697 LYS A N     1 
ATOM   1970  C  CA    . LYS A 1 1697 ? 176.845 239.321 186.727 1.00 13.29 ? 1697 LYS A CA    1 
ATOM   1971  C  C     . LYS A 1 1697 ? 176.294 237.897 186.681 1.00 13.84 ? 1697 LYS A C     1 
ATOM   1972  O  O     . LYS A 1 1697 ? 175.086 237.681 186.560 1.00 11.92 ? 1697 LYS A O     1 
ATOM   1973  C  CB    . LYS A 1 1697 ? 176.870 239.879 188.151 1.00 13.28 ? 1697 LYS A CB    1 
ATOM   1974  C  CG    . LYS A 1 1697 ? 177.707 239.094 189.138 1.00 16.58 ? 1697 LYS A CG    1 
ATOM   1975  C  CD    . LYS A 1 1697 ? 177.756 239.798 190.482 1.00 17.30 ? 1697 LYS A CD    1 
ATOM   1976  C  CE    . LYS A 1 1697 ? 178.468 238.952 191.524 1.00 24.02 ? 1697 LYS A CE    1 
ATOM   1977  N  NZ    . LYS A 1 1697 ? 179.910 238.777 191.196 1.00 17.60 ? 1697 LYS A NZ    1 
ATOM   1978  N  N     . ILE A 1 1698 ? 177.204 236.923 186.770 1.00 17.56 ? 1698 ILE A N     1 
ATOM   1979  C  CA    . ILE A 1 1698 ? 176.905 235.550 186.367 1.00 8.39  ? 1698 ILE A CA    1 
ATOM   1980  C  C     . ILE A 1 1698 ? 175.828 234.927 187.252 1.00 9.55  ? 1698 ILE A C     1 
ATOM   1981  O  O     . ILE A 1 1698 ? 174.984 234.160 186.774 1.00 13.27 ? 1698 ILE A O     1 
ATOM   1982  C  CB    . ILE A 1 1698 ? 178.199 234.711 186.357 1.00 10.26 ? 1698 ILE A CB    1 
ATOM   1983  C  CG1   . ILE A 1 1698 ? 177.985 233.365 185.663 1.00 8.99  ? 1698 ILE A CG1   1 
ATOM   1984  C  CG2   . ILE A 1 1698 ? 178.751 234.523 187.755 1.00 11.30 ? 1698 ILE A CG2   1 
ATOM   1985  C  CD1   . ILE A 1 1698 ? 177.699 233.474 184.201 1.00 8.11  ? 1698 ILE A CD1   1 
ATOM   1986  N  N     . ASN A 1 1699 ? 175.836 235.236 188.549 1.00 11.41 ? 1699 ASN A N     1 
ATOM   1987  C  CA    . ASN A 1 1699 ? 174.959 234.531 189.477 1.00 8.39  ? 1699 ASN A CA    1 
ATOM   1988  C  C     . ASN A 1 1699 ? 173.529 235.057 189.472 1.00 10.89 ? 1699 ASN A C     1 
ATOM   1989  O  O     . ASN A 1 1699 ? 172.637 234.381 189.995 1.00 11.81 ? 1699 ASN A O     1 
ATOM   1990  C  CB    . ASN A 1 1699 ? 175.533 234.594 190.890 1.00 7.91  ? 1699 ASN A CB    1 
ATOM   1991  C  CG    . ASN A 1 1699 ? 175.515 235.992 191.459 1.00 12.30 ? 1699 ASN A CG    1 
ATOM   1992  O  OD1   . ASN A 1 1699 ? 176.164 236.889 190.933 1.00 14.28 ? 1699 ASN A OD1   1 
ATOM   1993  N  ND2   . ASN A 1 1699 ? 174.754 236.191 192.526 1.00 14.25 ? 1699 ASN A ND2   1 
ATOM   1994  N  N     . GLU A 1 1700 ? 173.280 236.238 188.906 1.00 8.63  ? 1700 GLU A N     1 
ATOM   1995  C  CA    . GLU A 1 1700 ? 171.917 236.758 188.870 1.00 9.77  ? 1700 GLU A CA    1 
ATOM   1996  C  C     . GLU A 1 1700 ? 171.149 236.281 187.644 1.00 9.92  ? 1700 GLU A C     1 
ATOM   1997  O  O     . GLU A 1 1700 ? 170.000 235.843 187.766 1.00 10.12 ? 1700 GLU A O     1 
ATOM   1998  C  CB    . GLU A 1 1700 ? 171.923 238.285 188.950 1.00 11.17 ? 1700 GLU A CB    1 
ATOM   1999  C  CG    . GLU A 1 1700 ? 172.395 238.824 190.290 1.00 15.69 ? 1700 GLU A CG    1 
ATOM   2000  C  CD    . GLU A 1 1700 ? 173.892 238.871 190.402 1.00 23.15 ? 1700 GLU A CD    1 
ATOM   2001  O  OE1   . GLU A 1 1700 ? 174.554 238.536 189.403 1.00 28.64 ? 1700 GLU A OE1   1 
ATOM   2002  O  OE2   . GLU A 1 1700 ? 174.406 239.240 191.477 1.00 26.40 ? 1700 GLU A OE2   1 
ATOM   2003  N  N     . TRP A 1 1701 ? 171.748 236.358 186.452 1.00 7.25  ? 1701 TRP A N     1 
ATOM   2004  C  CA    . TRP A 1 1701 ? 171.024 235.870 185.285 1.00 5.26  ? 1701 TRP A CA    1 
ATOM   2005  C  C     . TRP A 1 1701 ? 170.933 234.350 185.273 1.00 3.97  ? 1701 TRP A C     1 
ATOM   2006  O  O     . TRP A 1 1701 ? 169.980 233.805 184.710 1.00 6.63  ? 1701 TRP A O     1 
ATOM   2007  C  CB    . TRP A 1 1701 ? 171.649 236.385 183.979 1.00 7.28  ? 1701 TRP A CB    1 
ATOM   2008  C  CG    . TRP A 1 1701 ? 172.966 235.780 183.582 1.00 6.91  ? 1701 TRP A CG    1 
ATOM   2009  C  CD1   . TRP A 1 1701 ? 174.208 236.291 183.816 1.00 7.51  ? 1701 TRP A CD1   1 
ATOM   2010  C  CD2   . TRP A 1 1701 ? 173.167 234.565 182.848 1.00 6.72  ? 1701 TRP A CD2   1 
ATOM   2011  N  NE1   . TRP A 1 1701 ? 175.168 235.463 183.286 1.00 7.04  ? 1701 TRP A NE1   1 
ATOM   2012  C  CE2   . TRP A 1 1701 ? 174.554 234.396 182.688 1.00 6.09  ? 1701 TRP A CE2   1 
ATOM   2013  C  CE3   . TRP A 1 1701 ? 172.306 233.598 182.319 1.00 4.11  ? 1701 TRP A CE3   1 
ATOM   2014  C  CZ2   . TRP A 1 1701 ? 175.100 233.302 182.019 1.00 4.26  ? 1701 TRP A CZ2   1 
ATOM   2015  C  CZ3   . TRP A 1 1701 ? 172.851 232.515 181.661 1.00 4.32  ? 1701 TRP A CZ3   1 
ATOM   2016  C  CH2   . TRP A 1 1701 ? 174.234 232.375 181.517 1.00 3.71  ? 1701 TRP A CH2   1 
ATOM   2017  N  N     . LEU A 1 1702 ? 171.892 233.657 185.890 1.00 5.02  ? 1702 LEU A N     1 
ATOM   2018  C  CA    . LEU A 1 1702 ? 171.749 232.218 186.089 1.00 4.58  ? 1702 LEU A CA    1 
ATOM   2019  C  C     . LEU A 1 1702 ? 170.567 231.910 186.997 1.00 5.00  ? 1702 LEU A C     1 
ATOM   2020  O  O     . LEU A 1 1702 ? 169.847 230.929 186.782 1.00 7.45  ? 1702 LEU A O     1 
ATOM   2021  C  CB    . LEU A 1 1702 ? 173.036 231.632 186.668 1.00 4.79  ? 1702 LEU A CB    1 
ATOM   2022  C  CG    . LEU A 1 1702 ? 174.043 231.061 185.670 1.00 3.57  ? 1702 LEU A CG    1 
ATOM   2023  C  CD1   . LEU A 1 1702 ? 175.229 230.461 186.404 1.00 5.48  ? 1702 LEU A CD1   1 
ATOM   2024  C  CD2   . LEU A 1 1702 ? 173.386 230.026 184.772 1.00 3.15  ? 1702 LEU A CD2   1 
ATOM   2025  N  N     . THR A 1 1703 ? 170.362 232.734 188.030 1.00 3.80  ? 1703 THR A N     1 
ATOM   2026  C  CA    . THR A 1 1703 ? 169.181 232.590 188.872 1.00 3.97  ? 1703 THR A CA    1 
ATOM   2027  C  C     . THR A 1 1703 ? 167.906 232.875 188.087 1.00 4.14  ? 1703 THR A C     1 
ATOM   2028  O  O     . THR A 1 1703 ? 166.903 232.167 188.237 1.00 7.10  ? 1703 THR A O     1 
ATOM   2029  C  CB    . THR A 1 1703 ? 169.285 233.515 190.086 1.00 4.17  ? 1703 THR A CB    1 
ATOM   2030  O  OG1   . THR A 1 1703 ? 170.443 233.169 190.854 1.00 9.79  ? 1703 THR A OG1   1 
ATOM   2031  C  CG2   . THR A 1 1703 ? 168.052 233.393 190.966 1.00 6.69  ? 1703 THR A CG2   1 
ATOM   2032  N  N     . LEU A 1 1704 ? 167.925 233.907 187.238 1.00 2.91  ? 1704 LEU A N     1 
ATOM   2033  C  CA    . LEU A 1 1704 ? 166.749 234.221 186.433 1.00 3.42  ? 1704 LEU A CA    1 
ATOM   2034  C  C     . LEU A 1 1704 ? 166.462 233.124 185.415 1.00 5.82  ? 1704 LEU A C     1 
ATOM   2035  O  O     . LEU A 1 1704 ? 165.299 232.848 185.104 1.00 6.12  ? 1704 LEU A O     1 
ATOM   2036  C  CB    . LEU A 1 1704 ? 166.928 235.569 185.734 1.00 4.76  ? 1704 LEU A CB    1 
ATOM   2037  C  CG    . LEU A 1 1704 ? 167.141 236.789 186.633 1.00 4.11  ? 1704 LEU A CG    1 
ATOM   2038  C  CD1   . LEU A 1 1704 ? 167.428 238.024 185.800 1.00 7.46  ? 1704 LEU A CD1   1 
ATOM   2039  C  CD2   . LEU A 1 1704 ? 165.937 237.015 187.525 1.00 2.99  ? 1704 LEU A CD2   1 
ATOM   2040  N  N     . VAL A 1 1705 ? 167.510 232.495 184.877 1.00 5.56  ? 1705 VAL A N     1 
ATOM   2041  C  CA    . VAL A 1 1705 ? 167.315 231.361 183.978 1.00 4.64  ? 1705 VAL A CA    1 
ATOM   2042  C  C     . VAL A 1 1705 ? 166.666 230.200 184.721 1.00 3.42  ? 1705 VAL A C     1 
ATOM   2043  O  O     . VAL A 1 1705 ? 165.763 229.535 184.199 1.00 7.52  ? 1705 VAL A O     1 
ATOM   2044  C  CB    . VAL A 1 1705 ? 168.653 230.953 183.330 1.00 3.74  ? 1705 VAL A CB    1 
ATOM   2045  C  CG1   . VAL A 1 1705 ? 168.554 229.569 182.707 1.00 1.16  ? 1705 VAL A CG1   1 
ATOM   2046  C  CG2   . VAL A 1 1705 ? 169.052 231.970 182.277 1.00 1.88  ? 1705 VAL A CG2   1 
ATOM   2047  N  N     . GLU A 1 1706 ? 167.111 229.942 185.952 1.00 2.47  ? 1706 GLU A N     1 
ATOM   2048  C  CA    . GLU A 1 1706 ? 166.533 228.863 186.745 1.00 3.41  ? 1706 GLU A CA    1 
ATOM   2049  C  C     . GLU A 1 1706 ? 165.064 229.135 187.058 1.00 4.75  ? 1706 GLU A C     1 
ATOM   2050  O  O     . GLU A 1 1706 ? 164.245 228.210 187.101 1.00 4.04  ? 1706 GLU A O     1 
ATOM   2051  C  CB    . GLU A 1 1706 ? 167.351 228.675 188.027 1.00 3.73  ? 1706 GLU A CB    1 
ATOM   2052  C  CG    . GLU A 1 1706 ? 166.696 227.829 189.105 1.00 5.18  ? 1706 GLU A CG    1 
ATOM   2053  C  CD    . GLU A 1 1706 ? 167.388 227.968 190.450 1.00 14.52 ? 1706 GLU A CD    1 
ATOM   2054  O  OE1   . GLU A 1 1706 ? 167.490 229.106 190.952 1.00 17.36 ? 1706 GLU A OE1   1 
ATOM   2055  O  OE2   . GLU A 1 1706 ? 167.832 226.942 191.004 1.00 16.00 ? 1706 GLU A OE2   1 
ATOM   2056  N  N     . LYS A 1 1707 ? 164.710 230.403 187.278 1.00 5.29  ? 1707 LYS A N     1 
ATOM   2057  C  CA    . LYS A 1 1707 ? 163.317 230.747 187.554 1.00 3.69  ? 1707 LYS A CA    1 
ATOM   2058  C  C     . LYS A 1 1707 ? 162.461 230.668 186.294 1.00 4.13  ? 1707 LYS A C     1 
ATOM   2059  O  O     . LYS A 1 1707 ? 161.345 230.139 186.324 1.00 6.31  ? 1707 LYS A O     1 
ATOM   2060  C  CB    . LYS A 1 1707 ? 163.230 232.138 188.182 1.00 4.20  ? 1707 LYS A CB    1 
ATOM   2061  C  CG    . LYS A 1 1707 ? 163.830 232.221 189.572 1.00 6.63  ? 1707 LYS A CG    1 
ATOM   2062  C  CD    . LYS A 1 1707 ? 163.663 233.608 190.164 1.00 9.60  ? 1707 LYS A CD    1 
ATOM   2063  C  CE    . LYS A 1 1707 ? 164.336 233.707 191.520 1.00 10.73 ? 1707 LYS A CE    1 
ATOM   2064  N  NZ    . LYS A 1 1707 ? 163.650 232.865 192.535 1.00 12.77 ? 1707 LYS A NZ    1 
ATOM   2065  N  N     . GLU A 1 1708 ? 162.961 231.198 185.173 1.00 3.68  ? 1708 GLU A N     1 
ATOM   2066  C  CA    . GLU A 1 1708 ? 162.201 231.127 183.927 1.00 4.79  ? 1708 GLU A CA    1 
ATOM   2067  C  C     . GLU A 1 1708 ? 162.013 229.692 183.461 1.00 3.58  ? 1708 GLU A C     1 
ATOM   2068  O  O     . GLU A 1 1708 ? 161.007 229.372 182.821 1.00 3.51  ? 1708 GLU A O     1 
ATOM   2069  C  CB    . GLU A 1 1708 ? 162.871 231.954 182.831 1.00 3.60  ? 1708 GLU A CB    1 
ATOM   2070  C  CG    . GLU A 1 1708 ? 162.867 233.439 183.085 1.00 13.04 ? 1708 GLU A CG    1 
ATOM   2071  C  CD    . GLU A 1 1708 ? 161.470 234.019 183.046 1.00 26.25 ? 1708 GLU A CD    1 
ATOM   2072  O  OE1   . GLU A 1 1708 ? 160.629 233.493 182.284 1.00 18.34 ? 1708 GLU A OE1   1 
ATOM   2073  O  OE2   . GLU A 1 1708 ? 161.208 235.002 183.774 1.00 28.61 ? 1708 GLU A OE2   1 
ATOM   2074  N  N     . MET A 1 1709 ? 162.968 228.813 183.764 1.00 2.54  ? 1709 MET A N     1 
ATOM   2075  C  CA    . MET A 1 1709 ? 162.781 227.402 183.442 1.00 1.95  ? 1709 MET A CA    1 
ATOM   2076  C  C     . MET A 1 1709 ? 161.563 226.846 184.168 1.00 2.61  ? 1709 MET A C     1 
ATOM   2077  O  O     . MET A 1 1709 ? 160.738 226.144 183.574 1.00 2.79  ? 1709 MET A O     1 
ATOM   2078  C  CB    . MET A 1 1709 ? 164.039 226.608 183.791 1.00 1.85  ? 1709 MET A CB    1 
ATOM   2079  C  CG    . MET A 1 1709 ? 163.785 225.149 184.131 1.00 1.75  ? 1709 MET A CG    1 
ATOM   2080  S  SD    . MET A 1 1709 ? 165.181 224.348 184.941 1.00 3.45  ? 1709 MET A SD    1 
ATOM   2081  C  CE    . MET A 1 1709 ? 164.869 224.761 186.655 1.00 1.55  ? 1709 MET A CE    1 
ATOM   2082  N  N     . ARG A 1 1710 ? 161.419 227.179 185.451 1.00 3.35  ? 1710 ARG A N     1 
ATOM   2083  C  CA    . ARG A 1 1710 ? 160.277 226.699 186.222 1.00 1.72  ? 1710 ARG A CA    1 
ATOM   2084  C  C     . ARG A 1 1710 ? 158.983 227.370 185.776 1.00 1.87  ? 1710 ARG A C     1 
ATOM   2085  O  O     . ARG A 1 1710 ? 157.937 226.721 185.677 1.00 4.08  ? 1710 ARG A O     1 
ATOM   2086  C  CB    . ARG A 1 1710 ? 160.525 226.925 187.712 1.00 1.88  ? 1710 ARG A CB    1 
ATOM   2087  C  CG    . ARG A 1 1710 ? 161.656 226.087 188.273 1.00 1.11  ? 1710 ARG A CG    1 
ATOM   2088  C  CD    . ARG A 1 1710 ? 161.776 226.246 189.774 1.00 1.20  ? 1710 ARG A CD    1 
ATOM   2089  N  NE    . ARG A 1 1710 ? 162.807 225.378 190.330 1.00 4.42  ? 1710 ARG A NE    1 
ATOM   2090  C  CZ    . ARG A 1 1710 ? 163.875 225.809 190.988 1.00 7.30  ? 1710 ARG A CZ    1 
ATOM   2091  N  NH1   . ARG A 1 1710 ? 164.097 227.100 191.177 1.00 6.39  ? 1710 ARG A NH1   1 
ATOM   2092  N  NH2   . ARG A 1 1710 ? 164.743 224.923 191.465 1.00 3.52  ? 1710 ARG A NH2   1 
ATOM   2093  N  N     . VAL A 1 1711 ? 159.036 228.674 185.499 1.00 3.63  ? 1711 VAL A N     1 
ATOM   2094  C  CA    . VAL A 1 1711 ? 157.828 229.404 185.122 1.00 2.29  ? 1711 VAL A CA    1 
ATOM   2095  C  C     . VAL A 1 1711 ? 157.355 228.989 183.734 1.00 2.31  ? 1711 VAL A C     1 
ATOM   2096  O  O     . VAL A 1 1711 ? 156.153 228.821 183.498 1.00 4.75  ? 1711 VAL A O     1 
ATOM   2097  C  CB    . VAL A 1 1711 ? 158.075 230.922 185.217 1.00 2.99  ? 1711 VAL A CB    1 
ATOM   2098  C  CG1   . VAL A 1 1711 ? 156.931 231.694 184.587 1.00 3.20  ? 1711 VAL A CG1   1 
ATOM   2099  C  CG2   . VAL A 1 1711 ? 158.252 231.330 186.668 1.00 1.83  ? 1711 VAL A CG2   1 
ATOM   2100  N  N     . THR A 1 1712 ? 158.287 228.820 182.794 1.00 2.83  ? 1712 THR A N     1 
ATOM   2101  C  CA    . THR A 1 1712 ? 157.913 228.429 181.438 1.00 3.27  ? 1712 THR A CA    1 
ATOM   2102  C  C     . THR A 1 1712 ? 157.287 227.040 181.418 1.00 2.44  ? 1712 THR A C     1 
ATOM   2103  O  O     . THR A 1 1712 ? 156.277 226.811 180.743 1.00 2.44  ? 1712 THR A O     1 
ATOM   2104  C  CB    . THR A 1 1712 ? 159.137 228.479 180.520 1.00 3.30  ? 1712 THR A CB    1 
ATOM   2105  O  OG1   . THR A 1 1712 ? 159.619 229.825 180.437 1.00 5.33  ? 1712 THR A OG1   1 
ATOM   2106  C  CG2   . THR A 1 1712 ? 158.792 227.979 179.130 1.00 2.63  ? 1712 THR A CG2   1 
ATOM   2107  N  N     . LEU A 1 1713 ? 157.878 226.100 182.156 1.00 2.34  ? 1713 LEU A N     1 
ATOM   2108  C  CA    . LEU A 1 1713 ? 157.344 224.743 182.209 1.00 1.26  ? 1713 LEU A CA    1 
ATOM   2109  C  C     . LEU A 1 1713 ? 155.948 224.714 182.819 1.00 1.71  ? 1713 LEU A C     1 
ATOM   2110  O  O     . LEU A 1 1713 ? 155.073 223.982 182.344 1.00 5.23  ? 1713 LEU A O     1 
ATOM   2111  C  CB    . LEU A 1 1713 ? 158.293 223.845 182.995 1.00 1.28  ? 1713 LEU A CB    1 
ATOM   2112  C  CG    . LEU A 1 1713 ? 159.605 223.515 182.286 1.00 0.97  ? 1713 LEU A CG    1 
ATOM   2113  C  CD1   . LEU A 1 1713 ? 160.470 222.639 183.162 1.00 0.74  ? 1713 LEU A CD1   1 
ATOM   2114  C  CD2   . LEU A 1 1713 ? 159.319 222.840 180.955 1.00 0.88  ? 1713 LEU A CD2   1 
ATOM   2115  N  N     . ALA A 1 1714 ? 155.723 225.493 183.879 1.00 1.78  ? 1714 ALA A N     1 
ATOM   2116  C  CA    . ALA A 1 1714 ? 154.392 225.563 184.472 1.00 1.71  ? 1714 ALA A CA    1 
ATOM   2117  C  C     . ALA A 1 1714 ? 153.389 226.190 183.510 1.00 1.43  ? 1714 ALA A C     1 
ATOM   2118  O  O     . ALA A 1 1714 ? 152.248 225.724 183.405 1.00 2.02  ? 1714 ALA A O     1 
ATOM   2119  C  CB    . ALA A 1 1714 ? 154.443 226.337 185.789 1.00 1.80  ? 1714 ALA A CB    1 
ATOM   2120  N  N     . LYS A 1 1715 ? 153.789 227.252 182.808 1.00 1.96  ? 1715 LYS A N     1 
ATOM   2121  C  CA    . LYS A 1 1715 ? 152.919 227.835 181.791 1.00 3.08  ? 1715 LYS A CA    1 
ATOM   2122  C  C     . LYS A 1 1715 ? 152.684 226.864 180.643 1.00 2.29  ? 1715 LYS A C     1 
ATOM   2123  O  O     . LYS A 1 1715 ? 151.567 226.771 180.121 1.00 4.28  ? 1715 LYS A O     1 
ATOM   2124  C  CB    . LYS A 1 1715 ? 153.515 229.143 181.274 1.00 4.50  ? 1715 LYS A CB    1 
ATOM   2125  C  CG    . LYS A 1 1715 ? 153.406 230.303 182.240 1.00 4.13  ? 1715 LYS A CG    1 
ATOM   2126  C  CD    . LYS A 1 1715 ? 153.400 231.630 181.499 1.00 8.28  ? 1715 LYS A CD    1 
ATOM   2127  C  CE    . LYS A 1 1715 ? 154.125 232.708 182.284 1.00 8.15  ? 1715 LYS A CE    1 
ATOM   2128  N  NZ    . LYS A 1 1715 ? 153.873 232.596 183.743 1.00 14.34 ? 1715 LYS A NZ    1 
ATOM   2129  N  N     . LEU A 1 1716 ? 153.725 226.138 180.233 1.00 2.24  ? 1716 LEU A N     1 
ATOM   2130  C  CA    . LEU A 1 1716 ? 153.567 225.141 179.179 1.00 2.40  ? 1716 LEU A CA    1 
ATOM   2131  C  C     . LEU A 1 1716 ? 152.702 223.977 179.635 1.00 2.99  ? 1716 LEU A C     1 
ATOM   2132  O  O     . LEU A 1 1716 ? 151.969 223.398 178.827 1.00 3.89  ? 1716 LEU A O     1 
ATOM   2133  C  CB    . LEU A 1 1716 ? 154.936 224.641 178.722 1.00 1.89  ? 1716 LEU A CB    1 
ATOM   2134  C  CG    . LEU A 1 1716 ? 155.679 225.482 177.685 1.00 1.79  ? 1716 LEU A CG    1 
ATOM   2135  C  CD1   . LEU A 1 1716 ? 157.094 224.970 177.510 1.00 2.16  ? 1716 LEU A CD1   1 
ATOM   2136  C  CD2   . LEU A 1 1716 ? 154.939 225.480 176.359 1.00 1.94  ? 1716 LEU A CD2   1 
ATOM   2137  N  N     . LEU A 1 1717 ? 152.780 223.612 180.919 1.00 2.51  ? 1717 LEU A N     1 
ATOM   2138  C  CA    . LEU A 1 1717 ? 151.922 222.556 181.442 1.00 2.06  ? 1717 LEU A CA    1 
ATOM   2139  C  C     . LEU A 1 1717 ? 150.453 222.948 181.357 1.00 3.72  ? 1717 LEU A C     1 
ATOM   2140  O  O     . LEU A 1 1717 ? 149.607 222.129 180.985 1.00 4.98  ? 1717 LEU A O     1 
ATOM   2141  C  CB    . LEU A 1 1717 ? 152.306 222.229 182.884 1.00 2.18  ? 1717 LEU A CB    1 
ATOM   2142  C  CG    . LEU A 1 1717 ? 151.463 221.151 183.573 1.00 2.54  ? 1717 LEU A CG    1 
ATOM   2143  C  CD1   . LEU A 1 1717 ? 151.630 219.803 182.885 1.00 0.99  ? 1717 LEU A CD1   1 
ATOM   2144  C  CD2   . LEU A 1 1717 ? 151.808 221.051 185.048 1.00 0.56  ? 1717 LEU A CD2   1 
ATOM   2145  N  N     . ALA A 1 1718 ? 150.133 224.201 181.686 1.00 3.21  ? 1718 ALA A N     1 
ATOM   2146  C  CA    . ALA A 1 1718 ? 148.744 224.647 181.642 1.00 4.07  ? 1718 ALA A CA    1 
ATOM   2147  C  C     . ALA A 1 1718 ? 148.185 224.573 180.227 1.00 9.25  ? 1718 ALA A C     1 
ATOM   2148  O  O     . ALA A 1 1718 ? 147.035 224.165 180.026 1.00 12.28 ? 1718 ALA A O     1 
ATOM   2149  C  CB    . ALA A 1 1718 ? 148.629 226.067 182.191 1.00 4.53  ? 1718 ALA A CB    1 
ATOM   2150  N  N     . GLU A 1 1719 ? 148.981 224.969 179.234 1.00 11.23 ? 1719 GLU A N     1 
ATOM   2151  C  CA    . GLU A 1 1719 ? 148.547 224.850 177.847 1.00 7.40  ? 1719 GLU A CA    1 
ATOM   2152  C  C     . GLU A 1 1719 ? 148.390 223.391 177.439 1.00 5.98  ? 1719 GLU A C     1 
ATOM   2153  O  O     . GLU A 1 1719 ? 147.447 223.038 176.720 1.00 10.63 ? 1719 GLU A O     1 
ATOM   2154  C  CB    . GLU A 1 1719 ? 149.536 225.566 176.928 1.00 7.58  ? 1719 GLU A CB    1 
ATOM   2155  C  CG    . GLU A 1 1719 ? 149.612 227.064 177.165 1.00 10.73 ? 1719 GLU A CG    1 
ATOM   2156  C  CD    . GLU A 1 1719 ? 151.005 227.621 176.953 1.00 15.34 ? 1719 GLU A CD    1 
ATOM   2157  O  OE1   . GLU A 1 1719 ? 151.939 226.823 176.737 1.00 12.12 ? 1719 GLU A OE1   1 
ATOM   2158  O  OE2   . GLU A 1 1719 ? 151.166 228.857 177.006 1.00 21.21 ? 1719 GLU A OE2   1 
ATOM   2159  N  N     . SER A 1 1720 ? 149.307 222.528 177.884 1.00 4.41  ? 1720 SER A N     1 
ATOM   2160  C  CA    . SER A 1 1720 ? 149.221 221.110 177.552 1.00 4.18  ? 1720 SER A CA    1 
ATOM   2161  C  C     . SER A 1 1720 ? 148.013 220.452 178.209 1.00 5.91  ? 1720 SER A C     1 
ATOM   2162  O  O     . SER A 1 1720 ? 147.344 219.620 177.588 1.00 6.55  ? 1720 SER A O     1 
ATOM   2163  C  CB    . SER A 1 1720 ? 150.511 220.400 177.961 1.00 3.80  ? 1720 SER A CB    1 
ATOM   2164  O  OG    . SER A 1 1720 ? 150.531 219.065 177.490 1.00 2.89  ? 1720 SER A OG    1 
ATOM   2165  N  N     . VAL A 1 1721 ? 147.726 220.801 179.466 1.00 8.31  ? 1721 VAL A N     1 
ATOM   2166  C  CA    . VAL A 1 1721 ? 146.570 220.229 180.155 1.00 6.90  ? 1721 VAL A CA    1 
ATOM   2167  C  C     . VAL A 1 1721 ? 145.280 220.590 179.430 1.00 8.77  ? 1721 VAL A C     1 
ATOM   2168  O  O     . VAL A 1 1721 ? 144.353 219.776 179.342 1.00 13.84 ? 1721 VAL A O     1 
ATOM   2169  C  CB    . VAL A 1 1721 ? 146.544 220.674 181.631 1.00 4.75  ? 1721 VAL A CB    1 
ATOM   2170  C  CG1   . VAL A 1 1721 ? 145.271 220.203 182.309 1.00 4.39  ? 1721 VAL A CG1   1 
ATOM   2171  C  CG2   . VAL A 1 1721 ? 147.738 220.107 182.371 1.00 3.22  ? 1721 VAL A CG2   1 
ATOM   2172  N  N     . THR A 1 1722 ? 145.201 221.808 178.892 1.00 9.65  ? 1722 THR A N     1 
ATOM   2173  C  CA    . THR A 1 1722 ? 144.004 222.219 178.166 1.00 9.57  ? 1722 THR A CA    1 
ATOM   2174  C  C     . THR A 1 1722 ? 143.758 221.331 176.954 1.00 12.77 ? 1722 THR A C     1 
ATOM   2175  O  O     . THR A 1 1722 ? 142.619 220.928 176.689 1.00 21.37 ? 1722 THR A O     1 
ATOM   2176  C  CB    . THR A 1 1722 ? 144.125 223.683 177.738 1.00 9.43  ? 1722 THR A CB    1 
ATOM   2177  O  OG1   . THR A 1 1722 ? 144.274 224.510 178.897 1.00 13.35 ? 1722 THR A OG1   1 
ATOM   2178  C  CG2   . THR A 1 1722 ? 142.891 224.119 176.971 1.00 11.12 ? 1722 THR A CG2   1 
ATOM   2179  N  N     . GLU A 1 1723 ? 144.816 221.012 176.205 1.00 14.69 ? 1723 GLU A N     1 
ATOM   2180  C  CA    . GLU A 1 1723 ? 144.655 220.209 174.997 1.00 10.67 ? 1723 GLU A CA    1 
ATOM   2181  C  C     . GLU A 1 1723 ? 144.417 218.738 175.320 1.00 13.66 ? 1723 GLU A C     1 
ATOM   2182  O  O     . GLU A 1 1723 ? 143.589 218.084 174.675 1.00 14.51 ? 1723 GLU A O     1 
ATOM   2183  C  CB    . GLU A 1 1723 ? 145.882 220.368 174.099 1.00 9.23  ? 1723 GLU A CB    1 
ATOM   2184  C  CG    . GLU A 1 1723 ? 146.155 221.799 173.677 1.00 11.53 ? 1723 GLU A CG    1 
ATOM   2185  C  CD    . GLU A 1 1723 ? 147.313 221.908 172.705 1.00 19.15 ? 1723 GLU A CD    1 
ATOM   2186  O  OE1   . GLU A 1 1723 ? 147.836 220.857 172.281 1.00 20.25 ? 1723 GLU A OE1   1 
ATOM   2187  O  OE2   . GLU A 1 1723 ? 147.702 223.046 172.369 1.00 22.31 ? 1723 GLU A OE2   1 
ATOM   2188  N  N     . VAL A 1 1724 ? 145.136 218.195 176.308 1.00 11.52 ? 1724 VAL A N     1 
ATOM   2189  C  CA    . VAL A 1 1724 ? 145.046 216.765 176.589 1.00 10.02 ? 1724 VAL A CA    1 
ATOM   2190  C  C     . VAL A 1 1724 ? 143.681 216.392 177.154 1.00 14.44 ? 1724 VAL A C     1 
ATOM   2191  O  O     . VAL A 1 1724 ? 143.268 215.230 177.045 1.00 17.05 ? 1724 VAL A O     1 
ATOM   2192  C  CB    . VAL A 1 1724 ? 146.178 216.327 177.542 1.00 7.76  ? 1724 VAL A CB    1 
ATOM   2193  C  CG1   . VAL A 1 1724 ? 146.006 216.950 178.913 1.00 8.94  ? 1724 VAL A CG1   1 
ATOM   2194  C  CG2   . VAL A 1 1724 ? 146.266 214.808 177.633 1.00 7.84  ? 1724 VAL A CG2   1 
ATOM   2195  N  N     . GLU A 1 1725 ? 142.960 217.348 177.748 1.00 15.45 ? 1725 GLU A N     1 
ATOM   2196  C  CA    . GLU A 1 1725 ? 141.629 217.055 178.271 1.00 15.42 ? 1725 GLU A CA    1 
ATOM   2197  C  C     . GLU A 1 1725 ? 140.665 216.651 177.165 1.00 19.09 ? 1725 GLU A C     1 
ATOM   2198  O  O     . GLU A 1 1725 ? 139.749 215.856 177.405 1.00 25.85 ? 1725 GLU A O     1 
ATOM   2199  C  CB    . GLU A 1 1725 ? 141.081 218.259 179.034 1.00 16.20 ? 1725 GLU A CB    1 
ATOM   2200  C  CG    . GLU A 1 1725 ? 141.678 218.442 180.417 1.00 16.10 ? 1725 GLU A CG    1 
ATOM   2201  C  CD    . GLU A 1 1725 ? 141.282 219.759 181.050 1.00 20.93 ? 1725 GLU A CD    1 
ATOM   2202  O  OE1   . GLU A 1 1725 ? 141.534 220.816 180.433 1.00 21.02 ? 1725 GLU A OE1   1 
ATOM   2203  O  OE2   . GLU A 1 1725 ? 140.727 219.738 182.167 1.00 25.87 ? 1725 GLU A OE2   1 
ATOM   2204  N  N     . ILE A 1 1726 ? 140.848 217.187 175.956 1.00 17.01 ? 1726 ILE A N     1 
ATOM   2205  C  CA    . ILE A 1 1726 ? 140.018 216.778 174.826 1.00 17.32 ? 1726 ILE A CA    1 
ATOM   2206  C  C     . ILE A 1 1726 ? 140.221 215.299 174.527 1.00 18.31 ? 1726 ILE A C     1 
ATOM   2207  O  O     . ILE A 1 1726 ? 139.262 214.563 174.269 1.00 23.06 ? 1726 ILE A O     1 
ATOM   2208  C  CB    . ILE A 1 1726 ? 140.323 217.649 173.594 1.00 14.34 ? 1726 ILE A CB    1 
ATOM   2209  C  CG1   . ILE A 1 1726 ? 140.388 219.130 173.984 1.00 15.25 ? 1726 ILE A CG1   1 
ATOM   2210  C  CG2   . ILE A 1 1726 ? 139.289 217.420 172.508 1.00 20.38 ? 1726 ILE A CG2   1 
ATOM   2211  C  CD1   . ILE A 1 1726 ? 139.127 219.657 174.622 1.00 17.83 ? 1726 ILE A CD1   1 
ATOM   2212  N  N     . PHE A 1 1727 ? 141.475 214.841 174.557 1.00 17.18 ? 1727 PHE A N     1 
ATOM   2213  C  CA    . PHE A 1 1727 ? 141.761 213.426 174.343 1.00 12.42 ? 1727 PHE A CA    1 
ATOM   2214  C  C     . PHE A 1 1727 ? 141.142 212.566 175.436 1.00 15.14 ? 1727 PHE A C     1 
ATOM   2215  O  O     . PHE A 1 1727 ? 140.622 211.478 175.160 1.00 20.89 ? 1727 PHE A O     1 
ATOM   2216  C  CB    . PHE A 1 1727 ? 143.271 213.207 174.275 1.00 9.29  ? 1727 PHE A CB    1 
ATOM   2217  C  CG    . PHE A 1 1727 ? 143.945 213.988 173.190 1.00 11.17 ? 1727 PHE A CG    1 
ATOM   2218  C  CD1   . PHE A 1 1727 ? 143.350 214.127 171.947 1.00 10.85 ? 1727 PHE A CD1   1 
ATOM   2219  C  CD2   . PHE A 1 1727 ? 145.168 214.598 173.416 1.00 10.28 ? 1727 PHE A CD2   1 
ATOM   2220  C  CE1   . PHE A 1 1727 ? 143.970 214.848 170.946 1.00 9.54  ? 1727 PHE A CE1   1 
ATOM   2221  C  CE2   . PHE A 1 1727 ? 145.791 215.319 172.418 1.00 6.55  ? 1727 PHE A CE2   1 
ATOM   2222  C  CZ    . PHE A 1 1727 ? 145.191 215.445 171.182 1.00 7.84  ? 1727 PHE A CZ    1 
ATOM   2223  N  N     . GLY A 1 1728 ? 141.201 213.028 176.683 1.00 17.30 ? 1728 GLY A N     1 
ATOM   2224  C  CA    . GLY A 1 1728 ? 140.548 212.312 177.759 1.00 14.30 ? 1728 GLY A CA    1 
ATOM   2225  C  C     . GLY A 1 1728 ? 139.040 212.313 177.604 1.00 17.64 ? 1728 GLY A C     1 
ATOM   2226  O  O     . GLY A 1 1728 ? 138.451 213.229 177.029 1.00 21.32 ? 1728 GLY A O     1 
ATOM   2227  N  N     . LYS A 1 1729 ? 138.417 211.261 178.136 1.00 21.43 ? 1729 LYS A N     1 
ATOM   2228  C  CA    . LYS A 1 1729 ? 136.977 210.996 178.018 1.00 28.16 ? 1729 LYS A CA    1 
ATOM   2229  C  C     . LYS A 1 1729 ? 136.457 211.324 176.617 1.00 31.58 ? 1729 LYS A C     1 
ATOM   2230  O  O     . LYS A 1 1729 ? 135.436 211.992 176.433 1.00 33.40 ? 1729 LYS A O     1 
ATOM   2231  C  CB    . LYS A 1 1729 ? 136.177 211.727 179.107 1.00 26.95 ? 1729 LYS A CB    1 
ATOM   2232  C  CG    . LYS A 1 1729 ? 136.307 213.246 179.158 1.00 26.27 ? 1729 LYS A CG    1 
ATOM   2233  C  CD    . LYS A 1 1729 ? 135.535 213.832 180.329 1.00 26.35 ? 1729 LYS A CD    1 
ATOM   2234  C  CE    . LYS A 1 1729 ? 135.954 213.190 181.643 1.00 21.55 ? 1729 LYS A CE    1 
ATOM   2235  N  NZ    . LYS A 1 1729 ? 135.239 213.785 182.805 1.00 28.31 ? 1729 LYS A NZ    1 
ATOM   2236  N  N     . ALA A 1 1730 ? 137.181 210.831 175.615 1.00 27.64 ? 1730 ALA A N     1 
ATOM   2237  C  CA    . ALA A 1 1730 ? 136.789 210.934 174.218 1.00 22.32 ? 1730 ALA A CA    1 
ATOM   2238  C  C     . ALA A 1 1730 ? 136.679 209.535 173.629 1.00 28.85 ? 1730 ALA A C     1 
ATOM   2239  O  O     . ALA A 1 1730 ? 137.522 208.672 173.897 1.00 28.80 ? 1730 ALA A O     1 
ATOM   2240  C  CB    . ALA A 1 1730 ? 137.790 211.766 173.416 1.00 21.40 ? 1730 ALA A CB    1 
ATOM   2241  N  N     . THR A 1 1731 ? 135.627 209.311 172.839 1.00 22.58 ? 1731 THR A N     1 
ATOM   2242  C  CA    . THR A 1 1731 ? 135.378 207.978 172.300 1.00 22.61 ? 1731 THR A CA    1 
ATOM   2243  C  C     . THR A 1 1731 ? 136.469 207.553 171.324 1.00 28.23 ? 1731 THR A C     1 
ATOM   2244  O  O     . THR A 1 1731 ? 136.930 206.406 171.362 1.00 31.87 ? 1731 THR A O     1 
ATOM   2245  C  CB    . THR A 1 1731 ? 134.008 207.934 171.620 1.00 26.53 ? 1731 THR A CB    1 
ATOM   2246  O  OG1   . THR A 1 1731 ? 133.981 208.865 170.531 1.00 34.17 ? 1731 THR A OG1   1 
ATOM   2247  C  CG2   . THR A 1 1731 ? 132.913 208.292 172.612 1.00 26.01 ? 1731 THR A CG2   1 
ATOM   2248  N  N     . SER A 1 1732 ? 136.894 208.454 170.442 1.00 22.50 ? 1732 SER A N     1 
ATOM   2249  C  CA    . SER A 1 1732 ? 137.879 208.136 169.419 1.00 21.66 ? 1732 SER A CA    1 
ATOM   2250  C  C     . SER A 1 1732 ? 138.928 209.232 169.352 1.00 18.44 ? 1732 SER A C     1 
ATOM   2251  O  O     . SER A 1 1732 ? 138.602 210.422 169.394 1.00 24.75 ? 1732 SER A O     1 
ATOM   2252  C  CB    . SER A 1 1732 ? 137.219 207.963 168.045 1.00 26.47 ? 1732 SER A CB    1 
ATOM   2253  O  OG    . SER A 1 1732 ? 136.572 209.156 167.640 1.00 28.51 ? 1732 SER A OG    1 
ATOM   2254  N  N     . ILE A 1 1733 ? 140.188 208.826 169.231 1.00 11.92 ? 1733 ILE A N     1 
ATOM   2255  C  CA    . ILE A 1 1733 ? 141.311 209.747 169.131 1.00 9.78  ? 1733 ILE A CA    1 
ATOM   2256  C  C     . ILE A 1 1733 ? 141.921 209.615 167.743 1.00 14.54 ? 1733 ILE A C     1 
ATOM   2257  O  O     . ILE A 1 1733 ? 142.300 208.515 167.324 1.00 21.41 ? 1733 ILE A O     1 
ATOM   2258  C  CB    . ILE A 1 1733 ? 142.361 209.484 170.219 1.00 11.45 ? 1733 ILE A CB    1 
ATOM   2259  C  CG1   . ILE A 1 1733 ? 141.745 209.694 171.602 1.00 15.99 ? 1733 ILE A CG1   1 
ATOM   2260  C  CG2   . ILE A 1 1733 ? 143.581 210.373 170.011 1.00 11.73 ? 1733 ILE A CG2   1 
ATOM   2261  C  CD1   . ILE A 1 1733 ? 142.744 209.667 172.716 1.00 6.96  ? 1733 ILE A CD1   1 
ATOM   2262  N  N     . ASP A 1 1734 ? 142.010 210.730 167.037 1.00 12.84 ? 1734 ASP A N     1 
ATOM   2263  C  CA    . ASP A 1 1734 ? 142.716 210.764 165.765 1.00 14.99 ? 1734 ASP A CA    1 
ATOM   2264  C  C     . ASP A 1 1734 ? 144.216 210.714 166.020 1.00 16.62 ? 1734 ASP A C     1 
ATOM   2265  O  O     . ASP A 1 1734 ? 144.734 211.553 166.768 1.00 11.68 ? 1734 ASP A O     1 
ATOM   2266  C  CB    . ASP A 1 1734 ? 142.347 212.024 164.990 1.00 14.86 ? 1734 ASP A CB    1 
ATOM   2267  C  CG    . ASP A 1 1734 ? 143.288 212.295 163.837 1.00 23.09 ? 1734 ASP A CG    1 
ATOM   2268  O  OD1   . ASP A 1 1734 ? 143.435 211.413 162.966 1.00 23.14 ? 1734 ASP A OD1   1 
ATOM   2269  O  OD2   . ASP A 1 1734 ? 143.886 213.389 163.804 1.00 23.56 ? 1734 ASP A OD2   1 
ATOM   2270  N  N     . PRO A 1 1735 ? 144.945 209.756 165.442 1.00 12.79 ? 1735 PRO A N     1 
ATOM   2271  C  CA    . PRO A 1 1735 ? 146.393 209.690 165.705 1.00 13.66 ? 1735 PRO A CA    1 
ATOM   2272  C  C     . PRO A 1 1735 ? 147.147 210.944 165.304 1.00 15.25 ? 1735 PRO A C     1 
ATOM   2273  O  O     . PRO A 1 1735 ? 148.091 211.337 166.000 1.00 12.35 ? 1735 PRO A O     1 
ATOM   2274  C  CB    . PRO A 1 1735 ? 146.836 208.467 164.887 1.00 15.58 ? 1735 PRO A CB    1 
ATOM   2275  C  CG    . PRO A 1 1735 ? 145.605 207.636 164.759 1.00 15.36 ? 1735 PRO A CG    1 
ATOM   2276  C  CD    . PRO A 1 1735 ? 144.476 208.616 164.637 1.00 15.16 ? 1735 PRO A CD    1 
ATOM   2277  N  N     . ASN A 1 1736 ? 146.753 211.595 164.206 1.00 15.85 ? 1736 ASN A N     1 
ATOM   2278  C  CA    . ASN A 1 1736 ? 147.480 212.775 163.747 1.00 15.86 ? 1736 ASN A CA    1 
ATOM   2279  C  C     . ASN A 1 1736 ? 147.406 213.907 164.764 1.00 14.77 ? 1736 ASN A C     1 
ATOM   2280  O  O     . ASN A 1 1736 ? 148.415 214.566 165.042 1.00 15.92 ? 1736 ASN A O     1 
ATOM   2281  C  CB    . ASN A 1 1736 ? 146.938 213.230 162.393 1.00 17.75 ? 1736 ASN A CB    1 
ATOM   2282  C  CG    . ASN A 1 1736 ? 146.976 212.130 161.352 1.00 21.48 ? 1736 ASN A CG    1 
ATOM   2283  O  OD1   . ASN A 1 1736 ? 148.008 211.491 161.147 1.00 16.05 ? 1736 ASN A OD1   1 
ATOM   2284  N  ND2   . ASN A 1 1736 ? 145.849 211.905 160.684 1.00 23.53 ? 1736 ASN A ND2   1 
ATOM   2285  N  N     . THR A 1 1737 ? 146.224 214.149 165.333 1.00 12.21 ? 1737 THR A N     1 
ATOM   2286  C  CA    . THR A 1 1737 ? 146.101 215.168 166.367 1.00 12.35 ? 1737 THR A CA    1 
ATOM   2287  C  C     . THR A 1 1737 ? 146.883 214.782 167.618 1.00 10.27 ? 1737 THR A C     1 
ATOM   2288  O  O     . THR A 1 1737 ? 147.571 215.621 168.212 1.00 13.14 ? 1737 THR A O     1 
ATOM   2289  C  CB    . THR A 1 1737 ? 144.627 215.400 166.704 1.00 12.11 ? 1737 THR A CB    1 
ATOM   2290  O  OG1   . THR A 1 1737 ? 143.920 215.782 165.519 1.00 19.77 ? 1737 THR A OG1   1 
ATOM   2291  C  CG2   . THR A 1 1737 ? 144.485 216.499 167.742 1.00 12.83 ? 1737 THR A CG2   1 
ATOM   2292  N  N     . TYR A 1 1738 ? 146.794 213.515 168.028 1.00 9.11  ? 1738 TYR A N     1 
ATOM   2293  C  CA    . TYR A 1 1738 ? 147.486 213.065 169.231 1.00 4.63  ? 1738 TYR A CA    1 
ATOM   2294  C  C     . TYR A 1 1738 ? 149.000 213.119 169.061 1.00 7.83  ? 1738 TYR A C     1 
ATOM   2295  O  O     . TYR A 1 1738 ? 149.718 213.530 169.979 1.00 8.58  ? 1738 TYR A O     1 
ATOM   2296  C  CB    . TYR A 1 1738 ? 147.030 211.652 169.590 1.00 7.86  ? 1738 TYR A CB    1 
ATOM   2297  C  CG    . TYR A 1 1738 ? 147.374 211.238 170.997 1.00 6.57  ? 1738 TYR A CG    1 
ATOM   2298  C  CD1   . TYR A 1 1738 ? 146.780 211.854 172.087 1.00 4.11  ? 1738 TYR A CD1   1 
ATOM   2299  C  CD2   . TYR A 1 1738 ? 148.289 210.224 171.237 1.00 4.93  ? 1738 TYR A CD2   1 
ATOM   2300  C  CE1   . TYR A 1 1738 ? 147.092 211.478 173.376 1.00 6.24  ? 1738 TYR A CE1   1 
ATOM   2301  C  CE2   . TYR A 1 1738 ? 148.607 209.840 172.521 1.00 4.22  ? 1738 TYR A CE2   1 
ATOM   2302  C  CZ    . TYR A 1 1738 ? 148.006 210.471 173.587 1.00 3.73  ? 1738 TYR A CZ    1 
ATOM   2303  O  OH    . TYR A 1 1738 ? 148.322 210.090 174.868 1.00 8.03  ? 1738 TYR A OH    1 
ATOM   2304  N  N     . ILE A 1 1739 ? 149.504 212.704 167.897 1.00 10.79 ? 1739 ILE A N     1 
ATOM   2305  C  CA    . ILE A 1 1739 ? 150.938 212.787 167.638 1.00 7.67  ? 1739 ILE A CA    1 
ATOM   2306  C  C     . ILE A 1 1739 ? 151.381 214.243 167.569 1.00 8.32  ? 1739 ILE A C     1 
ATOM   2307  O  O     . ILE A 1 1739 ? 152.486 214.592 168.003 1.00 10.64 ? 1739 ILE A O     1 
ATOM   2308  C  CB    . ILE A 1 1739 ? 151.291 212.011 166.355 1.00 9.38  ? 1739 ILE A CB    1 
ATOM   2309  C  CG1   . ILE A 1 1739 ? 151.071 210.511 166.561 1.00 10.41 ? 1739 ILE A CG1   1 
ATOM   2310  C  CG2   . ILE A 1 1739 ? 152.722 212.280 165.930 1.00 4.52  ? 1739 ILE A CG2   1 
ATOM   2311  C  CD1   . ILE A 1 1739 ? 152.075 209.864 167.488 1.00 10.71 ? 1739 ILE A CD1   1 
ATOM   2312  N  N     . THR A 1 1740 ? 150.526 215.116 167.035 1.00 8.94  ? 1740 THR A N     1 
ATOM   2313  C  CA    . THR A 1 1740 ? 150.838 216.540 167.006 1.00 7.45  ? 1740 THR A CA    1 
ATOM   2314  C  C     . THR A 1 1740 ? 150.999 217.098 168.415 1.00 7.87  ? 1740 THR A C     1 
ATOM   2315  O  O     . THR A 1 1740 ? 151.923 217.876 168.680 1.00 10.21 ? 1740 THR A O     1 
ATOM   2316  C  CB    . THR A 1 1740 ? 149.749 217.300 166.249 1.00 5.41  ? 1740 THR A CB    1 
ATOM   2317  O  OG1   . THR A 1 1740 ? 149.678 216.817 164.902 1.00 16.90 ? 1740 THR A OG1   1 
ATOM   2318  C  CG2   . THR A 1 1740 ? 150.044 218.790 166.228 1.00 6.76  ? 1740 THR A CG2   1 
ATOM   2319  N  N     . TRP A 1 1741 ? 150.114 216.705 169.334 1.00 4.95  ? 1741 TRP A N     1 
ATOM   2320  C  CA    . TRP A 1 1741 ? 150.209 217.190 170.707 1.00 3.49  ? 1741 TRP A CA    1 
ATOM   2321  C  C     . TRP A 1 1741 ? 151.447 216.638 171.410 1.00 4.02  ? 1741 TRP A C     1 
ATOM   2322  O  O     . TRP A 1 1741 ? 152.075 217.338 172.209 1.00 5.66  ? 1741 TRP A O     1 
ATOM   2323  C  CB    . TRP A 1 1741 ? 148.941 216.831 171.479 1.00 3.58  ? 1741 TRP A CB    1 
ATOM   2324  C  CG    . TRP A 1 1741 ? 149.099 216.936 172.965 1.00 3.16  ? 1741 TRP A CG    1 
ATOM   2325  C  CD1   . TRP A 1 1741 ? 148.975 218.061 173.722 1.00 3.11  ? 1741 TRP A CD1   1 
ATOM   2326  C  CD2   . TRP A 1 1741 ? 149.410 215.874 173.871 1.00 2.23  ? 1741 TRP A CD2   1 
ATOM   2327  N  NE1   . TRP A 1 1741 ? 149.193 217.768 175.043 1.00 2.57  ? 1741 TRP A NE1   1 
ATOM   2328  C  CE2   . TRP A 1 1741 ? 149.463 216.430 175.162 1.00 2.98  ? 1741 TRP A CE2   1 
ATOM   2329  C  CE3   . TRP A 1 1741 ? 149.650 214.506 173.717 1.00 1.89  ? 1741 TRP A CE3   1 
ATOM   2330  C  CZ2   . TRP A 1 1741 ? 149.745 215.668 176.292 1.00 3.79  ? 1741 TRP A CZ2   1 
ATOM   2331  C  CZ3   . TRP A 1 1741 ? 149.931 213.753 174.838 1.00 2.09  ? 1741 TRP A CZ3   1 
ATOM   2332  C  CH2   . TRP A 1 1741 ? 149.975 214.334 176.110 1.00 2.15  ? 1741 TRP A CH2   1 
ATOM   2333  N  N     . ILE A 1 1742 ? 151.808 215.384 171.128 1.00 3.62  ? 1742 ILE A N     1 
ATOM   2334  C  CA    . ILE A 1 1742 ? 153.014 214.807 171.717 1.00 5.15  ? 1742 ILE A CA    1 
ATOM   2335  C  C     . ILE A 1 1742 ? 154.251 215.564 171.251 1.00 7.02  ? 1742 ILE A C     1 
ATOM   2336  O  O     . ILE A 1 1742 ? 155.154 215.860 172.042 1.00 8.89  ? 1742 ILE A O     1 
ATOM   2337  C  CB    . ILE A 1 1742 ? 153.110 213.307 171.377 1.00 6.09  ? 1742 ILE A CB    1 
ATOM   2338  C  CG1   . ILE A 1 1742 ? 151.967 212.534 172.035 1.00 5.11  ? 1742 ILE A CG1   1 
ATOM   2339  C  CG2   . ILE A 1 1742 ? 154.453 212.742 171.805 1.00 2.42  ? 1742 ILE A CG2   1 
ATOM   2340  C  CD1   . ILE A 1 1742 ? 151.823 211.123 171.531 1.00 5.05  ? 1742 ILE A CD1   1 
ATOM   2341  N  N     . ASP A 1 1743 ? 154.309 215.891 169.959 1.00 7.45  ? 1743 ASP A N     1 
ATOM   2342  C  CA    . ASP A 1 1743 ? 155.481 216.563 169.410 1.00 7.90  ? 1743 ASP A CA    1 
ATOM   2343  C  C     . ASP A 1 1743 ? 155.602 217.999 169.904 1.00 8.85  ? 1743 ASP A C     1 
ATOM   2344  O  O     . ASP A 1 1743 ? 156.716 218.523 170.011 1.00 8.39  ? 1743 ASP A O     1 
ATOM   2345  C  CB    . ASP A 1 1743 ? 155.423 216.534 167.883 1.00 9.39  ? 1743 ASP A CB    1 
ATOM   2346  C  CG    . ASP A 1 1743 ? 156.032 215.280 167.304 1.00 9.58  ? 1743 ASP A CG    1 
ATOM   2347  O  OD1   . ASP A 1 1743 ? 156.793 214.604 168.024 1.00 16.11 ? 1743 ASP A OD1   1 
ATOM   2348  O  OD2   . ASP A 1 1743 ? 155.747 214.969 166.130 1.00 17.24 ? 1743 ASP A OD2   1 
ATOM   2349  N  N     . LYS A 1 1744 ? 154.475 218.648 170.205 1.00 4.92  ? 1744 LYS A N     1 
ATOM   2350  C  CA    . LYS A 1 1744 ? 154.501 220.063 170.558 1.00 4.39  ? 1744 LYS A CA    1 
ATOM   2351  C  C     . LYS A 1 1744 ? 155.078 220.302 171.949 1.00 4.59  ? 1744 LYS A C     1 
ATOM   2352  O  O     . LYS A 1 1744 ? 155.746 221.317 172.171 1.00 6.72  ? 1744 LYS A O     1 
ATOM   2353  C  CB    . LYS A 1 1744 ? 153.093 220.647 170.455 1.00 5.91  ? 1744 LYS A CB    1 
ATOM   2354  C  CG    . LYS A 1 1744 ? 152.974 222.106 170.872 1.00 6.08  ? 1744 LYS A CG    1 
ATOM   2355  C  CD    . LYS A 1 1744 ? 151.518 222.528 170.957 1.00 4.76  ? 1744 LYS A CD    1 
ATOM   2356  C  CE    . LYS A 1 1744 ? 151.320 223.957 170.488 1.00 11.22 ? 1744 LYS A CE    1 
ATOM   2357  N  NZ    . LYS A 1 1744 ? 151.272 224.917 171.624 1.00 17.50 ? 1744 LYS A NZ    1 
ATOM   2358  N  N     . TYR A 1 1745 ? 154.843 219.394 172.891 1.00 5.10  ? 1745 TYR A N     1 
ATOM   2359  C  CA    . TYR A 1 1745 ? 155.235 219.609 174.276 1.00 3.17  ? 1745 TYR A CA    1 
ATOM   2360  C  C     . TYR A 1 1745 ? 156.366 218.671 174.675 1.00 2.67  ? 1745 TYR A C     1 
ATOM   2361  O  O     . TYR A 1 1745 ? 156.637 217.666 174.014 1.00 6.02  ? 1745 TYR A O     1 
ATOM   2362  C  CB    . TYR A 1 1745 ? 154.036 219.429 175.213 1.00 1.41  ? 1745 TYR A CB    1 
ATOM   2363  C  CG    . TYR A 1 1745 ? 152.971 220.473 174.997 1.00 2.37  ? 1745 TYR A CG    1 
ATOM   2364  C  CD1   . TYR A 1 1745 ? 153.106 221.750 175.523 1.00 2.99  ? 1745 TYR A CD1   1 
ATOM   2365  C  CD2   . TYR A 1 1745 ? 151.839 220.189 174.250 1.00 3.44  ? 1745 TYR A CD2   1 
ATOM   2366  C  CE1   . TYR A 1 1745 ? 152.140 222.710 175.318 1.00 3.27  ? 1745 TYR A CE1   1 
ATOM   2367  C  CE2   . TYR A 1 1745 ? 150.867 221.142 174.042 1.00 4.37  ? 1745 TYR A CE2   1 
ATOM   2368  C  CZ    . TYR A 1 1745 ? 151.022 222.400 174.575 1.00 4.22  ? 1745 TYR A CZ    1 
ATOM   2369  O  OH    . TYR A 1 1745 ? 150.052 223.352 174.368 1.00 8.63  ? 1745 TYR A OH    1 
ATOM   2370  N  N     . GLN A 1 1746 ? 157.028 219.027 175.771 1.00 1.77  ? 1746 GLN A N     1 
ATOM   2371  C  CA    . GLN A 1 1746 ? 158.198 218.300 176.231 1.00 2.31  ? 1746 GLN A CA    1 
ATOM   2372  C  C     . GLN A 1 1746 ? 157.804 216.935 176.786 1.00 2.83  ? 1746 GLN A C     1 
ATOM   2373  O  O     . GLN A 1 1746 ? 156.656 216.694 177.165 1.00 9.22  ? 1746 GLN A O     1 
ATOM   2374  C  CB    . GLN A 1 1746 ? 158.946 219.113 177.287 1.00 2.86  ? 1746 GLN A CB    1 
ATOM   2375  C  CG    . GLN A 1 1746 ? 159.799 220.231 176.712 1.00 3.02  ? 1746 GLN A CG    1 
ATOM   2376  C  CD    . GLN A 1 1746 ? 158.987 221.442 176.290 1.00 2.72  ? 1746 GLN A CD    1 
ATOM   2377  O  OE1   . GLN A 1 1746 ? 157.781 221.508 176.521 1.00 3.36  ? 1746 GLN A OE1   1 
ATOM   2378  N  NE2   . GLN A 1 1746 ? 159.646 222.404 175.658 1.00 2.86  ? 1746 GLN A NE2   1 
ATOM   2379  N  N     . ALA A 1 1747 ? 158.786 216.032 176.831 1.00 2.13  ? 1747 ALA A N     1 
ATOM   2380  C  CA    . ALA A 1 1747 ? 158.515 214.662 177.252 1.00 2.42  ? 1747 ALA A CA    1 
ATOM   2381  C  C     . ALA A 1 1747 ? 157.989 214.610 178.681 1.00 2.30  ? 1747 ALA A C     1 
ATOM   2382  O  O     . ALA A 1 1747 ? 157.036 213.879 178.972 1.00 3.36  ? 1747 ALA A O     1 
ATOM   2383  C  CB    . ALA A 1 1747 ? 159.777 213.812 177.115 1.00 2.00  ? 1747 ALA A CB    1 
ATOM   2384  N  N     . GLN A 1 1748 ? 158.594 215.380 179.585 1.00 2.49  ? 1748 GLN A N     1 
ATOM   2385  C  CA    . GLN A 1 1748 ? 158.139 215.392 180.971 1.00 1.66  ? 1748 GLN A CA    1 
ATOM   2386  C  C     . GLN A 1 1748 ? 156.720 215.937 181.099 1.00 1.77  ? 1748 GLN A C     1 
ATOM   2387  O  O     . GLN A 1 1748 ? 155.937 215.431 181.911 1.00 1.58  ? 1748 GLN A O     1 
ATOM   2388  C  CB    . GLN A 1 1748 ? 159.119 216.191 181.830 1.00 1.32  ? 1748 GLN A CB    1 
ATOM   2389  C  CG    . GLN A 1 1748 ? 159.203 217.663 181.481 1.00 3.37  ? 1748 GLN A CG    1 
ATOM   2390  C  CD    . GLN A 1 1748 ? 160.225 218.401 182.311 1.00 4.22  ? 1748 GLN A CD    1 
ATOM   2391  O  OE1   . GLN A 1 1748 ? 160.851 217.831 183.199 1.00 2.39  ? 1748 GLN A OE1   1 
ATOM   2392  N  NE2   . GLN A 1 1748 ? 160.419 219.673 182.005 1.00 7.74  ? 1748 GLN A NE2   1 
ATOM   2393  N  N     . LEU A 1 1749 ? 156.368 216.957 180.316 1.00 2.51  ? 1749 LEU A N     1 
ATOM   2394  C  CA    . LEU A 1 1749 ? 155.033 217.534 180.396 1.00 2.00  ? 1749 LEU A CA    1 
ATOM   2395  C  C     . LEU A 1 1749 ? 153.985 216.657 179.725 1.00 2.42  ? 1749 LEU A C     1 
ATOM   2396  O  O     . LEU A 1 1749 ? 152.819 216.675 180.131 1.00 1.95  ? 1749 LEU A O     1 
ATOM   2397  C  CB    . LEU A 1 1749 ? 155.027 218.926 179.767 1.00 2.45  ? 1749 LEU A CB    1 
ATOM   2398  C  CG    . LEU A 1 1749 ? 155.870 219.988 180.468 1.00 3.73  ? 1749 LEU A CG    1 
ATOM   2399  C  CD1   . LEU A 1 1749 ? 155.491 221.362 179.963 1.00 2.90  ? 1749 LEU A CD1   1 
ATOM   2400  C  CD2   . LEU A 1 1749 ? 155.702 219.905 181.977 1.00 2.60  ? 1749 LEU A CD2   1 
ATOM   2401  N  N     . VAL A 1 1750 ? 154.377 215.899 178.700 1.00 2.19  ? 1750 VAL A N     1 
ATOM   2402  C  CA    . VAL A 1 1750 ? 153.434 215.025 178.008 1.00 2.05  ? 1750 VAL A CA    1 
ATOM   2403  C  C     . VAL A 1 1750 ? 152.946 213.924 178.941 1.00 1.28  ? 1750 VAL A C     1 
ATOM   2404  O  O     . VAL A 1 1750 ? 151.745 213.638 179.022 1.00 2.74  ? 1750 VAL A O     1 
ATOM   2405  C  CB    . VAL A 1 1750 ? 154.079 214.455 176.732 1.00 2.38  ? 1750 VAL A CB    1 
ATOM   2406  C  CG1   . VAL A 1 1750 ? 153.321 213.249 176.246 1.00 2.46  ? 1750 VAL A CG1   1 
ATOM   2407  C  CG2   . VAL A 1 1750 ? 154.119 215.515 175.648 1.00 1.81  ? 1750 VAL A CG2   1 
ATOM   2408  N  N     . VAL A 1 1751 ? 153.869 213.290 179.666 1.00 1.11  ? 1751 VAL A N     1 
ATOM   2409  C  CA    . VAL A 1 1751 ? 153.477 212.278 180.640 1.00 1.66  ? 1751 VAL A CA    1 
ATOM   2410  C  C     . VAL A 1 1751 ? 152.728 212.919 181.800 1.00 0.96  ? 1751 VAL A C     1 
ATOM   2411  O  O     . VAL A 1 1751 ? 151.740 212.370 182.298 1.00 1.65  ? 1751 VAL A O     1 
ATOM   2412  C  CB    . VAL A 1 1751 ? 154.711 211.491 181.116 1.00 1.74  ? 1751 VAL A CB    1 
ATOM   2413  C  CG1   . VAL A 1 1751 ? 154.360 210.608 182.304 1.00 2.06  ? 1751 VAL A CG1   1 
ATOM   2414  C  CG2   . VAL A 1 1751 ? 155.260 210.655 179.982 1.00 0.98  ? 1751 VAL A CG2   1 
ATOM   2415  N  N     . LEU A 1 1752 ? 153.177 214.097 182.236 1.00 1.04  ? 1752 LEU A N     1 
ATOM   2416  C  CA    . LEU A 1 1752 ? 152.493 214.809 183.309 1.00 0.76  ? 1752 LEU A CA    1 
ATOM   2417  C  C     . LEU A 1 1752 ? 151.070 215.180 182.909 1.00 0.79  ? 1752 LEU A C     1 
ATOM   2418  O  O     . LEU A 1 1752 ? 150.144 215.082 183.721 1.00 0.96  ? 1752 LEU A O     1 
ATOM   2419  C  CB    . LEU A 1 1752 ? 153.292 216.054 183.685 1.00 0.79  ? 1752 LEU A CB    1 
ATOM   2420  C  CG    . LEU A 1 1752 ? 153.098 216.659 185.072 1.00 0.52  ? 1752 LEU A CG    1 
ATOM   2421  C  CD1   . LEU A 1 1752 ? 153.346 215.622 186.152 1.00 0.34  ? 1752 LEU A CD1   1 
ATOM   2422  C  CD2   . LEU A 1 1752 ? 154.028 217.845 185.236 1.00 0.38  ? 1752 LEU A CD2   1 
ATOM   2423  N  N     . SER A 1 1753 ? 150.878 215.616 181.663 1.00 2.29  ? 1753 SER A N     1 
ATOM   2424  C  CA    . SER A 1 1753 ? 149.538 215.953 181.194 1.00 2.08  ? 1753 SER A CA    1 
ATOM   2425  C  C     . SER A 1 1753 ? 148.639 214.726 181.150 1.00 1.26  ? 1753 SER A C     1 
ATOM   2426  O  O     . SER A 1 1753 ? 147.449 214.807 181.479 1.00 0.99  ? 1753 SER A O     1 
ATOM   2427  C  CB    . SER A 1 1753 ? 149.616 216.613 179.819 1.00 1.23  ? 1753 SER A CB    1 
ATOM   2428  O  OG    . SER A 1 1753 ? 150.196 217.897 179.916 1.00 4.35  ? 1753 SER A OG    1 
ATOM   2429  N  N     . ALA A 1 1754 ? 149.183 213.581 180.734 1.00 1.21  ? 1754 ALA A N     1 
ATOM   2430  C  CA    . ALA A 1 1754 ? 148.394 212.355 180.705 1.00 1.45  ? 1754 ALA A CA    1 
ATOM   2431  C  C     . ALA A 1 1754 ? 147.974 211.934 182.107 1.00 1.20  ? 1754 ALA A C     1 
ATOM   2432  O  O     . ALA A 1 1754 ? 146.842 211.482 182.313 1.00 1.96  ? 1754 ALA A O     1 
ATOM   2433  C  CB    . ALA A 1 1754 ? 149.181 211.239 180.020 1.00 1.12  ? 1754 ALA A CB    1 
ATOM   2434  N  N     . GLN A 1 1755 ? 148.876 212.065 183.082 1.00 0.73  ? 1755 GLN A N     1 
ATOM   2435  C  CA    . GLN A 1 1755 ? 148.538 211.705 184.455 1.00 0.60  ? 1755 GLN A CA    1 
ATOM   2436  C  C     . GLN A 1 1755 ? 147.471 212.630 185.024 1.00 0.94  ? 1755 GLN A C     1 
ATOM   2437  O  O     . GLN A 1 1755 ? 146.571 212.181 185.743 1.00 8.31  ? 1755 GLN A O     1 
ATOM   2438  C  CB    . GLN A 1 1755 ? 149.793 211.727 185.327 1.00 0.57  ? 1755 GLN A CB    1 
ATOM   2439  C  CG    . GLN A 1 1755 ? 150.852 210.740 184.890 1.00 1.52  ? 1755 GLN A CG    1 
ATOM   2440  C  CD    . GLN A 1 1755 ? 152.114 210.820 185.722 1.00 0.85  ? 1755 GLN A CD    1 
ATOM   2441  O  OE1   . GLN A 1 1755 ? 152.744 211.870 185.815 1.00 0.88  ? 1755 GLN A OE1   1 
ATOM   2442  N  NE2   . GLN A 1 1755 ? 152.495 209.702 186.325 1.00 0.83  ? 1755 GLN A NE2   1 
ATOM   2443  N  N     . ILE A 1 1756 ? 147.555 213.926 184.715 1.00 0.68  ? 1756 ILE A N     1 
ATOM   2444  C  CA    . ILE A 1 1756 ? 146.562 214.881 185.201 1.00 0.74  ? 1756 ILE A CA    1 
ATOM   2445  C  C     . ILE A 1 1756 ? 145.187 214.553 184.635 1.00 1.46  ? 1756 ILE A C     1 
ATOM   2446  O  O     . ILE A 1 1756 ? 144.186 214.530 185.359 1.00 10.69 ? 1756 ILE A O     1 
ATOM   2447  C  CB    . ILE A 1 1756 ? 146.989 216.319 184.857 1.00 2.05  ? 1756 ILE A CB    1 
ATOM   2448  C  CG1   . ILE A 1 1756 ? 148.180 216.745 185.716 1.00 1.17  ? 1756 ILE A CG1   1 
ATOM   2449  C  CG2   . ILE A 1 1756 ? 145.830 217.285 185.039 1.00 1.00  ? 1756 ILE A CG2   1 
ATOM   2450  C  CD1   . ILE A 1 1756 ? 148.978 217.877 185.126 1.00 1.08  ? 1756 ILE A CD1   1 
ATOM   2451  N  N     . ALA A 1 1757 ? 145.120 214.292 183.327 1.00 1.41  ? 1757 ALA A N     1 
ATOM   2452  C  CA    . ALA A 1 1757 ? 143.837 214.009 182.695 1.00 1.19  ? 1757 ALA A CA    1 
ATOM   2453  C  C     . ALA A 1 1757 ? 143.214 212.733 183.247 1.00 2.71  ? 1757 ALA A C     1 
ATOM   2454  O  O     . ALA A 1 1757 ? 142.009 212.688 183.516 1.00 3.43  ? 1757 ALA A O     1 
ATOM   2455  C  CB    . ALA A 1 1757 ? 144.010 213.912 181.180 1.00 1.60  ? 1757 ALA A CB    1 
ATOM   2456  N  N     . TRP A 1 1758 ? 144.023 211.687 183.429 1.00 2.30  ? 1758 TRP A N     1 
ATOM   2457  C  CA    . TRP A 1 1758 ? 143.499 210.431 183.952 1.00 2.20  ? 1758 TRP A CA    1 
ATOM   2458  C  C     . TRP A 1 1758 ? 143.002 210.589 185.384 1.00 3.83  ? 1758 TRP A C     1 
ATOM   2459  O  O     . TRP A 1 1758 ? 141.954 210.042 185.746 1.00 6.83  ? 1758 TRP A O     1 
ATOM   2460  C  CB    . TRP A 1 1758 ? 144.568 209.345 183.868 1.00 2.35  ? 1758 TRP A CB    1 
ATOM   2461  C  CG    . TRP A 1 1758 ? 144.183 208.070 184.540 1.00 1.59  ? 1758 TRP A CG    1 
ATOM   2462  C  CD1   . TRP A 1 1758 ? 143.256 207.167 184.114 1.00 1.39  ? 1758 TRP A CD1   1 
ATOM   2463  C  CD2   . TRP A 1 1758 ? 144.713 207.554 185.764 1.00 1.18  ? 1758 TRP A CD2   1 
ATOM   2464  N  NE1   . TRP A 1 1758 ? 143.176 206.120 184.996 1.00 1.34  ? 1758 TRP A NE1   1 
ATOM   2465  C  CE2   . TRP A 1 1758 ? 144.061 206.333 186.019 1.00 0.93  ? 1758 TRP A CE2   1 
ATOM   2466  C  CE3   . TRP A 1 1758 ? 145.675 208.006 186.671 1.00 1.61  ? 1758 TRP A CE3   1 
ATOM   2467  C  CZ2   . TRP A 1 1758 ? 144.341 205.559 187.140 1.00 1.03  ? 1758 TRP A CZ2   1 
ATOM   2468  C  CZ3   . TRP A 1 1758 ? 145.951 207.237 187.781 1.00 4.21  ? 1758 TRP A CZ3   1 
ATOM   2469  C  CH2   . TRP A 1 1758 ? 145.287 206.028 188.007 1.00 1.53  ? 1758 TRP A CH2   1 
ATOM   2470  N  N     . SER A 1 1759 ? 143.740 211.332 186.212 1.00 2.90  ? 1759 SER A N     1 
ATOM   2471  C  CA    . SER A 1 1759 ? 143.323 211.531 187.598 1.00 2.08  ? 1759 SER A CA    1 
ATOM   2472  C  C     . SER A 1 1759 ? 141.987 212.257 187.675 1.00 3.65  ? 1759 SER A C     1 
ATOM   2473  O  O     . SER A 1 1759 ? 141.106 211.867 188.449 1.00 8.14  ? 1759 SER A O     1 
ATOM   2474  C  CB    . SER A 1 1759 ? 144.394 212.303 188.368 1.00 1.98  ? 1759 SER A CB    1 
ATOM   2475  O  OG    . SER A 1 1759 ? 145.452 211.456 188.772 1.00 2.60  ? 1759 SER A OG    1 
ATOM   2476  N  N     . GLU A 1 1760 ? 141.813 213.312 186.876 1.00 3.75  ? 1760 GLU A N     1 
ATOM   2477  C  CA    . GLU A 1 1760 ? 140.563 214.061 186.912 1.00 5.90  ? 1760 GLU A CA    1 
ATOM   2478  C  C     . GLU A 1 1760 ? 139.398 213.245 186.368 1.00 6.57  ? 1760 GLU A C     1 
ATOM   2479  O  O     . GLU A 1 1760 ? 138.260 213.425 186.813 1.00 11.28 ? 1760 GLU A O     1 
ATOM   2480  C  CB    . GLU A 1 1760 ? 140.713 215.373 186.140 1.00 12.09 ? 1760 GLU A CB    1 
ATOM   2481  C  CG    . GLU A 1 1760 ? 141.672 216.358 186.796 1.00 14.69 ? 1760 GLU A CG    1 
ATOM   2482  C  CD    . GLU A 1 1760 ? 141.824 217.648 186.011 1.00 22.63 ? 1760 GLU A CD    1 
ATOM   2483  O  OE1   . GLU A 1 1760 ? 141.283 217.737 184.890 1.00 27.85 ? 1760 GLU A OE1   1 
ATOM   2484  O  OE2   . GLU A 1 1760 ? 142.482 218.579 186.523 1.00 20.37 ? 1760 GLU A OE2   1 
ATOM   2485  N  N     . ASN A 1 1761 ? 139.655 212.354 185.408 1.00 4.52  ? 1761 ASN A N     1 
ATOM   2486  C  CA    . ASN A 1 1761 ? 138.601 211.467 184.923 1.00 6.68  ? 1761 ASN A CA    1 
ATOM   2487  C  C     . ASN A 1 1761 ? 138.146 210.501 186.009 1.00 7.45  ? 1761 ASN A C     1 
ATOM   2488  O  O     . ASN A 1 1761 ? 136.944 210.262 186.170 1.00 8.59  ? 1761 ASN A O     1 
ATOM   2489  C  CB    . ASN A 1 1761 ? 139.082 210.701 183.692 1.00 6.94  ? 1761 ASN A CB    1 
ATOM   2490  C  CG    . ASN A 1 1761 ? 139.209 211.584 182.470 1.00 7.72  ? 1761 ASN A CG    1 
ATOM   2491  O  OD1   . ASN A 1 1761 ? 138.998 212.793 182.540 1.00 8.66  ? 1761 ASN A OD1   1 
ATOM   2492  N  ND2   . ASN A 1 1761 ? 139.561 210.983 181.341 1.00 10.51 ? 1761 ASN A ND2   1 
ATOM   2493  N  N     . VAL A 1 1762 ? 139.091 209.931 186.761 1.00 4.60  ? 1762 VAL A N     1 
ATOM   2494  C  CA    . VAL A 1 1762 ? 138.732 209.017 187.842 1.00 4.41  ? 1762 VAL A CA    1 
ATOM   2495  C  C     . VAL A 1 1762 ? 137.996 209.768 188.946 1.00 9.61  ? 1762 VAL A C     1 
ATOM   2496  O  O     . VAL A 1 1762 ? 136.992 209.285 189.485 1.00 9.97  ? 1762 VAL A O     1 
ATOM   2497  C  CB    . VAL A 1 1762 ? 139.984 208.302 188.381 1.00 2.37  ? 1762 VAL A CB    1 
ATOM   2498  C  CG1   . VAL A 1 1762 ? 139.634 207.472 189.608 1.00 2.08  ? 1762 VAL A CG1   1 
ATOM   2499  C  CG2   . VAL A 1 1762 ? 140.607 207.435 187.300 1.00 1.73  ? 1762 VAL A CG2   1 
ATOM   2500  N  N     . GLU A 1 1763 ? 138.478 210.965 189.290 1.00 5.49  ? 1763 GLU A N     1 
ATOM   2501  C  CA    . GLU A 1 1763 ? 137.778 211.804 190.261 1.00 6.26  ? 1763 GLU A CA    1 
ATOM   2502  C  C     . GLU A 1 1763 ? 136.357 212.105 189.802 1.00 8.26  ? 1763 GLU A C     1 
ATOM   2503  O  O     . GLU A 1 1763 ? 135.415 212.083 190.602 1.00 7.29  ? 1763 GLU A O     1 
ATOM   2504  C  CB    . GLU A 1 1763 ? 138.546 213.106 190.490 1.00 5.57  ? 1763 GLU A CB    1 
ATOM   2505  C  CG    . GLU A 1 1763 ? 139.890 212.971 191.181 1.00 7.83  ? 1763 GLU A CG    1 
ATOM   2506  C  CD    . GLU A 1 1763 ? 139.764 212.532 192.625 1.00 8.32  ? 1763 GLU A CD    1 
ATOM   2507  O  OE1   . GLU A 1 1763 ? 138.756 212.886 193.267 1.00 13.81 ? 1763 GLU A OE1   1 
ATOM   2508  O  OE2   . GLU A 1 1763 ? 140.680 211.848 193.125 1.00 9.77  ? 1763 GLU A OE2   1 
ATOM   2509  N  N     . THR A 1 1764 ? 136.186 212.409 188.513 1.00 6.52  ? 1764 THR A N     1 
ATOM   2510  C  CA    . THR A 1 1764 ? 134.855 212.695 187.989 1.00 7.22  ? 1764 THR A CA    1 
ATOM   2511  C  C     . THR A 1 1764 ? 133.962 211.462 188.054 1.00 9.29  ? 1764 THR A C     1 
ATOM   2512  O  O     . THR A 1 1764 ? 132.788 211.549 188.432 1.00 12.82 ? 1764 THR A O     1 
ATOM   2513  C  CB    . THR A 1 1764 ? 134.957 213.212 186.555 1.00 10.22 ? 1764 THR A CB    1 
ATOM   2514  O  OG1   . THR A 1 1764 ? 135.896 214.292 186.502 1.00 16.82 ? 1764 THR A OG1   1 
ATOM   2515  C  CG2   . THR A 1 1764 ? 133.607 213.705 186.071 1.00 9.48  ? 1764 THR A CG2   1 
ATOM   2516  N  N     . ALA A 1 1765 ? 134.505 210.300 187.686 1.00 11.83 ? 1765 ALA A N     1 
ATOM   2517  C  CA    . ALA A 1 1765 ? 133.716 209.073 187.690 1.00 11.36 ? 1765 ALA A CA    1 
ATOM   2518  C  C     . ALA A 1 1765 ? 133.320 208.671 189.105 1.00 13.10 ? 1765 ALA A C     1 
ATOM   2519  O  O     . ALA A 1 1765 ? 132.163 208.320 189.363 1.00 20.54 ? 1765 ALA A O     1 
ATOM   2520  C  CB    . ALA A 1 1765 ? 134.494 207.949 187.008 1.00 11.00 ? 1765 ALA A CB    1 
ATOM   2521  N  N     . LEU A 1 1766 ? 134.272 208.721 190.041 1.00 9.85  ? 1766 LEU A N     1 
ATOM   2522  C  CA    . LEU A 1 1766 ? 133.977 208.330 191.415 1.00 12.00 ? 1766 LEU A CA    1 
ATOM   2523  C  C     . LEU A 1 1766 ? 132.966 209.274 192.055 1.00 14.04 ? 1766 LEU A C     1 
ATOM   2524  O  O     . LEU A 1 1766 ? 132.164 208.857 192.899 1.00 25.31 ? 1766 LEU A O     1 
ATOM   2525  C  CB    . LEU A 1 1766 ? 135.265 208.284 192.238 1.00 7.75  ? 1766 LEU A CB    1 
ATOM   2526  C  CG    . LEU A 1 1766 ? 136.297 207.225 191.842 1.00 9.42  ? 1766 LEU A CG    1 
ATOM   2527  C  CD1   . LEU A 1 1766 ? 137.506 207.279 192.760 1.00 4.86  ? 1766 LEU A CD1   1 
ATOM   2528  C  CD2   . LEU A 1 1766 ? 135.681 205.839 191.843 1.00 6.76  ? 1766 LEU A CD2   1 
ATOM   2529  N  N     . SER A 1 1767 ? 132.988 210.548 191.665 1.00 16.34 ? 1767 SER A N     1 
ATOM   2530  C  CA    . SER A 1 1767 ? 132.022 211.501 192.198 1.00 18.16 ? 1767 SER A CA    1 
ATOM   2531  C  C     . SER A 1 1767 ? 130.601 211.143 191.777 1.00 19.92 ? 1767 SER A C     1 
ATOM   2532  O  O     . SER A 1 1767 ? 129.658 211.286 192.562 1.00 31.60 ? 1767 SER A O     1 
ATOM   2533  C  CB    . SER A 1 1767 ? 132.379 212.915 191.747 1.00 12.28 ? 1767 SER A CB    1 
ATOM   2534  O  OG    . SER A 1 1767 ? 133.707 213.237 192.111 1.00 20.45 ? 1767 SER A OG    1 
ATOM   2535  N  N     . SER A 1 1768 ? 130.429 210.682 190.537 1.00 17.12 ? 1768 SER A N     1 
ATOM   2536  C  CA    . SER A 1 1768 ? 129.110 210.286 190.059 1.00 15.79 ? 1768 SER A CA    1 
ATOM   2537  C  C     . SER A 1 1768 ? 128.604 209.013 190.727 1.00 22.01 ? 1768 SER A C     1 
ATOM   2538  O  O     . SER A 1 1768 ? 127.390 208.791 190.764 1.00 32.39 ? 1768 SER A O     1 
ATOM   2539  C  CB    . SER A 1 1768 ? 129.141 210.099 188.542 1.00 16.95 ? 1768 SER A CB    1 
ATOM   2540  O  OG    . SER A 1 1768 ? 127.878 209.678 188.055 1.00 27.82 ? 1768 SER A OG    1 
ATOM   2541  N  N     . MET A 1 1769 ? 129.501 208.179 191.251 1.00 21.03 ? 1769 MET A N     1 
ATOM   2542  C  CA    . MET A 1 1769 ? 129.136 206.920 191.883 1.00 19.47 ? 1769 MET A CA    1 
ATOM   2543  C  C     . MET A 1 1769 ? 128.841 207.075 193.371 1.00 31.11 ? 1769 MET A C     1 
ATOM   2544  O  O     . MET A 1 1769 ? 128.926 206.090 194.116 1.00 27.33 ? 1769 MET A O     1 
ATOM   2545  C  CB    . MET A 1 1769 ? 130.246 205.890 191.672 1.00 16.99 ? 1769 MET A CB    1 
ATOM   2546  C  CG    . MET A 1 1769 ? 130.427 205.470 190.225 1.00 22.78 ? 1769 MET A CG    1 
ATOM   2547  S  SD    . MET A 1 1769 ? 131.790 204.319 189.971 1.00 29.22 ? 1769 MET A SD    1 
ATOM   2548  C  CE    . MET A 1 1769 ? 131.132 202.842 190.741 1.00 19.12 ? 1769 MET A CE    1 
ATOM   2549  N  N     . GLY A 1 1770 ? 128.496 208.286 193.815 1.00 29.81 ? 1770 GLY A N     1 
ATOM   2550  C  CA    . GLY A 1 1770 ? 128.286 208.519 195.235 1.00 28.22 ? 1770 GLY A CA    1 
ATOM   2551  C  C     . GLY A 1 1770 ? 127.142 207.704 195.809 1.00 30.97 ? 1770 GLY A C     1 
ATOM   2552  O  O     . GLY A 1 1770 ? 127.173 207.309 196.977 1.00 34.45 ? 1770 GLY A O     1 
ATOM   2553  N  N     . GLY A 1 1771 ? 126.116 207.442 194.997 1.00 26.85 ? 1771 GLY A N     1 
ATOM   2554  C  CA    . GLY A 1 1771 ? 124.979 206.673 195.470 1.00 29.71 ? 1771 GLY A CA    1 
ATOM   2555  C  C     . GLY A 1 1771 ? 125.262 205.198 195.650 1.00 33.83 ? 1771 GLY A C     1 
ATOM   2556  O  O     . GLY A 1 1771 ? 124.438 204.486 196.232 1.00 34.74 ? 1771 GLY A O     1 
ATOM   2557  N  N     . GLY A 1 1772 ? 126.408 204.723 195.168 1.00 31.66 ? 1772 GLY A N     1 
ATOM   2558  C  CA    . GLY A 1 1772 ? 126.761 203.324 195.301 1.00 26.99 ? 1772 GLY A CA    1 
ATOM   2559  C  C     . GLY A 1 1772 ? 126.155 202.455 194.219 1.00 29.59 ? 1772 GLY A C     1 
ATOM   2560  O  O     . GLY A 1 1772 ? 126.876 201.841 193.427 1.00 28.45 ? 1772 GLY A O     1 
ATOM   2561  N  N     . GLY A 1 1773 ? 124.823 202.399 194.176 1.00 28.66 ? 1773 GLY A N     1 
ATOM   2562  C  CA    . GLY A 1 1773 ? 124.141 201.608 193.167 1.00 29.05 ? 1773 GLY A CA    1 
ATOM   2563  C  C     . GLY A 1 1773 ? 124.094 202.264 191.804 1.00 32.40 ? 1773 GLY A C     1 
ATOM   2564  O  O     . GLY A 1 1773 ? 123.598 201.654 190.850 1.00 34.91 ? 1773 GLY A O     1 
ATOM   2565  N  N     . ASP A 1 1774 ? 124.589 203.495 191.689 1.00 32.76 ? 1774 ASP A N     1 
ATOM   2566  C  CA    . ASP A 1 1774 ? 124.613 204.178 190.403 1.00 31.61 ? 1774 ASP A CA    1 
ATOM   2567  C  C     . ASP A 1 1774 ? 125.533 203.448 189.434 1.00 32.34 ? 1774 ASP A C     1 
ATOM   2568  O  O     . ASP A 1 1774 ? 126.480 202.768 189.837 1.00 34.35 ? 1774 ASP A O     1 
ATOM   2569  C  CB    . ASP A 1 1774 ? 125.076 205.625 190.576 1.00 28.77 ? 1774 ASP A CB    1 
ATOM   2570  C  CG    . ASP A 1 1774 ? 124.067 206.477 191.320 1.00 32.36 ? 1774 ASP A CG    1 
ATOM   2571  O  OD1   . ASP A 1 1774 ? 122.857 206.183 191.227 1.00 31.94 ? 1774 ASP A OD1   1 
ATOM   2572  O  OD2   . ASP A 1 1774 ? 124.484 207.439 191.997 1.00 33.75 ? 1774 ASP A OD2   1 
ATOM   2573  N  N     . ALA A 1 1775 ? 125.240 203.589 188.142 1.00 35.06 ? 1775 ALA A N     1 
ATOM   2574  C  CA    . ALA A 1 1775 ? 126.073 202.973 187.122 1.00 31.24 ? 1775 ALA A CA    1 
ATOM   2575  C  C     . ALA A 1 1775 ? 127.500 203.496 187.222 1.00 29.71 ? 1775 ALA A C     1 
ATOM   2576  O  O     . ALA A 1 1775 ? 127.743 204.626 187.652 1.00 28.77 ? 1775 ALA A O     1 
ATOM   2577  C  CB    . ALA A 1 1775 ? 125.506 203.248 185.729 1.00 18.84 ? 1775 ALA A CB    1 
ATOM   2578  N  N     . ALA A 1 1776 ? 128.452 202.654 186.825 1.00 25.64 ? 1776 ALA A N     1 
ATOM   2579  C  CA    . ALA A 1 1776 ? 129.863 202.988 186.957 1.00 22.88 ? 1776 ALA A CA    1 
ATOM   2580  C  C     . ALA A 1 1776 ? 130.367 203.616 185.664 1.00 24.85 ? 1776 ALA A C     1 
ATOM   2581  O  O     . ALA A 1 1776 ? 130.443 202.919 184.640 1.00 17.50 ? 1776 ALA A O     1 
ATOM   2582  C  CB    . ALA A 1 1776 ? 130.676 201.748 187.296 1.00 10.48 ? 1776 ALA A CB    1 
ATOM   2583  N  N     . PRO A 1 1777 ? 130.715 204.906 185.654 1.00 25.88 ? 1777 PRO A N     1 
ATOM   2584  C  CA    . PRO A 1 1777 ? 131.431 205.477 184.509 1.00 22.25 ? 1777 PRO A CA    1 
ATOM   2585  C  C     . PRO A 1 1777 ? 132.933 205.261 184.564 1.00 17.80 ? 1777 PRO A C     1 
ATOM   2586  O  O     . PRO A 1 1777 ? 133.653 205.825 183.732 1.00 19.08 ? 1777 PRO A O     1 
ATOM   2587  C  CB    . PRO A 1 1777 ? 131.086 206.973 184.594 1.00 21.51 ? 1777 PRO A CB    1 
ATOM   2588  C  CG    . PRO A 1 1777 ? 130.651 207.213 186.006 1.00 21.51 ? 1777 PRO A CG    1 
ATOM   2589  C  CD    . PRO A 1 1777 ? 130.479 205.899 186.712 1.00 24.16 ? 1777 PRO A CD    1 
ATOM   2590  N  N     . LEU A 1 1778 ? 133.422 204.479 185.530 1.00 14.87 ? 1778 LEU A N     1 
ATOM   2591  C  CA    . LEU A 1 1778 ? 134.832 204.107 185.549 1.00 10.55 ? 1778 LEU A CA    1 
ATOM   2592  C  C     . LEU A 1 1778 ? 135.210 203.303 184.316 1.00 12.93 ? 1778 LEU A C     1 
ATOM   2593  O  O     . LEU A 1 1778 ? 136.365 203.348 183.875 1.00 14.00 ? 1778 LEU A O     1 
ATOM   2594  C  CB    . LEU A 1 1778 ? 135.151 203.304 186.808 1.00 11.85 ? 1778 LEU A CB    1 
ATOM   2595  C  CG    . LEU A 1 1778 ? 135.791 204.020 187.992 1.00 10.67 ? 1778 LEU A CG    1 
ATOM   2596  C  CD1   . LEU A 1 1778 ? 136.152 203.002 189.059 1.00 11.41 ? 1778 LEU A CD1   1 
ATOM   2597  C  CD2   . LEU A 1 1778 ? 137.018 204.795 187.552 1.00 7.15  ? 1778 LEU A CD2   1 
ATOM   2598  N  N     . HIS A 1 1779 ? 134.257 202.558 183.754 1.00 11.80 ? 1779 HIS A N     1 
ATOM   2599  C  CA    . HIS A 1 1779 ? 134.531 201.791 182.546 1.00 10.52 ? 1779 HIS A CA    1 
ATOM   2600  C  C     . HIS A 1 1779 ? 134.888 202.710 181.386 1.00 9.40  ? 1779 HIS A C     1 
ATOM   2601  O  O     . HIS A 1 1779 ? 135.719 202.359 180.539 1.00 8.86  ? 1779 HIS A O     1 
ATOM   2602  C  CB    . HIS A 1 1779 ? 133.327 200.916 182.201 1.00 15.84 ? 1779 HIS A CB    1 
ATOM   2603  C  CG    . HIS A 1 1779 ? 133.197 199.702 183.067 1.00 18.31 ? 1779 HIS A CG    1 
ATOM   2604  N  ND1   . HIS A 1 1779 ? 132.333 199.641 184.138 1.00 15.35 ? 1779 HIS A ND1   1 
ATOM   2605  C  CD2   . HIS A 1 1779 ? 133.830 198.505 183.026 1.00 17.66 ? 1779 HIS A CD2   1 
ATOM   2606  C  CE1   . HIS A 1 1779 ? 132.436 198.459 184.718 1.00 15.02 ? 1779 HIS A CE1   1 
ATOM   2607  N  NE2   . HIS A 1 1779 ? 133.336 197.750 184.062 1.00 19.76 ? 1779 HIS A NE2   1 
ATOM   2608  N  N     . SER A 1 1780 ? 134.270 203.891 181.329 1.00 11.95 ? 1780 SER A N     1 
ATOM   2609  C  CA    . SER A 1 1780 ? 134.643 204.873 180.315 1.00 12.29 ? 1780 SER A CA    1 
ATOM   2610  C  C     . SER A 1 1780 ? 136.067 205.374 180.527 1.00 9.91  ? 1780 SER A C     1 
ATOM   2611  O  O     . SER A 1 1780 ? 136.800 205.604 179.559 1.00 12.35 ? 1780 SER A O     1 
ATOM   2612  C  CB    . SER A 1 1780 ? 133.654 206.036 180.322 1.00 8.27  ? 1780 SER A CB    1 
ATOM   2613  O  OG    . SER A 1 1780 ? 132.359 205.597 179.954 1.00 15.65 ? 1780 SER A OG    1 
ATOM   2614  N  N     . VAL A 1 1781 ? 136.472 205.561 181.786 1.00 7.48  ? 1781 VAL A N     1 
ATOM   2615  C  CA    . VAL A 1 1781 ? 137.855 205.932 182.072 1.00 7.66  ? 1781 VAL A CA    1 
ATOM   2616  C  C     . VAL A 1 1781 ? 138.799 204.846 181.579 1.00 8.76  ? 1781 VAL A C     1 
ATOM   2617  O  O     . VAL A 1 1781 ? 139.822 205.129 180.943 1.00 12.45 ? 1781 VAL A O     1 
ATOM   2618  C  CB    . VAL A 1 1781 ? 138.042 206.205 183.576 1.00 8.46  ? 1781 VAL A CB    1 
ATOM   2619  C  CG1   . VAL A 1 1781 ? 139.521 206.337 183.916 1.00 4.93  ? 1781 VAL A CG1   1 
ATOM   2620  C  CG2   . VAL A 1 1781 ? 137.284 207.453 183.987 1.00 7.96  ? 1781 VAL A CG2   1 
ATOM   2621  N  N     . LEU A 1 1782 ? 138.467 203.584 181.857 1.00 8.39  ? 1782 LEU A N     1 
ATOM   2622  C  CA    . LEU A 1 1782 ? 139.223 202.476 181.288 1.00 5.07  ? 1782 LEU A CA    1 
ATOM   2623  C  C     . LEU A 1 1782 ? 139.128 202.475 179.768 1.00 8.81  ? 1782 LEU A C     1 
ATOM   2624  O  O     . LEU A 1 1782 ? 140.124 202.233 179.078 1.00 10.99 ? 1782 LEU A O     1 
ATOM   2625  C  CB    . LEU A 1 1782 ? 138.720 201.153 181.862 1.00 4.39  ? 1782 LEU A CB    1 
ATOM   2626  C  CG    . LEU A 1 1782 ? 139.442 199.880 181.422 1.00 8.75  ? 1782 LEU A CG    1 
ATOM   2627  C  CD1   . LEU A 1 1782 ? 140.923 199.951 181.761 1.00 4.29  ? 1782 LEU A CD1   1 
ATOM   2628  C  CD2   . LEU A 1 1782 ? 138.799 198.660 182.055 1.00 5.19  ? 1782 LEU A CD2   1 
ATOM   2629  N  N     . SER A 1 1783 ? 137.938 202.759 179.232 1.00 7.84  ? 1783 SER A N     1 
ATOM   2630  C  CA    . SER A 1 1783 ? 137.752 202.775 177.785 1.00 7.18  ? 1783 SER A CA    1 
ATOM   2631  C  C     . SER A 1 1783 ? 138.648 203.813 177.120 1.00 10.83 ? 1783 SER A C     1 
ATOM   2632  O  O     . SER A 1 1783 ? 139.252 203.543 176.075 1.00 11.93 ? 1783 SER A O     1 
ATOM   2633  C  CB    . SER A 1 1783 ? 136.284 203.046 177.451 1.00 10.93 ? 1783 SER A CB    1 
ATOM   2634  O  OG    . SER A 1 1783 ? 136.078 203.106 176.051 1.00 19.10 ? 1783 SER A OG    1 
ATOM   2635  N  N     . ASN A 1 1784 ? 138.739 205.009 177.705 1.00 12.67 ? 1784 ASN A N     1 
ATOM   2636  C  CA    . ASN A 1 1784 ? 139.603 206.041 177.143 1.00 8.07  ? 1784 ASN A CA    1 
ATOM   2637  C  C     . ASN A 1 1784 ? 141.064 205.614 177.174 1.00 6.67  ? 1784 ASN A C     1 
ATOM   2638  O  O     . ASN A 1 1784 ? 141.813 205.868 176.225 1.00 10.41 ? 1784 ASN A O     1 
ATOM   2639  C  CB    . ASN A 1 1784 ? 139.412 207.355 177.899 1.00 12.41 ? 1784 ASN A CB    1 
ATOM   2640  C  CG    . ASN A 1 1784 ? 140.163 208.507 177.263 1.00 16.13 ? 1784 ASN A CG    1 
ATOM   2641  O  OD1   . ASN A 1 1784 ? 141.137 209.011 177.820 1.00 16.09 ? 1784 ASN A OD1   1 
ATOM   2642  N  ND2   . ASN A 1 1784 ? 139.710 208.935 176.092 1.00 12.25 ? 1784 ASN A ND2   1 
ATOM   2643  N  N     . VAL A 1 1785 ? 141.488 204.970 178.262 1.00 8.78  ? 1785 VAL A N     1 
ATOM   2644  C  CA    . VAL A 1 1785 ? 142.866 204.497 178.359 1.00 7.52  ? 1785 VAL A CA    1 
ATOM   2645  C  C     . VAL A 1 1785 ? 143.133 203.403 177.329 1.00 9.17  ? 1785 VAL A C     1 
ATOM   2646  O  O     . VAL A 1 1785 ? 144.198 203.374 176.703 1.00 8.48  ? 1785 VAL A O     1 
ATOM   2647  C  CB    . VAL A 1 1785 ? 143.166 204.023 179.792 1.00 4.90  ? 1785 VAL A CB    1 
ATOM   2648  C  CG1   . VAL A 1 1785 ? 144.541 203.389 179.869 1.00 3.63  ? 1785 VAL A CG1   1 
ATOM   2649  C  CG2   . VAL A 1 1785 ? 143.066 205.189 180.762 1.00 3.89  ? 1785 VAL A CG2   1 
ATOM   2650  N  N     . GLU A 1 1786 ? 142.176 202.490 177.135 1.00 8.69  ? 1786 GLU A N     1 
ATOM   2651  C  CA    . GLU A 1 1786 ? 142.334 201.452 176.120 1.00 10.00 ? 1786 GLU A CA    1 
ATOM   2652  C  C     . GLU A 1 1786 ? 142.494 202.059 174.732 1.00 9.42  ? 1786 GLU A C     1 
ATOM   2653  O  O     . GLU A 1 1786 ? 143.374 201.654 173.963 1.00 10.04 ? 1786 GLU A O     1 
ATOM   2654  C  CB    . GLU A 1 1786 ? 141.137 200.500 176.140 1.00 12.51 ? 1786 GLU A CB    1 
ATOM   2655  C  CG    . GLU A 1 1786 ? 140.939 199.739 177.430 1.00 12.34 ? 1786 GLU A CG    1 
ATOM   2656  C  CD    . GLU A 1 1786 ? 141.912 198.596 177.574 1.00 17.86 ? 1786 GLU A CD    1 
ATOM   2657  O  OE1   . GLU A 1 1786 ? 141.714 197.554 176.912 1.00 24.63 ? 1786 GLU A OE1   1 
ATOM   2658  O  OE2   . GLU A 1 1786 ? 142.879 198.739 178.344 1.00 19.94 ? 1786 GLU A OE2   1 
ATOM   2659  N  N     . VAL A 1 1787 ? 141.649 203.034 174.394 1.00 8.09  ? 1787 VAL A N     1 
ATOM   2660  C  CA    . VAL A 1 1787 ? 141.700 203.640 173.068 1.00 8.56  ? 1787 VAL A CA    1 
ATOM   2661  C  C     . VAL A 1 1787 ? 143.017 204.382 172.875 1.00 7.69  ? 1787 VAL A C     1 
ATOM   2662  O  O     . VAL A 1 1787 ? 143.682 204.244 171.841 1.00 9.68  ? 1787 VAL A O     1 
ATOM   2663  C  CB    . VAL A 1 1787 ? 140.492 204.571 172.858 1.00 7.88  ? 1787 VAL A CB    1 
ATOM   2664  C  CG1   . VAL A 1 1787 ? 140.760 205.554 171.727 1.00 12.36 ? 1787 VAL A CG1   1 
ATOM   2665  C  CG2   . VAL A 1 1787 ? 139.238 203.761 172.586 1.00 10.99 ? 1787 VAL A CG2   1 
ATOM   2666  N  N     . THR A 1 1788 ? 143.419 205.168 173.874 1.00 5.68  ? 1788 THR A N     1 
ATOM   2667  C  CA    . THR A 1 1788 ? 144.647 205.945 173.759 1.00 6.05  ? 1788 THR A CA    1 
ATOM   2668  C  C     . THR A 1 1788 ? 145.861 205.029 173.675 1.00 6.37  ? 1788 THR A C     1 
ATOM   2669  O  O     . THR A 1 1788 ? 146.806 205.302 172.926 1.00 7.49  ? 1788 THR A O     1 
ATOM   2670  C  CB    . THR A 1 1788 ? 144.776 206.895 174.949 1.00 4.91  ? 1788 THR A CB    1 
ATOM   2671  O  OG1   . THR A 1 1788 ? 143.650 207.776 174.976 1.00 10.17 ? 1788 THR A OG1   1 
ATOM   2672  C  CG2   . THR A 1 1788 ? 146.022 207.745 174.805 1.00 5.16  ? 1788 THR A CG2   1 
ATOM   2673  N  N     . LEU A 1 1789 ? 145.848 203.932 174.433 1.00 7.87  ? 1789 LEU A N     1 
ATOM   2674  C  CA    . LEU A 1 1789 ? 146.982 203.016 174.439 1.00 5.42  ? 1789 LEU A CA    1 
ATOM   2675  C  C     . LEU A 1 1789 ? 147.094 202.271 173.114 1.00 6.15  ? 1789 LEU A C     1 
ATOM   2676  O  O     . LEU A 1 1789 ? 148.199 201.926 172.679 1.00 12.34 ? 1789 LEU A O     1 
ATOM   2677  C  CB    . LEU A 1 1789 ? 146.848 202.045 175.612 1.00 4.71  ? 1789 LEU A CB    1 
ATOM   2678  C  CG    . LEU A 1 1789 ? 147.954 201.027 175.875 1.00 10.58 ? 1789 LEU A CG    1 
ATOM   2679  C  CD1   . LEU A 1 1789 ? 149.248 201.748 176.205 1.00 3.22  ? 1789 LEU A CD1   1 
ATOM   2680  C  CD2   . LEU A 1 1789 ? 147.550 200.105 177.011 1.00 11.13 ? 1789 LEU A CD2   1 
ATOM   2681  N  N     . ASN A 1 1790 ? 145.960 202.009 172.456 1.00 8.19  ? 1790 ASN A N     1 
ATOM   2682  C  CA    . ASN A 1 1790 ? 145.999 201.372 171.141 1.00 6.82  ? 1790 ASN A CA    1 
ATOM   2683  C  C     . ASN A 1 1790 ? 146.654 202.276 170.104 1.00 9.00  ? 1790 ASN A C     1 
ATOM   2684  O  O     . ASN A 1 1790 ? 147.416 201.801 169.254 1.00 12.22 ? 1790 ASN A O     1 
ATOM   2685  C  CB    . ASN A 1 1790 ? 144.590 200.980 170.699 1.00 9.08  ? 1790 ASN A CB    1 
ATOM   2686  C  CG    . ASN A 1 1790 ? 144.053 199.782 171.458 1.00 15.43 ? 1790 ASN A CG    1 
ATOM   2687  O  OD1   . ASN A 1 1790 ? 144.792 198.849 171.769 1.00 15.45 ? 1790 ASN A OD1   1 
ATOM   2688  N  ND2   . ASN A 1 1790 ? 142.760 199.804 171.762 1.00 15.76 ? 1790 ASN A ND2   1 
ATOM   2689  N  N     . VAL A 1 1791 ? 146.362 203.577 170.151 1.00 7.09  ? 1791 VAL A N     1 
ATOM   2690  C  CA    . VAL A 1 1791 ? 147.011 204.519 169.243 1.00 7.92  ? 1791 VAL A CA    1 
ATOM   2691  C  C     . VAL A 1 1791 ? 148.506 204.588 169.527 1.00 9.05  ? 1791 VAL A C     1 
ATOM   2692  O  O     . VAL A 1 1791 ? 149.327 204.615 168.601 1.00 9.79  ? 1791 VAL A O     1 
ATOM   2693  C  CB    . VAL A 1 1791 ? 146.346 205.903 169.346 1.00 7.99  ? 1791 VAL A CB    1 
ATOM   2694  C  CG1   . VAL A 1 1791 ? 147.102 206.920 168.512 1.00 8.22  ? 1791 VAL A CG1   1 
ATOM   2695  C  CG2   . VAL A 1 1791 ? 144.899 205.827 168.906 1.00 9.48  ? 1791 VAL A CG2   1 
ATOM   2696  N  N     . LEU A 1 1792 ? 148.883 204.626 170.807 1.00 7.13  ? 1792 LEU A N     1 
ATOM   2697  C  CA    . LEU A 1 1792 ? 150.299 204.635 171.160 1.00 6.49  ? 1792 LEU A CA    1 
ATOM   2698  C  C     . LEU A 1 1792 ? 150.988 203.357 170.701 1.00 6.90  ? 1792 LEU A C     1 
ATOM   2699  O  O     . LEU A 1 1792 ? 152.104 203.400 170.171 1.00 6.51  ? 1792 LEU A O     1 
ATOM   2700  C  CB    . LEU A 1 1792 ? 150.460 204.817 172.668 1.00 5.35  ? 1792 LEU A CB    1 
ATOM   2701  C  CG    . LEU A 1 1792 ? 150.030 206.160 173.255 1.00 4.54  ? 1792 LEU A CG    1 
ATOM   2702  C  CD1   . LEU A 1 1792 ? 150.014 206.091 174.772 1.00 5.27  ? 1792 LEU A CD1   1 
ATOM   2703  C  CD2   . LEU A 1 1792 ? 150.949 207.264 172.779 1.00 3.55  ? 1792 LEU A CD2   1 
ATOM   2704  N  N     . ALA A 1 1793 ? 150.334 202.210 170.897 1.00 9.29  ? 1793 ALA A N     1 
ATOM   2705  C  CA    . ALA A 1 1793 ? 150.913 200.943 170.460 1.00 7.06  ? 1793 ALA A CA    1 
ATOM   2706  C  C     . ALA A 1 1793 ? 151.043 200.890 168.944 1.00 10.20 ? 1793 ALA A C     1 
ATOM   2707  O  O     . ALA A 1 1793 ? 152.024 200.355 168.417 1.00 13.31 ? 1793 ALA A O     1 
ATOM   2708  C  CB    . ALA A 1 1793 ? 150.068 199.777 170.970 1.00 8.94  ? 1793 ALA A CB    1 
ATOM   2709  N  N     . ASP A 1 1794 ? 150.057 201.432 168.224 1.00 10.20 ? 1794 ASP A N     1 
ATOM   2710  C  CA    . ASP A 1 1794 ? 150.144 201.476 166.768 1.00 9.32  ? 1794 ASP A CA    1 
ATOM   2711  C  C     . ASP A 1 1794 ? 151.280 202.380 166.306 1.00 11.24 ? 1794 ASP A C     1 
ATOM   2712  O  O     . ASP A 1 1794 ? 151.954 202.080 165.313 1.00 15.83 ? 1794 ASP A O     1 
ATOM   2713  C  CB    . ASP A 1 1794 ? 148.815 201.941 166.174 1.00 11.93 ? 1794 ASP A CB    1 
ATOM   2714  C  CG    . ASP A 1 1794 ? 147.843 200.799 165.960 1.00 27.37 ? 1794 ASP A CG    1 
ATOM   2715  O  OD1   . ASP A 1 1794 ? 148.208 199.643 166.262 1.00 27.98 ? 1794 ASP A OD1   1 
ATOM   2716  O  OD2   . ASP A 1 1794 ? 146.717 201.054 165.487 1.00 36.78 ? 1794 ASP A OD2   1 
ATOM   2717  N  N     . SER A 1 1795 ? 151.502 203.494 167.006 1.00 12.77 ? 1795 SER A N     1 
ATOM   2718  C  CA    . SER A 1 1795 ? 152.544 204.431 166.600 1.00 7.04  ? 1795 SER A CA    1 
ATOM   2719  C  C     . SER A 1 1795 ? 153.932 203.810 166.709 1.00 9.16  ? 1795 SER A C     1 
ATOM   2720  O  O     . SER A 1 1795 ? 154.790 204.038 165.848 1.00 13.57 ? 1795 SER A O     1 
ATOM   2721  C  CB    . SER A 1 1795 ? 152.458 205.707 167.436 1.00 6.40  ? 1795 SER A CB    1 
ATOM   2722  O  OG    . SER A 1 1795 ? 151.203 206.340 167.269 1.00 6.97  ? 1795 SER A OG    1 
ATOM   2723  N  N     . VAL A 1 1796 ? 154.175 203.023 167.762 1.00 6.87  ? 1796 VAL A N     1 
ATOM   2724  C  CA    . VAL A 1 1796 ? 155.494 202.421 167.953 1.00 8.42  ? 1796 VAL A CA    1 
ATOM   2725  C  C     . VAL A 1 1796 ? 155.697 201.172 167.112 1.00 11.49 ? 1796 VAL A C     1 
ATOM   2726  O  O     . VAL A 1 1796 ? 156.808 200.626 167.093 1.00 11.10 ? 1796 VAL A O     1 
ATOM   2727  C  CB    . VAL A 1 1796 ? 155.748 202.088 169.439 1.00 7.18  ? 1796 VAL A CB    1 
ATOM   2728  C  CG1   . VAL A 1 1796 ? 155.698 203.353 170.278 1.00 6.80  ? 1796 VAL A CG1   1 
ATOM   2729  C  CG2   . VAL A 1 1796 ? 154.752 201.065 169.941 1.00 7.10  ? 1796 VAL A CG2   1 
ATOM   2730  N  N     . LEU A 1 1797 ? 154.664 200.701 166.413 1.00 11.56 ? 1797 LEU A N     1 
ATOM   2731  C  CA    . LEU A 1 1797 ? 154.828 199.589 165.485 1.00 12.29 ? 1797 LEU A CA    1 
ATOM   2732  C  C     . LEU A 1 1797 ? 155.491 200.014 164.183 1.00 13.60 ? 1797 LEU A C     1 
ATOM   2733  O  O     . LEU A 1 1797 ? 155.888 199.150 163.394 1.00 19.65 ? 1797 LEU A O     1 
ATOM   2734  C  CB    . LEU A 1 1797 ? 153.474 198.943 165.185 1.00 10.82 ? 1797 LEU A CB    1 
ATOM   2735  C  CG    . LEU A 1 1797 ? 152.834 198.120 166.303 1.00 13.89 ? 1797 LEU A CG    1 
ATOM   2736  C  CD1   . LEU A 1 1797 ? 151.421 197.703 165.926 1.00 14.02 ? 1797 LEU A CD1   1 
ATOM   2737  C  CD2   . LEU A 1 1797 ? 153.678 196.907 166.630 1.00 10.60 ? 1797 LEU A CD2   1 
ATOM   2738  N  N     . MET A 1 1798 ? 155.619 201.312 163.946 1.00 9.56  ? 1798 MET A N     1 
ATOM   2739  C  CA    . MET A 1 1798 ? 156.223 201.866 162.745 1.00 13.28 ? 1798 MET A CA    1 
ATOM   2740  C  C     . MET A 1 1798 ? 157.373 202.792 163.134 1.00 17.10 ? 1798 MET A C     1 
ATOM   2741  O  O     . MET A 1 1798 ? 157.598 203.082 164.310 1.00 18.54 ? 1798 MET A O     1 
ATOM   2742  C  CB    . MET A 1 1798 ? 155.171 202.593 161.906 1.00 16.62 ? 1798 MET A CB    1 
ATOM   2743  C  CG    . MET A 1 1798 ? 154.587 203.823 162.575 1.00 15.56 ? 1798 MET A CG    1 
ATOM   2744  S  SD    . MET A 1 1798 ? 153.314 204.618 161.580 1.00 45.47 ? 1798 MET A SD    1 
ATOM   2745  C  CE    . MET A 1 1798 ? 152.847 205.977 162.649 1.00 19.16 ? 1798 MET A CE    1 
ATOM   2746  N  N     . GLU A 1 1799 ? 158.112 203.248 162.125 1.00 16.65 ? 1799 GLU A N     1 
ATOM   2747  C  CA    . GLU A 1 1799 ? 159.267 204.100 162.372 1.00 15.09 ? 1799 GLU A CA    1 
ATOM   2748  C  C     . GLU A 1 1799 ? 158.826 205.477 162.849 1.00 18.76 ? 1799 GLU A C     1 
ATOM   2749  O  O     . GLU A 1 1799 ? 157.845 206.040 162.356 1.00 17.67 ? 1799 GLU A O     1 
ATOM   2750  C  CB    . GLU A 1 1799 ? 160.116 204.225 161.107 1.00 17.27 ? 1799 GLU A CB    1 
ATOM   2751  C  CG    . GLU A 1 1799 ? 161.600 204.410 161.376 1.00 21.08 ? 1799 GLU A CG    1 
ATOM   2752  C  CD    . GLU A 1 1799 ? 162.359 204.878 160.152 1.00 31.32 ? 1799 GLU A CD    1 
ATOM   2753  O  OE1   . GLU A 1 1799 ? 161.722 205.090 159.100 1.00 33.21 ? 1799 GLU A OE1   1 
ATOM   2754  O  OE2   . GLU A 1 1799 ? 163.594 205.040 160.244 1.00 31.00 ? 1799 GLU A OE2   1 
ATOM   2755  N  N     . GLN A 1 1800 ? 159.552 206.012 163.821 1.00 18.46 ? 1800 GLN A N     1 
ATOM   2756  C  CA    . GLN A 1 1800 ? 159.255 207.302 164.421 1.00 13.34 ? 1800 GLN A CA    1 
ATOM   2757  C  C     . GLN A 1 1800 ? 160.556 208.055 164.641 1.00 9.35  ? 1800 GLN A C     1 
ATOM   2758  O  O     . GLN A 1 1800 ? 161.629 207.446 164.711 1.00 13.04 ? 1800 GLN A O     1 
ATOM   2759  C  CB    . GLN A 1 1800 ? 158.512 207.151 165.758 1.00 6.19  ? 1800 GLN A CB    1 
ATOM   2760  C  CG    . GLN A 1 1800 ? 157.182 206.421 165.675 1.00 7.26  ? 1800 GLN A CG    1 
ATOM   2761  C  CD    . GLN A 1 1800 ? 156.048 207.311 165.204 1.00 10.95 ? 1800 GLN A CD    1 
ATOM   2762  O  OE1   . GLN A 1 1800 ? 156.260 208.461 164.824 1.00 12.66 ? 1800 GLN A OE1   1 
ATOM   2763  N  NE2   . GLN A 1 1800 ? 154.833 206.780 165.228 1.00 8.50  ? 1800 GLN A NE2   1 
ATOM   2764  N  N     . PRO A 1 1801 ? 160.496 209.382 164.740 1.00 7.87  ? 1801 PRO A N     1 
ATOM   2765  C  CA    . PRO A 1 1801 ? 161.684 210.136 165.127 1.00 6.11  ? 1801 PRO A CA    1 
ATOM   2766  C  C     . PRO A 1 1801 ? 162.161 209.707 166.498 1.00 7.83  ? 1801 PRO A C     1 
ATOM   2767  O  O     . PRO A 1 1801 ? 161.354 209.320 167.365 1.00 9.68  ? 1801 PRO A O     1 
ATOM   2768  C  CB    . PRO A 1 1801 ? 161.193 211.589 165.130 1.00 8.23  ? 1801 PRO A CB    1 
ATOM   2769  C  CG    . PRO A 1 1801 ? 160.047 211.599 164.187 1.00 8.98  ? 1801 PRO A CG    1 
ATOM   2770  C  CD    . PRO A 1 1801 ? 159.388 210.261 164.328 1.00 8.36  ? 1801 PRO A CD    1 
ATOM   2771  N  N     . PRO A 1 1802 ? 163.476 209.743 166.741 1.00 9.92  ? 1802 PRO A N     1 
ATOM   2772  C  CA    . PRO A 1 1802 ? 164.001 209.218 168.015 1.00 7.14  ? 1802 PRO A CA    1 
ATOM   2773  C  C     . PRO A 1 1802 ? 163.439 209.905 169.247 1.00 7.93  ? 1802 PRO A C     1 
ATOM   2774  O  O     . PRO A 1 1802 ? 163.214 209.242 170.266 1.00 7.70  ? 1802 PRO A O     1 
ATOM   2775  C  CB    . PRO A 1 1802 ? 165.515 209.437 167.880 1.00 4.10  ? 1802 PRO A CB    1 
ATOM   2776  C  CG    . PRO A 1 1802 ? 165.756 209.524 166.409 1.00 7.22  ? 1802 PRO A CG    1 
ATOM   2777  C  CD    . PRO A 1 1802 ? 164.553 210.220 165.858 1.00 8.68  ? 1802 PRO A CD    1 
ATOM   2778  N  N     . LEU A 1 1803 ? 163.208 211.217 169.190 1.00 7.70  ? 1803 LEU A N     1 
ATOM   2779  C  CA    . LEU A 1 1803 ? 162.633 211.905 170.341 1.00 4.47  ? 1803 LEU A CA    1 
ATOM   2780  C  C     . LEU A 1 1803 ? 161.166 211.540 170.525 1.00 6.48  ? 1803 LEU A C     1 
ATOM   2781  O  O     . LEU A 1 1803 ? 160.718 211.297 171.651 1.00 6.66  ? 1803 LEU A O     1 
ATOM   2782  C  CB    . LEU A 1 1803 ? 162.795 213.416 170.190 1.00 5.03  ? 1803 LEU A CB    1 
ATOM   2783  C  CG    . LEU A 1 1803 ? 162.223 214.260 171.330 1.00 4.14  ? 1803 LEU A CG    1 
ATOM   2784  C  CD1   . LEU A 1 1803 ? 163.049 214.083 172.592 1.00 5.42  ? 1803 LEU A CD1   1 
ATOM   2785  C  CD2   . LEU A 1 1803 ? 162.144 215.725 170.937 1.00 5.94  ? 1803 LEU A CD2   1 
ATOM   2786  N  N     . ARG A 1 1804 ? 160.402 211.495 169.430 1.00 4.83  ? 1804 ARG A N     1 
ATOM   2787  C  CA    . ARG A 1 1804 ? 158.993 211.133 169.529 1.00 5.42  ? 1804 ARG A CA    1 
ATOM   2788  C  C     . ARG A 1 1804 ? 158.821 209.684 169.967 1.00 4.98  ? 1804 ARG A C     1 
ATOM   2789  O  O     . ARG A 1 1804 ? 157.928 209.374 170.765 1.00 5.51  ? 1804 ARG A O     1 
ATOM   2790  C  CB    . ARG A 1 1804 ? 158.289 211.375 168.196 1.00 6.50  ? 1804 ARG A CB    1 
ATOM   2791  C  CG    . ARG A 1 1804 ? 156.799 211.093 168.239 1.00 5.32  ? 1804 ARG A CG    1 
ATOM   2792  C  CD    . ARG A 1 1804 ? 156.231 210.885 166.854 1.00 8.25  ? 1804 ARG A CD    1 
ATOM   2793  N  NE    . ARG A 1 1804 ? 156.272 212.099 166.047 1.00 9.28  ? 1804 ARG A NE    1 
ATOM   2794  C  CZ    . ARG A 1 1804 ? 155.960 212.146 164.759 1.00 7.97  ? 1804 ARG A CZ    1 
ATOM   2795  N  NH1   . ARG A 1 1804 ? 155.609 211.058 164.094 1.00 10.18 ? 1804 ARG A NH1   1 
ATOM   2796  N  NH2   . ARG A 1 1804 ? 155.999 213.313 164.126 1.00 12.05 ? 1804 ARG A NH2   1 
ATOM   2797  N  N     . ARG A 1 1805 ? 159.670 208.786 169.461 1.00 4.98  ? 1805 ARG A N     1 
ATOM   2798  C  CA    . ARG A 1 1805 ? 159.568 207.379 169.834 1.00 3.59  ? 1805 ARG A CA    1 
ATOM   2799  C  C     . ARG A 1 1805 ? 159.760 207.192 171.332 1.00 5.69  ? 1805 ARG A C     1 
ATOM   2800  O  O     . ARG A 1 1805 ? 159.042 206.410 171.966 1.00 8.79  ? 1805 ARG A O     1 
ATOM   2801  C  CB    . ARG A 1 1805 ? 160.596 206.555 169.058 1.00 7.31  ? 1805 ARG A CB    1 
ATOM   2802  C  CG    . ARG A 1 1805 ? 160.501 205.063 169.313 1.00 6.51  ? 1805 ARG A CG    1 
ATOM   2803  C  CD    . ARG A 1 1805 ? 161.839 204.377 169.125 1.00 8.33  ? 1805 ARG A CD    1 
ATOM   2804  N  NE    . ARG A 1 1805 ? 162.706 204.544 170.284 1.00 15.89 ? 1805 ARG A NE    1 
ATOM   2805  C  CZ    . ARG A 1 1805 ? 163.962 204.963 170.227 1.00 15.22 ? 1805 ARG A CZ    1 
ATOM   2806  N  NH1   . ARG A 1 1805 ? 164.542 205.260 169.075 1.00 10.75 ? 1805 ARG A NH1   1 
ATOM   2807  N  NH2   . ARG A 1 1805 ? 164.658 205.083 171.353 1.00 13.50 ? 1805 ARG A NH2   1 
ATOM   2808  N  N     . ARG A 1 1806 ? 160.733 207.893 171.914 1.00 4.95  ? 1806 ARG A N     1 
ATOM   2809  C  CA    . ARG A 1 1806 ? 160.926 207.812 173.356 1.00 5.47  ? 1806 ARG A CA    1 
ATOM   2810  C  C     . ARG A 1 1806 ? 159.745 208.413 174.110 1.00 3.31  ? 1806 ARG A C     1 
ATOM   2811  O  O     . ARG A 1 1806 ? 159.297 207.835 175.104 1.00 3.38  ? 1806 ARG A O     1 
ATOM   2812  C  CB    . ARG A 1 1806 ? 162.248 208.478 173.739 1.00 7.90  ? 1806 ARG A CB    1 
ATOM   2813  C  CG    . ARG A 1 1806 ? 163.439 207.756 173.123 1.00 6.29  ? 1806 ARG A CG    1 
ATOM   2814  C  CD    . ARG A 1 1806 ? 164.784 208.324 173.530 1.00 8.28  ? 1806 ARG A CD    1 
ATOM   2815  N  NE    . ARG A 1 1806 ? 165.110 208.054 174.924 1.00 16.56 ? 1806 ARG A NE    1 
ATOM   2816  C  CZ    . ARG A 1 1806 ? 165.668 208.936 175.743 1.00 14.10 ? 1806 ARG A CZ    1 
ATOM   2817  N  NH1   . ARG A 1 1806 ? 165.996 210.150 175.332 1.00 14.28 ? 1806 ARG A NH1   1 
ATOM   2818  N  NH2   . ARG A 1 1806 ? 165.913 208.587 177.003 1.00 7.76  ? 1806 ARG A NH2   1 
ATOM   2819  N  N     . LYS A 1 1807 ? 159.203 209.537 173.633 1.00 4.25  ? 1807 LYS A N     1 
ATOM   2820  C  CA    . LYS A 1 1807 ? 157.989 210.087 174.230 1.00 2.22  ? 1807 LYS A CA    1 
ATOM   2821  C  C     . LYS A 1 1807 ? 156.850 209.078 174.195 1.00 2.45  ? 1807 LYS A C     1 
ATOM   2822  O  O     . LYS A 1 1807 ? 156.105 208.935 175.171 1.00 2.44  ? 1807 LYS A O     1 
ATOM   2823  C  CB    . LYS A 1 1807 ? 157.568 211.364 173.507 1.00 1.97  ? 1807 LYS A CB    1 
ATOM   2824  C  CG    . LYS A 1 1807 ? 158.354 212.604 173.856 1.00 1.23  ? 1807 LYS A CG    1 
ATOM   2825  C  CD    . LYS A 1 1807 ? 157.861 213.770 173.021 1.00 1.80  ? 1807 LYS A CD    1 
ATOM   2826  C  CE    . LYS A 1 1807 ? 158.532 215.068 173.405 1.00 3.79  ? 1807 LYS A CE    1 
ATOM   2827  N  NZ    . LYS A 1 1807 ? 158.143 216.162 172.476 1.00 4.51  ? 1807 LYS A NZ    1 
ATOM   2828  N  N     . LEU A 1 1808 ? 156.691 208.380 173.069 1.00 5.73  ? 1808 LEU A N     1 
ATOM   2829  C  CA    . LEU A 1 1808 ? 155.660 207.356 172.968 1.00 2.31  ? 1808 LEU A CA    1 
ATOM   2830  C  C     . LEU A 1 1808 ? 155.924 206.212 173.940 1.00 2.56  ? 1808 LEU A C     1 
ATOM   2831  O  O     . LEU A 1 1808 ? 154.985 205.643 174.507 1.00 3.25  ? 1808 LEU A O     1 
ATOM   2832  C  CB    . LEU A 1 1808 ? 155.579 206.840 171.533 1.00 3.41  ? 1808 LEU A CB    1 
ATOM   2833  C  CG    . LEU A 1 1808 ? 155.143 207.847 170.468 1.00 3.34  ? 1808 LEU A CG    1 
ATOM   2834  C  CD1   . LEU A 1 1808 ? 155.661 207.436 169.098 1.00 2.19  ? 1808 LEU A CD1   1 
ATOM   2835  C  CD2   . LEU A 1 1808 ? 153.635 207.992 170.449 1.00 6.37  ? 1808 LEU A CD2   1 
ATOM   2836  N  N     . GLU A 1 1809 ? 157.194 205.856 174.137 1.00 3.05  ? 1809 GLU A N     1 
ATOM   2837  C  CA    . GLU A 1 1809 ? 157.526 204.813 175.102 1.00 3.11  ? 1809 GLU A CA    1 
ATOM   2838  C  C     . GLU A 1 1809 ? 157.178 205.244 176.521 1.00 2.25  ? 1809 GLU A C     1 
ATOM   2839  O  O     . GLU A 1 1809 ? 156.734 204.426 177.333 1.00 1.92  ? 1809 GLU A O     1 
ATOM   2840  C  CB    . GLU A 1 1809 ? 159.006 204.446 174.996 1.00 3.01  ? 1809 GLU A CB    1 
ATOM   2841  C  CG    . GLU A 1 1809 ? 159.349 203.613 173.777 1.00 6.73  ? 1809 GLU A CG    1 
ATOM   2842  C  CD    . GLU A 1 1809 ? 160.821 203.676 173.416 1.00 18.94 ? 1809 GLU A CD    1 
ATOM   2843  O  OE1   . GLU A 1 1809 ? 161.560 204.452 174.054 1.00 18.24 ? 1809 GLU A OE1   1 
ATOM   2844  O  OE2   . GLU A 1 1809 ? 161.239 202.946 172.494 1.00 16.97 ? 1809 GLU A OE2   1 
ATOM   2845  N  N     . HIS A 1 1810 ? 157.385 206.524 176.844 1.00 5.35  ? 1810 HIS A N     1 
ATOM   2846  C  CA    . HIS A 1 1810 ? 157.028 207.007 178.174 1.00 2.59  ? 1810 HIS A CA    1 
ATOM   2847  C  C     . HIS A 1 1810 ? 155.518 206.979 178.380 1.00 2.16  ? 1810 HIS A C     1 
ATOM   2848  O  O     . HIS A 1 1810 ? 155.037 206.621 179.460 1.00 2.70  ? 1810 HIS A O     1 
ATOM   2849  C  CB    . HIS A 1 1810 ? 157.563 208.421 178.400 1.00 2.91  ? 1810 HIS A CB    1 
ATOM   2850  C  CG    . HIS A 1 1810 ? 159.057 208.516 178.395 1.00 5.44  ? 1810 HIS A CG    1 
ATOM   2851  N  ND1   . HIS A 1 1810 ? 159.833 208.079 179.443 1.00 13.33 ? 1810 HIS A ND1   1 
ATOM   2852  C  CD2   . HIS A 1 1810 ? 159.910 209.075 177.507 1.00 12.89 ? 1810 HIS A CD2   1 
ATOM   2853  C  CE1   . HIS A 1 1810 ? 161.106 208.308 179.174 1.00 10.44 ? 1810 HIS A CE1   1 
ATOM   2854  N  NE2   . HIS A 1 1810 ? 161.179 208.915 178.006 1.00 11.52 ? 1810 HIS A NE2   1 
ATOM   2855  N  N     . LEU A 1 1811 ? 154.757 207.361 177.352 1.00 1.60  ? 1811 LEU A N     1 
ATOM   2856  C  CA    . LEU A 1 1811 ? 153.303 207.381 177.469 1.00 1.25  ? 1811 LEU A CA    1 
ATOM   2857  C  C     . LEU A 1 1811 ? 152.734 205.977 177.606 1.00 1.62  ? 1811 LEU A C     1 
ATOM   2858  O  O     . LEU A 1 1811 ? 151.786 205.759 178.370 1.00 3.19  ? 1811 LEU A O     1 
ATOM   2859  C  CB    . LEU A 1 1811 ? 152.693 208.089 176.262 1.00 1.34  ? 1811 LEU A CB    1 
ATOM   2860  C  CG    . LEU A 1 1811 ? 152.631 209.614 176.331 1.00 2.56  ? 1811 LEU A CG    1 
ATOM   2861  C  CD1   . LEU A 1 1811 ? 152.083 210.161 175.032 1.00 4.83  ? 1811 LEU A CD1   1 
ATOM   2862  C  CD2   . LEU A 1 1811 ? 151.785 210.068 177.507 1.00 1.68  ? 1811 LEU A CD2   1 
ATOM   2863  N  N     . ILE A 1 1812 ? 153.290 205.014 176.868 1.00 1.41  ? 1812 ILE A N     1 
ATOM   2864  C  CA    . ILE A 1 1812 ? 152.828 203.634 176.975 1.00 1.11  ? 1812 ILE A CA    1 
ATOM   2865  C  C     . ILE A 1 1812 ? 153.047 203.113 178.389 1.00 1.11  ? 1812 ILE A C     1 
ATOM   2866  O  O     . ILE A 1 1812 ? 152.168 202.469 178.973 1.00 1.25  ? 1812 ILE A O     1 
ATOM   2867  C  CB    . ILE A 1 1812 ? 153.530 202.752 175.927 1.00 1.64  ? 1812 ILE A CB    1 
ATOM   2868  C  CG1   . ILE A 1 1812 ? 152.947 203.006 174.537 1.00 2.70  ? 1812 ILE A CG1   1 
ATOM   2869  C  CG2   . ILE A 1 1812 ? 153.411 201.281 176.290 1.00 1.58  ? 1812 ILE A CG2   1 
ATOM   2870  C  CD1   . ILE A 1 1812 ? 153.724 202.354 173.417 1.00 2.56  ? 1812 ILE A CD1   1 
ATOM   2871  N  N     . THR A 1 1813 ? 154.217 203.397 178.965 1.00 1.18  ? 1813 THR A N     1 
ATOM   2872  C  CA    . THR A 1 1813 ? 154.502 202.952 180.324 1.00 0.96  ? 1813 THR A CA    1 
ATOM   2873  C  C     . THR A 1 1813 ? 153.548 203.591 181.326 1.00 1.12  ? 1813 THR A C     1 
ATOM   2874  O  O     . THR A 1 1813 ? 153.064 202.923 182.246 1.00 1.56  ? 1813 THR A O     1 
ATOM   2875  C  CB    . THR A 1 1813 ? 155.955 203.269 180.680 1.00 1.66  ? 1813 THR A CB    1 
ATOM   2876  O  OG1   . THR A 1 1813 ? 156.819 202.754 179.661 1.00 6.45  ? 1813 THR A OG1   1 
ATOM   2877  C  CG2   . THR A 1 1813 ? 156.333 202.643 182.012 1.00 1.09  ? 1813 THR A CG2   1 
ATOM   2878  N  N     . GLU A 1 1814 ? 153.263 204.884 181.160 1.00 1.65  ? 1814 GLU A N     1 
ATOM   2879  C  CA    . GLU A 1 1814 ? 152.340 205.566 182.059 1.00 1.53  ? 1814 GLU A CA    1 
ATOM   2880  C  C     . GLU A 1 1814 ? 150.924 205.015 181.934 1.00 1.66  ? 1814 GLU A C     1 
ATOM   2881  O  O     . GLU A 1 1814 ? 150.240 204.816 182.944 1.00 1.24  ? 1814 GLU A O     1 
ATOM   2882  C  CB    . GLU A 1 1814 ? 152.353 207.069 181.780 1.00 1.92  ? 1814 GLU A CB    1 
ATOM   2883  C  CG    . GLU A 1 1814 ? 151.533 207.889 182.761 1.00 1.84  ? 1814 GLU A CG    1 
ATOM   2884  C  CD    . GLU A 1 1814 ? 151.703 207.428 184.197 1.00 9.63  ? 1814 GLU A CD    1 
ATOM   2885  O  OE1   . GLU A 1 1814 ? 152.855 207.387 184.678 1.00 5.65  ? 1814 GLU A OE1   1 
ATOM   2886  O  OE2   . GLU A 1 1814 ? 150.685 207.109 184.844 1.00 15.45 ? 1814 GLU A OE2   1 
ATOM   2887  N  N     . LEU A 1 1815 ? 150.465 204.767 180.706 1.00 1.27  ? 1815 LEU A N     1 
ATOM   2888  C  CA    . LEU A 1 1815 ? 149.083 204.341 180.513 1.00 1.05  ? 1815 LEU A CA    1 
ATOM   2889  C  C     . LEU A 1 1815 ? 148.867 202.884 180.896 1.00 0.86  ? 1815 LEU A C     1 
ATOM   2890  O  O     . LEU A 1 1815 ? 147.766 202.521 181.325 1.00 0.96  ? 1815 LEU A O     1 
ATOM   2891  C  CB    . LEU A 1 1815 ? 148.652 204.578 179.070 1.00 0.98  ? 1815 LEU A CB    1 
ATOM   2892  C  CG    . LEU A 1 1815 ? 147.911 205.894 178.831 1.00 2.21  ? 1815 LEU A CG    1 
ATOM   2893  C  CD1   . LEU A 1 1815 ? 148.754 207.114 179.189 1.00 2.11  ? 1815 LEU A CD1   1 
ATOM   2894  C  CD2   . LEU A 1 1815 ? 147.449 205.957 177.402 1.00 3.02  ? 1815 LEU A CD2   1 
ATOM   2895  N  N     . VAL A 1 1816 ? 149.885 202.035 180.744 1.00 1.00  ? 1816 VAL A N     1 
ATOM   2896  C  CA    . VAL A 1 1816 ? 149.763 200.655 181.204 1.00 1.99  ? 1816 VAL A CA    1 
ATOM   2897  C  C     . VAL A 1 1816 ? 149.500 200.625 182.702 1.00 2.34  ? 1816 VAL A C     1 
ATOM   2898  O  O     . VAL A 1 1816 ? 148.687 199.830 183.191 1.00 3.57  ? 1816 VAL A O     1 
ATOM   2899  C  CB    . VAL A 1 1816 ? 151.019 199.849 180.819 1.00 1.98  ? 1816 VAL A CB    1 
ATOM   2900  C  CG1   . VAL A 1 1816 ? 151.125 198.583 181.650 1.00 3.54  ? 1816 VAL A CG1   1 
ATOM   2901  C  CG2   . VAL A 1 1816 ? 150.981 199.498 179.344 1.00 1.02  ? 1816 VAL A CG2   1 
ATOM   2902  N  N     . HIS A 1 1817 ? 150.169 201.501 183.453 1.00 1.14  ? 1817 HIS A N     1 
ATOM   2903  C  CA    . HIS A 1 1817 ? 149.896 201.608 184.881 1.00 0.78  ? 1817 HIS A CA    1 
ATOM   2904  C  C     . HIS A 1 1817 ? 148.498 202.155 185.145 1.00 0.97  ? 1817 HIS A C     1 
ATOM   2905  O  O     . HIS A 1 1817 ? 147.789 201.658 186.026 1.00 2.93  ? 1817 HIS A O     1 
ATOM   2906  C  CB    . HIS A 1 1817 ? 150.957 202.476 185.553 1.00 0.95  ? 1817 HIS A CB    1 
ATOM   2907  C  CG    . HIS A 1 1817 ? 150.684 202.745 186.998 1.00 0.96  ? 1817 HIS A CG    1 
ATOM   2908  N  ND1   . HIS A 1 1817 ? 150.830 201.784 187.974 1.00 1.27  ? 1817 HIS A ND1   1 
ATOM   2909  C  CD2   . HIS A 1 1817 ? 150.290 203.873 187.636 1.00 0.96  ? 1817 HIS A CD2   1 
ATOM   2910  C  CE1   . HIS A 1 1817 ? 150.527 202.304 189.149 1.00 1.81  ? 1817 HIS A CE1   1 
ATOM   2911  N  NE2   . HIS A 1 1817 ? 150.199 203.570 188.973 1.00 2.28  ? 1817 HIS A NE2   1 
ATOM   2912  N  N     . GLN A 1 1818 ? 148.082 203.181 184.397 1.00 1.09  ? 1818 GLN A N     1 
ATOM   2913  C  CA    . GLN A 1 1818 ? 146.736 203.719 184.570 1.00 0.66  ? 1818 GLN A CA    1 
ATOM   2914  C  C     . GLN A 1 1818 ? 145.682 202.681 184.212 1.00 1.57  ? 1818 GLN A C     1 
ATOM   2915  O  O     . GLN A 1 1818 ? 144.630 202.605 184.857 1.00 3.24  ? 1818 GLN A O     1 
ATOM   2916  C  CB    . GLN A 1 1818 ? 146.550 204.980 183.724 1.00 0.67  ? 1818 GLN A CB    1 
ATOM   2917  C  CG    . GLN A 1 1818 ? 147.419 206.150 184.136 1.00 1.39  ? 1818 GLN A CG    1 
ATOM   2918  C  CD    . GLN A 1 1818 ? 147.297 207.322 183.183 1.00 2.55  ? 1818 GLN A CD    1 
ATOM   2919  O  OE1   . GLN A 1 1818 ? 146.611 207.237 182.166 1.00 2.65  ? 1818 GLN A OE1   1 
ATOM   2920  N  NE2   . GLN A 1 1818 ? 147.958 208.424 183.509 1.00 1.89  ? 1818 GLN A NE2   1 
ATOM   2921  N  N     . ARG A 1 1819 ? 145.945 201.877 183.181 1.00 1.29  ? 1819 ARG A N     1 
ATOM   2922  C  CA    . ARG A 1 1819 ? 145.044 200.782 182.845 1.00 1.67  ? 1819 ARG A CA    1 
ATOM   2923  C  C     . ARG A 1 1819 ? 144.947 199.776 183.985 1.00 2.38  ? 1819 ARG A C     1 
ATOM   2924  O  O     . ARG A 1 1819 ? 143.855 199.296 184.308 1.00 2.08  ? 1819 ARG A O     1 
ATOM   2925  C  CB    . ARG A 1 1819 ? 145.519 200.096 181.566 1.00 4.06  ? 1819 ARG A CB    1 
ATOM   2926  C  CG    . ARG A 1 1819 ? 144.650 198.941 181.119 1.00 2.42  ? 1819 ARG A CG    1 
ATOM   2927  C  CD    . ARG A 1 1819 ? 145.343 198.132 180.048 1.00 2.98  ? 1819 ARG A CD    1 
ATOM   2928  N  NE    . ARG A 1 1819 ? 146.638 197.626 180.484 1.00 4.61  ? 1819 ARG A NE    1 
ATOM   2929  C  CZ    . ARG A 1 1819 ? 147.522 197.055 179.677 1.00 5.88  ? 1819 ARG A CZ    1 
ATOM   2930  N  NH1   . ARG A 1 1819 ? 147.286 196.919 178.382 1.00 3.55  ? 1819 ARG A NH1   1 
ATOM   2931  N  NH2   . ARG A 1 1819 ? 148.670 196.613 180.180 1.00 10.95 ? 1819 ARG A NH2   1 
ATOM   2932  N  N     . ASP A 1 1820 ? 146.083 199.445 184.602 1.00 3.03  ? 1820 ASP A N     1 
ATOM   2933  C  CA    . ASP A 1 1820 ? 146.084 198.479 185.695 1.00 1.86  ? 1820 ASP A CA    1 
ATOM   2934  C  C     . ASP A 1 1820 ? 145.379 199.031 186.928 1.00 3.14  ? 1820 ASP A C     1 
ATOM   2935  O  O     . ASP A 1 1820 ? 144.636 198.306 187.600 1.00 6.39  ? 1820 ASP A O     1 
ATOM   2936  C  CB    . ASP A 1 1820 ? 147.518 198.075 186.030 1.00 2.84  ? 1820 ASP A CB    1 
ATOM   2937  C  CG    . ASP A 1 1820 ? 148.096 197.098 185.025 1.00 18.99 ? 1820 ASP A CG    1 
ATOM   2938  O  OD1   . ASP A 1 1820 ? 147.317 196.537 184.225 1.00 14.57 ? 1820 ASP A OD1   1 
ATOM   2939  O  OD2   . ASP A 1 1820 ? 149.328 196.893 185.031 1.00 18.58 ? 1820 ASP A OD2   1 
ATOM   2940  N  N     . VAL A 1 1821 ? 145.605 200.306 187.247 1.00 2.17  ? 1821 VAL A N     1 
ATOM   2941  C  CA    . VAL A 1 1821 ? 144.956 200.909 188.406 1.00 3.15  ? 1821 VAL A CA    1 
ATOM   2942  C  C     . VAL A 1 1821 ? 143.451 201.005 188.188 1.00 2.36  ? 1821 VAL A C     1 
ATOM   2943  O  O     . VAL A 1 1821 ? 142.660 200.708 189.092 1.00 3.78  ? 1821 VAL A O     1 
ATOM   2944  C  CB    . VAL A 1 1821 ? 145.576 202.284 188.710 1.00 1.38  ? 1821 VAL A CB    1 
ATOM   2945  C  CG1   . VAL A 1 1821 ? 144.758 203.018 189.757 1.00 0.98  ? 1821 VAL A CG1   1 
ATOM   2946  C  CG2   . VAL A 1 1821 ? 147.011 202.122 189.172 1.00 0.83  ? 1821 VAL A CG2   1 
ATOM   2947  N  N     . THR A 1 1822 ? 143.030 201.418 186.992 1.00 1.85  ? 1822 THR A N     1 
ATOM   2948  C  CA    . THR A 1 1822 ? 141.605 201.536 186.710 1.00 2.75  ? 1822 THR A CA    1 
ATOM   2949  C  C     . THR A 1 1822 ? 140.928 200.171 186.740 1.00 4.43  ? 1822 THR A C     1 
ATOM   2950  O  O     . THR A 1 1822 ? 139.802 200.039 187.233 1.00 5.29  ? 1822 THR A O     1 
ATOM   2951  C  CB    . THR A 1 1822 ? 141.390 202.220 185.360 1.00 3.48  ? 1822 THR A CB    1 
ATOM   2952  O  OG1   . THR A 1 1822 ? 141.982 203.522 185.389 1.00 2.37  ? 1822 THR A OG1   1 
ATOM   2953  C  CG2   . THR A 1 1822 ? 139.906 202.374 185.076 1.00 3.59  ? 1822 THR A CG2   1 
ATOM   2954  N  N     . ARG A 1 1823 ? 141.602 199.142 186.220 1.00 4.29  ? 1823 ARG A N     1 
ATOM   2955  C  CA    . ARG A 1 1823 ? 141.065 197.788 186.299 1.00 3.32  ? 1823 ARG A CA    1 
ATOM   2956  C  C     . ARG A 1 1823 ? 140.931 197.333 187.747 1.00 4.90  ? 1823 ARG A C     1 
ATOM   2957  O  O     . ARG A 1 1823 ? 139.935 196.700 188.116 1.00 7.16  ? 1823 ARG A O     1 
ATOM   2958  C  CB    . ARG A 1 1823 ? 141.955 196.822 185.518 1.00 2.35  ? 1823 ARG A CB    1 
ATOM   2959  C  CG    . ARG A 1 1823 ? 141.658 196.757 184.035 1.00 2.35  ? 1823 ARG A CG    1 
ATOM   2960  C  CD    . ARG A 1 1823 ? 142.770 196.041 183.294 1.00 3.10  ? 1823 ARG A CD    1 
ATOM   2961  N  NE    . ARG A 1 1823 ? 142.461 195.866 181.882 1.00 4.73  ? 1823 ARG A NE    1 
ATOM   2962  C  CZ    . ARG A 1 1823 ? 143.320 195.420 180.977 1.00 6.95  ? 1823 ARG A CZ    1 
ATOM   2963  N  NH1   . ARG A 1 1823 ? 144.561 195.097 181.302 1.00 8.96  ? 1823 ARG A NH1   1 
ATOM   2964  N  NH2   . ARG A 1 1823 ? 142.926 195.296 179.713 1.00 7.45  ? 1823 ARG A NH2   1 
ATOM   2965  N  N     . SER A 1 1824 ? 141.926 197.645 188.578 1.00 3.47  ? 1824 SER A N     1 
ATOM   2966  C  CA    . SER A 1 1824 ? 141.847 197.303 189.994 1.00 4.42  ? 1824 SER A CA    1 
ATOM   2967  C  C     . SER A 1 1824 ? 140.697 198.037 190.674 1.00 7.58  ? 1824 SER A C     1 
ATOM   2968  O  O     . SER A 1 1824 ? 140.007 197.469 191.527 1.00 11.73 ? 1824 SER A O     1 
ATOM   2969  C  CB    . SER A 1 1824 ? 143.173 197.621 190.683 1.00 3.23  ? 1824 SER A CB    1 
ATOM   2970  O  OG    . SER A 1 1824 ? 143.120 197.327 192.065 1.00 9.74  ? 1824 SER A OG    1 
ATOM   2971  N  N     . LEU A 1 1825 ? 140.478 199.303 190.310 1.00 5.86  ? 1825 LEU A N     1 
ATOM   2972  C  CA    . LEU A 1 1825 ? 139.372 200.062 190.884 1.00 5.48  ? 1825 LEU A CA    1 
ATOM   2973  C  C     . LEU A 1 1825 ? 138.026 199.464 190.491 1.00 7.49  ? 1825 LEU A C     1 
ATOM   2974  O  O     . LEU A 1 1825 ? 137.105 199.396 191.312 1.00 14.42 ? 1825 LEU A O     1 
ATOM   2975  C  CB    . LEU A 1 1825 ? 139.457 201.524 190.445 1.00 6.90  ? 1825 LEU A CB    1 
ATOM   2976  C  CG    . LEU A 1 1825 ? 140.610 202.361 191.003 1.00 5.73  ? 1825 LEU A CG    1 
ATOM   2977  C  CD1   . LEU A 1 1825 ? 140.497 203.800 190.537 1.00 4.53  ? 1825 LEU A CD1   1 
ATOM   2978  C  CD2   . LEU A 1 1825 ? 140.661 202.289 192.520 1.00 4.29  ? 1825 LEU A CD2   1 
ATOM   2979  N  N     . ILE A 1 1826 ? 137.887 199.037 189.235 1.00 6.93  ? 1826 ILE A N     1 
ATOM   2980  C  CA    . ILE A 1 1826 ? 136.632 198.443 188.786 1.00 8.93  ? 1826 ILE A CA    1 
ATOM   2981  C  C     . ILE A 1 1826 ? 136.416 197.084 189.441 1.00 10.05 ? 1826 ILE A C     1 
ATOM   2982  O  O     . ILE A 1 1826 ? 135.302 196.754 189.863 1.00 14.34 ? 1826 ILE A O     1 
ATOM   2983  C  CB    . ILE A 1 1826 ? 136.610 198.344 187.249 1.00 5.49  ? 1826 ILE A CB    1 
ATOM   2984  C  CG1   . ILE A 1 1826 ? 136.638 199.739 186.626 1.00 8.76  ? 1826 ILE A CG1   1 
ATOM   2985  C  CG2   . ILE A 1 1826 ? 135.387 197.574 186.780 1.00 6.70  ? 1826 ILE A CG2   1 
ATOM   2986  C  CD1   . ILE A 1 1826 ? 136.809 199.734 185.122 1.00 8.85  ? 1826 ILE A CD1   1 
ATOM   2987  N  N     . LYS A 1 1827 ? 137.475 196.277 189.539 1.00 9.27  ? 1827 LYS A N     1 
ATOM   2988  C  CA    . LYS A 1 1827 ? 137.345 194.947 190.126 1.00 11.25 ? 1827 LYS A CA    1 
ATOM   2989  C  C     . LYS A 1 1827 ? 136.982 195.018 191.603 1.00 13.65 ? 1827 LYS A C     1 
ATOM   2990  O  O     . LYS A 1 1827 ? 136.288 194.133 192.116 1.00 26.04 ? 1827 LYS A O     1 
ATOM   2991  C  CB    . LYS A 1 1827 ? 138.644 194.164 189.927 1.00 11.68 ? 1827 LYS A CB    1 
ATOM   2992  C  CG    . LYS A 1 1827 ? 138.621 192.743 190.460 1.00 15.20 ? 1827 LYS A CG    1 
ATOM   2993  C  CD    . LYS A 1 1827 ? 139.959 192.058 190.242 1.00 19.01 ? 1827 LYS A CD    1 
ATOM   2994  C  CE    . LYS A 1 1827 ? 139.878 190.570 190.532 1.00 24.37 ? 1827 LYS A CE    1 
ATOM   2995  N  NZ    . LYS A 1 1827 ? 138.892 189.886 189.651 1.00 26.27 ? 1827 LYS A NZ    1 
ATOM   2996  N  N     . SER A 1 1828 ? 137.424 196.062 192.296 1.00 9.67  ? 1828 SER A N     1 
ATOM   2997  C  CA    . SER A 1 1828 ? 137.157 196.225 193.718 1.00 9.97  ? 1828 SER A CA    1 
ATOM   2998  C  C     . SER A 1 1828 ? 135.881 197.005 193.999 1.00 12.33 ? 1828 SER A C     1 
ATOM   2999  O  O     . SER A 1 1828 ? 135.577 197.260 195.169 1.00 13.57 ? 1828 SER A O     1 
ATOM   3000  C  CB    . SER A 1 1828 ? 138.341 196.913 194.398 1.00 12.06 ? 1828 SER A CB    1 
ATOM   3001  O  OG    . SER A 1 1828 ? 139.443 196.032 194.506 1.00 17.76 ? 1828 SER A OG    1 
ATOM   3002  N  N     . LYS A 1 1829 ? 135.138 197.391 192.960 1.00 12.57 ? 1829 LYS A N     1 
ATOM   3003  C  CA    . LYS A 1 1829 ? 133.848 198.067 193.103 1.00 13.56 ? 1829 LYS A CA    1 
ATOM   3004  C  C     . LYS A 1 1829 ? 133.965 199.341 193.937 1.00 13.48 ? 1829 LYS A C     1 
ATOM   3005  O  O     . LYS A 1 1829 ? 133.148 199.606 194.820 1.00 18.40 ? 1829 LYS A O     1 
ATOM   3006  C  CB    . LYS A 1 1829 ? 132.799 197.123 193.696 1.00 17.20 ? 1829 LYS A CB    1 
ATOM   3007  C  CG    . LYS A 1 1829 ? 132.518 195.900 192.843 1.00 17.40 ? 1829 LYS A CG    1 
ATOM   3008  C  CD    . LYS A 1 1829 ? 131.964 196.292 191.484 1.00 22.57 ? 1829 LYS A CD    1 
ATOM   3009  C  CE    . LYS A 1 1829 ? 130.584 196.915 191.607 1.00 25.41 ? 1829 LYS A CE    1 
ATOM   3010  N  NZ    . LYS A 1 1829 ? 129.584 195.941 192.124 1.00 25.49 ? 1829 LYS A NZ    1 
ATOM   3011  N  N     . ILE A 1 1830 ? 134.988 200.145 193.649 1.00 14.28 ? 1830 ILE A N     1 
ATOM   3012  C  CA    . ILE A 1 1830 ? 135.163 201.413 194.345 1.00 14.28 ? 1830 ILE A CA    1 
ATOM   3013  C  C     . ILE A 1 1830 ? 134.216 202.449 193.757 1.00 15.88 ? 1830 ILE A C     1 
ATOM   3014  O  O     . ILE A 1 1830 ? 134.197 202.682 192.541 1.00 28.09 ? 1830 ILE A O     1 
ATOM   3015  C  CB    . ILE A 1 1830 ? 136.623 201.878 194.261 1.00 11.75 ? 1830 ILE A CB    1 
ATOM   3016  C  CG1   . ILE A 1 1830 ? 137.540 200.827 194.886 1.00 11.39 ? 1830 ILE A CG1   1 
ATOM   3017  C  CG2   . ILE A 1 1830 ? 136.796 203.225 194.937 1.00 12.46 ? 1830 ILE A CG2   1 
ATOM   3018  C  CD1   . ILE A 1 1830 ? 137.252 200.578 196.345 1.00 17.42 ? 1830 ILE A CD1   1 
ATOM   3019  N  N     . ASP A 1 1831 ? 133.424 203.080 194.624 1.00 14.65 ? 1831 ASP A N     1 
ATOM   3020  C  CA    . ASP A 1 1831 ? 132.426 204.051 194.198 1.00 14.17 ? 1831 ASP A CA    1 
ATOM   3021  C  C     . ASP A 1 1831 ? 132.574 205.394 194.904 1.00 17.66 ? 1831 ASP A C     1 
ATOM   3022  O  O     . ASP A 1 1831 ? 131.753 206.291 194.679 1.00 18.17 ? 1831 ASP A O     1 
ATOM   3023  C  CB    . ASP A 1 1831 ? 131.016 203.496 194.422 1.00 19.15 ? 1831 ASP A CB    1 
ATOM   3024  C  CG    . ASP A 1 1831 ? 130.806 202.993 195.838 1.00 24.02 ? 1831 ASP A CG    1 
ATOM   3025  O  OD1   . ASP A 1 1831 ? 131.728 203.131 196.667 1.00 27.24 ? 1831 ASP A OD1   1 
ATOM   3026  O  OD2   . ASP A 1 1831 ? 129.718 202.454 196.122 1.00 30.63 ? 1831 ASP A OD2   1 
ATOM   3027  N  N     . ASN A 1 1832 ? 133.590 205.557 195.744 1.00 11.71 ? 1832 ASN A N     1 
ATOM   3028  C  CA    . ASN A 1 1832 ? 133.792 206.781 196.502 1.00 10.36 ? 1832 ASN A CA    1 
ATOM   3029  C  C     . ASN A 1 1832 ? 135.204 207.295 196.263 1.00 11.76 ? 1832 ASN A C     1 
ATOM   3030  O  O     . ASN A 1 1832 ? 136.163 206.519 196.252 1.00 10.05 ? 1832 ASN A O     1 
ATOM   3031  C  CB    . ASN A 1 1832 ? 133.552 206.539 197.999 1.00 10.08 ? 1832 ASN A CB    1 
ATOM   3032  C  CG    . ASN A 1 1832 ? 134.007 207.696 198.861 1.00 16.86 ? 1832 ASN A CG    1 
ATOM   3033  O  OD1   . ASN A 1 1832 ? 133.910 208.858 198.468 1.00 21.15 ? 1832 ASN A OD1   1 
ATOM   3034  N  ND2   . ASN A 1 1832 ? 134.503 207.381 200.051 1.00 22.79 ? 1832 ASN A ND2   1 
ATOM   3035  N  N     . ALA A 1 1833 ? 135.323 208.610 196.068 1.00 10.49 ? 1833 ALA A N     1 
ATOM   3036  C  CA    . ALA A 1 1833 ? 136.630 209.219 195.855 1.00 5.75  ? 1833 ALA A CA    1 
ATOM   3037  C  C     . ALA A 1 1833 ? 137.487 209.205 197.112 1.00 8.77  ? 1833 ALA A C     1 
ATOM   3038  O  O     . ALA A 1 1833 ? 138.714 209.311 197.010 1.00 7.74  ? 1833 ALA A O     1 
ATOM   3039  C  CB    . ALA A 1 1833 ? 136.471 210.654 195.355 1.00 9.91  ? 1833 ALA A CB    1 
ATOM   3040  N  N     . LYS A 1 1834 ? 136.877 209.074 198.286 1.00 10.01 ? 1834 LYS A N     1 
ATOM   3041  C  CA    . LYS A 1 1834 ? 137.609 209.039 199.544 1.00 9.38  ? 1834 LYS A CA    1 
ATOM   3042  C  C     . LYS A 1 1834 ? 138.005 207.628 199.956 1.00 8.27  ? 1834 LYS A C     1 
ATOM   3043  O  O     . LYS A 1 1834 ? 138.572 207.452 201.038 1.00 9.56  ? 1834 LYS A O     1 
ATOM   3044  C  CB    . LYS A 1 1834 ? 136.782 209.691 200.653 1.00 12.02 ? 1834 LYS A CB    1 
ATOM   3045  C  CG    . LYS A 1 1834 ? 136.668 211.202 200.533 1.00 10.81 ? 1834 LYS A CG    1 
ATOM   3046  C  CD    . LYS A 1 1834 ? 138.033 211.860 200.521 1.00 14.12 ? 1834 LYS A CD    1 
ATOM   3047  C  CE    . LYS A 1 1834 ? 137.993 213.197 199.796 1.00 18.17 ? 1834 LYS A CE    1 
ATOM   3048  N  NZ    . LYS A 1 1834 ? 137.965 213.029 198.315 1.00 17.47 ? 1834 LYS A NZ    1 
ATOM   3049  N  N     . SER A 1 1835 ? 137.712 206.628 199.129 1.00 7.91  ? 1835 SER A N     1 
ATOM   3050  C  CA    . SER A 1 1835 ? 138.170 205.274 199.397 1.00 5.86  ? 1835 SER A CA    1 
ATOM   3051  C  C     . SER A 1 1835 ? 139.689 205.217 199.352 1.00 5.75  ? 1835 SER A C     1 
ATOM   3052  O  O     . SER A 1 1835 ? 140.328 205.882 198.532 1.00 9.82  ? 1835 SER A O     1 
ATOM   3053  C  CB    . SER A 1 1835 ? 137.578 204.301 198.380 1.00 8.25  ? 1835 SER A CB    1 
ATOM   3054  O  OG    . SER A 1 1835 ? 138.151 203.013 198.512 1.00 18.09 ? 1835 SER A OG    1 
ATOM   3055  N  N     . PHE A 1 1836 ? 140.274 204.417 200.246 1.00 5.33  ? 1836 PHE A N     1 
ATOM   3056  C  CA    . PHE A 1 1836 ? 141.725 204.380 200.344 1.00 3.41  ? 1836 PHE A CA    1 
ATOM   3057  C  C     . PHE A 1 1836 ? 142.383 203.740 199.132 1.00 2.95  ? 1836 PHE A C     1 
ATOM   3058  O  O     . PHE A 1 1836 ? 143.521 204.093 198.809 1.00 2.55  ? 1836 PHE A O     1 
ATOM   3059  C  CB    . PHE A 1 1836 ? 142.164 203.650 201.611 1.00 1.70  ? 1836 PHE A CB    1 
ATOM   3060  C  CG    . PHE A 1 1836 ? 143.615 203.828 201.922 1.00 1.26  ? 1836 PHE A CG    1 
ATOM   3061  C  CD1   . PHE A 1 1836 ? 144.101 205.058 202.330 1.00 1.37  ? 1836 PHE A CD1   1 
ATOM   3062  C  CD2   . PHE A 1 1836 ? 144.502 202.778 201.784 1.00 0.67  ? 1836 PHE A CD2   1 
ATOM   3063  C  CE1   . PHE A 1 1836 ? 145.438 205.232 202.608 1.00 1.25  ? 1836 PHE A CE1   1 
ATOM   3064  C  CE2   . PHE A 1 1836 ? 145.841 202.948 202.060 1.00 0.60  ? 1836 PHE A CE2   1 
ATOM   3065  C  CZ    . PHE A 1 1836 ? 146.309 204.171 202.473 1.00 0.80  ? 1836 PHE A CZ    1 
ATOM   3066  N  N     . GLU A 1 1837 ? 141.705 202.811 198.454 1.00 5.61  ? 1837 GLU A N     1 
ATOM   3067  C  CA    . GLU A 1 1837 ? 142.301 202.202 197.270 1.00 6.29  ? 1837 GLU A CA    1 
ATOM   3068  C  C     . GLU A 1 1837 ? 142.480 203.215 196.148 1.00 3.36  ? 1837 GLU A C     1 
ATOM   3069  O  O     . GLU A 1 1837 ? 143.281 202.992 195.235 1.00 6.01  ? 1837 GLU A O     1 
ATOM   3070  C  CB    . GLU A 1 1837 ? 141.462 201.012 196.805 1.00 7.14  ? 1837 GLU A CB    1 
ATOM   3071  C  CG    . GLU A 1 1837 ? 141.477 199.852 197.783 1.00 12.13 ? 1837 GLU A CG    1 
ATOM   3072  C  CD    . GLU A 1 1837 ? 140.632 198.687 197.324 1.00 27.37 ? 1837 GLU A CD    1 
ATOM   3073  O  OE1   . GLU A 1 1837 ? 139.932 198.829 196.302 1.00 30.75 ? 1837 GLU A OE1   1 
ATOM   3074  O  OE2   . GLU A 1 1837 ? 140.666 197.629 197.985 1.00 28.26 ? 1837 GLU A OE2   1 
ATOM   3075  N  N     . TRP A 1 1838 ? 141.751 204.329 196.196 1.00 3.13  ? 1838 TRP A N     1 
ATOM   3076  C  CA    . TRP A 1 1838 ? 142.021 205.449 195.304 1.00 2.07  ? 1838 TRP A CA    1 
ATOM   3077  C  C     . TRP A 1 1838 ? 142.993 206.449 195.921 1.00 2.34  ? 1838 TRP A C     1 
ATOM   3078  O  O     . TRP A 1 1838 ? 143.861 206.978 195.219 1.00 2.56  ? 1838 TRP A O     1 
ATOM   3079  C  CB    . TRP A 1 1838 ? 140.717 206.156 194.927 1.00 1.90  ? 1838 TRP A CB    1 
ATOM   3080  C  CG    . TRP A 1 1838 ? 140.911 207.384 194.079 1.00 1.51  ? 1838 TRP A CG    1 
ATOM   3081  C  CD1   . TRP A 1 1838 ? 140.404 208.627 194.316 1.00 1.58  ? 1838 TRP A CD1   1 
ATOM   3082  C  CD2   . TRP A 1 1838 ? 141.651 207.482 192.853 1.00 1.42  ? 1838 TRP A CD2   1 
ATOM   3083  N  NE1   . TRP A 1 1838 ? 140.787 209.492 193.325 1.00 1.49  ? 1838 TRP A NE1   1 
ATOM   3084  C  CE2   . TRP A 1 1838 ? 141.552 208.815 192.412 1.00 1.68  ? 1838 TRP A CE2   1 
ATOM   3085  C  CE3   . TRP A 1 1838 ? 142.390 206.574 192.087 1.00 1.04  ? 1838 TRP A CE3   1 
ATOM   3086  C  CZ2   . TRP A 1 1838 ? 142.164 209.264 191.244 1.00 1.44  ? 1838 TRP A CZ2   1 
ATOM   3087  C  CZ3   . TRP A 1 1838 ? 142.994 207.020 190.930 1.00 0.90  ? 1838 TRP A CZ3   1 
ATOM   3088  C  CH2   . TRP A 1 1838 ? 142.878 208.353 190.519 1.00 1.12  ? 1838 TRP A CH2   1 
ATOM   3089  N  N     . LEU A 1 1839 ? 142.866 206.716 197.222 1.00 2.11  ? 1839 LEU A N     1 
ATOM   3090  C  CA    . LEU A 1 1839 ? 143.771 207.656 197.877 1.00 1.06  ? 1839 LEU A CA    1 
ATOM   3091  C  C     . LEU A 1 1839 ? 145.199 207.129 197.902 1.00 0.79  ? 1839 LEU A C     1 
ATOM   3092  O  O     . LEU A 1 1839 ? 146.153 207.908 197.799 1.00 3.16  ? 1839 LEU A O     1 
ATOM   3093  C  CB    . LEU A 1 1839 ? 143.289 207.958 199.295 1.00 2.00  ? 1839 LEU A CB    1 
ATOM   3094  C  CG    . LEU A 1 1839 ? 141.970 208.716 199.438 1.00 1.91  ? 1839 LEU A CG    1 
ATOM   3095  C  CD1   . LEU A 1 1839 ? 141.609 208.856 200.903 1.00 1.91  ? 1839 LEU A CD1   1 
ATOM   3096  C  CD2   . LEU A 1 1839 ? 142.047 210.079 198.768 1.00 1.57  ? 1839 LEU A CD2   1 
ATOM   3097  N  N     . SER A 1 1840 ? 145.368 205.813 198.042 1.00 1.00  ? 1840 SER A N     1 
ATOM   3098  C  CA    . SER A 1 1840 ? 146.703 205.227 198.023 1.00 0.96  ? 1840 SER A CA    1 
ATOM   3099  C  C     . SER A 1 1840 ? 147.385 205.382 196.671 1.00 1.17  ? 1840 SER A C     1 
ATOM   3100  O  O     . SER A 1 1840 ? 148.617 205.340 196.605 1.00 1.77  ? 1840 SER A O     1 
ATOM   3101  C  CB    . SER A 1 1840 ? 146.633 203.749 198.408 1.00 0.95  ? 1840 SER A CB    1 
ATOM   3102  O  OG    . SER A 1 1840 ? 145.761 203.039 197.547 1.00 2.33  ? 1840 SER A OG    1 
ATOM   3103  N  N     . GLN A 1 1841 ? 146.618 205.552 195.597 1.00 0.92  ? 1841 GLN A N     1 
ATOM   3104  C  CA    . GLN A 1 1841 ? 147.197 205.819 194.290 1.00 0.82  ? 1841 GLN A CA    1 
ATOM   3105  C  C     . GLN A 1 1841 ? 147.781 207.226 194.237 1.00 0.65  ? 1841 GLN A C     1 
ATOM   3106  O  O     . GLN A 1 1841 ? 147.328 208.137 194.935 1.00 0.81  ? 1841 GLN A O     1 
ATOM   3107  C  CB    . GLN A 1 1841 ? 146.143 205.657 193.194 1.00 0.80  ? 1841 GLN A CB    1 
ATOM   3108  C  CG    . GLN A 1 1841 ? 145.464 204.304 193.170 1.00 1.09  ? 1841 GLN A CG    1 
ATOM   3109  C  CD    . GLN A 1 1841 ? 146.449 203.155 193.185 1.00 1.17  ? 1841 GLN A CD    1 
ATOM   3110  O  OE1   . GLN A 1 1841 ? 147.339 203.077 192.341 1.00 3.71  ? 1841 GLN A OE1   1 
ATOM   3111  N  NE2   . GLN A 1 1841 ? 146.294 202.256 194.144 1.00 2.23  ? 1841 GLN A NE2   1 
ATOM   3112  N  N     . MET A 1 1842 ? 148.798 207.398 193.400 1.00 0.53  ? 1842 MET A N     1 
ATOM   3113  C  CA    . MET A 1 1842 ? 149.378 208.714 193.170 1.00 0.39  ? 1842 MET A CA    1 
ATOM   3114  C  C     . MET A 1 1842 ? 148.464 209.506 192.243 1.00 0.25  ? 1842 MET A C     1 
ATOM   3115  O  O     . MET A 1 1842 ? 148.232 209.104 191.098 1.00 0.40  ? 1842 MET A O     1 
ATOM   3116  C  CB    . MET A 1 1842 ? 150.777 208.588 192.577 1.00 0.33  ? 1842 MET A CB    1 
ATOM   3117  C  CG    . MET A 1 1842 ? 151.454 209.920 192.320 1.00 0.44  ? 1842 MET A CG    1 
ATOM   3118  S  SD    . MET A 1 1842 ? 153.249 209.791 192.296 1.00 7.95  ? 1842 MET A SD    1 
ATOM   3119  C  CE    . MET A 1 1842 ? 153.620 209.879 194.041 1.00 0.14  ? 1842 MET A CE    1 
ATOM   3120  N  N     . ARG A 1 1843 ? 147.942 210.621 192.737 1.00 0.35  ? 1843 ARG A N     1 
ATOM   3121  C  CA    . ARG A 1 1843 ? 146.949 211.408 192.026 1.00 0.35  ? 1843 ARG A CA    1 
ATOM   3122  C  C     . ARG A 1 1843 ? 147.514 212.775 191.665 1.00 0.25  ? 1843 ARG A C     1 
ATOM   3123  O  O     . ARG A 1 1843 ? 148.494 213.244 192.249 1.00 0.45  ? 1843 ARG A O     1 
ATOM   3124  C  CB    . ARG A 1 1843 ? 145.674 211.549 192.863 1.00 0.90  ? 1843 ARG A CB    1 
ATOM   3125  C  CG    . ARG A 1 1843 ? 145.218 210.234 193.478 1.00 1.11  ? 1843 ARG A CG    1 
ATOM   3126  C  CD    . ARG A 1 1843 ? 143.920 210.375 194.251 1.00 3.31  ? 1843 ARG A CD    1 
ATOM   3127  N  NE    . ARG A 1 1843 ? 143.970 211.422 195.265 1.00 4.30  ? 1843 ARG A NE    1 
ATOM   3128  C  CZ    . ARG A 1 1843 ? 144.653 211.346 196.399 1.00 1.73  ? 1843 ARG A CZ    1 
ATOM   3129  N  NH1   . ARG A 1 1843 ? 145.354 210.270 196.714 1.00 0.53  ? 1843 ARG A NH1   1 
ATOM   3130  N  NH2   . ARG A 1 1843 ? 144.629 212.374 197.239 1.00 6.16  ? 1843 ARG A NH2   1 
ATOM   3131  N  N     . PHE A 1 1844 ? 146.891 213.404 190.672 1.00 0.60  ? 1844 PHE A N     1 
ATOM   3132  C  CA    . PHE A 1 1844 ? 147.384 214.646 190.086 1.00 0.54  ? 1844 PHE A CA    1 
ATOM   3133  C  C     . PHE A 1 1844 ? 146.212 215.598 189.905 1.00 0.65  ? 1844 PHE A C     1 
ATOM   3134  O  O     . PHE A 1 1844 ? 145.358 215.381 189.041 1.00 1.21  ? 1844 PHE A O     1 
ATOM   3135  C  CB    . PHE A 1 1844 ? 148.086 214.385 188.751 1.00 0.36  ? 1844 PHE A CB    1 
ATOM   3136  C  CG    . PHE A 1 1844 ? 149.204 213.389 188.842 1.00 0.21  ? 1844 PHE A CG    1 
ATOM   3137  C  CD1   . PHE A 1 1844 ? 148.946 212.027 188.802 1.00 0.33  ? 1844 PHE A CD1   1 
ATOM   3138  C  CD2   . PHE A 1 1844 ? 150.510 213.812 188.977 1.00 0.14  ? 1844 PHE A CD2   1 
ATOM   3139  C  CE1   . PHE A 1 1844 ? 149.973 211.113 188.895 1.00 0.34  ? 1844 PHE A CE1   1 
ATOM   3140  C  CE2   . PHE A 1 1844 ? 151.539 212.903 189.069 1.00 0.27  ? 1844 PHE A CE2   1 
ATOM   3141  C  CZ    . PHE A 1 1844 ? 151.271 211.551 189.026 1.00 0.23  ? 1844 PHE A CZ    1 
ATOM   3142  N  N     . TYR A 1 1845 ? 146.177 216.652 190.715 1.00 0.80  ? 1845 TYR A N     1 
ATOM   3143  C  CA    . TYR A 1 1845 ? 145.121 217.654 190.670 1.00 1.88  ? 1845 TYR A CA    1 
ATOM   3144  C  C     . TYR A 1 1845 ? 145.685 218.950 190.109 1.00 2.09  ? 1845 TYR A C     1 
ATOM   3145  O  O     . TYR A 1 1845 ? 146.736 219.420 190.554 1.00 1.20  ? 1845 TYR A O     1 
ATOM   3146  C  CB    . TYR A 1 1845 ? 144.526 217.886 192.060 1.00 1.27  ? 1845 TYR A CB    1 
ATOM   3147  C  CG    . TYR A 1 1845 ? 143.961 216.634 192.683 1.00 5.55  ? 1845 TYR A CG    1 
ATOM   3148  C  CD1   . TYR A 1 1845 ? 144.771 215.770 193.407 1.00 3.88  ? 1845 TYR A CD1   1 
ATOM   3149  C  CD2   . TYR A 1 1845 ? 142.620 216.311 192.538 1.00 5.52  ? 1845 TYR A CD2   1 
ATOM   3150  C  CE1   . TYR A 1 1845 ? 144.258 214.623 193.972 1.00 3.21  ? 1845 TYR A CE1   1 
ATOM   3151  C  CE2   . TYR A 1 1845 ? 142.100 215.167 193.101 1.00 4.27  ? 1845 TYR A CE2   1 
ATOM   3152  C  CZ    . TYR A 1 1845 ? 142.924 214.326 193.815 1.00 5.26  ? 1845 TYR A CZ    1 
ATOM   3153  O  OH    . TYR A 1 1845 ? 142.407 213.184 194.378 1.00 8.64  ? 1845 TYR A OH    1 
ATOM   3154  N  N     . PHE A 1 1846 ? 144.987 219.520 189.133 1.00 2.42  ? 1846 PHE A N     1 
ATOM   3155  C  CA    . PHE A 1 1846 ? 145.420 220.733 188.457 1.00 2.93  ? 1846 PHE A CA    1 
ATOM   3156  C  C     . PHE A 1 1846 ? 144.342 221.795 188.625 1.00 6.37  ? 1846 PHE A C     1 
ATOM   3157  O  O     . PHE A 1 1846 ? 143.182 221.569 188.268 1.00 11.03 ? 1846 PHE A O     1 
ATOM   3158  C  CB    . PHE A 1 1846 ? 145.697 220.456 186.979 1.00 5.37  ? 1846 PHE A CB    1 
ATOM   3159  C  CG    . PHE A 1 1846 ? 146.226 221.639 186.224 1.00 5.86  ? 1846 PHE A CG    1 
ATOM   3160  C  CD1   . PHE A 1 1846 ? 147.588 221.879 186.161 1.00 4.14  ? 1846 PHE A CD1   1 
ATOM   3161  C  CD2   . PHE A 1 1846 ? 145.368 222.498 185.562 1.00 7.15  ? 1846 PHE A CD2   1 
ATOM   3162  C  CE1   . PHE A 1 1846 ? 148.080 222.960 185.463 1.00 5.08  ? 1846 PHE A CE1   1 
ATOM   3163  C  CE2   . PHE A 1 1846 ? 145.855 223.580 184.862 1.00 9.00  ? 1846 PHE A CE2   1 
ATOM   3164  C  CZ    . PHE A 1 1846 ? 147.212 223.810 184.813 1.00 7.51  ? 1846 PHE A CZ    1 
ATOM   3165  N  N     . ASP A 1 1847 ? 144.725 222.949 189.165 1.00 10.09 ? 1847 ASP A N     1 
ATOM   3166  C  CA    . ASP A 1 1847 ? 143.803 224.066 189.340 1.00 11.44 ? 1847 ASP A CA    1 
ATOM   3167  C  C     . ASP A 1 1847 ? 144.201 225.186 188.391 1.00 15.94 ? 1847 ASP A C     1 
ATOM   3168  O  O     . ASP A 1 1847 ? 145.170 225.913 188.659 1.00 18.69 ? 1847 ASP A O     1 
ATOM   3169  C  CB    . ASP A 1 1847 ? 143.814 224.559 190.791 1.00 9.03  ? 1847 ASP A CB    1 
ATOM   3170  C  CG    . ASP A 1 1847 ? 142.840 225.701 191.032 1.00 19.23 ? 1847 ASP A CG    1 
ATOM   3171  O  OD1   . ASP A 1 1847 ? 142.037 226.016 190.129 1.00 20.38 ? 1847 ASP A OD1   1 
ATOM   3172  O  OD2   . ASP A 1 1847 ? 142.879 226.291 192.131 1.00 29.45 ? 1847 ASP A OD2   1 
ATOM   3173  N  N     . PRO A 1 1848 ? 143.499 225.364 187.269 1.00 15.62 ? 1848 PRO A N     1 
ATOM   3174  C  CA    . PRO A 1 1848 ? 143.823 226.481 186.371 1.00 16.66 ? 1848 PRO A CA    1 
ATOM   3175  C  C     . PRO A 1 1848 ? 143.551 227.848 186.977 1.00 18.44 ? 1848 PRO A C     1 
ATOM   3176  O  O     . PRO A 1 1848 ? 144.127 228.836 186.510 1.00 25.89 ? 1848 PRO A O     1 
ATOM   3177  C  CB    . PRO A 1 1848 ? 142.925 226.218 185.156 1.00 16.22 ? 1848 PRO A CB    1 
ATOM   3178  C  CG    . PRO A 1 1848 ? 141.755 225.493 185.736 1.00 12.56 ? 1848 PRO A CG    1 
ATOM   3179  C  CD    . PRO A 1 1848 ? 142.357 224.579 186.771 1.00 12.01 ? 1848 PRO A CD    1 
ATOM   3180  N  N     . LYS A 1 1849 ? 142.695 227.934 187.995 1.00 19.46 ? 1849 LYS A N     1 
ATOM   3181  C  CA    . LYS A 1 1849 ? 142.348 229.212 188.602 1.00 18.49 ? 1849 LYS A CA    1 
ATOM   3182  C  C     . LYS A 1 1849 ? 143.395 229.705 189.591 1.00 18.36 ? 1849 LYS A C     1 
ATOM   3183  O  O     . LYS A 1 1849 ? 143.301 230.852 190.041 1.00 22.58 ? 1849 LYS A O     1 
ATOM   3184  C  CB    . LYS A 1 1849 ? 140.992 229.104 189.304 1.00 23.29 ? 1849 LYS A CB    1 
ATOM   3185  C  CG    . LYS A 1 1849 ? 139.818 228.930 188.358 1.00 23.84 ? 1849 LYS A CG    1 
ATOM   3186  C  CD    . LYS A 1 1849 ? 138.513 228.756 189.119 1.00 28.39 ? 1849 LYS A CD    1 
ATOM   3187  C  CE    . LYS A 1 1849 ? 138.088 230.052 189.789 1.00 30.91 ? 1849 LYS A CE    1 
ATOM   3188  N  NZ    . LYS A 1 1849 ? 137.705 231.090 188.792 1.00 32.11 ? 1849 LYS A NZ    1 
ATOM   3189  N  N     . GLN A 1 1850 ? 144.375 228.875 189.938 1.00 19.23 ? 1850 GLN A N     1 
ATOM   3190  C  CA    . GLN A 1 1850 ? 145.406 229.276 190.886 1.00 16.59 ? 1850 GLN A CA    1 
ATOM   3191  C  C     . GLN A 1 1850 ? 146.251 230.401 190.297 1.00 18.17 ? 1850 GLN A C     1 
ATOM   3192  O  O     . GLN A 1 1850 ? 146.659 230.342 189.134 1.00 18.24 ? 1850 GLN A O     1 
ATOM   3193  C  CB    . GLN A 1 1850 ? 146.276 228.069 191.239 1.00 18.49 ? 1850 GLN A CB    1 
ATOM   3194  C  CG    . GLN A 1 1850 ? 147.551 228.386 191.991 1.00 15.20 ? 1850 GLN A CG    1 
ATOM   3195  C  CD    . GLN A 1 1850 ? 147.291 228.868 193.402 1.00 17.90 ? 1850 GLN A CD    1 
ATOM   3196  O  OE1   . GLN A 1 1850 ? 147.309 230.067 193.671 1.00 26.19 ? 1850 GLN A OE1   1 
ATOM   3197  N  NE2   . GLN A 1 1850 ? 147.037 227.934 194.311 1.00 15.40 ? 1850 GLN A NE2   1 
ATOM   3198  N  N     . THR A 1 1851 ? 146.503 231.434 191.105 1.00 21.34 ? 1851 THR A N     1 
ATOM   3199  C  CA    . THR A 1 1851 ? 147.221 232.605 190.607 1.00 16.84 ? 1851 THR A CA    1 
ATOM   3200  C  C     . THR A 1 1851 ? 148.692 232.294 190.351 1.00 21.27 ? 1851 THR A C     1 
ATOM   3201  O  O     . THR A 1 1851 ? 149.246 232.697 189.322 1.00 22.79 ? 1851 THR A O     1 
ATOM   3202  C  CB    . THR A 1 1851 ? 147.087 233.764 191.594 1.00 20.70 ? 1851 THR A CB    1 
ATOM   3203  O  OG1   . THR A 1 1851 ? 147.953 233.541 192.714 1.00 28.68 ? 1851 THR A OG1   1 
ATOM   3204  C  CG2   . THR A 1 1851 ? 145.653 233.877 192.088 1.00 19.70 ? 1851 THR A CG2   1 
ATOM   3205  N  N     . ASP A 1 1852 ? 149.339 231.587 191.271 1.00 21.01 ? 1852 ASP A N     1 
ATOM   3206  C  CA    . ASP A 1 1852 ? 150.742 231.223 191.109 1.00 14.10 ? 1852 ASP A CA    1 
ATOM   3207  C  C     . ASP A 1 1852 ? 150.838 230.004 190.197 1.00 16.09 ? 1852 ASP A C     1 
ATOM   3208  O  O     . ASP A 1 1852 ? 150.285 228.945 190.509 1.00 16.59 ? 1852 ASP A O     1 
ATOM   3209  C  CB    . ASP A 1 1852 ? 151.379 230.941 192.467 1.00 10.57 ? 1852 ASP A CB    1 
ATOM   3210  C  CG    . ASP A 1 1852 ? 152.875 230.682 192.375 1.00 20.30 ? 1852 ASP A CG    1 
ATOM   3211  O  OD1   . ASP A 1 1852 ? 153.445 230.805 191.270 1.00 23.53 ? 1852 ASP A OD1   1 
ATOM   3212  O  OD2   . ASP A 1 1852 ? 153.483 230.352 193.414 1.00 17.09 ? 1852 ASP A OD2   1 
ATOM   3213  N  N     . VAL A 1 1853 ? 151.538 230.155 189.072 1.00 11.92 ? 1853 VAL A N     1 
ATOM   3214  C  CA    . VAL A 1 1853 ? 151.646 229.058 188.114 1.00 9.66  ? 1853 VAL A CA    1 
ATOM   3215  C  C     . VAL A 1 1853 ? 152.418 227.889 188.707 1.00 9.24  ? 1853 VAL A C     1 
ATOM   3216  O  O     . VAL A 1 1853 ? 152.206 226.734 188.319 1.00 13.75 ? 1853 VAL A O     1 
ATOM   3217  C  CB    . VAL A 1 1853 ? 152.288 229.551 186.803 1.00 11.20 ? 1853 VAL A CB    1 
ATOM   3218  C  CG1   . VAL A 1 1853 ? 151.313 230.425 186.037 1.00 9.75  ? 1853 VAL A CG1   1 
ATOM   3219  C  CG2   . VAL A 1 1853 ? 153.581 230.301 187.085 1.00 10.33 ? 1853 VAL A CG2   1 
ATOM   3220  N  N     . LEU A 1 1854 ? 153.314 228.157 189.656 1.00 8.13  ? 1854 LEU A N     1 
ATOM   3221  C  CA    . LEU A 1 1854 ? 154.123 227.107 190.257 1.00 6.96  ? 1854 LEU A CA    1 
ATOM   3222  C  C     . LEU A 1 1854 ? 153.348 226.232 191.232 1.00 8.12  ? 1854 LEU A C     1 
ATOM   3223  O  O     . LEU A 1 1854 ? 153.876 225.205 191.666 1.00 9.37  ? 1854 LEU A O     1 
ATOM   3224  C  CB    . LEU A 1 1854 ? 155.329 227.721 190.970 1.00 7.19  ? 1854 LEU A CB    1 
ATOM   3225  C  CG    . LEU A 1 1854 ? 156.386 228.358 190.067 1.00 6.21  ? 1854 LEU A CG    1 
ATOM   3226  C  CD1   . LEU A 1 1854 ? 157.607 228.752 190.872 1.00 3.50  ? 1854 LEU A CD1   1 
ATOM   3227  C  CD2   . LEU A 1 1854 ? 156.767 227.416 188.934 1.00 3.04  ? 1854 LEU A CD2   1 
ATOM   3228  N  N     . GLN A 1 1855 ? 152.116 226.606 191.585 1.00 9.55  ? 1855 GLN A N     1 
ATOM   3229  C  CA    . GLN A 1 1855 ? 151.314 225.840 192.533 1.00 4.85  ? 1855 GLN A CA    1 
ATOM   3230  C  C     . GLN A 1 1855 ? 149.997 225.364 191.928 1.00 5.99  ? 1855 GLN A C     1 
ATOM   3231  O  O     . GLN A 1 1855 ? 149.088 224.973 192.666 1.00 9.99  ? 1855 GLN A O     1 
ATOM   3232  C  CB    . GLN A 1 1855 ? 151.048 226.661 193.796 1.00 6.81  ? 1855 GLN A CB    1 
ATOM   3233  C  CG    . GLN A 1 1855 ? 152.298 227.027 194.581 1.00 5.71  ? 1855 GLN A CG    1 
ATOM   3234  C  CD    . GLN A 1 1855 ? 153.066 225.811 195.060 1.00 11.73 ? 1855 GLN A CD    1 
ATOM   3235  O  OE1   . GLN A 1 1855 ? 152.478 224.836 195.527 1.00 17.39 ? 1855 GLN A OE1   1 
ATOM   3236  N  NE2   . GLN A 1 1855 ? 154.388 225.861 194.942 1.00 14.36 ? 1855 GLN A NE2   1 
ATOM   3237  N  N     . GLN A 1 1856 ? 149.875 225.383 190.599 1.00 4.79  ? 1856 GLN A N     1 
ATOM   3238  C  CA    . GLN A 1 1856 ? 148.646 224.905 189.973 1.00 5.53  ? 1856 GLN A CA    1 
ATOM   3239  C  C     . GLN A 1 1856 ? 148.545 223.386 190.009 1.00 4.47  ? 1856 GLN A C     1 
ATOM   3240  O  O     . GLN A 1 1856 ? 147.438 222.841 190.012 1.00 5.84  ? 1856 GLN A O     1 
ATOM   3241  C  CB    . GLN A 1 1856 ? 148.552 225.401 188.531 1.00 8.26  ? 1856 GLN A CB    1 
ATOM   3242  C  CG    . GLN A 1 1856 ? 148.713 226.900 188.372 1.00 9.33  ? 1856 GLN A CG    1 
ATOM   3243  C  CD    . GLN A 1 1856 ? 148.104 227.418 187.085 1.00 14.22 ? 1856 GLN A CD    1 
ATOM   3244  O  OE1   . GLN A 1 1856 ? 148.382 226.908 186.000 1.00 17.79 ? 1856 GLN A OE1   1 
ATOM   3245  N  NE2   . GLN A 1 1856 ? 147.268 228.442 187.198 1.00 20.48 ? 1856 GLN A NE2   1 
ATOM   3246  N  N     . LEU A 1 1857 ? 149.677 222.693 190.043 1.00 3.21  ? 1857 LEU A N     1 
ATOM   3247  C  CA    . LEU A 1 1857 ? 149.700 221.238 190.041 1.00 0.91  ? 1857 LEU A CA    1 
ATOM   3248  C  C     . LEU A 1 1857 ? 149.984 220.722 191.443 1.00 1.05  ? 1857 LEU A C     1 
ATOM   3249  O  O     . LEU A 1 1857 ? 150.972 221.116 192.069 1.00 1.47  ? 1857 LEU A O     1 
ATOM   3250  C  CB    . LEU A 1 1857 ? 150.750 220.710 189.064 1.00 0.87  ? 1857 LEU A CB    1 
ATOM   3251  C  CG    . LEU A 1 1857 ? 150.948 219.195 189.097 1.00 0.69  ? 1857 LEU A CG    1 
ATOM   3252  C  CD1   . LEU A 1 1857 ? 149.652 218.483 188.745 1.00 0.60  ? 1857 LEU A CD1   1 
ATOM   3253  C  CD2   . LEU A 1 1857 ? 152.064 218.780 188.162 1.00 0.59  ? 1857 LEU A CD2   1 
ATOM   3254  N  N     . SER A 1 1858 ? 149.114 219.843 191.929 1.00 1.37  ? 1858 SER A N     1 
ATOM   3255  C  CA    . SER A 1 1858 ? 149.282 219.192 193.219 1.00 0.76  ? 1858 SER A CA    1 
ATOM   3256  C  C     . SER A 1 1858 ? 149.316 217.685 193.011 1.00 0.58  ? 1858 SER A C     1 
ATOM   3257  O  O     . SER A 1 1858 ? 148.421 217.123 192.373 1.00 0.78  ? 1858 SER A O     1 
ATOM   3258  C  CB    . SER A 1 1858 ? 148.153 219.578 194.181 1.00 1.02  ? 1858 SER A CB    1 
ATOM   3259  O  OG    . SER A 1 1858 ? 148.340 218.985 195.453 1.00 7.58  ? 1858 SER A OG    1 
ATOM   3260  N  N     . ILE A 1 1859 ? 150.349 217.040 193.540 1.00 0.45  ? 1859 ILE A N     1 
ATOM   3261  C  CA    . ILE A 1 1859 ? 150.502 215.592 193.473 1.00 0.45  ? 1859 ILE A CA    1 
ATOM   3262  C  C     . ILE A 1 1859 ? 150.269 215.037 194.868 1.00 0.62  ? 1859 ILE A C     1 
ATOM   3263  O  O     . ILE A 1 1859 ? 150.971 215.406 195.817 1.00 0.94  ? 1859 ILE A O     1 
ATOM   3264  C  CB    . ILE A 1 1859 ? 151.882 215.188 192.935 1.00 0.29  ? 1859 ILE A CB    1 
ATOM   3265  C  CG1   . ILE A 1 1859 ? 152.089 215.754 191.529 1.00 0.31  ? 1859 ILE A CG1   1 
ATOM   3266  C  CG2   . ILE A 1 1859 ? 152.034 213.678 192.933 1.00 0.22  ? 1859 ILE A CG2   1 
ATOM   3267  C  CD1   . ILE A 1 1859 ? 153.527 216.057 191.202 1.00 0.14  ? 1859 ILE A CD1   1 
ATOM   3268  N  N     . GLN A 1 1860 ? 149.282 214.156 194.997 1.00 1.11  ? 1860 GLN A N     1 
ATOM   3269  C  CA    . GLN A 1 1860 ? 148.876 213.625 196.290 1.00 0.86  ? 1860 GLN A CA    1 
ATOM   3270  C  C     . GLN A 1 1860 ? 148.890 212.106 196.256 1.00 0.36  ? 1860 GLN A C     1 
ATOM   3271  O  O     . GLN A 1 1860 ? 148.362 211.497 195.323 1.00 0.36  ? 1860 GLN A O     1 
ATOM   3272  C  CB    . GLN A 1 1860 ? 147.488 214.136 196.681 1.00 1.95  ? 1860 GLN A CB    1 
ATOM   3273  C  CG    . GLN A 1 1860 ? 147.326 215.636 196.534 1.00 2.27  ? 1860 GLN A CG    1 
ATOM   3274  C  CD    . GLN A 1 1860 ? 145.948 216.112 196.928 1.00 3.40  ? 1860 GLN A CD    1 
ATOM   3275  O  OE1   . GLN A 1 1860 ? 145.101 215.321 197.336 1.00 9.91  ? 1860 GLN A OE1   1 
ATOM   3276  N  NE2   . GLN A 1 1860 ? 145.714 217.412 196.810 1.00 6.24  ? 1860 GLN A NE2   1 
ATOM   3277  N  N     . MET A 1 1861 ? 149.505 211.505 197.271 1.00 0.78  ? 1861 MET A N     1 
ATOM   3278  C  CA    . MET A 1 1861 ? 149.499 210.060 197.466 1.00 0.90  ? 1861 MET A CA    1 
ATOM   3279  C  C     . MET A 1 1861 ? 149.188 209.787 198.929 1.00 0.46  ? 1861 MET A C     1 
ATOM   3280  O  O     . MET A 1 1861 ? 149.963 210.174 199.809 1.00 0.46  ? 1861 MET A O     1 
ATOM   3281  C  CB    . MET A 1 1861 ? 150.839 209.437 197.067 1.00 0.70  ? 1861 MET A CB    1 
ATOM   3282  C  CG    . MET A 1 1861 ? 150.755 207.966 196.702 1.00 0.38  ? 1861 MET A CG    1 
ATOM   3283  S  SD    . MET A 1 1861 ? 152.350 207.254 196.270 1.00 4.29  ? 1861 MET A SD    1 
ATOM   3284  C  CE    . MET A 1 1861 ? 151.869 205.589 195.825 1.00 0.70  ? 1861 MET A CE    1 
ATOM   3285  N  N     . ALA A 1 1862 ? 148.056 209.125 199.183 1.00 1.52  ? 1862 ALA A N     1 
ATOM   3286  C  CA    . ALA A 1 1862 ? 147.502 208.929 200.530 1.00 0.93  ? 1862 ALA A CA    1 
ATOM   3287  C  C     . ALA A 1 1862 ? 147.281 210.310 201.134 1.00 1.39  ? 1862 ALA A C     1 
ATOM   3288  O  O     . ALA A 1 1862 ? 146.538 211.109 200.538 1.00 4.48  ? 1862 ALA A O     1 
ATOM   3289  C  CB    . ALA A 1 1862 ? 148.399 207.983 201.331 1.00 0.67  ? 1862 ALA A CB    1 
ATOM   3290  N  N     . ASN A 1 1863 ? 147.883 210.645 202.272 1.00 0.67  ? 1863 ASN A N     1 
ATOM   3291  C  CA    . ASN A 1 1863 ? 147.757 211.980 202.838 1.00 0.97  ? 1863 ASN A CA    1 
ATOM   3292  C  C     . ASN A 1 1863 ? 148.889 212.907 202.421 1.00 2.36  ? 1863 ASN A C     1 
ATOM   3293  O  O     . ASN A 1 1863 ? 148.823 214.106 202.706 1.00 5.67  ? 1863 ASN A O     1 
ATOM   3294  C  CB    . ASN A 1 1863 ? 147.698 211.912 204.369 1.00 1.16  ? 1863 ASN A CB    1 
ATOM   3295  C  CG    . ASN A 1 1863 ? 148.848 211.129 204.961 1.00 2.69  ? 1863 ASN A CG    1 
ATOM   3296  O  OD1   . ASN A 1 1863 ? 149.006 209.937 204.697 1.00 4.08  ? 1863 ASN A OD1   1 
ATOM   3297  N  ND2   . ASN A 1 1863 ? 149.664 211.799 205.763 1.00 2.59  ? 1863 ASN A ND2   1 
ATOM   3298  N  N     . ALA A 1 1864 ? 149.917 212.385 201.759 1.00 1.44  ? 1864 ALA A N     1 
ATOM   3299  C  CA    . ALA A 1 1864 ? 151.045 213.208 201.351 1.00 1.06  ? 1864 ALA A CA    1 
ATOM   3300  C  C     . ALA A 1 1864 ? 150.664 214.081 200.163 1.00 1.07  ? 1864 ALA A C     1 
ATOM   3301  O  O     . ALA A 1 1864 ? 150.100 213.597 199.179 1.00 2.13  ? 1864 ALA A O     1 
ATOM   3302  C  CB    . ALA A 1 1864 ? 152.243 212.327 201.002 1.00 0.52  ? 1864 ALA A CB    1 
ATOM   3303  N  N     . LYS A 1 1865 ? 150.966 215.371 200.262 1.00 1.18  ? 1865 LYS A N     1 
ATOM   3304  C  CA    . LYS A 1 1865 ? 150.744 216.324 199.186 1.00 1.21  ? 1865 LYS A CA    1 
ATOM   3305  C  C     . LYS A 1 1865 ? 152.064 216.979 198.817 1.00 0.48  ? 1865 LYS A C     1 
ATOM   3306  O  O     . LYS A 1 1865 ? 152.857 217.339 199.691 1.00 0.82  ? 1865 LYS A O     1 
ATOM   3307  C  CB    . LYS A 1 1865 ? 149.724 217.395 199.581 1.00 0.93  ? 1865 LYS A CB    1 
ATOM   3308  C  CG    . LYS A 1 1865 ? 148.333 216.858 199.794 1.00 2.91  ? 1865 LYS A CG    1 
ATOM   3309  C  CD    . LYS A 1 1865 ? 147.358 217.955 200.168 1.00 5.71  ? 1865 LYS A CD    1 
ATOM   3310  C  CE    . LYS A 1 1865 ? 145.956 217.391 200.286 1.00 11.88 ? 1865 LYS A CE    1 
ATOM   3311  N  NZ    . LYS A 1 1865 ? 145.858 216.449 201.434 1.00 7.30  ? 1865 LYS A NZ    1 
ATOM   3312  N  N     . PHE A 1 1866 ? 152.296 217.124 197.518 1.00 0.37  ? 1866 PHE A N     1 
ATOM   3313  C  CA    . PHE A 1 1866 ? 153.537 217.687 197.019 1.00 0.50  ? 1866 PHE A CA    1 
ATOM   3314  C  C     . PHE A 1 1866 ? 153.233 218.705 195.934 1.00 0.33  ? 1866 PHE A C     1 
ATOM   3315  O  O     . PHE A 1 1866 ? 152.262 218.570 195.185 1.00 0.58  ? 1866 PHE A O     1 
ATOM   3316  C  CB    . PHE A 1 1866 ? 154.465 216.604 196.456 1.00 0.29  ? 1866 PHE A CB    1 
ATOM   3317  C  CG    . PHE A 1 1866 ? 154.830 215.545 197.447 1.00 0.27  ? 1866 PHE A CG    1 
ATOM   3318  C  CD1   . PHE A 1 1866 ? 155.922 215.706 198.277 1.00 0.24  ? 1866 PHE A CD1   1 
ATOM   3319  C  CD2   . PHE A 1 1866 ? 154.079 214.387 197.549 1.00 0.10  ? 1866 PHE A CD2   1 
ATOM   3320  C  CE1   . PHE A 1 1866 ? 156.260 214.730 199.189 1.00 1.31  ? 1866 PHE A CE1   1 
ATOM   3321  C  CE2   . PHE A 1 1866 ? 154.410 213.412 198.457 1.00 0.11  ? 1866 PHE A CE2   1 
ATOM   3322  C  CZ    . PHE A 1 1866 ? 155.501 213.581 199.281 1.00 0.34  ? 1866 PHE A CZ    1 
ATOM   3323  N  N     . ASN A 1 1867 ? 154.071 219.729 195.864 1.00 0.43  ? 1867 ASN A N     1 
ATOM   3324  C  CA    . ASN A 1 1867 ? 154.104 220.610 194.713 1.00 0.64  ? 1867 ASN A CA    1 
ATOM   3325  C  C     . ASN A 1 1867 ? 155.077 220.052 193.684 1.00 0.40  ? 1867 ASN A C     1 
ATOM   3326  O  O     . ASN A 1 1867 ? 156.028 219.344 194.021 1.00 0.32  ? 1867 ASN A O     1 
ATOM   3327  C  CB    . ASN A 1 1867 ? 154.520 222.025 195.116 1.00 1.57  ? 1867 ASN A CB    1 
ATOM   3328  C  CG    . ASN A 1 1867 ? 155.991 222.118 195.477 1.00 5.27  ? 1867 ASN A CG    1 
ATOM   3329  O  OD1   . ASN A 1 1867 ? 156.458 221.450 196.398 1.00 6.31  ? 1867 ASN A OD1   1 
ATOM   3330  N  ND2   . ASN A 1 1867 ? 156.729 222.944 194.748 1.00 6.76  ? 1867 ASN A ND2   1 
ATOM   3331  N  N     . TYR A 1 1868 ? 154.824 220.368 192.421 1.00 0.40  ? 1868 TYR A N     1 
ATOM   3332  C  CA    . TYR A 1 1868 ? 155.738 219.988 191.356 1.00 0.24  ? 1868 TYR A CA    1 
ATOM   3333  C  C     . TYR A 1 1868 ? 156.892 220.982 191.301 1.00 0.53  ? 1868 TYR A C     1 
ATOM   3334  O  O     . TYR A 1 1868 ? 156.675 222.197 191.250 1.00 1.01  ? 1868 TYR A O     1 
ATOM   3335  C  CB    . TYR A 1 1868 ? 155.001 219.936 190.019 1.00 0.33  ? 1868 TYR A CB    1 
ATOM   3336  C  CG    . TYR A 1 1868 ? 155.717 219.154 188.944 1.00 0.44  ? 1868 TYR A CG    1 
ATOM   3337  C  CD1   . TYR A 1 1868 ? 155.809 217.769 189.005 1.00 0.19  ? 1868 TYR A CD1   1 
ATOM   3338  C  CD2   . TYR A 1 1868 ? 156.293 219.802 187.862 1.00 0.13  ? 1868 TYR A CD2   1 
ATOM   3339  C  CE1   . TYR A 1 1868 ? 156.462 217.056 188.020 1.00 0.16  ? 1868 TYR A CE1   1 
ATOM   3340  C  CE2   . TYR A 1 1868 ? 156.943 219.099 186.876 1.00 0.10  ? 1868 TYR A CE2   1 
ATOM   3341  C  CZ    . TYR A 1 1868 ? 157.028 217.728 186.956 1.00 0.17  ? 1868 TYR A CZ    1 
ATOM   3342  O  OH    . TYR A 1 1868 ? 157.677 217.031 185.967 1.00 1.26  ? 1868 TYR A OH    1 
ATOM   3343  N  N     . GLY A 1 1869 ? 158.122 220.465 191.329 1.00 0.15  ? 1869 GLY A N     1 
ATOM   3344  C  CA    . GLY A 1 1869 ? 159.281 221.339 191.370 1.00 0.62  ? 1869 GLY A CA    1 
ATOM   3345  C  C     . GLY A 1 1869 ? 159.537 222.072 190.070 1.00 0.81  ? 1869 GLY A C     1 
ATOM   3346  O  O     . GLY A 1 1869 ? 160.153 223.141 190.069 1.00 1.90  ? 1869 GLY A O     1 
ATOM   3347  N  N     . PHE A 1 1870 ? 159.065 221.516 188.953 1.00 0.51  ? 1870 PHE A N     1 
ATOM   3348  C  CA    . PHE A 1 1870 ? 159.242 222.095 187.620 1.00 0.63  ? 1870 PHE A CA    1 
ATOM   3349  C  C     . PHE A 1 1870 ? 160.716 222.258 187.260 1.00 0.84  ? 1870 PHE A C     1 
ATOM   3350  O  O     . PHE A 1 1870 ? 161.100 223.199 186.565 1.00 1.71  ? 1870 PHE A O     1 
ATOM   3351  C  CB    . PHE A 1 1870 ? 158.492 223.424 187.486 1.00 0.53  ? 1870 PHE A CB    1 
ATOM   3352  C  CG    . PHE A 1 1870 ? 157.011 223.255 187.334 1.00 0.73  ? 1870 PHE A CG    1 
ATOM   3353  C  CD1   . PHE A 1 1870 ? 156.476 222.739 186.166 1.00 0.46  ? 1870 PHE A CD1   1 
ATOM   3354  C  CD2   . PHE A 1 1870 ? 156.152 223.586 188.368 1.00 0.67  ? 1870 PHE A CD2   1 
ATOM   3355  C  CE1   . PHE A 1 1870 ? 155.118 222.568 186.027 1.00 0.52  ? 1870 PHE A CE1   1 
ATOM   3356  C  CE2   . PHE A 1 1870 ? 154.791 223.421 188.232 1.00 0.66  ? 1870 PHE A CE2   1 
ATOM   3357  C  CZ    . PHE A 1 1870 ? 154.273 222.910 187.059 1.00 0.77  ? 1870 PHE A CZ    1 
ATOM   3358  N  N     . GLU A 1 1871 ? 161.544 221.336 187.742 1.00 1.04  ? 1871 GLU A N     1 
ATOM   3359  C  CA    . GLU A 1 1871 ? 162.900 221.198 187.236 1.00 0.66  ? 1871 GLU A CA    1 
ATOM   3360  C  C     . GLU A 1 1871 ? 162.855 220.576 185.847 1.00 1.02  ? 1871 GLU A C     1 
ATOM   3361  O  O     . GLU A 1 1871 ? 162.165 219.576 185.632 1.00 4.28  ? 1871 GLU A O     1 
ATOM   3362  C  CB    . GLU A 1 1871 ? 163.727 220.327 188.181 1.00 0.47  ? 1871 GLU A CB    1 
ATOM   3363  C  CG    . GLU A 1 1871 ? 165.168 220.110 187.759 1.00 1.52  ? 1871 GLU A CG    1 
ATOM   3364  C  CD    . GLU A 1 1871 ? 166.075 221.268 188.131 1.00 2.34  ? 1871 GLU A CD    1 
ATOM   3365  O  OE1   . GLU A 1 1871 ? 165.583 222.260 188.707 1.00 4.13  ? 1871 GLU A OE1   1 
ATOM   3366  O  OE2   . GLU A 1 1871 ? 167.286 221.183 187.852 1.00 2.87  ? 1871 GLU A OE2   1 
ATOM   3367  N  N     . TYR A 1 1872 ? 163.576 221.166 184.899 1.00 1.29  ? 1872 TYR A N     1 
ATOM   3368  C  CA    . TYR A 1 1872 ? 163.646 220.589 183.562 1.00 0.95  ? 1872 TYR A CA    1 
ATOM   3369  C  C     . TYR A 1 1872 ? 164.425 219.284 183.636 1.00 1.52  ? 1872 TYR A C     1 
ATOM   3370  O  O     . TYR A 1 1872 ? 165.629 219.286 183.911 1.00 3.19  ? 1872 TYR A O     1 
ATOM   3371  C  CB    . TYR A 1 1872 ? 164.306 221.548 182.577 1.00 1.20  ? 1872 TYR A CB    1 
ATOM   3372  C  CG    . TYR A 1 1872 ? 164.323 220.998 181.169 1.00 1.56  ? 1872 TYR A CG    1 
ATOM   3373  C  CD1   . TYR A 1 1872 ? 163.215 220.341 180.652 1.00 2.45  ? 1872 TYR A CD1   1 
ATOM   3374  C  CD2   . TYR A 1 1872 ? 165.460 221.082 180.379 1.00 2.02  ? 1872 TYR A CD2   1 
ATOM   3375  C  CE1   . TYR A 1 1872 ? 163.221 219.821 179.378 1.00 2.24  ? 1872 TYR A CE1   1 
ATOM   3376  C  CE2   . TYR A 1 1872 ? 165.478 220.560 179.099 1.00 3.35  ? 1872 TYR A CE2   1 
ATOM   3377  C  CZ    . TYR A 1 1872 ? 164.354 219.929 178.606 1.00 2.82  ? 1872 TYR A CZ    1 
ATOM   3378  O  OH    . TYR A 1 1872 ? 164.362 219.406 177.336 1.00 4.17  ? 1872 TYR A OH    1 
ATOM   3379  N  N     . LEU A 1 1873 ? 163.744 218.166 183.404 1.00 1.74  ? 1873 LEU A N     1 
ATOM   3380  C  CA    . LEU A 1 1873 ? 164.378 216.861 183.478 1.00 2.52  ? 1873 LEU A CA    1 
ATOM   3381  C  C     . LEU A 1 1873 ? 164.880 216.357 182.135 1.00 2.77  ? 1873 LEU A C     1 
ATOM   3382  O  O     . LEU A 1 1873 ? 165.571 215.335 182.096 1.00 8.63  ? 1873 LEU A O     1 
ATOM   3383  C  CB    . LEU A 1 1873 ? 163.405 215.842 184.078 1.00 3.27  ? 1873 LEU A CB    1 
ATOM   3384  C  CG    . LEU A 1 1873 ? 162.821 216.240 185.433 1.00 1.26  ? 1873 LEU A CG    1 
ATOM   3385  C  CD1   . LEU A 1 1873 ? 161.758 215.258 185.863 1.00 0.97  ? 1873 LEU A CD1   1 
ATOM   3386  C  CD2   . LEU A 1 1873 ? 163.920 216.335 186.479 1.00 1.94  ? 1873 LEU A CD2   1 
ATOM   3387  N  N     . GLY A 1 1874 ? 164.577 217.054 181.043 1.00 2.90  ? 1874 GLY A N     1 
ATOM   3388  C  CA    . GLY A 1 1874 ? 164.936 216.535 179.737 1.00 2.79  ? 1874 GLY A CA    1 
ATOM   3389  C  C     . GLY A 1 1874 ? 164.148 215.283 179.420 1.00 2.52  ? 1874 GLY A C     1 
ATOM   3390  O  O     . GLY A 1 1874 ? 162.936 215.207 179.646 1.00 5.46  ? 1874 GLY A O     1 
ATOM   3391  N  N     . VAL A 1 1875 ? 164.838 214.281 178.884 1.00 3.75  ? 1875 VAL A N     1 
ATOM   3392  C  CA    . VAL A 1 1875 ? 164.199 213.007 178.581 1.00 4.60  ? 1875 VAL A CA    1 
ATOM   3393  C  C     . VAL A 1 1875 ? 164.856 211.916 179.414 1.00 6.45  ? 1875 VAL A C     1 
ATOM   3394  O  O     . VAL A 1 1875 ? 165.849 211.312 178.996 1.00 14.61 ? 1875 VAL A O     1 
ATOM   3395  C  CB    . VAL A 1 1875 ? 164.279 212.684 177.077 1.00 5.42  ? 1875 VAL A CB    1 
ATOM   3396  C  CG1   . VAL A 1 1875 ? 163.335 211.546 176.729 1.00 7.29  ? 1875 VAL A CG1   1 
ATOM   3397  C  CG2   . VAL A 1 1875 ? 163.967 213.917 176.246 1.00 3.87  ? 1875 VAL A CG2   1 
ATOM   3398  N  N     . GLN A 1 1876 ? 164.303 211.653 180.595 1.00 8.23  ? 1876 GLN A N     1 
ATOM   3399  C  CA    . GLN A 1 1876 ? 164.814 210.614 181.478 1.00 8.32  ? 1876 GLN A CA    1 
ATOM   3400  C  C     . GLN A 1 1876 ? 164.042 209.323 181.258 1.00 10.80 ? 1876 GLN A C     1 
ATOM   3401  O  O     . GLN A 1 1876 ? 162.810 209.321 181.263 1.00 16.32 ? 1876 GLN A O     1 
ATOM   3402  C  CB    . GLN A 1 1876 ? 164.697 211.032 182.945 1.00 11.71 ? 1876 GLN A CB    1 
ATOM   3403  C  CG    . GLN A 1 1876 ? 165.181 212.435 183.259 1.00 8.82  ? 1876 GLN A CG    1 
ATOM   3404  C  CD    . GLN A 1 1876 ? 166.628 212.471 183.711 1.00 15.16 ? 1876 GLN A CD    1 
ATOM   3405  O  OE1   . GLN A 1 1876 ? 167.290 211.438 183.797 1.00 15.84 ? 1876 GLN A OE1   1 
ATOM   3406  N  NE2   . GLN A 1 1876 ? 167.125 213.666 184.010 1.00 17.28 ? 1876 GLN A NE2   1 
ATOM   3407  N  N     . ASP A 1 1877 ? 164.775 208.227 181.072 1.00 15.75 ? 1877 ASP A N     1 
ATOM   3408  C  CA    . ASP A 1 1877 ? 164.143 206.922 180.922 1.00 11.76 ? 1877 ASP A CA    1 
ATOM   3409  C  C     . ASP A 1 1877 ? 163.308 206.600 182.155 1.00 9.17  ? 1877 ASP A C     1 
ATOM   3410  O  O     . ASP A 1 1877 ? 163.778 206.721 183.288 1.00 8.57  ? 1877 ASP A O     1 
ATOM   3411  C  CB    . ASP A 1 1877 ? 165.202 205.843 180.705 1.00 9.20  ? 1877 ASP A CB    1 
ATOM   3412  C  CG    . ASP A 1 1877 ? 165.803 205.885 179.315 1.00 19.38 ? 1877 ASP A CG    1 
ATOM   3413  O  OD1   . ASP A 1 1877 ? 165.036 205.979 178.333 1.00 23.13 ? 1877 ASP A OD1   1 
ATOM   3414  O  OD2   . ASP A 1 1877 ? 167.045 205.827 179.203 1.00 22.81 ? 1877 ASP A OD2   1 
ATOM   3415  N  N     . LYS A 1 1878 ? 162.065 206.188 181.929 1.00 10.44 ? 1878 LYS A N     1 
ATOM   3416  C  CA    . LYS A 1 1878 ? 161.145 205.919 183.024 1.00 7.91  ? 1878 LYS A CA    1 
ATOM   3417  C  C     . LYS A 1 1878 ? 161.135 204.446 183.399 1.00 6.68  ? 1878 LYS A C     1 
ATOM   3418  O  O     . LYS A 1 1878 ? 161.405 203.572 182.572 1.00 10.83 ? 1878 LYS A O     1 
ATOM   3419  C  CB    . LYS A 1 1878 ? 159.727 206.371 182.680 1.00 6.53  ? 1878 LYS A CB    1 
ATOM   3420  C  CG    . LYS A 1 1878 ? 159.580 207.869 182.558 1.00 11.96 ? 1878 LYS A CG    1 
ATOM   3421  C  CD    . LYS A 1 1878 ? 158.142 208.250 182.271 1.00 13.09 ? 1878 LYS A CD    1 
ATOM   3422  C  CE    . LYS A 1 1878 ? 158.003 209.741 182.071 1.00 10.49 ? 1878 LYS A CE    1 
ATOM   3423  N  NZ    . LYS A 1 1878 ? 158.264 210.491 183.323 1.00 13.13 ? 1878 LYS A NZ    1 
ATOM   3424  N  N     . LEU A 1 1879 ? 160.820 204.188 184.662 1.00 4.10  ? 1879 LEU A N     1 
ATOM   3425  C  CA    . LEU A 1 1879 ? 160.704 202.836 185.171 1.00 1.26  ? 1879 LEU A CA    1 
ATOM   3426  C  C     . LEU A 1 1879 ? 159.307 202.300 184.898 1.00 1.24  ? 1879 LEU A C     1 
ATOM   3427  O  O     . LEU A 1 1879 ? 158.334 203.055 184.824 1.00 1.93  ? 1879 LEU A O     1 
ATOM   3428  C  CB    . LEU A 1 1879 ? 160.981 202.811 186.674 1.00 0.53  ? 1879 LEU A CB    1 
ATOM   3429  C  CG    . LEU A 1 1879 ? 162.409 203.046 187.165 1.00 0.46  ? 1879 LEU A CG    1 
ATOM   3430  C  CD1   . LEU A 1 1879 ? 162.518 202.697 188.640 1.00 0.11  ? 1879 LEU A CD1   1 
ATOM   3431  C  CD2   . LEU A 1 1879 ? 163.424 202.271 186.344 1.00 0.51  ? 1879 LEU A CD2   1 
ATOM   3432  N  N     . VAL A 1 1880 ? 159.210 200.981 184.744 1.00 0.78  ? 1880 VAL A N     1 
ATOM   3433  C  CA    . VAL A 1 1880 ? 157.901 200.345 184.714 1.00 0.65  ? 1880 VAL A CA    1 
ATOM   3434  C  C     . VAL A 1 1880 ? 157.305 200.406 186.112 1.00 0.80  ? 1880 VAL A C     1 
ATOM   3435  O  O     . VAL A 1 1880 ? 157.943 200.009 187.094 1.00 0.93  ? 1880 VAL A O     1 
ATOM   3436  C  CB    . VAL A 1 1880 ? 158.007 198.900 184.206 1.00 0.94  ? 1880 VAL A CB    1 
ATOM   3437  C  CG1   . VAL A 1 1880 ? 156.668 198.185 184.358 1.00 0.37  ? 1880 VAL A CG1   1 
ATOM   3438  C  CG2   . VAL A 1 1880 ? 158.469 198.881 182.761 1.00 0.69  ? 1880 VAL A CG2   1 
ATOM   3439  N  N     . GLN A 1 1881 ? 156.085 200.917 186.209 1.00 1.33  ? 1881 GLN A N     1 
ATOM   3440  C  CA    . GLN A 1 1881 ? 155.474 201.206 187.503 1.00 2.16  ? 1881 GLN A CA    1 
ATOM   3441  C  C     . GLN A 1 1881 ? 154.883 199.910 188.050 1.00 1.63  ? 1881 GLN A C     1 
ATOM   3442  O  O     . GLN A 1 1881 ? 153.699 199.622 187.866 1.00 3.96  ? 1881 GLN A O     1 
ATOM   3443  C  CB    . GLN A 1 1881 ? 154.423 202.297 187.335 1.00 2.73  ? 1881 GLN A CB    1 
ATOM   3444  C  CG    . GLN A 1 1881 ? 153.763 202.794 188.603 1.00 2.55  ? 1881 GLN A CG    1 
ATOM   3445  C  CD    . GLN A 1 1881 ? 154.732 203.449 189.564 1.00 3.71  ? 1881 GLN A CD    1 
ATOM   3446  O  OE1   . GLN A 1 1881 ? 155.101 202.870 190.580 1.00 5.66  ? 1881 GLN A OE1   1 
ATOM   3447  N  NE2   . GLN A 1 1881 ? 155.152 204.665 189.242 1.00 7.50  ? 1881 GLN A NE2   1 
ATOM   3448  N  N     . THR A 1 1882 ? 155.720 199.113 188.718 1.00 1.92  ? 1882 THR A N     1 
ATOM   3449  C  CA    . THR A 1 1882 ? 155.400 197.796 189.249 1.00 0.95  ? 1882 THR A CA    1 
ATOM   3450  C  C     . THR A 1 1882 ? 154.819 197.893 190.653 1.00 1.21  ? 1882 THR A C     1 
ATOM   3451  O  O     . THR A 1 1882 ? 154.924 198.933 191.309 1.00 1.59  ? 1882 THR A O     1 
ATOM   3452  C  CB    . THR A 1 1882 ? 156.655 196.912 189.271 1.00 1.09  ? 1882 THR A CB    1 
ATOM   3453  O  OG1   . THR A 1 1882 ? 157.536 197.344 190.316 1.00 1.32  ? 1882 THR A OG1   1 
ATOM   3454  C  CG2   . THR A 1 1882 ? 157.377 196.974 187.942 1.00 0.70  ? 1882 THR A CG2   1 
ATOM   3455  N  N     . PRO A 1 1883 ? 154.176 196.825 191.141 1.00 3.02  ? 1883 PRO A N     1 
ATOM   3456  C  CA    . PRO A 1 1883 ? 153.695 196.833 192.534 1.00 1.11  ? 1883 PRO A CA    1 
ATOM   3457  C  C     . PRO A 1 1883 ? 154.778 197.113 193.565 1.00 1.13  ? 1883 PRO A C     1 
ATOM   3458  O  O     . PRO A 1 1883 ? 154.501 197.779 194.569 1.00 1.74  ? 1883 PRO A O     1 
ATOM   3459  C  CB    . PRO A 1 1883 ? 153.110 195.425 192.688 1.00 0.92  ? 1883 PRO A CB    1 
ATOM   3460  C  CG    . PRO A 1 1883 ? 152.602 195.117 191.331 1.00 1.97  ? 1883 PRO A CG    1 
ATOM   3461  C  CD    . PRO A 1 1883 ? 153.654 195.659 190.403 1.00 1.04  ? 1883 PRO A CD    1 
ATOM   3462  N  N     . LEU A 1 1884 ? 155.999 196.618 193.357 1.00 1.22  ? 1884 LEU A N     1 
ATOM   3463  C  CA    . LEU A 1 1884 ? 157.103 196.999 194.233 1.00 0.72  ? 1884 LEU A CA    1 
ATOM   3464  C  C     . LEU A 1 1884 ? 157.373 198.495 194.142 1.00 0.58  ? 1884 LEU A C     1 
ATOM   3465  O  O     . LEU A 1 1884 ? 157.609 199.159 195.157 1.00 0.79  ? 1884 LEU A O     1 
ATOM   3466  C  CB    . LEU A 1 1884 ? 158.362 196.204 193.883 1.00 1.16  ? 1884 LEU A CB    1 
ATOM   3467  C  CG    . LEU A 1 1884 ? 159.579 196.467 194.776 1.00 1.60  ? 1884 LEU A CG    1 
ATOM   3468  C  CD1   . LEU A 1 1884 ? 159.251 196.225 196.247 1.00 1.41  ? 1884 LEU A CD1   1 
ATOM   3469  C  CD2   . LEU A 1 1884 ? 160.776 195.636 194.344 1.00 0.57  ? 1884 LEU A CD2   1 
ATOM   3470  N  N     . THR A 1 1885 ? 157.330 199.044 192.927 1.00 1.33  ? 1885 THR A N     1 
ATOM   3471  C  CA    . THR A 1 1885 ? 157.545 200.475 192.754 1.00 1.11  ? 1885 THR A CA    1 
ATOM   3472  C  C     . THR A 1 1885 ? 156.390 201.271 193.354 1.00 0.91  ? 1885 THR A C     1 
ATOM   3473  O  O     . THR A 1 1885 ? 156.597 202.351 193.917 1.00 0.78  ? 1885 THR A O     1 
ATOM   3474  C  CB    . THR A 1 1885 ? 157.717 200.802 191.269 1.00 0.66  ? 1885 THR A CB    1 
ATOM   3475  O  OG1   . THR A 1 1885 ? 158.808 200.042 190.739 1.00 3.34  ? 1885 THR A OG1   1 
ATOM   3476  C  CG2   . THR A 1 1885 ? 158.053 202.271 191.089 1.00 0.60  ? 1885 THR A CG2   1 
ATOM   3477  N  N     . ASP A 1 1886 ? 155.166 200.747 193.245 1.00 0.82  ? 1886 ASP A N     1 
ATOM   3478  C  CA    . ASP A 1 1886 ? 154.022 201.377 193.896 1.00 0.62  ? 1886 ASP A CA    1 
ATOM   3479  C  C     . ASP A 1 1886 ? 154.207 201.410 195.406 1.00 0.37  ? 1886 ASP A C     1 
ATOM   3480  O  O     . ASP A 1 1886 ? 153.957 202.431 196.056 1.00 0.18  ? 1886 ASP A O     1 
ATOM   3481  C  CB    . ASP A 1 1886 ? 152.734 200.631 193.541 1.00 1.01  ? 1886 ASP A CB    1 
ATOM   3482  C  CG    . ASP A 1 1886 ? 152.155 201.058 192.212 1.00 3.60  ? 1886 ASP A CG    1 
ATOM   3483  O  OD1   . ASP A 1 1886 ? 152.934 201.418 191.312 1.00 6.31  ? 1886 ASP A OD1   1 
ATOM   3484  O  OD2   . ASP A 1 1886 ? 150.915 201.030 192.066 1.00 11.07 ? 1886 ASP A OD2   1 
ATOM   3485  N  N     . ARG A 1 1887 ? 154.647 200.289 195.978 1.00 0.35  ? 1887 ARG A N     1 
ATOM   3486  C  CA    . ARG A 1 1887 ? 154.916 200.243 197.409 1.00 0.14  ? 1887 ARG A CA    1 
ATOM   3487  C  C     . ARG A 1 1887 ? 156.060 201.179 197.779 1.00 0.15  ? 1887 ARG A C     1 
ATOM   3488  O  O     . ARG A 1 1887 ? 156.037 201.813 198.839 1.00 0.16  ? 1887 ARG A O     1 
ATOM   3489  C  CB    . ARG A 1 1887 ? 155.227 198.805 197.823 1.00 0.25  ? 1887 ARG A CB    1 
ATOM   3490  C  CG    . ARG A 1 1887 ? 155.383 198.585 199.309 1.00 0.44  ? 1887 ARG A CG    1 
ATOM   3491  C  CD    . ARG A 1 1887 ? 155.879 197.180 199.586 1.00 0.64  ? 1887 ARG A CD    1 
ATOM   3492  N  NE    . ARG A 1 1887 ? 156.051 196.932 201.012 1.00 1.91  ? 1887 ARG A NE    1 
ATOM   3493  C  CZ    . ARG A 1 1887 ? 155.469 195.944 201.676 1.00 1.02  ? 1887 ARG A CZ    1 
ATOM   3494  N  NH1   . ARG A 1 1887 ? 154.699 195.061 201.064 1.00 2.43  ? 1887 ARG A NH1   1 
ATOM   3495  N  NH2   . ARG A 1 1887 ? 155.670 195.835 202.985 1.00 1.21  ? 1887 ARG A NH2   1 
ATOM   3496  N  N     . CYS A 1 1888 ? 157.070 201.279 196.910 1.00 0.22  ? 1888 CYS A N     1 
ATOM   3497  C  CA    . CYS A 1 1888 ? 158.161 202.218 197.151 1.00 0.23  ? 1888 CYS A CA    1 
ATOM   3498  C  C     . CYS A 1 1888 ? 157.660 203.654 197.158 1.00 0.07  ? 1888 CYS A C     1 
ATOM   3499  O  O     . CYS A 1 1888 ? 158.045 204.450 198.021 1.00 0.06  ? 1888 CYS A O     1 
ATOM   3500  C  CB    . CYS A 1 1888 ? 159.259 202.029 196.103 1.00 0.24  ? 1888 CYS A CB    1 
ATOM   3501  S  SG    . CYS A 1 1888 ? 160.788 202.928 196.446 1.00 6.60  ? 1888 CYS A SG    1 
ATOM   3502  N  N     . TYR A 1 1889 ? 156.787 204.000 196.212 1.00 0.10  ? 1889 TYR A N     1 
ATOM   3503  C  CA    . TYR A 1 1889 ? 156.247 205.355 196.156 1.00 0.13  ? 1889 TYR A CA    1 
ATOM   3504  C  C     . TYR A 1 1889 ? 155.441 205.678 197.407 1.00 0.07  ? 1889 TYR A C     1 
ATOM   3505  O  O     . TYR A 1 1889 ? 155.560 206.770 197.972 1.00 0.04  ? 1889 TYR A O     1 
ATOM   3506  C  CB    . TYR A 1 1889 ? 155.383 205.520 194.905 1.00 0.12  ? 1889 TYR A CB    1 
ATOM   3507  C  CG    . TYR A 1 1889 ? 156.150 205.845 193.647 1.00 0.14  ? 1889 TYR A CG    1 
ATOM   3508  C  CD1   . TYR A 1 1889 ? 157.468 205.440 193.485 1.00 0.19  ? 1889 TYR A CD1   1 
ATOM   3509  C  CD2   . TYR A 1 1889 ? 155.547 206.545 192.610 1.00 0.42  ? 1889 TYR A CD2   1 
ATOM   3510  C  CE1   . TYR A 1 1889 ? 158.167 205.733 192.332 1.00 0.26  ? 1889 TYR A CE1   1 
ATOM   3511  C  CE2   . TYR A 1 1889 ? 156.238 206.841 191.453 1.00 0.69  ? 1889 TYR A CE2   1 
ATOM   3512  C  CZ    . TYR A 1 1889 ? 157.547 206.432 191.319 1.00 0.52  ? 1889 TYR A CZ    1 
ATOM   3513  O  OH    . TYR A 1 1889 ? 158.238 206.724 190.170 1.00 0.51  ? 1889 TYR A OH    1 
ATOM   3514  N  N     . LEU A 1 1890 ? 154.613 204.734 197.854 1.00 0.07  ? 1890 LEU A N     1 
ATOM   3515  C  CA    . LEU A 1 1890 ? 153.775 204.974 199.023 1.00 0.05  ? 1890 LEU A CA    1 
ATOM   3516  C  C     . LEU A 1 1890 ? 154.619 205.177 200.275 1.00 0.07  ? 1890 LEU A C     1 
ATOM   3517  O  O     . LEU A 1 1890 ? 154.372 206.094 201.065 1.00 0.07  ? 1890 LEU A O     1 
ATOM   3518  C  CB    . LEU A 1 1890 ? 152.802 203.813 199.207 1.00 0.14  ? 1890 LEU A CB    1 
ATOM   3519  C  CG    . LEU A 1 1890 ? 151.792 203.938 200.347 1.00 0.06  ? 1890 LEU A CG    1 
ATOM   3520  C  CD1   . LEU A 1 1890 ? 150.835 205.083 200.087 1.00 0.03  ? 1890 LEU A CD1   1 
ATOM   3521  C  CD2   . LEU A 1 1890 ? 151.043 202.630 200.536 1.00 0.09  ? 1890 LEU A CD2   1 
ATOM   3522  N  N     . THR A 1 1891 ? 155.634 204.334 200.464 1.00 0.06  ? 1891 THR A N     1 
ATOM   3523  C  CA    . THR A 1 1891 ? 156.446 204.405 201.674 1.00 0.05  ? 1891 THR A CA    1 
ATOM   3524  C  C     . THR A 1 1891 ? 157.285 205.677 201.703 1.00 0.04  ? 1891 THR A C     1 
ATOM   3525  O  O     . THR A 1 1891 ? 157.343 206.372 202.723 1.00 0.09  ? 1891 THR A O     1 
ATOM   3526  C  CB    . THR A 1 1891 ? 157.336 203.165 201.774 1.00 0.12  ? 1891 THR A CB    1 
ATOM   3527  O  OG1   . THR A 1 1891 ? 156.541 201.990 201.579 1.00 1.63  ? 1891 THR A OG1   1 
ATOM   3528  C  CG2   . THR A 1 1891 ? 158.007 203.094 203.134 1.00 0.11  ? 1891 THR A CG2   1 
ATOM   3529  N  N     . MET A 1 1892 ? 157.943 206.000 200.588 1.00 0.05  ? 1892 MET A N     1 
ATOM   3530  C  CA    . MET A 1 1892 ? 158.809 207.174 200.561 1.00 0.03  ? 1892 MET A CA    1 
ATOM   3531  C  C     . MET A 1 1892 ? 158.011 208.465 200.704 1.00 0.03  ? 1892 MET A C     1 
ATOM   3532  O  O     . MET A 1 1892 ? 158.452 209.396 201.387 1.00 0.02  ? 1892 MET A O     1 
ATOM   3533  C  CB    . MET A 1 1892 ? 159.645 207.189 199.282 1.00 0.03  ? 1892 MET A CB    1 
ATOM   3534  C  CG    . MET A 1 1892 ? 160.514 205.962 199.083 1.00 0.02  ? 1892 MET A CG    1 
ATOM   3535  S  SD    . MET A 1 1892 ? 161.766 205.742 200.355 1.00 2.09  ? 1892 MET A SD    1 
ATOM   3536  C  CE    . MET A 1 1892 ? 161.151 204.295 201.209 1.00 0.06  ? 1892 MET A CE    1 
ATOM   3537  N  N     . THR A 1 1893 ? 156.837 208.545 200.075 1.00 0.03  ? 1893 THR A N     1 
ATOM   3538  C  CA    . THR A 1 1893 ? 156.024 209.749 200.218 1.00 0.04  ? 1893 THR A CA    1 
ATOM   3539  C  C     . THR A 1 1893 ? 155.465 209.885 201.629 1.00 0.06  ? 1893 THR A C     1 
ATOM   3540  O  O     . THR A 1 1893 ? 155.233 211.006 202.091 1.00 0.10  ? 1893 THR A O     1 
ATOM   3541  C  CB    . THR A 1 1893 ? 154.889 209.767 199.191 1.00 0.05  ? 1893 THR A CB    1 
ATOM   3542  O  OG1   . THR A 1 1893 ? 154.126 208.557 199.281 1.00 0.13  ? 1893 THR A OG1   1 
ATOM   3543  C  CG2   . THR A 1 1893 ? 155.442 209.921 197.788 1.00 0.03  ? 1893 THR A CG2   1 
ATOM   3544  N  N     . GLN A 1 1894 ? 155.235 208.768 202.322 1.00 0.06  ? 1894 GLN A N     1 
ATOM   3545  C  CA    . GLN A 1 1894 ? 154.875 208.848 203.734 1.00 0.08  ? 1894 GLN A CA    1 
ATOM   3546  C  C     . GLN A 1 1894 ? 156.015 209.436 204.552 1.00 0.17  ? 1894 GLN A C     1 
ATOM   3547  O  O     . GLN A 1 1894 ? 155.785 210.250 205.453 1.00 0.37  ? 1894 GLN A O     1 
ATOM   3548  C  CB    . GLN A 1 1894 ? 154.485 207.468 204.267 1.00 0.26  ? 1894 GLN A CB    1 
ATOM   3549  C  CG    . GLN A 1 1894 ? 153.106 206.999 203.847 1.00 0.07  ? 1894 GLN A CG    1 
ATOM   3550  C  CD    . GLN A 1 1894 ? 151.995 207.831 204.449 1.00 0.23  ? 1894 GLN A CD    1 
ATOM   3551  O  OE1   . GLN A 1 1894 ? 151.860 207.918 205.669 1.00 4.51  ? 1894 GLN A OE1   1 
ATOM   3552  N  NE2   . GLN A 1 1894 ? 151.191 208.451 203.596 1.00 0.34  ? 1894 GLN A NE2   1 
ATOM   3553  N  N     . ALA A 1 1895 ? 157.252 209.037 204.249 1.00 0.18  ? 1895 ALA A N     1 
ATOM   3554  C  CA    . ALA A 1 1895 ? 158.409 209.613 204.926 1.00 0.11  ? 1895 ALA A CA    1 
ATOM   3555  C  C     . ALA A 1 1895 ? 158.556 211.094 204.606 1.00 0.15  ? 1895 ALA A C     1 
ATOM   3556  O  O     . ALA A 1 1895 ? 158.914 211.890 205.482 1.00 0.28  ? 1895 ALA A O     1 
ATOM   3557  C  CB    . ALA A 1 1895 ? 159.675 208.851 204.541 1.00 0.08  ? 1895 ALA A CB    1 
ATOM   3558  N  N     . LEU A 1 1896 ? 158.296 211.480 203.356 1.00 0.11  ? 1896 LEU A N     1 
ATOM   3559  C  CA    . LEU A 1 1896 ? 158.398 212.884 202.975 1.00 0.14  ? 1896 LEU A CA    1 
ATOM   3560  C  C     . LEU A 1 1896 ? 157.362 213.733 203.701 1.00 0.78  ? 1896 LEU A C     1 
ATOM   3561  O  O     . LEU A 1 1896 ? 157.662 214.853 204.129 1.00 2.98  ? 1896 LEU A O     1 
ATOM   3562  C  CB    . LEU A 1 1896 ? 158.250 213.028 201.463 1.00 0.19  ? 1896 LEU A CB    1 
ATOM   3563  C  CG    . LEU A 1 1896 ? 159.350 212.403 200.603 1.00 0.13  ? 1896 LEU A CG    1 
ATOM   3564  C  CD1   . LEU A 1 1896 ? 158.975 212.444 199.134 1.00 0.14  ? 1896 LEU A CD1   1 
ATOM   3565  C  CD2   . LEU A 1 1896 ? 160.674 213.096 200.838 1.00 0.07  ? 1896 LEU A CD2   1 
ATOM   3566  N  N     . GLU A 1 1897 ? 156.136 213.226 203.840 1.00 0.34  ? 1897 GLU A N     1 
ATOM   3567  C  CA    . GLU A 1 1897 ? 155.123 213.953 204.595 1.00 0.67  ? 1897 GLU A CA    1 
ATOM   3568  C  C     . GLU A 1 1897 ? 155.490 214.056 206.069 1.00 1.18  ? 1897 GLU A C     1 
ATOM   3569  O  O     . GLU A 1 1897 ? 155.233 215.086 206.702 1.00 2.16  ? 1897 GLU A O     1 
ATOM   3570  C  CB    . GLU A 1 1897 ? 153.755 213.288 204.429 1.00 0.88  ? 1897 GLU A CB    1 
ATOM   3571  C  CG    . GLU A 1 1897 ? 152.577 214.207 204.737 1.00 1.08  ? 1897 GLU A CG    1 
ATOM   3572  C  CD    . GLU A 1 1897 ? 152.411 215.339 203.733 1.00 6.36  ? 1897 GLU A CD    1 
ATOM   3573  O  OE1   . GLU A 1 1897 ? 153.186 215.412 202.756 1.00 9.21  ? 1897 GLU A OE1   1 
ATOM   3574  O  OE2   . GLU A 1 1897 ? 151.498 216.167 203.926 1.00 11.59 ? 1897 GLU A OE2   1 
ATOM   3575  N  N     . ALA A 1 1898 ? 156.088 213.010 206.630 1.00 0.64  ? 1898 ALA A N     1 
ATOM   3576  C  CA    . ALA A 1 1898 ? 156.571 213.032 208.003 1.00 0.48  ? 1898 ALA A CA    1 
ATOM   3577  C  C     . ALA A 1 1898 ? 157.892 213.774 208.147 1.00 0.89  ? 1898 ALA A C     1 
ATOM   3578  O  O     . ALA A 1 1898 ? 158.457 213.792 209.245 1.00 1.04  ? 1898 ALA A O     1 
ATOM   3579  C  CB    . ALA A 1 1898 ? 156.718 211.603 208.533 1.00 0.35  ? 1898 ALA A CB    1 
ATOM   3580  N  N     . ARG A 1 1899 ? 158.384 214.375 207.063 1.00 0.97  ? 1899 ARG A N     1 
ATOM   3581  C  CA    . ARG A 1 1899 ? 159.669 215.074 207.049 1.00 1.08  ? 1899 ARG A CA    1 
ATOM   3582  C  C     . ARG A 1 1899 ? 160.797 214.147 207.492 1.00 0.81  ? 1899 ARG A C     1 
ATOM   3583  O  O     . ARG A 1 1899 ? 161.712 214.545 208.212 1.00 1.93  ? 1899 ARG A O     1 
ATOM   3584  C  CB    . ARG A 1 1899 ? 159.632 216.349 207.899 1.00 2.01  ? 1899 ARG A CB    1 
ATOM   3585  C  CG    . ARG A 1 1899 ? 159.052 217.576 207.195 1.00 3.90  ? 1899 ARG A CG    1 
ATOM   3586  C  CD    . ARG A 1 1899 ? 157.641 217.346 206.677 1.00 4.57  ? 1899 ARG A CD    1 
ATOM   3587  N  NE    . ARG A 1 1899 ? 157.263 218.299 205.642 1.00 12.14 ? 1899 ARG A NE    1 
ATOM   3588  C  CZ    . ARG A 1 1899 ? 156.082 218.317 205.038 1.00 10.75 ? 1899 ARG A CZ    1 
ATOM   3589  N  NH1   . ARG A 1 1899 ? 155.137 217.445 205.341 1.00 5.98  ? 1899 ARG A NH1   1 
ATOM   3590  N  NH2   . ARG A 1 1899 ? 155.845 219.234 204.103 1.00 12.71 ? 1899 ARG A NH2   1 
ATOM   3591  N  N     . LEU A 1 1900 ? 160.718 212.895 207.061 1.00 0.86  ? 1900 LEU A N     1 
ATOM   3592  C  CA    . LEU A 1 1900 ? 161.735 211.893 207.314 1.00 0.17  ? 1900 LEU A CA    1 
ATOM   3593  C  C     . LEU A 1 1900 ? 162.411 211.511 206.008 1.00 0.15  ? 1900 LEU A C     1 
ATOM   3594  O  O     . LEU A 1 1900 ? 161.903 211.777 204.916 1.00 0.19  ? 1900 LEU A O     1 
ATOM   3595  C  CB    . LEU A 1 1900 ? 161.130 210.647 207.974 1.00 0.48  ? 1900 LEU A CB    1 
ATOM   3596  C  CG    . LEU A 1 1900 ? 160.678 210.778 209.428 1.00 1.57  ? 1900 LEU A CG    1 
ATOM   3597  C  CD1   . LEU A 1 1900 ? 159.923 209.534 209.867 1.00 1.01  ? 1900 LEU A CD1   1 
ATOM   3598  C  CD2   . LEU A 1 1900 ? 161.866 211.036 210.338 1.00 0.46  ? 1900 LEU A CD2   1 
ATOM   3599  N  N     . GLY A 1 1901 ? 163.575 210.890 206.130 1.00 0.12  ? 1901 GLY A N     1 
ATOM   3600  C  CA    . GLY A 1 1901 ? 164.255 210.384 204.964 1.00 0.05  ? 1901 GLY A CA    1 
ATOM   3601  C  C     . GLY A 1 1901 ? 163.744 209.023 204.541 1.00 0.06  ? 1901 GLY A C     1 
ATOM   3602  O  O     . GLY A 1 1901 ? 163.146 208.278 205.315 1.00 0.12  ? 1901 GLY A O     1 
ATOM   3603  N  N     . GLY A 1 1902 ? 163.979 208.700 203.276 1.00 0.03  ? 1902 GLY A N     1 
ATOM   3604  C  CA    . GLY A 1 1902 ? 163.659 207.389 202.741 1.00 0.03  ? 1902 GLY A CA    1 
ATOM   3605  C  C     . GLY A 1 1902 ? 164.889 206.499 202.754 1.00 0.02  ? 1902 GLY A C     1 
ATOM   3606  O  O     . GLY A 1 1902 ? 165.990 206.940 202.427 1.00 0.03  ? 1902 GLY A O     1 
ATOM   3607  N  N     . SER A 1 1903 ? 164.691 205.245 203.145 1.00 0.04  ? 1903 SER A N     1 
ATOM   3608  C  CA    . SER A 1 1903 ? 165.777 204.269 203.243 1.00 0.03  ? 1903 SER A CA    1 
ATOM   3609  C  C     . SER A 1 1903 ? 165.379 202.955 202.582 1.00 0.06  ? 1903 SER A C     1 
ATOM   3610  O  O     . SER A 1 1903 ? 165.127 201.954 203.262 1.00 0.09  ? 1903 SER A O     1 
ATOM   3611  C  CB    . SER A 1 1903 ? 166.172 204.045 204.702 1.00 0.05  ? 1903 SER A CB    1 
ATOM   3612  O  OG    . SER A 1 1903 ? 167.227 203.107 204.800 1.00 5.69  ? 1903 SER A OG    1 
ATOM   3613  N  N     . PRO A 1 1904 ? 165.321 202.915 201.251 1.00 0.06  ? 1904 PRO A N     1 
ATOM   3614  C  CA    . PRO A 1 1904 ? 165.143 201.626 200.567 1.00 0.05  ? 1904 PRO A CA    1 
ATOM   3615  C  C     . PRO A 1 1904 ? 166.373 200.749 200.756 1.00 0.06  ? 1904 PRO A C     1 
ATOM   3616  O  O     . PRO A 1 1904 ? 167.504 201.190 200.546 1.00 0.31  ? 1904 PRO A O     1 
ATOM   3617  C  CB    . PRO A 1 1904 ? 164.948 202.023 199.098 1.00 0.05  ? 1904 PRO A CB    1 
ATOM   3618  C  CG    . PRO A 1 1904 ? 164.620 203.484 199.129 1.00 0.05  ? 1904 PRO A CG    1 
ATOM   3619  C  CD    . PRO A 1 1904 ? 165.373 204.028 200.290 1.00 0.05  ? 1904 PRO A CD    1 
ATOM   3620  N  N     . PHE A 1 1905 ? 166.146 199.503 201.163 1.00 0.06  ? 1905 PHE A N     1 
ATOM   3621  C  CA    . PHE A 1 1905 ? 167.225 198.564 201.424 1.00 0.11  ? 1905 PHE A CA    1 
ATOM   3622  C  C     . PHE A 1 1905 ? 166.916 197.226 200.769 1.00 0.07  ? 1905 PHE A C     1 
ATOM   3623  O  O     . PHE A 1 1905 ? 165.754 196.836 200.633 1.00 0.14  ? 1905 PHE A O     1 
ATOM   3624  C  CB    . PHE A 1 1905 ? 167.455 198.371 202.933 1.00 0.17  ? 1905 PHE A CB    1 
ATOM   3625  C  CG    . PHE A 1 1905 ? 166.319 197.693 203.641 1.00 0.08  ? 1905 PHE A CG    1 
ATOM   3626  C  CD1   . PHE A 1 1905 ? 165.264 198.431 204.147 1.00 0.08  ? 1905 PHE A CD1   1 
ATOM   3627  C  CD2   . PHE A 1 1905 ? 166.313 196.320 203.815 1.00 0.09  ? 1905 PHE A CD2   1 
ATOM   3628  C  CE1   . PHE A 1 1905 ? 164.222 197.812 204.800 1.00 0.15  ? 1905 PHE A CE1   1 
ATOM   3629  C  CE2   . PHE A 1 1905 ? 165.272 195.699 204.467 1.00 0.19  ? 1905 PHE A CE2   1 
ATOM   3630  C  CZ    . PHE A 1 1905 ? 164.226 196.446 204.962 1.00 0.38  ? 1905 PHE A CZ    1 
ATOM   3631  N  N     . GLY A 1 1906 ? 167.972 196.526 200.370 1.00 0.10  ? 1906 GLY A N     1 
ATOM   3632  C  CA    . GLY A 1 1906 ? 167.840 195.226 199.762 1.00 0.35  ? 1906 GLY A CA    1 
ATOM   3633  C  C     . GLY A 1 1906 ? 169.101 194.803 199.041 1.00 0.74  ? 1906 GLY A C     1 
ATOM   3634  O  O     . GLY A 1 1906 ? 170.120 195.499 199.058 1.00 0.86  ? 1906 GLY A O     1 
ATOM   3635  N  N     . PRO A 1 1907 ? 169.092 193.623 198.377 1.00 2.28  ? 1907 PRO A N     1 
ATOM   3636  C  CA    . PRO A 1 1907 ? 170.248 193.178 197.612 1.00 1.36  ? 1907 PRO A CA    1 
ATOM   3637  C  C     . PRO A 1 1907 ? 170.446 194.028 196.367 1.00 1.94  ? 1907 PRO A C     1 
ATOM   3638  O  O     . PRO A 1 1907 ? 169.584 194.870 196.056 1.00 2.30  ? 1907 PRO A O     1 
ATOM   3639  C  CB    . PRO A 1 1907 ? 169.895 191.725 197.280 1.00 1.18  ? 1907 PRO A CB    1 
ATOM   3640  C  CG    . PRO A 1 1907 ? 168.388 191.732 197.198 1.00 1.62  ? 1907 PRO A CG    1 
ATOM   3641  C  CD    . PRO A 1 1907 ? 167.977 192.675 198.312 1.00 1.12  ? 1907 PRO A CD    1 
ATOM   3642  N  N     . ALA A 1 1908 ? 171.551 193.807 195.655 1.00 2.83  ? 1908 ALA A N     1 
ATOM   3643  C  CA    . ALA A 1 1908 ? 171.878 194.634 194.469 1.00 2.35  ? 1908 ALA A CA    1 
ATOM   3644  C  C     . ALA A 1 1908 ? 170.943 194.331 193.295 1.00 1.69  ? 1908 ALA A C     1 
ATOM   3645  O  O     . ALA A 1 1908 ? 170.506 193.172 193.149 1.00 4.60  ? 1908 ALA A O     1 
ATOM   3646  C  CB    . ALA A 1 1908 ? 173.322 194.407 194.086 1.00 3.80  ? 1908 ALA A CB    1 
ATOM   3647  N  N     . GLY A 1 1909 ? 170.653 195.346 192.481 1.00 0.67  ? 1909 GLY A N     1 
ATOM   3648  C  CA    . GLY A 1 1909 ? 169.836 195.145 191.271 1.00 0.90  ? 1909 GLY A CA    1 
ATOM   3649  C  C     . GLY A 1 1909 ? 168.366 194.959 191.579 1.00 0.99  ? 1909 GLY A C     1 
ATOM   3650  O  O     . GLY A 1 1909 ? 167.717 194.169 190.870 1.00 1.51  ? 1909 GLY A O     1 
ATOM   3651  N  N     . THR A 1 1910 ? 167.842 195.659 192.583 1.00 1.20  ? 1910 THR A N     1 
ATOM   3652  C  CA    . THR A 1 1910 ? 166.412 195.558 192.831 1.00 0.93  ? 1910 THR A CA    1 
ATOM   3653  C  C     . THR A 1 1910 ? 165.653 196.834 192.498 1.00 0.49  ? 1910 THR A C     1 
ATOM   3654  O  O     . THR A 1 1910 ? 164.435 196.874 192.691 1.00 2.75  ? 1910 THR A O     1 
ATOM   3655  C  CB    . THR A 1 1910 ? 166.142 195.176 194.295 1.00 1.13  ? 1910 THR A CB    1 
ATOM   3656  O  OG1   . THR A 1 1910 ? 166.826 196.081 195.169 1.00 1.66  ? 1910 THR A OG1   1 
ATOM   3657  C  CG2   . THR A 1 1910 ? 166.613 193.760 194.568 1.00 0.63  ? 1910 THR A CG2   1 
ATOM   3658  N  N     . GLY A 1 1911 ? 166.332 197.860 192.001 1.00 0.15  ? 1911 GLY A N     1 
ATOM   3659  C  CA    . GLY A 1 1911 ? 165.688 199.104 191.647 1.00 0.11  ? 1911 GLY A CA    1 
ATOM   3660  C  C     . GLY A 1 1911 ? 165.663 200.157 192.728 1.00 0.12  ? 1911 GLY A C     1 
ATOM   3661  O  O     . GLY A 1 1911 ? 164.910 201.125 192.597 1.00 0.16  ? 1911 GLY A O     1 
ATOM   3662  N  N     . LYS A 1 1912 ? 166.463 199.992 193.777 1.00 0.22  ? 1912 LYS A N     1 
ATOM   3663  C  CA    . LYS A 1 1912 ? 166.439 200.941 194.920 1.00 0.08  ? 1912 LYS A CA    1 
ATOM   3664  C  C     . LYS A 1 1912 ? 166.758 202.369 194.442 1.00 0.06  ? 1912 LYS A C     1 
ATOM   3665  O  O     . LYS A 1 1912 ? 165.935 203.268 194.699 1.00 0.05  ? 1912 LYS A O     1 
ATOM   3666  C  CB    . LYS A 1 1912 ? 167.417 200.466 195.999 1.00 0.25  ? 1912 LYS A CB    1 
ATOM   3667  C  CG    . LYS A 1 1912 ? 167.028 199.181 196.712 1.00 0.19  ? 1912 LYS A CG    1 
ATOM   3668  C  CD    . LYS A 1 1912 ? 167.971 198.825 197.855 1.00 0.12  ? 1912 LYS A CD    1 
ATOM   3669  C  CE    . LYS A 1 1912 ? 169.392 198.685 197.415 1.00 0.22  ? 1912 LYS A CE    1 
ATOM   3670  N  NZ    . LYS A 1 1912 ? 169.552 197.633 196.408 1.00 0.47  ? 1912 LYS A NZ    1 
ATOM   3671  N  N     . THR A 1 1913 ? 167.892 202.565 193.765 1.00 0.09  ? 1913 THR A N     1 
ATOM   3672  C  CA    . THR A 1 1913 ? 168.321 203.919 193.344 1.00 0.11  ? 1913 THR A CA    1 
ATOM   3673  C  C     . THR A 1 1913 ? 167.396 204.458 192.274 1.00 0.08  ? 1913 THR A C     1 
ATOM   3674  O  O     . THR A 1 1913 ? 167.024 205.646 192.362 1.00 0.05  ? 1913 THR A O     1 
ATOM   3675  C  CB    . THR A 1 1913 ? 169.772 203.855 192.861 1.00 0.18  ? 1913 THR A CB    1 
ATOM   3676  O  OG1   . THR A 1 1913 ? 170.505 203.247 193.920 1.00 0.46  ? 1913 THR A OG1   1 
ATOM   3677  C  CG2   . THR A 1 1913 ? 170.343 205.224 192.539 1.00 0.41  ? 1913 THR A CG2   1 
ATOM   3678  N  N     . GLU A 1 1914 ? 167.024 203.624 191.305 1.00 0.05  ? 1914 GLU A N     1 
ATOM   3679  C  CA    . GLU A 1 1914 ? 166.192 204.094 190.168 1.00 0.09  ? 1914 GLU A CA    1 
ATOM   3680  C  C     . GLU A 1 1914 ? 164.798 204.496 190.675 1.00 0.03  ? 1914 GLU A C     1 
ATOM   3681  O  O     . GLU A 1 1914 ? 164.227 205.457 190.130 1.00 0.04  ? 1914 GLU A O     1 
ATOM   3682  C  CB    . GLU A 1 1914 ? 166.138 203.019 189.082 1.00 0.91  ? 1914 GLU A CB    1 
ATOM   3683  C  CG    . GLU A 1 1914 ? 167.496 202.767 188.437 1.00 0.99  ? 1914 GLU A CG    1 
ATOM   3684  C  CD    . GLU A 1 1914 ? 168.290 204.034 188.175 1.00 4.12  ? 1914 GLU A CD    1 
ATOM   3685  O  OE1   . GLU A 1 1914 ? 167.806 204.890 187.404 1.00 4.40  ? 1914 GLU A OE1   1 
ATOM   3686  O  OE2   . GLU A 1 1914 ? 169.391 204.168 188.748 1.00 5.58  ? 1914 GLU A OE2   1 
ATOM   3687  N  N     . SER A 1 1915 ? 164.291 203.798 191.690 1.00 0.06  ? 1915 SER A N     1 
ATOM   3688  C  CA    . SER A 1 1915 ? 162.975 204.138 192.217 1.00 0.04  ? 1915 SER A CA    1 
ATOM   3689  C  C     . SER A 1 1915 ? 162.989 205.494 192.909 1.00 0.02  ? 1915 SER A C     1 
ATOM   3690  O  O     . SER A 1 1915 ? 162.033 206.269 192.788 1.00 0.04  ? 1915 SER A O     1 
ATOM   3691  C  CB    . SER A 1 1915 ? 162.496 203.050 193.176 1.00 0.06  ? 1915 SER A CB    1 
ATOM   3692  O  OG    . SER A 1 1915 ? 162.445 201.795 192.529 1.00 0.30  ? 1915 SER A OG    1 
ATOM   3693  N  N     . VAL A 1 1916 ? 164.062 205.795 193.644 1.00 0.04  ? 1916 VAL A N     1 
ATOM   3694  C  CA    . VAL A 1 1916 ? 164.175 207.094 194.301 1.00 0.05  ? 1916 VAL A CA    1 
ATOM   3695  C  C     . VAL A 1 1916 ? 164.228 208.207 193.262 1.00 0.05  ? 1916 VAL A C     1 
ATOM   3696  O  O     . VAL A 1 1916 ? 163.552 209.233 193.392 1.00 0.02  ? 1916 VAL A O     1 
ATOM   3697  C  CB    . VAL A 1 1916 ? 165.404 207.123 195.229 1.00 0.03  ? 1916 VAL A CB    1 
ATOM   3698  C  CG1   . VAL A 1 1916 ? 165.680 208.540 195.714 1.00 0.02  ? 1916 VAL A CG1   1 
ATOM   3699  C  CG2   . VAL A 1 1916 ? 165.201 206.188 196.406 1.00 0.06  ? 1916 VAL A CG2   1 
ATOM   3700  N  N     . LYS A 1 1917 ? 165.032 208.018 192.212 1.00 0.02  ? 1917 LYS A N     1 
ATOM   3701  C  CA    . LYS A 1 1917 ? 165.087 209.013 191.145 1.00 0.03  ? 1917 LYS A CA    1 
ATOM   3702  C  C     . LYS A 1 1917 ? 163.759 209.106 190.412 1.00 0.03  ? 1917 LYS A C     1 
ATOM   3703  O  O     . LYS A 1 1917 ? 163.319 210.202 190.049 1.00 0.03  ? 1917 LYS A O     1 
ATOM   3704  C  CB    . LYS A 1 1917 ? 166.219 208.695 190.166 1.00 0.06  ? 1917 LYS A CB    1 
ATOM   3705  C  CG    . LYS A 1 1917 ? 167.607 208.800 190.762 1.00 1.09  ? 1917 LYS A CG    1 
ATOM   3706  C  CD    . LYS A 1 1917 ? 168.679 208.851 189.685 1.00 2.82  ? 1917 LYS A CD    1 
ATOM   3707  C  CE    . LYS A 1 1917 ? 168.642 207.635 188.790 1.00 2.41  ? 1917 LYS A CE    1 
ATOM   3708  N  NZ    . LYS A 1 1917 ? 169.631 207.725 187.684 1.00 1.21  ? 1917 LYS A NZ    1 
ATOM   3709  N  N     . ALA A 1 1918 ? 163.106 207.965 190.181 1.00 0.02  ? 1918 ALA A N     1 
ATOM   3710  C  CA    . ALA A 1 1918 ? 161.819 207.976 189.497 1.00 0.03  ? 1918 ALA A CA    1 
ATOM   3711  C  C     . ALA A 1 1918 ? 160.788 208.771 190.288 1.00 0.04  ? 1918 ALA A C     1 
ATOM   3712  O  O     . ALA A 1 1918 ? 160.035 209.570 189.722 1.00 0.02  ? 1918 ALA A O     1 
ATOM   3713  C  CB    . ALA A 1 1918 ? 161.339 206.545 189.257 1.00 0.03  ? 1918 ALA A CB    1 
ATOM   3714  N  N     . LEU A 1 1919 ? 160.750 208.575 191.607 1.00 0.03  ? 1919 LEU A N     1 
ATOM   3715  C  CA    . LEU A 1 1919 ? 159.841 209.347 192.444 1.00 0.04  ? 1919 LEU A CA    1 
ATOM   3716  C  C     . LEU A 1 1919 ? 160.189 210.830 192.403 1.00 0.06  ? 1919 LEU A C     1 
ATOM   3717  O  O     . LEU A 1 1919 ? 159.302 211.687 192.318 1.00 0.01  ? 1919 LEU A O     1 
ATOM   3718  C  CB    . LEU A 1 1919 ? 159.870 208.825 193.880 1.00 0.08  ? 1919 LEU A CB    1 
ATOM   3719  C  CG    . LEU A 1 1919 ? 158.984 209.590 194.865 1.00 0.02  ? 1919 LEU A CG    1 
ATOM   3720  C  CD1   . LEU A 1 1919 ? 157.540 209.626 194.378 1.00 0.01  ? 1919 LEU A CD1   1 
ATOM   3721  C  CD2   . LEU A 1 1919 ? 159.072 208.987 196.249 1.00 0.03  ? 1919 LEU A CD2   1 
ATOM   3722  N  N     . GLY A 1 1920 ? 161.483 211.149 192.458 1.00 0.20  ? 1920 GLY A N     1 
ATOM   3723  C  CA    . GLY A 1 1920 ? 161.897 212.538 192.349 1.00 0.03  ? 1920 GLY A CA    1 
ATOM   3724  C  C     . GLY A 1 1920 ? 161.541 213.152 191.010 1.00 0.05  ? 1920 GLY A C     1 
ATOM   3725  O  O     . GLY A 1 1920 ? 161.064 214.285 190.939 1.00 0.04  ? 1920 GLY A O     1 
ATOM   3726  N  N     . HIS A 1 1921 ? 161.773 212.410 189.925 1.00 0.03  ? 1921 HIS A N     1 
ATOM   3727  C  CA    . HIS A 1 1921 ? 161.398 212.903 188.605 1.00 0.07  ? 1921 HIS A CA    1 
ATOM   3728  C  C     . HIS A 1 1921 ? 159.886 213.002 188.466 1.00 0.03  ? 1921 HIS A C     1 
ATOM   3729  O  O     . HIS A 1 1921 ? 159.376 213.870 187.750 1.00 0.07  ? 1921 HIS A O     1 
ATOM   3730  C  CB    . HIS A 1 1921 ? 161.985 212.007 187.513 1.00 0.21  ? 1921 HIS A CB    1 
ATOM   3731  C  CG    . HIS A 1 1921 ? 163.477 211.904 187.557 1.00 1.28  ? 1921 HIS A CG    1 
ATOM   3732  N  ND1   . HIS A 1 1921 ? 164.175 210.927 186.879 1.00 11.11 ? 1921 HIS A ND1   1 
ATOM   3733  C  CD2   . HIS A 1 1921 ? 164.405 212.655 188.194 1.00 0.52  ? 1921 HIS A CD2   1 
ATOM   3734  C  CE1   . HIS A 1 1921 ? 165.469 211.083 187.097 1.00 5.25  ? 1921 HIS A CE1   1 
ATOM   3735  N  NE2   . HIS A 1 1921 ? 165.635 212.124 187.892 1.00 5.25  ? 1921 HIS A NE2   1 
ATOM   3736  N  N     . GLN A 1 1922 ? 159.153 212.117 189.143 1.00 0.04  ? 1922 GLN A N     1 
ATOM   3737  C  CA    . GLN A 1 1922 ? 157.700 212.221 189.168 1.00 0.05  ? 1922 GLN A CA    1 
ATOM   3738  C  C     . GLN A 1 1922 ? 157.256 213.537 189.795 1.00 0.03  ? 1922 GLN A C     1 
ATOM   3739  O  O     . GLN A 1 1922 ? 156.299 214.165 189.331 1.00 0.05  ? 1922 GLN A O     1 
ATOM   3740  C  CB    . GLN A 1 1922 ? 157.105 211.038 189.930 1.00 0.09  ? 1922 GLN A CB    1 
ATOM   3741  C  CG    . GLN A 1 1922 ? 155.596 211.029 189.958 1.00 0.21  ? 1922 GLN A CG    1 
ATOM   3742  C  CD    . GLN A 1 1922 ? 154.995 210.892 188.579 1.00 0.61  ? 1922 GLN A CD    1 
ATOM   3743  O  OE1   . GLN A 1 1922 ? 155.076 209.835 187.957 1.00 0.41  ? 1922 GLN A OE1   1 
ATOM   3744  N  NE2   . GLN A 1 1922 ? 154.406 211.971 188.083 1.00 1.07  ? 1922 GLN A NE2   1 
ATOM   3745  N  N     . LEU A 1 1923 ? 157.943 213.967 190.847 1.00 0.04  ? 1923 LEU A N     1 
ATOM   3746  C  CA    . LEU A 1 1923 ? 157.625 215.204 191.543 1.00 0.05  ? 1923 LEU A CA    1 
ATOM   3747  C  C     . LEU A 1 1923 ? 158.348 216.412 190.964 1.00 0.09  ? 1923 LEU A C     1 
ATOM   3748  O  O     . LEU A 1 1923 ? 158.241 217.507 191.526 1.00 0.31  ? 1923 LEU A O     1 
ATOM   3749  C  CB    . LEU A 1 1923 ? 157.954 215.064 193.032 1.00 0.12  ? 1923 LEU A CB    1 
ATOM   3750  C  CG    . LEU A 1 1923 ? 157.217 213.943 193.773 1.00 0.05  ? 1923 LEU A CG    1 
ATOM   3751  C  CD1   . LEU A 1 1923 ? 157.496 213.994 195.265 1.00 0.03  ? 1923 LEU A CD1   1 
ATOM   3752  C  CD2   . LEU A 1 1923 ? 155.723 214.002 193.500 1.00 0.02  ? 1923 LEU A CD2   1 
ATOM   3753  N  N     . GLY A 1 1924 ? 159.073 216.244 189.863 1.00 0.09  ? 1924 GLY A N     1 
ATOM   3754  C  CA    . GLY A 1 1924 ? 159.793 217.342 189.241 1.00 0.09  ? 1924 GLY A CA    1 
ATOM   3755  C  C     . GLY A 1 1924 ? 160.940 217.881 190.067 1.00 0.09  ? 1924 GLY A C     1 
ATOM   3756  O  O     . GLY A 1 1924 ? 161.205 219.088 190.038 1.00 0.26  ? 1924 GLY A O     1 
ATOM   3757  N  N     . ARG A 1 1925 ? 161.634 217.016 190.792 1.00 0.05  ? 1925 ARG A N     1 
ATOM   3758  C  CA    . ARG A 1 1925 ? 162.727 217.424 191.657 1.00 0.07  ? 1925 ARG A CA    1 
ATOM   3759  C  C     . ARG A 1 1925 ? 164.068 217.112 191.011 1.00 0.06  ? 1925 ARG A C     1 
ATOM   3760  O  O     . ARG A 1 1925 ? 164.195 216.186 190.208 1.00 0.06  ? 1925 ARG A O     1 
ATOM   3761  C  CB    . ARG A 1 1925 ? 162.636 216.729 193.018 1.00 0.06  ? 1925 ARG A CB    1 
ATOM   3762  C  CG    . ARG A 1 1925 ? 161.322 216.937 193.738 1.00 0.06  ? 1925 ARG A CG    1 
ATOM   3763  C  CD    . ARG A 1 1925 ? 161.336 218.211 194.563 1.00 0.19  ? 1925 ARG A CD    1 
ATOM   3764  N  NE    . ARG A 1 1925 ? 160.190 218.306 195.459 1.00 0.39  ? 1925 ARG A NE    1 
ATOM   3765  C  CZ    . ARG A 1 1925 ? 158.942 218.524 195.069 1.00 0.63  ? 1925 ARG A CZ    1 
ATOM   3766  N  NH1   . ARG A 1 1925 ? 158.633 218.688 193.793 1.00 0.42  ? 1925 ARG A NH1   1 
ATOM   3767  N  NH2   . ARG A 1 1925 ? 157.978 218.584 195.981 1.00 0.51  ? 1925 ARG A NH2   1 
ATOM   3768  N  N     . PHE A 1 1926 ? 165.071 217.906 191.372 1.00 0.10  ? 1926 PHE A N     1 
ATOM   3769  C  CA    . PHE A 1 1926 ? 166.450 217.645 190.980 1.00 0.11  ? 1926 PHE A CA    1 
ATOM   3770  C  C     . PHE A 1 1926 ? 167.012 216.589 191.927 1.00 0.03  ? 1926 PHE A C     1 
ATOM   3771  O  O     . PHE A 1 1926 ? 167.232 216.862 193.110 1.00 0.04  ? 1926 PHE A O     1 
ATOM   3772  C  CB    . PHE A 1 1926 ? 167.255 218.943 191.023 1.00 0.22  ? 1926 PHE A CB    1 
ATOM   3773  C  CG    . PHE A 1 1926 ? 168.670 218.819 190.527 1.00 0.33  ? 1926 PHE A CG    1 
ATOM   3774  C  CD1   . PHE A 1 1926 ? 169.109 217.682 189.869 1.00 0.25  ? 1926 PHE A CD1   1 
ATOM   3775  C  CD2   . PHE A 1 1926 ? 169.563 219.864 190.707 1.00 0.53  ? 1926 PHE A CD2   1 
ATOM   3776  C  CE1   . PHE A 1 1926 ? 170.409 217.584 189.415 1.00 0.36  ? 1926 PHE A CE1   1 
ATOM   3777  C  CE2   . PHE A 1 1926 ? 170.863 219.772 190.253 1.00 1.08  ? 1926 PHE A CE2   1 
ATOM   3778  C  CZ    . PHE A 1 1926 ? 171.287 218.632 189.606 1.00 1.25  ? 1926 PHE A CZ    1 
ATOM   3779  N  N     . VAL A 1 1927 ? 167.233 215.385 191.414 1.00 0.02  ? 1927 VAL A N     1 
ATOM   3780  C  CA    . VAL A 1 1927 ? 167.725 214.265 192.207 1.00 0.02  ? 1927 VAL A CA    1 
ATOM   3781  C  C     . VAL A 1 1927 ? 169.217 214.118 191.949 1.00 0.02  ? 1927 VAL A C     1 
ATOM   3782  O  O     . VAL A 1 1927 ? 169.643 213.956 190.799 1.00 0.05  ? 1927 VAL A O     1 
ATOM   3783  C  CB    . VAL A 1 1927 ? 166.979 212.964 191.869 1.00 0.03  ? 1927 VAL A CB    1 
ATOM   3784  C  CG1   . VAL A 1 1927 ? 167.414 211.840 192.800 1.00 0.02  ? 1927 VAL A CG1   1 
ATOM   3785  C  CG2   . VAL A 1 1927 ? 165.480 213.172 191.941 1.00 0.02  ? 1927 VAL A CG2   1 
ATOM   3786  N  N     . LEU A 1 1928 ? 170.011 214.172 193.011 1.00 0.03  ? 1928 LEU A N     1 
ATOM   3787  C  CA    . LEU A 1 1928 ? 171.452 213.986 192.924 1.00 0.03  ? 1928 LEU A CA    1 
ATOM   3788  C  C     . LEU A 1 1928 ? 171.832 212.674 193.592 1.00 0.04  ? 1928 LEU A C     1 
ATOM   3789  O  O     . LEU A 1 1928 ? 171.467 212.429 194.745 1.00 0.09  ? 1928 LEU A O     1 
ATOM   3790  C  CB    . LEU A 1 1928 ? 172.218 215.141 193.573 1.00 0.19  ? 1928 LEU A CB    1 
ATOM   3791  C  CG    . LEU A 1 1928 ? 172.335 216.457 192.799 1.00 0.21  ? 1928 LEU A CG    1 
ATOM   3792  C  CD1   . LEU A 1 1928 ? 171.017 217.209 192.789 1.00 0.11  ? 1928 LEU A CD1   1 
ATOM   3793  C  CD2   . LEU A 1 1928 ? 173.458 217.319 193.342 1.00 0.29  ? 1928 LEU A CD2   1 
ATOM   3794  N  N     . VAL A 1 1929 ? 172.562 211.844 192.864 1.00 0.09  ? 1929 VAL A N     1 
ATOM   3795  C  CA    . VAL A 1 1929 ? 173.032 210.555 193.350 1.00 0.12  ? 1929 VAL A CA    1 
ATOM   3796  C  C     . VAL A 1 1929 ? 174.472 210.717 193.807 1.00 0.11  ? 1929 VAL A C     1 
ATOM   3797  O  O     . VAL A 1 1929 ? 175.280 211.354 193.123 1.00 0.32  ? 1929 VAL A O     1 
ATOM   3798  C  CB    . VAL A 1 1929 ? 172.908 209.477 192.258 1.00 0.29  ? 1929 VAL A CB    1 
ATOM   3799  C  CG1   . VAL A 1 1929 ? 173.752 208.263 192.591 1.00 0.93  ? 1929 VAL A CG1   1 
ATOM   3800  C  CG2   . VAL A 1 1929 ? 171.456 209.088 192.067 1.00 0.16  ? 1929 VAL A CG2   1 
ATOM   3801  N  N     . PHE A 1 1930 ? 174.790 210.167 194.975 1.00 0.16  ? 1930 PHE A N     1 
ATOM   3802  C  CA    . PHE A 1 1930 ? 176.153 210.157 195.491 1.00 0.14  ? 1930 PHE A CA    1 
ATOM   3803  C  C     . PHE A 1 1930 ? 176.550 208.722 195.796 1.00 0.56  ? 1930 PHE A C     1 
ATOM   3804  O  O     . PHE A 1 1930 ? 175.839 208.019 196.520 1.00 0.89  ? 1930 PHE A O     1 
ATOM   3805  C  CB    . PHE A 1 1930 ? 176.282 211.034 196.739 1.00 0.16  ? 1930 PHE A CB    1 
ATOM   3806  C  CG    . PHE A 1 1930 ? 175.892 212.465 196.511 1.00 0.08  ? 1930 PHE A CG    1 
ATOM   3807  C  CD1   . PHE A 1 1930 ? 176.831 213.392 196.100 1.00 0.07  ? 1930 PHE A CD1   1 
ATOM   3808  C  CD2   . PHE A 1 1930 ? 174.587 212.880 196.699 1.00 0.07  ? 1930 PHE A CD2   1 
ATOM   3809  C  CE1   . PHE A 1 1930 ? 176.477 214.706 195.884 1.00 0.12  ? 1930 PHE A CE1   1 
ATOM   3810  C  CE2   . PHE A 1 1930 ? 174.228 214.192 196.482 1.00 0.07  ? 1930 PHE A CE2   1 
ATOM   3811  C  CZ    . PHE A 1 1930 ? 175.175 215.106 196.074 1.00 0.09  ? 1930 PHE A CZ    1 
ATOM   3812  N  N     . ASN A 1 1931 ? 177.671 208.287 195.230 1.00 0.66  ? 1931 ASN A N     1 
ATOM   3813  C  CA    . ASN A 1 1931 ? 178.246 206.979 195.533 1.00 0.48  ? 1931 ASN A CA    1 
ATOM   3814  C  C     . ASN A 1 1931 ? 179.119 207.155 196.768 1.00 0.69  ? 1931 ASN A C     1 
ATOM   3815  O  O     . ASN A 1 1931 ? 180.261 207.608 196.680 1.00 1.68  ? 1931 ASN A O     1 
ATOM   3816  C  CB    . ASN A 1 1931 ? 179.037 206.451 194.341 1.00 0.55  ? 1931 ASN A CB    1 
ATOM   3817  C  CG    . ASN A 1 1931 ? 179.558 205.040 194.545 1.00 0.90  ? 1931 ASN A CG    1 
ATOM   3818  O  OD1   . ASN A 1 1931 ? 180.010 204.669 195.627 1.00 2.32  ? 1931 ASN A OD1   1 
ATOM   3819  N  ND2   . ASN A 1 1931 ? 179.516 204.250 193.486 1.00 0.41  ? 1931 ASN A ND2   1 
ATOM   3820  N  N     . CYS A 1 1932 ? 178.577 206.798 197.925 1.00 0.93  ? 1932 CYS A N     1 
ATOM   3821  C  CA    . CYS A 1 1932 ? 179.244 207.045 199.193 1.00 0.95  ? 1932 CYS A CA    1 
ATOM   3822  C  C     . CYS A 1 1932 ? 180.366 206.044 199.436 1.00 1.38  ? 1932 CYS A C     1 
ATOM   3823  O  O     . CYS A 1 1932 ? 180.294 204.884 199.024 1.00 2.62  ? 1932 CYS A O     1 
ATOM   3824  C  CB    . CYS A 1 1932 ? 178.235 206.975 200.338 1.00 1.06  ? 1932 CYS A CB    1 
ATOM   3825  S  SG    . CYS A 1 1932 ? 176.950 208.234 200.289 1.00 4.43  ? 1932 CYS A SG    1 
ATOM   3826  N  N     . ASP A 1 1933 ? 181.415 206.509 200.112 1.00 1.07  ? 1933 ASP A N     1 
ATOM   3827  C  CA    . ASP A 1 1933 ? 182.455 205.627 200.620 1.00 1.60  ? 1933 ASP A CA    1 
ATOM   3828  C  C     . ASP A 1 1933 ? 182.916 206.152 201.974 1.00 1.91  ? 1933 ASP A C     1 
ATOM   3829  O  O     . ASP A 1 1933 ? 182.324 207.076 202.539 1.00 1.69  ? 1933 ASP A O     1 
ATOM   3830  C  CB    . ASP A 1 1933 ? 183.624 205.488 199.631 1.00 3.07  ? 1933 ASP A CB    1 
ATOM   3831  C  CG    . ASP A 1 1933 ? 184.354 206.797 199.371 1.00 3.55  ? 1933 ASP A CG    1 
ATOM   3832  O  OD1   . ASP A 1 1933 ? 183.958 207.848 199.908 1.00 3.23  ? 1933 ASP A OD1   1 
ATOM   3833  O  OD2   . ASP A 1 1933 ? 185.354 206.768 198.625 1.00 14.37 ? 1933 ASP A OD2   1 
ATOM   3834  N  N     . GLU A 1 1934 ? 183.991 205.554 202.491 1.00 4.84  ? 1934 GLU A N     1 
ATOM   3835  C  CA    . GLU A 1 1934 ? 184.515 205.934 203.797 1.00 2.66  ? 1934 GLU A CA    1 
ATOM   3836  C  C     . GLU A 1 1934 ? 185.095 207.343 203.819 1.00 3.13  ? 1934 GLU A C     1 
ATOM   3837  O  O     . GLU A 1 1934 ? 185.327 207.880 204.906 1.00 7.03  ? 1934 GLU A O     1 
ATOM   3838  C  CB    . GLU A 1 1934 ? 185.575 204.926 204.246 1.00 6.08  ? 1934 GLU A CB    1 
ATOM   3839  C  CG    . GLU A 1 1934 ? 186.889 205.016 203.486 1.00 6.68  ? 1934 GLU A CG    1 
ATOM   3840  C  CD    . GLU A 1 1934 ? 186.833 204.333 202.134 1.00 12.71 ? 1934 GLU A CD    1 
ATOM   3841  O  OE1   . GLU A 1 1934 ? 185.816 203.668 201.844 1.00 14.46 ? 1934 GLU A OE1   1 
ATOM   3842  O  OE2   . GLU A 1 1934 ? 187.804 204.465 201.362 1.00 16.55 ? 1934 GLU A OE2   1 
ATOM   3843  N  N     . THR A 1 1935 ? 185.335 207.952 202.658 1.00 3.17  ? 1935 THR A N     1 
ATOM   3844  C  CA    . THR A 1 1935 ? 185.841 209.318 202.611 1.00 1.70  ? 1935 THR A CA    1 
ATOM   3845  C  C     . THR A 1 1935 ? 184.742 210.365 202.741 1.00 2.03  ? 1935 THR A C     1 
ATOM   3846  O  O     . THR A 1 1935 ? 185.055 211.555 202.841 1.00 2.71  ? 1935 THR A O     1 
ATOM   3847  C  CB    . THR A 1 1935 ? 186.623 209.549 201.316 1.00 2.23  ? 1935 THR A CB    1 
ATOM   3848  O  OG1   . THR A 1 1935 ? 185.730 209.493 200.197 1.00 3.63  ? 1935 THR A OG1   1 
ATOM   3849  C  CG2   . THR A 1 1935 ? 187.702 208.495 201.155 1.00 1.80  ? 1935 THR A CG2   1 
ATOM   3850  N  N     . PHE A 1 1936 ? 183.475 209.959 202.738 1.00 2.58  ? 1936 PHE A N     1 
ATOM   3851  C  CA    . PHE A 1 1936 ? 182.360 210.873 202.982 1.00 1.66  ? 1936 PHE A CA    1 
ATOM   3852  C  C     . PHE A 1 1936 ? 182.254 211.082 204.486 1.00 2.39  ? 1936 PHE A C     1 
ATOM   3853  O  O     . PHE A 1 1936 ? 181.517 210.385 205.184 1.00 7.19  ? 1936 PHE A O     1 
ATOM   3854  C  CB    . PHE A 1 1936 ? 181.065 210.318 202.401 1.00 1.07  ? 1936 PHE A CB    1 
ATOM   3855  C  CG    . PHE A 1 1936 ? 180.916 210.541 200.925 1.00 1.33  ? 1936 PHE A CG    1 
ATOM   3856  C  CD1   . PHE A 1 1936 ? 181.735 209.883 200.023 1.00 0.91  ? 1936 PHE A CD1   1 
ATOM   3857  C  CD2   . PHE A 1 1936 ? 179.950 211.406 200.436 1.00 0.94  ? 1936 PHE A CD2   1 
ATOM   3858  C  CE1   . PHE A 1 1936 ? 181.598 210.086 198.667 1.00 0.72  ? 1936 PHE A CE1   1 
ATOM   3859  C  CE2   . PHE A 1 1936 ? 179.808 211.612 199.080 1.00 0.72  ? 1936 PHE A CE2   1 
ATOM   3860  C  CZ    . PHE A 1 1936 ? 180.633 210.951 198.195 1.00 0.70  ? 1936 PHE A CZ    1 
ATOM   3861  N  N     . ASP A 1 1937 ? 183.009 212.048 204.995 1.00 2.36  ? 1937 ASP A N     1 
ATOM   3862  C  CA    . ASP A 1 1937 ? 183.079 212.291 206.427 1.00 1.54  ? 1937 ASP A CA    1 
ATOM   3863  C  C     . ASP A 1 1937 ? 182.033 213.326 206.843 1.00 1.66  ? 1937 ASP A C     1 
ATOM   3864  O  O     . ASP A 1 1937 ? 181.163 213.721 206.064 1.00 1.63  ? 1937 ASP A O     1 
ATOM   3865  C  CB    . ASP A 1 1937 ? 184.500 212.698 206.821 1.00 1.79  ? 1937 ASP A CB    1 
ATOM   3866  C  CG    . ASP A 1 1937 ? 184.995 213.933 206.081 1.00 4.32  ? 1937 ASP A CG    1 
ATOM   3867  O  OD1   . ASP A 1 1937 ? 184.176 214.767 205.646 1.00 3.36  ? 1937 ASP A OD1   1 
ATOM   3868  O  OD2   . ASP A 1 1937 ? 186.227 214.068 205.936 1.00 15.10 ? 1937 ASP A OD2   1 
ATOM   3869  N  N     . PHE A 1 1938 ? 182.119 213.774 208.097 1.00 1.70  ? 1938 PHE A N     1 
ATOM   3870  C  CA    . PHE A 1 1938 ? 181.156 214.735 208.625 1.00 1.11  ? 1938 PHE A CA    1 
ATOM   3871  C  C     . PHE A 1 1938 ? 181.218 216.058 207.869 1.00 0.87  ? 1938 PHE A C     1 
ATOM   3872  O  O     . PHE A 1 1938 ? 180.183 216.659 207.561 1.00 0.60  ? 1938 PHE A O     1 
ATOM   3873  C  CB    . PHE A 1 1938 ? 181.410 214.938 210.120 1.00 1.17  ? 1938 PHE A CB    1 
ATOM   3874  C  CG    . PHE A 1 1938 ? 180.580 216.022 210.741 1.00 0.83  ? 1938 PHE A CG    1 
ATOM   3875  C  CD1   . PHE A 1 1938 ? 179.290 215.768 211.166 1.00 0.62  ? 1938 PHE A CD1   1 
ATOM   3876  C  CD2   . PHE A 1 1938 ? 181.105 217.289 210.930 1.00 0.77  ? 1938 PHE A CD2   1 
ATOM   3877  C  CE1   . PHE A 1 1938 ? 178.530 216.760 211.747 1.00 0.71  ? 1938 PHE A CE1   1 
ATOM   3878  C  CE2   . PHE A 1 1938 ? 180.349 218.284 211.511 1.00 1.14  ? 1938 PHE A CE2   1 
ATOM   3879  C  CZ    . PHE A 1 1938 ? 179.059 218.019 211.918 1.00 0.73  ? 1938 PHE A CZ    1 
ATOM   3880  N  N     . GLN A 1 1939 ? 182.427 216.527 207.565 1.00 1.57  ? 1939 GLN A N     1 
ATOM   3881  C  CA    . GLN A 1 1939 ? 182.569 217.804 206.872 1.00 1.68  ? 1939 GLN A CA    1 
ATOM   3882  C  C     . GLN A 1 1939 ? 182.116 217.708 205.420 1.00 1.62  ? 1939 GLN A C     1 
ATOM   3883  O  O     . GLN A 1 1939 ? 181.519 218.649 204.889 1.00 1.37  ? 1939 GLN A O     1 
ATOM   3884  C  CB    . GLN A 1 1939 ? 184.015 218.286 206.962 1.00 2.99  ? 1939 GLN A CB    1 
ATOM   3885  C  CG    . GLN A 1 1939 ? 184.485 218.539 208.384 1.00 2.47  ? 1939 GLN A CG    1 
ATOM   3886  C  CD    . GLN A 1 1939 ? 185.931 218.982 208.453 1.00 12.51 ? 1939 GLN A CD    1 
ATOM   3887  O  OE1   . GLN A 1 1939 ? 186.300 220.021 207.908 1.00 17.23 ? 1939 GLN A OE1   1 
ATOM   3888  N  NE2   . GLN A 1 1939 ? 186.760 218.192 209.123 1.00 13.50 ? 1939 GLN A NE2   1 
ATOM   3889  N  N     . ALA A 1 1940 ? 182.401 216.583 204.758 1.00 1.22  ? 1940 ALA A N     1 
ATOM   3890  C  CA    . ALA A 1 1940 ? 182.002 216.424 203.364 1.00 0.76  ? 1940 ALA A CA    1 
ATOM   3891  C  C     . ALA A 1 1940 ? 180.489 216.300 203.235 1.00 0.53  ? 1940 ALA A C     1 
ATOM   3892  O  O     . ALA A 1 1940 ? 179.877 216.926 202.362 1.00 0.28  ? 1940 ALA A O     1 
ATOM   3893  C  CB    . ALA A 1 1940 ? 182.699 215.208 202.751 1.00 0.98  ? 1940 ALA A CB    1 
ATOM   3894  N  N     . MET A 1 1941 ? 179.866 215.497 204.101 1.00 0.72  ? 1941 MET A N     1 
ATOM   3895  C  CA    . MET A 1 1941 ? 178.417 215.333 204.058 1.00 0.64  ? 1941 MET A CA    1 
ATOM   3896  C  C     . MET A 1 1941 ? 177.702 216.646 204.338 1.00 0.58  ? 1941 MET A C     1 
ATOM   3897  O  O     . MET A 1 1941 ? 176.697 216.963 203.691 1.00 2.65  ? 1941 MET A O     1 
ATOM   3898  C  CB    . MET A 1 1941 ? 177.980 214.262 205.058 1.00 0.48  ? 1941 MET A CB    1 
ATOM   3899  C  CG    . MET A 1 1941 ? 178.377 212.848 204.673 1.00 0.94  ? 1941 MET A CG    1 
ATOM   3900  S  SD    . MET A 1 1941 ? 177.543 212.264 203.187 1.00 4.37  ? 1941 MET A SD    1 
ATOM   3901  C  CE    . MET A 1 1941 ? 175.838 212.271 203.732 1.00 0.55  ? 1941 MET A CE    1 
ATOM   3902  N  N     . GLY A 1 1942 ? 178.206 217.425 205.296 1.00 0.27  ? 1942 GLY A N     1 
ATOM   3903  C  CA    . GLY A 1 1942 ? 177.560 218.682 205.630 1.00 0.38  ? 1942 GLY A CA    1 
ATOM   3904  C  C     . GLY A 1 1942 ? 177.562 219.662 204.476 1.00 0.53  ? 1942 GLY A C     1 
ATOM   3905  O  O     . GLY A 1 1942 ? 176.561 220.331 204.211 1.00 0.82  ? 1942 GLY A O     1 
ATOM   3906  N  N     . ARG A 1 1943 ? 178.690 219.761 203.772 1.00 0.45  ? 1943 ARG A N     1 
ATOM   3907  C  CA    . ARG A 1 1943 ? 178.764 220.654 202.620 1.00 0.29  ? 1943 ARG A CA    1 
ATOM   3908  C  C     . ARG A 1 1943 ? 177.807 220.216 201.520 1.00 0.22  ? 1943 ARG A C     1 
ATOM   3909  O  O     . ARG A 1 1943 ? 177.187 221.053 200.857 1.00 0.49  ? 1943 ARG A O     1 
ATOM   3910  C  CB    . ARG A 1 1943 ? 180.201 220.721 202.104 1.00 0.78  ? 1943 ARG A CB    1 
ATOM   3911  C  CG    . ARG A 1 1943 ? 180.419 221.775 201.041 1.00 0.65  ? 1943 ARG A CG    1 
ATOM   3912  C  CD    . ARG A 1 1943 ? 181.897 222.054 200.836 1.00 2.98  ? 1943 ARG A CD    1 
ATOM   3913  N  NE    . ARG A 1 1943 ? 182.156 222.831 199.627 1.00 7.82  ? 1943 ARG A NE    1 
ATOM   3914  C  CZ    . ARG A 1 1943 ? 181.905 222.419 198.392 1.00 4.73  ? 1943 ARG A CZ    1 
ATOM   3915  N  NH1   . ARG A 1 1943 ? 181.436 221.207 198.147 1.00 1.92  ? 1943 ARG A NH1   1 
ATOM   3916  N  NH2   . ARG A 1 1943 ? 182.144 223.239 197.374 1.00 6.80  ? 1943 ARG A NH2   1 
ATOM   3917  N  N     . ILE A 1 1944 ? 177.679 218.906 201.309 1.00 0.16  ? 1944 ILE A N     1 
ATOM   3918  C  CA    . ILE A 1 1944 ? 176.703 218.397 200.349 1.00 0.18  ? 1944 ILE A CA    1 
ATOM   3919  C  C     . ILE A 1 1944 ? 175.289 218.753 200.790 1.00 0.21  ? 1944 ILE A C     1 
ATOM   3920  O  O     . ILE A 1 1944 ? 174.440 219.119 199.967 1.00 0.18  ? 1944 ILE A O     1 
ATOM   3921  C  CB    . ILE A 1 1944 ? 176.884 216.880 200.156 1.00 0.19  ? 1944 ILE A CB    1 
ATOM   3922  C  CG1   . ILE A 1 1944 ? 178.266 216.581 199.570 1.00 0.16  ? 1944 ILE A CG1   1 
ATOM   3923  C  CG2   . ILE A 1 1944 ? 175.784 216.308 199.281 1.00 0.09  ? 1944 ILE A CG2   1 
ATOM   3924  C  CD1   . ILE A 1 1944 ? 178.554 215.107 199.396 1.00 0.19  ? 1944 ILE A CD1   1 
ATOM   3925  N  N     . PHE A 1 1945 ? 175.013 218.657 202.093 1.00 0.21  ? 1945 PHE A N     1 
ATOM   3926  C  CA    . PHE A 1 1945 ? 173.704 219.047 202.603 1.00 0.19  ? 1945 PHE A CA    1 
ATOM   3927  C  C     . PHE A 1 1945 ? 173.445 220.532 202.383 1.00 0.17  ? 1945 PHE A C     1 
ATOM   3928  O  O     . PHE A 1 1945 ? 172.319 220.932 202.069 1.00 0.24  ? 1945 PHE A O     1 
ATOM   3929  C  CB    . PHE A 1 1945 ? 173.589 218.699 204.087 1.00 0.28  ? 1945 PHE A CB    1 
ATOM   3930  C  CG    . PHE A 1 1945 ? 173.438 217.232 204.355 1.00 0.18  ? 1945 PHE A CG    1 
ATOM   3931  C  CD1   . PHE A 1 1945 ? 172.700 216.431 203.499 1.00 0.12  ? 1945 PHE A CD1   1 
ATOM   3932  C  CD2   . PHE A 1 1945 ? 174.035 216.652 205.460 1.00 0.20  ? 1945 PHE A CD2   1 
ATOM   3933  C  CE1   . PHE A 1 1945 ? 172.562 215.080 203.743 1.00 0.08  ? 1945 PHE A CE1   1 
ATOM   3934  C  CE2   . PHE A 1 1945 ? 173.900 215.303 205.707 1.00 0.20  ? 1945 PHE A CE2   1 
ATOM   3935  C  CZ    . PHE A 1 1945 ? 173.162 214.514 204.847 1.00 0.12  ? 1945 PHE A CZ    1 
ATOM   3936  N  N     . VAL A 1 1946 ? 174.476 221.362 202.549 1.00 0.32  ? 1946 VAL A N     1 
ATOM   3937  C  CA    . VAL A 1 1946 ? 174.319 222.800 202.349 1.00 0.51  ? 1946 VAL A CA    1 
ATOM   3938  C  C     . VAL A 1 1946 ? 173.880 223.089 200.920 1.00 0.29  ? 1946 VAL A C     1 
ATOM   3939  O  O     . VAL A 1 1946 ? 172.965 223.884 200.680 1.00 0.95  ? 1946 VAL A O     1 
ATOM   3940  C  CB    . VAL A 1 1946 ? 175.628 223.535 202.702 1.00 0.39  ? 1946 VAL A CB    1 
ATOM   3941  C  CG1   . VAL A 1 1946 ? 175.566 224.986 202.259 1.00 0.18  ? 1946 VAL A CG1   1 
ATOM   3942  C  CG2   . VAL A 1 1946 ? 175.898 223.446 204.189 1.00 0.32  ? 1946 VAL A CG2   1 
ATOM   3943  N  N     . GLY A 1 1947 ? 174.522 222.437 199.949 1.00 0.21  ? 1947 GLY A N     1 
ATOM   3944  C  CA    . GLY A 1 1947 ? 174.100 222.594 198.568 1.00 0.23  ? 1947 GLY A CA    1 
ATOM   3945  C  C     . GLY A 1 1947 ? 172.698 222.071 198.320 1.00 0.32  ? 1947 GLY A C     1 
ATOM   3946  O  O     . GLY A 1 1947 ? 171.895 222.719 197.646 1.00 0.77  ? 1947 GLY A O     1 
ATOM   3947  N  N     . LEU A 1 1948 ? 172.384 220.894 198.865 1.00 0.16  ? 1948 LEU A N     1 
ATOM   3948  C  CA    . LEU A 1 1948 ? 171.053 220.323 198.679 1.00 0.33  ? 1948 LEU A CA    1 
ATOM   3949  C  C     . LEU A 1 1948 ? 169.978 221.200 199.308 1.00 0.42  ? 1948 LEU A C     1 
ATOM   3950  O  O     . LEU A 1 1948 ? 168.907 221.396 198.722 1.00 0.69  ? 1948 LEU A O     1 
ATOM   3951  C  CB    . LEU A 1 1948 ? 170.998 218.915 199.268 1.00 0.28  ? 1948 LEU A CB    1 
ATOM   3952  C  CG    . LEU A 1 1948 ? 171.717 217.783 198.535 1.00 0.21  ? 1948 LEU A CG    1 
ATOM   3953  C  CD1   . LEU A 1 1948 ? 171.785 216.552 199.425 1.00 0.05  ? 1948 LEU A CD1   1 
ATOM   3954  C  CD2   . LEU A 1 1948 ? 171.033 217.461 197.217 1.00 0.05  ? 1948 LEU A CD2   1 
ATOM   3955  N  N     . CYS A 1 1949 ? 170.242 221.732 200.504 1.00 0.28  ? 1949 CYS A N     1 
ATOM   3956  C  CA    . CYS A 1 1949 ? 169.230 222.511 201.212 1.00 0.60  ? 1949 CYS A CA    1 
ATOM   3957  C  C     . CYS A 1 1949 ? 168.897 223.806 200.481 1.00 0.83  ? 1949 CYS A C     1 
ATOM   3958  O  O     . CYS A 1 1949 ? 167.721 224.166 200.357 1.00 1.32  ? 1949 CYS A O     1 
ATOM   3959  C  CB    . CYS A 1 1949 ? 169.696 222.804 202.638 1.00 0.99  ? 1949 CYS A CB    1 
ATOM   3960  S  SG    . CYS A 1 1949 ? 169.586 221.395 203.760 1.00 0.74  ? 1949 CYS A SG    1 
ATOM   3961  N  N     . GLN A 1 1950 ? 169.911 224.522 199.997 1.00 1.14  ? 1950 GLN A N     1 
ATOM   3962  C  CA    . GLN A 1 1950 ? 169.653 225.805 199.352 1.00 1.75  ? 1950 GLN A CA    1 
ATOM   3963  C  C     . GLN A 1 1950 ? 169.061 225.625 197.960 1.00 1.44  ? 1950 GLN A C     1 
ATOM   3964  O  O     . GLN A 1 1950 ? 168.183 226.393 197.550 1.00 4.63  ? 1950 GLN A O     1 
ATOM   3965  C  CB    . GLN A 1 1950 ? 170.933 226.632 199.287 1.00 2.93  ? 1950 GLN A CB    1 
ATOM   3966  C  CG    . GLN A 1 1950 ? 171.578 226.886 200.629 1.00 2.78  ? 1950 GLN A CG    1 
ATOM   3967  C  CD    . GLN A 1 1950 ? 172.687 227.907 200.547 1.00 4.90  ? 1950 GLN A CD    1 
ATOM   3968  O  OE1   . GLN A 1 1950 ? 172.440 229.087 200.306 1.00 14.99 ? 1950 GLN A OE1   1 
ATOM   3969  N  NE2   . GLN A 1 1950 ? 173.920 227.459 200.740 1.00 5.68  ? 1950 GLN A NE2   1 
ATOM   3970  N  N     . VAL A 1 1951 ? 169.533 224.624 197.217 1.00 1.14  ? 1951 VAL A N     1 
ATOM   3971  C  CA    . VAL A 1 1951 ? 168.993 224.371 195.885 1.00 0.69  ? 1951 VAL A CA    1 
ATOM   3972  C  C     . VAL A 1 1951 ? 167.559 223.866 195.977 1.00 0.51  ? 1951 VAL A C     1 
ATOM   3973  O  O     . VAL A 1 1951 ? 166.706 224.222 195.156 1.00 1.32  ? 1951 VAL A O     1 
ATOM   3974  C  CB    . VAL A 1 1951 ? 169.898 223.385 195.120 1.00 1.03  ? 1951 VAL A CB    1 
ATOM   3975  C  CG1   . VAL A 1 1951 ? 169.206 222.875 193.867 1.00 0.46  ? 1951 VAL A CG1   1 
ATOM   3976  C  CG2   . VAL A 1 1951 ? 171.217 224.047 194.766 1.00 0.62  ? 1951 VAL A CG2   1 
ATOM   3977  N  N     . GLY A 1 1952 ? 167.264 223.053 196.985 1.00 1.01  ? 1952 GLY A N     1 
ATOM   3978  C  CA    . GLY A 1 1952 ? 166.001 222.351 197.033 1.00 0.64  ? 1952 GLY A CA    1 
ATOM   3979  C  C     . GLY A 1 1952 ? 166.033 221.016 196.338 1.00 0.28  ? 1952 GLY A C     1 
ATOM   3980  O  O     . GLY A 1 1952 ? 164.994 220.546 195.863 1.00 3.14  ? 1952 GLY A O     1 
ATOM   3981  N  N     . ALA A 1 1953 ? 167.198 220.392 196.254 1.00 0.26  ? 1953 ALA A N     1 
ATOM   3982  C  CA    . ALA A 1 1953 ? 167.395 219.161 195.510 1.00 0.32  ? 1953 ALA A CA    1 
ATOM   3983  C  C     . ALA A 1 1953 ? 167.356 217.954 196.438 1.00 0.09  ? 1953 ALA A C     1 
ATOM   3984  O  O     . ALA A 1 1953 ? 167.592 218.054 197.643 1.00 0.30  ? 1953 ALA A O     1 
ATOM   3985  C  CB    . ALA A 1 1953 ? 168.725 219.206 194.756 1.00 0.19  ? 1953 ALA A CB    1 
ATOM   3986  N  N     . TRP A 1 1954 ? 167.045 216.804 195.853 1.00 0.07  ? 1954 TRP A N     1 
ATOM   3987  C  CA    . TRP A 1 1954 ? 167.019 215.542 196.576 1.00 0.03  ? 1954 TRP A CA    1 
ATOM   3988  C  C     . TRP A 1 1954 ? 168.408 214.919 196.567 1.00 0.03  ? 1954 TRP A C     1 
ATOM   3989  O  O     . TRP A 1 1954 ? 169.062 214.863 195.522 1.00 0.04  ? 1954 TRP A O     1 
ATOM   3990  C  CB    . TRP A 1 1954 ? 166.011 214.578 195.951 1.00 0.04  ? 1954 TRP A CB    1 
ATOM   3991  C  CG    . TRP A 1 1954 ? 164.584 214.862 196.290 1.00 0.06  ? 1954 TRP A CG    1 
ATOM   3992  C  CD1   . TRP A 1 1954 ? 164.066 216.038 196.732 1.00 0.03  ? 1954 TRP A CD1   1 
ATOM   3993  C  CD2   . TRP A 1 1954 ? 163.488 213.950 196.195 1.00 0.05  ? 1954 TRP A CD2   1 
ATOM   3994  N  NE1   . TRP A 1 1954 ? 162.715 215.916 196.926 1.00 0.01  ? 1954 TRP A NE1   1 
ATOM   3995  C  CE2   . TRP A 1 1954 ? 162.335 214.642 196.601 1.00 0.02  ? 1954 TRP A CE2   1 
ATOM   3996  C  CE3   . TRP A 1 1954 ? 163.370 212.613 195.805 1.00 0.00  ? 1954 TRP A CE3   1 
ATOM   3997  C  CZ2   . TRP A 1 1954 ? 161.080 214.044 196.633 1.00 0.02  ? 1954 TRP A CZ2   1 
ATOM   3998  C  CZ3   . TRP A 1 1954 ? 162.126 212.023 195.836 1.00 0.02  ? 1954 TRP A CZ3   1 
ATOM   3999  C  CH2   . TRP A 1 1954 ? 160.997 212.737 196.244 1.00 0.02  ? 1954 TRP A CH2   1 
ATOM   4000  N  N     . GLY A 1 1955 ? 168.850 214.455 197.727 1.00 0.03  ? 1955 GLY A N     1 
ATOM   4001  C  CA    . GLY A 1 1955 ? 170.096 213.728 197.816 1.00 0.03  ? 1955 GLY A CA    1 
ATOM   4002  C  C     . GLY A 1 1955 ? 169.876 212.243 197.999 1.00 0.05  ? 1955 GLY A C     1 
ATOM   4003  O  O     . GLY A 1 1955 ? 169.369 211.808 199.037 1.00 0.03  ? 1955 GLY A O     1 
ATOM   4004  N  N     . CYS A 1 1956 ? 170.233 211.454 196.992 1.00 0.03  ? 1956 CYS A N     1 
ATOM   4005  C  CA    . CYS A 1 1956 ? 170.158 209.999 197.069 1.00 0.02  ? 1956 CYS A CA    1 
ATOM   4006  C  C     . CYS A 1 1956 ? 171.567 209.484 197.337 1.00 0.05  ? 1956 CYS A C     1 
ATOM   4007  O  O     . CYS A 1 1956 ? 172.401 209.421 196.432 1.00 0.25  ? 1956 CYS A O     1 
ATOM   4008  C  CB    . CYS A 1 1956 ? 169.572 209.410 195.789 1.00 0.08  ? 1956 CYS A CB    1 
ATOM   4009  S  SG    . CYS A 1 1956 ? 169.514 207.603 195.763 1.00 2.56  ? 1956 CYS A SG    1 
ATOM   4010  N  N     . PHE A 1 1957 ? 171.824 209.134 198.597 1.00 0.05  ? 1957 PHE A N     1 
ATOM   4011  C  CA    . PHE A 1 1957 ? 173.157 208.625 199.008 1.00 0.17  ? 1957 PHE A CA    1 
ATOM   4012  C  C     . PHE A 1 1957 ? 173.163 207.102 198.937 1.00 0.26  ? 1957 PHE A C     1 
ATOM   4013  O  O     . PHE A 1 1957 ? 172.698 206.439 199.882 1.00 0.40  ? 1957 PHE A O     1 
ATOM   4014  C  CB    . PHE A 1 1957 ? 173.443 209.193 200.402 1.00 0.09  ? 1957 PHE A CB    1 
ATOM   4015  C  CG    . PHE A 1 1957 ? 173.525 210.712 200.437 1.00 0.03  ? 1957 PHE A CG    1 
ATOM   4016  C  CD1   . PHE A 1 1957 ? 172.384 211.484 200.616 1.00 0.02  ? 1957 PHE A CD1   1 
ATOM   4017  C  CD2   . PHE A 1 1957 ? 174.745 211.363 200.286 1.00 0.04  ? 1957 PHE A CD2   1 
ATOM   4018  C  CE1   . PHE A 1 1957 ? 172.462 212.866 200.644 1.00 0.02  ? 1957 PHE A CE1   1 
ATOM   4019  C  CE2   . PHE A 1 1957 ? 174.816 212.746 200.316 1.00 0.04  ? 1957 PHE A CE2   1 
ATOM   4020  C  CZ    . PHE A 1 1957 ? 173.676 213.493 200.496 1.00 0.04  ? 1957 PHE A CZ    1 
ATOM   4021  N  N     . ASP A 1 1958 ? 173.701 206.557 197.844 1.00 0.76  ? 1958 ASP A N     1 
ATOM   4022  C  CA    . ASP A 1 1958 ? 173.758 205.083 197.650 1.00 0.59  ? 1958 ASP A CA    1 
ATOM   4023  C  C     . ASP A 1 1958 ? 174.957 204.507 198.409 1.00 1.43  ? 1958 ASP A C     1 
ATOM   4024  O  O     . ASP A 1 1958 ? 175.904 205.272 198.680 1.00 1.92  ? 1958 ASP A O     1 
ATOM   4025  C  CB    . ASP A 1 1958 ? 173.766 204.747 196.168 1.00 1.44  ? 1958 ASP A CB    1 
ATOM   4026  C  CG    . ASP A 1 1958 ? 172.618 205.347 195.370 1.00 4.14  ? 1958 ASP A CG    1 
ATOM   4027  O  OD1   . ASP A 1 1958 ? 171.453 205.067 195.717 1.00 5.32  ? 1958 ASP A OD1   1 
ATOM   4028  O  OD2   . ASP A 1 1958 ? 172.898 206.092 194.411 1.00 8.53  ? 1958 ASP A OD2   1 
ATOM   4029  N  N     . GLU A 1 1959 ? 174.915 203.210 198.732 1.00 2.33  ? 1959 GLU A N     1 
ATOM   4030  C  CA    . GLU A 1 1959 ? 176.005 202.576 199.522 1.00 1.70  ? 1959 GLU A CA    1 
ATOM   4031  C  C     . GLU A 1 1959 ? 176.284 203.468 200.740 1.00 1.12  ? 1959 GLU A C     1 
ATOM   4032  O  O     . GLU A 1 1959 ? 177.471 203.667 201.070 1.00 1.35  ? 1959 GLU A O     1 
ATOM   4033  C  CB    . GLU A 1 1959 ? 177.220 202.332 198.625 1.00 1.90  ? 1959 GLU A CB    1 
ATOM   4034  C  CG    . GLU A 1 1959 ? 176.918 201.394 197.461 1.00 6.64  ? 1959 GLU A CG    1 
ATOM   4035  C  CD    . GLU A 1 1959 ? 176.473 202.078 196.181 1.00 13.61 ? 1959 GLU A CD    1 
ATOM   4036  O  OE1   . GLU A 1 1959 ? 176.551 203.323 196.110 1.00 15.15 ? 1959 GLU A OE1   1 
ATOM   4037  O  OE2   . GLU A 1 1959 ? 176.028 201.362 195.259 1.00 17.15 ? 1959 GLU A OE2   1 
ATOM   4038  N  N     . PHE A 1 1960 ? 175.226 203.973 201.381 1.00 0.92  ? 1960 PHE A N     1 
ATOM   4039  C  CA    . PHE A 1 1960 ? 175.373 204.888 202.507 1.00 0.53  ? 1960 PHE A CA    1 
ATOM   4040  C  C     . PHE A 1 1960 ? 176.011 204.212 203.713 1.00 0.92  ? 1960 PHE A C     1 
ATOM   4041  O  O     . PHE A 1 1960 ? 176.626 204.888 204.546 1.00 0.71  ? 1960 PHE A O     1 
ATOM   4042  C  CB    . PHE A 1 1960 ? 174.006 205.473 202.858 1.00 0.29  ? 1960 PHE A CB    1 
ATOM   4043  C  CG    . PHE A 1 1960 ? 174.023 206.446 203.997 1.00 0.22  ? 1960 PHE A CG    1 
ATOM   4044  C  CD1   . PHE A 1 1960 ? 174.463 207.743 203.810 1.00 0.16  ? 1960 PHE A CD1   1 
ATOM   4045  C  CD2   . PHE A 1 1960 ? 173.541 206.080 205.241 1.00 0.14  ? 1960 PHE A CD2   1 
ATOM   4046  C  CE1   . PHE A 1 1960 ? 174.462 208.643 204.850 1.00 0.08  ? 1960 PHE A CE1   1 
ATOM   4047  C  CE2   . PHE A 1 1960 ? 173.532 206.981 206.282 1.00 0.19  ? 1960 PHE A CE2   1 
ATOM   4048  C  CZ    . PHE A 1 1960 ? 173.994 208.263 206.086 1.00 0.11  ? 1960 PHE A CZ    1 
ATOM   4049  N  N     . ASN A 1 1961 ? 175.899 202.889 203.818 1.00 1.41  ? 1961 ASN A N     1 
ATOM   4050  C  CA    . ASN A 1 1961 ? 176.534 202.161 204.907 1.00 0.73  ? 1961 ASN A CA    1 
ATOM   4051  C  C     . ASN A 1 1961 ? 178.007 201.877 204.648 1.00 0.67  ? 1961 ASN A C     1 
ATOM   4052  O  O     . ASN A 1 1961 ? 178.624 201.140 205.422 1.00 1.22  ? 1961 ASN A O     1 
ATOM   4053  C  CB    . ASN A 1 1961 ? 175.789 200.852 205.186 1.00 1.83  ? 1961 ASN A CB    1 
ATOM   4054  C  CG    . ASN A 1 1961 ? 175.648 199.977 203.956 1.00 3.10  ? 1961 ASN A CG    1 
ATOM   4055  O  OD1   . ASN A 1 1961 ? 176.054 200.352 202.858 1.00 3.73  ? 1961 ASN A OD1   1 
ATOM   4056  N  ND2   . ASN A 1 1961 ? 175.079 198.794 204.141 1.00 4.09  ? 1961 ASN A ND2   1 
ATOM   4057  N  N     . ARG A 1 1962 ? 178.579 202.421 203.574 1.00 1.53  ? 1962 ARG A N     1 
ATOM   4058  C  CA    . ARG A 1 1962 ? 180.021 202.353 203.381 1.00 1.42  ? 1962 ARG A CA    1 
ATOM   4059  C  C     . ARG A 1 1962 ? 180.756 203.448 204.141 1.00 1.11  ? 1962 ARG A C     1 
ATOM   4060  O  O     . ARG A 1 1962 ? 181.988 203.409 204.216 1.00 2.11  ? 1962 ARG A O     1 
ATOM   4061  C  CB    . ARG A 1 1962 ? 180.355 202.418 201.887 1.00 1.05  ? 1962 ARG A CB    1 
ATOM   4062  C  CG    . ARG A 1 1962 ? 179.796 201.233 201.111 1.00 2.36  ? 1962 ARG A CG    1 
ATOM   4063  C  CD    . ARG A 1 1962 ? 180.665 200.791 199.941 1.00 2.73  ? 1962 ARG A CD    1 
ATOM   4064  N  NE    . ARG A 1 1962 ? 180.927 201.853 198.978 1.00 2.07  ? 1962 ARG A NE    1 
ATOM   4065  C  CZ    . ARG A 1 1962 ? 182.136 202.218 198.575 1.00 1.25  ? 1962 ARG A CZ    1 
ATOM   4066  N  NH1   . ARG A 1 1962 ? 183.223 201.606 199.014 1.00 1.16  ? 1962 ARG A NH1   1 
ATOM   4067  N  NH2   . ARG A 1 1962 ? 182.256 203.212 197.701 1.00 1.68  ? 1962 ARG A NH2   1 
ATOM   4068  N  N     . LEU A 1 1963 ? 180.034 204.411 204.709 1.00 1.04  ? 1963 LEU A N     1 
ATOM   4069  C  CA    . LEU A 1 1963 ? 180.632 205.364 205.630 1.00 0.79  ? 1963 LEU A CA    1 
ATOM   4070  C  C     . LEU A 1 1963 ? 181.081 204.657 206.901 1.00 1.58  ? 1963 LEU A C     1 
ATOM   4071  O  O     . LEU A 1 1963 ? 180.550 203.610 207.275 1.00 1.90  ? 1963 LEU A O     1 
ATOM   4072  C  CB    . LEU A 1 1963 ? 179.636 206.466 205.992 1.00 0.90  ? 1963 LEU A CB    1 
ATOM   4073  C  CG    . LEU A 1 1963 ? 179.526 207.725 205.132 1.00 0.94  ? 1963 LEU A CG    1 
ATOM   4074  C  CD1   . LEU A 1 1963 ? 179.034 207.404 203.739 1.00 1.10  ? 1963 LEU A CD1   1 
ATOM   4075  C  CD2   . LEU A 1 1963 ? 178.613 208.735 205.804 1.00 0.43  ? 1963 LEU A CD2   1 
ATOM   4076  N  N     . GLU A 1 1964 ? 182.075 205.236 207.566 1.00 3.93  ? 1964 GLU A N     1 
ATOM   4077  C  CA    . GLU A 1 1964 ? 182.483 204.716 208.862 1.00 3.14  ? 1964 GLU A CA    1 
ATOM   4078  C  C     . GLU A 1 1964 ? 181.374 204.922 209.888 1.00 1.54  ? 1964 GLU A C     1 
ATOM   4079  O  O     . GLU A 1 1964 ? 180.563 205.845 209.782 1.00 1.90  ? 1964 GLU A O     1 
ATOM   4080  C  CB    . GLU A 1 1964 ? 183.775 205.389 209.323 1.00 3.99  ? 1964 GLU A CB    1 
ATOM   4081  C  CG    . GLU A 1 1964 ? 184.973 205.056 208.457 1.00 4.24  ? 1964 GLU A CG    1 
ATOM   4082  C  CD    . GLU A 1 1964 ? 185.360 203.590 208.555 1.00 19.53 ? 1964 GLU A CD    1 
ATOM   4083  O  OE1   . GLU A 1 1964 ? 185.164 202.995 209.635 1.00 20.69 ? 1964 GLU A OE1   1 
ATOM   4084  O  OE2   . GLU A 1 1964 ? 185.856 203.034 207.555 1.00 21.24 ? 1964 GLU A OE2   1 
ATOM   4085  N  N     . GLU A 1 1965 ? 181.337 204.037 210.887 1.00 1.82  ? 1965 GLU A N     1 
ATOM   4086  C  CA    . GLU A 1 1965 ? 180.284 204.108 211.896 1.00 1.11  ? 1965 GLU A CA    1 
ATOM   4087  C  C     . GLU A 1 1965 ? 180.347 205.415 212.675 1.00 0.94  ? 1965 GLU A C     1 
ATOM   4088  O  O     . GLU A 1 1965 ? 179.308 205.998 213.004 1.00 1.12  ? 1965 GLU A O     1 
ATOM   4089  C  CB    . GLU A 1 1965 ? 180.373 202.913 212.844 1.00 1.75  ? 1965 GLU A CB    1 
ATOM   4090  C  CG    . GLU A 1 1965 ? 180.089 201.581 212.182 1.00 5.18  ? 1965 GLU A CG    1 
ATOM   4091  C  CD    . GLU A 1 1965 ? 179.757 200.487 213.175 1.00 15.33 ? 1965 GLU A CD    1 
ATOM   4092  O  OE1   . GLU A 1 1965 ? 179.442 199.361 212.734 1.00 7.57  ? 1965 GLU A OE1   1 
ATOM   4093  O  OE2   . GLU A 1 1965 ? 179.808 200.751 214.394 1.00 21.70 ? 1965 GLU A OE2   1 
ATOM   4094  N  N     . ARG A 1 1966 ? 181.556 205.894 212.981 1.00 0.99  ? 1966 ARG A N     1 
ATOM   4095  C  CA    . ARG A 1 1966 ? 181.680 207.176 213.665 1.00 1.26  ? 1966 ARG A CA    1 
ATOM   4096  C  C     . ARG A 1 1966 ? 181.141 208.320 212.815 1.00 1.08  ? 1966 ARG A C     1 
ATOM   4097  O  O     . ARG A 1 1966 ? 180.546 209.261 213.351 1.00 0.81  ? 1966 ARG A O     1 
ATOM   4098  C  CB    . ARG A 1 1966 ? 183.138 207.431 214.059 1.00 3.39  ? 1966 ARG A CB    1 
ATOM   4099  C  CG    . ARG A 1 1966 ? 184.117 207.567 212.901 1.00 2.10  ? 1966 ARG A CG    1 
ATOM   4100  C  CD    . ARG A 1 1966 ? 185.555 207.493 213.392 1.00 5.63  ? 1966 ARG A CD    1 
ATOM   4101  N  NE    . ARG A 1 1966 ? 186.518 207.858 212.359 1.00 6.89  ? 1966 ARG A NE    1 
ATOM   4102  C  CZ    . ARG A 1 1966 ? 187.111 209.041 212.272 1.00 8.93  ? 1966 ARG A CZ    1 
ATOM   4103  N  NH1   . ARG A 1 1966 ? 186.859 210.006 213.141 1.00 7.37  ? 1966 ARG A NH1   1 
ATOM   4104  N  NH2   . ARG A 1 1966 ? 187.973 209.263 211.285 1.00 23.47 ? 1966 ARG A NH2   1 
ATOM   4105  N  N     . MET A 1 1967 ? 181.322 208.253 211.495 1.00 2.25  ? 1967 MET A N     1 
ATOM   4106  C  CA    . MET A 1 1967 ? 180.796 209.302 210.629 1.00 1.16  ? 1967 MET A CA    1 
ATOM   4107  C  C     . MET A 1 1967 ? 179.278 209.231 210.514 1.00 0.46  ? 1967 MET A C     1 
ATOM   4108  O  O     . MET A 1 1967 ? 178.620 210.270 210.404 1.00 0.30  ? 1967 MET A O     1 
ATOM   4109  C  CB    . MET A 1 1967 ? 181.442 209.215 209.247 1.00 0.95  ? 1967 MET A CB    1 
ATOM   4110  C  CG    . MET A 1 1967 ? 182.827 209.822 209.183 1.00 1.19  ? 1967 MET A CG    1 
ATOM   4111  S  SD    . MET A 1 1967 ? 182.988 211.300 210.202 1.00 8.49  ? 1967 MET A SD    1 
ATOM   4112  C  CE    . MET A 1 1967 ? 184.766 211.416 210.347 1.00 2.70  ? 1967 MET A CE    1 
ATOM   4113  N  N     . LEU A 1 1968 ? 178.710 208.025 210.538 1.00 0.87  ? 1968 LEU A N     1 
ATOM   4114  C  CA    . LEU A 1 1968 ? 177.258 207.889 210.486 1.00 0.64  ? 1968 LEU A CA    1 
ATOM   4115  C  C     . LEU A 1 1968 ? 176.602 208.532 211.699 1.00 0.55  ? 1968 LEU A C     1 
ATOM   4116  O  O     . LEU A 1 1968 ? 175.573 209.206 211.573 1.00 0.53  ? 1968 LEU A O     1 
ATOM   4117  C  CB    . LEU A 1 1968 ? 176.870 206.415 210.382 1.00 0.73  ? 1968 LEU A CB    1 
ATOM   4118  C  CG    . LEU A 1 1968 ? 177.293 205.711 209.094 1.00 0.85  ? 1968 LEU A CG    1 
ATOM   4119  C  CD1   . LEU A 1 1968 ? 177.137 204.206 209.226 1.00 1.58  ? 1968 LEU A CD1   1 
ATOM   4120  C  CD2   . LEU A 1 1968 ? 176.502 206.238 207.910 1.00 0.47  ? 1968 LEU A CD2   1 
ATOM   4121  N  N     . SER A 1 1969 ? 177.182 208.332 212.885 1.00 0.67  ? 1969 SER A N     1 
ATOM   4122  C  CA    . SER A 1 1969 ? 176.658 208.975 214.084 1.00 0.56  ? 1969 SER A CA    1 
ATOM   4123  C  C     . SER A 1 1969 ? 176.738 210.492 213.973 1.00 0.61  ? 1969 SER A C     1 
ATOM   4124  O  O     . SER A 1 1969 ? 175.769 211.196 214.278 1.00 1.29  ? 1969 SER A O     1 
ATOM   4125  C  CB    . SER A 1 1969 ? 177.418 208.484 215.315 1.00 0.49  ? 1969 SER A CB    1 
ATOM   4126  O  OG    . SER A 1 1969 ? 177.138 209.285 216.448 1.00 2.22  ? 1969 SER A OG    1 
ATOM   4127  N  N     . ALA A 1 1970 ? 177.880 211.009 213.516 1.00 0.83  ? 1970 ALA A N     1 
ATOM   4128  C  CA    . ALA A 1 1970 ? 178.050 212.453 213.396 1.00 0.95  ? 1970 ALA A CA    1 
ATOM   4129  C  C     . ALA A 1 1970 ? 177.076 213.048 212.386 1.00 0.52  ? 1970 ALA A C     1 
ATOM   4130  O  O     . ALA A 1 1970 ? 176.512 214.124 212.616 1.00 1.09  ? 1970 ALA A O     1 
ATOM   4131  C  CB    . ALA A 1 1970 ? 179.490 212.774 213.005 1.00 0.91  ? 1970 ALA A CB    1 
ATOM   4132  N  N     . VAL A 1 1971 ? 176.871 212.363 211.260 1.00 0.33  ? 1971 VAL A N     1 
ATOM   4133  C  CA    . VAL A 1 1971 ? 175.987 212.875 210.218 1.00 0.74  ? 1971 VAL A CA    1 
ATOM   4134  C  C     . VAL A 1 1971 ? 174.544 212.935 210.709 1.00 0.50  ? 1971 VAL A C     1 
ATOM   4135  O  O     . VAL A 1 1971 ? 173.775 213.810 210.292 1.00 0.41  ? 1971 VAL A O     1 
ATOM   4136  C  CB    . VAL A 1 1971 ? 176.140 212.020 208.943 1.00 0.38  ? 1971 VAL A CB    1 
ATOM   4137  C  CG1   . VAL A 1 1971 ? 174.939 212.167 208.022 1.00 0.39  ? 1971 VAL A CG1   1 
ATOM   4138  C  CG2   . VAL A 1 1971 ? 177.412 212.406 208.212 1.00 0.31  ? 1971 VAL A CG2   1 
ATOM   4139  N  N     . SER A 1 1972 ? 174.163 212.034 211.620 1.00 0.41  ? 1972 SER A N     1 
ATOM   4140  C  CA    . SER A 1 1972 ? 172.798 212.014 212.140 1.00 0.61  ? 1972 SER A CA    1 
ATOM   4141  C  C     . SER A 1 1972 ? 172.396 213.353 212.748 1.00 0.85  ? 1972 SER A C     1 
ATOM   4142  O  O     . SER A 1 1972 ? 171.216 213.716 212.714 1.00 0.69  ? 1972 SER A O     1 
ATOM   4143  C  CB    . SER A 1 1972 ? 172.652 210.898 213.173 1.00 0.46  ? 1972 SER A CB    1 
ATOM   4144  O  OG    . SER A 1 1972 ? 173.465 211.143 214.305 1.00 0.58  ? 1972 SER A OG    1 
ATOM   4145  N  N     . GLN A 1 1973 ? 173.353 214.093 213.310 1.00 2.07  ? 1973 GLN A N     1 
ATOM   4146  C  CA    . GLN A 1 1973 ? 173.042 215.418 213.835 1.00 1.39  ? 1973 GLN A CA    1 
ATOM   4147  C  C     . GLN A 1 1973 ? 172.639 216.377 212.720 1.00 1.71  ? 1973 GLN A C     1 
ATOM   4148  O  O     . GLN A 1 1973 ? 171.677 217.139 212.867 1.00 1.23  ? 1973 GLN A O     1 
ATOM   4149  C  CB    . GLN A 1 1973 ? 174.237 215.963 214.616 1.00 1.77  ? 1973 GLN A CB    1 
ATOM   4150  C  CG    . GLN A 1 1973 ? 173.901 217.110 215.555 1.00 5.21  ? 1973 GLN A CG    1 
ATOM   4151  C  CD    . GLN A 1 1973 ? 173.846 218.449 214.848 1.00 13.53 ? 1973 GLN A CD    1 
ATOM   4152  O  OE1   . GLN A 1 1973 ? 174.828 218.888 214.252 1.00 16.89 ? 1973 GLN A OE1   1 
ATOM   4153  N  NE2   . GLN A 1 1973 ? 172.694 219.107 214.913 1.00 13.25 ? 1973 GLN A NE2   1 
ATOM   4154  N  N     . GLN A 1 1974 ? 173.364 216.356 211.599 1.00 3.26  ? 1974 GLN A N     1 
ATOM   4155  C  CA    . GLN A 1 1974 ? 173.022 217.234 210.484 1.00 0.79  ? 1974 GLN A CA    1 
ATOM   4156  C  C     . GLN A 1 1974 ? 171.686 216.846 209.864 1.00 0.68  ? 1974 GLN A C     1 
ATOM   4157  O  O     . GLN A 1 1974 ? 170.886 217.718 209.507 1.00 1.35  ? 1974 GLN A O     1 
ATOM   4158  C  CB    . GLN A 1 1974 ? 174.129 217.205 209.431 1.00 0.65  ? 1974 GLN A CB    1 
ATOM   4159  C  CG    . GLN A 1 1974 ? 175.525 217.308 210.009 1.00 0.95  ? 1974 GLN A CG    1 
ATOM   4160  C  CD    . GLN A 1 1974 ? 176.604 217.278 208.947 1.00 0.56  ? 1974 GLN A CD    1 
ATOM   4161  O  OE1   . GLN A 1 1974 ? 177.445 218.172 208.876 1.00 0.90  ? 1974 GLN A OE1   1 
ATOM   4162  N  NE2   . GLN A 1 1974 ? 176.588 216.245 208.118 1.00 0.74  ? 1974 GLN A NE2   1 
ATOM   4163  N  N     . VAL A 1 1975 ? 171.429 215.545 209.721 1.00 1.01  ? 1975 VAL A N     1 
ATOM   4164  C  CA    . VAL A 1 1975 ? 170.163 215.099 209.149 1.00 0.78  ? 1975 VAL A CA    1 
ATOM   4165  C  C     . VAL A 1 1975 ? 169.004 215.536 210.032 1.00 1.13  ? 1975 VAL A C     1 
ATOM   4166  O  O     . VAL A 1 1975 ? 167.948 215.952 209.539 1.00 1.64  ? 1975 VAL A O     1 
ATOM   4167  C  CB    . VAL A 1 1975 ? 170.176 213.573 208.940 1.00 0.57  ? 1975 VAL A CB    1 
ATOM   4168  C  CG1   . VAL A 1 1975 ? 168.796 213.073 208.526 1.00 0.38  ? 1975 VAL A CG1   1 
ATOM   4169  C  CG2   . VAL A 1 1975 ? 171.219 213.188 207.905 1.00 0.17  ? 1975 VAL A CG2   1 
ATOM   4170  N  N     . GLN A 1 1976 ? 169.187 215.462 211.351 1.00 1.11  ? 1976 GLN A N     1 
ATOM   4171  C  CA    . GLN A 1 1976 ? 168.117 215.831 212.269 1.00 0.95  ? 1976 GLN A CA    1 
ATOM   4172  C  C     . GLN A 1 1976 ? 167.787 217.317 212.187 1.00 2.25  ? 1976 GLN A C     1 
ATOM   4173  O  O     . GLN A 1 1976 ? 166.609 217.692 212.134 1.00 5.66  ? 1976 GLN A O     1 
ATOM   4174  C  CB    . GLN A 1 1976 ? 168.495 215.439 213.694 1.00 2.48  ? 1976 GLN A CB    1 
ATOM   4175  C  CG    . GLN A 1 1976 ? 167.311 215.333 214.634 1.00 6.04  ? 1976 GLN A CG    1 
ATOM   4176  C  CD    . GLN A 1 1976 ? 167.673 214.680 215.950 1.00 9.92  ? 1976 GLN A CD    1 
ATOM   4177  O  OE1   . GLN A 1 1976 ? 167.160 213.614 216.289 1.00 14.40 ? 1976 GLN A OE1   1 
ATOM   4178  N  NE2   . GLN A 1 1976 ? 168.570 215.313 216.697 1.00 9.01  ? 1976 GLN A NE2   1 
ATOM   4179  N  N     . CYS A 1 1977 ? 168.805 218.182 212.165 1.00 2.64  ? 1977 CYS A N     1 
ATOM   4180  C  CA    . CYS A 1 1977 ? 168.536 219.619 212.194 1.00 2.24  ? 1977 CYS A CA    1 
ATOM   4181  C  C     . CYS A 1 1977 ? 167.853 220.078 210.911 1.00 2.34  ? 1977 CYS A C     1 
ATOM   4182  O  O     . CYS A 1 1977 ? 167.009 220.982 210.940 1.00 4.43  ? 1977 CYS A O     1 
ATOM   4183  C  CB    . CYS A 1 1977 ? 169.826 220.409 212.431 1.00 2.19  ? 1977 CYS A CB    1 
ATOM   4184  S  SG    . CYS A 1 1977 ? 171.071 220.293 211.136 1.00 32.26 ? 1977 CYS A SG    1 
ATOM   4185  N  N     . ILE A 1 1978 ? 168.204 219.471 209.776 1.00 1.44  ? 1978 ILE A N     1 
ATOM   4186  C  CA    . ILE A 1 1978 ? 167.503 219.768 208.531 1.00 1.78  ? 1978 ILE A CA    1 
ATOM   4187  C  C     . ILE A 1 1978 ? 166.041 219.354 208.635 1.00 1.89  ? 1978 ILE A C     1 
ATOM   4188  O  O     . ILE A 1 1978 ? 165.140 220.084 208.209 1.00 2.66  ? 1978 ILE A O     1 
ATOM   4189  C  CB    . ILE A 1 1978 ? 168.203 219.086 207.340 1.00 2.64  ? 1978 ILE A CB    1 
ATOM   4190  C  CG1   . ILE A 1 1978 ? 169.590 219.690 207.110 1.00 0.59  ? 1978 ILE A CG1   1 
ATOM   4191  C  CG2   . ILE A 1 1978 ? 167.353 219.184 206.083 1.00 1.17  ? 1978 ILE A CG2   1 
ATOM   4192  C  CD1   . ILE A 1 1978 ? 170.569 218.735 206.472 1.00 0.55  ? 1978 ILE A CD1   1 
ATOM   4193  N  N     . GLN A 1 1979 ? 165.785 218.178 209.212 1.00 2.08  ? 1979 GLN A N     1 
ATOM   4194  C  CA    . GLN A 1 1979 ? 164.419 217.678 209.311 1.00 2.23  ? 1979 GLN A CA    1 
ATOM   4195  C  C     . GLN A 1 1979 ? 163.564 218.564 210.211 1.00 3.88  ? 1979 GLN A C     1 
ATOM   4196  O  O     . GLN A 1 1979 ? 162.376 218.770 209.936 1.00 7.10  ? 1979 GLN A O     1 
ATOM   4197  C  CB    . GLN A 1 1979 ? 164.429 216.234 209.808 1.00 2.01  ? 1979 GLN A CB    1 
ATOM   4198  C  CG    . GLN A 1 1979 ? 164.810 215.235 208.730 1.00 1.73  ? 1979 GLN A CG    1 
ATOM   4199  C  CD    . GLN A 1 1979 ? 164.902 213.817 209.243 1.00 0.81  ? 1979 GLN A CD    1 
ATOM   4200  O  OE1   . GLN A 1 1979 ? 164.757 213.564 210.435 1.00 2.86  ? 1979 GLN A OE1   1 
ATOM   4201  N  NE2   . GLN A 1 1979 ? 165.143 212.880 208.340 1.00 0.42  ? 1979 GLN A NE2   1 
ATOM   4202  N  N     . GLU A 1 1980 ? 164.144 219.092 211.294 1.00 3.87  ? 1980 GLU A N     1 
ATOM   4203  C  CA    . GLU A 1 1980 ? 163.413 220.055 212.114 1.00 4.48  ? 1980 GLU A CA    1 
ATOM   4204  C  C     . GLU A 1 1980 ? 163.103 221.321 211.328 1.00 4.99  ? 1980 GLU A C     1 
ATOM   4205  O  O     . GLU A 1 1980 ? 162.017 221.896 211.465 1.00 12.64 ? 1980 GLU A O     1 
ATOM   4206  C  CB    . GLU A 1 1980 ? 164.200 220.394 213.383 1.00 7.85  ? 1980 GLU A CB    1 
ATOM   4207  C  CG    . GLU A 1 1980 ? 164.793 219.215 214.173 1.00 9.75  ? 1980 GLU A CG    1 
ATOM   4208  C  CD    . GLU A 1 1980 ? 163.840 218.045 214.421 1.00 21.30 ? 1980 GLU A CD    1 
ATOM   4209  O  OE1   . GLU A 1 1980 ? 164.331 216.989 214.874 1.00 23.90 ? 1980 GLU A OE1   1 
ATOM   4210  O  OE2   . GLU A 1 1980 ? 162.612 218.173 214.223 1.00 23.70 ? 1980 GLU A OE2   1 
ATOM   4211  N  N     . ALA A 1 1981 ? 164.047 221.773 210.502 1.00 4.68  ? 1981 ALA A N     1 
ATOM   4212  C  CA    . ALA A 1 1981 ? 163.791 222.929 209.651 1.00 7.79  ? 1981 ALA A CA    1 
ATOM   4213  C  C     . ALA A 1 1981 ? 162.694 222.634 208.636 1.00 10.75 ? 1981 ALA A C     1 
ATOM   4214  O  O     . ALA A 1 1981 ? 161.860 223.499 208.342 1.00 14.61 ? 1981 ALA A O     1 
ATOM   4215  C  CB    . ALA A 1 1981 ? 165.078 223.354 208.945 1.00 4.97  ? 1981 ALA A CB    1 
ATOM   4216  N  N     . LEU A 1 1982 ? 162.679 221.418 208.087 1.00 6.70  ? 1982 LEU A N     1 
ATOM   4217  C  CA    . LEU A 1 1982 ? 161.655 221.059 207.110 1.00 6.02  ? 1982 LEU A CA    1 
ATOM   4218  C  C     . LEU A 1 1982 ? 160.263 221.114 207.723 1.00 6.85  ? 1982 LEU A C     1 
ATOM   4219  O  O     . LEU A 1 1982 ? 159.299 221.513 207.058 1.00 10.83 ? 1982 LEU A O     1 
ATOM   4220  C  CB    . LEU A 1 1982 ? 161.939 219.671 206.541 1.00 6.16  ? 1982 LEU A CB    1 
ATOM   4221  C  CG    . LEU A 1 1982 ? 163.103 219.563 205.557 1.00 5.09  ? 1982 LEU A CG    1 
ATOM   4222  C  CD1   . LEU A 1 1982 ? 163.414 218.107 205.259 1.00 3.47  ? 1982 LEU A CD1   1 
ATOM   4223  C  CD2   . LEU A 1 1982 ? 162.790 220.322 204.283 1.00 6.20  ? 1982 LEU A CD2   1 
ATOM   4224  N  N     . ARG A 1 1983 ? 160.135 220.714 208.989 1.00 6.28  ? 1983 ARG A N     1 
ATOM   4225  C  CA    . ARG A 1 1983 ? 158.851 220.803 209.670 1.00 8.05  ? 1983 ARG A CA    1 
ATOM   4226  C  C     . ARG A 1 1983 ? 158.416 222.244 209.908 1.00 12.61 ? 1983 ARG A C     1 
ATOM   4227  O  O     . ARG A 1 1983 ? 157.221 222.490 210.108 1.00 17.07 ? 1983 ARG A O     1 
ATOM   4228  C  CB    . ARG A 1 1983 ? 158.908 220.038 210.992 1.00 4.13  ? 1983 ARG A CB    1 
ATOM   4229  C  CG    . ARG A 1 1983 ? 158.933 218.537 210.799 1.00 3.77  ? 1983 ARG A CG    1 
ATOM   4230  C  CD    . ARG A 1 1983 ? 159.276 217.788 212.068 1.00 2.86  ? 1983 ARG A CD    1 
ATOM   4231  N  NE    . ARG A 1 1983 ? 159.607 216.400 211.772 1.00 4.23  ? 1983 ARG A NE    1 
ATOM   4232  C  CZ    . ARG A 1 1983 ? 160.800 215.855 211.966 1.00 8.83  ? 1983 ARG A CZ    1 
ATOM   4233  N  NH1   . ARG A 1 1983 ? 161.797 216.544 212.497 1.00 6.33  ? 1983 ARG A NH1   1 
ATOM   4234  N  NH2   . ARG A 1 1983 ? 160.998 214.588 211.615 1.00 4.06  ? 1983 ARG A NH2   1 
ATOM   4235  N  N     . GLU A 1 1984 ? 159.349 223.199 209.892 1.00 14.21 ? 1984 GLU A N     1 
ATOM   4236  C  CA    . GLU A 1 1984 ? 158.963 224.599 210.014 1.00 14.62 ? 1984 GLU A CA    1 
ATOM   4237  C  C     . GLU A 1 1984 ? 158.230 225.091 208.770 1.00 16.85 ? 1984 GLU A C     1 
ATOM   4238  O  O     . GLU A 1 1984 ? 157.365 225.969 208.874 1.00 25.98 ? 1984 GLU A O     1 
ATOM   4239  C  CB    . GLU A 1 1984 ? 160.189 225.465 210.302 1.00 14.79 ? 1984 GLU A CB    1 
ATOM   4240  C  CG    . GLU A 1 1984 ? 160.622 225.439 211.759 1.00 17.93 ? 1984 GLU A CG    1 
ATOM   4241  C  CD    . GLU A 1 1984 ? 162.118 225.605 211.940 1.00 24.96 ? 1984 GLU A CD    1 
ATOM   4242  O  OE1   . GLU A 1 1984 ? 162.748 226.305 211.119 1.00 22.89 ? 1984 GLU A OE1   1 
ATOM   4243  O  OE2   . GLU A 1 1984 ? 162.667 225.034 212.907 1.00 20.49 ? 1984 GLU A OE2   1 
ATOM   4244  N  N     . HIS A 1 1985 ? 158.558 224.550 207.594 1.00 14.72 ? 1985 HIS A N     1 
ATOM   4245  C  CA    . HIS A 1 1985 ? 157.763 224.842 206.405 1.00 22.10 ? 1985 HIS A CA    1 
ATOM   4246  C  C     . HIS A 1 1985 ? 156.339 224.330 206.563 1.00 22.48 ? 1985 HIS A C     1 
ATOM   4247  O  O     . HIS A 1 1985 ? 155.378 225.015 206.194 1.00 28.86 ? 1985 HIS A O     1 
ATOM   4248  C  CB    . HIS A 1 1985 ? 158.401 224.216 205.163 1.00 16.88 ? 1985 HIS A CB    1 
ATOM   4249  C  CG    . HIS A 1 1985 ? 159.709 224.828 204.772 1.00 13.32 ? 1985 HIS A CG    1 
ATOM   4250  N  ND1   . HIS A 1 1985 ? 160.921 224.290 205.145 1.00 21.81 ? 1985 HIS A ND1   1 
ATOM   4251  C  CD2   . HIS A 1 1985 ? 159.994 225.918 204.022 1.00 14.41 ? 1985 HIS A CD2   1 
ATOM   4252  C  CE1   . HIS A 1 1985 ? 161.897 225.031 204.653 1.00 17.15 ? 1985 HIS A CE1   1 
ATOM   4253  N  NE2   . HIS A 1 1985 ? 161.362 226.026 203.968 1.00 15.76 ? 1985 HIS A NE2   1 
ATOM   4254  N  N     . SER A 1 1986 ? 156.188 223.124 207.110 1.00 18.84 ? 1986 SER A N     1 
ATOM   4255  C  CA    . SER A 1 1986 ? 154.890 222.474 207.220 1.00 16.57 ? 1986 SER A CA    1 
ATOM   4256  C  C     . SER A 1 1986 ? 153.991 223.103 208.276 1.00 21.08 ? 1986 SER A C     1 
ATOM   4257  O  O     . SER A 1 1986 ? 152.810 222.749 208.342 1.00 25.65 ? 1986 SER A O     1 
ATOM   4258  C  CB    . SER A 1 1986 ? 155.087 220.988 207.524 1.00 11.54 ? 1986 SER A CB    1 
ATOM   4259  O  OG    . SER A 1 1986 ? 155.351 220.777 208.897 1.00 10.33 ? 1986 SER A OG    1 
ATOM   4260  N  N     . ASN A 1 1987 ? 154.509 224.007 209.094 1.00 20.32 ? 1987 ASN A N     1 
ATOM   4261  C  CA    . ASN A 1 1987 ? 153.690 224.644 210.118 1.00 26.31 ? 1987 ASN A CA    1 
ATOM   4262  C  C     . ASN A 1 1987 ? 152.706 225.613 209.474 1.00 34.08 ? 1987 ASN A C     1 
ATOM   4263  O  O     . ASN A 1 1987 ? 153.131 226.526 208.753 1.00 33.54 ? 1987 ASN A O     1 
ATOM   4264  C  CB    . ASN A 1 1987 ? 154.570 225.376 211.127 1.00 26.54 ? 1987 ASN A CB    1 
ATOM   4265  C  CG    . ASN A 1 1987 ? 155.276 224.430 212.079 1.00 32.46 ? 1987 ASN A CG    1 
ATOM   4266  O  OD1   . ASN A 1 1987 ? 156.504 224.393 212.140 1.00 32.94 ? 1987 ASN A OD1   1 
ATOM   4267  N  ND2   . ASN A 1 1987 ? 154.498 223.659 212.830 1.00 27.84 ? 1987 ASN A ND2   1 
ATOM   4268  N  N     . PRO A 1 1988 ? 151.398 225.450 209.688 1.00 36.24 ? 1988 PRO A N     1 
ATOM   4269  C  CA    . PRO A 1 1988 ? 150.439 226.416 209.126 1.00 32.06 ? 1988 PRO A CA    1 
ATOM   4270  C  C     . PRO A 1 1988 ? 150.606 227.821 209.673 1.00 38.08 ? 1988 PRO A C     1 
ATOM   4271  O  O     . PRO A 1 1988 ? 150.292 228.791 208.972 1.00 38.56 ? 1988 PRO A O     1 
ATOM   4272  C  CB    . PRO A 1 1988 ? 149.078 225.816 209.505 1.00 31.33 ? 1988 PRO A CB    1 
ATOM   4273  C  CG    . PRO A 1 1988 ? 149.362 224.966 210.701 1.00 36.74 ? 1988 PRO A CG    1 
ATOM   4274  C  CD    . PRO A 1 1988 ? 150.732 224.398 210.474 1.00 33.08 ? 1988 PRO A CD    1 
ATOM   4275  N  N     . ASN A 1 1989 ? 151.085 227.960 210.913 1.00 36.11 ? 1989 ASN A N     1 
ATOM   4276  C  CA    . ASN A 1 1989 ? 151.255 229.286 211.499 1.00 33.21 ? 1989 ASN A CA    1 
ATOM   4277  C  C     . ASN A 1 1989 ? 152.313 230.088 210.751 1.00 38.35 ? 1989 ASN A C     1 
ATOM   4278  O  O     . ASN A 1 1989 ? 152.201 231.315 210.629 1.00 41.94 ? 1989 ASN A O     1 
ATOM   4279  C  CB    . ASN A 1 1989 ? 151.618 229.163 212.979 1.00 33.84 ? 1989 ASN A CB    1 
ATOM   4280  C  CG    . ASN A 1 1989 ? 152.740 228.172 213.225 1.00 37.31 ? 1989 ASN A CG    1 
ATOM   4281  O  OD1   . ASN A 1 1989 ? 153.875 228.382 212.799 1.00 36.74 ? 1989 ASN A OD1   1 
ATOM   4282  N  ND2   . ASN A 1 1989 ? 152.425 227.083 213.918 1.00 32.03 ? 1989 ASN A ND2   1 
ATOM   4283  N  N     . TYR A 1 1990 ? 153.349 229.417 210.254 1.00 37.09 ? 1990 TYR A N     1 
ATOM   4284  C  CA    . TYR A 1 1990 ? 154.389 230.098 209.495 1.00 35.42 ? 1990 TYR A CA    1 
ATOM   4285  C  C     . TYR A 1 1990 ? 153.820 230.689 208.210 1.00 35.54 ? 1990 TYR A C     1 
ATOM   4286  O  O     . TYR A 1 1990 ? 153.020 230.057 207.516 1.00 37.17 ? 1990 TYR A O     1 
ATOM   4287  C  CB    . TYR A 1 1990 ? 155.528 229.127 209.176 1.00 31.14 ? 1990 TYR A CB    1 
ATOM   4288  C  CG    . TYR A 1 1990 ? 156.322 229.496 207.944 1.00 28.66 ? 1990 TYR A CG    1 
ATOM   4289  C  CD1   . TYR A 1 1990 ? 157.284 230.496 207.987 1.00 32.85 ? 1990 TYR A CD1   1 
ATOM   4290  C  CD2   . TYR A 1 1990 ? 156.115 228.839 206.737 1.00 29.58 ? 1990 TYR A CD2   1 
ATOM   4291  C  CE1   . TYR A 1 1990 ? 158.014 230.835 206.863 1.00 29.00 ? 1990 TYR A CE1   1 
ATOM   4292  C  CE2   . TYR A 1 1990 ? 156.837 229.170 205.609 1.00 30.60 ? 1990 TYR A CE2   1 
ATOM   4293  C  CZ    . TYR A 1 1990 ? 157.781 230.171 205.677 1.00 33.49 ? 1990 TYR A CZ    1 
ATOM   4294  O  OH    . TYR A 1 1990 ? 158.507 230.503 204.556 1.00 31.16 ? 1990 TYR A OH    1 
ATOM   4295  N  N     . ASP A 1 1991 ? 154.241 231.911 207.899 1.00 36.37 ? 1991 ASP A N     1 
ATOM   4296  C  CA    . ASP A 1 1991 ? 153.810 232.615 206.703 1.00 34.31 ? 1991 ASP A CA    1 
ATOM   4297  C  C     . ASP A 1 1991 ? 154.992 232.826 205.765 1.00 37.55 ? 1991 ASP A C     1 
ATOM   4298  O  O     . ASP A 1 1991 ? 156.109 233.115 206.203 1.00 39.00 ? 1991 ASP A O     1 
ATOM   4299  C  CB    . ASP A 1 1991 ? 153.176 233.964 207.056 1.00 34.13 ? 1991 ASP A CB    1 
ATOM   4300  C  CG    . ASP A 1 1991 ? 154.126 234.878 207.805 1.00 40.53 ? 1991 ASP A CG    1 
ATOM   4301  O  OD1   . ASP A 1 1991 ? 154.658 234.455 208.853 1.00 35.72 ? 1991 ASP A OD1   1 
ATOM   4302  O  OD2   . ASP A 1 1991 ? 154.342 236.019 207.344 1.00 39.15 ? 1991 ASP A OD2   1 
ATOM   4303  N  N     . LYS A 1 1992 ? 154.729 232.681 204.463 1.00 36.78 ? 1992 LYS A N     1 
ATOM   4304  C  CA    . LYS A 1 1992 ? 155.797 232.782 203.472 1.00 36.15 ? 1992 LYS A CA    1 
ATOM   4305  C  C     . LYS A 1 1992 ? 156.453 234.157 203.480 1.00 37.35 ? 1992 LYS A C     1 
ATOM   4306  O  O     . LYS A 1 1992 ? 157.616 234.290 203.083 1.00 35.95 ? 1992 LYS A O     1 
ATOM   4307  C  CB    . LYS A 1 1992 ? 155.250 232.465 202.080 1.00 33.61 ? 1992 LYS A CB    1 
ATOM   4308  C  CG    . LYS A 1 1992 ? 154.661 231.069 201.948 1.00 31.44 ? 1992 LYS A CG    1 
ATOM   4309  C  CD    . LYS A 1 1992 ? 153.990 230.877 200.598 1.00 27.57 ? 1992 LYS A CD    1 
ATOM   4310  C  CE    . LYS A 1 1992 ? 152.834 231.847 200.413 1.00 31.43 ? 1992 LYS A CE    1 
ATOM   4311  N  NZ    . LYS A 1 1992 ? 152.143 231.647 199.110 1.00 35.79 ? 1992 LYS A NZ    1 
ATOM   4312  N  N     . THR A 1 1993 ? 155.733 235.185 203.924 1.00 36.86 ? 1993 THR A N     1 
ATOM   4313  C  CA    . THR A 1 1993 ? 156.282 236.539 204.003 1.00 34.59 ? 1993 THR A CA    1 
ATOM   4314  C  C     . THR A 1 1993 ? 156.876 236.796 205.390 1.00 37.64 ? 1993 THR A C     1 
ATOM   4315  O  O     . THR A 1 1993 ? 156.429 237.655 206.149 1.00 39.64 ? 1993 THR A O     1 
ATOM   4316  C  CB    . THR A 1 1993 ? 155.207 237.565 203.662 1.00 33.83 ? 1993 THR A CB    1 
ATOM   4317  O  OG1   . THR A 1 1993 ? 154.104 237.423 204.566 1.00 38.43 ? 1993 THR A OG1   1 
ATOM   4318  C  CG2   . THR A 1 1993 ? 154.716 237.367 202.236 1.00 30.20 ? 1993 THR A CG2   1 
ATOM   4319  N  N     . SER A 1 1994 ? 157.909 236.020 205.712 1.00 35.89 ? 1994 SER A N     1 
ATOM   4320  C  CA    . SER A 1 1994 ? 158.587 236.121 206.997 1.00 36.86 ? 1994 SER A CA    1 
ATOM   4321  C  C     . SER A 1 1994 ? 160.055 235.765 206.794 1.00 35.04 ? 1994 SER A C     1 
ATOM   4322  O  O     . SER A 1 1994 ? 160.541 235.657 205.663 1.00 35.45 ? 1994 SER A O     1 
ATOM   4323  C  CB    . SER A 1 1994 ? 157.913 235.222 208.041 1.00 32.32 ? 1994 SER A CB    1 
ATOM   4324  O  OG    . SER A 1 1994 ? 158.291 233.868 207.861 1.00 34.24 ? 1994 SER A OG    1 
ATOM   4325  N  N     . ALA A 1 1995 ? 160.766 235.585 207.901 1.00 29.07 ? 1995 ALA A N     1 
ATOM   4326  C  CA    . ALA A 1 1995 ? 162.161 235.171 207.834 1.00 30.67 ? 1995 ALA A CA    1 
ATOM   4327  C  C     . ALA A 1 1995 ? 162.252 233.750 207.290 1.00 32.34 ? 1995 ALA A C     1 
ATOM   4328  O  O     . ALA A 1 1995 ? 161.510 232.871 207.742 1.00 31.78 ? 1995 ALA A O     1 
ATOM   4329  C  CB    . ALA A 1 1995 ? 162.814 235.254 209.211 1.00 23.28 ? 1995 ALA A CB    1 
ATOM   4330  N  N     . PRO A 1 1996 ? 163.133 233.487 206.325 1.00 31.17 ? 1996 PRO A N     1 
ATOM   4331  C  CA    . PRO A 1 1996 ? 163.211 232.140 205.747 1.00 26.67 ? 1996 PRO A CA    1 
ATOM   4332  C  C     . PRO A 1 1996 ? 163.627 231.105 206.780 1.00 23.01 ? 1996 PRO A C     1 
ATOM   4333  O  O     . PRO A 1 1996 ? 164.380 231.392 207.713 1.00 23.69 ? 1996 PRO A O     1 
ATOM   4334  C  CB    . PRO A 1 1996 ? 164.271 232.288 204.648 1.00 24.40 ? 1996 PRO A CB    1 
ATOM   4335  C  CG    . PRO A 1 1996 ? 164.308 233.752 204.342 1.00 28.36 ? 1996 PRO A CG    1 
ATOM   4336  C  CD    . PRO A 1 1996 ? 164.032 234.434 205.648 1.00 23.52 ? 1996 PRO A CD    1 
ATOM   4337  N  N     . ILE A 1 1997 ? 163.115 229.887 206.605 1.00 20.51 ? 1997 ILE A N     1 
ATOM   4338  C  CA    . ILE A 1 1997 ? 163.516 228.774 207.456 1.00 13.33 ? 1997 ILE A CA    1 
ATOM   4339  C  C     . ILE A 1 1997 ? 164.999 228.499 207.257 1.00 14.71 ? 1997 ILE A C     1 
ATOM   4340  O  O     . ILE A 1 1997 ? 165.504 228.506 206.127 1.00 15.18 ? 1997 ILE A O     1 
ATOM   4341  C  CB    . ILE A 1 1997 ? 162.675 227.521 207.161 1.00 13.82 ? 1997 ILE A CB    1 
ATOM   4342  C  CG1   . ILE A 1 1997 ? 161.197 227.760 207.477 1.00 18.14 ? 1997 ILE A CG1   1 
ATOM   4343  C  CG2   . ILE A 1 1997 ? 163.202 226.329 207.926 1.00 13.51 ? 1997 ILE A CG2   1 
ATOM   4344  C  CD1   . ILE A 1 1997 ? 160.411 228.315 206.332 1.00 22.05 ? 1997 ILE A CD1   1 
ATOM   4345  N  N     . THR A 1 1998 ? 165.701 228.260 208.358 1.00 11.05 ? 1998 THR A N     1 
ATOM   4346  C  CA    . THR A 1 1998 ? 167.141 228.084 208.344 1.00 9.46  ? 1998 THR A CA    1 
ATOM   4347  C  C     . THR A 1 1998 ? 167.540 227.050 209.388 1.00 10.55 ? 1998 THR A C     1 
ATOM   4348  O  O     . THR A 1 1998 ? 167.011 227.033 210.502 1.00 17.98 ? 1998 THR A O     1 
ATOM   4349  C  CB    . THR A 1 1998 ? 167.851 229.425 208.609 1.00 11.57 ? 1998 THR A CB    1 
ATOM   4350  O  OG1   . THR A 1 1998 ? 167.728 230.270 207.459 1.00 12.97 ? 1998 THR A OG1   1 
ATOM   4351  C  CG2   . THR A 1 1998 ? 169.306 229.211 208.898 1.00 12.64 ? 1998 THR A CG2   1 
ATOM   4352  N  N     . CYS A 1 1999 ? 168.470 226.175 209.014 1.00 6.20  ? 1999 CYS A N     1 
ATOM   4353  C  CA    . CYS A 1 1999 ? 169.079 225.238 209.945 1.00 9.31  ? 1999 CYS A CA    1 
ATOM   4354  C  C     . CYS A 1 1999 ? 170.582 225.484 209.994 1.00 8.55  ? 1999 CYS A C     1 
ATOM   4355  O  O     . CYS A 1 1999 ? 171.161 226.102 209.098 1.00 8.23  ? 1999 CYS A O     1 
ATOM   4356  C  CB    . CYS A 1 1999 ? 168.792 223.782 209.555 1.00 5.31  ? 1999 CYS A CB    1 
ATOM   4357  S  SG    . CYS A 1 1999 ? 169.870 223.114 208.277 1.00 18.41 ? 1999 CYS A SG    1 
ATOM   4358  N  N     . GLU A 1 2000 ? 171.211 225.000 211.060 1.00 6.03  ? 2000 GLU A N     1 
ATOM   4359  C  CA    . GLU A 1 2000 ? 172.640 225.201 211.265 1.00 9.76  ? 2000 GLU A CA    1 
ATOM   4360  C  C     . GLU A 1 2000 ? 173.405 224.026 210.669 1.00 7.29  ? 2000 GLU A C     1 
ATOM   4361  O  O     . GLU A 1 2000 ? 173.341 222.905 211.184 1.00 4.76  ? 2000 GLU A O     1 
ATOM   4362  C  CB    . GLU A 1 2000 ? 172.958 225.369 212.748 1.00 11.36 ? 2000 GLU A CB    1 
ATOM   4363  C  CG    . GLU A 1 2000 ? 174.315 225.996 213.005 1.00 8.78  ? 2000 GLU A CG    1 
ATOM   4364  C  CD    . GLU A 1 2000 ? 174.683 226.016 214.473 1.00 19.53 ? 2000 GLU A CD    1 
ATOM   4365  O  OE1   . GLU A 1 2000 ? 173.866 225.560 215.299 1.00 24.32 ? 2000 GLU A OE1   1 
ATOM   4366  O  OE2   . GLU A 1 2000 ? 175.790 226.489 214.799 1.00 17.40 ? 2000 GLU A OE2   1 
ATOM   4367  N  N     . LEU A 1 2001 ? 174.134 224.285 209.588 1.00 5.34  ? 2001 LEU A N     1 
ATOM   4368  C  CA    . LEU A 1 2001 ? 174.999 223.298 208.957 1.00 4.39  ? 2001 LEU A CA    1 
ATOM   4369  C  C     . LEU A 1 2001 ? 176.424 223.826 208.977 1.00 6.61  ? 2001 LEU A C     1 
ATOM   4370  O  O     . LEU A 1 2001 ? 176.685 224.930 208.488 1.00 11.59 ? 2001 LEU A O     1 
ATOM   4371  C  CB    . LEU A 1 2001 ? 174.547 223.003 207.526 1.00 5.03  ? 2001 LEU A CB    1 
ATOM   4372  C  CG    . LEU A 1 2001 ? 173.289 222.145 207.389 1.00 1.22  ? 2001 LEU A CG    1 
ATOM   4373  C  CD1   . LEU A 1 2001 ? 172.898 221.982 205.928 1.00 0.84  ? 2001 LEU A CD1   1 
ATOM   4374  C  CD2   . LEU A 1 2001 ? 173.505 220.792 208.046 1.00 1.08  ? 2001 LEU A CD2   1 
ATOM   4375  N  N     . LEU A 1 2002 ? 177.338 223.038 209.543 1.00 6.28  ? 2002 LEU A N     1 
ATOM   4376  C  CA    . LEU A 1 2002 ? 178.755 223.395 209.625 1.00 4.87  ? 2002 LEU A CA    1 
ATOM   4377  C  C     . LEU A 1 2002 ? 178.946 224.754 210.296 1.00 7.84  ? 2002 LEU A C     1 
ATOM   4378  O  O     . LEU A 1 2002 ? 179.707 225.606 209.835 1.00 12.90 ? 2002 LEU A O     1 
ATOM   4379  C  CB    . LEU A 1 2002 ? 179.403 223.364 208.239 1.00 3.80  ? 2002 LEU A CB    1 
ATOM   4380  C  CG    . LEU A 1 2002 ? 179.393 221.997 207.553 1.00 4.18  ? 2002 LEU A CG    1 
ATOM   4381  C  CD1   . LEU A 1 2002 ? 180.082 222.057 206.202 1.00 0.98  ? 2002 LEU A CD1   1 
ATOM   4382  C  CD2   . LEU A 1 2002 ? 180.039 220.946 208.443 1.00 4.44  ? 2002 LEU A CD2   1 
ATOM   4383  N  N     . ASN A 1 2003 ? 178.220 224.952 211.400 1.00 8.02  ? 2003 ASN A N     1 
ATOM   4384  C  CA    . ASN A 1 2003 ? 178.307 226.164 212.220 1.00 9.87  ? 2003 ASN A CA    1 
ATOM   4385  C  C     . ASN A 1 2003 ? 177.935 227.417 211.428 1.00 9.53  ? 2003 ASN A C     1 
ATOM   4386  O  O     . ASN A 1 2003 ? 178.417 228.515 211.710 1.00 18.08 ? 2003 ASN A O     1 
ATOM   4387  C  CB    . ASN A 1 2003 ? 179.695 226.315 212.846 1.00 9.20  ? 2003 ASN A CB    1 
ATOM   4388  C  CG    . ASN A 1 2003 ? 180.130 225.079 213.600 1.00 14.24 ? 2003 ASN A CG    1 
ATOM   4389  O  OD1   . ASN A 1 2003 ? 181.110 224.430 213.237 1.00 18.00 ? 2003 ASN A OD1   1 
ATOM   4390  N  ND2   . ASN A 1 2003 ? 179.399 224.742 214.656 1.00 15.10 ? 2003 ASN A ND2   1 
ATOM   4391  N  N     . LYS A 1 2004 ? 177.067 227.255 210.434 1.00 9.11  ? 2004 LYS A N     1 
ATOM   4392  C  CA    . LYS A 1 2004 ? 176.569 228.380 209.658 1.00 6.90  ? 2004 LYS A CA    1 
ATOM   4393  C  C     . LYS A 1 2004 ? 175.065 228.237 209.491 1.00 9.50  ? 2004 LYS A C     1 
ATOM   4394  O  O     . LYS A 1 2004 ? 174.546 227.121 209.416 1.00 8.49  ? 2004 LYS A O     1 
ATOM   4395  C  CB    . LYS A 1 2004 ? 177.246 228.473 208.285 1.00 5.75  ? 2004 LYS A CB    1 
ATOM   4396  C  CG    . LYS A 1 2004 ? 178.742 228.693 208.340 1.00 14.03 ? 2004 LYS A CG    1 
ATOM   4397  C  CD    . LYS A 1 2004 ? 179.070 230.065 208.903 1.00 18.93 ? 2004 LYS A CD    1 
ATOM   4398  C  CE    . LYS A 1 2004 ? 180.564 230.329 208.892 1.00 20.39 ? 2004 LYS A CE    1 
ATOM   4399  N  NZ    . LYS A 1 2004 ? 180.886 231.657 209.483 1.00 24.34 ? 2004 LYS A NZ    1 
ATOM   4400  N  N     . GLN A 1 2005 ? 174.376 229.371 209.431 1.00 9.65  ? 2005 GLN A N     1 
ATOM   4401  C  CA    . GLN A 1 2005 ? 172.929 229.380 209.255 1.00 8.00  ? 2005 GLN A CA    1 
ATOM   4402  C  C     . GLN A 1 2005 ? 172.606 229.254 207.770 1.00 7.23  ? 2005 GLN A C     1 
ATOM   4403  O  O     . GLN A 1 2005 ? 172.899 230.162 206.986 1.00 12.46 ? 2005 GLN A O     1 
ATOM   4404  C  CB    . GLN A 1 2005 ? 172.335 230.658 209.841 1.00 7.17  ? 2005 GLN A CB    1 
ATOM   4405  C  CG    . GLN A 1 2005 ? 172.343 230.711 211.366 1.00 8.99  ? 2005 GLN A CG    1 
ATOM   4406  C  CD    . GLN A 1 2005 ? 171.707 229.493 212.011 1.00 11.22 ? 2005 GLN A CD    1 
ATOM   4407  O  OE1   . GLN A 1 2005 ? 170.544 229.181 211.766 1.00 12.49 ? 2005 GLN A OE1   1 
ATOM   4408  N  NE2   . GLN A 1 2005 ? 172.475 228.796 212.842 1.00 16.18 ? 2005 GLN A NE2   1 
ATOM   4409  N  N     . VAL A 1 2006 ? 171.999 228.134 207.385 1.00 5.10  ? 2006 VAL A N     1 
ATOM   4410  C  CA    . VAL A 1 2006 ? 171.766 227.795 205.986 1.00 5.95  ? 2006 VAL A CA    1 
ATOM   4411  C  C     . VAL A 1 2006 ? 170.266 227.739 205.734 1.00 5.28  ? 2006 VAL A C     1 
ATOM   4412  O  O     . VAL A 1 2006 ? 169.538 227.044 206.449 1.00 9.19  ? 2006 VAL A O     1 
ATOM   4413  C  CB    . VAL A 1 2006 ? 172.429 226.456 205.616 1.00 5.20  ? 2006 VAL A CB    1 
ATOM   4414  C  CG1   . VAL A 1 2006 ? 172.206 226.137 204.148 1.00 4.16  ? 2006 VAL A CG1   1 
ATOM   4415  C  CG2   . VAL A 1 2006 ? 173.914 226.489 205.939 1.00 5.05  ? 2006 VAL A CG2   1 
ATOM   4416  N  N     . LYS A 1 2007 ? 169.809 228.465 204.717 1.00 4.23  ? 2007 LYS A N     1 
ATOM   4417  C  CA    . LYS A 1 2007 ? 168.406 228.409 204.329 1.00 9.07  ? 2007 LYS A CA    1 
ATOM   4418  C  C     . LYS A 1 2007 ? 168.066 227.032 203.771 1.00 8.91  ? 2007 LYS A C     1 
ATOM   4419  O  O     . LYS A 1 2007 ? 168.866 226.414 203.064 1.00 4.13  ? 2007 LYS A O     1 
ATOM   4420  C  CB    . LYS A 1 2007 ? 168.092 229.485 203.291 1.00 7.62  ? 2007 LYS A CB    1 
ATOM   4421  C  CG    . LYS A 1 2007 ? 168.260 230.906 203.794 1.00 14.99 ? 2007 LYS A CG    1 
ATOM   4422  C  CD    . LYS A 1 2007 ? 167.864 231.917 202.729 1.00 25.32 ? 2007 LYS A CD    1 
ATOM   4423  C  CE    . LYS A 1 2007 ? 168.870 231.940 201.590 1.00 21.89 ? 2007 LYS A CE    1 
ATOM   4424  N  NZ    . LYS A 1 2007 ? 170.201 232.442 202.025 1.00 24.86 ? 2007 LYS A NZ    1 
ATOM   4425  N  N     . VAL A 1 2008 ? 166.869 226.552 204.093 1.00 8.28  ? 2008 VAL A N     1 
ATOM   4426  C  CA    . VAL A 1 2008 ? 166.421 225.222 203.704 1.00 3.48  ? 2008 VAL A CA    1 
ATOM   4427  C  C     . VAL A 1 2008 ? 165.224 225.366 202.777 1.00 5.70  ? 2008 VAL A C     1 
ATOM   4428  O  O     . VAL A 1 2008 ? 164.219 225.986 203.141 1.00 14.38 ? 2008 VAL A O     1 
ATOM   4429  C  CB    . VAL A 1 2008 ? 166.068 224.366 204.934 1.00 4.05  ? 2008 VAL A CB    1 
ATOM   4430  C  CG1   . VAL A 1 2008 ? 165.627 222.976 204.506 1.00 5.44  ? 2008 VAL A CG1   1 
ATOM   4431  C  CG2   . VAL A 1 2008 ? 167.255 224.286 205.881 1.00 3.11  ? 2008 VAL A CG2   1 
ATOM   4432  N  N     . SER A 1 2009 ? 165.337 224.808 201.578 1.00 7.41  ? 2009 SER A N     1 
ATOM   4433  C  CA    . SER A 1 2009 ? 164.172 224.825 200.705 1.00 6.28  ? 2009 SER A CA    1 
ATOM   4434  C  C     . SER A 1 2009 ? 163.252 223.655 201.039 1.00 7.74  ? 2009 SER A C     1 
ATOM   4435  O  O     . SER A 1 2009 ? 163.730 222.553 201.323 1.00 10.04 ? 2009 SER A O     1 
ATOM   4436  C  CB    . SER A 1 2009 ? 164.590 224.749 199.241 1.00 4.52  ? 2009 SER A CB    1 
ATOM   4437  O  OG    . SER A 1 2009 ? 163.461 224.724 198.384 1.00 9.84  ? 2009 SER A OG    1 
ATOM   4438  N  N     . PRO A 1 2010 ? 161.935 223.870 201.027 1.00 7.09  ? 2010 PRO A N     1 
ATOM   4439  C  CA    . PRO A 1 2010 ? 161.012 222.775 201.375 1.00 6.71  ? 2010 PRO A CA    1 
ATOM   4440  C  C     . PRO A 1 2010 ? 161.060 221.603 200.412 1.00 4.83  ? 2010 PRO A C     1 
ATOM   4441  O  O     . PRO A 1 2010 ? 160.615 220.508 200.772 1.00 8.75  ? 2010 PRO A O     1 
ATOM   4442  C  CB    . PRO A 1 2010 ? 159.636 223.459 201.357 1.00 7.80  ? 2010 PRO A CB    1 
ATOM   4443  C  CG    . PRO A 1 2010 ? 159.825 224.684 200.529 1.00 4.18  ? 2010 PRO A CG    1 
ATOM   4444  C  CD    . PRO A 1 2010 ? 161.226 225.133 200.776 1.00 6.49  ? 2010 PRO A CD    1 
ATOM   4445  N  N     . ASP A 1 2011 ? 161.582 221.793 199.201 1.00 4.36  ? 2011 ASP A N     1 
ATOM   4446  C  CA    . ASP A 1 2011 ? 161.591 220.733 198.203 1.00 2.57  ? 2011 ASP A CA    1 
ATOM   4447  C  C     . ASP A 1 2011 ? 162.717 219.727 198.392 1.00 1.54  ? 2011 ASP A C     1 
ATOM   4448  O  O     . ASP A 1 2011 ? 162.699 218.681 197.734 1.00 1.35  ? 2011 ASP A O     1 
ATOM   4449  C  CB    . ASP A 1 2011 ? 161.679 221.330 196.798 1.00 1.51  ? 2011 ASP A CB    1 
ATOM   4450  C  CG    . ASP A 1 2011 ? 160.362 221.916 196.328 1.00 8.19  ? 2011 ASP A CG    1 
ATOM   4451  O  OD1   . ASP A 1 2011 ? 159.412 221.975 197.137 1.00 9.79  ? 2011 ASP A OD1   1 
ATOM   4452  O  OD2   . ASP A 1 2011 ? 160.273 222.306 195.148 1.00 9.55  ? 2011 ASP A OD2   1 
ATOM   4453  N  N     . MET A 1 2012 ? 163.688 220.000 199.258 1.00 1.07  ? 2012 MET A N     1 
ATOM   4454  C  CA    . MET A 1 2012 ? 164.823 219.100 199.392 1.00 0.68  ? 2012 MET A CA    1 
ATOM   4455  C  C     . MET A 1 2012 ? 164.446 217.869 200.207 1.00 1.02  ? 2012 MET A C     1 
ATOM   4456  O  O     . MET A 1 2012 ? 163.561 217.915 201.065 1.00 4.09  ? 2012 MET A O     1 
ATOM   4457  C  CB    . MET A 1 2012 ? 166.014 219.828 200.021 1.00 0.62  ? 2012 MET A CB    1 
ATOM   4458  C  CG    . MET A 1 2012 ? 165.898 220.172 201.501 1.00 1.57  ? 2012 MET A CG    1 
ATOM   4459  S  SD    . MET A 1 2012 ? 166.291 218.808 202.615 1.00 16.39 ? 2012 MET A SD    1 
ATOM   4460  C  CE    . MET A 1 2012 ? 167.947 218.399 202.076 1.00 0.61  ? 2012 MET A CE    1 
ATOM   4461  N  N     . ALA A 1 2013 ? 165.133 216.762 199.936 1.00 0.17  ? 2013 ALA A N     1 
ATOM   4462  C  CA    . ALA A 1 2013 ? 164.877 215.506 200.620 1.00 0.03  ? 2013 ALA A CA    1 
ATOM   4463  C  C     . ALA A 1 2013 ? 166.166 214.702 200.667 1.00 0.04  ? 2013 ALA A C     1 
ATOM   4464  O  O     . ALA A 1 2013 ? 167.082 214.915 199.870 1.00 0.06  ? 2013 ALA A O     1 
ATOM   4465  C  CB    . ALA A 1 2013 ? 163.765 214.704 199.933 1.00 0.01  ? 2013 ALA A CB    1 
ATOM   4466  N  N     . ILE A 1 2014 ? 166.226 213.769 201.614 1.00 0.06  ? 2014 ILE A N     1 
ATOM   4467  C  CA    . ILE A 1 2014 ? 167.391 212.916 201.815 1.00 0.03  ? 2014 ILE A CA    1 
ATOM   4468  C  C     . ILE A 1 2014 ? 166.957 211.464 201.686 1.00 0.03  ? 2014 ILE A C     1 
ATOM   4469  O  O     . ILE A 1 2014 ? 166.003 211.034 202.343 1.00 0.04  ? 2014 ILE A O     1 
ATOM   4470  C  CB    . ILE A 1 2014 ? 168.055 213.167 203.182 1.00 0.04  ? 2014 ILE A CB    1 
ATOM   4471  C  CG1   . ILE A 1 2014 ? 168.309 214.660 203.392 1.00 0.04  ? 2014 ILE A CG1   1 
ATOM   4472  C  CG2   . ILE A 1 2014 ? 169.351 212.387 203.298 1.00 0.03  ? 2014 ILE A CG2   1 
ATOM   4473  C  CD1   . ILE A 1 2014 ? 168.920 214.995 204.735 1.00 0.12  ? 2014 ILE A CD1   1 
ATOM   4474  N  N     . PHE A 1 2015 ? 167.653 210.713 200.841 1.00 0.03  ? 2015 PHE A N     1 
ATOM   4475  C  CA    . PHE A 1 2015 ? 167.394 209.294 200.653 1.00 0.04  ? 2015 PHE A CA    1 
ATOM   4476  C  C     . PHE A 1 2015 ? 168.702 208.526 200.746 1.00 0.10  ? 2015 PHE A C     1 
ATOM   4477  O  O     . PHE A 1 2015 ? 169.739 208.989 200.265 1.00 0.03  ? 2015 PHE A O     1 
ATOM   4478  C  CB    . PHE A 1 2015 ? 166.724 209.014 199.303 1.00 0.00  ? 2015 PHE A CB    1 
ATOM   4479  C  CG    . PHE A 1 2015 ? 165.292 209.444 199.234 1.00 0.02  ? 2015 PHE A CG    1 
ATOM   4480  C  CD1   . PHE A 1 2015 ? 164.962 210.753 198.920 1.00 0.00  ? 2015 PHE A CD1   1 
ATOM   4481  C  CD2   . PHE A 1 2015 ? 164.271 208.542 199.477 1.00 0.02  ? 2015 PHE A CD2   1 
ATOM   4482  C  CE1   . PHE A 1 2015 ? 163.647 211.152 198.853 1.00 0.03  ? 2015 PHE A CE1   1 
ATOM   4483  C  CE2   . PHE A 1 2015 ? 162.950 208.937 199.410 1.00 0.01  ? 2015 PHE A CE2   1 
ATOM   4484  C  CZ    . PHE A 1 2015 ? 162.638 210.244 199.098 1.00 0.03  ? 2015 PHE A CZ    1 
ATOM   4485  N  N     . ILE A 1 2016 ? 168.636 207.356 201.373 1.00 0.02  ? 2016 ILE A N     1 
ATOM   4486  C  CA    . ILE A 1 2016 ? 169.834 206.481 201.492 1.00 0.03  ? 2016 ILE A CA    1 
ATOM   4487  C  C     . ILE A 1 2016 ? 169.426 205.090 200.992 1.00 0.05  ? 2016 ILE A C     1 
ATOM   4488  O  O     . ILE A 1 2016 ? 168.346 204.611 201.381 1.00 0.07  ? 2016 ILE A O     1 
ATOM   4489  C  CB    . ILE A 1 2016 ? 170.362 206.461 202.938 1.00 0.07  ? 2016 ILE A CB    1 
ATOM   4490  C  CG1   . ILE A 1 2016 ? 169.329 205.894 203.913 1.00 0.05  ? 2016 ILE A CG1   1 
ATOM   4491  C  CG2   . ILE A 1 2016 ? 170.834 207.852 203.365 1.00 0.02  ? 2016 ILE A CG2   1 
ATOM   4492  C  CD1   . ILE A 1 2016 ? 169.794 205.846 205.357 1.00 0.04  ? 2016 ILE A CD1   1 
ATOM   4493  N  N     . THR A 1 2017 ? 170.241 204.496 200.123 1.00 0.32  ? 2017 THR A N     1 
ATOM   4494  C  CA    . THR A 1 2017 ? 169.961 203.137 199.621 1.00 0.57  ? 2017 THR A CA    1 
ATOM   4495  C  C     . THR A 1 2017 ? 171.084 202.256 200.097 1.00 0.90  ? 2017 THR A C     1 
ATOM   4496  O  O     . THR A 1 2017 ? 172.253 202.654 199.927 1.00 1.63  ? 2017 THR A O     1 
ATOM   4497  C  CB    . THR A 1 2017 ? 169.832 203.152 198.097 1.00 0.87  ? 2017 THR A CB    1 
ATOM   4498  O  OG1   . THR A 1 2017 ? 171.123 203.501 197.608 1.00 3.57  ? 2017 THR A OG1   1 
ATOM   4499  C  CG2   . THR A 1 2017 ? 168.800 204.153 197.609 1.00 0.50  ? 2017 THR A CG2   1 
ATOM   4500  N  N     . MET A 1 2018 ? 170.761 201.109 200.692 1.00 1.32  ? 2018 MET A N     1 
ATOM   4501  C  CA    . MET A 1 2018 ? 171.838 200.281 201.285 1.00 1.11  ? 2018 MET A CA    1 
ATOM   4502  C  C     . MET A 1 2018 ? 171.560 198.786 201.112 1.00 1.13  ? 2018 MET A C     1 
ATOM   4503  O  O     . MET A 1 2018 ? 170.380 198.411 200.966 1.00 1.16  ? 2018 MET A O     1 
ATOM   4504  C  CB    . MET A 1 2018 ? 171.959 200.542 202.790 1.00 2.20  ? 2018 MET A CB    1 
ATOM   4505  C  CG    . MET A 1 2018 ? 172.247 201.980 203.163 1.00 3.50  ? 2018 MET A CG    1 
ATOM   4506  S  SD    . MET A 1 2018 ? 172.193 202.210 204.951 1.00 12.11 ? 2018 MET A SD    1 
ATOM   4507  C  CE    . MET A 1 2018 ? 170.481 201.789 205.301 1.00 3.47  ? 2018 MET A CE    1 
ATOM   4508  N  N     . ASN A 1 2019 ? 172.618 197.978 201.107 1.00 5.67  ? 2019 ASN A N     1 
ATOM   4509  C  CA    . ASN A 1 2019 ? 172.464 196.499 201.078 1.00 4.41  ? 2019 ASN A CA    1 
ATOM   4510  C  C     . ASN A 1 2019 ? 172.849 196.004 202.473 1.00 5.25  ? 2019 ASN A C     1 
ATOM   4511  O  O     . ASN A 1 2019 ? 174.056 195.789 202.718 1.00 13.56 ? 2019 ASN A O     1 
ATOM   4512  C  CB    . ASN A 1 2019 ? 173.271 195.859 199.956 1.00 4.15  ? 2019 ASN A CB    1 
ATOM   4513  C  CG    . ASN A 1 2019 ? 173.013 194.376 199.836 1.00 7.05  ? 2019 ASN A CG    1 
ATOM   4514  O  OD1   . ASN A 1 2019 ? 172.312 193.791 200.669 1.00 6.37  ? 2019 ASN A OD1   1 
ATOM   4515  N  ND2   . ASN A 1 2019 ? 173.575 193.750 198.812 1.00 8.07  ? 2019 ASN A ND2   1 
ATOM   4516  N  N     . PRO A 1 2020 ? 171.889 195.835 203.404 1.00 6.95  ? 2020 PRO A N     1 
ATOM   4517  C  CA    . PRO A 1 2020 ? 172.217 195.460 204.775 1.00 10.02 ? 2020 PRO A CA    1 
ATOM   4518  C  C     . PRO A 1 2020 ? 172.798 194.058 204.875 1.00 12.98 ? 2020 PRO A C     1 
ATOM   4519  O  O     . PRO A 1 2020 ? 173.269 193.679 205.962 1.00 16.50 ? 2020 PRO A O     1 
ATOM   4520  C  CB    . PRO A 1 2020 ? 170.862 195.583 205.501 1.00 7.98  ? 2020 PRO A CB    1 
ATOM   4521  C  CG    . PRO A 1 2020 ? 170.003 196.400 204.563 1.00 5.77  ? 2020 PRO A CG    1 
ATOM   4522  C  CD    . PRO A 1 2020 ? 170.467 196.007 203.174 1.00 6.46  ? 2020 PRO A CD    1 
ATOM   4523  N  N     . GLY A 1 2021 ? 172.767 193.306 203.774 1.00 13.70 ? 2021 GLY A N     1 
ATOM   4524  C  CA    . GLY A 1 2021 ? 173.266 191.919 203.784 1.00 10.66 ? 2021 GLY A CA    1 
ATOM   4525  C  C     . GLY A 1 2021 ? 174.752 191.851 203.502 1.00 15.83 ? 2021 GLY A C     1 
ATOM   4526  O  O     . GLY A 1 2021 ? 175.336 190.765 203.686 1.00 31.39 ? 2021 GLY A O     1 
ATOM   4527  N  N     . TYR A 1 2022 ? 175.349 192.958 203.061 1.00 12.15 ? 2022 TYR A N     1 
ATOM   4528  C  CA    . TYR A 1 2022 ? 176.792 192.948 202.700 1.00 10.72 ? 2022 TYR A CA    1 
ATOM   4529  C  C     . TYR A 1 2022 ? 177.614 192.926 203.987 1.00 11.13 ? 2022 TYR A C     1 
ATOM   4530  O  O     . TYR A 1 2022 ? 177.467 193.844 204.820 1.00 13.67 ? 2022 TYR A O     1 
ATOM   4531  C  CB    . TYR A 1 2022 ? 177.123 194.126 201.773 1.00 9.99  ? 2022 TYR A CB    1 
ATOM   4532  C  CG    . TYR A 1 2022 ? 177.021 193.794 200.291 1.00 12.46 ? 2022 TYR A CG    1 
ATOM   4533  C  CD1   . TYR A 1 2022 ? 176.292 192.695 199.850 1.00 12.68 ? 2022 TYR A CD1   1 
ATOM   4534  C  CD2   . TYR A 1 2022 ? 177.629 194.591 199.330 1.00 9.93  ? 2022 TYR A CD2   1 
ATOM   4535  C  CE1   . TYR A 1 2022 ? 176.193 192.387 198.504 1.00 11.85 ? 2022 TYR A CE1   1 
ATOM   4536  C  CE2   . TYR A 1 2022 ? 177.534 194.296 197.980 1.00 11.56 ? 2022 TYR A CE2   1 
ATOM   4537  C  CZ    . TYR A 1 2022 ? 176.811 193.193 197.565 1.00 16.51 ? 2022 TYR A CZ    1 
ATOM   4538  O  OH    . TYR A 1 2022 ? 176.711 192.896 196.237 1.00 14.04 ? 2022 TYR A OH    1 
ATOM   4539  N  N     . ALA A 1 2023 ? 178.446 191.894 204.152 1.00 15.43 ? 2023 ALA A N     1 
ATOM   4540  C  CA    . ALA A 1 2023 ? 179.326 191.806 205.341 1.00 17.43 ? 2023 ALA A CA    1 
ATOM   4541  C  C     . ALA A 1 2023 ? 180.422 192.869 205.243 1.00 13.89 ? 2023 ALA A C     1 
ATOM   4542  O  O     . ALA A 1 2023 ? 180.795 193.244 204.111 1.00 12.85 ? 2023 ALA A O     1 
ATOM   4543  C  CB    . ALA A 1 2023 ? 179.908 190.419 205.447 1.00 18.72 ? 2023 ALA A CB    1 
ATOM   4544  N  N     . GLY A 1 2024 ? 180.921 193.342 206.388 1.00 13.04 ? 2024 GLY A N     1 
ATOM   4545  C  CA    . GLY A 1 2024 ? 181.926 194.379 206.381 1.00 11.72 ? 2024 GLY A CA    1 
ATOM   4546  C  C     . GLY A 1 2024 ? 181.375 195.788 206.326 1.00 12.80 ? 2024 GLY A C     1 
ATOM   4547  O  O     . GLY A 1 2024 ? 182.130 196.741 206.549 1.00 17.73 ? 2024 GLY A O     1 
ATOM   4548  N  N     . ARG A 1 2025 ? 180.087 195.946 206.035 1.00 9.60  ? 2025 ARG A N     1 
ATOM   4549  C  CA    . ARG A 1 2025 ? 179.475 197.262 206.017 1.00 6.76  ? 2025 ARG A CA    1 
ATOM   4550  C  C     . ARG A 1 2025 ? 179.307 197.790 207.440 1.00 6.77  ? 2025 ARG A C     1 
ATOM   4551  O  O     . ARG A 1 2025 ? 179.352 197.045 208.422 1.00 15.69 ? 2025 ARG A O     1 
ATOM   4552  C  CB    . ARG A 1 2025 ? 178.122 197.218 205.308 1.00 9.96  ? 2025 ARG A CB    1 
ATOM   4553  C  CG    . ARG A 1 2025 ? 178.202 196.840 203.847 1.00 5.05  ? 2025 ARG A CG    1 
ATOM   4554  C  CD    . ARG A 1 2025 ? 178.696 197.996 203.000 1.00 4.47  ? 2025 ARG A CD    1 
ATOM   4555  N  NE    . ARG A 1 2025 ? 179.222 197.537 201.721 1.00 9.38  ? 2025 ARG A NE    1 
ATOM   4556  C  CZ    . ARG A 1 2025 ? 178.674 197.801 200.544 1.00 8.70  ? 2025 ARG A CZ    1 
ATOM   4557  N  NH1   . ARG A 1 2025 ? 177.554 198.495 200.443 1.00 8.81  ? 2025 ARG A NH1   1 
ATOM   4558  N  NH2   . ARG A 1 2025 ? 179.260 197.350 199.441 1.00 9.38  ? 2025 ARG A NH2   1 
ATOM   4559  N  N     . SER A 1 2026 ? 179.111 199.097 207.540 1.00 4.03  ? 2026 SER A N     1 
ATOM   4560  C  CA    . SER A 1 2026 ? 178.906 199.746 208.824 1.00 3.87  ? 2026 SER A CA    1 
ATOM   4561  C  C     . SER A 1 2026 ? 177.448 199.633 209.242 1.00 5.47  ? 2026 SER A C     1 
ATOM   4562  O  O     . SER A 1 2026 ? 176.538 199.810 208.428 1.00 7.08  ? 2026 SER A O     1 
ATOM   4563  C  CB    . SER A 1 2026 ? 179.310 201.217 208.759 1.00 2.81  ? 2026 SER A CB    1 
ATOM   4564  O  OG    . SER A 1 2026 ? 180.592 201.379 208.185 1.00 3.64  ? 2026 SER A OG    1 
ATOM   4565  N  N     . ASN A 1 2027 ? 177.233 199.334 210.518 1.00 6.24  ? 2027 ASN A N     1 
ATOM   4566  C  CA    . ASN A 1 2027 ? 175.891 199.336 211.076 1.00 5.44  ? 2027 ASN A CA    1 
ATOM   4567  C  C     . ASN A 1 2027 ? 175.486 200.761 211.417 1.00 4.37  ? 2027 ASN A C     1 
ATOM   4568  O  O     . ASN A 1 2027 ? 176.253 201.502 212.038 1.00 15.28 ? 2027 ASN A O     1 
ATOM   4569  C  CB    . ASN A 1 2027 ? 175.825 198.448 212.318 1.00 4.99  ? 2027 ASN A CB    1 
ATOM   4570  C  CG    . ASN A 1 2027 ? 176.039 196.986 211.997 1.00 10.79 ? 2027 ASN A CG    1 
ATOM   4571  O  OD1   . ASN A 1 2027 ? 175.413 196.440 211.087 1.00 10.92 ? 2027 ASN A OD1   1 
ATOM   4572  N  ND2   . ASN A 1 2027 ? 176.931 196.340 212.739 1.00 13.46 ? 2027 ASN A ND2   1 
ATOM   4573  N  N     . LEU A 1 2028 ? 174.297 201.151 210.994 1.00 2.77  ? 2028 LEU A N     1 
ATOM   4574  C  CA    . LEU A 1 2028 ? 173.809 202.485 211.306 1.00 3.18  ? 2028 LEU A CA    1 
ATOM   4575  C  C     . LEU A 1 2028 ? 173.418 202.562 212.777 1.00 6.30  ? 2028 LEU A C     1 
ATOM   4576  O  O     . LEU A 1 2028 ? 172.737 201.661 213.278 1.00 16.40 ? 2028 LEU A O     1 
ATOM   4577  C  CB    . LEU A 1 2028 ? 172.615 202.845 210.428 1.00 2.33  ? 2028 LEU A CB    1 
ATOM   4578  C  CG    . LEU A 1 2028 ? 172.896 203.568 209.110 1.00 2.90  ? 2028 LEU A CG    1 
ATOM   4579  C  CD1   . LEU A 1 2028 ? 173.827 202.766 208.210 1.00 0.79  ? 2028 LEU A CD1   1 
ATOM   4580  C  CD2   . LEU A 1 2028 ? 171.597 203.909 208.405 1.00 1.57  ? 2028 LEU A CD2   1 
ATOM   4581  N  N     . PRO A 1 2029 ? 173.840 203.596 213.500 1.00 5.15  ? 2029 PRO A N     1 
ATOM   4582  C  CA    . PRO A 1 2029 ? 173.335 203.788 214.863 1.00 2.93  ? 2029 PRO A CA    1 
ATOM   4583  C  C     . PRO A 1 2029 ? 171.835 204.045 214.854 1.00 2.10  ? 2029 PRO A C     1 
ATOM   4584  O  O     . PRO A 1 2029 ? 171.282 204.586 213.895 1.00 3.74  ? 2029 PRO A O     1 
ATOM   4585  C  CB    . PRO A 1 2029 ? 174.116 205.007 215.367 1.00 2.47  ? 2029 PRO A CB    1 
ATOM   4586  C  CG    . PRO A 1 2029 ? 174.618 205.687 214.135 1.00 1.67  ? 2029 PRO A CG    1 
ATOM   4587  C  CD    . PRO A 1 2029 ? 174.850 204.601 213.132 1.00 2.63  ? 2029 PRO A CD    1 
ATOM   4588  N  N     . ASP A 1 2030 ? 171.177 203.642 215.944 1.00 3.11  ? 2030 ASP A N     1 
ATOM   4589  C  CA    . ASP A 1 2030 ? 169.720 203.708 216.003 1.00 2.46  ? 2030 ASP A CA    1 
ATOM   4590  C  C     . ASP A 1 2030 ? 169.216 205.141 215.886 1.00 1.81  ? 2030 ASP A C     1 
ATOM   4591  O  O     . ASP A 1 2030 ? 168.177 205.389 215.263 1.00 2.95  ? 2030 ASP A O     1 
ATOM   4592  C  CB    . ASP A 1 2030 ? 169.214 203.070 217.295 1.00 4.40  ? 2030 ASP A CB    1 
ATOM   4593  C  CG    . ASP A 1 2030 ? 169.450 201.578 217.339 1.00 11.93 ? 2030 ASP A CG    1 
ATOM   4594  O  OD1   . ASP A 1 2030 ? 169.670 201.043 218.444 1.00 10.73 ? 2030 ASP A OD1   1 
ATOM   4595  O  OD2   . ASP A 1 2030 ? 169.415 200.935 216.268 1.00 19.27 ? 2030 ASP A OD2   1 
ATOM   4596  N  N     . ASN A 1 2031 ? 169.930 206.097 216.483 1.00 2.58  ? 2031 ASN A N     1 
ATOM   4597  C  CA    . ASN A 1 2031 ? 169.499 207.489 216.407 1.00 1.12  ? 2031 ASN A CA    1 
ATOM   4598  C  C     . ASN A 1 2031 ? 169.496 207.998 214.971 1.00 1.86  ? 2031 ASN A C     1 
ATOM   4599  O  O     . ASN A 1 2031 ? 168.709 208.888 214.632 1.00 2.37  ? 2031 ASN A O     1 
ATOM   4600  C  CB    . ASN A 1 2031 ? 170.389 208.365 217.291 1.00 0.79  ? 2031 ASN A CB    1 
ATOM   4601  C  CG    . ASN A 1 2031 ? 171.738 208.644 216.666 1.00 0.77  ? 2031 ASN A CG    1 
ATOM   4602  O  OD1   . ASN A 1 2031 ? 172.481 207.725 216.331 1.00 1.25  ? 2031 ASN A OD1   1 
ATOM   4603  N  ND2   . ASN A 1 2031 ? 172.063 209.920 216.509 1.00 0.60  ? 2031 ASN A ND2   1 
ATOM   4604  N  N     . LEU A 1 2032 ? 170.366 207.456 214.117 1.00 1.30  ? 2032 LEU A N     1 
ATOM   4605  C  CA    . LEU A 1 2032 ? 170.311 207.792 212.700 1.00 0.70  ? 2032 LEU A CA    1 
ATOM   4606  C  C     . LEU A 1 2032 ? 169.165 207.069 212.003 1.00 1.04  ? 2032 LEU A C     1 
ATOM   4607  O  O     . LEU A 1 2032 ? 168.483 207.649 211.151 1.00 0.52  ? 2032 LEU A O     1 
ATOM   4608  C  CB    . LEU A 1 2032 ? 171.643 207.459 212.028 1.00 1.27  ? 2032 LEU A CB    1 
ATOM   4609  C  CG    . LEU A 1 2032 ? 171.728 207.665 210.514 1.00 0.58  ? 2032 LEU A CG    1 
ATOM   4610  C  CD1   . LEU A 1 2032 ? 171.547 209.127 210.149 1.00 0.24  ? 2032 LEU A CD1   1 
ATOM   4611  C  CD2   . LEU A 1 2032 ? 173.043 207.133 209.973 1.00 0.36  ? 2032 LEU A CD2   1 
ATOM   4612  N  N     . LYS A 1 2033 ? 168.930 205.804 212.363 1.00 1.77  ? 2033 LYS A N     1 
ATOM   4613  C  CA    . LYS A 1 2033 ? 167.910 205.010 211.688 1.00 1.12  ? 2033 LYS A CA    1 
ATOM   4614  C  C     . LYS A 1 2033 ? 166.505 205.537 211.949 1.00 0.73  ? 2033 LYS A C     1 
ATOM   4615  O  O     . LYS A 1 2033 ? 165.634 205.413 211.082 1.00 0.73  ? 2033 LYS A O     1 
ATOM   4616  C  CB    . LYS A 1 2033 ? 168.017 203.545 212.113 1.00 1.54  ? 2033 LYS A CB    1 
ATOM   4617  C  CG    . LYS A 1 2033 ? 169.246 202.852 211.564 1.00 1.79  ? 2033 LYS A CG    1 
ATOM   4618  C  CD    . LYS A 1 2033 ? 169.106 201.343 211.555 1.00 3.69  ? 2033 LYS A CD    1 
ATOM   4619  C  CE    . LYS A 1 2033 ? 169.675 200.720 212.813 1.00 8.61  ? 2033 LYS A CE    1 
ATOM   4620  N  NZ    . LYS A 1 2033 ? 170.071 199.306 212.584 1.00 8.17  ? 2033 LYS A NZ    1 
ATOM   4621  N  N     . LYS A 1 2034 ? 166.262 206.131 213.119 1.00 1.06  ? 2034 LYS A N     1 
ATOM   4622  C  CA    . LYS A 1 2034 ? 164.934 206.666 213.402 1.00 1.24  ? 2034 LYS A CA    1 
ATOM   4623  C  C     . LYS A 1 2034 ? 164.599 207.867 212.528 1.00 0.62  ? 2034 LYS A C     1 
ATOM   4624  O  O     . LYS A 1 2034 ? 163.432 208.264 212.464 1.00 0.72  ? 2034 LYS A O     1 
ATOM   4625  C  CB    . LYS A 1 2034 ? 164.811 207.053 214.877 1.00 1.37  ? 2034 LYS A CB    1 
ATOM   4626  C  CG    . LYS A 1 2034 ? 165.704 208.197 215.304 1.00 2.46  ? 2034 LYS A CG    1 
ATOM   4627  C  CD    . LYS A 1 2034 ? 165.557 208.488 216.784 1.00 3.23  ? 2034 LYS A CD    1 
ATOM   4628  C  CE    . LYS A 1 2034 ? 166.442 209.647 217.212 1.00 9.18  ? 2034 LYS A CE    1 
ATOM   4629  N  NZ    . LYS A 1 2034 ? 166.301 209.927 218.668 1.00 9.61  ? 2034 LYS A NZ    1 
ATOM   4630  N  N     . LEU A 1 2035 ? 165.588 208.451 211.859 1.00 0.52  ? 2035 LEU A N     1 
ATOM   4631  C  CA    . LEU A 1 2035 ? 165.368 209.571 210.958 1.00 0.23  ? 2035 LEU A CA    1 
ATOM   4632  C  C     . LEU A 1 2035 ? 164.967 209.132 209.556 1.00 0.14  ? 2035 LEU A C     1 
ATOM   4633  O  O     . LEU A 1 2035 ? 164.690 209.987 208.711 1.00 0.08  ? 2035 LEU A O     1 
ATOM   4634  C  CB    . LEU A 1 2035 ? 166.626 210.438 210.881 1.00 0.44  ? 2035 LEU A CB    1 
ATOM   4635  C  CG    . LEU A 1 2035 ? 167.183 210.949 212.209 1.00 0.51  ? 2035 LEU A CG    1 
ATOM   4636  C  CD1   . LEU A 1 2035 ? 168.525 211.631 211.994 1.00 0.23  ? 2035 LEU A CD1   1 
ATOM   4637  C  CD2   . LEU A 1 2035 ? 166.197 211.888 212.882 1.00 0.87  ? 2035 LEU A CD2   1 
ATOM   4638  N  N     . PHE A 1 2036 ? 164.931 207.831 209.292 1.00 0.13  ? 2036 PHE A N     1 
ATOM   4639  C  CA    . PHE A 1 2036 ? 164.632 207.317 207.966 1.00 0.11  ? 2036 PHE A CA    1 
ATOM   4640  C  C     . PHE A 1 2036 ? 163.541 206.264 208.052 1.00 0.14  ? 2036 PHE A C     1 
ATOM   4641  O  O     . PHE A 1 2036 ? 163.506 205.464 208.990 1.00 0.43  ? 2036 PHE A O     1 
ATOM   4642  C  CB    . PHE A 1 2036 ? 165.882 206.718 207.309 1.00 0.06  ? 2036 PHE A CB    1 
ATOM   4643  C  CG    . PHE A 1 2036 ? 166.936 207.732 206.982 1.00 0.05  ? 2036 PHE A CG    1 
ATOM   4644  C  CD1   . PHE A 1 2036 ? 167.915 208.054 207.906 1.00 0.06  ? 2036 PHE A CD1   1 
ATOM   4645  C  CD2   . PHE A 1 2036 ? 166.943 208.373 205.756 1.00 0.05  ? 2036 PHE A CD2   1 
ATOM   4646  C  CE1   . PHE A 1 2036 ? 168.884 208.990 207.611 1.00 0.08  ? 2036 PHE A CE1   1 
ATOM   4647  C  CE2   . PHE A 1 2036 ? 167.908 209.311 205.456 1.00 0.05  ? 2036 PHE A CE2   1 
ATOM   4648  C  CZ    . PHE A 1 2036 ? 168.881 209.620 206.386 1.00 0.06  ? 2036 PHE A CZ    1 
ATOM   4649  N  N     . ARG A 1 2037 ? 162.646 206.276 207.071 1.00 0.25  ? 2037 ARG A N     1 
ATOM   4650  C  CA    . ARG A 1 2037 ? 161.664 205.217 206.905 1.00 0.18  ? 2037 ARG A CA    1 
ATOM   4651  C  C     . ARG A 1 2037 ? 162.203 204.213 205.895 1.00 0.06  ? 2037 ARG A C     1 
ATOM   4652  O  O     . ARG A 1 2037 ? 162.542 204.581 204.768 1.00 0.13  ? 2037 ARG A O     1 
ATOM   4653  C  CB    . ARG A 1 2037 ? 160.322 205.786 206.447 1.00 0.11  ? 2037 ARG A CB    1 
ATOM   4654  C  CG    . ARG A 1 2037 ? 159.647 206.661 207.489 1.00 0.77  ? 2037 ARG A CG    1 
ATOM   4655  C  CD    . ARG A 1 2037 ? 159.036 205.826 208.605 1.00 0.83  ? 2037 ARG A CD    1 
ATOM   4656  N  NE    . ARG A 1 2037 ? 157.851 205.100 208.162 1.00 2.91  ? 2037 ARG A NE    1 
ATOM   4657  C  CZ    . ARG A 1 2037 ? 156.722 205.668 207.760 1.00 5.59  ? 2037 ARG A CZ    1 
ATOM   4658  N  NH1   . ARG A 1 2037 ? 156.539 206.977 207.832 1.00 3.42  ? 2037 ARG A NH1   1 
ATOM   4659  N  NH2   . ARG A 1 2037 ? 155.744 204.902 207.289 1.00 4.13  ? 2037 ARG A NH2   1 
ATOM   4660  N  N     . SER A 1 2038 ? 162.296 202.956 206.307 1.00 0.10  ? 2038 SER A N     1 
ATOM   4661  C  CA    . SER A 1 2038 ? 162.934 201.926 205.506 1.00 0.09  ? 2038 SER A CA    1 
ATOM   4662  C  C     . SER A 1 2038 ? 161.891 201.077 204.793 1.00 0.15  ? 2038 SER A C     1 
ATOM   4663  O  O     . SER A 1 2038 ? 160.810 200.819 205.328 1.00 0.65  ? 2038 SER A O     1 
ATOM   4664  C  CB    . SER A 1 2038 ? 163.831 201.040 206.372 1.00 0.12  ? 2038 SER A CB    1 
ATOM   4665  O  OG    . SER A 1 2038 ? 163.067 200.242 207.257 1.00 1.00  ? 2038 SER A OG    1 
ATOM   4666  N  N     . LEU A 1 2039 ? 162.220 200.658 203.574 1.00 0.15  ? 2039 LEU A N     1 
ATOM   4667  C  CA    . LEU A 1 2039 ? 161.385 199.747 202.805 1.00 0.15  ? 2039 LEU A CA    1 
ATOM   4668  C  C     . LEU A 1 2039 ? 162.258 198.672 202.184 1.00 0.15  ? 2039 LEU A C     1 
ATOM   4669  O  O     . LEU A 1 2039 ? 163.295 198.978 201.591 1.00 0.10  ? 2039 LEU A O     1 
ATOM   4670  C  CB    . LEU A 1 2039 ? 160.611 200.480 201.708 1.00 0.22  ? 2039 LEU A CB    1 
ATOM   4671  C  CG    . LEU A 1 2039 ? 159.686 199.549 200.923 1.00 0.53  ? 2039 LEU A CG    1 
ATOM   4672  C  CD1   . LEU A 1 2039 ? 158.610 198.957 201.809 1.00 0.76  ? 2039 LEU A CD1   1 
ATOM   4673  C  CD2   . LEU A 1 2039 ? 159.076 200.272 199.769 1.00 0.34  ? 2039 LEU A CD2   1 
ATOM   4674  N  N     . ALA A 1 2040 ? 161.836 197.419 202.317 1.00 0.25  ? 2040 ALA A N     1 
ATOM   4675  C  CA    . ALA A 1 2040 ? 162.570 196.304 201.734 1.00 0.30  ? 2040 ALA A CA    1 
ATOM   4676  C  C     . ALA A 1 2040 ? 162.207 196.167 200.260 1.00 0.35  ? 2040 ALA A C     1 
ATOM   4677  O  O     . ALA A 1 2040 ? 161.039 195.961 199.917 1.00 0.32  ? 2040 ALA A O     1 
ATOM   4678  C  CB    . ALA A 1 2040 ? 162.264 195.011 202.485 1.00 0.36  ? 2040 ALA A CB    1 
ATOM   4679  N  N     . MET A 1 2041 ? 163.203 196.297 199.395 1.00 0.42  ? 2041 MET A N     1 
ATOM   4680  C  CA    . MET A 1 2041 ? 163.053 196.068 197.962 1.00 0.56  ? 2041 MET A CA    1 
ATOM   4681  C  C     . MET A 1 2041 ? 163.919 194.859 197.629 1.00 0.66  ? 2041 MET A C     1 
ATOM   4682  O  O     . MET A 1 2041 ? 165.124 194.992 197.400 1.00 2.12  ? 2041 MET A O     1 
ATOM   4683  C  CB    . MET A 1 2041 ? 163.451 197.305 197.160 1.00 0.52  ? 2041 MET A CB    1 
ATOM   4684  C  CG    . MET A 1 2041 ? 162.612 198.536 197.474 1.00 0.32  ? 2041 MET A CG    1 
ATOM   4685  S  SD    . MET A 1 2041 ? 162.946 199.951 196.410 1.00 13.17 ? 2041 MET A SD    1 
ATOM   4686  C  CE    . MET A 1 2041 ? 162.643 199.251 194.790 1.00 0.39  ? 2041 MET A CE    1 
ATOM   4687  N  N     . THR A 1 2042 ? 163.305 193.681 197.621 1.00 1.07  ? 2042 THR A N     1 
ATOM   4688  C  CA    . THR A 1 2042 ? 164.033 192.423 197.502 1.00 1.48  ? 2042 THR A CA    1 
ATOM   4689  C  C     . THR A 1 2042 ? 163.705 191.647 196.240 1.00 2.68  ? 2042 THR A C     1 
ATOM   4690  O  O     . THR A 1 2042 ? 164.609 191.088 195.618 1.00 7.08  ? 2042 THR A O     1 
ATOM   4691  C  CB    . THR A 1 2042 ? 163.756 191.538 198.731 1.00 2.46  ? 2042 THR A CB    1 
ATOM   4692  O  OG1   . THR A 1 2042 ? 163.958 192.298 199.927 1.00 1.77  ? 2042 THR A OG1   1 
ATOM   4693  C  CG2   . THR A 1 2042 ? 164.686 190.338 198.746 1.00 3.33  ? 2042 THR A CG2   1 
ATOM   4694  N  N     . LYS A 1 2043 ? 162.434 191.592 195.838 1.00 4.61  ? 2043 LYS A N     1 
ATOM   4695  C  CA    . LYS A 1 2043 ? 161.996 190.823 194.674 1.00 2.91  ? 2043 LYS A CA    1 
ATOM   4696  C  C     . LYS A 1 2043 ? 161.370 191.763 193.653 1.00 3.08  ? 2043 LYS A C     1 
ATOM   4697  O  O     . LYS A 1 2043 ? 160.170 192.070 193.730 1.00 4.38  ? 2043 LYS A O     1 
ATOM   4698  C  CB    . LYS A 1 2043 ? 161.011 189.728 195.077 1.00 4.17  ? 2043 LYS A CB    1 
ATOM   4699  C  CG    . LYS A 1 2043 ? 161.574 188.691 196.029 1.00 9.55  ? 2043 LYS A CG    1 
ATOM   4700  C  CD    . LYS A 1 2043 ? 162.649 187.848 195.366 1.00 17.76 ? 2043 LYS A CD    1 
ATOM   4701  C  CE    . LYS A 1 2043 ? 163.151 186.762 196.302 1.00 18.43 ? 2043 LYS A CE    1 
ATOM   4702  N  NZ    . LYS A 1 2043 ? 164.236 185.950 195.685 1.00 27.99 ? 2043 LYS A NZ    1 
ATOM   4703  N  N     . PRO A 1 2044 ? 162.140 192.242 192.679 1.00 3.94  ? 2044 PRO A N     1 
ATOM   4704  C  CA    . PRO A 1 2044 ? 161.550 193.053 191.609 1.00 1.50  ? 2044 PRO A CA    1 
ATOM   4705  C  C     . PRO A 1 2044 ? 160.599 192.234 190.753 1.00 2.89  ? 2044 PRO A C     1 
ATOM   4706  O  O     . PRO A 1 2044 ? 160.762 191.023 190.582 1.00 3.65  ? 2044 PRO A O     1 
ATOM   4707  C  CB    . PRO A 1 2044 ? 162.765 193.522 190.798 1.00 1.66  ? 2044 PRO A CB    1 
ATOM   4708  C  CG    . PRO A 1 2044 ? 163.958 193.213 191.637 1.00 1.11  ? 2044 PRO A CG    1 
ATOM   4709  C  CD    . PRO A 1 2044 ? 163.590 192.071 192.514 1.00 1.97  ? 2044 PRO A CD    1 
ATOM   4710  N  N     . ASP A 1 2045 ? 159.592 192.915 190.210 1.00 2.67  ? 2045 ASP A N     1 
ATOM   4711  C  CA    . ASP A 1 2045 ? 158.561 192.274 189.394 1.00 1.85  ? 2045 ASP A CA    1 
ATOM   4712  C  C     . ASP A 1 2045 ? 159.064 192.186 187.954 1.00 2.15  ? 2045 ASP A C     1 
ATOM   4713  O  O     . ASP A 1 2045 ? 158.719 192.988 187.083 1.00 1.78  ? 2045 ASP A O     1 
ATOM   4714  C  CB    . ASP A 1 2045 ? 157.250 193.042 189.503 1.00 1.92  ? 2045 ASP A CB    1 
ATOM   4715  C  CG    . ASP A 1 2045 ? 156.833 193.274 190.946 1.00 5.47  ? 2045 ASP A CG    1 
ATOM   4716  O  OD1   . ASP A 1 2045 ? 156.866 192.309 191.738 1.00 7.47  ? 2045 ASP A OD1   1 
ATOM   4717  O  OD2   . ASP A 1 2045 ? 156.473 194.416 191.292 1.00 3.83  ? 2045 ASP A OD2   1 
ATOM   4718  N  N     . ARG A 1 2046 ? 159.896 191.168 187.710 1.00 2.04  ? 2046 ARG A N     1 
ATOM   4719  C  CA    . ARG A 1 2046 ? 160.626 191.076 186.448 1.00 1.11  ? 2046 ARG A CA    1 
ATOM   4720  C  C     . ARG A 1 2046 ? 159.695 190.879 185.258 1.00 1.58  ? 2046 ARG A C     1 
ATOM   4721  O  O     . ARG A 1 2046 ? 159.890 191.499 184.207 1.00 1.58  ? 2046 ARG A O     1 
ATOM   4722  C  CB    . ARG A 1 2046 ? 161.643 189.940 186.513 1.00 1.29  ? 2046 ARG A CB    1 
ATOM   4723  C  CG    . ARG A 1 2046 ? 162.779 190.179 187.480 1.00 1.68  ? 2046 ARG A CG    1 
ATOM   4724  C  CD    . ARG A 1 2046 ? 163.737 189.009 187.485 1.00 4.45  ? 2046 ARG A CD    1 
ATOM   4725  N  NE    . ARG A 1 2046 ? 164.832 189.207 188.426 1.00 7.45  ? 2046 ARG A NE    1 
ATOM   4726  C  CZ    . ARG A 1 2046 ? 165.780 188.313 188.667 1.00 13.73 ? 2046 ARG A CZ    1 
ATOM   4727  N  NH1   . ARG A 1 2046 ? 165.801 187.144 188.046 1.00 18.46 ? 2046 ARG A NH1   1 
ATOM   4728  N  NH2   . ARG A 1 2046 ? 166.729 188.597 189.552 1.00 13.74 ? 2046 ARG A NH2   1 
ATOM   4729  N  N     . GLN A 1 2047 ? 158.685 190.019 185.397 1.00 1.69  ? 2047 GLN A N     1 
ATOM   4730  C  CA    . GLN A 1 2047 ? 157.833 189.708 184.254 1.00 1.95  ? 2047 GLN A CA    1 
ATOM   4731  C  C     . GLN A 1 2047 ? 157.007 190.916 183.829 1.00 3.78  ? 2047 GLN A C     1 
ATOM   4732  O  O     . GLN A 1 2047 ? 156.721 191.090 182.638 1.00 5.04  ? 2047 GLN A O     1 
ATOM   4733  C  CB    . GLN A 1 2047 ? 156.945 188.499 184.572 1.00 4.94  ? 2047 GLN A CB    1 
ATOM   4734  C  CG    . GLN A 1 2047 ? 155.955 188.675 185.714 1.00 17.03 ? 2047 GLN A CG    1 
ATOM   4735  C  CD    . GLN A 1 2047 ? 154.663 189.345 185.287 1.00 15.99 ? 2047 GLN A CD    1 
ATOM   4736  O  OE1   . GLN A 1 2047 ? 154.232 189.213 184.142 1.00 15.01 ? 2047 GLN A OE1   1 
ATOM   4737  N  NE2   . GLN A 1 2047 ? 154.035 190.063 186.212 1.00 14.33 ? 2047 GLN A NE2   1 
ATOM   4738  N  N     . LEU A 1 2048 ? 156.621 191.769 184.779 1.00 2.91  ? 2048 LEU A N     1 
ATOM   4739  C  CA    . LEU A 1 2048 ? 155.893 192.982 184.421 1.00 1.28  ? 2048 LEU A CA    1 
ATOM   4740  C  C     . LEU A 1 2048 ? 156.810 193.993 183.740 1.00 1.89  ? 2048 LEU A C     1 
ATOM   4741  O  O     . LEU A 1 2048 ? 156.416 194.639 182.763 1.00 5.01  ? 2048 LEU A O     1 
ATOM   4742  C  CB    . LEU A 1 2048 ? 155.238 193.594 185.660 1.00 2.77  ? 2048 LEU A CB    1 
ATOM   4743  C  CG    . LEU A 1 2048 ? 154.446 194.879 185.403 1.00 2.13  ? 2048 LEU A CG    1 
ATOM   4744  C  CD1   . LEU A 1 2048 ? 153.328 194.636 184.399 1.00 0.47  ? 2048 LEU A CD1   1 
ATOM   4745  C  CD2   . LEU A 1 2048 ? 153.896 195.448 186.696 1.00 1.33  ? 2048 LEU A CD2   1 
ATOM   4746  N  N     . ILE A 1 2049 ? 158.038 194.145 184.242 1.00 1.14  ? 2049 ILE A N     1 
ATOM   4747  C  CA    . ILE A 1 2049 ? 158.996 195.050 183.609 1.00 1.08  ? 2049 ILE A CA    1 
ATOM   4748  C  C     . ILE A 1 2049 ? 159.289 194.598 182.184 1.00 1.82  ? 2049 ILE A C     1 
ATOM   4749  O  O     . ILE A 1 2049 ? 159.318 195.407 181.251 1.00 5.93  ? 2049 ILE A O     1 
ATOM   4750  C  CB    . ILE A 1 2049 ? 160.288 195.145 184.444 1.00 1.06  ? 2049 ILE A CB    1 
ATOM   4751  C  CG1   . ILE A 1 2049 ? 159.989 195.648 185.855 1.00 0.88  ? 2049 ILE A CG1   1 
ATOM   4752  C  CG2   . ILE A 1 2049 ? 161.311 196.028 183.750 1.00 0.39  ? 2049 ILE A CG2   1 
ATOM   4753  C  CD1   . ILE A 1 2049 ? 161.171 195.577 186.796 1.00 0.41  ? 2049 ILE A CD1   1 
ATOM   4754  N  N     . ALA A 1 2050 ? 159.510 193.296 181.998 1.00 1.65  ? 2050 ALA A N     1 
ATOM   4755  C  CA    . ALA A 1 2050 ? 159.799 192.778 180.667 1.00 0.94  ? 2050 ALA A CA    1 
ATOM   4756  C  C     . ALA A 1 2050 ? 158.615 192.969 179.728 1.00 1.50  ? 2050 ALA A C     1 
ATOM   4757  O  O     . ALA A 1 2050 ? 158.793 193.332 178.560 1.00 2.66  ? 2050 ALA A O     1 
ATOM   4758  C  CB    . ALA A 1 2050 ? 160.188 191.303 180.751 1.00 1.10  ? 2050 ALA A CB    1 
ATOM   4759  N  N     . GLN A 1 2051 ? 157.397 192.737 180.222 1.00 2.70  ? 2051 GLN A N     1 
ATOM   4760  C  CA    . GLN A 1 2051 ? 156.220 192.827 179.365 1.00 2.22  ? 2051 GLN A CA    1 
ATOM   4761  C  C     . GLN A 1 2051 ? 155.981 194.261 178.906 1.00 2.37  ? 2051 GLN A C     1 
ATOM   4762  O  O     . GLN A 1 2051 ? 155.696 194.508 177.730 1.00 5.03  ? 2051 GLN A O     1 
ATOM   4763  C  CB    . GLN A 1 2051 ? 154.999 192.273 180.102 1.00 4.15  ? 2051 GLN A CB    1 
ATOM   4764  C  CG    . GLN A 1 2051 ? 153.746 192.130 179.250 1.00 6.67  ? 2051 GLN A CG    1 
ATOM   4765  C  CD    . GLN A 1 2051 ? 152.927 193.404 179.176 1.00 14.94 ? 2051 GLN A CD    1 
ATOM   4766  O  OE1   . GLN A 1 2051 ? 152.927 194.213 180.103 1.00 12.11 ? 2051 GLN A OE1   1 
ATOM   4767  N  NE2   . GLN A 1 2051 ? 152.228 193.591 178.063 1.00 12.72 ? 2051 GLN A NE2   1 
ATOM   4768  N  N     . VAL A 1 2052 ? 156.098 195.222 179.823 1.00 3.92  ? 2052 VAL A N     1 
ATOM   4769  C  CA    . VAL A 1 2052 ? 155.829 196.615 179.477 1.00 2.55  ? 2052 VAL A CA    1 
ATOM   4770  C  C     . VAL A 1 2052 ? 156.918 197.167 178.566 1.00 2.53  ? 2052 VAL A C     1 
ATOM   4771  O  O     . VAL A 1 2052 ? 156.632 197.896 177.609 1.00 4.60  ? 2052 VAL A O     1 
ATOM   4772  C  CB    . VAL A 1 2052 ? 155.663 197.458 180.755 1.00 1.70  ? 2052 VAL A CB    1 
ATOM   4773  C  CG1   . VAL A 1 2052 ? 155.488 198.929 180.414 1.00 0.92  ? 2052 VAL A CG1   1 
ATOM   4774  C  CG2   . VAL A 1 2052 ? 154.477 196.958 181.558 1.00 2.27  ? 2052 VAL A CG2   1 
ATOM   4775  N  N     . MET A 1 2053 ? 158.183 196.835 178.843 1.00 2.37  ? 2053 MET A N     1 
ATOM   4776  C  CA    . MET A 1 2053 ? 159.275 197.332 178.009 1.00 2.69  ? 2053 MET A CA    1 
ATOM   4777  C  C     . MET A 1 2053 ? 159.182 196.802 176.584 1.00 4.77  ? 2053 MET A C     1 
ATOM   4778  O  O     . MET A 1 2053 ? 159.365 197.555 175.622 1.00 7.56  ? 2053 MET A O     1 
ATOM   4779  C  CB    . MET A 1 2053 ? 160.625 196.960 178.617 1.00 3.62  ? 2053 MET A CB    1 
ATOM   4780  C  CG    . MET A 1 2053 ? 161.062 197.842 179.763 1.00 3.14  ? 2053 MET A CG    1 
ATOM   4781  S  SD    . MET A 1 2053 ? 162.576 197.221 180.504 1.00 27.24 ? 2053 MET A SD    1 
ATOM   4782  C  CE    . MET A 1 2053 ? 163.760 197.704 179.250 1.00 4.88  ? 2053 MET A CE    1 
ATOM   4783  N  N     . LEU A 1 2054 ? 158.909 195.505 176.427 1.00 2.71  ? 2054 LEU A N     1 
ATOM   4784  C  CA    . LEU A 1 2054 ? 158.773 194.943 175.088 1.00 3.26  ? 2054 LEU A CA    1 
ATOM   4785  C  C     . LEU A 1 2054 ? 157.543 195.487 174.378 1.00 6.25  ? 2054 LEU A C     1 
ATOM   4786  O  O     . LEU A 1 2054 ? 157.565 195.677 173.158 1.00 11.18 ? 2054 LEU A O     1 
ATOM   4787  C  CB    . LEU A 1 2054 ? 158.722 193.417 175.156 1.00 3.68  ? 2054 LEU A CB    1 
ATOM   4788  C  CG    . LEU A 1 2054 ? 160.024 192.718 175.546 1.00 4.09  ? 2054 LEU A CG    1 
ATOM   4789  C  CD1   . LEU A 1 2054 ? 159.777 191.254 175.857 1.00 3.38  ? 2054 LEU A CD1   1 
ATOM   4790  C  CD2   . LEU A 1 2054 ? 161.074 192.870 174.455 1.00 3.13  ? 2054 LEU A CD2   1 
ATOM   4791  N  N     . TYR A 1 2055 ? 156.467 195.742 175.124 1.00 3.89  ? 2055 TYR A N     1 
ATOM   4792  C  CA    . TYR A 1 2055 ? 155.265 196.313 174.532 1.00 4.62  ? 2055 TYR A CA    1 
ATOM   4793  C  C     . TYR A 1 2055 ? 155.473 197.770 174.133 1.00 3.62  ? 2055 TYR A C     1 
ATOM   4794  O  O     . TYR A 1 2055 ? 154.920 198.219 173.123 1.00 4.60  ? 2055 TYR A O     1 
ATOM   4795  C  CB    . TYR A 1 2055 ? 154.100 196.169 175.511 1.00 5.17  ? 2055 TYR A CB    1 
ATOM   4796  C  CG    . TYR A 1 2055 ? 152.805 196.811 175.075 1.00 3.43  ? 2055 TYR A CG    1 
ATOM   4797  C  CD1   . TYR A 1 2055 ? 152.060 196.278 174.034 1.00 3.14  ? 2055 TYR A CD1   1 
ATOM   4798  C  CD2   . TYR A 1 2055 ? 152.308 197.926 175.731 1.00 4.61  ? 2055 TYR A CD2   1 
ATOM   4799  C  CE1   . TYR A 1 2055 ? 150.870 196.855 173.641 1.00 6.43  ? 2055 TYR A CE1   1 
ATOM   4800  C  CE2   . TYR A 1 2055 ? 151.118 198.507 175.349 1.00 6.62  ? 2055 TYR A CE2   1 
ATOM   4801  C  CZ    . TYR A 1 2055 ? 150.402 197.968 174.304 1.00 11.52 ? 2055 TYR A CZ    1 
ATOM   4802  O  OH    . TYR A 1 2055 ? 149.217 198.547 173.921 1.00 15.46 ? 2055 TYR A OH    1 
ATOM   4803  N  N     . SER A 1 2056 ? 156.264 198.518 174.905 1.00 4.56  ? 2056 SER A N     1 
ATOM   4804  C  CA    . SER A 1 2056 ? 156.537 199.910 174.563 1.00 3.88  ? 2056 SER A CA    1 
ATOM   4805  C  C     . SER A 1 2056 ? 157.514 200.032 173.402 1.00 6.78  ? 2056 SER A C     1 
ATOM   4806  O  O     . SER A 1 2056 ? 157.523 201.057 172.712 1.00 10.39 ? 2056 SER A O     1 
ATOM   4807  C  CB    . SER A 1 2056 ? 157.078 200.655 175.783 1.00 3.73  ? 2056 SER A CB    1 
ATOM   4808  O  OG    . SER A 1 2056 ? 158.297 200.092 176.227 1.00 6.92  ? 2056 SER A OG    1 
ATOM   4809  N  N     . GLN A 1 2057 ? 158.340 199.011 173.174 1.00 7.76  ? 2057 GLN A N     1 
ATOM   4810  C  CA    . GLN A 1 2057 ? 159.284 199.026 172.068 1.00 4.29  ? 2057 GLN A CA    1 
ATOM   4811  C  C     . GLN A 1 2057 ? 158.653 198.620 170.743 1.00 7.81  ? 2057 GLN A C     1 
ATOM   4812  O  O     . GLN A 1 2057 ? 159.287 198.795 169.697 1.00 12.93 ? 2057 GLN A O     1 
ATOM   4813  C  CB    . GLN A 1 2057 ? 160.467 198.106 172.374 1.00 5.99  ? 2057 GLN A CB    1 
ATOM   4814  C  CG    . GLN A 1 2057 ? 161.615 198.783 173.102 1.00 4.59  ? 2057 GLN A CG    1 
ATOM   4815  C  CD    . GLN A 1 2057 ? 162.336 197.845 174.054 1.00 10.09 ? 2057 GLN A CD    1 
ATOM   4816  O  OE1   . GLN A 1 2057 ? 162.251 196.625 173.921 1.00 11.76 ? 2057 GLN A OE1   1 
ATOM   4817  N  NE2   . GLN A 1 2057 ? 163.052 198.413 175.017 1.00 9.17  ? 2057 GLN A NE2   1 
ATOM   4818  N  N     . GLY A 1 2058 ? 157.433 198.094 170.755 1.00 6.71  ? 2058 GLY A N     1 
ATOM   4819  C  CA    . GLY A 1 2058 ? 156.746 197.713 169.541 1.00 5.10  ? 2058 GLY A CA    1 
ATOM   4820  C  C     . GLY A 1 2058 ? 156.685 196.229 169.248 1.00 6.46  ? 2058 GLY A C     1 
ATOM   4821  O  O     . GLY A 1 2058 ? 156.264 195.856 168.148 1.00 13.86 ? 2058 GLY A O     1 
ATOM   4822  N  N     . PHE A 1 2059 ? 157.089 195.373 170.181 1.00 6.12  ? 2059 PHE A N     1 
ATOM   4823  C  CA    . PHE A 1 2059 ? 156.993 193.933 169.971 1.00 6.06  ? 2059 PHE A CA    1 
ATOM   4824  C  C     . PHE A 1 2059 ? 155.536 193.498 170.073 1.00 8.97  ? 2059 PHE A C     1 
ATOM   4825  O  O     . PHE A 1 2059 ? 154.895 193.697 171.109 1.00 14.60 ? 2059 PHE A O     1 
ATOM   4826  C  CB    . PHE A 1 2059 ? 157.846 193.190 170.994 1.00 6.26  ? 2059 PHE A CB    1 
ATOM   4827  C  CG    . PHE A 1 2059 ? 159.324 193.300 170.756 1.00 5.96  ? 2059 PHE A CG    1 
ATOM   4828  C  CD1   . PHE A 1 2059 ? 160.036 194.389 171.229 1.00 6.16  ? 2059 PHE A CD1   1 
ATOM   4829  C  CD2   . PHE A 1 2059 ? 160.005 192.305 170.076 1.00 6.56  ? 2059 PHE A CD2   1 
ATOM   4830  C  CE1   . PHE A 1 2059 ? 161.396 194.488 171.020 1.00 4.99  ? 2059 PHE A CE1   1 
ATOM   4831  C  CE2   . PHE A 1 2059 ? 161.365 192.400 169.864 1.00 8.47  ? 2059 PHE A CE2   1 
ATOM   4832  C  CZ    . PHE A 1 2059 ? 162.061 193.493 170.337 1.00 4.52  ? 2059 PHE A CZ    1 
ATOM   4833  N  N     . ARG A 1 2060 ? 155.011 192.903 169.001 1.00 9.33  ? 2060 ARG A N     1 
ATOM   4834  C  CA    . ARG A 1 2060 ? 153.609 192.498 168.999 1.00 10.77 ? 2060 ARG A CA    1 
ATOM   4835  C  C     . ARG A 1 2060 ? 153.349 191.348 169.964 1.00 11.56 ? 2060 ARG A C     1 
ATOM   4836  O  O     . ARG A 1 2060 ? 152.273 191.279 170.569 1.00 18.41 ? 2060 ARG A O     1 
ATOM   4837  C  CB    . ARG A 1 2060 ? 153.172 192.116 167.586 1.00 17.09 ? 2060 ARG A CB    1 
ATOM   4838  C  CG    . ARG A 1 2060 ? 151.687 191.801 167.459 1.00 31.01 ? 2060 ARG A CG    1 
ATOM   4839  C  CD    . ARG A 1 2060 ? 151.307 191.495 166.020 1.00 26.81 ? 2060 ARG A CD    1 
ATOM   4840  N  NE    . ARG A 1 2060 ? 151.957 190.285 165.533 1.00 28.91 ? 2060 ARG A NE    1 
ATOM   4841  C  CZ    . ARG A 1 2060 ? 152.873 190.263 164.575 1.00 32.99 ? 2060 ARG A CZ    1 
ATOM   4842  N  NH1   . ARG A 1 2060 ? 153.277 191.374 163.981 1.00 34.63 ? 2060 ARG A NH1   1 
ATOM   4843  N  NH2   . ARG A 1 2060 ? 153.397 189.097 164.205 1.00 30.16 ? 2060 ARG A NH2   1 
ATOM   4844  N  N     . THR A 1 2061 ? 154.315 190.447 170.131 1.00 12.96 ? 2061 THR A N     1 
ATOM   4845  C  CA    . THR A 1 2061 ? 154.186 189.288 171.013 1.00 8.63  ? 2061 THR A CA    1 
ATOM   4846  C  C     . THR A 1 2061 ? 154.857 189.523 172.357 1.00 10.97 ? 2061 THR A C     1 
ATOM   4847  O  O     . THR A 1 2061 ? 155.477 188.615 172.918 1.00 14.27 ? 2061 THR A O     1 
ATOM   4848  C  CB    . THR A 1 2061 ? 154.758 188.043 170.342 1.00 10.84 ? 2061 THR A CB    1 
ATOM   4849  O  OG1   . THR A 1 2061 ? 156.064 188.330 169.829 1.00 16.03 ? 2061 THR A OG1   1 
ATOM   4850  C  CG2   . THR A 1 2061 ? 153.861 187.594 169.203 1.00 10.17 ? 2061 THR A CG2   1 
ATOM   4851  N  N     . ALA A 1 2062 ? 154.750 190.746 172.889 1.00 12.82 ? 2062 ALA A N     1 
ATOM   4852  C  CA    . ALA A 1 2062 ? 155.450 191.096 174.121 1.00 7.76  ? 2062 ALA A CA    1 
ATOM   4853  C  C     . ALA A 1 2062 ? 155.043 190.194 175.279 1.00 10.48 ? 2062 ALA A C     1 
ATOM   4854  O  O     . ALA A 1 2062 ? 155.884 189.817 176.103 1.00 15.71 ? 2062 ALA A O     1 
ATOM   4855  C  CB    . ALA A 1 2062 ? 155.193 192.561 174.470 1.00 6.50  ? 2062 ALA A CB    1 
ATOM   4856  N  N     . GLU A 1 2063 ? 153.757 189.843 175.367 1.00 13.62 ? 2063 GLU A N     1 
ATOM   4857  C  CA    . GLU A 1 2063 ? 153.315 188.954 176.436 1.00 13.57 ? 2063 GLU A CA    1 
ATOM   4858  C  C     . GLU A 1 2063 ? 153.941 187.571 176.302 1.00 10.19 ? 2063 GLU A C     1 
ATOM   4859  O  O     . GLU A 1 2063 ? 154.368 186.976 177.299 1.00 13.54 ? 2063 GLU A O     1 
ATOM   4860  C  CB    . GLU A 1 2063 ? 151.789 188.855 176.444 1.00 19.83 ? 2063 GLU A CB    1 
ATOM   4861  C  CG    . GLU A 1 2063 ? 151.089 190.145 176.827 1.00 24.31 ? 2063 GLU A CG    1 
ATOM   4862  C  CD    . GLU A 1 2063 ? 149.578 190.017 176.806 1.00 32.31 ? 2063 GLU A CD    1 
ATOM   4863  O  OE1   . GLU A 1 2063 ? 149.076 188.960 176.372 1.00 32.55 ? 2063 GLU A OE1   1 
ATOM   4864  O  OE2   . GLU A 1 2063 ? 148.895 190.974 177.225 1.00 31.55 ? 2063 GLU A OE2   1 
ATOM   4865  N  N     . VAL A 1 2064 ? 153.999 187.041 175.081 1.00 10.91 ? 2064 VAL A N     1 
ATOM   4866  C  CA    . VAL A 1 2064 ? 154.645 185.750 174.866 1.00 10.75 ? 2064 VAL A CA    1 
ATOM   4867  C  C     . VAL A 1 2064 ? 156.136 185.845 175.157 1.00 10.59 ? 2064 VAL A C     1 
ATOM   4868  O  O     . VAL A 1 2064 ? 156.710 184.975 175.822 1.00 11.66 ? 2064 VAL A O     1 
ATOM   4869  C  CB    . VAL A 1 2064 ? 154.374 185.247 173.437 1.00 10.61 ? 2064 VAL A CB    1 
ATOM   4870  C  CG1   . VAL A 1 2064 ? 155.156 183.972 173.165 1.00 14.71 ? 2064 VAL A CG1   1 
ATOM   4871  C  CG2   . VAL A 1 2064 ? 152.890 185.020 173.228 1.00 8.63  ? 2064 VAL A CG2   1 
ATOM   4872  N  N     . LEU A 1 2065 ? 156.788 186.905 174.672 1.00 10.29 ? 2065 LEU A N     1 
ATOM   4873  C  CA    . LEU A 1 2065 ? 158.224 187.055 174.885 1.00 9.12  ? 2065 LEU A CA    1 
ATOM   4874  C  C     . LEU A 1 2065 ? 158.556 187.231 176.361 1.00 7.05  ? 2065 LEU A C     1 
ATOM   4875  O  O     . LEU A 1 2065 ? 159.540 186.665 176.852 1.00 11.71 ? 2065 LEU A O     1 
ATOM   4876  C  CB    . LEU A 1 2065 ? 158.750 188.237 174.072 1.00 9.40  ? 2065 LEU A CB    1 
ATOM   4877  C  CG    . LEU A 1 2065 ? 158.665 188.091 172.553 1.00 7.86  ? 2065 LEU A CG    1 
ATOM   4878  C  CD1   . LEU A 1 2065 ? 159.134 189.360 171.872 1.00 9.76  ? 2065 LEU A CD1   1 
ATOM   4879  C  CD2   . LEU A 1 2065 ? 159.470 186.898 172.084 1.00 9.46  ? 2065 LEU A CD2   1 
ATOM   4880  N  N     . ALA A 1 2066 ? 157.751 188.010 177.085 1.00 7.94  ? 2066 ALA A N     1 
ATOM   4881  C  CA    . ALA A 1 2066 ? 158.013 188.227 178.504 1.00 8.57  ? 2066 ALA A CA    1 
ATOM   4882  C  C     . ALA A 1 2066 ? 157.827 186.946 179.307 1.00 10.13 ? 2066 ALA A C     1 
ATOM   4883  O  O     . ALA A 1 2066 ? 158.577 186.688 180.255 1.00 9.25  ? 2066 ALA A O     1 
ATOM   4884  C  CB    . ALA A 1 2066 ? 157.111 189.336 179.040 1.00 6.43  ? 2066 ALA A CB    1 
ATOM   4885  N  N     . ASN A 1 2067 ? 156.833 186.132 178.944 1.00 11.48 ? 2067 ASN A N     1 
ATOM   4886  C  CA    . ASN A 1 2067 ? 156.604 184.869 179.637 1.00 11.35 ? 2067 ASN A CA    1 
ATOM   4887  C  C     . ASN A 1 2067 ? 157.696 183.845 179.377 1.00 10.35 ? 2067 ASN A C     1 
ATOM   4888  O  O     . ASN A 1 2067 ? 157.732 182.819 180.063 1.00 21.44 ? 2067 ASN A O     1 
ATOM   4889  C  CB    . ASN A 1 2067 ? 155.251 184.278 179.238 1.00 14.99 ? 2067 ASN A CB    1 
ATOM   4890  C  CG    . ASN A 1 2067 ? 154.094 184.955 179.932 1.00 19.25 ? 2067 ASN A CG    1 
ATOM   4891  O  OD1   . ASN A 1 2067 ? 154.040 185.010 181.159 1.00 20.75 ? 2067 ASN A OD1   1 
ATOM   4892  N  ND2   . ASN A 1 2067 ? 153.153 185.468 179.150 1.00 18.18 ? 2067 ASN A ND2   1 
ATOM   4893  N  N     . LYS A 1 2068 ? 158.571 184.085 178.407 1.00 7.27  ? 2068 LYS A N     1 
ATOM   4894  C  CA    . LYS A 1 2068 ? 159.686 183.193 178.120 1.00 7.43  ? 2068 LYS A CA    1 
ATOM   4895  C  C     . LYS A 1 2068 ? 161.023 183.724 178.607 1.00 7.73  ? 2068 LYS A C     1 
ATOM   4896  O  O     . LYS A 1 2068 ? 161.814 182.961 179.163 1.00 7.07  ? 2068 LYS A O     1 
ATOM   4897  C  CB    . LYS A 1 2068 ? 159.773 182.926 176.613 1.00 8.69  ? 2068 LYS A CB    1 
ATOM   4898  C  CG    . LYS A 1 2068 ? 158.521 182.320 176.015 1.00 12.08 ? 2068 LYS A CG    1 
ATOM   4899  C  CD    . LYS A 1 2068 ? 158.669 182.120 174.520 1.00 8.23  ? 2068 LYS A CD    1 
ATOM   4900  C  CE    . LYS A 1 2068 ? 157.615 181.166 173.990 1.00 13.83 ? 2068 LYS A CE    1 
ATOM   4901  N  NZ    . LYS A 1 2068 ? 157.669 179.849 174.680 1.00 15.60 ? 2068 LYS A NZ    1 
ATOM   4902  N  N     . ILE A 1 2069 ? 161.291 185.017 178.417 1.00 5.57  ? 2069 ILE A N     1 
ATOM   4903  C  CA    . ILE A 1 2069 ? 162.609 185.556 178.735 1.00 4.69  ? 2069 ILE A CA    1 
ATOM   4904  C  C     . ILE A 1 2069 ? 162.863 185.579 180.240 1.00 5.90  ? 2069 ILE A C     1 
ATOM   4905  O  O     . ILE A 1 2069 ? 163.988 185.330 180.686 1.00 6.80  ? 2069 ILE A O     1 
ATOM   4906  C  CB    . ILE A 1 2069 ? 162.784 186.950 178.097 1.00 5.22  ? 2069 ILE A CB    1 
ATOM   4907  C  CG1   . ILE A 1 2069 ? 164.251 187.375 178.165 1.00 8.52  ? 2069 ILE A CG1   1 
ATOM   4908  C  CG2   . ILE A 1 2069 ? 161.878 187.986 178.749 1.00 3.08  ? 2069 ILE A CG2   1 
ATOM   4909  C  CD1   . ILE A 1 2069 ? 165.154 186.507 177.340 1.00 4.49  ? 2069 ILE A CD1   1 
ATOM   4910  N  N     . VAL A 1 2070 ? 161.845 185.866 181.044 1.00 4.55  ? 2070 VAL A N     1 
ATOM   4911  C  CA    . VAL A 1 2070 ? 162.024 185.986 182.489 1.00 4.65  ? 2070 VAL A CA    1 
ATOM   4912  C  C     . VAL A 1 2070 ? 162.247 184.607 183.108 1.00 5.22  ? 2070 VAL A C     1 
ATOM   4913  O  O     . VAL A 1 2070 ? 163.178 184.452 183.912 1.00 4.50  ? 2070 VAL A O     1 
ATOM   4914  C  CB    . VAL A 1 2070 ? 160.842 186.725 183.140 1.00 4.41  ? 2070 VAL A CB    1 
ATOM   4915  C  CG1   . VAL A 1 2070 ? 161.008 186.776 184.649 1.00 1.77  ? 2070 VAL A CG1   1 
ATOM   4916  C  CG2   . VAL A 1 2070 ? 160.727 188.124 182.569 1.00 3.10  ? 2070 VAL A CG2   1 
ATOM   4917  N  N     . PRO A 1 2071 ? 161.443 183.582 182.793 1.00 5.52  ? 2071 PRO A N     1 
ATOM   4918  C  CA    . PRO A 1 2071 ? 161.801 182.232 183.257 1.00 5.87  ? 2071 PRO A CA    1 
ATOM   4919  C  C     . PRO A 1 2071 ? 163.129 181.739 182.714 1.00 6.02  ? 2071 PRO A C     1 
ATOM   4920  O  O     . PRO A 1 2071 ? 163.820 180.977 183.401 1.00 7.32  ? 2071 PRO A O     1 
ATOM   4921  C  CB    . PRO A 1 2071 ? 160.631 181.372 182.758 1.00 5.43  ? 2071 PRO A CB    1 
ATOM   4922  C  CG    . PRO A 1 2071 ? 159.512 182.317 182.636 1.00 9.00  ? 2071 PRO A CG    1 
ATOM   4923  C  CD    . PRO A 1 2071 ? 160.132 183.572 182.120 1.00 5.26  ? 2071 PRO A CD    1 
ATOM   4924  N  N     . PHE A 1 2072 ? 163.505 182.147 181.499 1.00 5.02  ? 2072 PHE A N     1 
ATOM   4925  C  CA    . PHE A 1 2072 ? 164.777 181.710 180.932 1.00 6.14  ? 2072 PHE A CA    1 
ATOM   4926  C  C     . PHE A 1 2072 ? 165.951 182.200 181.768 1.00 8.45  ? 2072 PHE A C     1 
ATOM   4927  O  O     . PHE A 1 2072 ? 166.918 181.461 181.989 1.00 11.58 ? 2072 PHE A O     1 
ATOM   4928  C  CB    . PHE A 1 2072 ? 164.907 182.199 179.490 1.00 5.26  ? 2072 PHE A CB    1 
ATOM   4929  C  CG    . PHE A 1 2072 ? 166.272 182.000 178.907 1.00 9.58  ? 2072 PHE A CG    1 
ATOM   4930  C  CD1   . PHE A 1 2072 ? 166.663 180.760 178.433 1.00 7.77  ? 2072 PHE A CD1   1 
ATOM   4931  C  CD2   . PHE A 1 2072 ? 167.170 183.054 178.832 1.00 8.01  ? 2072 PHE A CD2   1 
ATOM   4932  C  CE1   . PHE A 1 2072 ? 167.919 180.575 177.899 1.00 6.86  ? 2072 PHE A CE1   1 
ATOM   4933  C  CE2   . PHE A 1 2072 ? 168.427 182.872 178.299 1.00 5.59  ? 2072 PHE A CE2   1 
ATOM   4934  C  CZ    . PHE A 1 2072 ? 168.802 181.633 177.831 1.00 7.07  ? 2072 PHE A CZ    1 
ATOM   4935  N  N     . PHE A 1 2073 ? 165.891 183.450 182.231 1.00 6.61  ? 2073 PHE A N     1 
ATOM   4936  C  CA    . PHE A 1 2073 ? 166.940 183.967 183.101 1.00 5.86  ? 2073 PHE A CA    1 
ATOM   4937  C  C     . PHE A 1 2073 ? 166.968 183.215 184.425 1.00 8.65  ? 2073 PHE A C     1 
ATOM   4938  O  O     . PHE A 1 2073 ? 168.039 182.971 184.988 1.00 14.94 ? 2073 PHE A O     1 
ATOM   4939  C  CB    . PHE A 1 2073 ? 166.735 185.464 183.333 1.00 5.31  ? 2073 PHE A CB    1 
ATOM   4940  C  CG    . PHE A 1 2073 ? 167.498 186.333 182.381 1.00 3.55  ? 2073 PHE A CG    1 
ATOM   4941  C  CD1   . PHE A 1 2073 ? 167.121 186.424 181.053 1.00 3.19  ? 2073 PHE A CD1   1 
ATOM   4942  C  CD2   . PHE A 1 2073 ? 168.587 187.066 182.815 1.00 3.49  ? 2073 PHE A CD2   1 
ATOM   4943  C  CE1   . PHE A 1 2073 ? 167.822 187.222 180.174 1.00 3.72  ? 2073 PHE A CE1   1 
ATOM   4944  C  CE2   . PHE A 1 2073 ? 169.290 187.868 181.941 1.00 3.05  ? 2073 PHE A CE2   1 
ATOM   4945  C  CZ    . PHE A 1 2073 ? 168.907 187.946 180.619 1.00 3.57  ? 2073 PHE A CZ    1 
ATOM   4946  N  N     . LYS A 1 2074 ? 165.790 182.852 184.939 1.00 9.57  ? 2074 LYS A N     1 
ATOM   4947  C  CA    . LYS A 1 2074 ? 165.722 182.050 186.155 1.00 9.23  ? 2074 LYS A CA    1 
ATOM   4948  C  C     . LYS A 1 2074 ? 166.361 180.683 185.936 1.00 8.60  ? 2074 LYS A C     1 
ATOM   4949  O  O     . LYS A 1 2074 ? 167.106 180.192 186.791 1.00 9.62  ? 2074 LYS A O     1 
ATOM   4950  C  CB    . LYS A 1 2074 ? 164.260 181.916 186.592 1.00 11.02 ? 2074 LYS A CB    1 
ATOM   4951  C  CG    . LYS A 1 2074 ? 163.965 180.913 187.705 1.00 13.27 ? 2074 LYS A CG    1 
ATOM   4952  C  CD    . LYS A 1 2074 ? 164.927 181.039 188.877 1.00 16.45 ? 2074 LYS A CD    1 
ATOM   4953  C  CE    . LYS A 1 2074 ? 164.289 180.543 190.164 1.00 21.16 ? 2074 LYS A CE    1 
ATOM   4954  N  NZ    . LYS A 1 2074 ? 163.734 179.169 190.022 1.00 23.18 ? 2074 LYS A NZ    1 
ATOM   4955  N  N     . LEU A 1 2075 ? 166.094 180.062 184.784 1.00 8.23  ? 2075 LEU A N     1 
ATOM   4956  C  CA    . LEU A 1 2075 ? 166.687 178.762 184.482 1.00 7.77  ? 2075 LEU A CA    1 
ATOM   4957  C  C     . LEU A 1 2075 ? 168.202 178.854 184.357 1.00 11.58 ? 2075 LEU A C     1 
ATOM   4958  O  O     . LEU A 1 2075 ? 168.921 177.956 184.807 1.00 20.27 ? 2075 LEU A O     1 
ATOM   4959  C  CB    . LEU A 1 2075 ? 166.079 178.191 183.202 1.00 10.92 ? 2075 LEU A CB    1 
ATOM   4960  C  CG    . LEU A 1 2075 ? 164.708 177.526 183.312 1.00 14.09 ? 2075 LEU A CG    1 
ATOM   4961  C  CD1   . LEU A 1 2075 ? 163.939 177.676 182.009 1.00 11.03 ? 2075 LEU A CD1   1 
ATOM   4962  C  CD2   . LEU A 1 2075 ? 164.849 176.059 183.689 1.00 19.61 ? 2075 LEU A CD2   1 
ATOM   4963  N  N     . CYS A 1 2076 ? 168.708 179.928 183.745 1.00 10.88 ? 2076 CYS A N     1 
ATOM   4964  C  CA    . CYS A 1 2076 ? 170.153 180.073 183.583 1.00 10.70 ? 2076 CYS A CA    1 
ATOM   4965  C  C     . CYS A 1 2076 ? 170.855 180.163 184.931 1.00 7.53  ? 2076 CYS A C     1 
ATOM   4966  O  O     . CYS A 1 2076 ? 171.941 179.602 185.113 1.00 8.20  ? 2076 CYS A O     1 
ATOM   4967  C  CB    . CYS A 1 2076 ? 170.469 181.302 182.732 1.00 5.44  ? 2076 CYS A CB    1 
ATOM   4968  S  SG    . CYS A 1 2076 ? 170.169 181.070 180.970 1.00 14.32 ? 2076 CYS A SG    1 
ATOM   4969  N  N     . ASP A 1 2077 ? 170.246 180.861 185.891 1.00 10.07 ? 2077 ASP A N     1 
ATOM   4970  C  CA    . ASP A 1 2077 ? 170.836 180.989 187.216 1.00 6.99  ? 2077 ASP A CA    1 
ATOM   4971  C  C     . ASP A 1 2077 ? 170.940 179.655 187.942 1.00 8.24  ? 2077 ASP A C     1 
ATOM   4972  O  O     . ASP A 1 2077 ? 171.734 179.536 188.881 1.00 15.61 ? 2077 ASP A O     1 
ATOM   4973  C  CB    . ASP A 1 2077 ? 170.021 181.971 188.055 1.00 8.21  ? 2077 ASP A CB    1 
ATOM   4974  C  CG    . ASP A 1 2077 ? 170.789 182.493 189.247 1.00 15.30 ? 2077 ASP A CG    1 
ATOM   4975  O  OD1   . ASP A 1 2077 ? 172.021 182.656 189.137 1.00 21.89 ? 2077 ASP A OD1   1 
ATOM   4976  O  OD2   . ASP A 1 2077 ? 170.159 182.736 190.297 1.00 26.87 ? 2077 ASP A OD2   1 
ATOM   4977  N  N     . GLU A 1 2078 ? 170.168 178.653 187.533 1.00 12.88 ? 2078 GLU A N     1 
ATOM   4978  C  CA    . GLU A 1 2078 ? 170.161 177.354 188.194 1.00 11.52 ? 2078 GLU A CA    1 
ATOM   4979  C  C     . GLU A 1 2078 ? 170.680 176.223 187.323 1.00 12.03 ? 2078 GLU A C     1 
ATOM   4980  O  O     . GLU A 1 2078 ? 171.406 175.361 187.818 1.00 20.90 ? 2078 GLU A O     1 
ATOM   4981  C  CB    . GLU A 1 2078 ? 168.745 177.018 188.668 1.00 13.80 ? 2078 GLU A CB    1 
ATOM   4982  C  CG    . GLU A 1 2078 ? 168.396 177.621 190.013 1.00 17.10 ? 2078 GLU A CG    1 
ATOM   4983  C  CD    . GLU A 1 2078 ? 166.939 178.014 190.116 1.00 24.30 ? 2078 GLU A CD    1 
ATOM   4984  O  OE1   . GLU A 1 2078 ? 166.199 177.813 189.132 1.00 23.66 ? 2078 GLU A OE1   1 
ATOM   4985  O  OE2   . GLU A 1 2078 ? 166.535 178.523 191.181 1.00 21.72 ? 2078 GLU A OE2   1 
ATOM   4986  N  N     . GLN A 1 2079 ? 170.329 176.203 186.036 1.00 10.28 ? 2079 GLN A N     1 
ATOM   4987  C  CA    . GLN A 1 2079 ? 170.759 175.107 185.175 1.00 12.77 ? 2079 GLN A CA    1 
ATOM   4988  C  C     . GLN A 1 2079 ? 172.245 175.211 184.845 1.00 18.17 ? 2079 GLN A C     1 
ATOM   4989  O  O     . GLN A 1 2079 ? 172.938 174.191 184.757 1.00 28.19 ? 2079 GLN A O     1 
ATOM   4990  C  CB    . GLN A 1 2079 ? 169.922 175.089 183.896 1.00 13.59 ? 2079 GLN A CB    1 
ATOM   4991  C  CG    . GLN A 1 2079 ? 168.435 174.852 184.126 1.00 18.28 ? 2079 GLN A CG    1 
ATOM   4992  C  CD    . GLN A 1 2079 ? 168.130 173.476 184.679 1.00 19.07 ? 2079 GLN A CD    1 
ATOM   4993  O  OE1   . GLN A 1 2079 ? 168.742 172.488 184.288 1.00 22.18 ? 2079 GLN A OE1   1 
ATOM   4994  N  NE2   . GLN A 1 2079 ? 167.177 173.409 185.599 1.00 25.48 ? 2079 GLN A NE2   1 
ATOM   4995  N  N     . LEU A 1 2080 ? 172.749 176.427 184.654 1.00 15.20 ? 2080 LEU A N     1 
ATOM   4996  C  CA    . LEU A 1 2080 ? 174.152 176.629 184.330 1.00 11.40 ? 2080 LEU A CA    1 
ATOM   4997  C  C     . LEU A 1 2080 ? 175.020 176.498 185.577 1.00 12.42 ? 2080 LEU A C     1 
ATOM   4998  O  O     . LEU A 1 2080 ? 174.557 176.652 186.710 1.00 20.15 ? 2080 LEU A O     1 
ATOM   4999  C  CB    . LEU A 1 2080 ? 174.372 178.005 183.700 1.00 7.64  ? 2080 LEU A CB    1 
ATOM   5000  C  CG    . LEU A 1 2080 ? 173.594 178.345 182.432 1.00 5.16  ? 2080 LEU A CG    1 
ATOM   5001  C  CD1   . LEU A 1 2080 ? 173.894 179.771 182.001 1.00 11.77 ? 2080 LEU A CD1   1 
ATOM   5002  C  CD2   . LEU A 1 2080 ? 173.917 177.362 181.325 1.00 7.21  ? 2080 LEU A CD2   1 
ATOM   5003  N  N     . SER A 1 2081 ? 176.302 176.230 185.351 1.00 9.64  ? 2081 SER A N     1 
ATOM   5004  C  CA    . SER A 1 2081 ? 177.245 176.091 186.448 1.00 11.11 ? 2081 SER A CA    1 
ATOM   5005  C  C     . SER A 1 2081 ? 177.400 177.413 187.196 1.00 10.41 ? 2081 SER A C     1 
ATOM   5006  O  O     . SER A 1 2081 ? 177.057 178.487 186.698 1.00 11.95 ? 2081 SER A O     1 
ATOM   5007  C  CB    . SER A 1 2081 ? 178.605 175.621 185.936 1.00 13.05 ? 2081 SER A CB    1 
ATOM   5008  O  OG    . SER A 1 2081 ? 179.348 176.698 185.392 1.00 7.32  ? 2081 SER A OG    1 
ATOM   5009  N  N     . SER A 1 2082 ? 177.927 177.319 188.411 1.00 11.93 ? 2082 SER A N     1 
ATOM   5010  C  CA    . SER A 1 2082 ? 178.089 178.479 189.275 1.00 9.57  ? 2082 SER A CA    1 
ATOM   5011  C  C     . SER A 1 2082 ? 179.464 179.094 189.045 1.00 10.41 ? 2082 SER A C     1 
ATOM   5012  O  O     . SER A 1 2082 ? 180.488 178.423 189.220 1.00 8.62  ? 2082 SER A O     1 
ATOM   5013  C  CB    . SER A 1 2082 ? 177.909 178.087 190.739 1.00 13.77 ? 2082 SER A CB    1 
ATOM   5014  O  OG    . SER A 1 2082 ? 176.590 177.631 190.980 1.00 17.42 ? 2082 SER A OG    1 
ATOM   5015  N  N     . GLN A 1 2083 ? 179.483 180.363 188.645 1.00 13.08 ? 2083 GLN A N     1 
ATOM   5016  C  CA    . GLN A 1 2083 ? 180.711 181.112 188.433 1.00 4.84  ? 2083 GLN A CA    1 
ATOM   5017  C  C     . GLN A 1 2083 ? 180.587 182.475 189.098 1.00 2.56  ? 2083 GLN A C     1 
ATOM   5018  O  O     . GLN A 1 2083 ? 179.495 183.041 189.186 1.00 2.65  ? 2083 GLN A O     1 
ATOM   5019  C  CB    . GLN A 1 2083 ? 181.016 181.282 186.938 1.00 2.80  ? 2083 GLN A CB    1 
ATOM   5020  C  CG    . GLN A 1 2083 ? 180.921 179.999 186.127 1.00 2.11  ? 2083 GLN A CG    1 
ATOM   5021  C  CD    . GLN A 1 2083 ? 182.121 179.093 186.310 1.00 3.35  ? 2083 GLN A CD    1 
ATOM   5022  O  OE1   . GLN A 1 2083 ? 183.115 179.473 186.926 1.00 7.37  ? 2083 GLN A OE1   1 
ATOM   5023  N  NE2   . GLN A 1 2083 ? 182.031 177.880 185.781 1.00 3.80  ? 2083 GLN A NE2   1 
ATOM   5024  N  N     . SER A 1 2084 ? 181.720 183.001 189.570 1.00 6.58  ? 2084 SER A N     1 
ATOM   5025  C  CA    . SER A 1 2084 ? 181.710 184.305 190.223 1.00 5.44  ? 2084 SER A CA    1 
ATOM   5026  C  C     . SER A 1 2084 ? 181.387 185.439 189.258 1.00 3.58  ? 2084 SER A C     1 
ATOM   5027  O  O     . SER A 1 2084 ? 180.915 186.493 189.695 1.00 5.75  ? 2084 SER A O     1 
ATOM   5028  C  CB    . SER A 1 2084 ? 183.052 184.567 190.907 1.00 4.17  ? 2084 SER A CB    1 
ATOM   5029  O  OG    . SER A 1 2084 ? 184.139 184.228 190.065 1.00 19.36 ? 2084 SER A OG    1 
ATOM   5030  N  N     . HIS A 1 2085 ? 181.619 185.247 187.960 1.00 1.87  ? 2085 HIS A N     1 
ATOM   5031  C  CA    . HIS A 1 2085 ? 181.344 186.262 186.954 1.00 2.26  ? 2085 HIS A CA    1 
ATOM   5032  C  C     . HIS A 1 2085 ? 180.000 186.049 186.265 1.00 3.03  ? 2085 HIS A C     1 
ATOM   5033  O  O     . HIS A 1 2085 ? 179.810 186.508 185.135 1.00 7.04  ? 2085 HIS A O     1 
ATOM   5034  C  CB    . HIS A 1 2085 ? 182.469 186.298 185.921 1.00 1.31  ? 2085 HIS A CB    1 
ATOM   5035  C  CG    . HIS A 1 2085 ? 182.589 185.044 185.113 1.00 1.29  ? 2085 HIS A CG    1 
ATOM   5036  N  ND1   . HIS A 1 2085 ? 183.243 183.922 185.572 1.00 0.98  ? 2085 HIS A ND1   1 
ATOM   5037  C  CD2   . HIS A 1 2085 ? 182.144 184.738 183.872 1.00 1.52  ? 2085 HIS A CD2   1 
ATOM   5038  C  CE1   . HIS A 1 2085 ? 183.192 182.977 184.651 1.00 0.68  ? 2085 HIS A CE1   1 
ATOM   5039  N  NE2   . HIS A 1 2085 ? 182.530 183.447 183.610 1.00 0.74  ? 2085 HIS A NE2   1 
ATOM   5040  N  N     . TYR A 1 2086 ? 179.069 185.366 186.920 1.00 2.15  ? 2086 TYR A N     1 
ATOM   5041  C  CA    . TYR A 1 2086 ? 177.754 185.099 186.360 1.00 2.08  ? 2086 TYR A CA    1 
ATOM   5042  C  C     . TYR A 1 2086 ? 176.725 186.002 187.025 1.00 4.27  ? 2086 TYR A C     1 
ATOM   5043  O  O     . TYR A 1 2086 ? 176.657 186.073 188.255 1.00 7.91  ? 2086 TYR A O     1 
ATOM   5044  C  CB    . TYR A 1 2086 ? 177.363 183.633 186.549 1.00 2.54  ? 2086 TYR A CB    1 
ATOM   5045  C  CG    . TYR A 1 2086 ? 177.877 182.706 185.472 1.00 3.00  ? 2086 TYR A CG    1 
ATOM   5046  C  CD1   . TYR A 1 2086 ? 178.887 183.103 184.608 1.00 2.22  ? 2086 TYR A CD1   1 
ATOM   5047  C  CD2   . TYR A 1 2086 ? 177.360 181.425 185.332 1.00 3.25  ? 2086 TYR A CD2   1 
ATOM   5048  C  CE1   . TYR A 1 2086 ? 179.359 182.257 183.627 1.00 1.48  ? 2086 TYR A CE1   1 
ATOM   5049  C  CE2   . TYR A 1 2086 ? 177.829 180.571 184.356 1.00 2.90  ? 2086 TYR A CE2   1 
ATOM   5050  C  CZ    . TYR A 1 2086 ? 178.828 180.991 183.506 1.00 3.26  ? 2086 TYR A CZ    1 
ATOM   5051  O  OH    . TYR A 1 2086 ? 179.297 180.143 182.532 1.00 2.03  ? 2086 TYR A OH    1 
ATOM   5052  N  N     . ASP A 1 2087 ? 175.938 186.696 186.209 1.00 4.41  ? 2087 ASP A N     1 
ATOM   5053  C  CA    . ASP A 1 2087 ? 174.837 187.508 186.704 1.00 5.71  ? 2087 ASP A CA    1 
ATOM   5054  C  C     . ASP A 1 2087 ? 173.638 187.321 185.792 1.00 4.65  ? 2087 ASP A C     1 
ATOM   5055  O  O     . ASP A 1 2087 ? 173.752 187.474 184.572 1.00 6.17  ? 2087 ASP A O     1 
ATOM   5056  C  CB    . ASP A 1 2087 ? 175.208 188.992 186.775 1.00 9.48  ? 2087 ASP A CB    1 
ATOM   5057  C  CG    . ASP A 1 2087 ? 174.068 189.846 187.284 1.00 15.26 ? 2087 ASP A CG    1 
ATOM   5058  O  OD1   . ASP A 1 2087 ? 173.563 189.567 188.393 1.00 14.36 ? 2087 ASP A OD1   1 
ATOM   5059  O  OD2   . ASP A 1 2087 ? 173.656 190.780 186.563 1.00 11.62 ? 2087 ASP A OD2   1 
ATOM   5060  N  N     . PHE A 1 2088 ? 172.498 186.990 186.384 1.00 4.44  ? 2088 PHE A N     1 
ATOM   5061  C  CA    . PHE A 1 2088 ? 171.250 186.825 185.657 1.00 4.26  ? 2088 PHE A CA    1 
ATOM   5062  C  C     . PHE A 1 2088 ? 170.137 187.591 186.350 1.00 5.05  ? 2088 PHE A C     1 
ATOM   5063  O  O     . PHE A 1 2088 ? 168.975 187.177 186.356 1.00 11.90 ? 2088 PHE A O     1 
ATOM   5064  C  CB    . PHE A 1 2088 ? 170.900 185.347 185.511 1.00 6.92  ? 2088 PHE A CB    1 
ATOM   5065  C  CG    . PHE A 1 2088 ? 171.962 184.544 184.818 1.00 7.02  ? 2088 PHE A CG    1 
ATOM   5066  C  CD1   . PHE A 1 2088 ? 172.124 184.623 183.446 1.00 5.92  ? 2088 PHE A CD1   1 
ATOM   5067  C  CD2   . PHE A 1 2088 ? 172.805 183.716 185.539 1.00 6.16  ? 2088 PHE A CD2   1 
ATOM   5068  C  CE1   . PHE A 1 2088 ? 173.105 183.888 182.806 1.00 7.20  ? 2088 PHE A CE1   1 
ATOM   5069  C  CE2   . PHE A 1 2088 ? 173.786 182.981 184.905 1.00 4.03  ? 2088 PHE A CE2   1 
ATOM   5070  C  CZ    . PHE A 1 2088 ? 173.936 183.068 183.538 1.00 5.37  ? 2088 PHE A CZ    1 
ATOM   5071  N  N     . GLY A 1 2089 ? 170.485 188.729 186.941 1.00 3.10  ? 2089 GLY A N     1 
ATOM   5072  C  CA    . GLY A 1 2089 ? 169.547 189.552 187.672 1.00 3.28  ? 2089 GLY A CA    1 
ATOM   5073  C  C     . GLY A 1 2089 ? 168.842 190.557 186.789 1.00 2.43  ? 2089 GLY A C     1 
ATOM   5074  O  O     . GLY A 1 2089 ? 168.782 190.420 185.565 1.00 4.68  ? 2089 GLY A O     1 
ATOM   5075  N  N     . LEU A 1 2090 ? 168.297 191.591 187.433 1.00 2.09  ? 2090 LEU A N     1 
ATOM   5076  C  CA    . LEU A 1 2090 ? 167.481 192.564 186.713 1.00 1.49  ? 2090 LEU A CA    1 
ATOM   5077  C  C     . LEU A 1 2090 ? 168.319 193.415 185.764 1.00 1.33  ? 2090 LEU A C     1 
ATOM   5078  O  O     . LEU A 1 2090 ? 167.847 193.786 184.685 1.00 0.99  ? 2090 LEU A O     1 
ATOM   5079  C  CB    . LEU A 1 2090 ? 166.716 193.442 187.701 1.00 1.86  ? 2090 LEU A CB    1 
ATOM   5080  C  CG    . LEU A 1 2090 ? 165.657 194.353 187.078 1.00 1.72  ? 2090 LEU A CG    1 
ATOM   5081  C  CD1   . LEU A 1 2090 ? 164.721 193.555 186.186 1.00 0.95  ? 2090 LEU A CD1   1 
ATOM   5082  C  CD2   . LEU A 1 2090 ? 164.877 195.075 188.156 1.00 0.72  ? 2090 LEU A CD2   1 
ATOM   5083  N  N     . ARG A 1 2091 ? 169.558 193.743 186.146 1.00 1.30  ? 2091 ARG A N     1 
ATOM   5084  C  CA    . ARG A 1 2091 ? 170.433 194.474 185.231 1.00 0.87  ? 2091 ARG A CA    1 
ATOM   5085  C  C     . ARG A 1 2091 ? 170.682 193.677 183.959 1.00 1.18  ? 2091 ARG A C     1 
ATOM   5086  O  O     . ARG A 1 2091 ? 170.633 194.228 182.853 1.00 1.03  ? 2091 ARG A O     1 
ATOM   5087  C  CB    . ARG A 1 2091 ? 171.764 194.809 185.903 1.00 0.71  ? 2091 ARG A CB    1 
ATOM   5088  C  CG    . ARG A 1 2091 ? 171.696 195.812 187.031 1.00 1.30  ? 2091 ARG A CG    1 
ATOM   5089  C  CD    . ARG A 1 2091 ? 173.099 196.124 187.542 1.00 2.23  ? 2091 ARG A CD    1 
ATOM   5090  N  NE    . ARG A 1 2091 ? 173.099 196.711 188.876 1.00 4.96  ? 2091 ARG A NE    1 
ATOM   5091  C  CZ    . ARG A 1 2091 ? 172.579 197.890 189.187 1.00 1.30  ? 2091 ARG A CZ    1 
ATOM   5092  N  NH1   . ARG A 1 2091 ? 172.102 198.704 188.260 1.00 0.99  ? 2091 ARG A NH1   1 
ATOM   5093  N  NH2   . ARG A 1 2091 ? 172.554 198.271 190.459 1.00 0.80  ? 2091 ARG A NH2   1 
ATOM   5094  N  N     . ALA A 1 2092 ? 170.955 192.379 184.098 1.00 1.04  ? 2092 ALA A N     1 
ATOM   5095  C  CA    . ALA A 1 2092 ? 171.153 191.530 182.928 1.00 1.00  ? 2092 ALA A CA    1 
ATOM   5096  C  C     . ALA A 1 2092 ? 169.886 191.455 182.087 1.00 0.99  ? 2092 ALA A C     1 
ATOM   5097  O  O     . ALA A 1 2092 ? 169.939 191.535 180.856 1.00 1.08  ? 2092 ALA A O     1 
ATOM   5098  C  CB    . ALA A 1 2092 ? 171.600 190.136 183.367 1.00 2.69  ? 2092 ALA A CB    1 
ATOM   5099  N  N     . LEU A 1 2093 ? 168.731 191.303 182.741 1.00 1.29  ? 2093 LEU A N     1 
ATOM   5100  C  CA    . LEU A 1 2093 ? 167.463 191.293 182.020 1.00 1.06  ? 2093 LEU A CA    1 
ATOM   5101  C  C     . LEU A 1 2093 ? 167.209 192.630 181.337 1.00 0.81  ? 2093 LEU A C     1 
ATOM   5102  O  O     . LEU A 1 2093 ? 166.791 192.678 180.177 1.00 0.97  ? 2093 LEU A O     1 
ATOM   5103  C  CB    . LEU A 1 2093 ? 166.318 190.953 182.975 1.00 0.93  ? 2093 LEU A CB    1 
ATOM   5104  C  CG    . LEU A 1 2093 ? 164.919 190.961 182.354 1.00 0.61  ? 2093 LEU A CG    1 
ATOM   5105  C  CD1   . LEU A 1 2093 ? 164.794 189.892 181.275 1.00 1.07  ? 2093 LEU A CD1   1 
ATOM   5106  C  CD2   . LEU A 1 2093 ? 163.852 190.790 183.419 1.00 0.94  ? 2093 LEU A CD2   1 
ATOM   5107  N  N     . LYS A 1 2094 ? 167.465 193.731 182.049 1.00 0.91  ? 2094 LYS A N     1 
ATOM   5108  C  CA    . LYS A 1 2094 ? 167.281 195.056 181.464 1.00 0.79  ? 2094 LYS A CA    1 
ATOM   5109  C  C     . LYS A 1 2094 ? 168.192 195.258 180.262 1.00 1.04  ? 2094 LYS A C     1 
ATOM   5110  O  O     . LYS A 1 2094 ? 167.783 195.846 179.255 1.00 1.13  ? 2094 LYS A O     1 
ATOM   5111  C  CB    . LYS A 1 2094 ? 167.541 196.129 182.521 1.00 1.68  ? 2094 LYS A CB    1 
ATOM   5112  C  CG    . LYS A 1 2094 ? 167.081 197.521 182.135 1.00 1.24  ? 2094 LYS A CG    1 
ATOM   5113  C  CD    . LYS A 1 2094 ? 165.607 197.716 182.429 1.00 2.00  ? 2094 LYS A CD    1 
ATOM   5114  C  CE    . LYS A 1 2094 ? 165.181 199.151 182.172 1.00 2.26  ? 2094 LYS A CE    1 
ATOM   5115  N  NZ    . LYS A 1 2094 ? 165.884 200.109 183.061 1.00 2.64  ? 2094 LYS A NZ    1 
ATOM   5116  N  N     . SER A 1 2095 ? 169.436 194.780 180.355 1.00 1.29  ? 2095 SER A N     1 
ATOM   5117  C  CA    . SER A 1 2095 ? 170.377 194.909 179.248 1.00 0.60  ? 2095 SER A CA    1 
ATOM   5118  C  C     . SER A 1 2095 ? 169.867 194.193 178.002 1.00 1.25  ? 2095 SER A C     1 
ATOM   5119  O  O     . SER A 1 2095 ? 169.930 194.731 176.892 1.00 2.03  ? 2095 SER A O     1 
ATOM   5120  C  CB    . SER A 1 2095 ? 171.742 194.361 179.664 1.00 1.16  ? 2095 SER A CB    1 
ATOM   5121  O  OG    . SER A 1 2095 ? 172.642 194.333 178.569 1.00 15.11 ? 2095 SER A OG    1 
ATOM   5122  N  N     . VAL A 1 2096 ? 169.357 192.972 178.172 1.00 0.95  ? 2096 VAL A N     1 
ATOM   5123  C  CA    . VAL A 1 2096 ? 168.825 192.223 177.038 1.00 1.45  ? 2096 VAL A CA    1 
ATOM   5124  C  C     . VAL A 1 2096 ? 167.590 192.913 176.471 1.00 1.63  ? 2096 VAL A C     1 
ATOM   5125  O  O     . VAL A 1 2096 ? 167.430 193.023 175.250 1.00 2.83  ? 2096 VAL A O     1 
ATOM   5126  C  CB    . VAL A 1 2096 ? 168.527 190.769 177.453 1.00 2.90  ? 2096 VAL A CB    1 
ATOM   5127  C  CG1   . VAL A 1 2096 ? 167.789 190.038 176.349 1.00 1.97  ? 2096 VAL A CG1   1 
ATOM   5128  C  CG2   . VAL A 1 2096 ? 169.817 190.046 177.803 1.00 3.70  ? 2096 VAL A CG2   1 
ATOM   5129  N  N     . LEU A 1 2097 ? 166.700 193.388 177.347 1.00 1.52  ? 2097 LEU A N     1 
ATOM   5130  C  CA    . LEU A 1 2097 ? 165.475 194.037 176.887 1.00 1.44  ? 2097 LEU A CA    1 
ATOM   5131  C  C     . LEU A 1 2097 ? 165.776 195.313 176.110 1.00 4.36  ? 2097 LEU A C     1 
ATOM   5132  O  O     . LEU A 1 2097 ? 165.163 195.571 175.068 1.00 5.99  ? 2097 LEU A O     1 
ATOM   5133  C  CB    . LEU A 1 2097 ? 164.567 194.341 178.078 1.00 1.58  ? 2097 LEU A CB    1 
ATOM   5134  C  CG    . LEU A 1 2097 ? 163.962 193.145 178.815 1.00 1.04  ? 2097 LEU A CG    1 
ATOM   5135  C  CD1   . LEU A 1 2097 ? 163.249 193.608 180.074 1.00 0.93  ? 2097 LEU A CD1   1 
ATOM   5136  C  CD2   . LEU A 1 2097 ? 163.022 192.368 177.912 1.00 1.00  ? 2097 LEU A CD2   1 
ATOM   5137  N  N     . VAL A 1 2098 ? 166.704 196.132 176.608 1.00 2.74  ? 2098 VAL A N     1 
ATOM   5138  C  CA    . VAL A 1 2098 ? 167.090 197.340 175.890 1.00 2.59  ? 2098 VAL A CA    1 
ATOM   5139  C  C     . VAL A 1 2098 ? 167.767 196.983 174.573 1.00 3.41  ? 2098 VAL A C     1 
ATOM   5140  O  O     . VAL A 1 2098 ? 167.490 197.590 173.532 1.00 2.84  ? 2098 VAL A O     1 
ATOM   5141  C  CB    . VAL A 1 2098 ? 167.987 198.224 176.777 1.00 3.33  ? 2098 VAL A CB    1 
ATOM   5142  C  CG1   . VAL A 1 2098 ? 168.649 199.320 175.956 1.00 0.96  ? 2098 VAL A CG1   1 
ATOM   5143  C  CG2   . VAL A 1 2098 ? 167.175 198.825 177.911 1.00 5.01  ? 2098 VAL A CG2   1 
ATOM   5144  N  N     . SER A 1 2099 ? 168.658 195.988 174.598 1.00 3.62  ? 2099 SER A N     1 
ATOM   5145  C  CA    . SER A 1 2099 ? 169.305 195.537 173.371 1.00 2.22  ? 2099 SER A CA    1 
ATOM   5146  C  C     . SER A 1 2099 ? 168.299 194.957 172.387 1.00 2.37  ? 2099 SER A C     1 
ATOM   5147  O  O     . SER A 1 2099 ? 168.494 195.059 171.171 1.00 5.26  ? 2099 SER A O     1 
ATOM   5148  C  CB    . SER A 1 2099 ? 170.385 194.505 173.704 1.00 3.76  ? 2099 SER A CB    1 
ATOM   5149  O  OG    . SER A 1 2099 ? 171.154 194.177 172.562 1.00 13.31 ? 2099 SER A OG    1 
ATOM   5150  N  N     . ALA A 1 2100 ? 167.220 194.352 172.887 1.00 3.50  ? 2100 ALA A N     1 
ATOM   5151  C  CA    . ALA A 1 2100 ? 166.198 193.805 172.000 1.00 5.12  ? 2100 ALA A CA    1 
ATOM   5152  C  C     . ALA A 1 2100 ? 165.562 194.898 171.151 1.00 6.50  ? 2100 ALA A C     1 
ATOM   5153  O  O     . ALA A 1 2100 ? 165.330 194.707 169.952 1.00 7.64  ? 2100 ALA A O     1 
ATOM   5154  C  CB    . ALA A 1 2100 ? 165.135 193.068 172.812 1.00 5.02  ? 2100 ALA A CB    1 
ATOM   5155  N  N     . GLY A 1 2101 ? 165.270 196.050 171.755 1.00 5.27  ? 2101 GLY A N     1 
ATOM   5156  C  CA    . GLY A 1 2101 ? 164.725 197.158 170.988 1.00 3.95  ? 2101 GLY A CA    1 
ATOM   5157  C  C     . GLY A 1 2101 ? 165.704 197.689 169.959 1.00 5.71  ? 2101 GLY A C     1 
ATOM   5158  O  O     . GLY A 1 2101 ? 165.316 198.049 168.845 1.00 7.10  ? 2101 GLY A O     1 
ATOM   5159  N  N     . ASN A 1 2102 ? 166.987 197.754 170.321 1.00 6.60  ? 2102 ASN A N     1 
ATOM   5160  C  CA    . ASN A 1 2102 ? 168.001 198.198 169.373 1.00 4.73  ? 2102 ASN A CA    1 
ATOM   5161  C  C     . ASN A 1 2102 ? 168.141 197.219 168.212 1.00 6.22  ? 2102 ASN A C     1 
ATOM   5162  O  O     . ASN A 1 2102 ? 168.271 197.632 167.055 1.00 11.52 ? 2102 ASN A O     1 
ATOM   5163  C  CB    . ASN A 1 2102 ? 169.338 198.388 170.086 1.00 7.16  ? 2102 ASN A CB    1 
ATOM   5164  C  CG    . ASN A 1 2102 ? 169.376 199.649 170.923 1.00 10.57 ? 2102 ASN A CG    1 
ATOM   5165  O  OD1   . ASN A 1 2102 ? 168.993 200.722 170.463 1.00 20.08 ? 2102 ASN A OD1   1 
ATOM   5166  N  ND2   . ASN A 1 2102 ? 169.841 199.526 172.160 1.00 6.35  ? 2102 ASN A ND2   1 
ATOM   5167  N  N     . VAL A 1 2103 ? 168.113 195.916 168.503 1.00 5.62  ? 2103 VAL A N     1 
ATOM   5168  C  CA    . VAL A 1 2103 ? 168.220 194.916 167.443 1.00 6.51  ? 2103 VAL A CA    1 
ATOM   5169  C  C     . VAL A 1 2103 ? 166.988 194.951 166.548 1.00 8.78  ? 2103 VAL A C     1 
ATOM   5170  O  O     . VAL A 1 2103 ? 167.080 194.759 165.329 1.00 10.36 ? 2103 VAL A O     1 
ATOM   5171  C  CB    . VAL A 1 2103 ? 168.450 193.517 168.046 1.00 7.40  ? 2103 VAL A CB    1 
ATOM   5172  C  CG1   . VAL A 1 2103 ? 168.353 192.448 166.973 1.00 5.14  ? 2103 VAL A CG1   1 
ATOM   5173  C  CG2   . VAL A 1 2103 ? 169.803 193.449 168.733 1.00 9.10  ? 2103 VAL A CG2   1 
ATOM   5174  N  N     . LYS A 1 2104 ? 165.812 195.187 167.131 1.00 8.22  ? 2104 LYS A N     1 
ATOM   5175  C  CA    . LYS A 1 2104 ? 164.603 195.264 166.318 1.00 8.04  ? 2104 LYS A CA    1 
ATOM   5176  C  C     . LYS A 1 2104 ? 164.653 196.453 165.365 1.00 7.42  ? 2104 LYS A C     1 
ATOM   5177  O  O     . LYS A 1 2104 ? 164.227 196.348 164.211 1.00 8.16  ? 2104 LYS A O     1 
ATOM   5178  C  CB    . LYS A 1 2104 ? 163.365 195.340 167.210 1.00 10.76 ? 2104 LYS A CB    1 
ATOM   5179  C  CG    . LYS A 1 2104 ? 162.064 195.141 166.451 1.00 7.28  ? 2104 LYS A CG    1 
ATOM   5180  C  CD    . LYS A 1 2104 ? 160.889 194.932 167.384 1.00 9.35  ? 2104 LYS A CD    1 
ATOM   5181  C  CE    . LYS A 1 2104 ? 160.390 196.248 167.953 1.00 11.58 ? 2104 LYS A CE    1 
ATOM   5182  N  NZ    . LYS A 1 2104 ? 159.536 196.982 166.981 1.00 8.13  ? 2104 LYS A NZ    1 
ATOM   5183  N  N     . ARG A 1 2105 ? 165.172 197.591 165.831 1.00 11.36 ? 2105 ARG A N     1 
ATOM   5184  C  CA    . ARG A 1 2105 ? 165.244 198.774 164.979 1.00 7.24  ? 2105 ARG A CA    1 
ATOM   5185  C  C     . ARG A 1 2105 ? 166.207 198.570 163.814 1.00 12.17 ? 2105 ARG A C     1 
ATOM   5186  O  O     . ARG A 1 2105 ? 165.924 198.999 162.691 1.00 19.50 ? 2105 ARG A O     1 
ATOM   5187  C  CB    . ARG A 1 2105 ? 165.649 199.995 165.806 1.00 7.44  ? 2105 ARG A CB    1 
ATOM   5188  C  CG    . ARG A 1 2105 ? 164.510 200.610 166.608 1.00 7.54  ? 2105 ARG A CG    1 
ATOM   5189  C  CD    . ARG A 1 2105 ? 164.926 201.932 167.232 1.00 7.28  ? 2105 ARG A CD    1 
ATOM   5190  N  NE    . ARG A 1 2105 ? 165.781 201.742 168.398 1.00 12.29 ? 2105 ARG A NE    1 
ATOM   5191  C  CZ    . ARG A 1 2105 ? 165.356 201.331 169.584 1.00 10.33 ? 2105 ARG A CZ    1 
ATOM   5192  N  NH1   . ARG A 1 2105 ? 164.077 201.087 169.815 1.00 13.33 ? 2105 ARG A NH1   1 
ATOM   5193  N  NH2   . ARG A 1 2105 ? 166.237 201.161 170.567 1.00 10.63 ? 2105 ARG A NH2   1 
ATOM   5194  N  N     . GLU A 1 2106 ? 167.349 197.921 164.059 1.00 11.75 ? 2106 GLU A N     1 
ATOM   5195  C  CA    . GLU A 1 2106 ? 168.325 197.736 162.989 1.00 15.98 ? 2106 GLU A CA    1 
ATOM   5196  C  C     . GLU A 1 2106 ? 167.818 196.757 161.935 1.00 18.30 ? 2106 GLU A C     1 
ATOM   5197  O  O     . GLU A 1 2106 ? 168.083 196.931 160.740 1.00 25.56 ? 2106 GLU A O     1 
ATOM   5198  C  CB    . GLU A 1 2106 ? 169.670 197.279 163.562 1.00 9.17  ? 2106 GLU A CB    1 
ATOM   5199  C  CG    . GLU A 1 2106 ? 169.654 195.911 164.210 1.00 20.32 ? 2106 GLU A CG    1 
ATOM   5200  C  CD    . GLU A 1 2106 ? 170.986 195.527 164.822 1.00 24.14 ? 2106 GLU A CD    1 
ATOM   5201  O  OE1   . GLU A 1 2106 ? 171.928 196.343 164.764 1.00 19.37 ? 2106 GLU A OE1   1 
ATOM   5202  O  OE2   . GLU A 1 2106 ? 171.086 194.406 165.362 1.00 26.25 ? 2106 GLU A OE2   1 
ATOM   5203  N  N     . ARG A 1 2107 ? 167.088 195.718 162.353 1.00 11.15 ? 2107 ARG A N     1 
ATOM   5204  C  CA    . ARG A 1 2107 ? 166.508 194.794 161.381 1.00 12.30 ? 2107 ARG A CA    1 
ATOM   5205  C  C     . ARG A 1 2107 ? 165.472 195.482 160.506 1.00 17.32 ? 2107 ARG A C     1 
ATOM   5206  O  O     . ARG A 1 2107 ? 165.430 195.257 159.291 1.00 24.87 ? 2107 ARG A O     1 
ATOM   5207  C  CB    . ARG A 1 2107 ? 165.889 193.590 162.083 1.00 12.89 ? 2107 ARG A CB    1 
ATOM   5208  C  CG    . ARG A 1 2107 ? 166.872 192.672 162.767 1.00 13.49 ? 2107 ARG A CG    1 
ATOM   5209  C  CD    . ARG A 1 2107 ? 166.118 191.516 163.380 1.00 19.09 ? 2107 ARG A CD    1 
ATOM   5210  N  NE    . ARG A 1 2107 ? 166.973 190.612 164.138 1.00 26.59 ? 2107 ARG A NE    1 
ATOM   5211  C  CZ    . ARG A 1 2107 ? 167.599 189.568 163.615 1.00 18.53 ? 2107 ARG A CZ    1 
ATOM   5212  N  NH1   . ARG A 1 2107 ? 167.481 189.264 162.333 1.00 21.26 ? 2107 ARG A NH1   1 
ATOM   5213  N  NH2   . ARG A 1 2107 ? 168.353 188.803 164.400 1.00 21.63 ? 2107 ARG A NH2   1 
ATOM   5214  N  N     . ILE A 1 2108 ? 164.618 196.316 161.102 1.00 16.89 ? 2108 ILE A N     1 
ATOM   5215  C  CA    . ILE A 1 2108 ? 163.630 197.045 160.312 1.00 17.81 ? 2108 ILE A CA    1 
ATOM   5216  C  C     . ILE A 1 2108 ? 164.330 197.959 159.316 1.00 22.63 ? 2108 ILE A C     1 
ATOM   5217  O  O     . ILE A 1 2108 ? 163.935 198.046 158.147 1.00 27.37 ? 2108 ILE A O     1 
ATOM   5218  C  CB    . ILE A 1 2108 ? 162.673 197.825 161.232 1.00 16.22 ? 2108 ILE A CB    1 
ATOM   5219  C  CG1   . ILE A 1 2108 ? 161.865 196.857 162.095 1.00 15.13 ? 2108 ILE A CG1   1 
ATOM   5220  C  CG2   . ILE A 1 2108 ? 161.744 198.709 160.416 1.00 14.40 ? 2108 ILE A CG2   1 
ATOM   5221  C  CD1   . ILE A 1 2108 ? 160.873 197.534 163.013 1.00 10.67 ? 2108 ILE A CD1   1 
ATOM   5222  N  N     . GLN A 1 2109 ? 165.387 198.643 159.758 1.00 22.48 ? 2109 GLN A N     1 
ATOM   5223  C  CA    . GLN A 1 2109 ? 166.182 199.450 158.840 1.00 23.03 ? 2109 GLN A CA    1 
ATOM   5224  C  C     . GLN A 1 2109 ? 166.871 198.588 157.792 1.00 27.26 ? 2109 GLN A C     1 
ATOM   5225  O  O     . GLN A 1 2109 ? 167.024 199.013 156.642 1.00 28.54 ? 2109 GLN A O     1 
ATOM   5226  C  CB    . GLN A 1 2109 ? 167.216 200.265 159.616 1.00 20.57 ? 2109 GLN A CB    1 
ATOM   5227  C  CG    . GLN A 1 2109 ? 166.622 201.410 160.413 1.00 23.10 ? 2109 GLN A CG    1 
ATOM   5228  C  CD    . GLN A 1 2109 ? 165.898 202.408 159.537 1.00 33.36 ? 2109 GLN A CD    1 
ATOM   5229  O  OE1   . GLN A 1 2109 ? 164.673 202.517 159.584 1.00 36.67 ? 2109 GLN A OE1   1 
ATOM   5230  N  NE2   . GLN A 1 2109 ? 166.652 203.145 158.731 1.00 29.37 ? 2109 GLN A NE2   1 
ATOM   5231  N  N     . LYS A 1 2110 ? 167.300 197.381 158.169 1.00 21.09 ? 2110 LYS A N     1 
ATOM   5232  C  CA    . LYS A 1 2110 ? 167.942 196.488 157.209 1.00 21.20 ? 2110 LYS A CA    1 
ATOM   5233  C  C     . LYS A 1 2110 ? 166.936 195.930 156.209 1.00 22.79 ? 2110 LYS A C     1 
ATOM   5234  O  O     . LYS A 1 2110 ? 167.250 195.790 155.021 1.00 26.93 ? 2110 LYS A O     1 
ATOM   5235  C  CB    . LYS A 1 2110 ? 168.656 195.355 157.945 1.00 20.08 ? 2110 LYS A CB    1 
ATOM   5236  C  CG    . LYS A 1 2110 ? 169.285 194.318 157.036 1.00 22.38 ? 2110 LYS A CG    1 
ATOM   5237  C  CD    . LYS A 1 2110 ? 169.393 192.971 157.729 1.00 28.08 ? 2110 LYS A CD    1 
ATOM   5238  C  CE    . LYS A 1 2110 ? 170.557 192.161 157.183 1.00 25.18 ? 2110 LYS A CE    1 
ATOM   5239  N  NZ    . LYS A 1 2110 ? 170.331 191.753 155.769 1.00 29.23 ? 2110 LYS A NZ    1 
ATOM   5240  N  N     . ILE A 1 2111 ? 165.727 195.600 156.668 1.00 24.44 ? 2111 ILE A N     1 
ATOM   5241  C  CA    . ILE A 1 2111 ? 164.718 195.031 155.775 1.00 22.73 ? 2111 ILE A CA    1 
ATOM   5242  C  C     . ILE A 1 2111 ? 164.340 196.032 154.692 1.00 26.33 ? 2111 ILE A C     1 
ATOM   5243  O  O     . ILE A 1 2111 ? 164.271 195.693 153.504 1.00 31.89 ? 2111 ILE A O     1 
ATOM   5244  C  CB    . ILE A 1 2111 ? 163.484 194.578 156.576 1.00 17.58 ? 2111 ILE A CB    1 
ATOM   5245  C  CG1   . ILE A 1 2111 ? 163.808 193.340 157.411 1.00 18.51 ? 2111 ILE A CG1   1 
ATOM   5246  C  CG2   . ILE A 1 2111 ? 162.315 194.299 155.646 1.00 16.08 ? 2111 ILE A CG2   1 
ATOM   5247  C  CD1   . ILE A 1 2111 ? 162.678 192.905 158.312 1.00 15.26 ? 2111 ILE A CD1   1 
ATOM   5248  N  N     . LYS A 1 2112 ? 164.097 197.284 155.083 1.00 26.96 ? 2112 LYS A N     1 
ATOM   5249  C  CA    . LYS A 1 2112 ? 163.743 198.299 154.099 1.00 25.62 ? 2112 LYS A CA    1 
ATOM   5250  C  C     . LYS A 1 2112 ? 164.939 198.692 153.241 1.00 30.51 ? 2112 LYS A C     1 
ATOM   5251  O  O     . LYS A 1 2112 ? 164.763 199.080 152.082 1.00 31.27 ? 2112 LYS A O     1 
ATOM   5252  C  CB    . LYS A 1 2112 ? 163.144 199.526 154.790 1.00 26.28 ? 2112 LYS A CB    1 
ATOM   5253  C  CG    . LYS A 1 2112 ? 164.043 200.186 155.812 1.00 26.94 ? 2112 LYS A CG    1 
ATOM   5254  C  CD    . LYS A 1 2112 ? 163.308 201.303 156.533 1.00 34.18 ? 2112 LYS A CD    1 
ATOM   5255  C  CE    . LYS A 1 2112 ? 162.052 200.782 157.218 1.00 33.16 ? 2112 LYS A CE    1 
ATOM   5256  N  NZ    . LYS A 1 2112 ? 161.355 201.848 157.988 1.00 29.39 ? 2112 LYS A NZ    1 
ATOM   5257  N  N     . ARG A 1 2113 ? 166.157 198.595 153.783 1.00 31.95 ? 2113 ARG A N     1 
ATOM   5258  C  CA    . ARG A 1 2113 ? 167.345 198.833 152.967 1.00 24.50 ? 2113 ARG A CA    1 
ATOM   5259  C  C     . ARG A 1 2113 ? 167.438 197.816 151.837 1.00 30.48 ? 2113 ARG A C     1 
ATOM   5260  O  O     . ARG A 1 2113 ? 167.820 198.161 150.711 1.00 36.67 ? 2113 ARG A O     1 
ATOM   5261  C  CB    . ARG A 1 2113 ? 168.603 198.795 153.830 1.00 25.63 ? 2113 ARG A CB    1 
ATOM   5262  C  CG    . ARG A 1 2113 ? 169.071 200.160 154.307 1.00 27.63 ? 2113 ARG A CG    1 
ATOM   5263  C  CD    . ARG A 1 2113 ? 170.231 200.037 155.284 1.00 23.86 ? 2113 ARG A CD    1 
ATOM   5264  N  NE    . ARG A 1 2113 ? 169.817 199.460 156.557 1.00 29.43 ? 2113 ARG A NE    1 
ATOM   5265  C  CZ    . ARG A 1 2113 ? 170.632 199.237 157.578 1.00 32.04 ? 2113 ARG A CZ    1 
ATOM   5266  N  NH1   . ARG A 1 2113 ? 171.921 199.528 157.510 1.00 28.59 ? 2113 ARG A NH1   1 
ATOM   5267  N  NH2   . ARG A 1 2113 ? 170.144 198.708 158.697 1.00 27.16 ? 2113 ARG A NH2   1 
ATOM   5268  N  N     . GLU A 1 2114 ? 167.100 196.556 152.119 1.00 27.41 ? 2114 GLU A N     1 
ATOM   5269  C  CA    . GLU A 1 2114 ? 166.976 195.571 151.050 1.00 30.91 ? 2114 GLU A CA    1 
ATOM   5270  C  C     . GLU A 1 2114 ? 165.838 195.924 150.106 1.00 32.05 ? 2114 GLU A C     1 
ATOM   5271  O  O     . GLU A 1 2114 ? 165.908 195.626 148.907 1.00 34.94 ? 2114 GLU A O     1 
ATOM   5272  C  CB    . GLU A 1 2114 ? 166.762 194.175 151.636 1.00 29.20 ? 2114 GLU A CB    1 
ATOM   5273  C  CG    . GLU A 1 2114 ? 167.821 193.741 152.632 1.00 28.95 ? 2114 GLU A CG    1 
ATOM   5274  C  CD    . GLU A 1 2114 ? 169.221 194.137 152.208 1.00 36.16 ? 2114 GLU A CD    1 
ATOM   5275  O  OE1   . GLU A 1 2114 ? 169.668 193.682 151.133 1.00 35.67 ? 2114 GLU A OE1   1 
ATOM   5276  O  OE2   . GLU A 1 2114 ? 169.873 194.903 152.947 1.00 32.65 ? 2114 GLU A OE2   1 
ATOM   5277  N  N     . LYS A 1 2115 ? 164.781 196.553 150.623 1.00 29.75 ? 2115 LYS A N     1 
ATOM   5278  C  CA    . LYS A 1 2115 ? 163.643 196.902 149.781 1.00 29.63 ? 2115 LYS A CA    1 
ATOM   5279  C  C     . LYS A 1 2115 ? 163.978 198.050 148.835 1.00 31.36 ? 2115 LYS A C     1 
ATOM   5280  O  O     . LYS A 1 2115 ? 163.428 198.126 147.731 1.00 35.74 ? 2115 LYS A O     1 
ATOM   5281  C  CB    . LYS A 1 2115 ? 162.436 197.253 150.649 1.00 27.31 ? 2115 LYS A CB    1 
ATOM   5282  C  CG    . LYS A 1 2115 ? 161.717 196.043 151.226 1.00 29.44 ? 2115 LYS A CG    1 
ATOM   5283  C  CD    . LYS A 1 2115 ? 160.329 196.415 151.719 1.00 32.62 ? 2115 LYS A CD    1 
ATOM   5284  C  CE    . LYS A 1 2115 ? 159.505 195.182 152.038 1.00 25.41 ? 2115 LYS A CE    1 
ATOM   5285  N  NZ    . LYS A 1 2115 ? 160.029 194.447 153.220 1.00 27.16 ? 2115 LYS A NZ    1 
ATOM   5286  N  N     . GLU A 1 2116 ? 164.870 198.955 149.247 1.00 30.58 ? 2116 GLU A N     1 
ATOM   5287  C  CA    . GLU A 1 2116 ? 165.255 200.059 148.371 1.00 33.35 ? 2116 GLU A CA    1 
ATOM   5288  C  C     . GLU A 1 2116 ? 165.906 199.545 147.093 1.00 34.61 ? 2116 GLU A C     1 
ATOM   5289  O  O     . GLU A 1 2116 ? 165.641 200.062 146.001 1.00 32.25 ? 2116 GLU A O     1 
ATOM   5290  C  CB    . GLU A 1 2116 ? 166.195 201.020 149.100 1.00 30.92 ? 2116 GLU A CB    1 
ATOM   5291  C  CG    . GLU A 1 2116 ? 165.644 201.586 150.396 1.00 33.61 ? 2116 GLU A CG    1 
ATOM   5292  C  CD    . GLU A 1 2116 ? 164.183 201.977 150.292 1.00 38.58 ? 2116 GLU A CD    1 
ATOM   5293  O  OE1   . GLU A 1 2116 ? 163.851 202.822 149.435 1.00 36.56 ? 2116 GLU A OE1   1 
ATOM   5294  O  OE2   . GLU A 1 2116 ? 163.368 201.440 151.072 1.00 36.31 ? 2116 GLU A OE2   1 
ATOM   5295  N  N     . GLU A 1 2117 ? 166.757 198.531 147.208 1.00 32.59 ? 2117 GLU A N     1 
ATOM   5296  C  CA    . GLU A 1 2117 ? 167.408 197.925 146.054 1.00 35.78 ? 2117 GLU A CA    1 
ATOM   5297  C  C     . GLU A 1 2117 ? 166.612 196.770 145.457 1.00 33.63 ? 2117 GLU A C     1 
ATOM   5298  O  O     . GLU A 1 2117 ? 167.042 196.197 144.452 1.00 37.81 ? 2117 GLU A O     1 
ATOM   5299  C  CB    . GLU A 1 2117 ? 168.824 197.471 146.435 1.00 33.84 ? 2117 GLU A CB    1 
ATOM   5300  C  CG    . GLU A 1 2117 ? 168.902 196.441 147.558 1.00 38.80 ? 2117 GLU A CG    1 
ATOM   5301  C  CD    . GLU A 1 2117 ? 168.778 195.011 147.074 1.00 41.34 ? 2117 GLU A CD    1 
ATOM   5302  O  OE1   . GLU A 1 2117 ? 169.003 194.765 145.872 1.00 41.46 ? 2117 GLU A OE1   1 
ATOM   5303  O  OE2   . GLU A 1 2117 ? 168.466 194.130 147.904 1.00 40.60 ? 2117 GLU A OE2   1 
ATOM   5304  N  N     . ARG A 1 2118 ? 165.464 196.422 146.042 1.00 33.84 ? 2118 ARG A N     1 
ATOM   5305  C  CA    . ARG A 1 2118 ? 164.546 195.425 145.485 1.00 34.76 ? 2118 ARG A CA    1 
ATOM   5306  C  C     . ARG A 1 2118 ? 163.143 196.028 145.476 1.00 34.74 ? 2118 ARG A C     1 
ATOM   5307  O  O     . ARG A 1 2118 ? 162.372 195.841 146.422 1.00 40.30 ? 2118 ARG A O     1 
ATOM   5308  C  CB    . ARG A 1 2118 ? 164.586 194.118 146.279 1.00 31.25 ? 2118 ARG A CB    1 
ATOM   5309  C  CG    . ARG A 1 2118 ? 165.897 193.362 146.189 1.00 32.04 ? 2118 ARG A CG    1 
ATOM   5310  C  CD    . ARG A 1 2118 ? 166.274 193.074 144.745 1.00 36.32 ? 2118 ARG A CD    1 
ATOM   5311  N  NE    . ARG A 1 2118 ? 165.187 192.436 144.014 1.00 37.68 ? 2118 ARG A NE    1 
ATOM   5312  C  CZ    . ARG A 1 2118 ? 164.624 192.932 142.920 1.00 38.37 ? 2118 ARG A CZ    1 
ATOM   5313  N  NH1   . ARG A 1 2118 ? 165.023 194.081 142.399 1.00 37.83 ? 2118 ARG A NH1   1 
ATOM   5314  N  NH2   . ARG A 1 2118 ? 163.638 192.259 142.334 1.00 38.94 ? 2118 ARG A NH2   1 
ATOM   5315  N  N     . GLY A 1 2119 ? 162.814 196.746 144.407 1.00 32.94 ? 2119 GLY A N     1 
ATOM   5316  C  CA    . GLY A 1 2119 ? 161.490 197.311 144.257 1.00 33.75 ? 2119 GLY A CA    1 
ATOM   5317  C  C     . GLY A 1 2119 ? 161.265 198.551 145.103 1.00 37.03 ? 2119 GLY A C     1 
ATOM   5318  O  O     . GLY A 1 2119 ? 162.194 199.213 145.574 1.00 36.93 ? 2119 GLY A O     1 
ATOM   5319  N  N     . GLU A 1 2120 ? 159.988 198.880 145.269 1.00 32.73 ? 2120 GLU A N     1 
ATOM   5320  C  CA    . GLU A 1 2120 ? 159.556 200.028 146.064 1.00 36.90 ? 2120 GLU A CA    1 
ATOM   5321  C  C     . GLU A 1 2120 ? 158.336 199.650 146.899 1.00 36.07 ? 2120 GLU A C     1 
ATOM   5322  O  O     . GLU A 1 2120 ? 157.336 200.369 146.947 1.00 35.87 ? 2120 GLU A O     1 
ATOM   5323  C  CB    . GLU A 1 2120 ? 159.269 201.236 145.172 1.00 34.90 ? 2120 GLU A CB    1 
ATOM   5324  C  CG    . GLU A 1 2120 ? 160.517 201.961 144.694 1.00 34.48 ? 2120 GLU A CG    1 
ATOM   5325  C  CD    . GLU A 1 2120 ? 160.197 203.213 143.903 1.00 40.32 ? 2120 GLU A CD    1 
ATOM   5326  O  OE1   . GLU A 1 2120 ? 159.512 204.105 144.448 1.00 40.28 ? 2120 GLU A OE1   1 
ATOM   5327  O  OE2   . GLU A 1 2120 ? 160.632 203.308 142.736 1.00 38.65 ? 2120 GLU A OE2   1 
ATOM   5328  N  N     . ALA A 1 2121 ? 158.410 198.502 147.568 1.00 32.58 ? 2121 ALA A N     1 
ATOM   5329  C  CA    . ALA A 1 2121 ? 157.277 197.925 148.288 1.00 31.17 ? 2121 ALA A CA    1 
ATOM   5330  C  C     . ALA A 1 2121 ? 157.325 198.218 149.784 1.00 30.95 ? 2121 ALA A C     1 
ATOM   5331  O  O     . ALA A 1 2121 ? 156.959 197.364 150.596 1.00 31.13 ? 2121 ALA A O     1 
ATOM   5332  C  CB    . ALA A 1 2121 ? 157.209 196.422 148.041 1.00 28.92 ? 2121 ALA A CB    1 
ATOM   5333  N  N     . VAL A 1 2122 ? 157.777 199.410 150.177 1.00 32.16 ? 2122 VAL A N     1 
ATOM   5334  C  CA    . VAL A 1 2122 ? 157.836 199.780 151.588 1.00 29.19 ? 2122 VAL A CA    1 
ATOM   5335  C  C     . VAL A 1 2122 ? 156.424 199.792 152.162 1.00 31.49 ? 2122 VAL A C     1 
ATOM   5336  O  O     . VAL A 1 2122 ? 155.596 200.632 151.796 1.00 34.92 ? 2122 VAL A O     1 
ATOM   5337  C  CB    . VAL A 1 2122 ? 158.523 201.143 151.781 1.00 29.90 ? 2122 VAL A CB    1 
ATOM   5338  C  CG1   . VAL A 1 2122 ? 158.395 201.600 153.227 1.00 31.01 ? 2122 VAL A CG1   1 
ATOM   5339  C  CG2   . VAL A 1 2122 ? 159.985 201.064 151.368 1.00 23.11 ? 2122 VAL A CG2   1 
ATOM   5340  N  N     . ASP A 1 2123 ? 156.145 198.850 153.061 1.00 28.74 ? 2123 ASP A N     1 
ATOM   5341  C  CA    . ASP A 1 2123 ? 154.816 198.651 153.631 1.00 31.15 ? 2123 ASP A CA    1 
ATOM   5342  C  C     . ASP A 1 2123 ? 154.915 198.440 155.137 1.00 33.58 ? 2123 ASP A C     1 
ATOM   5343  O  O     . ASP A 1 2123 ? 154.432 197.436 155.672 1.00 32.73 ? 2123 ASP A O     1 
ATOM   5344  C  CB    . ASP A 1 2123 ? 154.092 197.486 152.959 1.00 28.62 ? 2123 ASP A CB    1 
ATOM   5345  C  CG    . ASP A 1 2123 ? 152.589 197.548 153.150 1.00 35.25 ? 2123 ASP A CG    1 
ATOM   5346  O  OD1   . ASP A 1 2123 ? 151.983 198.566 152.754 1.00 36.80 ? 2123 ASP A OD1   1 
ATOM   5347  O  OD2   . ASP A 1 2123 ? 152.009 196.582 153.685 1.00 39.28 ? 2123 ASP A OD2   1 
ATOM   5348  N  N     . GLU A 1 2124 ? 155.555 199.388 155.831 1.00 31.81 ? 2124 GLU A N     1 
ATOM   5349  C  CA    . GLU A 1 2124 ? 156.005 199.278 157.220 1.00 26.78 ? 2124 GLU A CA    1 
ATOM   5350  C  C     . GLU A 1 2124 ? 155.075 198.471 158.122 1.00 27.01 ? 2124 GLU A C     1 
ATOM   5351  O  O     . GLU A 1 2124 ? 155.547 197.685 158.951 1.00 32.86 ? 2124 GLU A O     1 
ATOM   5352  C  CB    . GLU A 1 2124 ? 156.208 200.675 157.823 1.00 27.87 ? 2124 GLU A CB    1 
ATOM   5353  C  CG    . GLU A 1 2124 ? 155.011 201.621 157.719 1.00 29.75 ? 2124 GLU A CG    1 
ATOM   5354  C  CD    . GLU A 1 2124 ? 154.855 202.249 156.345 1.00 38.06 ? 2124 GLU A CD    1 
ATOM   5355  O  OE1   . GLU A 1 2124 ? 155.696 201.980 155.464 1.00 35.37 ? 2124 GLU A OE1   1 
ATOM   5356  O  OE2   . GLU A 1 2124 ? 153.888 203.017 156.151 1.00 35.94 ? 2124 GLU A OE2   1 
ATOM   5357  N  N     . GLY A 1 2125 ? 153.765 198.666 157.993 1.00 27.26 ? 2125 GLY A N     1 
ATOM   5358  C  CA    . GLY A 1 2125 ? 152.818 197.879 158.757 1.00 31.48 ? 2125 GLY A CA    1 
ATOM   5359  C  C     . GLY A 1 2125 ? 152.969 196.388 158.536 1.00 30.12 ? 2125 GLY A C     1 
ATOM   5360  O  O     . GLY A 1 2125 ? 152.981 195.610 159.493 1.00 30.74 ? 2125 GLY A O     1 
ATOM   5361  N  N     . GLU A 1 2126 ? 153.098 195.975 157.271 1.00 31.54 ? 2126 GLU A N     1 
ATOM   5362  C  CA    . GLU A 1 2126 ? 153.341 194.568 156.976 1.00 32.31 ? 2126 GLU A CA    1 
ATOM   5363  C  C     . GLU A 1 2126 ? 154.759 194.155 157.354 1.00 31.18 ? 2126 GLU A C     1 
ATOM   5364  O  O     . GLU A 1 2126 ? 155.003 192.980 157.651 1.00 27.23 ? 2126 GLU A O     1 
ATOM   5365  C  CB    . GLU A 1 2126 ? 153.080 194.287 155.496 1.00 30.95 ? 2126 GLU A CB    1 
ATOM   5366  C  CG    . GLU A 1 2126 ? 153.305 192.845 155.069 1.00 34.83 ? 2126 GLU A CG    1 
ATOM   5367  C  CD    . GLU A 1 2126 ? 153.023 192.622 153.596 1.00 39.85 ? 2126 GLU A CD    1 
ATOM   5368  O  OE1   . GLU A 1 2126 ? 152.650 193.594 152.906 1.00 41.60 ? 2126 GLU A OE1   1 
ATOM   5369  O  OE2   . GLU A 1 2126 ? 153.175 191.474 153.128 1.00 38.08 ? 2126 GLU A OE2   1 
ATOM   5370  N  N     . ILE A 1 2127 ? 155.698 195.103 157.353 1.00 26.91 ? 2127 ILE A N     1 
ATOM   5371  C  CA    . ILE A 1 2127 ? 157.070 194.792 157.740 1.00 26.88 ? 2127 ILE A CA    1 
ATOM   5372  C  C     . ILE A 1 2127 ? 157.117 194.300 159.180 1.00 26.21 ? 2127 ILE A C     1 
ATOM   5373  O  O     . ILE A 1 2127 ? 157.859 193.365 159.510 1.00 29.68 ? 2127 ILE A O     1 
ATOM   5374  C  CB    . ILE A 1 2127 ? 157.976 196.019 157.525 1.00 28.03 ? 2127 ILE A CB    1 
ATOM   5375  C  CG1   . ILE A 1 2127 ? 157.918 196.471 156.064 1.00 29.69 ? 2127 ILE A CG1   1 
ATOM   5376  C  CG2   . ILE A 1 2127 ? 159.407 195.710 157.935 1.00 17.59 ? 2127 ILE A CG2   1 
ATOM   5377  C  CD1   . ILE A 1 2127 ? 158.902 197.568 155.719 1.00 28.35 ? 2127 ILE A CD1   1 
ATOM   5378  N  N     . ALA A 1 2128 ? 156.323 194.912 160.058 1.00 28.28 ? 2128 ALA A N     1 
ATOM   5379  C  CA    . ALA A 1 2128 ? 156.244 194.458 161.441 1.00 27.22 ? 2128 ALA A CA    1 
ATOM   5380  C  C     . ALA A 1 2128 ? 155.448 193.169 161.590 1.00 30.44 ? 2128 ALA A C     1 
ATOM   5381  O  O     . ALA A 1 2128 ? 155.587 192.488 162.612 1.00 26.69 ? 2128 ALA A O     1 
ATOM   5382  C  CB    . ALA A 1 2128 ? 155.626 195.547 162.320 1.00 19.35 ? 2128 ALA A CB    1 
ATOM   5383  N  N     . GLU A 1 2129 ? 154.615 192.822 160.607 1.00 27.80 ? 2129 GLU A N     1 
ATOM   5384  C  CA    . GLU A 1 2129 ? 153.845 191.584 160.691 1.00 25.08 ? 2129 GLU A CA    1 
ATOM   5385  C  C     . GLU A 1 2129 ? 154.751 190.366 160.576 1.00 27.84 ? 2129 GLU A C     1 
ATOM   5386  O  O     . GLU A 1 2129 ? 154.657 189.431 161.378 1.00 29.48 ? 2129 GLU A O     1 
ATOM   5387  C  CB    . GLU A 1 2129 ? 152.767 191.559 159.607 1.00 29.17 ? 2129 GLU A CB    1 
ATOM   5388  C  CG    . GLU A 1 2129 ? 151.667 192.595 159.791 1.00 29.91 ? 2129 GLU A CG    1 
ATOM   5389  C  CD    . GLU A 1 2129 ? 150.699 192.238 160.905 1.00 39.25 ? 2129 GLU A CD    1 
ATOM   5390  O  OE1   . GLU A 1 2129 ? 150.811 191.128 161.467 1.00 38.03 ? 2129 GLU A OE1   1 
ATOM   5391  O  OE2   . GLU A 1 2129 ? 149.823 193.070 161.221 1.00 46.44 ? 2129 GLU A OE2   1 
ATOM   5392  N  N     . ASN A 1 2130 ? 155.632 190.354 159.575 1.00 27.93 ? 2130 ASN A N     1 
ATOM   5393  C  CA    . ASN A 1 2130 ? 156.586 189.264 159.383 1.00 23.14 ? 2130 ASN A CA    1 
ATOM   5394  C  C     . ASN A 1 2130 ? 157.944 189.715 159.915 1.00 26.02 ? 2130 ASN A C     1 
ATOM   5395  O  O     . ASN A 1 2130 ? 158.862 190.045 159.166 1.00 30.02 ? 2130 ASN A O     1 
ATOM   5396  C  CB    . ASN A 1 2130 ? 156.653 188.864 157.914 1.00 23.75 ? 2130 ASN A CB    1 
ATOM   5397  C  CG    . ASN A 1 2130 ? 155.339 188.313 157.401 1.00 28.63 ? 2130 ASN A CG    1 
ATOM   5398  O  OD1   . ASN A 1 2130 ? 154.698 188.910 156.536 1.00 31.77 ? 2130 ASN A OD1   1 
ATOM   5399  N  ND2   . ASN A 1 2130 ? 154.928 187.169 157.936 1.00 30.36 ? 2130 ASN A ND2   1 
ATOM   5400  N  N     . LEU A 1 2131 ? 158.063 189.723 161.241 1.00 25.48 ? 2131 LEU A N     1 
ATOM   5401  C  CA    . LEU A 1 2131 ? 159.305 190.099 161.907 1.00 19.45 ? 2131 LEU A CA    1 
ATOM   5402  C  C     . LEU A 1 2131 ? 159.605 189.059 162.977 1.00 21.54 ? 2131 LEU A C     1 
ATOM   5403  O  O     . LEU A 1 2131 ? 158.785 188.867 163.899 1.00 25.32 ? 2131 LEU A O     1 
ATOM   5404  C  CB    . LEU A 1 2131 ? 159.209 191.501 162.514 1.00 21.90 ? 2131 LEU A CB    1 
ATOM   5405  C  CG    . LEU A 1 2131 ? 160.486 192.013 163.178 1.00 21.06 ? 2131 LEU A CG    1 
ATOM   5406  C  CD1   . LEU A 1 2131 ? 161.598 192.130 162.148 1.00 20.44 ? 2131 LEU A CD1   1 
ATOM   5407  C  CD2   . LEU A 1 2131 ? 160.244 193.344 163.868 1.00 11.21 ? 2131 LEU A CD2   1 
ATOM   5408  N  N     . PRO A 1 2132 ? 160.747 188.370 162.910 1.00 22.99 ? 2132 PRO A N     1 
ATOM   5409  C  CA    . PRO A 1 2132 ? 161.033 187.308 163.883 1.00 17.69 ? 2132 PRO A CA    1 
ATOM   5410  C  C     . PRO A 1 2132 ? 161.354 187.858 165.262 1.00 15.57 ? 2132 PRO A C     1 
ATOM   5411  O  O     . PRO A 1 2132 ? 162.526 187.986 165.629 1.00 18.31 ? 2132 PRO A O     1 
ATOM   5412  C  CB    . PRO A 1 2132 ? 162.243 186.589 163.272 1.00 20.17 ? 2132 PRO A CB    1 
ATOM   5413  C  CG    . PRO A 1 2132 ? 162.272 187.023 161.834 1.00 17.17 ? 2132 PRO A CG    1 
ATOM   5414  C  CD    . PRO A 1 2132 ? 161.758 188.420 161.846 1.00 16.91 ? 2132 PRO A CD    1 
ATOM   5415  N  N     . GLU A 1 2133 ? 160.314 188.186 166.032 1.00 14.55 ? 2133 GLU A N     1 
ATOM   5416  C  CA    . GLU A 1 2133 ? 160.518 188.815 167.333 1.00 13.32 ? 2133 GLU A CA    1 
ATOM   5417  C  C     . GLU A 1 2133 ? 161.262 187.892 168.291 1.00 12.83 ? 2133 GLU A C     1 
ATOM   5418  O  O     . GLU A 1 2133 ? 162.101 188.352 169.074 1.00 18.99 ? 2133 GLU A O     1 
ATOM   5419  C  CB    . GLU A 1 2133 ? 159.175 189.243 167.923 1.00 17.62 ? 2133 GLU A CB    1 
ATOM   5420  C  CG    . GLU A 1 2133 ? 158.594 190.479 167.266 1.00 13.78 ? 2133 GLU A CG    1 
ATOM   5421  C  CD    . GLU A 1 2133 ? 157.272 190.898 167.872 1.00 14.39 ? 2133 GLU A CD    1 
ATOM   5422  O  OE1   . GLU A 1 2133 ? 156.822 190.239 168.830 1.00 13.59 ? 2133 GLU A OE1   1 
ATOM   5423  O  OE2   . GLU A 1 2133 ? 156.682 191.886 167.388 1.00 17.42 ? 2133 GLU A OE2   1 
ATOM   5424  N  N     . GLN A 1 2134 ? 160.962 186.593 168.256 1.00 11.11 ? 2134 GLN A N     1 
ATOM   5425  C  CA    . GLN A 1 2134 ? 161.703 185.650 169.088 1.00 12.27 ? 2134 GLN A CA    1 
ATOM   5426  C  C     . GLN A 1 2134 ? 163.174 185.603 168.692 1.00 11.08 ? 2134 GLN A C     1 
ATOM   5427  O  O     . GLN A 1 2134 ? 164.052 185.568 169.559 1.00 10.94 ? 2134 GLN A O     1 
ATOM   5428  C  CB    . GLN A 1 2134 ? 161.077 184.259 169.007 1.00 12.15 ? 2134 GLN A CB    1 
ATOM   5429  C  CG    . GLN A 1 2134 ? 159.751 184.139 169.734 1.00 11.02 ? 2134 GLN A CG    1 
ATOM   5430  C  CD    . GLN A 1 2134 ? 159.446 182.724 170.169 1.00 15.46 ? 2134 GLN A CD    1 
ATOM   5431  O  OE1   . GLN A 1 2134 ? 160.271 181.823 170.019 1.00 18.09 ? 2134 GLN A OE1   1 
ATOM   5432  N  NE2   . GLN A 1 2134 ? 158.254 182.518 170.715 1.00 20.27 ? 2134 GLN A NE2   1 
ATOM   5433  N  N     . GLU A 1 2135 ? 163.460 185.611 167.388 1.00 14.21 ? 2135 GLU A N     1 
ATOM   5434  C  CA    . GLU A 1 2135 ? 164.847 185.599 166.935 1.00 10.79 ? 2135 GLU A CA    1 
ATOM   5435  C  C     . GLU A 1 2135 ? 165.582 186.868 167.344 1.00 9.89  ? 2135 GLU A C     1 
ATOM   5436  O  O     . GLU A 1 2135 ? 166.786 186.824 167.622 1.00 12.07 ? 2135 GLU A O     1 
ATOM   5437  C  CB    . GLU A 1 2135 ? 164.901 185.411 165.418 1.00 13.69 ? 2135 GLU A CB    1 
ATOM   5438  C  CG    . GLU A 1 2135 ? 166.294 185.207 164.859 1.00 15.51 ? 2135 GLU A CG    1 
ATOM   5439  C  CD    . GLU A 1 2135 ? 166.469 185.829 163.489 1.00 28.13 ? 2135 GLU A CD    1 
ATOM   5440  O  OE1   . GLU A 1 2135 ? 167.334 185.351 162.724 1.00 34.51 ? 2135 GLU A OE1   1 
ATOM   5441  O  OE2   . GLU A 1 2135 ? 165.744 186.796 163.173 1.00 29.61 ? 2135 GLU A OE2   1 
ATOM   5442  N  N     . ILE A 1 2136 ? 164.879 188.002 167.388 1.00 12.21 ? 2136 ILE A N     1 
ATOM   5443  C  CA    . ILE A 1 2136 ? 165.486 189.246 167.850 1.00 6.73  ? 2136 ILE A CA    1 
ATOM   5444  C  C     . ILE A 1 2136 ? 165.910 189.115 169.307 1.00 6.53  ? 2136 ILE A C     1 
ATOM   5445  O  O     . ILE A 1 2136 ? 167.019 189.508 169.690 1.00 8.12  ? 2136 ILE A O     1 
ATOM   5446  C  CB    . ILE A 1 2136 ? 164.511 190.421 167.651 1.00 10.11 ? 2136 ILE A CB    1 
ATOM   5447  C  CG1   . ILE A 1 2136 ? 164.260 190.655 166.164 1.00 10.12 ? 2136 ILE A CG1   1 
ATOM   5448  C  CG2   . ILE A 1 2136 ? 165.044 191.683 168.310 1.00 7.71  ? 2136 ILE A CG2   1 
ATOM   5449  C  CD1   . ILE A 1 2136 ? 163.139 191.622 165.876 1.00 12.24 ? 2136 ILE A CD1   1 
ATOM   5450  N  N     . LEU A 1 2137 ? 165.031 188.554 170.140 1.00 6.93  ? 2137 LEU A N     1 
ATOM   5451  C  CA    . LEU A 1 2137 ? 165.336 188.405 171.559 1.00 5.61  ? 2137 LEU A CA    1 
ATOM   5452  C  C     . LEU A 1 2137 ? 166.493 187.437 171.781 1.00 7.31  ? 2137 LEU A C     1 
ATOM   5453  O  O     . LEU A 1 2137 ? 167.320 187.644 172.677 1.00 8.78  ? 2137 LEU A O     1 
ATOM   5454  C  CB    . LEU A 1 2137 ? 164.089 187.943 172.313 1.00 4.85  ? 2137 LEU A CB    1 
ATOM   5455  C  CG    . LEU A 1 2137 ? 164.113 188.030 173.840 1.00 5.21  ? 2137 LEU A CG    1 
ATOM   5456  C  CD1   . LEU A 1 2137 ? 164.445 189.437 174.300 1.00 7.96  ? 2137 LEU A CD1   1 
ATOM   5457  C  CD2   . LEU A 1 2137 ? 162.781 187.580 174.414 1.00 8.36  ? 2137 LEU A CD2   1 
ATOM   5458  N  N     . ILE A 1 2138 ? 166.566 186.371 170.981 1.00 4.68  ? 2138 ILE A N     1 
ATOM   5459  C  CA    . ILE A 1 2138 ? 167.649 185.403 171.129 1.00 6.73  ? 2138 ILE A CA    1 
ATOM   5460  C  C     . ILE A 1 2138 ? 168.988 186.046 170.795 1.00 7.23  ? 2138 ILE A C     1 
ATOM   5461  O  O     . ILE A 1 2138 ? 170.001 185.782 171.457 1.00 7.92  ? 2138 ILE A O     1 
ATOM   5462  C  CB    . ILE A 1 2138 ? 167.384 184.161 170.259 1.00 8.89  ? 2138 ILE A CB    1 
ATOM   5463  C  CG1   . ILE A 1 2138 ? 166.064 183.508 170.659 1.00 10.31 ? 2138 ILE A CG1   1 
ATOM   5464  C  CG2   . ILE A 1 2138 ? 168.518 183.164 170.387 1.00 8.07  ? 2138 ILE A CG2   1 
ATOM   5465  C  CD1   . ILE A 1 2138 ? 166.029 183.037 172.075 1.00 11.52 ? 2138 ILE A CD1   1 
ATOM   5466  N  N     . GLN A 1 2139 ? 169.017 186.893 169.766 1.00 5.41  ? 2139 GLN A N     1 
ATOM   5467  C  CA    . GLN A 1 2139 ? 170.251 187.578 169.400 1.00 5.14  ? 2139 GLN A CA    1 
ATOM   5468  C  C     . GLN A 1 2139 ? 170.750 188.462 170.535 1.00 6.97  ? 2139 GLN A C     1 
ATOM   5469  O  O     . GLN A 1 2139 ? 171.949 188.483 170.832 1.00 10.73 ? 2139 GLN A O     1 
ATOM   5470  C  CB    . GLN A 1 2139 ? 170.032 188.399 168.130 1.00 4.83  ? 2139 GLN A CB    1 
ATOM   5471  C  CG    . GLN A 1 2139 ? 171.293 189.009 167.559 1.00 7.20  ? 2139 GLN A CG    1 
ATOM   5472  C  CD    . GLN A 1 2139 ? 171.009 190.001 166.451 1.00 7.50  ? 2139 GLN A CD    1 
ATOM   5473  O  OE1   . GLN A 1 2139 ? 170.220 189.728 165.548 1.00 15.19 ? 2139 GLN A OE1   1 
ATOM   5474  N  NE2   . GLN A 1 2139 ? 171.654 191.158 166.511 1.00 7.80  ? 2139 GLN A NE2   1 
ATOM   5475  N  N     . SER A 1 2140 ? 169.844 189.191 171.188 1.00 6.37  ? 2140 SER A N     1 
ATOM   5476  C  CA    . SER A 1 2140 ? 170.242 190.025 172.316 1.00 5.01  ? 2140 SER A CA    1 
ATOM   5477  C  C     . SER A 1 2140 ? 170.768 189.181 173.471 1.00 4.73  ? 2140 SER A C     1 
ATOM   5478  O  O     . SER A 1 2140 ? 171.736 189.565 174.135 1.00 11.23 ? 2140 SER A O     1 
ATOM   5479  C  CB    . SER A 1 2140 ? 169.068 190.887 172.772 1.00 4.86  ? 2140 SER A CB    1 
ATOM   5480  O  OG    . SER A 1 2140 ? 168.528 191.608 171.681 1.00 13.49 ? 2140 SER A OG    1 
ATOM   5481  N  N     . VAL A 1 2141 ? 170.138 188.033 173.727 1.00 5.72  ? 2141 VAL A N     1 
ATOM   5482  C  CA    . VAL A 1 2141 ? 170.596 187.149 174.795 1.00 5.94  ? 2141 VAL A CA    1 
ATOM   5483  C  C     . VAL A 1 2141 ? 171.998 186.634 174.492 1.00 4.61  ? 2141 VAL A C     1 
ATOM   5484  O  O     . VAL A 1 2141 ? 172.888 186.660 175.348 1.00 5.90  ? 2141 VAL A O     1 
ATOM   5485  C  CB    . VAL A 1 2141 ? 169.603 185.990 174.994 1.00 3.60  ? 2141 VAL A CB    1 
ATOM   5486  C  CG1   . VAL A 1 2141 ? 170.218 184.900 175.856 1.00 6.72  ? 2141 VAL A CG1   1 
ATOM   5487  C  CG2   . VAL A 1 2141 ? 168.320 186.496 175.615 1.00 2.79  ? 2141 VAL A CG2   1 
ATOM   5488  N  N     . CYS A 1 2142 ? 172.216 186.171 173.261 1.00 3.26  ? 2142 CYS A N     1 
ATOM   5489  C  CA    . CYS A 1 2142 ? 173.499 185.567 172.920 1.00 4.89  ? 2142 CYS A CA    1 
ATOM   5490  C  C     . CYS A 1 2142 ? 174.607 186.611 172.838 1.00 6.87  ? 2142 CYS A C     1 
ATOM   5491  O  O     . CYS A 1 2142 ? 175.747 186.343 173.233 1.00 6.28  ? 2142 CYS A O     1 
ATOM   5492  C  CB    . CYS A 1 2142 ? 173.375 184.798 171.607 1.00 5.03  ? 2142 CYS A CB    1 
ATOM   5493  S  SG    . CYS A 1 2142 ? 172.388 183.290 171.742 1.00 12.58 ? 2142 CYS A SG    1 
ATOM   5494  N  N     . GLU A 1 2143 ? 174.295 187.805 172.332 1.00 4.56  ? 2143 GLU A N     1 
ATOM   5495  C  CA    . GLU A 1 2143 ? 175.285 188.873 172.291 1.00 3.61  ? 2143 GLU A CA    1 
ATOM   5496  C  C     . GLU A 1 2143 ? 175.693 189.343 173.681 1.00 4.70  ? 2143 GLU A C     1 
ATOM   5497  O  O     . GLU A 1 2143 ? 176.737 189.986 173.821 1.00 10.31 ? 2143 GLU A O     1 
ATOM   5498  C  CB    . GLU A 1 2143 ? 174.747 190.058 171.488 1.00 6.66  ? 2143 GLU A CB    1 
ATOM   5499  C  CG    . GLU A 1 2143 ? 174.642 189.819 169.993 1.00 7.68  ? 2143 GLU A CG    1 
ATOM   5500  C  CD    . GLU A 1 2143 ? 174.565 191.112 169.211 1.00 14.43 ? 2143 GLU A CD    1 
ATOM   5501  O  OE1   . GLU A 1 2143 ? 173.700 191.222 168.319 1.00 11.66 ? 2143 GLU A OE1   1 
ATOM   5502  O  OE2   . GLU A 1 2143 ? 175.358 192.029 169.503 1.00 26.55 ? 2143 GLU A OE2   1 
ATOM   5503  N  N     . THR A 1 2144 ? 174.904 189.032 174.707 1.00 4.52  ? 2144 THR A N     1 
ATOM   5504  C  CA    . THR A 1 2144 ? 175.133 189.554 176.045 1.00 2.78  ? 2144 THR A CA    1 
ATOM   5505  C  C     . THR A 1 2144 ? 175.463 188.476 177.069 1.00 4.20  ? 2144 THR A C     1 
ATOM   5506  O  O     . THR A 1 2144 ? 176.309 188.706 177.936 1.00 8.85  ? 2144 THR A O     1 
ATOM   5507  C  CB    . THR A 1 2144 ? 173.902 190.349 176.509 1.00 6.98  ? 2144 THR A CB    1 
ATOM   5508  O  OG1   . THR A 1 2144 ? 173.809 191.563 175.758 1.00 10.96 ? 2144 THR A OG1   1 
ATOM   5509  C  CG2   . THR A 1 2144 ? 174.012 190.725 177.966 1.00 13.09 ? 2144 THR A CG2   1 
ATOM   5510  N  N     . MET A 1 2145 ? 174.844 187.298 176.975 1.00 5.64  ? 2145 MET A N     1 
ATOM   5511  C  CA    . MET A 1 2145 ? 175.093 186.185 177.886 1.00 3.42  ? 2145 MET A CA    1 
ATOM   5512  C  C     . MET A 1 2145 ? 176.209 185.249 177.448 1.00 2.02  ? 2145 MET A C     1 
ATOM   5513  O  O     . MET A 1 2145 ? 176.950 184.760 178.301 1.00 2.57  ? 2145 MET A O     1 
ATOM   5514  C  CB    . MET A 1 2145 ? 173.816 185.353 178.073 1.00 6.37  ? 2145 MET A CB    1 
ATOM   5515  C  CG    . MET A 1 2145 ? 172.647 186.041 178.770 1.00 8.61  ? 2145 MET A CG    1 
ATOM   5516  S  SD    . MET A 1 2145 ? 172.993 186.548 180.468 1.00 38.89 ? 2145 MET A SD    1 
ATOM   5517  C  CE    . MET A 1 2145 ? 173.273 188.300 180.296 1.00 11.11 ? 2145 MET A CE    1 
ATOM   5518  N  N     . VAL A 1 2146 ? 176.337 184.973 176.148 1.00 1.64  ? 2146 VAL A N     1 
ATOM   5519  C  CA    . VAL A 1 2146 ? 177.292 183.959 175.692 1.00 1.91  ? 2146 VAL A CA    1 
ATOM   5520  C  C     . VAL A 1 2146 ? 178.738 184.297 176.047 1.00 1.17  ? 2146 VAL A C     1 
ATOM   5521  O  O     . VAL A 1 2146 ? 179.459 183.399 176.515 1.00 1.65  ? 2146 VAL A O     1 
ATOM   5522  C  CB    . VAL A 1 2146 ? 177.099 183.689 174.189 1.00 1.92  ? 2146 VAL A CB    1 
ATOM   5523  C  CG1   . VAL A 1 2146 ? 178.349 183.066 173.583 1.00 1.13  ? 2146 VAL A CG1   1 
ATOM   5524  C  CG2   . VAL A 1 2146 ? 175.894 182.792 173.968 1.00 1.37  ? 2146 VAL A CG2   1 
ATOM   5525  N  N     . PRO A 1 2147 ? 179.229 185.529 175.859 1.00 1.78  ? 2147 PRO A N     1 
ATOM   5526  C  CA    . PRO A 1 2147 ? 180.653 185.790 176.137 1.00 1.55  ? 2147 PRO A CA    1 
ATOM   5527  C  C     . PRO A 1 2147 ? 181.074 185.530 177.574 1.00 0.78  ? 2147 PRO A C     1 
ATOM   5528  O  O     . PRO A 1 2147 ? 182.267 185.321 177.820 1.00 1.55  ? 2147 PRO A O     1 
ATOM   5529  C  CB    . PRO A 1 2147 ? 180.812 187.272 175.769 1.00 1.21  ? 2147 PRO A CB    1 
ATOM   5530  C  CG    . PRO A 1 2147 ? 179.764 187.500 174.758 1.00 0.93  ? 2147 PRO A CG    1 
ATOM   5531  C  CD    . PRO A 1 2147 ? 178.594 186.716 175.257 1.00 0.88  ? 2147 PRO A CD    1 
ATOM   5532  N  N     . LYS A 1 2148 ? 180.147 185.543 178.531 1.00 1.15  ? 2148 LYS A N     1 
ATOM   5533  C  CA    . LYS A 1 2148 ? 180.492 185.279 179.923 1.00 1.07  ? 2148 LYS A CA    1 
ATOM   5534  C  C     . LYS A 1 2148 ? 180.564 183.793 180.248 1.00 1.05  ? 2148 LYS A C     1 
ATOM   5535  O  O     . LYS A 1 2148 ? 181.029 183.437 181.335 1.00 2.51  ? 2148 LYS A O     1 
ATOM   5536  C  CB    . LYS A 1 2148 ? 179.479 185.952 180.852 1.00 1.17  ? 2148 LYS A CB    1 
ATOM   5537  C  CG    . LYS A 1 2148 ? 178.278 185.089 181.202 1.00 2.46  ? 2148 LYS A CG    1 
ATOM   5538  C  CD    . LYS A 1 2148 ? 177.386 185.758 182.230 1.00 4.09  ? 2148 LYS A CD    1 
ATOM   5539  C  CE    . LYS A 1 2148 ? 176.918 187.118 181.748 1.00 10.67 ? 2148 LYS A CE    1 
ATOM   5540  N  NZ    . LYS A 1 2148 ? 175.914 187.718 182.663 1.00 13.03 ? 2148 LYS A NZ    1 
ATOM   5541  N  N     . LEU A 1 2149 ? 180.136 182.926 179.340 1.00 1.23  ? 2149 LEU A N     1 
ATOM   5542  C  CA    . LEU A 1 2149 ? 179.982 181.514 179.651 1.00 1.46  ? 2149 LEU A CA    1 
ATOM   5543  C  C     . LEU A 1 2149 ? 181.307 180.771 179.557 1.00 1.66  ? 2149 LEU A C     1 
ATOM   5544  O  O     . LEU A 1 2149 ? 182.132 181.047 178.684 1.00 2.61  ? 2149 LEU A O     1 
ATOM   5545  C  CB    . LEU A 1 2149 ? 178.971 180.877 178.703 1.00 2.22  ? 2149 LEU A CB    1 
ATOM   5546  C  CG    . LEU A 1 2149 ? 177.536 181.378 178.827 1.00 2.04  ? 2149 LEU A CG    1 
ATOM   5547  C  CD1   . LEU A 1 2149 ? 176.666 180.661 177.818 1.00 2.12  ? 2149 LEU A CD1   1 
ATOM   5548  C  CD2   . LEU A 1 2149 ? 177.013 181.194 180.240 1.00 1.35  ? 2149 LEU A CD2   1 
ATOM   5549  N  N     . VAL A 1 2150 ? 181.503 179.817 180.466 1.00 2.37  ? 2150 VAL A N     1 
ATOM   5550  C  CA    . VAL A 1 2150 ? 182.606 178.872 180.354 1.00 3.63  ? 2150 VAL A CA    1 
ATOM   5551  C  C     . VAL A 1 2150 ? 182.240 177.871 179.268 1.00 4.30  ? 2150 VAL A C     1 
ATOM   5552  O  O     . VAL A 1 2150 ? 181.088 177.817 178.827 1.00 5.12  ? 2150 VAL A O     1 
ATOM   5553  C  CB    . VAL A 1 2150 ? 182.907 178.176 181.695 1.00 3.13  ? 2150 VAL A CB    1 
ATOM   5554  C  CG1   . VAL A 1 2150 ? 183.335 179.200 182.739 1.00 1.27  ? 2150 VAL A CG1   1 
ATOM   5555  C  CG2   . VAL A 1 2150 ? 181.702 177.378 182.172 1.00 4.94  ? 2150 VAL A CG2   1 
ATOM   5556  N  N     . ALA A 1 2151 ? 183.218 177.075 178.829 1.00 4.58  ? 2151 ALA A N     1 
ATOM   5557  C  CA    . ALA A 1 2151 ? 183.017 176.234 177.653 1.00 5.03  ? 2151 ALA A CA    1 
ATOM   5558  C  C     . ALA A 1 2151 ? 181.898 175.220 177.863 1.00 9.15  ? 2151 ALA A C     1 
ATOM   5559  O  O     . ALA A 1 2151 ? 181.105 174.966 176.949 1.00 6.90  ? 2151 ALA A O     1 
ATOM   5560  C  CB    . ALA A 1 2151 ? 184.320 175.523 177.289 1.00 2.84  ? 2151 ALA A CB    1 
ATOM   5561  N  N     . GLU A 1 2152 ? 181.815 174.629 179.057 1.00 9.65  ? 2152 GLU A N     1 
ATOM   5562  C  CA    . GLU A 1 2152 ? 180.837 173.569 179.279 1.00 7.48  ? 2152 GLU A CA    1 
ATOM   5563  C  C     . GLU A 1 2152 ? 179.428 174.113 179.494 1.00 10.18 ? 2152 GLU A C     1 
ATOM   5564  O  O     . GLU A 1 2152 ? 178.460 173.351 179.429 1.00 15.40 ? 2152 GLU A O     1 
ATOM   5565  C  CB    . GLU A 1 2152 ? 181.283 172.689 180.450 1.00 13.18 ? 2152 GLU A CB    1 
ATOM   5566  C  CG    . GLU A 1 2152 ? 181.452 173.405 181.782 1.00 18.37 ? 2152 GLU A CG    1 
ATOM   5567  C  CD    . GLU A 1 2152 ? 180.172 173.505 182.581 1.00 15.11 ? 2152 GLU A CD    1 
ATOM   5568  O  OE1   . GLU A 1 2152 ? 179.228 172.732 182.313 1.00 14.57 ? 2152 GLU A OE1   1 
ATOM   5569  O  OE2   . GLU A 1 2152 ? 180.119 174.352 183.493 1.00 18.37 ? 2152 GLU A OE2   1 
ATOM   5570  N  N     . ASP A 1 2153 ? 179.287 175.418 179.738 1.00 8.57  ? 2153 ASP A N     1 
ATOM   5571  C  CA    . ASP A 1 2153 ? 177.960 176.015 179.849 1.00 6.93  ? 2153 ASP A CA    1 
ATOM   5572  C  C     . ASP A 1 2153 ? 177.394 176.466 178.509 1.00 7.08  ? 2153 ASP A C     1 
ATOM   5573  O  O     . ASP A 1 2153 ? 176.178 176.658 178.405 1.00 11.98 ? 2153 ASP A O     1 
ATOM   5574  C  CB    . ASP A 1 2153 ? 177.985 177.203 180.811 1.00 6.88  ? 2153 ASP A CB    1 
ATOM   5575  C  CG    . ASP A 1 2153 ? 177.972 176.781 182.263 1.00 7.65  ? 2153 ASP A CG    1 
ATOM   5576  O  OD1   . ASP A 1 2153 ? 177.767 175.582 182.534 1.00 17.44 ? 2153 ASP A OD1   1 
ATOM   5577  O  OD2   . ASP A 1 2153 ? 178.165 177.648 183.135 1.00 8.94  ? 2153 ASP A OD2   1 
ATOM   5578  N  N     . ILE A 1 2154 ? 178.239 176.642 177.492 1.00 6.07  ? 2154 ILE A N     1 
ATOM   5579  C  CA    . ILE A 1 2154 ? 177.746 177.111 176.194 1.00 6.47  ? 2154 ILE A CA    1 
ATOM   5580  C  C     . ILE A 1 2154 ? 176.730 176.150 175.583 1.00 8.54  ? 2154 ILE A C     1 
ATOM   5581  O  O     . ILE A 1 2154 ? 175.652 176.610 175.172 1.00 15.53 ? 2154 ILE A O     1 
ATOM   5582  C  CB    . ILE A 1 2154 ? 178.930 177.407 175.256 1.00 4.66  ? 2154 ILE A CB    1 
ATOM   5583  C  CG1   . ILE A 1 2154 ? 179.843 178.470 175.871 1.00 4.93  ? 2154 ILE A CG1   1 
ATOM   5584  C  CG2   . ILE A 1 2154 ? 178.433 177.861 173.894 1.00 7.09  ? 2154 ILE A CG2   1 
ATOM   5585  C  CD1   . ILE A 1 2154 ? 181.146 178.653 175.138 1.00 6.31  ? 2154 ILE A CD1   1 
ATOM   5586  N  N     . PRO A 1 2155 ? 176.988 174.839 175.485 1.00 11.39 ? 2155 PRO A N     1 
ATOM   5587  C  CA    . PRO A 1 2155 ? 175.932 173.940 174.990 1.00 7.72  ? 2155 PRO A CA    1 
ATOM   5588  C  C     . PRO A 1 2155 ? 174.709 173.898 175.888 1.00 9.70  ? 2155 PRO A C     1 
ATOM   5589  O  O     . PRO A 1 2155 ? 173.595 173.699 175.389 1.00 14.45 ? 2155 PRO A O     1 
ATOM   5590  C  CB    . PRO A 1 2155 ? 176.635 172.576 174.924 1.00 8.53  ? 2155 PRO A CB    1 
ATOM   5591  C  CG    . PRO A 1 2155 ? 178.082 172.896 174.883 1.00 7.15  ? 2155 PRO A CG    1 
ATOM   5592  C  CD    . PRO A 1 2155 ? 178.227 174.091 175.758 1.00 6.89  ? 2155 PRO A CD    1 
ATOM   5593  N  N     . LEU A 1 2156 ? 174.886 174.070 177.201 1.00 9.84  ? 2156 LEU A N     1 
ATOM   5594  C  CA    . LEU A 1 2156 ? 173.749 174.056 178.115 1.00 7.57  ? 2156 LEU A CA    1 
ATOM   5595  C  C     . LEU A 1 2156 ? 172.778 175.188 177.813 1.00 8.33  ? 2156 LEU A C     1 
ATOM   5596  O  O     . LEU A 1 2156 ? 171.561 174.976 177.764 1.00 12.54 ? 2156 LEU A O     1 
ATOM   5597  C  CB    . LEU A 1 2156 ? 174.235 174.151 179.561 1.00 9.17  ? 2156 LEU A CB    1 
ATOM   5598  C  CG    . LEU A 1 2156 ? 174.975 172.970 180.185 1.00 10.17 ? 2156 LEU A CG    1 
ATOM   5599  C  CD1   . LEU A 1 2156 ? 174.944 173.084 181.695 1.00 18.59 ? 2156 LEU A CD1   1 
ATOM   5600  C  CD2   . LEU A 1 2156 ? 174.344 171.663 179.752 1.00 16.54 ? 2156 LEU A CD2   1 
ATOM   5601  N  N     . LEU A 1 2157 ? 173.297 176.399 177.601 1.00 14.38 ? 2157 LEU A N     1 
ATOM   5602  C  CA    . LEU A 1 2157 ? 172.421 177.547 177.393 1.00 9.54  ? 2157 LEU A CA    1 
ATOM   5603  C  C     . LEU A 1 2157 ? 171.681 177.448 176.064 1.00 6.90  ? 2157 LEU A C     1 
ATOM   5604  O  O     . LEU A 1 2157 ? 170.526 177.873 175.959 1.00 10.75 ? 2157 LEU A O     1 
ATOM   5605  C  CB    . LEU A 1 2157 ? 173.228 178.845 177.502 1.00 10.59 ? 2157 LEU A CB    1 
ATOM   5606  C  CG    . LEU A 1 2157 ? 172.481 180.184 177.494 1.00 6.08  ? 2157 LEU A CG    1 
ATOM   5607  C  CD1   . LEU A 1 2157 ? 173.232 181.219 178.294 1.00 10.97 ? 2157 LEU A CD1   1 
ATOM   5608  C  CD2   . LEU A 1 2157 ? 172.339 180.685 176.079 1.00 2.43  ? 2157 LEU A CD2   1 
ATOM   5609  N  N     . PHE A 1 2158 ? 172.323 176.882 175.041 1.00 5.67  ? 2158 PHE A N     1 
ATOM   5610  C  CA    . PHE A 1 2158 ? 171.632 176.700 173.769 1.00 10.33 ? 2158 PHE A CA    1 
ATOM   5611  C  C     . PHE A 1 2158 ? 170.575 175.607 173.849 1.00 9.33  ? 2158 PHE A C     1 
ATOM   5612  O  O     . PHE A 1 2158 ? 169.543 175.698 173.176 1.00 10.60 ? 2158 PHE A O     1 
ATOM   5613  C  CB    . PHE A 1 2158 ? 172.638 176.411 172.657 1.00 9.26  ? 2158 PHE A CB    1 
ATOM   5614  C  CG    . PHE A 1 2158 ? 173.323 177.641 172.141 1.00 11.29 ? 2158 PHE A CG    1 
ATOM   5615  C  CD1   . PHE A 1 2158 ? 172.663 178.504 171.286 1.00 8.97  ? 2158 PHE A CD1   1 
ATOM   5616  C  CD2   . PHE A 1 2158 ? 174.618 177.943 172.522 1.00 13.54 ? 2158 PHE A CD2   1 
ATOM   5617  C  CE1   . PHE A 1 2158 ? 173.284 179.641 170.815 1.00 12.44 ? 2158 PHE A CE1   1 
ATOM   5618  C  CE2   . PHE A 1 2158 ? 175.245 179.079 172.053 1.00 10.58 ? 2158 PHE A CE2   1 
ATOM   5619  C  CZ    . PHE A 1 2158 ? 174.577 179.928 171.199 1.00 10.41 ? 2158 PHE A CZ    1 
ATOM   5620  N  N     . SER A 1 2159 ? 170.807 174.569 174.657 1.00 10.44 ? 2159 SER A N     1 
ATOM   5621  C  CA    . SER A 1 2159 ? 169.743 173.610 174.929 1.00 11.54 ? 2159 SER A CA    1 
ATOM   5622  C  C     . SER A 1 2159 ? 168.587 174.280 175.658 1.00 11.59 ? 2159 SER A C     1 
ATOM   5623  O  O     . SER A 1 2159 ? 167.418 174.044 175.333 1.00 12.09 ? 2159 SER A O     1 
ATOM   5624  C  CB    . SER A 1 2159 ? 170.284 172.433 175.738 1.00 13.23 ? 2159 SER A CB    1 
ATOM   5625  O  OG    . SER A 1 2159 ? 171.245 171.714 174.992 1.00 24.39 ? 2159 SER A OG    1 
ATOM   5626  N  N     . LEU A 1 2160 ? 168.899 175.132 176.637 1.00 9.10  ? 2160 LEU A N     1 
ATOM   5627  C  CA    . LEU A 1 2160 ? 167.860 175.910 177.304 1.00 7.99  ? 2160 LEU A CA    1 
ATOM   5628  C  C     . LEU A 1 2160 ? 167.161 176.841 176.324 1.00 10.55 ? 2160 LEU A C     1 
ATOM   5629  O  O     . LEU A 1 2160 ? 165.944 177.043 176.408 1.00 14.47 ? 2160 LEU A O     1 
ATOM   5630  C  CB    . LEU A 1 2160 ? 168.460 176.708 178.459 1.00 6.72  ? 2160 LEU A CB    1 
ATOM   5631  C  CG    . LEU A 1 2160 ? 168.822 175.954 179.737 1.00 9.46  ? 2160 LEU A CG    1 
ATOM   5632  C  CD1   . LEU A 1 2160 ? 169.549 176.880 180.693 1.00 11.44 ? 2160 LEU A CD1   1 
ATOM   5633  C  CD2   . LEU A 1 2160 ? 167.578 175.381 180.391 1.00 14.22 ? 2160 LEU A CD2   1 
ATOM   5634  N  N     . LEU A 1 2161 ? 167.918 177.431 175.395 1.00 9.39  ? 2161 LEU A N     1 
ATOM   5635  C  CA    . LEU A 1 2161 ? 167.311 178.305 174.399 1.00 7.58  ? 2161 LEU A CA    1 
ATOM   5636  C  C     . LEU A 1 2161 ? 166.346 177.537 173.507 1.00 9.68  ? 2161 LEU A C     1 
ATOM   5637  O  O     . LEU A 1 2161 ? 165.257 178.027 173.189 1.00 13.76 ? 2161 LEU A O     1 
ATOM   5638  C  CB    . LEU A 1 2161 ? 168.387 178.977 173.550 1.00 10.31 ? 2161 LEU A CB    1 
ATOM   5639  C  CG    . LEU A 1 2161 ? 169.091 180.199 174.134 1.00 10.31 ? 2161 LEU A CG    1 
ATOM   5640  C  CD1   . LEU A 1 2161 ? 170.268 180.583 173.246 1.00 11.11 ? 2161 LEU A CD1   1 
ATOM   5641  C  CD2   . LEU A 1 2161 ? 168.132 181.357 174.327 1.00 6.13  ? 2161 LEU A CD2   1 
ATOM   5642  N  N     . SER A 1 2162 ? 166.732 176.330 173.086 1.00 10.62 ? 2162 SER A N     1 
ATOM   5643  C  CA    . SER A 1 2162 ? 165.833 175.515 172.281 1.00 12.91 ? 2162 SER A CA    1 
ATOM   5644  C  C     . SER A 1 2162 ? 164.629 175.058 173.090 1.00 12.45 ? 2162 SER A C     1 
ATOM   5645  O  O     . SER A 1 2162 ? 163.549 174.846 172.528 1.00 19.69 ? 2162 SER A O     1 
ATOM   5646  C  CB    . SER A 1 2162 ? 166.580 174.311 171.707 1.00 12.04 ? 2162 SER A CB    1 
ATOM   5647  O  OG    . SER A 1 2162 ? 166.993 173.431 172.735 1.00 17.71 ? 2162 SER A OG    1 
ATOM   5648  N  N     . ASP A 1 2163 ? 164.797 174.903 174.404 1.00 14.38 ? 2163 ASP A N     1 
ATOM   5649  C  CA    . ASP A 1 2163 ? 163.688 174.490 175.257 1.00 10.15 ? 2163 ASP A CA    1 
ATOM   5650  C  C     . ASP A 1 2163 ? 162.627 175.580 175.357 1.00 11.84 ? 2163 ASP A C     1 
ATOM   5651  O  O     . ASP A 1 2163 ? 161.426 175.299 175.287 1.00 21.61 ? 2163 ASP A O     1 
ATOM   5652  C  CB    . ASP A 1 2163 ? 164.210 174.118 176.644 1.00 12.00 ? 2163 ASP A CB    1 
ATOM   5653  C  CG    . ASP A 1 2163 ? 164.742 172.702 176.701 1.00 27.22 ? 2163 ASP A CG    1 
ATOM   5654  O  OD1   . ASP A 1 2163 ? 163.965 171.769 176.416 1.00 37.14 ? 2163 ASP A OD1   1 
ATOM   5655  O  OD2   . ASP A 1 2163 ? 165.929 172.517 177.040 1.00 25.82 ? 2163 ASP A OD2   1 
ATOM   5656  N  N     . VAL A 1 2164 ? 163.051 176.830 175.521 1.00 9.57  ? 2164 VAL A N     1 
ATOM   5657  C  CA    . VAL A 1 2164 ? 162.107 177.922 175.727 1.00 11.14 ? 2164 VAL A CA    1 
ATOM   5658  C  C     . VAL A 1 2164 ? 161.724 178.605 174.414 1.00 11.33 ? 2164 VAL A C     1 
ATOM   5659  O  O     . VAL A 1 2164 ? 160.643 179.194 174.316 1.00 13.59 ? 2164 VAL A O     1 
ATOM   5660  C  CB    . VAL A 1 2164 ? 162.691 178.928 176.735 1.00 10.44 ? 2164 VAL A CB    1 
ATOM   5661  C  CG1   . VAL A 1 2164 ? 161.643 179.939 177.156 1.00 10.44 ? 2164 VAL A CG1   1 
ATOM   5662  C  CG2   . VAL A 1 2164 ? 163.235 178.200 177.951 1.00 10.34 ? 2164 VAL A CG2   1 
ATOM   5663  N  N     . PHE A 1 2165 ? 162.580 178.532 173.398 1.00 9.57  ? 2165 PHE A N     1 
ATOM   5664  C  CA    . PHE A 1 2165 ? 162.335 179.158 172.099 1.00 9.42  ? 2165 PHE A CA    1 
ATOM   5665  C  C     . PHE A 1 2165 ? 162.559 178.120 171.007 1.00 14.88 ? 2165 PHE A C     1 
ATOM   5666  O  O     . PHE A 1 2165 ? 163.577 178.152 170.302 1.00 18.52 ? 2165 PHE A O     1 
ATOM   5667  C  CB    . PHE A 1 2165 ? 163.238 180.375 171.893 1.00 11.24 ? 2165 PHE A CB    1 
ATOM   5668  C  CG    . PHE A 1 2165 ? 163.089 181.435 172.951 1.00 13.02 ? 2165 PHE A CG    1 
ATOM   5669  C  CD1   . PHE A 1 2165 ? 163.794 181.352 174.142 1.00 13.35 ? 2165 PHE A CD1   1 
ATOM   5670  C  CD2   . PHE A 1 2165 ? 162.262 182.526 172.745 1.00 10.20 ? 2165 PHE A CD2   1 
ATOM   5671  C  CE1   . PHE A 1 2165 ? 163.667 182.328 175.108 1.00 8.48  ? 2165 PHE A CE1   1 
ATOM   5672  C  CE2   . PHE A 1 2165 ? 162.131 183.505 173.709 1.00 11.20 ? 2165 PHE A CE2   1 
ATOM   5673  C  CZ    . PHE A 1 2165 ? 162.835 183.407 174.892 1.00 8.14  ? 2165 PHE A CZ    1 
ATOM   5674  N  N     . PRO A 1 2166 ? 161.627 177.180 170.839 1.00 16.23 ? 2166 PRO A N     1 
ATOM   5675  C  CA    . PRO A 1 2166 ? 161.827 176.110 169.852 1.00 12.19 ? 2166 PRO A CA    1 
ATOM   5676  C  C     . PRO A 1 2166 ? 161.925 176.655 168.435 1.00 11.87 ? 2166 PRO A C     1 
ATOM   5677  O  O     . PRO A 1 2166 ? 161.221 177.595 168.057 1.00 20.90 ? 2166 PRO A O     1 
ATOM   5678  C  CB    . PRO A 1 2166 ? 160.584 175.231 170.028 1.00 10.89 ? 2166 PRO A CB    1 
ATOM   5679  C  CG    . PRO A 1 2166 ? 160.048 175.580 171.375 1.00 15.39 ? 2166 PRO A CG    1 
ATOM   5680  C  CD    . PRO A 1 2166 ? 160.350 177.032 171.552 1.00 14.12 ? 2166 PRO A CD    1 
ATOM   5681  N  N     . GLY A 1 2167 ? 162.807 176.047 167.645 1.00 15.71 ? 2167 GLY A N     1 
ATOM   5682  C  CA    . GLY A 1 2167 ? 162.928 176.390 166.243 1.00 14.06 ? 2167 GLY A CA    1 
ATOM   5683  C  C     . GLY A 1 2167 ? 163.562 177.728 165.953 1.00 18.50 ? 2167 GLY A C     1 
ATOM   5684  O  O     . GLY A 1 2167 ? 163.486 178.198 164.815 1.00 20.81 ? 2167 GLY A O     1 
ATOM   5685  N  N     . VAL A 1 2168 ? 164.183 178.362 166.943 1.00 19.67 ? 2168 VAL A N     1 
ATOM   5686  C  CA    . VAL A 1 2168 ? 164.793 179.675 166.783 1.00 12.17 ? 2168 VAL A CA    1 
ATOM   5687  C  C     . VAL A 1 2168 ? 166.300 179.500 166.893 1.00 16.70 ? 2168 VAL A C     1 
ATOM   5688  O  O     . VAL A 1 2168 ? 166.801 178.981 167.897 1.00 20.07 ? 2168 VAL A O     1 
ATOM   5689  C  CB    . VAL A 1 2168 ? 164.267 180.672 167.826 1.00 16.67 ? 2168 VAL A CB    1 
ATOM   5690  C  CG1   . VAL A 1 2168 ? 164.861 182.047 167.586 1.00 20.12 ? 2168 VAL A CG1   1 
ATOM   5691  C  CG2   . VAL A 1 2168 ? 162.750 180.722 167.786 1.00 15.34 ? 2168 VAL A CG2   1 
ATOM   5692  N  N     . GLN A 1 2169 ? 167.020 179.940 165.867 1.00 22.56 ? 2169 GLN A N     1 
ATOM   5693  C  CA    . GLN A 1 2169 ? 168.454 179.721 165.764 1.00 22.19 ? 2169 GLN A CA    1 
ATOM   5694  C  C     . GLN A 1 2169 ? 169.207 181.038 165.874 1.00 22.13 ? 2169 GLN A C     1 
ATOM   5695  O  O     . GLN A 1 2169 ? 168.723 182.085 165.434 1.00 24.66 ? 2169 GLN A O     1 
ATOM   5696  C  CB    . GLN A 1 2169 ? 168.809 179.027 164.446 1.00 25.10 ? 2169 GLN A CB    1 
ATOM   5697  C  CG    . GLN A 1 2169 ? 168.366 177.581 164.379 1.00 21.92 ? 2169 GLN A CG    1 
ATOM   5698  C  CD    . GLN A 1 2169 ? 168.755 176.801 165.620 1.00 27.14 ? 2169 GLN A CD    1 
ATOM   5699  O  OE1   . GLN A 1 2169 ? 167.897 176.336 166.370 1.00 27.71 ? 2169 GLN A OE1   1 
ATOM   5700  N  NE2   . GLN A 1 2169 ? 170.055 176.655 165.843 1.00 30.02 ? 2169 GLN A NE2   1 
ATOM   5701  N  N     . TYR A 1 2170 ? 170.396 180.974 166.464 1.00 18.95 ? 2170 TYR A N     1 
ATOM   5702  C  CA    . TYR A 1 2170 ? 171.272 182.125 166.613 1.00 14.15 ? 2170 TYR A CA    1 
ATOM   5703  C  C     . TYR A 1 2170 ? 172.360 182.066 165.552 1.00 17.76 ? 2170 TYR A C     1 
ATOM   5704  O  O     . TYR A 1 2170 ? 173.038 181.043 165.410 1.00 24.84 ? 2170 TYR A O     1 
ATOM   5705  C  CB    . TYR A 1 2170 ? 171.902 182.154 168.006 1.00 17.46 ? 2170 TYR A CB    1 
ATOM   5706  C  CG    . TYR A 1 2170 ? 172.924 183.251 168.185 1.00 17.47 ? 2170 TYR A CG    1 
ATOM   5707  C  CD1   . TYR A 1 2170 ? 172.604 184.571 167.906 1.00 13.24 ? 2170 TYR A CD1   1 
ATOM   5708  C  CD2   . TYR A 1 2170 ? 174.213 182.964 168.613 1.00 15.46 ? 2170 TYR A CD2   1 
ATOM   5709  C  CE1   . TYR A 1 2170 ? 173.534 185.579 168.062 1.00 16.12 ? 2170 TYR A CE1   1 
ATOM   5710  C  CE2   . TYR A 1 2170 ? 175.152 183.966 168.770 1.00 13.92 ? 2170 TYR A CE2   1 
ATOM   5711  C  CZ    . TYR A 1 2170 ? 174.807 185.272 168.493 1.00 13.97 ? 2170 TYR A CZ    1 
ATOM   5712  O  OH    . TYR A 1 2170 ? 175.733 186.276 168.650 1.00 15.59 ? 2170 TYR A OH    1 
ATOM   5713  N  N     . HIS A 1 2171 ? 172.527 183.157 164.812 1.00 20.64 ? 2171 HIS A N     1 
ATOM   5714  C  CA    . HIS A 1 2171 ? 173.562 183.238 163.785 1.00 24.69 ? 2171 HIS A CA    1 
ATOM   5715  C  C     . HIS A 1 2171 ? 174.266 184.580 163.914 1.00 20.64 ? 2171 HIS A C     1 
ATOM   5716  O  O     . HIS A 1 2171 ? 173.661 185.628 163.672 1.00 28.49 ? 2171 HIS A O     1 
ATOM   5717  C  CB    . HIS A 1 2171 ? 172.972 183.060 162.387 1.00 24.25 ? 2171 HIS A CB    1 
ATOM   5718  C  CG    . HIS A 1 2171 ? 172.518 181.663 162.100 1.00 29.93 ? 2171 HIS A CG    1 
ATOM   5719  N  ND1   . HIS A 1 2171 ? 171.267 181.201 162.446 1.00 33.77 ? 2171 HIS A ND1   1 
ATOM   5720  C  CD2   . HIS A 1 2171 ? 173.152 180.625 161.505 1.00 31.87 ? 2171 HIS A CD2   1 
ATOM   5721  C  CE1   . HIS A 1 2171 ? 171.148 179.939 162.072 1.00 34.58 ? 2171 HIS A CE1   1 
ATOM   5722  N  NE2   . HIS A 1 2171 ? 172.278 179.565 161.499 1.00 37.66 ? 2171 HIS A NE2   1 
ATOM   5723  N  N     . ARG A 1 2172 ? 175.539 184.544 164.298 1.00 19.61 ? 2172 ARG A N     1 
ATOM   5724  C  CA    . ARG A 1 2172 ? 176.325 185.763 164.392 1.00 19.22 ? 2172 ARG A CA    1 
ATOM   5725  C  C     . ARG A 1 2172 ? 176.526 186.372 163.011 1.00 24.60 ? 2172 ARG A C     1 
ATOM   5726  O  O     . ARG A 1 2172 ? 176.586 185.670 161.998 1.00 27.84 ? 2172 ARG A O     1 
ATOM   5727  C  CB    . ARG A 1 2172 ? 177.687 185.479 165.020 1.00 18.59 ? 2172 ARG A CB    1 
ATOM   5728  C  CG    . ARG A 1 2172 ? 177.645 185.017 166.461 1.00 17.40 ? 2172 ARG A CG    1 
ATOM   5729  C  CD    . ARG A 1 2172 ? 179.048 184.749 166.974 1.00 24.76 ? 2172 ARG A CD    1 
ATOM   5730  N  NE    . ARG A 1 2172 ? 179.828 185.977 167.054 1.00 33.48 ? 2172 ARG A NE    1 
ATOM   5731  C  CZ    . ARG A 1 2172 ? 180.843 186.278 166.253 1.00 28.34 ? 2172 ARG A CZ    1 
ATOM   5732  N  NH1   . ARG A 1 2172 ? 181.228 185.460 165.288 1.00 24.62 ? 2172 ARG A NH1   1 
ATOM   5733  N  NH2   . ARG A 1 2172 ? 181.482 187.431 166.422 1.00 20.70 ? 2172 ARG A NH2   1 
ATOM   5734  N  N     . GLY A 1 2173 ? 176.626 187.697 162.976 1.00 24.60 ? 2173 GLY A N     1 
ATOM   5735  C  CA    . GLY A 1 2173 ? 177.026 188.362 161.751 1.00 24.19 ? 2173 GLY A CA    1 
ATOM   5736  C  C     . GLY A 1 2173 ? 178.474 188.049 161.420 1.00 25.34 ? 2173 GLY A C     1 
ATOM   5737  O  O     . GLY A 1 2173 ? 179.354 188.080 162.282 1.00 23.29 ? 2173 GLY A O     1 
ATOM   5738  N  N     . GLU A 1 2174 ? 178.720 187.731 160.151 1.00 25.07 ? 2174 GLU A N     1 
ATOM   5739  C  CA    . GLU A 1 2174 ? 180.073 187.426 159.690 1.00 22.23 ? 2174 GLU A CA    1 
ATOM   5740  C  C     . GLU A 1 2174 ? 180.743 188.766 159.419 1.00 23.57 ? 2174 GLU A C     1 
ATOM   5741  O  O     . GLU A 1 2174 ? 180.594 189.362 158.352 1.00 30.47 ? 2174 GLU A O     1 
ATOM   5742  C  CB    . GLU A 1 2174 ? 180.042 186.523 158.462 1.00 21.06 ? 2174 GLU A CB    1 
ATOM   5743  C  CG    . GLU A 1 2174 ? 181.396 185.947 158.067 1.00 25.77 ? 2174 GLU A CG    1 
ATOM   5744  C  CD    . GLU A 1 2174 ? 182.222 186.883 157.208 1.00 33.66 ? 2174 GLU A CD    1 
ATOM   5745  O  OE1   . GLU A 1 2174 ? 181.631 187.693 156.465 1.00 32.19 ? 2174 GLU A OE1   1 
ATOM   5746  O  OE2   . GLU A 1 2174 ? 183.467 186.811 157.280 1.00 31.02 ? 2174 GLU A OE2   1 
ATOM   5747  N  N     . MET A 1 2175 ? 181.481 189.257 160.417 1.00 17.16 ? 2175 MET A N     1 
ATOM   5748  C  CA    . MET A 1 2175 ? 182.028 190.614 160.398 1.00 14.11 ? 2175 MET A CA    1 
ATOM   5749  C  C     . MET A 1 2175 ? 183.337 190.642 159.609 1.00 12.22 ? 2175 MET A C     1 
ATOM   5750  O  O     . MET A 1 2175 ? 184.438 190.710 160.156 1.00 15.29 ? 2175 MET A O     1 
ATOM   5751  C  CB    . MET A 1 2175 ? 182.215 191.124 161.820 1.00 17.31 ? 2175 MET A CB    1 
ATOM   5752  C  CG    . MET A 1 2175 ? 180.911 191.326 162.569 1.00 17.62 ? 2175 MET A CG    1 
ATOM   5753  S  SD    . MET A 1 2175 ? 181.130 191.987 164.228 1.00 31.78 ? 2175 MET A SD    1 
ATOM   5754  C  CE    . MET A 1 2175 ? 181.754 190.548 165.091 1.00 10.52 ? 2175 MET A CE    1 
ATOM   5755  N  N     . THR A 1 2176 ? 183.192 190.619 158.281 1.00 13.50 ? 2176 THR A N     1 
ATOM   5756  C  CA    . THR A 1 2176 ? 184.357 190.582 157.404 1.00 12.13 ? 2176 THR A CA    1 
ATOM   5757  C  C     . THR A 1 2176 ? 185.240 191.809 157.589 1.00 8.37  ? 2176 THR A C     1 
ATOM   5758  O  O     . THR A 1 2176 ? 186.469 191.691 157.649 1.00 13.65 ? 2176 THR A O     1 
ATOM   5759  C  CB    . THR A 1 2176 ? 183.913 190.470 155.944 1.00 12.67 ? 2176 THR A CB    1 
ATOM   5760  O  OG1   . THR A 1 2176 ? 183.157 189.270 155.764 1.00 12.42 ? 2176 THR A OG1   1 
ATOM   5761  C  CG2   . THR A 1 2176 ? 185.116 190.446 155.019 1.00 18.41 ? 2176 THR A CG2   1 
ATOM   5762  N  N     . ALA A 1 2177 ? 184.633 192.993 157.687 1.00 10.21 ? 2177 ALA A N     1 
ATOM   5763  C  CA    . ALA A 1 2177 ? 185.415 194.222 157.751 1.00 7.15  ? 2177 ALA A CA    1 
ATOM   5764  C  C     . ALA A 1 2177 ? 186.313 194.252 158.982 1.00 8.66  ? 2177 ALA A C     1 
ATOM   5765  O  O     . ALA A 1 2177 ? 187.490 194.617 158.892 1.00 14.35 ? 2177 ALA A O     1 
ATOM   5766  C  CB    . ALA A 1 2177 ? 184.486 195.435 157.733 1.00 8.01  ? 2177 ALA A CB    1 
ATOM   5767  N  N     . LEU A 1 2178 ? 185.780 193.864 160.142 1.00 6.86  ? 2178 LEU A N     1 
ATOM   5768  C  CA    . LEU A 1 2178 ? 186.595 193.863 161.352 1.00 8.23  ? 2178 LEU A CA    1 
ATOM   5769  C  C     . LEU A 1 2178 ? 187.610 192.728 161.337 1.00 8.33  ? 2178 LEU A C     1 
ATOM   5770  O  O     . LEU A 1 2178 ? 188.753 192.904 161.774 1.00 8.62  ? 2178 LEU A O     1 
ATOM   5771  C  CB    . LEU A 1 2178 ? 185.708 193.778 162.593 1.00 7.39  ? 2178 LEU A CB    1 
ATOM   5772  C  CG    . LEU A 1 2178 ? 186.448 193.792 163.933 1.00 3.75  ? 2178 LEU A CG    1 
ATOM   5773  C  CD1   . LEU A 1 2178 ? 187.295 195.046 164.075 1.00 5.69  ? 2178 LEU A CD1   1 
ATOM   5774  C  CD2   . LEU A 1 2178 ? 185.475 193.675 165.089 1.00 2.36  ? 2178 LEU A CD2   1 
ATOM   5775  N  N     . ARG A 1 2179 ? 187.216 191.556 160.830 1.00 9.14  ? 2179 ARG A N     1 
ATOM   5776  C  CA    . ARG A 1 2179 ? 188.129 190.417 160.812 1.00 7.08  ? 2179 ARG A CA    1 
ATOM   5777  C  C     . ARG A 1 2179 ? 189.334 190.676 159.914 1.00 8.97  ? 2179 ARG A C     1 
ATOM   5778  O  O     . ARG A 1 2179 ? 190.449 190.243 160.226 1.00 11.58 ? 2179 ARG A O     1 
ATOM   5779  C  CB    . ARG A 1 2179 ? 187.394 189.149 160.382 1.00 5.82  ? 2179 ARG A CB    1 
ATOM   5780  C  CG    . ARG A 1 2179 ? 186.348 188.671 161.373 1.00 7.66  ? 2179 ARG A CG    1 
ATOM   5781  C  CD    . ARG A 1 2179 ? 185.740 187.349 160.946 1.00 7.11  ? 2179 ARG A CD    1 
ATOM   5782  N  NE    . ARG A 1 2179 ? 186.499 186.222 161.473 1.00 12.27 ? 2179 ARG A NE    1 
ATOM   5783  C  CZ    . ARG A 1 2179 ? 186.017 185.330 162.328 1.00 15.53 ? 2179 ARG A CZ    1 
ATOM   5784  N  NH1   . ARG A 1 2179 ? 184.765 185.382 162.750 1.00 10.20 ? 2179 ARG A NH1   1 
ATOM   5785  N  NH2   . ARG A 1 2179 ? 186.813 184.359 162.767 1.00 18.22 ? 2179 ARG A NH2   1 
ATOM   5786  N  N     . GLU A 1 2180 ? 189.132 191.365 158.788 1.00 7.57  ? 2180 GLU A N     1 
ATOM   5787  C  CA    . GLU A 1 2180 ? 190.264 191.698 157.927 1.00 8.49  ? 2180 GLU A CA    1 
ATOM   5788  C  C     . GLU A 1 2180 ? 191.254 192.609 158.642 1.00 8.71  ? 2180 GLU A C     1 
ATOM   5789  O  O     . GLU A 1 2180 ? 192.470 192.408 158.548 1.00 11.37 ? 2180 GLU A O     1 
ATOM   5790  C  CB    . GLU A 1 2180 ? 189.782 192.341 156.627 1.00 9.56  ? 2180 GLU A CB    1 
ATOM   5791  C  CG    . GLU A 1 2180 ? 188.983 191.418 155.727 1.00 15.89 ? 2180 GLU A CG    1 
ATOM   5792  C  CD    . GLU A 1 2180 ? 189.819 190.280 155.170 1.00 29.07 ? 2180 GLU A CD    1 
ATOM   5793  O  OE1   . GLU A 1 2180 ? 191.032 190.482 154.952 1.00 27.91 ? 2180 GLU A OE1   1 
ATOM   5794  O  OE2   . GLU A 1 2180 ? 189.262 189.185 154.944 1.00 32.87 ? 2180 GLU A OE2   1 
ATOM   5795  N  N     . GLU A 1 2181 ? 190.756 193.614 159.364 1.00 9.57  ? 2181 GLU A N     1 
ATOM   5796  C  CA    . GLU A 1 2181 ? 191.654 194.495 160.101 1.00 5.66  ? 2181 GLU A CA    1 
ATOM   5797  C  C     . GLU A 1 2181 ? 192.327 193.762 161.255 1.00 6.52  ? 2181 GLU A C     1 
ATOM   5798  O  O     . GLU A 1 2181 ? 193.505 194.000 161.541 1.00 9.74  ? 2181 GLU A O     1 
ATOM   5799  C  CB    . GLU A 1 2181 ? 190.898 195.725 160.608 1.00 6.39  ? 2181 GLU A CB    1 
ATOM   5800  C  CG    . GLU A 1 2181 ? 190.324 196.616 159.511 1.00 8.57  ? 2181 GLU A CG    1 
ATOM   5801  C  CD    . GLU A 1 2181 ? 191.378 197.418 158.757 1.00 16.99 ? 2181 GLU A CD    1 
ATOM   5802  O  OE1   . GLU A 1 2181 ? 192.587 197.161 158.934 1.00 23.65 ? 2181 GLU A OE1   1 
ATOM   5803  O  OE2   . GLU A 1 2181 ? 190.991 198.314 157.980 1.00 15.64 ? 2181 GLU A OE2   1 
ATOM   5804  N  N     . LEU A 1 2182 ? 191.598 192.867 161.926 1.00 5.57  ? 2182 LEU A N     1 
ATOM   5805  C  CA    . LEU A 1 2182 ? 192.197 192.084 163.003 1.00 4.66  ? 2182 LEU A CA    1 
ATOM   5806  C  C     . LEU A 1 2182 ? 193.320 191.198 162.479 1.00 6.82  ? 2182 LEU A C     1 
ATOM   5807  O  O     . LEU A 1 2182 ? 194.364 191.058 163.124 1.00 6.91  ? 2182 LEU A O     1 
ATOM   5808  C  CB    . LEU A 1 2182 ? 191.130 191.238 163.698 1.00 2.27  ? 2182 LEU A CB    1 
ATOM   5809  C  CG    . LEU A 1 2182 ? 190.101 191.968 164.561 1.00 3.10  ? 2182 LEU A CG    1 
ATOM   5810  C  CD1   . LEU A 1 2182 ? 188.936 191.053 164.892 1.00 2.03  ? 2182 LEU A CD1   1 
ATOM   5811  C  CD2   . LEU A 1 2182 ? 190.739 192.502 165.829 1.00 1.67  ? 2182 LEU A CD2   1 
ATOM   5812  N  N     . LYS A 1 2183 ? 193.119 190.592 161.308 1.00 7.71  ? 2183 LYS A N     1 
ATOM   5813  C  CA    . LYS A 1 2183 ? 194.141 189.726 160.731 1.00 6.60  ? 2183 LYS A CA    1 
ATOM   5814  C  C     . LYS A 1 2183 ? 195.408 190.509 160.402 1.00 7.19  ? 2183 LYS A C     1 
ATOM   5815  O  O     . LYS A 1 2183 ? 196.523 190.014 160.604 1.00 7.74  ? 2183 LYS A O     1 
ATOM   5816  C  CB    . LYS A 1 2183 ? 193.586 189.032 159.489 1.00 6.02  ? 2183 LYS A CB    1 
ATOM   5817  C  CG    . LYS A 1 2183 ? 194.537 188.058 158.831 1.00 10.83 ? 2183 LYS A CG    1 
ATOM   5818  C  CD    . LYS A 1 2183 ? 193.862 187.338 157.680 1.00 12.13 ? 2183 LYS A CD    1 
ATOM   5819  C  CE    . LYS A 1 2183 ? 194.849 186.470 156.924 1.00 17.30 ? 2183 LYS A CE    1 
ATOM   5820  N  NZ    . LYS A 1 2183 ? 195.348 185.351 157.766 1.00 22.55 ? 2183 LYS A NZ    1 
ATOM   5821  N  N     . LYS A 1 2184 ? 195.258 191.735 159.895 1.00 7.11  ? 2184 LYS A N     1 
ATOM   5822  C  CA    . LYS A 1 2184 ? 196.424 192.566 159.609 1.00 5.95  ? 2184 LYS A CA    1 
ATOM   5823  C  C     . LYS A 1 2184 ? 197.118 193.020 160.889 1.00 5.76  ? 2184 LYS A C     1 
ATOM   5824  O  O     . LYS A 1 2184 ? 198.352 193.047 160.955 1.00 8.59  ? 2184 LYS A O     1 
ATOM   5825  C  CB    . LYS A 1 2184 ? 196.016 193.771 158.763 1.00 6.95  ? 2184 LYS A CB    1 
ATOM   5826  C  CG    . LYS A 1 2184 ? 196.025 193.508 157.266 1.00 9.51  ? 2184 LYS A CG    1 
ATOM   5827  C  CD    . LYS A 1 2184 ? 194.848 194.176 156.572 1.00 14.16 ? 2184 LYS A CD    1 
ATOM   5828  C  CE    . LYS A 1 2184 ? 194.795 195.661 156.881 1.00 17.88 ? 2184 LYS A CE    1 
ATOM   5829  N  NZ    . LYS A 1 2184 ? 193.921 196.399 155.931 1.00 27.38 ? 2184 LYS A NZ    1 
ATOM   5830  N  N     . VAL A 1 2185 ? 196.344 193.390 161.912 1.00 5.20  ? 2185 VAL A N     1 
ATOM   5831  C  CA    . VAL A 1 2185 ? 196.939 193.830 163.171 1.00 2.99  ? 2185 VAL A CA    1 
ATOM   5832  C  C     . VAL A 1 2185 ? 197.689 192.682 163.836 1.00 3.45  ? 2185 VAL A C     1 
ATOM   5833  O  O     . VAL A 1 2185 ? 198.754 192.881 164.431 1.00 6.35  ? 2185 VAL A O     1 
ATOM   5834  C  CB    . VAL A 1 2185 ? 195.856 194.423 164.095 1.00 4.89  ? 2185 VAL A CB    1 
ATOM   5835  C  CG1   . VAL A 1 2185 ? 196.394 194.623 165.506 1.00 3.24  ? 2185 VAL A CG1   1 
ATOM   5836  C  CG2   . VAL A 1 2185 ? 195.353 195.740 163.537 1.00 3.14  ? 2185 VAL A CG2   1 
ATOM   5837  N  N     . CYS A 1 2186 ? 197.153 191.463 163.735 1.00 6.11  ? 2186 CYS A N     1 
ATOM   5838  C  CA    . CYS A 1 2186 ? 197.833 190.301 164.300 1.00 3.73  ? 2186 CYS A CA    1 
ATOM   5839  C  C     . CYS A 1 2186 ? 199.168 190.049 163.609 1.00 2.76  ? 2186 CYS A C     1 
ATOM   5840  O  O     . CYS A 1 2186 ? 200.156 189.700 164.265 1.00 4.17  ? 2186 CYS A O     1 
ATOM   5841  C  CB    . CYS A 1 2186 ? 196.936 189.068 164.200 1.00 3.23  ? 2186 CYS A CB    1 
ATOM   5842  S  SG    . CYS A 1 2186 ? 195.676 188.952 165.487 1.00 4.91  ? 2186 CYS A SG    1 
ATOM   5843  N  N     . GLN A 1 2187 ? 199.213 190.216 162.285 1.00 5.43  ? 2187 GLN A N     1 
ATOM   5844  C  CA    . GLN A 1 2187 ? 200.461 190.029 161.551 1.00 5.05  ? 2187 GLN A CA    1 
ATOM   5845  C  C     . GLN A 1 2187 ? 201.519 191.033 161.992 1.00 6.17  ? 2187 GLN A C     1 
ATOM   5846  O  O     . GLN A 1 2187 ? 202.698 190.687 162.127 1.00 9.63  ? 2187 GLN A O     1 
ATOM   5847  C  CB    . GLN A 1 2187 ? 200.203 190.145 160.050 1.00 3.81  ? 2187 GLN A CB    1 
ATOM   5848  C  CG    . GLN A 1 2187 ? 201.418 189.900 159.164 1.00 10.33 ? 2187 GLN A CG    1 
ATOM   5849  C  CD    . GLN A 1 2187 ? 201.984 188.501 159.300 1.00 17.08 ? 2187 GLN A CD    1 
ATOM   5850  O  OE1   . GLN A 1 2187 ? 203.022 188.296 159.928 1.00 12.83 ? 2187 GLN A OE1   1 
ATOM   5851  N  NE2   . GLN A 1 2187 ? 201.301 187.527 158.709 1.00 16.54 ? 2187 GLN A NE2   1 
ATOM   5852  N  N     . GLU A 1 2188 ? 201.118 192.285 162.218 1.00 5.25  ? 2188 GLU A N     1 
ATOM   5853  C  CA    . GLU A 1 2188 ? 202.076 193.302 162.634 1.00 6.95  ? 2188 GLU A CA    1 
ATOM   5854  C  C     . GLU A 1 2188 ? 202.498 193.113 164.086 1.00 4.34  ? 2188 GLU A C     1 
ATOM   5855  O  O     . GLU A 1 2188 ? 203.571 193.579 164.486 1.00 4.06  ? 2188 GLU A O     1 
ATOM   5856  C  CB    . GLU A 1 2188 ? 201.482 194.695 162.411 1.00 7.42  ? 2188 GLU A CB    1 
ATOM   5857  C  CG    . GLU A 1 2188 ? 202.403 195.855 162.764 1.00 14.22 ? 2188 GLU A CG    1 
ATOM   5858  C  CD    . GLU A 1 2188 ? 203.634 195.924 161.877 1.00 31.58 ? 2188 GLU A CD    1 
ATOM   5859  O  OE1   . GLU A 1 2188 ? 203.574 195.436 160.728 1.00 29.77 ? 2188 GLU A OE1   1 
ATOM   5860  O  OE2   . GLU A 1 2188 ? 204.665 196.466 162.330 1.00 26.99 ? 2188 GLU A OE2   1 
ATOM   5861  N  N     . MET A 1 2189 ? 201.685 192.418 164.880 1.00 5.71  ? 2189 MET A N     1 
ATOM   5862  C  CA    . MET A 1 2189 ? 201.978 192.164 166.283 1.00 3.93  ? 2189 MET A CA    1 
ATOM   5863  C  C     . MET A 1 2189 ? 202.469 190.744 166.537 1.00 2.41  ? 2189 MET A C     1 
ATOM   5864  O  O     . MET A 1 2189 ? 202.515 190.316 167.695 1.00 5.21  ? 2189 MET A O     1 
ATOM   5865  C  CB    . MET A 1 2189 ? 200.741 192.455 167.134 1.00 2.26  ? 2189 MET A CB    1 
ATOM   5866  C  CG    . MET A 1 2189 ? 200.481 193.937 167.342 1.00 2.49  ? 2189 MET A CG    1 
ATOM   5867  S  SD    . MET A 1 2189 ? 198.981 194.283 168.278 1.00 8.11  ? 2189 MET A SD    1 
ATOM   5868  C  CE    . MET A 1 2189 ? 199.527 193.939 169.946 1.00 4.97  ? 2189 MET A CE    1 
ATOM   5869  N  N     . TYR A 1 2190 ? 202.831 190.008 165.483 1.00 2.48  ? 2190 TYR A N     1 
ATOM   5870  C  CA    . TYR A 1 2190 ? 203.355 188.643 165.597 1.00 2.61  ? 2190 TYR A CA    1 
ATOM   5871  C  C     . TYR A 1 2190 ? 202.378 187.724 166.326 1.00 2.83  ? 2190 TYR A C     1 
ATOM   5872  O  O     . TYR A 1 2190 ? 202.778 186.840 167.086 1.00 2.38  ? 2190 TYR A O     1 
ATOM   5873  C  CB    . TYR A 1 2190 ? 204.724 188.629 166.283 1.00 2.39  ? 2190 TYR A CB    1 
ATOM   5874  C  CG    . TYR A 1 2190 ? 205.700 189.627 165.715 1.00 3.88  ? 2190 TYR A CG    1 
ATOM   5875  C  CD1   . TYR A 1 2190 ? 206.385 189.364 164.537 1.00 3.40  ? 2190 TYR A CD1   1 
ATOM   5876  C  CD2   . TYR A 1 2190 ? 205.933 190.836 166.354 1.00 2.78  ? 2190 TYR A CD2   1 
ATOM   5877  C  CE1   . TYR A 1 2190 ? 207.273 190.275 164.014 1.00 4.21  ? 2190 TYR A CE1   1 
ATOM   5878  C  CE2   . TYR A 1 2190 ? 206.821 191.755 165.837 1.00 4.37  ? 2190 TYR A CE2   1 
ATOM   5879  C  CZ    . TYR A 1 2190 ? 207.488 191.470 164.668 1.00 7.09  ? 2190 TYR A CZ    1 
ATOM   5880  O  OH    . TYR A 1 2190 ? 208.376 192.383 164.149 1.00 12.24 ? 2190 TYR A OH    1 
ATOM   5881  N  N     . LEU A 1 2191 ? 201.089 187.923 166.087 1.00 3.74  ? 2191 LEU A N     1 
ATOM   5882  C  CA    . LEU A 1 2191 ? 200.051 187.133 166.726 1.00 0.96  ? 2191 LEU A CA    1 
ATOM   5883  C  C     . LEU A 1 2191 ? 199.435 186.163 165.728 1.00 2.27  ? 2191 LEU A C     1 
ATOM   5884  O  O     . LEU A 1 2191 ? 199.520 186.345 164.511 1.00 7.52  ? 2191 LEU A O     1 
ATOM   5885  C  CB    . LEU A 1 2191 ? 198.966 188.029 167.327 1.00 1.14  ? 2191 LEU A CB    1 
ATOM   5886  C  CG    . LEU A 1 2191 ? 199.381 188.856 168.544 1.00 0.95  ? 2191 LEU A CG    1 
ATOM   5887  C  CD1   . LEU A 1 2191 ? 198.160 189.425 169.232 1.00 2.24  ? 2191 LEU A CD1   1 
ATOM   5888  C  CD2   . LEU A 1 2191 ? 200.208 188.032 169.514 1.00 0.50  ? 2191 LEU A CD2   1 
ATOM   5889  N  N     . THR A 1 2192 ? 198.817 185.119 166.266 1.00 2.35  ? 2192 THR A N     1 
ATOM   5890  C  CA    . THR A 1 2192 ? 198.177 184.096 165.454 1.00 3.05  ? 2192 THR A CA    1 
ATOM   5891  C  C     . THR A 1 2192 ? 196.699 184.420 165.297 1.00 3.02  ? 2192 THR A C     1 
ATOM   5892  O  O     . THR A 1 2192 ? 195.986 184.604 166.288 1.00 1.86  ? 2192 THR A O     1 
ATOM   5893  C  CB    . THR A 1 2192 ? 198.354 182.714 166.084 1.00 3.63  ? 2192 THR A CB    1 
ATOM   5894  O  OG1   . THR A 1 2192 ? 199.745 182.377 166.115 1.00 3.95  ? 2192 THR A OG1   1 
ATOM   5895  C  CG2   . THR A 1 2192 ? 197.599 181.666 165.286 1.00 2.55  ? 2192 THR A CG2   1 
ATOM   5896  N  N     . TYR A 1 2193 ? 196.247 184.494 164.050 1.00 6.46  ? 2193 TYR A N     1 
ATOM   5897  C  CA    . TYR A 1 2193 ? 194.851 184.743 163.726 1.00 3.34  ? 2193 TYR A CA    1 
ATOM   5898  C  C     . TYR A 1 2193 ? 194.249 183.479 163.131 1.00 4.13  ? 2193 TYR A C     1 
ATOM   5899  O  O     . TYR A 1 2193 ? 194.862 182.840 162.270 1.00 9.17  ? 2193 TYR A O     1 
ATOM   5900  C  CB    . TYR A 1 2193 ? 194.715 185.916 162.751 1.00 2.30  ? 2193 TYR A CB    1 
ATOM   5901  C  CG    . TYR A 1 2193 ? 193.302 186.153 162.265 1.00 4.63  ? 2193 TYR A CG    1 
ATOM   5902  C  CD1   . TYR A 1 2193 ? 192.813 185.500 161.141 1.00 6.43  ? 2193 TYR A CD1   1 
ATOM   5903  C  CD2   . TYR A 1 2193 ? 192.458 187.028 162.932 1.00 4.19  ? 2193 TYR A CD2   1 
ATOM   5904  C  CE1   . TYR A 1 2193 ? 191.530 185.709 160.699 1.00 5.08  ? 2193 TYR A CE1   1 
ATOM   5905  C  CE2   . TYR A 1 2193 ? 191.166 187.243 162.495 1.00 5.33  ? 2193 TYR A CE2   1 
ATOM   5906  C  CZ    . TYR A 1 2193 ? 190.710 186.580 161.377 1.00 8.80  ? 2193 TYR A CZ    1 
ATOM   5907  O  OH    . TYR A 1 2193 ? 189.428 186.786 160.932 1.00 16.73 ? 2193 TYR A OH    1 
ATOM   5908  N  N     . GLY A 1 2194 ? 193.047 183.124 163.591 1.00 4.57  ? 2194 GLY A N     1 
ATOM   5909  C  CA    . GLY A 1 2194 ? 192.342 181.976 163.070 1.00 4.76  ? 2194 GLY A CA    1 
ATOM   5910  C  C     . GLY A 1 2194 ? 190.883 182.309 162.816 1.00 8.77  ? 2194 GLY A C     1 
ATOM   5911  O  O     . GLY A 1 2194 ? 190.371 183.341 163.256 1.00 10.51 ? 2194 GLY A O     1 
ATOM   5912  N  N     . ASP A 1 2195 ? 190.221 181.408 162.094 1.00 15.66 ? 2195 ASP A N     1 
ATOM   5913  C  CA    . ASP A 1 2195 ? 188.810 181.552 161.751 1.00 11.01 ? 2195 ASP A CA    1 
ATOM   5914  C  C     . ASP A 1 2195 ? 188.117 180.225 162.019 1.00 12.34 ? 2195 ASP A C     1 
ATOM   5915  O  O     . ASP A 1 2195 ? 188.358 179.241 161.313 1.00 16.82 ? 2195 ASP A O     1 
ATOM   5916  C  CB    . ASP A 1 2195 ? 188.640 181.977 160.292 1.00 8.25  ? 2195 ASP A CB    1 
ATOM   5917  C  CG    . ASP A 1 2195 ? 188.625 183.481 160.121 1.00 18.56 ? 2195 ASP A CG    1 
ATOM   5918  O  OD1   . ASP A 1 2195 ? 188.619 184.198 161.143 1.00 18.53 ? 2195 ASP A OD1   1 
ATOM   5919  O  OD2   . ASP A 1 2195 ? 188.623 183.950 158.964 1.00 24.58 ? 2195 ASP A OD2   1 
ATOM   5920  N  N     . GLY A 1 2196 ? 187.261 180.196 163.036 1.00 11.23 ? 2196 GLY A N     1 
ATOM   5921  C  CA    . GLY A 1 2196 ? 186.534 178.989 163.376 1.00 12.41 ? 2196 GLY A CA    1 
ATOM   5922  C  C     . GLY A 1 2196 ? 187.324 178.028 164.238 1.00 17.87 ? 2196 GLY A C     1 
ATOM   5923  O  O     . GLY A 1 2196 ? 187.686 178.354 165.373 1.00 19.15 ? 2196 GLY A O     1 
ATOM   5924  N  N     . GLU A 1 2197 ? 187.592 176.836 163.713 1.00 14.76 ? 2197 GLU A N     1 
ATOM   5925  C  CA    . GLU A 1 2197 ? 188.323 175.810 164.443 1.00 14.53 ? 2197 GLU A CA    1 
ATOM   5926  C  C     . GLU A 1 2197 ? 189.820 175.836 164.163 1.00 15.10 ? 2197 GLU A C     1 
ATOM   5927  O  O     . GLU A 1 2197 ? 190.542 174.969 164.662 1.00 13.53 ? 2197 GLU A O     1 
ATOM   5928  C  CB    . GLU A 1 2197 ? 187.762 174.423 164.110 1.00 22.40 ? 2197 GLU A CB    1 
ATOM   5929  C  CG    . GLU A 1 2197 ? 186.261 174.305 164.289 1.00 19.86 ? 2197 GLU A CG    1 
ATOM   5930  C  CD    . GLU A 1 2197 ? 185.767 175.001 165.543 1.00 24.32 ? 2197 GLU A CD    1 
ATOM   5931  O  OE1   . GLU A 1 2197 ? 185.969 174.452 166.646 1.00 29.01 ? 2197 GLU A OE1   1 
ATOM   5932  O  OE2   . GLU A 1 2197 ? 185.179 176.097 165.425 1.00 31.31 ? 2197 GLU A OE2   1 
ATOM   5933  N  N     . GLU A 1 2198 ? 190.298 176.801 163.384 1.00 11.56 ? 2198 GLU A N     1 
ATOM   5934  C  CA    . GLU A 1 2198 ? 191.721 176.917 163.122 1.00 9.35  ? 2198 GLU A CA    1 
ATOM   5935  C  C     . GLU A 1 2198 ? 192.464 177.346 164.387 1.00 10.24 ? 2198 GLU A C     1 
ATOM   5936  O  O     . GLU A 1 2198 ? 191.865 177.676 165.415 1.00 9.47  ? 2198 GLU A O     1 
ATOM   5937  C  CB    . GLU A 1 2198 ? 191.981 177.916 161.995 1.00 8.30  ? 2198 GLU A CB    1 
ATOM   5938  C  CG    . GLU A 1 2198 ? 191.144 177.687 160.752 1.00 8.62  ? 2198 GLU A CG    1 
ATOM   5939  C  CD    . GLU A 1 2198 ? 191.184 178.868 159.801 1.00 20.11 ? 2198 GLU A CD    1 
ATOM   5940  O  OE1   . GLU A 1 2198 ? 192.018 179.774 160.012 1.00 17.01 ? 2198 GLU A OE1   1 
ATOM   5941  O  OE2   . GLU A 1 2198 ? 190.384 178.890 158.845 1.00 24.94 ? 2198 GLU A OE2   1 
ATOM   5942  N  N     . VAL A 1 2199 ? 193.792 177.329 164.302 1.00 10.21 ? 2199 VAL A N     1 
ATOM   5943  C  CA    . VAL A 1 2199 ? 194.613 177.801 165.409 1.00 5.10  ? 2199 VAL A CA    1 
ATOM   5944  C  C     . VAL A 1 2199 ? 194.360 179.288 165.599 1.00 4.05  ? 2199 VAL A C     1 
ATOM   5945  O  O     . VAL A 1 2199 ? 194.486 180.079 164.657 1.00 9.15  ? 2199 VAL A O     1 
ATOM   5946  C  CB    . VAL A 1 2199 ? 196.095 177.507 165.151 1.00 6.05  ? 2199 VAL A CB    1 
ATOM   5947  C  CG1   . VAL A 1 2199 ? 196.946 177.992 166.313 1.00 5.02  ? 2199 VAL A CG1   1 
ATOM   5948  C  CG2   . VAL A 1 2199 ? 196.307 176.023 164.914 1.00 4.85  ? 2199 VAL A CG2   1 
ATOM   5949  N  N     . GLY A 1 2200 ? 193.996 179.675 166.817 1.00 2.84  ? 2200 GLY A N     1 
ATOM   5950  C  CA    . GLY A 1 2200 ? 193.656 181.050 167.111 1.00 2.94  ? 2200 GLY A CA    1 
ATOM   5951  C  C     . GLY A 1 2200 ? 192.207 181.418 166.888 1.00 2.52  ? 2200 GLY A C     1 
ATOM   5952  O  O     . GLY A 1 2200 ? 191.825 182.556 167.187 1.00 1.74  ? 2200 GLY A O     1 
ATOM   5953  N  N     . GLY A 1 2201 ? 191.388 180.495 166.380 1.00 5.07  ? 2201 GLY A N     1 
ATOM   5954  C  CA    . GLY A 1 2201 ? 189.997 180.818 166.111 1.00 4.36  ? 2201 GLY A CA    1 
ATOM   5955  C  C     . GLY A 1 2201 ? 189.209 181.142 167.366 1.00 1.73  ? 2201 GLY A C     1 
ATOM   5956  O  O     . GLY A 1 2201 ? 188.380 182.055 167.370 1.00 1.12  ? 2201 GLY A O     1 
ATOM   5957  N  N     . MET A 1 2202 ? 189.450 180.396 168.445 1.00 2.99  ? 2202 MET A N     1 
ATOM   5958  C  CA    . MET A 1 2202 ? 188.766 180.674 169.703 1.00 1.24  ? 2202 MET A CA    1 
ATOM   5959  C  C     . MET A 1 2202 ? 189.119 182.060 170.224 1.00 1.11  ? 2202 MET A C     1 
ATOM   5960  O  O     . MET A 1 2202 ? 188.253 182.786 170.725 1.00 1.36  ? 2202 MET A O     1 
ATOM   5961  C  CB    . MET A 1 2202 ? 189.119 179.611 170.741 1.00 2.64  ? 2202 MET A CB    1 
ATOM   5962  C  CG    . MET A 1 2202 ? 188.427 178.277 170.537 1.00 4.47  ? 2202 MET A CG    1 
ATOM   5963  S  SD    . MET A 1 2202 ? 188.598 177.198 171.971 1.00 32.34 ? 2202 MET A SD    1 
ATOM   5964  C  CE    . MET A 1 2202 ? 190.106 176.327 171.564 1.00 13.18 ? 2202 MET A CE    1 
ATOM   5965  N  N     . TRP A 1 2203 ? 190.392 182.442 170.113 1.00 1.15  ? 2203 TRP A N     1 
ATOM   5966  C  CA    . TRP A 1 2203 ? 190.823 183.759 170.564 1.00 0.52  ? 2203 TRP A CA    1 
ATOM   5967  C  C     . TRP A 1 2203 ? 190.201 184.869 169.724 1.00 0.46  ? 2203 TRP A C     1 
ATOM   5968  O  O     . TRP A 1 2203 ? 189.820 185.915 170.257 1.00 0.56  ? 2203 TRP A O     1 
ATOM   5969  C  CB    . TRP A 1 2203 ? 192.349 183.832 170.536 1.00 0.58  ? 2203 TRP A CB    1 
ATOM   5970  C  CG    . TRP A 1 2203 ? 192.912 185.150 170.941 1.00 0.25  ? 2203 TRP A CG    1 
ATOM   5971  C  CD1   . TRP A 1 2203 ? 193.138 185.589 172.208 1.00 0.13  ? 2203 TRP A CD1   1 
ATOM   5972  C  CD2   . TRP A 1 2203 ? 193.341 186.200 170.069 1.00 0.11  ? 2203 TRP A CD2   1 
ATOM   5973  N  NE1   . TRP A 1 2203 ? 193.674 186.850 172.184 1.00 0.06  ? 2203 TRP A NE1   1 
ATOM   5974  C  CE2   . TRP A 1 2203 ? 193.809 187.249 170.880 1.00 0.08  ? 2203 TRP A CE2   1 
ATOM   5975  C  CE3   . TRP A 1 2203 ? 193.372 186.355 168.681 1.00 0.13  ? 2203 TRP A CE3   1 
ATOM   5976  C  CZ2   . TRP A 1 2203 ? 194.302 188.438 170.351 1.00 0.10  ? 2203 TRP A CZ2   1 
ATOM   5977  C  CZ3   . TRP A 1 2203 ? 193.861 187.533 168.158 1.00 0.35  ? 2203 TRP A CZ3   1 
ATOM   5978  C  CH2   . TRP A 1 2203 ? 194.320 188.560 168.990 1.00 0.97  ? 2203 TRP A CH2   1 
ATOM   5979  N  N     . VAL A 1 2204 ? 190.088 184.657 168.411 1.00 0.40  ? 2204 VAL A N     1 
ATOM   5980  C  CA    . VAL A 1 2204 ? 189.495 185.669 167.540 1.00 0.50  ? 2204 VAL A CA    1 
ATOM   5981  C  C     . VAL A 1 2204 ? 188.014 185.849 167.857 1.00 0.88  ? 2204 VAL A C     1 
ATOM   5982  O  O     . VAL A 1 2204 ? 187.487 186.966 167.805 1.00 0.81  ? 2204 VAL A O     1 
ATOM   5983  C  CB    . VAL A 1 2204 ? 189.728 185.302 166.063 1.00 1.08  ? 2204 VAL A CB    1 
ATOM   5984  C  CG1   . VAL A 1 2204 ? 188.928 186.214 165.144 1.00 1.94  ? 2204 VAL A CG1   1 
ATOM   5985  C  CG2   . VAL A 1 2204 ? 191.206 185.382 165.731 1.00 0.88  ? 2204 VAL A CG2   1 
ATOM   5986  N  N     . GLU A 1 2205 ? 187.323 184.759 168.199 1.00 1.18  ? 2205 GLU A N     1 
ATOM   5987  C  CA    . GLU A 1 2205 ? 185.932 184.874 168.625 1.00 0.82  ? 2205 GLU A CA    1 
ATOM   5988  C  C     . GLU A 1 2205 ? 185.809 185.723 169.884 1.00 1.17  ? 2205 GLU A C     1 
ATOM   5989  O  O     . GLU A 1 2205 ? 184.873 186.518 170.016 1.00 1.52  ? 2205 GLU A O     1 
ATOM   5990  C  CB    . GLU A 1 2205 ? 185.332 183.486 168.855 1.00 1.39  ? 2205 GLU A CB    1 
ATOM   5991  C  CG    . GLU A 1 2205 ? 185.199 182.639 167.600 1.00 7.33  ? 2205 GLU A CG    1 
ATOM   5992  C  CD    . GLU A 1 2205 ? 184.191 183.201 166.616 1.00 17.92 ? 2205 GLU A CD    1 
ATOM   5993  O  OE1   . GLU A 1 2205 ? 183.204 183.824 167.060 1.00 15.45 ? 2205 GLU A OE1   1 
ATOM   5994  O  OE2   . GLU A 1 2205 ? 184.385 183.017 165.397 1.00 22.07 ? 2205 GLU A OE2   1 
ATOM   5995  N  N     . LYS A 1 2206 ? 186.748 185.569 170.822 1.00 0.84  ? 2206 LYS A N     1 
ATOM   5996  C  CA    . LYS A 1 2206 ? 186.709 186.371 172.040 1.00 0.38  ? 2206 LYS A CA    1 
ATOM   5997  C  C     . LYS A 1 2206 ? 186.968 187.844 171.746 1.00 0.35  ? 2206 LYS A C     1 
ATOM   5998  O  O     . LYS A 1 2206 ? 186.399 188.720 172.405 1.00 1.51  ? 2206 LYS A O     1 
ATOM   5999  C  CB    . LYS A 1 2206 ? 187.715 185.833 173.056 1.00 0.41  ? 2206 LYS A CB    1 
ATOM   6000  C  CG    . LYS A 1 2206 ? 187.261 184.552 173.729 1.00 0.53  ? 2206 LYS A CG    1 
ATOM   6001  C  CD    . LYS A 1 2206 ? 185.946 184.767 174.450 1.00 0.82  ? 2206 LYS A CD    1 
ATOM   6002  C  CE    . LYS A 1 2206 ? 185.323 183.459 174.886 1.00 0.27  ? 2206 LYS A CE    1 
ATOM   6003  N  NZ    . LYS A 1 2206 ? 184.126 183.687 175.729 1.00 0.13  ? 2206 LYS A NZ    1 
ATOM   6004  N  N     . VAL A 1 2207 ? 187.828 188.136 170.770 1.00 0.50  ? 2207 VAL A N     1 
ATOM   6005  C  CA    . VAL A 1 2207 ? 188.032 189.521 170.357 1.00 0.41  ? 2207 VAL A CA    1 
ATOM   6006  C  C     . VAL A 1 2207 ? 186.746 190.096 169.777 1.00 0.48  ? 2207 VAL A C     1 
ATOM   6007  O  O     . VAL A 1 2207 ? 186.364 191.231 170.082 1.00 0.45  ? 2207 VAL A O     1 
ATOM   6008  C  CB    . VAL A 1 2207 ? 189.200 189.619 169.358 1.00 0.37  ? 2207 VAL A CB    1 
ATOM   6009  C  CG1   . VAL A 1 2207 ? 189.397 191.054 168.907 1.00 0.27  ? 2207 VAL A CG1   1 
ATOM   6010  C  CG2   . VAL A 1 2207 ? 190.477 189.070 169.971 1.00 0.16  ? 2207 VAL A CG2   1 
ATOM   6011  N  N     . LEU A 1 2208 ? 186.060 189.322 168.935 1.00 0.62  ? 2208 LEU A N     1 
ATOM   6012  C  CA    . LEU A 1 2208 ? 184.796 189.777 168.364 1.00 0.53  ? 2208 LEU A CA    1 
ATOM   6013  C  C     . LEU A 1 2208 ? 183.716 189.905 169.431 1.00 0.31  ? 2208 LEU A C     1 
ATOM   6014  O  O     . LEU A 1 2208 ? 182.915 190.843 169.397 1.00 0.91  ? 2208 LEU A O     1 
ATOM   6015  C  CB    . LEU A 1 2208 ? 184.354 188.821 167.258 1.00 0.94  ? 2208 LEU A CB    1 
ATOM   6016  C  CG    . LEU A 1 2208 ? 185.310 188.723 166.071 1.00 1.25  ? 2208 LEU A CG    1 
ATOM   6017  C  CD1   . LEU A 1 2208 ? 184.873 187.627 165.125 1.00 1.85  ? 2208 LEU A CD1   1 
ATOM   6018  C  CD2   . LEU A 1 2208 ? 185.397 190.052 165.347 1.00 1.74  ? 2208 LEU A CD2   1 
ATOM   6019  N  N     . GLN A 1 2209 ? 183.672 188.966 170.379 1.00 0.34  ? 2209 GLN A N     1 
ATOM   6020  C  CA    . GLN A 1 2209 ? 182.722 189.073 171.481 1.00 0.37  ? 2209 GLN A CA    1 
ATOM   6021  C  C     . GLN A 1 2209 ? 183.002 190.307 172.326 1.00 0.41  ? 2209 GLN A C     1 
ATOM   6022  O  O     . GLN A 1 2209 ? 182.073 190.992 172.769 1.00 0.46  ? 2209 GLN A O     1 
ATOM   6023  C  CB    . GLN A 1 2209 ? 182.772 187.815 172.346 1.00 0.34  ? 2209 GLN A CB    1 
ATOM   6024  C  CG    . GLN A 1 2209 ? 182.190 186.576 171.696 1.00 0.32  ? 2209 GLN A CG    1 
ATOM   6025  C  CD    . GLN A 1 2209 ? 182.301 185.354 172.584 1.00 0.53  ? 2209 GLN A CD    1 
ATOM   6026  O  OE1   . GLN A 1 2209 ? 182.801 185.432 173.702 1.00 0.80  ? 2209 GLN A OE1   1 
ATOM   6027  N  NE2   . GLN A 1 2209 ? 181.836 184.216 172.086 1.00 1.31  ? 2209 GLN A NE2   1 
ATOM   6028  N  N     . LEU A 1 2210 ? 184.282 190.606 172.559 1.00 0.55  ? 2210 LEU A N     1 
ATOM   6029  C  CA    . LEU A 1 2210 ? 184.645 191.802 173.309 1.00 0.25  ? 2210 LEU A CA    1 
ATOM   6030  C  C     . LEU A 1 2210 ? 184.180 193.064 172.593 1.00 0.42  ? 2210 LEU A C     1 
ATOM   6031  O  O     . LEU A 1 2210 ? 183.745 194.026 173.235 1.00 0.47  ? 2210 LEU A O     1 
ATOM   6032  C  CB    . LEU A 1 2210 ? 186.156 191.826 173.536 1.00 0.24  ? 2210 LEU A CB    1 
ATOM   6033  C  CG    . LEU A 1 2210 ? 186.767 193.081 174.153 1.00 0.25  ? 2210 LEU A CG    1 
ATOM   6034  C  CD1   . LEU A 1 2210 ? 186.385 193.192 175.618 1.00 0.17  ? 2210 LEU A CD1   1 
ATOM   6035  C  CD2   . LEU A 1 2210 ? 188.276 193.066 173.983 1.00 0.04  ? 2210 LEU A CD2   1 
ATOM   6036  N  N     . TYR A 1 2211 ? 184.267 193.080 171.260 1.00 0.51  ? 2211 TYR A N     1 
ATOM   6037  C  CA    . TYR A 1 2211 ? 183.786 194.227 170.498 1.00 0.43  ? 2211 TYR A CA    1 
ATOM   6038  C  C     . TYR A 1 2211 ? 182.284 194.410 170.666 1.00 1.15  ? 2211 TYR A C     1 
ATOM   6039  O  O     . TYR A 1 2211 ? 181.799 195.540 170.785 1.00 2.06  ? 2211 TYR A O     1 
ATOM   6040  C  CB    . TYR A 1 2211 ? 184.139 194.069 169.020 1.00 0.48  ? 2211 TYR A CB    1 
ATOM   6041  C  CG    . TYR A 1 2211 ? 183.623 195.196 168.155 1.00 2.19  ? 2211 TYR A CG    1 
ATOM   6042  C  CD1   . TYR A 1 2211 ? 182.852 194.940 167.030 1.00 3.54  ? 2211 TYR A CD1   1 
ATOM   6043  C  CD2   . TYR A 1 2211 ? 183.909 196.519 168.465 1.00 2.44  ? 2211 TYR A CD2   1 
ATOM   6044  C  CE1   . TYR A 1 2211 ? 182.383 195.969 166.241 1.00 5.61  ? 2211 TYR A CE1   1 
ATOM   6045  C  CE2   . TYR A 1 2211 ? 183.442 197.551 167.684 1.00 4.05  ? 2211 TYR A CE2   1 
ATOM   6046  C  CZ    . TYR A 1 2211 ? 182.682 197.272 166.573 1.00 7.52  ? 2211 TYR A CZ    1 
ATOM   6047  O  OH    . TYR A 1 2211 ? 182.218 198.303 165.792 1.00 12.72 ? 2211 TYR A OH    1 
ATOM   6048  N  N     . GLN A 1 2212 ? 181.532 193.308 170.667 1.00 2.08  ? 2212 GLN A N     1 
ATOM   6049  C  CA    . GLN A 1 2212 ? 180.087 193.401 170.843 1.00 1.82  ? 2212 GLN A CA    1 
ATOM   6050  C  C     . GLN A 1 2212 ? 179.737 193.988 172.204 1.00 2.18  ? 2212 GLN A C     1 
ATOM   6051  O  O     . GLN A 1 2212 ? 178.808 194.794 172.318 1.00 6.82  ? 2212 GLN A O     1 
ATOM   6052  C  CB    . GLN A 1 2212 ? 179.450 192.024 170.671 1.00 4.65  ? 2212 GLN A CB    1 
ATOM   6053  C  CG    . GLN A 1 2212 ? 179.611 191.427 169.283 1.00 7.60  ? 2212 GLN A CG    1 
ATOM   6054  C  CD    . GLN A 1 2212 ? 178.873 192.205 168.215 1.00 19.68 ? 2212 GLN A CD    1 
ATOM   6055  O  OE1   . GLN A 1 2212 ? 177.764 192.690 168.437 1.00 13.60 ? 2212 GLN A OE1   1 
ATOM   6056  N  NE2   . GLN A 1 2212 ? 179.485 192.328 167.042 1.00 27.07 ? 2212 GLN A NE2   1 
ATOM   6057  N  N     . ILE A 1 2213 ? 180.474 193.598 173.246 1.00 1.13  ? 2213 ILE A N     1 
ATOM   6058  C  CA    . ILE A 1 2213 ? 180.216 194.121 174.583 1.00 1.44  ? 2213 ILE A CA    1 
ATOM   6059  C  C     . ILE A 1 2213 ? 180.539 195.609 174.651 1.00 1.99  ? 2213 ILE A C     1 
ATOM   6060  O  O     . ILE A 1 2213 ? 179.862 196.370 175.351 1.00 2.03  ? 2213 ILE A O     1 
ATOM   6061  C  CB    . ILE A 1 2213 ? 181.004 193.310 175.629 1.00 2.33  ? 2213 ILE A CB    1 
ATOM   6062  C  CG1   . ILE A 1 2213 ? 180.625 191.831 175.544 1.00 1.38  ? 2213 ILE A CG1   1 
ATOM   6063  C  CG2   . ILE A 1 2213 ? 180.746 193.839 177.030 1.00 1.55  ? 2213 ILE A CG2   1 
ATOM   6064  C  CD1   . ILE A 1 2213 ? 179.225 191.528 176.027 1.00 1.20  ? 2213 ILE A CD1   1 
ATOM   6065  N  N     . THR A 1 2214 ? 181.570 196.053 173.925 1.00 1.42  ? 2214 THR A N     1 
ATOM   6066  C  CA    . THR A 1 2214 ? 181.913 197.473 173.913 1.00 2.18  ? 2214 THR A CA    1 
ATOM   6067  C  C     . THR A 1 2214 ? 180.802 198.329 173.325 1.00 2.24  ? 2214 THR A C     1 
ATOM   6068  O  O     . THR A 1 2214 ? 180.721 199.520 173.641 1.00 4.84  ? 2214 THR A O     1 
ATOM   6069  C  CB    . THR A 1 2214 ? 183.201 197.721 173.123 1.00 0.97  ? 2214 THR A CB    1 
ATOM   6070  O  OG1   . THR A 1 2214 ? 183.104 197.107 171.832 1.00 6.74  ? 2214 THR A OG1   1 
ATOM   6071  C  CG2   . THR A 1 2214 ? 184.393 197.158 173.850 1.00 0.41  ? 2214 THR A CG2   1 
ATOM   6072  N  N     . GLN A 1 2215 ? 179.956 197.757 172.474 1.00 2.26  ? 2215 GLN A N     1 
ATOM   6073  C  CA    . GLN A 1 2215 ? 178.871 198.496 171.844 1.00 2.87  ? 2215 GLN A CA    1 
ATOM   6074  C  C     . GLN A 1 2215 ? 177.585 198.485 172.659 1.00 4.36  ? 2215 GLN A C     1 
ATOM   6075  O  O     . GLN A 1 2215 ? 176.636 199.185 172.292 1.00 10.99 ? 2215 GLN A O     1 
ATOM   6076  C  CB    . GLN A 1 2215 ? 178.594 197.927 170.449 1.00 2.53  ? 2215 GLN A CB    1 
ATOM   6077  C  CG    . GLN A 1 2215 ? 179.778 198.018 169.500 1.00 3.66  ? 2215 GLN A CG    1 
ATOM   6078  C  CD    . GLN A 1 2215 ? 179.609 197.149 168.271 1.00 8.07  ? 2215 GLN A CD    1 
ATOM   6079  O  OE1   . GLN A 1 2215 ? 179.555 195.924 168.364 1.00 16.96 ? 2215 GLN A OE1   1 
ATOM   6080  N  NE2   . GLN A 1 2215 ? 179.527 197.782 167.107 1.00 8.39  ? 2215 GLN A NE2   1 
ATOM   6081  N  N     . ILE A 1 2216 ? 177.528 197.716 173.745 1.00 3.89  ? 2216 ILE A N     1 
ATOM   6082  C  CA    . ILE A 1 2216 ? 176.313 197.600 174.543 1.00 3.94  ? 2216 ILE A CA    1 
ATOM   6083  C  C     . ILE A 1 2216 ? 176.564 198.130 175.949 1.00 3.33  ? 2216 ILE A C     1 
ATOM   6084  O  O     . ILE A 1 2216 ? 175.661 198.680 176.588 1.00 7.84  ? 2216 ILE A O     1 
ATOM   6085  C  CB    . ILE A 1 2216 ? 175.825 196.139 174.580 1.00 4.59  ? 2216 ILE A CB    1 
ATOM   6086  C  CG1   . ILE A 1 2216 ? 175.547 195.637 173.164 1.00 6.15  ? 2216 ILE A CG1   1 
ATOM   6087  C  CG2   . ILE A 1 2216 ? 174.583 196.001 175.443 1.00 10.78 ? 2216 ILE A CG2   1 
ATOM   6088  C  CD1   . ILE A 1 2216 ? 174.477 196.415 172.443 1.00 7.56  ? 2216 ILE A CD1   1 
ATOM   6089  N  N     . ASN A 1 2217 ? 177.795 197.993 176.430 1.00 1.90  ? 2217 ASN A N     1 
ATOM   6090  C  CA    . ASN A 1 2217 ? 178.152 198.371 177.789 1.00 1.83  ? 2217 ASN A CA    1 
ATOM   6091  C  C     . ASN A 1 2217 ? 179.235 199.436 177.769 1.00 1.28  ? 2217 ASN A C     1 
ATOM   6092  O  O     . ASN A 1 2217 ? 180.133 199.408 176.922 1.00 7.05  ? 2217 ASN A O     1 
ATOM   6093  C  CB    . ASN A 1 2217 ? 178.643 197.162 178.600 1.00 1.18  ? 2217 ASN A CB    1 
ATOM   6094  C  CG    . ASN A 1 2217 ? 177.746 195.951 178.449 1.00 1.52  ? 2217 ASN A CG    1 
ATOM   6095  O  OD1   . ASN A 1 2217 ? 177.595 195.406 177.356 1.00 6.31  ? 2217 ASN A OD1   1 
ATOM   6096  N  ND2   . ASN A 1 2217 ? 177.144 195.523 179.549 1.00 1.66  ? 2217 ASN A ND2   1 
ATOM   6097  N  N     . HIS A 1 2218 ? 179.138 200.386 178.696 1.00 0.57  ? 2218 HIS A N     1 
ATOM   6098  C  CA    . HIS A 1 2218 ? 180.229 201.318 178.935 1.00 0.43  ? 2218 HIS A CA    1 
ATOM   6099  C  C     . HIS A 1 2218 ? 181.212 200.805 179.979 1.00 0.28  ? 2218 HIS A C     1 
ATOM   6100  O  O     . HIS A 1 2218 ? 182.301 201.371 180.118 1.00 0.16  ? 2218 HIS A O     1 
ATOM   6101  C  CB    . HIS A 1 2218 ? 179.681 202.684 179.360 1.00 0.27  ? 2218 HIS A CB    1 
ATOM   6102  C  CG    . HIS A 1 2218 ? 178.874 202.649 180.618 1.00 0.37  ? 2218 HIS A CG    1 
ATOM   6103  N  ND1   . HIS A 1 2218 ? 177.508 202.472 180.620 1.00 0.60  ? 2218 HIS A ND1   1 
ATOM   6104  C  CD2   . HIS A 1 2218 ? 179.238 202.772 181.915 1.00 0.49  ? 2218 HIS A CD2   1 
ATOM   6105  C  CE1   . HIS A 1 2218 ? 177.066 202.483 181.864 1.00 0.59  ? 2218 HIS A CE1   1 
ATOM   6106  N  NE2   . HIS A 1 2218 ? 178.097 202.665 182.670 1.00 0.53  ? 2218 HIS A NE2   1 
ATOM   6107  N  N     . GLY A 1 2219 ? 180.851 199.748 180.702 1.00 0.27  ? 2219 GLY A N     1 
ATOM   6108  C  CA    . GLY A 1 2219 ? 181.743 199.085 181.631 1.00 0.15  ? 2219 GLY A CA    1 
ATOM   6109  C  C     . GLY A 1 2219 ? 181.744 197.585 181.416 1.00 0.26  ? 2219 GLY A C     1 
ATOM   6110  O  O     . GLY A 1 2219 ? 180.680 196.964 181.362 1.00 0.54  ? 2219 GLY A O     1 
ATOM   6111  N  N     . LEU A 1 2220 ? 182.926 196.989 181.283 1.00 0.17  ? 2220 LEU A N     1 
ATOM   6112  C  CA    . LEU A 1 2220 ? 183.032 195.573 180.969 1.00 0.12  ? 2220 LEU A CA    1 
ATOM   6113  C  C     . LEU A 1 2220 ? 184.267 194.977 181.625 1.00 0.10  ? 2220 LEU A C     1 
ATOM   6114  O  O     . LEU A 1 2220 ? 185.259 195.667 181.864 1.00 0.08  ? 2220 LEU A O     1 
ATOM   6115  C  CB    . LEU A 1 2220 ? 183.061 195.349 179.450 1.00 0.29  ? 2220 LEU A CB    1 
ATOM   6116  C  CG    . LEU A 1 2220 ? 184.187 195.952 178.602 1.00 0.21  ? 2220 LEU A CG    1 
ATOM   6117  C  CD1   . LEU A 1 2220 ? 185.472 195.131 178.620 1.00 0.14  ? 2220 LEU A CD1   1 
ATOM   6118  C  CD2   . LEU A 1 2220 ? 183.698 196.147 177.184 1.00 1.35  ? 2220 LEU A CD2   1 
ATOM   6119  N  N     . MET A 1 2221 ? 184.199 193.677 181.904 1.00 0.26  ? 2221 MET A N     1 
ATOM   6120  C  CA    . MET A 1 2221 ? 185.315 192.942 182.481 1.00 0.05  ? 2221 MET A CA    1 
ATOM   6121  C  C     . MET A 1 2221 ? 185.731 191.814 181.554 1.00 0.04  ? 2221 MET A C     1 
ATOM   6122  O  O     . MET A 1 2221 ? 184.879 191.099 181.016 1.00 0.05  ? 2221 MET A O     1 
ATOM   6123  C  CB    . MET A 1 2221 ? 184.981 192.387 183.867 1.00 0.08  ? 2221 MET A CB    1 
ATOM   6124  C  CG    . MET A 1 2221 ? 184.801 193.455 184.905 1.00 0.18  ? 2221 MET A CG    1 
ATOM   6125  S  SD    . MET A 1 2221 ? 184.410 192.850 186.547 1.00 26.23 ? 2221 MET A SD    1 
ATOM   6126  C  CE    . MET A 1 2221 ? 184.207 194.416 187.384 1.00 2.54  ? 2221 MET A CE    1 
ATOM   6127  N  N     . MET A 1 2222 ? 187.038 191.668 181.371 1.00 0.07  ? 2222 MET A N     1 
ATOM   6128  C  CA    . MET A 1 2222 ? 187.630 190.497 180.738 1.00 0.02  ? 2222 MET A CA    1 
ATOM   6129  C  C     . MET A 1 2222 ? 188.198 189.625 181.849 1.00 0.02  ? 2222 MET A C     1 
ATOM   6130  O  O     . MET A 1 2222 ? 189.168 190.005 182.510 1.00 0.04  ? 2222 MET A O     1 
ATOM   6131  C  CB    . MET A 1 2222 ? 188.711 190.918 179.747 1.00 0.03  ? 2222 MET A CB    1 
ATOM   6132  C  CG    . MET A 1 2222 ? 188.199 191.792 178.626 1.00 0.05  ? 2222 MET A CG    1 
ATOM   6133  S  SD    . MET A 1 2222 ? 189.514 192.558 177.668 1.00 0.09  ? 2222 MET A SD    1 
ATOM   6134  C  CE    . MET A 1 2222 ? 189.717 194.083 178.584 1.00 0.03  ? 2222 MET A CE    1 
ATOM   6135  N  N     . VAL A 1 2223 ? 187.585 188.467 182.069 1.00 0.03  ? 2223 VAL A N     1 
ATOM   6136  C  CA    . VAL A 1 2223 ? 187.925 187.593 183.183 1.00 0.03  ? 2223 VAL A CA    1 
ATOM   6137  C  C     . VAL A 1 2223 ? 188.502 186.300 182.631 1.00 0.04  ? 2223 VAL A C     1 
ATOM   6138  O  O     . VAL A 1 2223 ? 187.903 185.669 181.754 1.00 0.09  ? 2223 VAL A O     1 
ATOM   6139  C  CB    . VAL A 1 2223 ? 186.701 187.311 184.070 1.00 0.03  ? 2223 VAL A CB    1 
ATOM   6140  C  CG1   . VAL A 1 2223 ? 187.117 186.538 185.309 1.00 0.07  ? 2223 VAL A CG1   1 
ATOM   6141  C  CG2   . VAL A 1 2223 ? 186.005 188.610 184.442 1.00 0.05  ? 2223 VAL A CG2   1 
ATOM   6142  N  N     . GLY A 1 2224 ? 189.660 185.906 183.145 1.00 0.06  ? 2224 GLY A N     1 
ATOM   6143  C  CA    . GLY A 1 2224 ? 190.284 184.671 182.747 1.00 0.10  ? 2224 GLY A CA    1 
ATOM   6144  C  C     . GLY A 1 2224 ? 191.622 184.455 183.415 1.00 0.18  ? 2224 GLY A C     1 
ATOM   6145  O  O     . GLY A 1 2224 ? 192.278 185.400 183.856 1.00 0.22  ? 2224 GLY A O     1 
ATOM   6146  N  N     . PRO A 1 2225 ? 192.064 183.200 183.479 1.00 0.55  ? 2225 PRO A N     1 
ATOM   6147  C  CA    . PRO A 1 2225 ? 193.338 182.896 184.138 1.00 0.21  ? 2225 PRO A CA    1 
ATOM   6148  C  C     . PRO A 1 2225 ? 194.496 183.619 183.469 1.00 0.30  ? 2225 PRO A C     1 
ATOM   6149  O  O     . PRO A 1 2225 ? 194.423 184.032 182.311 1.00 0.43  ? 2225 PRO A O     1 
ATOM   6150  C  CB    . PRO A 1 2225 ? 193.468 181.376 183.977 1.00 0.52  ? 2225 PRO A CB    1 
ATOM   6151  C  CG    . PRO A 1 2225 ? 192.077 180.900 183.751 1.00 0.46  ? 2225 PRO A CG    1 
ATOM   6152  C  CD    . PRO A 1 2225 ? 191.396 181.986 182.986 1.00 0.20  ? 2225 PRO A CD    1 
ATOM   6153  N  N     . SER A 1 2226 ? 195.577 183.778 184.227 1.00 0.48  ? 2226 SER A N     1 
ATOM   6154  C  CA    . SER A 1 2226 ? 196.746 184.478 183.717 1.00 0.26  ? 2226 SER A CA    1 
ATOM   6155  C  C     . SER A 1 2226 ? 197.290 183.760 182.489 1.00 0.38  ? 2226 SER A C     1 
ATOM   6156  O  O     . SER A 1 2226 ? 197.557 182.554 182.526 1.00 1.35  ? 2226 SER A O     1 
ATOM   6157  C  CB    . SER A 1 2226 ? 197.816 184.582 184.803 1.00 0.45  ? 2226 SER A CB    1 
ATOM   6158  O  OG    . SER A 1 2226 ? 199.043 185.046 184.271 1.00 0.45  ? 2226 SER A OG    1 
ATOM   6159  N  N     . GLY A 1 2227 ? 197.439 184.500 181.396 1.00 0.15  ? 2227 GLY A N     1 
ATOM   6160  C  CA    . GLY A 1 2227 ? 197.900 183.925 180.150 1.00 0.17  ? 2227 GLY A CA    1 
ATOM   6161  C  C     . GLY A 1 2227 ? 196.783 183.348 179.306 1.00 0.54  ? 2227 GLY A C     1 
ATOM   6162  O  O     . GLY A 1 2227 ? 196.934 182.279 178.711 1.00 1.46  ? 2227 GLY A O     1 
ATOM   6163  N  N     . SER A 1 2228 ? 195.652 184.047 179.255 1.00 1.05  ? 2228 SER A N     1 
ATOM   6164  C  CA    . SER A 1 2228 ? 194.505 183.630 178.459 1.00 0.65  ? 2228 SER A CA    1 
ATOM   6165  C  C     . SER A 1 2228 ? 194.314 184.494 177.221 1.00 0.33  ? 2228 SER A C     1 
ATOM   6166  O  O     . SER A 1 2228 ? 193.350 184.292 176.478 1.00 0.42  ? 2228 SER A O     1 
ATOM   6167  C  CB    . SER A 1 2228 ? 193.236 183.651 179.311 1.00 0.37  ? 2228 SER A CB    1 
ATOM   6168  O  OG    . SER A 1 2228 ? 193.318 182.713 180.366 1.00 1.93  ? 2228 SER A OG    1 
ATOM   6169  N  N     . GLY A 1 2229 ? 195.207 185.451 176.986 1.00 0.06  ? 2229 GLY A N     1 
ATOM   6170  C  CA    . GLY A 1 2229 ? 195.076 186.328 175.844 1.00 0.04  ? 2229 GLY A CA    1 
ATOM   6171  C  C     . GLY A 1 2229 ? 194.153 187.503 176.039 1.00 0.05  ? 2229 GLY A C     1 
ATOM   6172  O  O     . GLY A 1 2229 ? 193.688 188.076 175.053 1.00 0.03  ? 2229 GLY A O     1 
ATOM   6173  N  N     . LYS A 1 2230 ? 193.850 187.828 177.290 1.00 0.01  ? 2230 LYS A N     1 
ATOM   6174  C  CA    . LYS A 1 2230 ? 192.910 188.941 177.574 1.00 0.05  ? 2230 LYS A CA    1 
ATOM   6175  C  C     . LYS A 1 2230 ? 193.544 190.263 177.106 1.00 0.02  ? 2230 LYS A C     1 
ATOM   6176  O  O     . LYS A 1 2230 ? 192.863 191.011 176.378 1.00 0.03  ? 2230 LYS A O     1 
ATOM   6177  C  CB    . LYS A 1 2230 ? 192.525 188.940 179.058 1.00 0.00  ? 2230 LYS A CB    1 
ATOM   6178  C  CG    . LYS A 1 2230 ? 192.027 187.629 179.631 1.00 0.04  ? 2230 LYS A CG    1 
ATOM   6179  C  CD    . LYS A 1 2230 ? 191.665 187.751 181.106 1.00 0.02  ? 2230 LYS A CD    1 
ATOM   6180  C  CE    . LYS A 1 2230 ? 192.806 188.230 181.948 1.00 0.02  ? 2230 LYS A CE    1 
ATOM   6181  N  NZ    . LYS A 1 2230 ? 193.954 187.322 181.904 1.00 0.02  ? 2230 LYS A NZ    1 
ATOM   6182  N  N     . SER A 1 2231 ? 194.796 190.529 177.481 1.00 0.03  ? 2231 SER A N     1 
ATOM   6183  C  CA    . SER A 1 2231 ? 195.451 191.821 177.133 1.00 0.03  ? 2231 SER A CA    1 
ATOM   6184  C  C     . SER A 1 2231 ? 195.557 191.978 175.612 1.00 0.05  ? 2231 SER A C     1 
ATOM   6185  O  O     . SER A 1 2231 ? 195.183 193.056 175.101 1.00 0.12  ? 2231 SER A O     1 
ATOM   6186  C  CB    . SER A 1 2231 ? 196.808 191.950 177.780 1.00 0.02  ? 2231 SER A CB    1 
ATOM   6187  O  OG    . SER A 1 2231 ? 196.707 192.030 179.192 1.00 0.08  ? 2231 SER A OG    1 
ATOM   6188  N  N     . MET A 1 2232 ? 196.037 190.946 174.925 1.00 0.04  ? 2232 MET A N     1 
ATOM   6189  C  CA    . MET A 1 2232 ? 196.223 191.020 173.455 1.00 0.04  ? 2232 MET A CA    1 
ATOM   6190  C  C     . MET A 1 2232 ? 194.854 191.172 172.777 1.00 0.05  ? 2232 MET A C     1 
ATOM   6191  O  O     . MET A 1 2232 ? 194.804 191.815 171.713 1.00 0.13  ? 2232 MET A O     1 
ATOM   6192  C  CB    . MET A 1 2232 ? 196.970 189.786 172.933 1.00 0.12  ? 2232 MET A CB    1 
ATOM   6193  C  CG    . MET A 1 2232 ? 198.421 189.708 173.364 1.00 0.11  ? 2232 MET A CG    1 
ATOM   6194  S  SD    . MET A 1 2232 ? 199.354 191.186 172.918 1.00 13.92 ? 2232 MET A SD    1 
ATOM   6195  C  CE    . MET A 1 2232 ? 201.032 190.622 173.233 1.00 6.08  ? 2232 MET A CE    1 
ATOM   6196  N  N     . ALA A 1 2233 ? 193.792 190.632 173.387 1.00 0.05  ? 2233 ALA A N     1 
ATOM   6197  C  CA    . ALA A 1 2233 ? 192.462 190.716 172.794 1.00 0.04  ? 2233 ALA A CA    1 
ATOM   6198  C  C     . ALA A 1 2233 ? 191.986 192.159 172.688 1.00 0.09  ? 2233 ALA A C     1 
ATOM   6199  O  O     . ALA A 1 2233 ? 191.419 192.555 171.664 1.00 1.04  ? 2233 ALA A O     1 
ATOM   6200  C  CB    . ALA A 1 2233 ? 191.469 189.884 173.602 1.00 0.05  ? 2233 ALA A CB    1 
ATOM   6201  N  N     . TRP A 1 2234 ? 192.202 192.961 173.729 1.00 0.04  ? 2234 TRP A N     1 
ATOM   6202  C  CA    . TRP A 1 2234 ? 191.759 194.348 173.680 1.00 0.06  ? 2234 TRP A CA    1 
ATOM   6203  C  C     . TRP A 1 2234 ? 192.804 195.285 173.094 1.00 0.23  ? 2234 TRP A C     1 
ATOM   6204  O  O     . TRP A 1 2234 ? 192.436 196.345 172.576 1.00 3.72  ? 2234 TRP A O     1 
ATOM   6205  C  CB    . TRP A 1 2234 ? 191.325 194.834 175.072 1.00 0.04  ? 2234 TRP A CB    1 
ATOM   6206  C  CG    . TRP A 1 2234 ? 192.419 195.061 176.087 1.00 0.04  ? 2234 TRP A CG    1 
ATOM   6207  C  CD1   . TRP A 1 2234 ? 192.734 194.254 177.135 1.00 0.02  ? 2234 TRP A CD1   1 
ATOM   6208  C  CD2   . TRP A 1 2234 ? 193.301 196.187 176.173 1.00 0.04  ? 2234 TRP A CD2   1 
ATOM   6209  N  NE1   . TRP A 1 2234 ? 193.763 194.791 177.858 1.00 0.02  ? 2234 TRP A NE1   1 
ATOM   6210  C  CE2   . TRP A 1 2234 ? 194.133 195.979 177.288 1.00 0.03  ? 2234 TRP A CE2   1 
ATOM   6211  C  CE3   . TRP A 1 2234 ? 193.476 197.345 175.410 1.00 0.02  ? 2234 TRP A CE3   1 
ATOM   6212  C  CZ2   . TRP A 1 2234 ? 195.124 196.882 177.658 1.00 0.04  ? 2234 TRP A CZ2   1 
ATOM   6213  C  CZ3   . TRP A 1 2234 ? 194.460 198.236 175.776 1.00 0.02  ? 2234 TRP A CZ3   1 
ATOM   6214  C  CH2   . TRP A 1 2234 ? 195.271 198.002 176.892 1.00 0.04  ? 2234 TRP A CH2   1 
ATOM   6215  N  N     . ARG A 1 2235 ? 194.089 194.931 173.160 1.00 0.11  ? 2235 ARG A N     1 
ATOM   6216  C  CA    . ARG A 1 2235 ? 195.102 195.744 172.495 1.00 0.11  ? 2235 ARG A CA    1 
ATOM   6217  C  C     . ARG A 1 2235 ? 194.998 195.622 170.980 1.00 0.28  ? 2235 ARG A C     1 
ATOM   6218  O  O     . ARG A 1 2235 ? 195.174 196.610 170.259 1.00 0.58  ? 2235 ARG A O     1 
ATOM   6219  C  CB    . ARG A 1 2235 ? 196.499 195.351 172.978 1.00 0.30  ? 2235 ARG A CB    1 
ATOM   6220  C  CG    . ARG A 1 2235 ? 196.842 195.837 174.379 1.00 0.75  ? 2235 ARG A CG    1 
ATOM   6221  C  CD    . ARG A 1 2235 ? 198.233 195.378 174.800 1.00 2.79  ? 2235 ARG A CD    1 
ATOM   6222  N  NE    . ARG A 1 2235 ? 198.726 196.072 175.987 1.00 6.27  ? 2235 ARG A NE    1 
ATOM   6223  C  CZ    . ARG A 1 2235 ? 199.024 197.364 176.042 1.00 6.85  ? 2235 ARG A CZ    1 
ATOM   6224  N  NH1   . ARG A 1 2235 ? 198.915 198.146 174.981 1.00 8.50  ? 2235 ARG A NH1   1 
ATOM   6225  N  NH2   . ARG A 1 2235 ? 199.450 197.882 177.188 1.00 2.92  ? 2235 ARG A NH2   1 
ATOM   6226  N  N     . VAL A 1 2236 ? 194.723 194.417 170.478 1.00 0.32  ? 2236 VAL A N     1 
ATOM   6227  C  CA    . VAL A 1 2236 ? 194.543 194.230 169.041 1.00 0.45  ? 2236 VAL A CA    1 
ATOM   6228  C  C     . VAL A 1 2236 ? 193.238 194.865 168.576 1.00 0.40  ? 2236 VAL A C     1 
ATOM   6229  O  O     . VAL A 1 2236 ? 193.186 195.499 167.517 1.00 0.33  ? 2236 VAL A O     1 
ATOM   6230  C  CB    . VAL A 1 2236 ? 194.612 192.734 168.686 1.00 0.29  ? 2236 VAL A CB    1 
ATOM   6231  C  CG1   . VAL A 1 2236 ? 194.045 192.475 167.306 1.00 0.58  ? 2236 VAL A CG1   1 
ATOM   6232  C  CG2   . VAL A 1 2236 ? 196.041 192.247 168.763 1.00 0.53  ? 2236 VAL A CG2   1 
ATOM   6233  N  N     . LEU A 1 2237 ? 192.168 194.708 169.360 1.00 0.48  ? 2237 LEU A N     1 
ATOM   6234  C  CA    . LEU A 1 2237 ? 190.884 195.290 168.981 1.00 0.32  ? 2237 LEU A CA    1 
ATOM   6235  C  C     . LEU A 1 2237 ? 190.967 196.808 168.914 1.00 0.42  ? 2237 LEU A C     1 
ATOM   6236  O  O     . LEU A 1 2237 ? 190.388 197.428 168.016 1.00 0.50  ? 2237 LEU A O     1 
ATOM   6237  C  CB    . LEU A 1 2237 ? 189.796 194.855 169.964 1.00 0.26  ? 2237 LEU A CB    1 
ATOM   6238  C  CG    . LEU A 1 2237 ? 188.396 195.435 169.734 1.00 0.20  ? 2237 LEU A CG    1 
ATOM   6239  C  CD1   . LEU A 1 2237 ? 187.865 195.066 168.356 1.00 0.23  ? 2237 LEU A CD1   1 
ATOM   6240  C  CD2   . LEU A 1 2237 ? 187.435 194.986 170.817 1.00 0.15  ? 2237 LEU A CD2   1 
ATOM   6241  N  N     . LEU A 1 2238 ? 191.687 197.425 169.855 1.00 0.58  ? 2238 LEU A N     1 
ATOM   6242  C  CA    . LEU A 1 2238 ? 191.819 198.877 169.858 1.00 0.24  ? 2238 LEU A CA    1 
ATOM   6243  C  C     . LEU A 1 2238 ? 192.518 199.373 168.599 1.00 0.64  ? 2238 LEU A C     1 
ATOM   6244  O  O     . LEU A 1 2238 ? 192.099 200.370 168.000 1.00 1.45  ? 2238 LEU A O     1 
ATOM   6245  C  CB    . LEU A 1 2238 ? 192.570 199.332 171.109 1.00 0.26  ? 2238 LEU A CB    1 
ATOM   6246  C  CG    . LEU A 1 2238 ? 192.588 200.832 171.416 1.00 0.32  ? 2238 LEU A CG    1 
ATOM   6247  C  CD1   . LEU A 1 2238 ? 191.176 201.372 171.580 1.00 0.18  ? 2238 LEU A CD1   1 
ATOM   6248  C  CD2   . LEU A 1 2238 ? 193.415 201.115 172.656 1.00 0.09  ? 2238 LEU A CD2   1 
ATOM   6249  N  N     . LYS A 1 2239 ? 193.588 198.692 168.181 1.00 0.71  ? 2239 LYS A N     1 
ATOM   6250  C  CA    . LYS A 1 2239 ? 194.271 199.070 166.948 1.00 0.80  ? 2239 LYS A CA    1 
ATOM   6251  C  C     . LYS A 1 2239 ? 193.402 198.807 165.725 1.00 0.84  ? 2239 LYS A C     1 
ATOM   6252  O  O     . LYS A 1 2239 ? 193.393 199.605 164.782 1.00 2.68  ? 2239 LYS A O     1 
ATOM   6253  C  CB    . LYS A 1 2239 ? 195.600 198.321 166.832 1.00 1.15  ? 2239 LYS A CB    1 
ATOM   6254  C  CG    . LYS A 1 2239 ? 196.600 198.672 167.910 1.00 4.57  ? 2239 LYS A CG    1 
ATOM   6255  C  CD    . LYS A 1 2239 ? 197.797 197.739 167.886 1.00 4.44  ? 2239 LYS A CD    1 
ATOM   6256  C  CE    . LYS A 1 2239 ? 198.888 198.225 168.825 1.00 3.45  ? 2239 LYS A CE    1 
ATOM   6257  N  NZ    . LYS A 1 2239 ? 200.039 197.289 168.873 1.00 5.59  ? 2239 LYS A NZ    1 
ATOM   6258  N  N     . ALA A 1 2240 ? 192.673 197.688 165.718 1.00 0.74  ? 2240 ALA A N     1 
ATOM   6259  C  CA    . ALA A 1 2240 ? 191.834 197.354 164.572 1.00 1.65  ? 2240 ALA A CA    1 
ATOM   6260  C  C     . ALA A 1 2240 ? 190.719 198.376 164.384 1.00 1.82  ? 2240 ALA A C     1 
ATOM   6261  O  O     . ALA A 1 2240 ? 190.405 198.759 163.251 1.00 2.83  ? 2240 ALA A O     1 
ATOM   6262  C  CB    . ALA A 1 2240 ? 191.257 195.950 164.736 1.00 1.08  ? 2240 ALA A CB    1 
ATOM   6263  N  N     . LEU A 1 2241 ? 190.108 198.822 165.482 1.00 1.03  ? 2241 LEU A N     1 
ATOM   6264  C  CA    . LEU A 1 2241 ? 189.060 199.831 165.382 1.00 1.23  ? 2241 LEU A CA    1 
ATOM   6265  C  C     . LEU A 1 2241 ? 189.610 201.166 164.901 1.00 3.25  ? 2241 LEU A C     1 
ATOM   6266  O  O     . LEU A 1 2241 ? 188.896 201.923 164.235 1.00 6.83  ? 2241 LEU A O     1 
ATOM   6267  C  CB    . LEU A 1 2241 ? 188.358 199.993 166.728 1.00 0.74  ? 2241 LEU A CB    1 
ATOM   6268  C  CG    . LEU A 1 2241 ? 187.607 198.750 167.205 1.00 0.74  ? 2241 LEU A CG    1 
ATOM   6269  C  CD1   . LEU A 1 2241 ? 187.046 198.945 168.603 1.00 0.31  ? 2241 LEU A CD1   1 
ATOM   6270  C  CD2   . LEU A 1 2241 ? 186.514 198.380 166.221 1.00 1.61  ? 2241 LEU A CD2   1 
ATOM   6271  N  N     . GLU A 1 2242 ? 190.867 201.474 165.228 1.00 2.33  ? 2242 GLU A N     1 
ATOM   6272  C  CA    . GLU A 1 2242 ? 191.485 202.690 164.711 1.00 2.72  ? 2242 GLU A CA    1 
ATOM   6273  C  C     . GLU A 1 2242 ? 191.592 202.647 163.194 1.00 3.92  ? 2242 GLU A C     1 
ATOM   6274  O  O     . GLU A 1 2242 ? 191.352 203.652 162.517 1.00 7.12  ? 2242 GLU A O     1 
ATOM   6275  C  CB    . GLU A 1 2242 ? 192.863 202.890 165.341 1.00 3.40  ? 2242 GLU A CB    1 
ATOM   6276  C  CG    . GLU A 1 2242 ? 193.578 204.148 164.880 1.00 3.06  ? 2242 GLU A CG    1 
ATOM   6277  C  CD    . GLU A 1 2242 ? 194.531 204.698 165.921 1.00 9.97  ? 2242 GLU A CD    1 
ATOM   6278  O  OE1   . GLU A 1 2242 ? 194.608 204.122 167.026 1.00 6.50  ? 2242 GLU A OE1   1 
ATOM   6279  O  OE2   . GLU A 1 2242 ? 195.203 205.712 165.634 1.00 15.04 ? 2242 GLU A OE2   1 
ATOM   6280  N  N     . ARG A 1 2243 ? 191.957 201.490 162.643 1.00 4.39  ? 2243 ARG A N     1 
ATOM   6281  C  CA    . ARG A 1 2243 ? 192.092 201.353 161.198 1.00 6.62  ? 2243 ARG A CA    1 
ATOM   6282  C  C     . ARG A 1 2243 ? 190.732 201.241 160.521 1.00 5.58  ? 2243 ARG A C     1 
ATOM   6283  O  O     . ARG A 1 2243 ? 190.526 201.798 159.438 1.00 11.87 ? 2243 ARG A O     1 
ATOM   6284  C  CB    . ARG A 1 2243 ? 192.948 200.130 160.880 1.00 6.18  ? 2243 ARG A CB    1 
ATOM   6285  C  CG    . ARG A 1 2243 ? 194.393 200.273 161.311 1.00 9.13  ? 2243 ARG A CG    1 
ATOM   6286  C  CD    . ARG A 1 2243 ? 195.190 199.032 160.975 1.00 15.54 ? 2243 ARG A CD    1 
ATOM   6287  N  NE    . ARG A 1 2243 ? 196.580 199.138 161.403 1.00 15.19 ? 2243 ARG A NE    1 
ATOM   6288  C  CZ    . ARG A 1 2243 ? 197.475 198.169 161.279 1.00 17.32 ? 2243 ARG A CZ    1 
ATOM   6289  N  NH1   . ARG A 1 2243 ? 197.169 197.016 160.711 1.00 15.71 ? 2243 ARG A NH1   1 
ATOM   6290  N  NH2   . ARG A 1 2243 ? 198.709 198.362 161.734 1.00 18.06 ? 2243 ARG A NH2   1 
ATOM   6291  N  N     . LEU A 1 2244 ? 189.797 200.528 161.150 1.00 5.98  ? 2244 LEU A N     1 
ATOM   6292  C  CA    . LEU A 1 2244 ? 188.486 200.312 160.550 1.00 5.10  ? 2244 LEU A CA    1 
ATOM   6293  C  C     . LEU A 1 2244 ? 187.656 201.590 160.543 1.00 5.80  ? 2244 LEU A C     1 
ATOM   6294  O  O     . LEU A 1 2244 ? 187.053 201.945 159.526 1.00 9.92  ? 2244 LEU A O     1 
ATOM   6295  C  CB    . LEU A 1 2244 ? 187.753 199.202 161.303 1.00 4.03  ? 2244 LEU A CB    1 
ATOM   6296  C  CG    . LEU A 1 2244 ? 186.396 198.772 160.747 1.00 6.94  ? 2244 LEU A CG    1 
ATOM   6297  C  CD1   . LEU A 1 2244 ? 186.578 197.812 159.590 1.00 8.76  ? 2244 LEU A CD1   1 
ATOM   6298  C  CD2   . LEU A 1 2244 ? 185.538 198.153 161.840 1.00 5.34  ? 2244 LEU A CD2   1 
ATOM   6299  N  N     . GLU A 1 2245 ? 187.618 202.296 161.673 1.00 5.53  ? 2245 GLU A N     1 
ATOM   6300  C  CA    . GLU A 1 2245 ? 186.717 203.424 161.856 1.00 4.32  ? 2245 GLU A CA    1 
ATOM   6301  C  C     . GLU A 1 2245 ? 187.389 204.777 161.667 1.00 6.88  ? 2245 GLU A C     1 
ATOM   6302  O  O     . GLU A 1 2245 ? 186.687 205.784 161.536 1.00 12.02 ? 2245 GLU A O     1 
ATOM   6303  C  CB    . GLU A 1 2245 ? 186.091 203.365 163.255 1.00 8.25  ? 2245 GLU A CB    1 
ATOM   6304  C  CG    . GLU A 1 2245 ? 185.153 202.190 163.465 1.00 10.42 ? 2245 GLU A CG    1 
ATOM   6305  C  CD    . GLU A 1 2245 ? 184.572 202.155 164.863 1.00 18.32 ? 2245 GLU A CD    1 
ATOM   6306  O  OE1   . GLU A 1 2245 ? 184.996 202.974 165.705 1.00 14.97 ? 2245 GLU A OE1   1 
ATOM   6307  O  OE2   . GLU A 1 2245 ? 183.691 201.307 165.121 1.00 24.07 ? 2245 GLU A OE2   1 
ATOM   6308  N  N     . GLY A 1 2246 ? 188.718 204.825 161.653 1.00 3.41  ? 2246 GLY A N     1 
ATOM   6309  C  CA    . GLY A 1 2246 ? 189.429 206.080 161.556 1.00 2.66  ? 2246 GLY A CA    1 
ATOM   6310  C  C     . GLY A 1 2246 ? 189.561 206.842 162.855 1.00 5.58  ? 2246 GLY A C     1 
ATOM   6311  O  O     . GLY A 1 2246 ? 190.152 207.930 162.857 1.00 6.50  ? 2246 GLY A O     1 
ATOM   6312  N  N     . VAL A 1 2247 ? 189.043 206.309 163.955 1.00 4.94  ? 2247 VAL A N     1 
ATOM   6313  C  CA    . VAL A 1 2247 ? 189.080 206.982 165.247 1.00 5.05  ? 2247 VAL A CA    1 
ATOM   6314  C  C     . VAL A 1 2247 ? 190.290 206.487 166.025 1.00 3.76  ? 2247 VAL A C     1 
ATOM   6315  O  O     . VAL A 1 2247 ? 190.467 205.279 166.215 1.00 5.16  ? 2247 VAL A O     1 
ATOM   6316  C  CB    . VAL A 1 2247 ? 187.780 206.737 166.029 1.00 3.09  ? 2247 VAL A CB    1 
ATOM   6317  C  CG1   . VAL A 1 2247 ? 187.844 207.393 167.397 1.00 1.74  ? 2247 VAL A CG1   1 
ATOM   6318  C  CG2   . VAL A 1 2247 ? 186.585 207.248 165.238 1.00 2.19  ? 2247 VAL A CG2   1 
ATOM   6319  N  N     . GLU A 1 2248 ? 191.126 207.420 166.473 1.00 3.62  ? 2248 GLU A N     1 
ATOM   6320  C  CA    . GLU A 1 2248 ? 192.314 207.063 167.235 1.00 3.76  ? 2248 GLU A CA    1 
ATOM   6321  C  C     . GLU A 1 2248 ? 191.922 206.435 168.567 1.00 4.10  ? 2248 GLU A C     1 
ATOM   6322  O  O     . GLU A 1 2248 ? 191.040 206.938 169.269 1.00 5.35  ? 2248 GLU A O     1 
ATOM   6323  C  CB    . GLU A 1 2248 ? 193.185 208.296 167.464 1.00 4.99  ? 2248 GLU A CB    1 
ATOM   6324  C  CG    . GLU A 1 2248 ? 194.308 208.091 168.465 1.00 7.63  ? 2248 GLU A CG    1 
ATOM   6325  C  CD    . GLU A 1 2248 ? 195.099 209.359 168.716 1.00 21.10 ? 2248 GLU A CD    1 
ATOM   6326  O  OE1   . GLU A 1 2248 ? 194.825 210.374 168.043 1.00 22.87 ? 2248 GLU A OE1   1 
ATOM   6327  O  OE2   . GLU A 1 2248 ? 195.993 209.341 169.587 1.00 23.85 ? 2248 GLU A OE2   1 
ATOM   6328  N  N     . GLY A 1 2249 ? 192.579 205.331 168.913 1.00 3.47  ? 2249 GLY A N     1 
ATOM   6329  C  CA    . GLY A 1 2249 ? 192.304 204.621 170.147 1.00 1.25  ? 2249 GLY A CA    1 
ATOM   6330  C  C     . GLY A 1 2249 ? 193.401 204.859 171.167 1.00 0.97  ? 2249 GLY A C     1 
ATOM   6331  O  O     . GLY A 1 2249 ? 194.587 204.696 170.873 1.00 3.91  ? 2249 GLY A O     1 
ATOM   6332  N  N     . VAL A 1 2250 ? 192.988 205.251 172.368 1.00 0.76  ? 2250 VAL A N     1 
ATOM   6333  C  CA    . VAL A 1 2250 ? 193.903 205.544 173.463 1.00 0.31  ? 2250 VAL A CA    1 
ATOM   6334  C  C     . VAL A 1 2250 ? 193.502 204.696 174.658 1.00 0.17  ? 2250 VAL A C     1 
ATOM   6335  O  O     . VAL A 1 2250 ? 192.334 204.697 175.062 1.00 0.24  ? 2250 VAL A O     1 
ATOM   6336  C  CB    . VAL A 1 2250 ? 193.891 207.040 173.830 1.00 0.27  ? 2250 VAL A CB    1 
ATOM   6337  C  CG1   . VAL A 1 2250 ? 194.731 207.292 175.074 1.00 0.20  ? 2250 VAL A CG1   1 
ATOM   6338  C  CG2   . VAL A 1 2250 ? 194.388 207.873 172.664 1.00 1.41  ? 2250 VAL A CG2   1 
ATOM   6339  N  N     . ALA A 1 2251 ? 194.465 203.977 175.224 1.00 0.12  ? 2251 ALA A N     1 
ATOM   6340  C  CA    . ALA A 1 2251 ? 194.238 203.144 176.395 1.00 0.03  ? 2251 ALA A CA    1 
ATOM   6341  C  C     . ALA A 1 2251 ? 195.046 203.681 177.567 1.00 0.04  ? 2251 ALA A C     1 
ATOM   6342  O  O     . ALA A 1 2251 ? 196.253 203.906 177.442 1.00 0.08  ? 2251 ALA A O     1 
ATOM   6343  C  CB    . ALA A 1 2251 ? 194.613 201.688 176.119 1.00 0.02  ? 2251 ALA A CB    1 
ATOM   6344  N  N     . HIS A 1 2252 ? 194.376 203.892 178.694 1.00 0.03  ? 2252 HIS A N     1 
ATOM   6345  C  CA    . HIS A 1 2252 ? 195.020 204.237 179.955 1.00 0.02  ? 2252 HIS A CA    1 
ATOM   6346  C  C     . HIS A 1 2252 ? 194.925 203.012 180.851 1.00 0.03  ? 2252 HIS A C     1 
ATOM   6347  O  O     . HIS A 1 2252 ? 193.841 202.678 181.340 1.00 0.06  ? 2252 HIS A O     1 
ATOM   6348  C  CB    . HIS A 1 2252 ? 194.352 205.446 180.609 1.00 0.03  ? 2252 HIS A CB    1 
ATOM   6349  C  CG    . HIS A 1 2252 ? 194.219 206.629 179.704 1.00 0.05  ? 2252 HIS A CG    1 
ATOM   6350  N  ND1   . HIS A 1 2252 ? 195.130 207.663 179.689 1.00 0.05  ? 2252 HIS A ND1   1 
ATOM   6351  C  CD2   . HIS A 1 2252 ? 193.274 206.948 178.789 1.00 0.11  ? 2252 HIS A CD2   1 
ATOM   6352  C  CE1   . HIS A 1 2252 ? 194.754 208.566 178.800 1.00 0.04  ? 2252 HIS A CE1   1 
ATOM   6353  N  NE2   . HIS A 1 2252 ? 193.631 208.156 178.241 1.00 0.07  ? 2252 HIS A NE2   1 
ATOM   6354  N  N     . ILE A 1 2253 ? 196.048 202.335 181.055 1.00 0.03  ? 2253 ILE A N     1 
ATOM   6355  C  CA    . ILE A 1 2253 ? 196.075 201.106 181.837 1.00 0.01  ? 2253 ILE A CA    1 
ATOM   6356  C  C     . ILE A 1 2253 ? 196.472 201.460 183.264 1.00 0.05  ? 2253 ILE A C     1 
ATOM   6357  O  O     . ILE A 1 2253 ? 197.514 202.077 183.493 1.00 0.03  ? 2253 ILE A O     1 
ATOM   6358  C  CB    . ILE A 1 2253 ? 197.039 200.073 181.234 1.00 0.06  ? 2253 ILE A CB    1 
ATOM   6359  C  CG1   . ILE A 1 2253 ? 196.589 199.654 179.833 1.00 0.04  ? 2253 ILE A CG1   1 
ATOM   6360  C  CG2   . ILE A 1 2253 ? 197.107 198.847 182.117 1.00 0.04  ? 2253 ILE A CG2   1 
ATOM   6361  C  CD1   . ILE A 1 2253 ? 197.119 200.521 178.718 1.00 0.03  ? 2253 ILE A CD1   1 
ATOM   6362  N  N     . ILE A 1 2254 ? 195.637 201.071 184.223 1.00 0.07  ? 2254 ILE A N     1 
ATOM   6363  C  CA    . ILE A 1 2254 ? 195.832 201.396 185.629 1.00 0.07  ? 2254 ILE A CA    1 
ATOM   6364  C  C     . ILE A 1 2254 ? 195.878 200.101 186.423 1.00 0.07  ? 2254 ILE A C     1 
ATOM   6365  O  O     . ILE A 1 2254 ? 195.037 199.218 186.226 1.00 0.15  ? 2254 ILE A O     1 
ATOM   6366  C  CB    . ILE A 1 2254 ? 194.717 202.318 186.159 1.00 0.05  ? 2254 ILE A CB    1 
ATOM   6367  C  CG1   . ILE A 1 2254 ? 194.732 203.657 185.423 1.00 0.02  ? 2254 ILE A CG1   1 
ATOM   6368  C  CG2   . ILE A 1 2254 ? 194.853 202.521 187.662 1.00 0.07  ? 2254 ILE A CG2   1 
ATOM   6369  C  CD1   . ILE A 1 2254 ? 193.627 204.594 185.844 1.00 0.01  ? 2254 ILE A CD1   1 
ATOM   6370  N  N     . ASP A 1 2255 ? 196.867 199.981 187.310 1.00 0.13  ? 2255 ASP A N     1 
ATOM   6371  C  CA    . ASP A 1 2255 ? 196.848 198.923 188.310 1.00 0.15  ? 2255 ASP A CA    1 
ATOM   6372  C  C     . ASP A 1 2255 ? 196.223 199.496 189.574 1.00 0.17  ? 2255 ASP A C     1 
ATOM   6373  O  O     . ASP A 1 2255 ? 196.906 200.201 190.332 1.00 0.19  ? 2255 ASP A O     1 
ATOM   6374  C  CB    . ASP A 1 2255 ? 198.256 198.394 188.590 1.00 0.13  ? 2255 ASP A CB    1 
ATOM   6375  C  CG    . ASP A 1 2255 ? 198.243 197.023 189.246 1.00 1.35  ? 2255 ASP A CG    1 
ATOM   6376  O  OD1   . ASP A 1 2255 ? 197.343 196.758 190.068 1.00 0.50  ? 2255 ASP A OD1   1 
ATOM   6377  O  OD2   . ASP A 1 2255 ? 199.137 196.208 188.938 1.00 6.11  ? 2255 ASP A OD2   1 
ATOM   6378  N  N     . PRO A 1 2256 ? 194.938 199.247 189.834 1.00 0.20  ? 2256 PRO A N     1 
ATOM   6379  C  CA    . PRO A 1 2256 ? 194.281 199.894 190.979 1.00 0.31  ? 2256 PRO A CA    1 
ATOM   6380  C  C     . PRO A 1 2256 ? 194.856 199.505 192.330 1.00 0.36  ? 2256 PRO A C     1 
ATOM   6381  O  O     . PRO A 1 2256 ? 194.832 200.326 193.253 1.00 1.42  ? 2256 PRO A O     1 
ATOM   6382  C  CB    . PRO A 1 2256 ? 192.822 199.445 190.832 1.00 0.08  ? 2256 PRO A CB    1 
ATOM   6383  C  CG    . PRO A 1 2256 ? 192.923 198.146 190.118 1.00 0.07  ? 2256 PRO A CG    1 
ATOM   6384  C  CD    . PRO A 1 2256 ? 194.047 198.297 189.151 1.00 0.11  ? 2256 PRO A CD    1 
ATOM   6385  N  N     . LYS A 1 2257 ? 195.359 198.284 192.484 1.00 0.29  ? 2257 LYS A N     1 
ATOM   6386  C  CA    . LYS A 1 2257 ? 195.866 197.814 193.766 1.00 0.32  ? 2257 LYS A CA    1 
ATOM   6387  C  C     . LYS A 1 2257 ? 197.366 198.013 193.929 1.00 0.35  ? 2257 LYS A C     1 
ATOM   6388  O  O     . LYS A 1 2257 ? 197.910 197.672 194.982 1.00 0.61  ? 2257 LYS A O     1 
ATOM   6389  C  CB    . LYS A 1 2257 ? 195.514 196.337 193.963 1.00 0.62  ? 2257 LYS A CB    1 
ATOM   6390  C  CG    . LYS A 1 2257 ? 194.026 196.071 194.112 1.00 0.36  ? 2257 LYS A CG    1 
ATOM   6391  C  CD    . LYS A 1 2257 ? 193.509 196.536 195.459 1.00 0.36  ? 2257 LYS A CD    1 
ATOM   6392  C  CE    . LYS A 1 2257 ? 194.029 195.668 196.592 1.00 2.08  ? 2257 LYS A CE    1 
ATOM   6393  N  NZ    . LYS A 1 2257 ? 193.152 194.496 196.856 1.00 0.55  ? 2257 LYS A NZ    1 
ATOM   6394  N  N     . ALA A 1 2258 ? 198.048 198.548 192.917 1.00 0.28  ? 2258 ALA A N     1 
ATOM   6395  C  CA    . ALA A 1 2258 ? 199.454 198.899 193.057 1.00 0.18  ? 2258 ALA A CA    1 
ATOM   6396  C  C     . ALA A 1 2258 ? 199.652 200.211 193.800 1.00 0.37  ? 2258 ALA A C     1 
ATOM   6397  O  O     . ALA A 1 2258 ? 200.786 200.538 194.162 1.00 0.65  ? 2258 ALA A O     1 
ATOM   6398  C  CB    . ALA A 1 2258 ? 200.120 198.980 191.682 1.00 0.08  ? 2258 ALA A CB    1 
ATOM   6399  N  N     . ILE A 1 2259 ? 198.576 200.960 194.029 1.00 0.66  ? 2259 ILE A N     1 
ATOM   6400  C  CA    . ILE A 1 2259 ? 198.610 202.236 194.724 1.00 0.61  ? 2259 ILE A CA    1 
ATOM   6401  C  C     . ILE A 1 2259 ? 197.521 202.225 195.787 1.00 0.56  ? 2259 ILE A C     1 
ATOM   6402  O  O     . ILE A 1 2259 ? 196.626 201.378 195.784 1.00 1.15  ? 2259 ILE A O     1 
ATOM   6403  C  CB    . ILE A 1 2259 ? 198.420 203.427 193.762 1.00 0.35  ? 2259 ILE A CB    1 
ATOM   6404  C  CG1   . ILE A 1 2259 ? 197.031 203.367 193.120 1.00 0.15  ? 2259 ILE A CG1   1 
ATOM   6405  C  CG2   . ILE A 1 2259 ? 199.505 203.435 192.699 1.00 0.07  ? 2259 ILE A CG2   1 
ATOM   6406  C  CD1   . ILE A 1 2259 ? 196.761 204.464 192.130 1.00 0.09  ? 2259 ILE A CD1   1 
ATOM   6407  N  N     . SER A 1 2260 ? 197.608 203.177 196.709 1.00 0.44  ? 2260 SER A N     1 
ATOM   6408  C  CA    . SER A 1 2260 ? 196.566 203.318 197.713 1.00 0.83  ? 2260 SER A CA    1 
ATOM   6409  C  C     . SER A 1 2260 ? 195.275 203.818 197.069 1.00 0.65  ? 2260 SER A C     1 
ATOM   6410  O  O     . SER A 1 2260 ? 195.280 204.441 196.004 1.00 0.47  ? 2260 SER A O     1 
ATOM   6411  C  CB    . SER A 1 2260 ? 197.009 204.272 198.821 1.00 1.54  ? 2260 SER A CB    1 
ATOM   6412  O  OG    . SER A 1 2260 ? 197.156 205.593 198.337 1.00 1.54  ? 2260 SER A OG    1 
ATOM   6413  N  N     . LYS A 1 2261 ? 194.153 203.519 197.727 1.00 0.33  ? 2261 LYS A N     1 
ATOM   6414  C  CA    . LYS A 1 2261 ? 192.869 204.008 197.239 1.00 0.62  ? 2261 LYS A CA    1 
ATOM   6415  C  C     . LYS A 1 2261 ? 192.814 205.529 197.259 1.00 0.60  ? 2261 LYS A C     1 
ATOM   6416  O  O     . LYS A 1 2261 ? 192.121 206.139 196.438 1.00 0.36  ? 2261 LYS A O     1 
ATOM   6417  C  CB    . LYS A 1 2261 ? 191.730 203.416 198.067 1.00 1.32  ? 2261 LYS A CB    1 
ATOM   6418  C  CG    . LYS A 1 2261 ? 190.347 203.788 197.573 1.00 0.71  ? 2261 LYS A CG    1 
ATOM   6419  C  CD    . LYS A 1 2261 ? 189.278 203.324 198.533 1.00 2.98  ? 2261 LYS A CD    1 
ATOM   6420  C  CE    . LYS A 1 2261 ? 187.905 203.781 198.087 1.00 2.60  ? 2261 LYS A CE    1 
ATOM   6421  N  NZ    . LYS A 1 2261 ? 186.858 203.354 199.050 1.00 4.46  ? 2261 LYS A NZ    1 
ATOM   6422  N  N     . ASP A 1 2262 ? 193.546 206.156 198.182 1.00 1.37  ? 2262 ASP A N     1 
ATOM   6423  C  CA    . ASP A 1 2262 ? 193.668 207.608 198.179 1.00 0.98  ? 2262 ASP A CA    1 
ATOM   6424  C  C     . ASP A 1 2262 ? 194.333 208.100 196.899 1.00 1.19  ? 2262 ASP A C     1 
ATOM   6425  O  O     . ASP A 1 2262 ? 193.951 209.140 196.351 1.00 1.33  ? 2262 ASP A O     1 
ATOM   6426  C  CB    . ASP A 1 2262 ? 194.461 208.067 199.402 1.00 5.15  ? 2262 ASP A CB    1 
ATOM   6427  C  CG    . ASP A 1 2262 ? 193.707 207.857 200.698 1.00 11.26 ? 2262 ASP A CG    1 
ATOM   6428  O  OD1   . ASP A 1 2262 ? 192.460 207.895 200.680 1.00 15.74 ? 2262 ASP A OD1   1 
ATOM   6429  O  OD2   . ASP A 1 2262 ? 194.365 207.659 201.741 1.00 13.74 ? 2262 ASP A OD2   1 
ATOM   6430  N  N     . HIS A 1 2263 ? 195.337 207.371 196.413 1.00 1.28  ? 2263 HIS A N     1 
ATOM   6431  C  CA    . HIS A 1 2263 ? 196.022 207.758 195.188 1.00 0.55  ? 2263 HIS A CA    1 
ATOM   6432  C  C     . HIS A 1 2263 ? 195.253 207.368 193.933 1.00 0.17  ? 2263 HIS A C     1 
ATOM   6433  O  O     . HIS A 1 2263 ? 195.566 207.870 192.850 1.00 0.13  ? 2263 HIS A O     1 
ATOM   6434  C  CB    . HIS A 1 2263 ? 197.421 207.138 195.155 1.00 0.40  ? 2263 HIS A CB    1 
ATOM   6435  C  CG    . HIS A 1 2263 ? 198.399 207.813 196.064 1.00 0.89  ? 2263 HIS A CG    1 
ATOM   6436  N  ND1   . HIS A 1 2263 ? 199.463 207.151 196.636 1.00 3.07  ? 2263 HIS A ND1   1 
ATOM   6437  C  CD2   . HIS A 1 2263 ? 198.473 209.092 196.500 1.00 1.74  ? 2263 HIS A CD2   1 
ATOM   6438  C  CE1   . HIS A 1 2263 ? 200.151 207.993 197.385 1.00 2.37  ? 2263 HIS A CE1   1 
ATOM   6439  N  NE2   . HIS A 1 2263 ? 199.571 209.177 197.320 1.00 4.37  ? 2263 HIS A NE2   1 
ATOM   6440  N  N     . LEU A 1 2264 ? 194.255 206.493 194.053 1.00 0.21  ? 2264 LEU A N     1 
ATOM   6441  C  CA    . LEU A 1 2264 ? 193.465 206.095 192.892 1.00 0.09  ? 2264 LEU A CA    1 
ATOM   6442  C  C     . LEU A 1 2264 ? 192.369 207.109 192.587 1.00 0.03  ? 2264 LEU A C     1 
ATOM   6443  O  O     . LEU A 1 2264 ? 192.196 207.520 191.436 1.00 0.05  ? 2264 LEU A O     1 
ATOM   6444  C  CB    . LEU A 1 2264 ? 192.866 204.705 193.120 1.00 0.09  ? 2264 LEU A CB    1 
ATOM   6445  C  CG    . LEU A 1 2264 ? 191.992 204.124 192.006 1.00 0.03  ? 2264 LEU A CG    1 
ATOM   6446  C  CD1   . LEU A 1 2264 ? 192.781 203.976 190.712 1.00 0.04  ? 2264 LEU A CD1   1 
ATOM   6447  C  CD2   . LEU A 1 2264 ? 191.411 202.788 192.435 1.00 0.04  ? 2264 LEU A CD2   1 
ATOM   6448  N  N     . TYR A 1 2265 ? 191.628 207.533 193.607 1.00 0.04  ? 2265 TYR A N     1 
ATOM   6449  C  CA    . TYR A 1 2265 ? 190.496 208.428 193.416 1.00 0.11  ? 2265 TYR A CA    1 
ATOM   6450  C  C     . TYR A 1 2265 ? 190.747 209.853 193.876 1.00 0.09  ? 2265 TYR A C     1 
ATOM   6451  O  O     . TYR A 1 2265 ? 190.118 210.773 193.353 1.00 0.08  ? 2265 TYR A O     1 
ATOM   6452  C  CB    . TYR A 1 2265 ? 189.263 207.886 194.144 1.00 0.04  ? 2265 TYR A CB    1 
ATOM   6453  C  CG    . TYR A 1 2265 ? 188.764 206.578 193.587 1.00 0.02  ? 2265 TYR A CG    1 
ATOM   6454  C  CD1   . TYR A 1 2265 ? 188.222 206.510 192.312 1.00 0.05  ? 2265 TYR A CD1   1 
ATOM   6455  C  CD2   . TYR A 1 2265 ? 188.834 205.411 194.335 1.00 0.04  ? 2265 TYR A CD2   1 
ATOM   6456  C  CE1   . TYR A 1 2265 ? 187.761 205.319 191.799 1.00 0.09  ? 2265 TYR A CE1   1 
ATOM   6457  C  CE2   . TYR A 1 2265 ? 188.377 204.216 193.830 1.00 0.08  ? 2265 TYR A CE2   1 
ATOM   6458  C  CZ    . TYR A 1 2265 ? 187.841 204.175 192.560 1.00 0.09  ? 2265 TYR A CZ    1 
ATOM   6459  O  OH    . TYR A 1 2265 ? 187.384 202.986 192.050 1.00 0.18  ? 2265 TYR A OH    1 
ATOM   6460  N  N     . GLY A 1 2266 ? 191.636 210.060 194.834 1.00 0.15  ? 2266 GLY A N     1 
ATOM   6461  C  CA    . GLY A 1 2266 ? 191.936 211.379 195.344 1.00 0.21  ? 2266 GLY A CA    1 
ATOM   6462  C  C     . GLY A 1 2266 ? 191.613 211.503 196.819 1.00 0.30  ? 2266 GLY A C     1 
ATOM   6463  O  O     . GLY A 1 2266 ? 191.033 210.614 197.441 1.00 0.81  ? 2266 GLY A O     1 
ATOM   6464  N  N     . THR A 1 2267 ? 192.012 212.642 197.376 1.00 0.53  ? 2267 THR A N     1 
ATOM   6465  C  CA    . THR A 1 2267 ? 191.824 212.926 198.790 1.00 0.95  ? 2267 THR A CA    1 
ATOM   6466  C  C     . THR A 1 2267 ? 191.237 214.316 198.955 1.00 0.84  ? 2267 THR A C     1 
ATOM   6467  O  O     . THR A 1 2267 ? 191.485 215.215 198.148 1.00 0.50  ? 2267 THR A O     1 
ATOM   6468  C  CB    . THR A 1 2267 ? 193.135 212.851 199.587 1.00 0.89  ? 2267 THR A CB    1 
ATOM   6469  O  OG1   . THR A 1 2267 ? 194.075 213.794 199.057 1.00 3.36  ? 2267 THR A OG1   1 
ATOM   6470  C  CG2   . THR A 1 2267 ? 193.727 211.465 199.524 1.00 1.16  ? 2267 THR A CG2   1 
ATOM   6471  N  N     . LEU A 1 2268 ? 190.458 214.478 200.015 1.00 1.28  ? 2268 LEU A N     1 
ATOM   6472  C  CA    . LEU A 1 2268 ? 189.971 215.777 200.453 1.00 2.88  ? 2268 LEU A CA    1 
ATOM   6473  C  C     . LEU A 1 2268 ? 190.798 216.188 201.665 1.00 3.37  ? 2268 LEU A C     1 
ATOM   6474  O  O     . LEU A 1 2268 ? 190.898 215.428 202.633 1.00 5.11  ? 2268 LEU A O     1 
ATOM   6475  C  CB    . LEU A 1 2268 ? 188.482 215.710 200.787 1.00 1.78  ? 2268 LEU A CB    1 
ATOM   6476  C  CG    . LEU A 1 2268 ? 187.680 217.008 200.793 1.00 3.22  ? 2268 LEU A CG    1 
ATOM   6477  C  CD1   . LEU A 1 2268 ? 187.982 217.832 199.557 1.00 2.67  ? 2268 LEU A CD1   1 
ATOM   6478  C  CD2   . LEU A 1 2268 ? 186.199 216.683 200.865 1.00 3.29  ? 2268 LEU A CD2   1 
ATOM   6479  N  N     . ASP A 1 2269 ? 191.401 217.369 201.600 1.00 6.89  ? 2269 ASP A N     1 
ATOM   6480  C  CA    . ASP A 1 2269 ? 192.301 217.813 202.653 1.00 9.55  ? 2269 ASP A CA    1 
ATOM   6481  C  C     . ASP A 1 2269 ? 191.534 217.964 203.966 1.00 10.89 ? 2269 ASP A C     1 
ATOM   6482  O  O     . ASP A 1 2269 ? 190.475 218.610 203.988 1.00 14.07 ? 2269 ASP A O     1 
ATOM   6483  C  CB    . ASP A 1 2269 ? 192.967 219.133 202.270 1.00 10.28 ? 2269 ASP A CB    1 
ATOM   6484  C  CG    . ASP A 1 2269 ? 194.013 219.583 203.280 1.00 17.95 ? 2269 ASP A CG    1 
ATOM   6485  O  OD1   . ASP A 1 2269 ? 193.664 219.835 204.453 1.00 20.87 ? 2269 ASP A OD1   1 
ATOM   6486  O  OD2   . ASP A 1 2269 ? 195.197 219.682 202.898 1.00 20.12 ? 2269 ASP A OD2   1 
ATOM   6487  N  N     . PRO A 1 2270 ? 192.023 217.386 205.063 1.00 9.63  ? 2270 PRO A N     1 
ATOM   6488  C  CA    . PRO A 1 2270 ? 191.289 217.476 206.337 1.00 11.30 ? 2270 PRO A CA    1 
ATOM   6489  C  C     . PRO A 1 2270 ? 191.067 218.895 206.831 1.00 17.32 ? 2270 PRO A C     1 
ATOM   6490  O  O     . PRO A 1 2270 ? 190.043 219.160 207.476 1.00 20.01 ? 2270 PRO A O     1 
ATOM   6491  C  CB    . PRO A 1 2270 ? 192.180 216.681 207.302 1.00 14.74 ? 2270 PRO A CB    1 
ATOM   6492  C  CG    . PRO A 1 2270 ? 192.950 215.750 206.426 1.00 11.63 ? 2270 PRO A CG    1 
ATOM   6493  C  CD    . PRO A 1 2270 ? 193.200 216.509 205.159 1.00 10.19 ? 2270 PRO A CD    1 
ATOM   6494  N  N     . ASN A 1 2271 ? 191.982 219.822 206.545 1.00 14.30 ? 2271 ASN A N     1 
ATOM   6495  C  CA    . ASN A 1 2271 ? 191.920 221.167 207.100 1.00 15.08 ? 2271 ASN A CA    1 
ATOM   6496  C  C     . ASN A 1 2271 ? 191.553 222.214 206.057 1.00 15.35 ? 2271 ASN A C     1 
ATOM   6497  O  O     . ASN A 1 2271 ? 190.570 222.939 206.231 1.00 20.30 ? 2271 ASN A O     1 
ATOM   6498  C  CB    . ASN A 1 2271 ? 193.260 221.517 207.760 1.00 18.90 ? 2271 ASN A CB    1 
ATOM   6499  C  CG    . ASN A 1 2271 ? 193.807 220.382 208.600 1.00 20.87 ? 2271 ASN A CG    1 
ATOM   6500  O  OD1   . ASN A 1 2271 ? 193.166 219.936 209.553 1.00 27.50 ? 2271 ASN A OD1   1 
ATOM   6501  N  ND2   . ASN A 1 2271 ? 194.994 219.907 208.251 1.00 16.21 ? 2271 ASN A ND2   1 
ATOM   6502  N  N     . THR A 1 2272 ? 192.314 222.312 204.964 1.00 12.52 ? 2272 THR A N     1 
ATOM   6503  C  CA    . THR A 1 2272 ? 192.002 223.307 203.944 1.00 10.79 ? 2272 THR A CA    1 
ATOM   6504  C  C     . THR A 1 2272 ? 190.810 222.897 203.091 1.00 8.23  ? 2272 THR A C     1 
ATOM   6505  O  O     . THR A 1 2272 ? 190.280 223.731 202.351 1.00 12.41 ? 2272 THR A O     1 
ATOM   6506  C  CB    . THR A 1 2272 ? 193.216 223.559 203.047 1.00 16.85 ? 2272 THR A CB    1 
ATOM   6507  O  OG1   . THR A 1 2272 ? 193.574 222.354 202.362 1.00 20.55 ? 2272 THR A OG1   1 
ATOM   6508  C  CG2   . THR A 1 2272 ? 194.402 224.023 203.878 1.00 20.17 ? 2272 THR A CG2   1 
ATOM   6509  N  N     . ARG A 1 2273 ? 190.382 221.636 203.185 1.00 11.14 ? 2273 ARG A N     1 
ATOM   6510  C  CA    . ARG A 1 2273 ? 189.264 221.097 202.406 1.00 9.47  ? 2273 ARG A CA    1 
ATOM   6511  C  C     . ARG A 1 2273 ? 189.511 221.220 200.904 1.00 11.07 ? 2273 ARG A C     1 
ATOM   6512  O  O     . ARG A 1 2273 ? 188.574 221.357 200.117 1.00 11.71 ? 2273 ARG A O     1 
ATOM   6513  C  CB    . ARG A 1 2273 ? 187.936 221.757 202.790 1.00 10.71 ? 2273 ARG A CB    1 
ATOM   6514  C  CG    . ARG A 1 2273 ? 187.767 221.987 204.286 1.00 12.43 ? 2273 ARG A CG    1 
ATOM   6515  C  CD    . ARG A 1 2273 ? 187.763 220.685 205.067 1.00 10.91 ? 2273 ARG A CD    1 
ATOM   6516  N  NE    . ARG A 1 2273 ? 186.806 219.719 204.546 1.00 9.57  ? 2273 ARG A NE    1 
ATOM   6517  C  CZ    . ARG A 1 2273 ? 186.854 218.416 204.787 1.00 8.03  ? 2273 ARG A CZ    1 
ATOM   6518  N  NH1   . ARG A 1 2273 ? 187.809 217.887 205.534 1.00 9.25  ? 2273 ARG A NH1   1 
ATOM   6519  N  NH2   . ARG A 1 2273 ? 185.922 217.624 204.265 1.00 5.73  ? 2273 ARG A NH2   1 
ATOM   6520  N  N     . GLU A 1 2274 ? 190.778 221.171 200.504 1.00 11.61 ? 2274 GLU A N     1 
ATOM   6521  C  CA    . GLU A 1 2274 ? 191.154 221.211 199.100 1.00 9.80  ? 2274 GLU A CA    1 
ATOM   6522  C  C     . GLU A 1 2274 ? 191.143 219.801 198.527 1.00 7.42  ? 2274 GLU A C     1 
ATOM   6523  O  O     . GLU A 1 2274 ? 191.587 218.851 199.177 1.00 6.47  ? 2274 GLU A O     1 
ATOM   6524  C  CB    . GLU A 1 2274 ? 192.540 221.836 198.936 1.00 11.19 ? 2274 GLU A CB    1 
ATOM   6525  C  CG    . GLU A 1 2274 ? 193.010 221.964 197.498 1.00 12.76 ? 2274 GLU A CG    1 
ATOM   6526  C  CD    . GLU A 1 2274 ? 192.162 222.922 196.684 1.00 21.38 ? 2274 GLU A CD    1 
ATOM   6527  O  OE1   . GLU A 1 2274 ? 191.550 223.833 197.281 1.00 27.20 ? 2274 GLU A OE1   1 
ATOM   6528  O  OE2   . GLU A 1 2274 ? 192.110 222.764 195.447 1.00 21.89 ? 2274 GLU A OE2   1 
ATOM   6529  N  N     . TRP A 1 2275 ? 190.630 219.667 197.308 1.00 4.40  ? 2275 TRP A N     1 
ATOM   6530  C  CA    . TRP A 1 2275 ? 190.540 218.367 196.662 1.00 2.13  ? 2275 TRP A CA    1 
ATOM   6531  C  C     . TRP A 1 2275 ? 191.727 218.148 195.735 1.00 2.66  ? 2275 TRP A C     1 
ATOM   6532  O  O     . TRP A 1 2275 ? 192.033 218.995 194.891 1.00 6.86  ? 2275 TRP A O     1 
ATOM   6533  C  CB    . TRP A 1 2275 ? 189.237 218.229 195.877 1.00 1.50  ? 2275 TRP A CB    1 
ATOM   6534  C  CG    . TRP A 1 2275 ? 189.196 216.966 195.083 1.00 0.90  ? 2275 TRP A CG    1 
ATOM   6535  C  CD1   . TRP A 1 2275 ? 189.404 216.831 193.745 1.00 0.41  ? 2275 TRP A CD1   1 
ATOM   6536  C  CD2   . TRP A 1 2275 ? 188.973 215.646 195.590 1.00 0.39  ? 2275 TRP A CD2   1 
ATOM   6537  N  NE1   . TRP A 1 2275 ? 189.307 215.511 193.383 1.00 0.32  ? 2275 TRP A NE1   1 
ATOM   6538  C  CE2   . TRP A 1 2275 ? 189.044 214.762 194.497 1.00 0.23  ? 2275 TRP A CE2   1 
ATOM   6539  C  CE3   . TRP A 1 2275 ? 188.716 215.126 196.862 1.00 0.45  ? 2275 TRP A CE3   1 
ATOM   6540  C  CZ2   . TRP A 1 2275 ? 188.862 213.390 194.636 1.00 0.17  ? 2275 TRP A CZ2   1 
ATOM   6541  C  CZ3   . TRP A 1 2275 ? 188.536 213.762 196.997 1.00 0.71  ? 2275 TRP A CZ3   1 
ATOM   6542  C  CH2   . TRP A 1 2275 ? 188.609 212.910 195.890 1.00 0.40  ? 2275 TRP A CH2   1 
ATOM   6543  N  N     . THR A 1 2276 ? 192.389 217.009 195.899 1.00 0.80  ? 2276 THR A N     1 
ATOM   6544  C  CA    . THR A 1 2276 ? 193.448 216.566 195.004 1.00 0.93  ? 2276 THR A CA    1 
ATOM   6545  C  C     . THR A 1 2276 ? 192.949 215.353 194.234 1.00 0.53  ? 2276 THR A C     1 
ATOM   6546  O  O     . THR A 1 2276 ? 192.431 214.407 194.835 1.00 0.46  ? 2276 THR A O     1 
ATOM   6547  C  CB    . THR A 1 2276 ? 194.723 216.217 195.776 1.00 1.11  ? 2276 THR A CB    1 
ATOM   6548  O  OG1   . THR A 1 2276 ? 195.237 217.391 196.415 1.00 6.66  ? 2276 THR A OG1   1 
ATOM   6549  C  CG2   . THR A 1 2276 ? 195.778 215.656 194.837 1.00 0.48  ? 2276 THR A CG2   1 
ATOM   6550  N  N     . ASP A 1 2277 ? 193.089 215.388 192.913 1.00 0.39  ? 2277 ASP A N     1 
ATOM   6551  C  CA    . ASP A 1 2277 ? 192.636 214.276 192.089 1.00 0.20  ? 2277 ASP A CA    1 
ATOM   6552  C  C     . ASP A 1 2277 ? 193.543 213.066 192.262 1.00 0.43  ? 2277 ASP A C     1 
ATOM   6553  O  O     . ASP A 1 2277 ? 194.763 213.192 192.393 1.00 0.20  ? 2277 ASP A O     1 
ATOM   6554  C  CB    . ASP A 1 2277 ? 192.595 214.681 190.616 1.00 0.15  ? 2277 ASP A CB    1 
ATOM   6555  C  CG    . ASP A 1 2277 ? 191.264 215.270 190.211 1.00 0.35  ? 2277 ASP A CG    1 
ATOM   6556  O  OD1   . ASP A 1 2277 ? 190.356 215.339 191.063 1.00 6.03  ? 2277 ASP A OD1   1 
ATOM   6557  O  OD2   . ASP A 1 2277 ? 191.123 215.663 189.037 1.00 0.78  ? 2277 ASP A OD2   1 
ATOM   6558  N  N     . GLY A 1 2278 ? 192.933 211.885 192.264 1.00 2.24  ? 2278 GLY A N     1 
ATOM   6559  C  CA    . GLY A 1 2278 ? 193.667 210.643 192.186 1.00 0.06  ? 2278 GLY A CA    1 
ATOM   6560  C  C     . GLY A 1 2278 ? 193.990 210.292 190.750 1.00 0.03  ? 2278 GLY A C     1 
ATOM   6561  O  O     . GLY A 1 2278 ? 193.764 211.062 189.818 1.00 0.04  ? 2278 GLY A O     1 
ATOM   6562  N  N     . LEU A 1 2279 ? 194.529 209.086 190.574 1.00 0.04  ? 2279 LEU A N     1 
ATOM   6563  C  CA    . LEU A 1 2279 ? 194.967 208.658 189.248 1.00 0.03  ? 2279 LEU A CA    1 
ATOM   6564  C  C     . LEU A 1 2279 ? 193.789 208.505 188.293 1.00 0.01  ? 2279 LEU A C     1 
ATOM   6565  O  O     . LEU A 1 2279 ? 193.807 209.046 187.183 1.00 0.03  ? 2279 LEU A O     1 
ATOM   6566  C  CB    . LEU A 1 2279 ? 195.753 207.353 189.358 1.00 0.04  ? 2279 LEU A CB    1 
ATOM   6567  C  CG    . LEU A 1 2279 ? 196.200 206.698 188.051 1.00 0.02  ? 2279 LEU A CG    1 
ATOM   6568  C  CD1   . LEU A 1 2279 ? 196.988 207.672 187.193 1.00 0.03  ? 2279 LEU A CD1   1 
ATOM   6569  C  CD2   . LEU A 1 2279 ? 197.019 205.461 188.351 1.00 0.04  ? 2279 LEU A CD2   1 
ATOM   6570  N  N     . PHE A 1 2280 ? 192.751 207.776 188.707 1.00 0.02  ? 2280 PHE A N     1 
ATOM   6571  C  CA    . PHE A 1 2280 ? 191.603 207.577 187.826 1.00 0.05  ? 2280 PHE A CA    1 
ATOM   6572  C  C     . PHE A 1 2280 ? 190.823 208.870 187.629 1.00 0.15  ? 2280 PHE A C     1 
ATOM   6573  O  O     . PHE A 1 2280 ? 190.371 209.164 186.518 1.00 0.05  ? 2280 PHE A O     1 
ATOM   6574  C  CB    . PHE A 1 2280 ? 190.693 206.481 188.378 1.00 0.02  ? 2280 PHE A CB    1 
ATOM   6575  C  CG    . PHE A 1 2280 ? 189.372 206.385 187.673 1.00 0.05  ? 2280 PHE A CG    1 
ATOM   6576  C  CD1   . PHE A 1 2280 ? 189.290 205.845 186.401 1.00 0.02  ? 2280 PHE A CD1   1 
ATOM   6577  C  CD2   . PHE A 1 2280 ? 188.214 206.841 188.278 1.00 0.01  ? 2280 PHE A CD2   1 
ATOM   6578  C  CE1   . PHE A 1 2280 ? 188.078 205.756 185.748 1.00 0.02  ? 2280 PHE A CE1   1 
ATOM   6579  C  CE2   . PHE A 1 2280 ? 187.000 206.756 187.629 1.00 0.04  ? 2280 PHE A CE2   1 
ATOM   6580  C  CZ    . PHE A 1 2280 ? 186.931 206.212 186.363 1.00 0.26  ? 2280 PHE A CZ    1 
ATOM   6581  N  N     . THR A 1 2281 ? 190.653 209.652 188.697 1.00 0.05  ? 2281 THR A N     1 
ATOM   6582  C  CA    . THR A 1 2281 ? 189.915 210.906 188.586 1.00 0.05  ? 2281 THR A CA    1 
ATOM   6583  C  C     . THR A 1 2281 ? 190.620 211.881 187.655 1.00 0.04  ? 2281 THR A C     1 
ATOM   6584  O  O     . THR A 1 2281 ? 189.971 212.587 186.878 1.00 0.05  ? 2281 THR A O     1 
ATOM   6585  C  CB    . THR A 1 2281 ? 189.724 211.527 189.971 1.00 0.10  ? 2281 THR A CB    1 
ATOM   6586  O  OG1   . THR A 1 2281 ? 189.318 210.512 190.897 1.00 0.14  ? 2281 THR A OG1   1 
ATOM   6587  C  CG2   . THR A 1 2281 ? 188.671 212.616 189.927 1.00 0.06  ? 2281 THR A CG2   1 
ATOM   6588  N  N     . HIS A 1 2282 ? 191.953 211.932 187.721 1.00 0.05  ? 2282 HIS A N     1 
ATOM   6589  C  CA    . HIS A 1 2282 ? 192.708 212.822 186.846 1.00 0.05  ? 2282 HIS A CA    1 
ATOM   6590  C  C     . HIS A 1 2282 ? 192.558 212.421 185.383 1.00 0.04  ? 2282 HIS A C     1 
ATOM   6591  O  O     . HIS A 1 2282 ? 192.391 213.281 184.511 1.00 0.09  ? 2282 HIS A O     1 
ATOM   6592  C  CB    . HIS A 1 2282 ? 194.179 212.829 187.260 1.00 0.08  ? 2282 HIS A CB    1 
ATOM   6593  C  CG    . HIS A 1 2282 ? 195.104 213.383 186.222 1.00 0.24  ? 2282 HIS A CG    1 
ATOM   6594  N  ND1   . HIS A 1 2282 ? 195.776 212.584 185.322 1.00 0.41  ? 2282 HIS A ND1   1 
ATOM   6595  C  CD2   . HIS A 1 2282 ? 195.473 214.655 185.945 1.00 0.16  ? 2282 HIS A CD2   1 
ATOM   6596  C  CE1   . HIS A 1 2282 ? 196.516 213.342 184.533 1.00 2.18  ? 2282 HIS A CE1   1 
ATOM   6597  N  NE2   . HIS A 1 2282 ? 196.350 214.603 184.889 1.00 1.40  ? 2282 HIS A NE2   1 
ATOM   6598  N  N     . VAL A 1 2283 ? 192.619 211.119 185.094 1.00 0.03  ? 2283 VAL A N     1 
ATOM   6599  C  CA    . VAL A 1 2283 ? 192.512 210.652 183.713 1.00 0.04  ? 2283 VAL A CA    1 
ATOM   6600  C  C     . VAL A 1 2283 ? 191.132 210.968 183.150 1.00 0.07  ? 2283 VAL A C     1 
ATOM   6601  O  O     . VAL A 1 2283 ? 190.999 211.489 182.037 1.00 0.11  ? 2283 VAL A O     1 
ATOM   6602  C  CB    . VAL A 1 2283 ? 192.823 209.146 183.631 1.00 0.06  ? 2283 VAL A CB    1 
ATOM   6603  C  CG1   . VAL A 1 2283 ? 192.450 208.593 182.263 1.00 0.05  ? 2283 VAL A CG1   1 
ATOM   6604  C  CG2   . VAL A 1 2283 ? 194.290 208.891 183.926 1.00 0.05  ? 2283 VAL A CG2   1 
ATOM   6605  N  N     . LEU A 1 2284 ? 190.084 210.663 183.917 1.00 0.06  ? 2284 LEU A N     1 
ATOM   6606  C  CA    . LEU A 1 2284 ? 188.725 210.908 183.451 1.00 0.08  ? 2284 LEU A CA    1 
ATOM   6607  C  C     . LEU A 1 2284 ? 188.449 212.398 183.302 1.00 0.10  ? 2284 LEU A C     1 
ATOM   6608  O  O     . LEU A 1 2284 ? 187.784 212.819 182.349 1.00 0.38  ? 2284 LEU A O     1 
ATOM   6609  C  CB    . LEU A 1 2284 ? 187.722 210.257 184.402 1.00 0.10  ? 2284 LEU A CB    1 
ATOM   6610  C  CG    . LEU A 1 2284 ? 186.239 210.583 184.218 1.00 0.10  ? 2284 LEU A CG    1 
ATOM   6611  C  CD1   . LEU A 1 2284 ? 185.754 210.157 182.842 1.00 1.57  ? 2284 LEU A CD1   1 
ATOM   6612  C  CD2   . LEU A 1 2284 ? 185.422 209.919 185.304 1.00 0.28  ? 2284 LEU A CD2   1 
ATOM   6613  N  N     . ARG A 1 2285 ? 188.953 213.215 184.231 1.00 0.08  ? 2285 ARG A N     1 
ATOM   6614  C  CA    . ARG A 1 2285 ? 188.755 214.656 184.133 1.00 0.20  ? 2285 ARG A CA    1 
ATOM   6615  C  C     . ARG A 1 2285 ? 189.485 215.242 182.932 1.00 0.50  ? 2285 ARG A C     1 
ATOM   6616  O  O     . ARG A 1 2285 ? 188.996 216.193 182.313 1.00 0.59  ? 2285 ARG A O     1 
ATOM   6617  C  CB    . ARG A 1 2285 ? 189.215 215.339 185.420 1.00 0.17  ? 2285 ARG A CB    1 
ATOM   6618  C  CG    . ARG A 1 2285 ? 188.807 216.795 185.528 1.00 0.40  ? 2285 ARG A CG    1 
ATOM   6619  C  CD    . ARG A 1 2285 ? 189.539 217.484 186.662 1.00 0.40  ? 2285 ARG A CD    1 
ATOM   6620  N  NE    . ARG A 1 2285 ? 189.199 216.915 187.961 1.00 0.35  ? 2285 ARG A NE    1 
ATOM   6621  C  CZ    . ARG A 1 2285 ? 188.060 217.129 188.604 1.00 0.50  ? 2285 ARG A CZ    1 
ATOM   6622  N  NH1   . ARG A 1 2285 ? 187.118 217.908 188.101 1.00 0.57  ? 2285 ARG A NH1   1 
ATOM   6623  N  NH2   . ARG A 1 2285 ? 187.863 216.550 189.783 1.00 0.64  ? 2285 ARG A NH2   1 
ATOM   6624  N  N     . LYS A 1 2286 ? 190.653 214.693 182.591 1.00 0.39  ? 2286 LYS A N     1 
ATOM   6625  C  CA    . LYS A 1 2286 ? 191.375 215.149 181.408 1.00 0.48  ? 2286 LYS A CA    1 
ATOM   6626  C  C     . LYS A 1 2286 ? 190.578 214.873 180.137 1.00 0.42  ? 2286 LYS A C     1 
ATOM   6627  O  O     . LYS A 1 2286 ? 190.586 215.682 179.204 1.00 0.86  ? 2286 LYS A O     1 
ATOM   6628  C  CB    . LYS A 1 2286 ? 192.745 214.475 181.347 1.00 1.01  ? 2286 LYS A CB    1 
ATOM   6629  C  CG    . LYS A 1 2286 ? 193.819 215.292 180.654 1.00 1.49  ? 2286 LYS A CG    1 
ATOM   6630  C  CD    . LYS A 1 2286 ? 195.058 214.453 180.400 1.00 2.54  ? 2286 LYS A CD    1 
ATOM   6631  C  CE    . LYS A 1 2286 ? 196.288 215.320 180.202 1.00 5.81  ? 2286 LYS A CE    1 
ATOM   6632  N  NZ    . LYS A 1 2286 ? 195.965 216.618 179.551 1.00 12.57 ? 2286 LYS A NZ    1 
ATOM   6633  N  N     . ILE A 1 2287 ? 189.887 213.733 180.083 1.00 0.32  ? 2287 ILE A N     1 
ATOM   6634  C  CA    . ILE A 1 2287 ? 189.080 213.400 178.911 1.00 0.53  ? 2287 ILE A CA    1 
ATOM   6635  C  C     . ILE A 1 2287 ? 187.853 214.302 178.825 1.00 0.73  ? 2287 ILE A C     1 
ATOM   6636  O  O     . ILE A 1 2287 ? 187.476 214.752 177.738 1.00 2.52  ? 2287 ILE A O     1 
ATOM   6637  C  CB    . ILE A 1 2287 ? 188.694 211.911 178.939 1.00 0.39  ? 2287 ILE A CB    1 
ATOM   6638  C  CG1   . ILE A 1 2287 ? 189.948 211.036 178.916 1.00 0.29  ? 2287 ILE A CG1   1 
ATOM   6639  C  CG2   . ILE A 1 2287 ? 187.779 211.569 177.775 1.00 0.34  ? 2287 ILE A CG2   1 
ATOM   6640  C  CD1   . ILE A 1 2287 ? 189.691 209.587 179.248 1.00 0.09  ? 2287 ILE A CD1   1 
ATOM   6641  N  N     . ILE A 1 2288 ? 187.209 214.575 179.961 1.00 0.55  ? 2288 ILE A N     1 
ATOM   6642  C  CA    . ILE A 1 2288 ? 186.027 215.432 179.964 1.00 0.67  ? 2288 ILE A CA    1 
ATOM   6643  C  C     . ILE A 1 2288 ? 186.389 216.856 179.557 1.00 0.95  ? 2288 ILE A C     1 
ATOM   6644  O  O     . ILE A 1 2288 ? 185.672 217.495 178.781 1.00 1.45  ? 2288 ILE A O     1 
ATOM   6645  C  CB    . ILE A 1 2288 ? 185.343 215.392 181.342 1.00 0.84  ? 2288 ILE A CB    1 
ATOM   6646  C  CG1   . ILE A 1 2288 ? 184.866 213.976 181.665 1.00 0.45  ? 2288 ILE A CG1   1 
ATOM   6647  C  CG2   . ILE A 1 2288 ? 184.185 216.377 181.400 1.00 0.52  ? 2288 ILE A CG2   1 
ATOM   6648  C  CD1   . ILE A 1 2288 ? 184.569 213.753 183.130 1.00 0.27  ? 2288 ILE A CD1   1 
ATOM   6649  N  N     . ASP A 1 2289 ? 187.504 217.377 180.079 1.00 1.46  ? 2289 ASP A N     1 
ATOM   6650  C  CA    . ASP A 1 2289 ? 187.911 218.741 179.754 1.00 1.45  ? 2289 ASP A CA    1 
ATOM   6651  C  C     . ASP A 1 2289 ? 188.233 218.885 178.274 1.00 3.91  ? 2289 ASP A C     1 
ATOM   6652  O  O     . ASP A 1 2289 ? 187.938 219.922 177.668 1.00 6.57  ? 2289 ASP A O     1 
ATOM   6653  C  CB    . ASP A 1 2289 ? 189.103 219.149 180.615 1.00 2.88  ? 2289 ASP A CB    1 
ATOM   6654  C  CG    . ASP A 1 2289 ? 188.728 219.339 182.072 1.00 17.56 ? 2289 ASP A CG    1 
ATOM   6655  O  OD1   . ASP A 1 2289 ? 189.610 219.183 182.942 1.00 12.95 ? 2289 ASP A OD1   1 
ATOM   6656  O  OD2   . ASP A 1 2289 ? 187.548 219.644 182.348 1.00 20.02 ? 2289 ASP A OD2   1 
ATOM   6657  N  N     . SER A 1 2290 ? 188.840 217.858 177.681 1.00 2.59  ? 2290 SER A N     1 
ATOM   6658  C  CA    . SER A 1 2290 ? 189.074 217.780 176.239 1.00 2.23  ? 2290 SER A CA    1 
ATOM   6659  C  C     . SER A 1 2290 ? 189.878 218.977 175.733 1.00 3.05  ? 2290 SER A C     1 
ATOM   6660  O  O     . SER A 1 2290 ? 189.548 219.600 174.721 1.00 3.00  ? 2290 SER A O     1 
ATOM   6661  C  CB    . SER A 1 2290 ? 187.757 217.644 175.478 1.00 2.88  ? 2290 SER A CB    1 
ATOM   6662  O  OG    . SER A 1 2290 ? 187.984 217.260 174.134 1.00 5.46  ? 2290 SER A OG    1 
ATOM   6663  N  N     . VAL A 1 2291 ? 190.953 219.295 176.456 1.00 3.64  ? 2291 VAL A N     1 
ATOM   6664  C  CA    . VAL A 1 2291 ? 191.846 220.362 176.027 1.00 3.01  ? 2291 VAL A CA    1 
ATOM   6665  C  C     . VAL A 1 2291 ? 192.568 219.995 174.738 1.00 3.47  ? 2291 VAL A C     1 
ATOM   6666  O  O     . VAL A 1 2291 ? 192.784 220.861 173.882 1.00 5.28  ? 2291 VAL A O     1 
ATOM   6667  C  CB    . VAL A 1 2291 ? 192.834 220.698 177.161 1.00 3.34  ? 2291 VAL A CB    1 
ATOM   6668  C  CG1   . VAL A 1 2291 ? 193.991 221.544 176.652 1.00 1.94  ? 2291 VAL A CG1   1 
ATOM   6669  C  CG2   . VAL A 1 2291 ? 192.107 221.402 178.299 1.00 2.58  ? 2291 VAL A CG2   1 
ATOM   6670  N  N     . ARG A 1 2292 ? 192.924 218.726 174.561 1.00 2.56  ? 2292 ARG A N     1 
ATOM   6671  C  CA    . ARG A 1 2292 ? 193.677 218.261 173.403 1.00 4.01  ? 2292 ARG A CA    1 
ATOM   6672  C  C     . ARG A 1 2292 ? 192.873 217.256 172.586 1.00 5.07  ? 2292 ARG A C     1 
ATOM   6673  O  O     . ARG A 1 2292 ? 193.417 216.295 172.037 1.00 7.52  ? 2292 ARG A O     1 
ATOM   6674  C  CB    . ARG A 1 2292 ? 195.011 217.665 173.844 1.00 3.30  ? 2292 ARG A CB    1 
ATOM   6675  C  CG    . ARG A 1 2292 ? 195.861 218.644 174.624 1.00 2.55  ? 2292 ARG A CG    1 
ATOM   6676  C  CD    . ARG A 1 2292 ? 197.102 217.994 175.205 1.00 2.75  ? 2292 ARG A CD    1 
ATOM   6677  N  NE    . ARG A 1 2292 ? 197.908 218.938 175.972 1.00 5.24  ? 2292 ARG A NE    1 
ATOM   6678  C  CZ    . ARG A 1 2292 ? 197.511 219.555 177.079 1.00 5.20  ? 2292 ARG A CZ    1 
ATOM   6679  N  NH1   . ARG A 1 2292 ? 196.338 219.298 177.634 1.00 8.30  ? 2292 ARG A NH1   1 
ATOM   6680  N  NH2   . ARG A 1 2292 ? 198.320 220.441 177.653 1.00 3.33  ? 2292 ARG A NH2   1 
ATOM   6681  N  N     . GLY A 1 2293 ? 191.565 217.471 172.493 1.00 3.89  ? 2293 GLY A N     1 
ATOM   6682  C  CA    . GLY A 1 2293 ? 190.706 216.642 171.664 1.00 2.52  ? 2293 GLY A CA    1 
ATOM   6683  C  C     . GLY A 1 2293 ? 190.551 215.203 172.113 1.00 4.79  ? 2293 GLY A C     1 
ATOM   6684  O  O     . GLY A 1 2293 ? 190.511 214.299 171.270 1.00 7.38  ? 2293 GLY A O     1 
ATOM   6685  N  N     . GLU A 1 2294 ? 190.453 214.968 173.422 1.00 3.29  ? 2294 GLU A N     1 
ATOM   6686  C  CA    . GLU A 1 2294 ? 190.245 213.615 173.926 1.00 2.48  ? 2294 GLU A CA    1 
ATOM   6687  C  C     . GLU A 1 2294 ? 188.826 213.108 173.702 1.00 3.28  ? 2294 GLU A C     1 
ATOM   6688  O  O     . GLU A 1 2294 ? 188.618 211.891 173.705 1.00 5.36  ? 2294 GLU A O     1 
ATOM   6689  C  CB    . GLU A 1 2294 ? 190.602 213.535 175.416 1.00 1.89  ? 2294 GLU A CB    1 
ATOM   6690  C  CG    . GLU A 1 2294 ? 192.034 213.938 175.796 1.00 1.35  ? 2294 GLU A CG    1 
ATOM   6691  C  CD    . GLU A 1 2294 ? 192.336 215.422 175.674 1.00 4.52  ? 2294 GLU A CD    1 
ATOM   6692  O  OE1   . GLU A 1 2294 ? 191.472 216.186 175.208 1.00 6.64  ? 2294 GLU A OE1   1 
ATOM   6693  O  OE2   . GLU A 1 2294 ? 193.454 215.823 176.052 1.00 10.17 ? 2294 GLU A OE2   1 
ATOM   6694  N  N     . LEU A 1 2295 ? 187.850 213.994 173.499 1.00 2.67  ? 2295 LEU A N     1 
ATOM   6695  C  CA    . LEU A 1 2295 ? 186.481 213.546 173.272 1.00 1.91  ? 2295 LEU A CA    1 
ATOM   6696  C  C     . LEU A 1 2295 ? 186.244 213.022 171.864 1.00 2.32  ? 2295 LEU A C     1 
ATOM   6697  O  O     . LEU A 1 2295 ? 185.206 212.397 171.623 1.00 4.56  ? 2295 LEU A O     1 
ATOM   6698  C  CB    . LEU A 1 2295 ? 185.488 214.672 173.562 1.00 2.02  ? 2295 LEU A CB    1 
ATOM   6699  C  CG    . LEU A 1 2295 ? 185.333 215.095 175.021 1.00 1.70  ? 2295 LEU A CG    1 
ATOM   6700  C  CD1   . LEU A 1 2295 ? 184.404 216.294 175.135 1.00 0.97  ? 2295 LEU A CD1   1 
ATOM   6701  C  CD2   . LEU A 1 2295 ? 184.831 213.936 175.861 1.00 0.77  ? 2295 LEU A CD2   1 
ATOM   6702  N  N     . GLN A 1 2296 ? 187.164 213.261 170.933 1.00 3.88  ? 2296 GLN A N     1 
ATOM   6703  C  CA    . GLN A 1 2296 ? 187.040 212.755 169.574 1.00 3.13  ? 2296 GLN A CA    1 
ATOM   6704  C  C     . GLN A 1 2296 ? 187.771 211.436 169.376 1.00 3.15  ? 2296 GLN A C     1 
ATOM   6705  O  O     . GLN A 1 2296 ? 187.787 210.912 168.259 1.00 6.55  ? 2296 GLN A O     1 
ATOM   6706  C  CB    . GLN A 1 2296 ? 187.559 213.791 168.571 1.00 3.20  ? 2296 GLN A CB    1 
ATOM   6707  C  CG    . GLN A 1 2296 ? 187.236 215.235 168.924 1.00 3.53  ? 2296 GLN A CG    1 
ATOM   6708  C  CD    . GLN A 1 2296 ? 185.787 215.442 169.317 1.00 6.03  ? 2296 GLN A CD    1 
ATOM   6709  O  OE1   . GLN A 1 2296 ? 185.492 215.927 170.408 1.00 3.37  ? 2296 GLN A OE1   1 
ATOM   6710  N  NE2   . GLN A 1 2296 ? 184.874 215.071 168.428 1.00 9.85  ? 2296 GLN A NE2   1 
ATOM   6711  N  N     . LYS A 1 2297 ? 188.366 210.888 170.429 1.00 4.38  ? 2297 LYS A N     1 
ATOM   6712  C  CA    . LYS A 1 2297 ? 189.116 209.647 170.361 1.00 2.36  ? 2297 LYS A CA    1 
ATOM   6713  C  C     . LYS A 1 2297 ? 188.411 208.575 171.179 1.00 1.22  ? 2297 LYS A C     1 
ATOM   6714  O  O     . LYS A 1 2297 ? 187.626 208.870 172.083 1.00 2.06  ? 2297 LYS A O     1 
ATOM   6715  C  CB    . LYS A 1 2297 ? 190.546 209.832 170.883 1.00 3.38  ? 2297 LYS A CB    1 
ATOM   6716  C  CG    . LYS A 1 2297 ? 191.311 210.963 170.230 1.00 7.13  ? 2297 LYS A CG    1 
ATOM   6717  C  CD    . LYS A 1 2297 ? 192.675 211.132 170.870 1.00 9.48  ? 2297 LYS A CD    1 
ATOM   6718  C  CE    . LYS A 1 2297 ? 193.399 212.347 170.321 1.00 10.26 ? 2297 LYS A CE    1 
ATOM   6719  N  NZ    . LYS A 1 2297 ? 194.753 212.493 170.916 1.00 14.54 ? 2297 LYS A NZ    1 
ATOM   6720  N  N     . ARG A 1 2298 ? 188.695 207.322 170.845 1.00 1.22  ? 2298 ARG A N     1 
ATOM   6721  C  CA    . ARG A 1 2298 ? 188.228 206.202 171.648 1.00 0.62  ? 2298 ARG A CA    1 
ATOM   6722  C  C     . ARG A 1 2298 ? 189.112 206.090 172.886 1.00 0.66  ? 2298 ARG A C     1 
ATOM   6723  O  O     . ARG A 1 2298 ? 190.321 205.859 172.775 1.00 1.08  ? 2298 ARG A O     1 
ATOM   6724  C  CB    . ARG A 1 2298 ? 188.251 204.915 170.830 1.00 0.36  ? 2298 ARG A CB    1 
ATOM   6725  C  CG    . ARG A 1 2298 ? 188.041 203.649 171.636 1.00 0.35  ? 2298 ARG A CG    1 
ATOM   6726  C  CD    . ARG A 1 2298 ? 187.816 202.451 170.730 1.00 0.52  ? 2298 ARG A CD    1 
ATOM   6727  N  NE    . ARG A 1 2298 ? 186.471 202.429 170.169 1.00 1.08  ? 2298 ARG A NE    1 
ATOM   6728  C  CZ    . ARG A 1 2298 ? 186.185 202.645 168.892 1.00 1.09  ? 2298 ARG A CZ    1 
ATOM   6729  N  NH1   . ARG A 1 2298 ? 187.130 202.914 168.008 1.00 0.65  ? 2298 ARG A NH1   1 
ATOM   6730  N  NH2   . ARG A 1 2298 ? 184.918 202.592 168.494 1.00 1.18  ? 2298 ARG A NH2   1 
ATOM   6731  N  N     . GLN A 1 2299 ? 188.516 206.271 174.061 1.00 0.40  ? 2299 GLN A N     1 
ATOM   6732  C  CA    . GLN A 1 2299 ? 189.248 206.305 175.323 1.00 0.17  ? 2299 GLN A CA    1 
ATOM   6733  C  C     . GLN A 1 2299 ? 188.881 205.072 176.137 1.00 0.05  ? 2299 GLN A C     1 
ATOM   6734  O  O     . GLN A 1 2299 ? 187.735 204.926 176.571 1.00 0.16  ? 2299 GLN A O     1 
ATOM   6735  C  CB    . GLN A 1 2299 ? 188.935 207.584 176.094 1.00 0.21  ? 2299 GLN A CB    1 
ATOM   6736  C  CG    . GLN A 1 2299 ? 189.316 208.856 175.362 1.00 0.28  ? 2299 GLN A CG    1 
ATOM   6737  C  CD    . GLN A 1 2299 ? 190.791 209.176 175.471 1.00 0.50  ? 2299 GLN A CD    1 
ATOM   6738  O  OE1   . GLN A 1 2299 ? 191.550 208.449 176.107 1.00 0.47  ? 2299 GLN A OE1   1 
ATOM   6739  N  NE2   . GLN A 1 2299 ? 191.206 210.266 174.845 1.00 3.23  ? 2299 GLN A NE2   1 
ATOM   6740  N  N     . TRP A 1 2300 ? 189.853 204.193 176.349 1.00 0.04  ? 2300 TRP A N     1 
ATOM   6741  C  CA    . TRP A 1 2300 ? 189.660 202.987 177.142 1.00 0.03  ? 2300 TRP A CA    1 
ATOM   6742  C  C     . TRP A 1 2300 ? 190.485 203.098 178.416 1.00 0.03  ? 2300 TRP A C     1 
ATOM   6743  O  O     . TRP A 1 2300 ? 191.703 203.281 178.357 1.00 0.04  ? 2300 TRP A O     1 
ATOM   6744  C  CB    . TRP A 1 2300 ? 190.050 201.739 176.351 1.00 0.05  ? 2300 TRP A CB    1 
ATOM   6745  C  CG    . TRP A 1 2300 ? 189.055 201.367 175.291 1.00 0.04  ? 2300 TRP A CG    1 
ATOM   6746  C  CD1   . TRP A 1 2300 ? 187.918 202.041 174.966 1.00 0.03  ? 2300 TRP A CD1   1 
ATOM   6747  C  CD2   . TRP A 1 2300 ? 189.111 200.232 174.424 1.00 0.05  ? 2300 TRP A CD2   1 
ATOM   6748  N  NE1   . TRP A 1 2300 ? 187.262 201.397 173.951 1.00 0.05  ? 2300 TRP A NE1   1 
ATOM   6749  C  CE2   . TRP A 1 2300 ? 187.973 200.283 173.598 1.00 0.07  ? 2300 TRP A CE2   1 
ATOM   6750  C  CE3   . TRP A 1 2300 ? 190.013 199.176 174.265 1.00 0.06  ? 2300 TRP A CE3   1 
ATOM   6751  C  CZ2   . TRP A 1 2300 ? 187.713 199.321 172.629 1.00 0.07  ? 2300 TRP A CZ2   1 
ATOM   6752  C  CZ3   . TRP A 1 2300 ? 189.752 198.224 173.304 1.00 0.09  ? 2300 TRP A CZ3   1 
ATOM   6753  C  CH2   . TRP A 1 2300 ? 188.612 198.302 172.496 1.00 0.14  ? 2300 TRP A CH2   1 
ATOM   6754  N  N     . ILE A 1 2301 ? 189.820 202.992 179.559 1.00 0.04  ? 2301 ILE A N     1 
ATOM   6755  C  CA    . ILE A 1 2301 ? 190.482 202.982 180.856 1.00 0.05  ? 2301 ILE A CA    1 
ATOM   6756  C  C     . ILE A 1 2301 ? 190.458 201.547 181.358 1.00 0.06  ? 2301 ILE A C     1 
ATOM   6757  O  O     . ILE A 1 2301 ? 189.410 201.034 181.765 1.00 0.05  ? 2301 ILE A O     1 
ATOM   6758  C  CB    . ILE A 1 2301 ? 189.813 203.947 181.843 1.00 0.02  ? 2301 ILE A CB    1 
ATOM   6759  C  CG1   . ILE A 1 2301 ? 189.794 205.361 181.261 1.00 0.08  ? 2301 ILE A CG1   1 
ATOM   6760  C  CG2   . ILE A 1 2301 ? 190.535 203.923 183.181 1.00 0.02  ? 2301 ILE A CG2   1 
ATOM   6761  C  CD1   . ILE A 1 2301 ? 188.996 206.350 182.064 1.00 0.02  ? 2301 ILE A CD1   1 
ATOM   6762  N  N     . VAL A 1 2302 ? 191.611 200.894 181.328 1.00 0.04  ? 2302 VAL A N     1 
ATOM   6763  C  CA    . VAL A 1 2302 ? 191.723 199.479 181.648 1.00 0.03  ? 2302 VAL A CA    1 
ATOM   6764  C  C     . VAL A 1 2302 ? 192.284 199.348 183.055 1.00 0.06  ? 2302 VAL A C     1 
ATOM   6765  O  O     . VAL A 1 2302 ? 193.428 199.732 183.316 1.00 0.04  ? 2302 VAL A O     1 
ATOM   6766  C  CB    . VAL A 1 2302 ? 192.607 198.745 180.627 1.00 0.04  ? 2302 VAL A CB    1 
ATOM   6767  C  CG1   . VAL A 1 2302 ? 192.609 197.248 180.900 1.00 0.03  ? 2302 VAL A CG1   1 
ATOM   6768  C  CG2   . VAL A 1 2302 ? 192.136 199.039 179.211 1.00 0.03  ? 2302 VAL A CG2   1 
ATOM   6769  N  N     . PHE A 1 2303 ? 191.464 198.805 183.954 1.00 0.05  ? 2303 PHE A N     1 
ATOM   6770  C  CA    . PHE A 1 2303 ? 191.953 198.520 185.327 1.00 0.03  ? 2303 PHE A CA    1 
ATOM   6771  C  C     . PHE A 1 2303 ? 192.543 197.112 185.303 1.00 0.03  ? 2303 PHE A C     1 
ATOM   6772  O  O     . PHE A 1 2303 ? 191.795 196.145 185.520 1.00 0.11  ? 2303 PHE A O     1 
ATOM   6773  C  CB    . PHE A 1 2303 ? 190.835 198.688 186.360 1.00 0.03  ? 2303 PHE A CB    1 
ATOM   6774  C  CG    . PHE A 1 2303 ? 190.327 200.107 186.573 1.00 0.03  ? 2303 PHE A CG    1 
ATOM   6775  C  CD1   . PHE A 1 2303 ? 190.983 200.976 187.437 1.00 0.04  ? 2303 PHE A CD1   1 
ATOM   6776  C  CD2   . PHE A 1 2303 ? 189.176 200.556 185.937 1.00 0.02  ? 2303 PHE A CD2   1 
ATOM   6777  C  CE1   . PHE A 1 2303 ? 190.514 202.263 187.638 1.00 0.02  ? 2303 PHE A CE1   1 
ATOM   6778  C  CE2   . PHE A 1 2303 ? 188.710 201.844 186.143 1.00 0.02  ? 2303 PHE A CE2   1 
ATOM   6779  C  CZ    . PHE A 1 2303 ? 189.378 202.692 186.994 1.00 0.02  ? 2303 PHE A CZ    1 
ATOM   6780  N  N     . ASP A 1 2304 ? 193.841 197.000 185.006 1.00 0.07  ? 2304 ASP A N     1 
ATOM   6781  C  CA    . ASP A 1 2304 ? 194.528 195.679 184.968 1.00 0.12  ? 2304 ASP A CA    1 
ATOM   6782  C  C     . ASP A 1 2304 ? 195.053 195.349 186.368 1.00 0.16  ? 2304 ASP A C     1 
ATOM   6783  O  O     . ASP A 1 2304 ? 196.140 195.843 186.729 1.00 0.31  ? 2304 ASP A O     1 
ATOM   6784  C  CB    . ASP A 1 2304 ? 195.626 195.645 183.918 1.00 0.12  ? 2304 ASP A CB    1 
ATOM   6785  C  CG    . ASP A 1 2304 ? 196.280 194.291 183.689 1.00 0.13  ? 2304 ASP A CG    1 
ATOM   6786  O  OD1   . ASP A 1 2304 ? 195.846 193.312 184.330 1.00 0.18  ? 2304 ASP A OD1   1 
ATOM   6787  O  OD2   . ASP A 1 2304 ? 197.224 194.229 182.876 1.00 0.35  ? 2304 ASP A OD2   1 
ATOM   6788  N  N     . GLY A 1 2305 ? 194.311 194.535 187.115 1.00 0.11  ? 2305 GLY A N     1 
ATOM   6789  C  CA    . GLY A 1 2305 ? 194.705 194.214 188.495 1.00 0.29  ? 2305 GLY A CA    1 
ATOM   6790  C  C     . GLY A 1 2305 ? 193.589 193.529 189.250 1.00 0.45  ? 2305 GLY A C     1 
ATOM   6791  O  O     . GLY A 1 2305 ? 192.584 193.161 188.615 1.00 0.91  ? 2305 GLY A O     1 
ATOM   6792  N  N     . ASP A 1 2306 ? 193.753 193.368 190.560 1.00 0.53  ? 2306 ASP A N     1 
ATOM   6793  C  CA    . ASP A 1 2306 ? 192.776 192.676 191.387 1.00 0.66  ? 2306 ASP A CA    1 
ATOM   6794  C  C     . ASP A 1 2306 ? 191.566 193.558 191.662 1.00 0.66  ? 2306 ASP A C     1 
ATOM   6795  O  O     . ASP A 1 2306 ? 191.686 194.774 191.827 1.00 2.88  ? 2306 ASP A O     1 
ATOM   6796  C  CB    . ASP A 1 2306 ? 193.406 192.237 192.708 1.00 1.42  ? 2306 ASP A CB    1 
ATOM   6797  C  CG    . ASP A 1 2306 ? 194.466 191.178 192.520 1.00 3.42  ? 2306 ASP A CG    1 
ATOM   6798  O  OD1   . ASP A 1 2306 ? 194.469 190.522 191.457 1.00 6.30  ? 2306 ASP A OD1   1 
ATOM   6799  O  OD2   . ASP A 1 2306 ? 195.289 190.992 193.438 1.00 6.01  ? 2306 ASP A OD2   1 
ATOM   6800  N  N     . VAL A 1 2307 ? 190.396 192.932 191.719 1.00 0.51  ? 2307 VAL A N     1 
ATOM   6801  C  CA    . VAL A 1 2307 ? 189.148 193.618 192.026 1.00 0.68  ? 2307 VAL A CA    1 
ATOM   6802  C  C     . VAL A 1 2307 ? 188.743 193.261 193.449 1.00 1.14  ? 2307 VAL A C     1 
ATOM   6803  O  O     . VAL A 1 2307 ? 188.596 192.080 193.785 1.00 2.95  ? 2307 VAL A O     1 
ATOM   6804  C  CB    . VAL A 1 2307 ? 188.039 193.248 191.028 1.00 0.83  ? 2307 VAL A CB    1 
ATOM   6805  C  CG1   . VAL A 1 2307 ? 186.676 193.623 191.588 1.00 0.72  ? 2307 VAL A CG1   1 
ATOM   6806  C  CG2   . VAL A 1 2307 ? 188.264 193.944 189.698 1.00 0.18  ? 2307 VAL A CG2   1 
ATOM   6807  N  N     . ASP A 1 2308 ? 188.574 194.274 194.286 1.00 0.63  ? 2308 ASP A N     1 
ATOM   6808  C  CA    . ASP A 1 2308 ? 188.036 194.118 195.628 1.00 1.00  ? 2308 ASP A CA    1 
ATOM   6809  C  C     . ASP A 1 2308 ? 186.958 195.165 195.858 1.00 1.15  ? 2308 ASP A C     1 
ATOM   6810  O  O     . ASP A 1 2308 ? 186.957 196.218 195.214 1.00 0.68  ? 2308 ASP A O     1 
ATOM   6811  C  CB    . ASP A 1 2308 ? 189.155 194.180 196.689 1.00 1.10  ? 2308 ASP A CB    1 
ATOM   6812  C  CG    . ASP A 1 2308 ? 189.686 195.594 196.986 1.00 2.03  ? 2308 ASP A CG    1 
ATOM   6813  O  OD1   . ASP A 1 2308 ? 189.059 196.628 196.692 1.00 2.91  ? 2308 ASP A OD1   1 
ATOM   6814  O  OD2   . ASP A 1 2308 ? 190.796 195.665 197.548 1.00 4.65  ? 2308 ASP A OD2   1 
ATOM   6815  N  N     . PRO A 1 2309 ? 185.997 194.889 196.743 1.00 1.66  ? 2309 PRO A N     1 
ATOM   6816  C  CA    . PRO A 1 2309 ? 184.893 195.842 196.938 1.00 1.09  ? 2309 PRO A CA    1 
ATOM   6817  C  C     . PRO A 1 2309 ? 185.334 197.195 197.465 1.00 1.33  ? 2309 PRO A C     1 
ATOM   6818  O  O     . PRO A 1 2309 ? 184.601 198.174 197.292 1.00 1.14  ? 2309 PRO A O     1 
ATOM   6819  C  CB    . PRO A 1 2309 ? 183.981 195.121 197.941 1.00 1.34  ? 2309 PRO A CB    1 
ATOM   6820  C  CG    . PRO A 1 2309 ? 184.855 194.119 198.601 1.00 1.99  ? 2309 PRO A CG    1 
ATOM   6821  C  CD    . PRO A 1 2309 ? 185.825 193.678 197.560 1.00 1.85  ? 2309 PRO A CD    1 
ATOM   6822  N  N     . GLU A 1 2310 ? 186.510 197.287 198.090 1.00 2.34  ? 2310 GLU A N     1 
ATOM   6823  C  CA    . GLU A 1 2310 ? 186.918 198.542 198.713 1.00 1.85  ? 2310 GLU A CA    1 
ATOM   6824  C  C     . GLU A 1 2310 ? 187.093 199.653 197.683 1.00 3.47  ? 2310 GLU A C     1 
ATOM   6825  O  O     . GLU A 1 2310 ? 186.692 200.796 197.923 1.00 8.90  ? 2310 GLU A O     1 
ATOM   6826  C  CB    . GLU A 1 2310 ? 188.204 198.339 199.513 1.00 5.17  ? 2310 GLU A CB    1 
ATOM   6827  C  CG    . GLU A 1 2310 ? 188.659 199.580 200.263 1.00 10.72 ? 2310 GLU A CG    1 
ATOM   6828  C  CD    . GLU A 1 2310 ? 189.908 199.343 201.091 1.00 26.61 ? 2310 GLU A CD    1 
ATOM   6829  O  OE1   . GLU A 1 2310 ? 190.437 198.211 201.067 1.00 24.30 ? 2310 GLU A OE1   1 
ATOM   6830  O  OE2   . GLU A 1 2310 ? 190.360 200.291 201.769 1.00 27.51 ? 2310 GLU A OE2   1 
ATOM   6831  N  N     . TRP A 1 2311 ? 187.684 199.345 196.527 1.00 1.52  ? 2311 TRP A N     1 
ATOM   6832  C  CA    . TRP A 1 2311 ? 187.923 200.378 195.528 1.00 0.59  ? 2311 TRP A CA    1 
ATOM   6833  C  C     . TRP A 1 2311 ? 186.939 200.356 194.364 1.00 0.44  ? 2311 TRP A C     1 
ATOM   6834  O  O     . TRP A 1 2311 ? 186.593 201.424 193.854 1.00 3.71  ? 2311 TRP A O     1 
ATOM   6835  C  CB    . TRP A 1 2311 ? 189.359 200.292 194.984 1.00 0.31  ? 2311 TRP A CB    1 
ATOM   6836  C  CG    . TRP A 1 2311 ? 189.615 199.177 194.011 1.00 0.33  ? 2311 TRP A CG    1 
ATOM   6837  C  CD1   . TRP A 1 2311 ? 190.120 197.947 194.296 1.00 0.17  ? 2311 TRP A CD1   1 
ATOM   6838  C  CD2   . TRP A 1 2311 ? 189.384 199.194 192.597 1.00 0.14  ? 2311 TRP A CD2   1 
ATOM   6839  N  NE1   . TRP A 1 2311 ? 190.212 197.196 193.157 1.00 0.17  ? 2311 TRP A NE1   1 
ATOM   6840  C  CE2   . TRP A 1 2311 ? 189.773 197.941 192.097 1.00 0.08  ? 2311 TRP A CE2   1 
ATOM   6841  C  CE3   . TRP A 1 2311 ? 188.889 200.149 191.708 1.00 0.04  ? 2311 TRP A CE3   1 
ATOM   6842  C  CZ2   . TRP A 1 2311 ? 189.666 197.610 190.751 1.00 0.04  ? 2311 TRP A CZ2   1 
ATOM   6843  C  CZ3   . TRP A 1 2311 ? 188.793 199.821 190.374 1.00 0.03  ? 2311 TRP A CZ3   1 
ATOM   6844  C  CH2   . TRP A 1 2311 ? 189.182 198.565 189.907 1.00 0.02  ? 2311 TRP A CH2   1 
ATOM   6845  N  N     . VAL A 1 2312 ? 186.464 199.186 193.928 1.00 0.23  ? 2312 VAL A N     1 
ATOM   6846  C  CA    . VAL A 1 2312 ? 185.641 199.164 192.720 1.00 0.38  ? 2312 VAL A CA    1 
ATOM   6847  C  C     . VAL A 1 2312 ? 184.224 199.656 192.990 1.00 0.38  ? 2312 VAL A C     1 
ATOM   6848  O  O     . VAL A 1 2312 ? 183.556 200.138 192.068 1.00 0.37  ? 2312 VAL A O     1 
ATOM   6849  C  CB    . VAL A 1 2312 ? 185.590 197.762 192.086 1.00 0.24  ? 2312 VAL A CB    1 
ATOM   6850  C  CG1   . VAL A 1 2312 ? 184.825 196.777 192.971 1.00 0.47  ? 2312 VAL A CG1   1 
ATOM   6851  C  CG2   . VAL A 1 2312 ? 185.045 197.815 190.665 1.00 0.13  ? 2312 VAL A CG2   1 
ATOM   6852  N  N     . GLU A 1 2313 ? 183.746 199.563 194.230 1.00 0.27  ? 2313 GLU A N     1 
ATOM   6853  C  CA    . GLU A 1 2313 ? 182.414 200.049 194.561 1.00 0.50  ? 2313 GLU A CA    1 
ATOM   6854  C  C     . GLU A 1 2313 ? 182.317 201.569 194.559 1.00 0.79  ? 2313 GLU A C     1 
ATOM   6855  O  O     . GLU A 1 2313 ? 181.206 202.099 194.651 1.00 2.49  ? 2313 GLU A O     1 
ATOM   6856  C  CB    . GLU A 1 2313 ? 181.971 199.481 195.909 1.00 1.35  ? 2313 GLU A CB    1 
ATOM   6857  C  CG    . GLU A 1 2313 ? 181.756 197.977 195.860 1.00 2.65  ? 2313 GLU A CG    1 
ATOM   6858  C  CD    . GLU A 1 2313 ? 181.341 197.394 197.187 1.00 15.99 ? 2313 GLU A CD    1 
ATOM   6859  O  OE1   . GLU A 1 2313 ? 181.340 198.138 198.192 1.00 16.62 ? 2313 GLU A OE1   1 
ATOM   6860  O  OE2   . GLU A 1 2313 ? 181.012 196.190 197.229 1.00 14.66 ? 2313 GLU A OE2   1 
ATOM   6861  N  N     . ASN A 1 2314 ? 183.443 202.278 194.461 1.00 0.89  ? 2314 ASN A N     1 
ATOM   6862  C  CA    . ASN A 1 2314 ? 183.413 203.696 194.124 1.00 0.44  ? 2314 ASN A CA    1 
ATOM   6863  C  C     . ASN A 1 2314 ? 182.961 203.935 192.692 1.00 0.26  ? 2314 ASN A C     1 
ATOM   6864  O  O     . ASN A 1 2314 ? 182.616 205.070 192.349 1.00 0.39  ? 2314 ASN A O     1 
ATOM   6865  C  CB    . ASN A 1 2314 ? 184.791 204.327 194.330 1.00 0.66  ? 2314 ASN A CB    1 
ATOM   6866  C  CG    . ASN A 1 2314 ? 185.101 204.595 195.787 1.00 1.40  ? 2314 ASN A CG    1 
ATOM   6867  O  OD1   . ASN A 1 2314 ? 184.851 203.758 196.651 1.00 4.16  ? 2314 ASN A OD1   1 
ATOM   6868  N  ND2   . ASN A 1 2314 ? 185.652 205.767 196.066 1.00 0.26  ? 2314 ASN A ND2   1 
ATOM   6869  N  N     . LEU A 1 2315 ? 182.961 202.899 191.857 1.00 0.29  ? 2315 LEU A N     1 
ATOM   6870  C  CA    . LEU A 1 2315 ? 182.551 202.992 190.464 1.00 0.23  ? 2315 LEU A CA    1 
ATOM   6871  C  C     . LEU A 1 2315 ? 181.133 202.490 190.234 1.00 0.26  ? 2315 LEU A C     1 
ATOM   6872  O  O     . LEU A 1 2315 ? 180.731 202.320 189.081 1.00 0.37  ? 2315 LEU A O     1 
ATOM   6873  C  CB    . LEU A 1 2315 ? 183.524 202.209 189.580 1.00 0.17  ? 2315 LEU A CB    1 
ATOM   6874  C  CG    . LEU A 1 2315 ? 184.989 202.645 189.596 1.00 0.11  ? 2315 LEU A CG    1 
ATOM   6875  C  CD1   . LEU A 1 2315 ? 185.845 201.649 188.831 1.00 0.08  ? 2315 LEU A CD1   1 
ATOM   6876  C  CD2   . LEU A 1 2315 ? 185.137 204.039 189.018 1.00 0.07  ? 2315 LEU A CD2   1 
ATOM   6877  N  N     . ASN A 1 2316 ? 180.369 202.244 191.302 1.00 0.51  ? 2316 ASN A N     1 
ATOM   6878  C  CA    . ASN A 1 2316 ? 179.005 201.748 191.135 1.00 0.49  ? 2316 ASN A CA    1 
ATOM   6879  C  C     . ASN A 1 2316 ? 178.158 202.737 190.346 1.00 0.38  ? 2316 ASN A C     1 
ATOM   6880  O  O     . ASN A 1 2316 ? 177.424 202.349 189.433 1.00 0.78  ? 2316 ASN A O     1 
ATOM   6881  C  CB    . ASN A 1 2316 ? 178.374 201.459 192.498 1.00 0.84  ? 2316 ASN A CB    1 
ATOM   6882  C  CG    . ASN A 1 2316 ? 178.740 200.093 193.033 1.00 1.45  ? 2316 ASN A CG    1 
ATOM   6883  O  OD1   . ASN A 1 2316 ? 179.425 199.316 192.371 1.00 3.04  ? 2316 ASN A OD1   1 
ATOM   6884  N  ND2   . ASN A 1 2316 ? 178.283 199.791 194.242 1.00 1.99  ? 2316 ASN A ND2   1 
ATOM   6885  N  N     . SER A 1 2317 ? 178.262 204.026 190.672 1.00 0.41  ? 2317 SER A N     1 
ATOM   6886  C  CA    . SER A 1 2317 ? 177.535 205.036 189.913 1.00 0.47  ? 2317 SER A CA    1 
ATOM   6887  C  C     . SER A 1 2317 ? 178.160 205.294 188.548 1.00 0.36  ? 2317 SER A C     1 
ATOM   6888  O  O     . SER A 1 2317 ? 177.506 205.885 187.684 1.00 0.81  ? 2317 SER A O     1 
ATOM   6889  C  CB    . SER A 1 2317 ? 177.448 206.339 190.711 1.00 0.44  ? 2317 SER A CB    1 
ATOM   6890  O  OG    . SER A 1 2317 ? 178.734 206.841 191.025 1.00 0.44  ? 2317 SER A OG    1 
ATOM   6891  N  N     . VAL A 1 2318 ? 179.410 204.877 188.337 1.00 0.32  ? 2318 VAL A N     1 
ATOM   6892  C  CA    . VAL A 1 2318 ? 180.027 204.992 187.020 1.00 0.34  ? 2318 VAL A CA    1 
ATOM   6893  C  C     . VAL A 1 2318 ? 179.548 203.873 186.104 1.00 0.26  ? 2318 VAL A C     1 
ATOM   6894  O  O     . VAL A 1 2318 ? 179.224 204.102 184.933 1.00 0.32  ? 2318 VAL A O     1 
ATOM   6895  C  CB    . VAL A 1 2318 ? 181.564 204.993 187.143 1.00 0.37  ? 2318 VAL A CB    1 
ATOM   6896  C  CG1   . VAL A 1 2318 ? 182.211 205.083 185.770 1.00 0.12  ? 2318 VAL A CG1   1 
ATOM   6897  C  CG2   . VAL A 1 2318 ? 182.030 206.133 188.026 1.00 0.14  ? 2318 VAL A CG2   1 
ATOM   6898  N  N     . LEU A 1 2319 ? 179.494 202.650 186.623 1.00 0.40  ? 2319 LEU A N     1 
ATOM   6899  C  CA    . LEU A 1 2319 ? 179.183 201.482 185.812 1.00 0.45  ? 2319 LEU A CA    1 
ATOM   6900  C  C     . LEU A 1 2319 ? 177.690 201.280 185.578 1.00 1.13  ? 2319 LEU A C     1 
ATOM   6901  O  O     . LEU A 1 2319 ? 177.327 200.513 184.682 1.00 2.26  ? 2319 LEU A O     1 
ATOM   6902  C  CB    . LEU A 1 2319 ? 179.777 200.234 186.464 1.00 0.65  ? 2319 LEU A CB    1 
ATOM   6903  C  CG    . LEU A 1 2319 ? 181.291 200.271 186.687 1.00 0.22  ? 2319 LEU A CG    1 
ATOM   6904  C  CD1   . LEU A 1 2319 ? 181.752 199.077 187.500 1.00 0.57  ? 2319 LEU A CD1   1 
ATOM   6905  C  CD2   . LEU A 1 2319 ? 182.034 200.345 185.364 1.00 0.12  ? 2319 LEU A CD2   1 
ATOM   6906  N  N     . ASP A 1 2320 ? 176.818 201.937 186.340 1.00 1.03  ? 2320 ASP A N     1 
ATOM   6907  C  CA    . ASP A 1 2320 ? 175.386 201.813 186.109 1.00 1.94  ? 2320 ASP A CA    1 
ATOM   6908  C  C     . ASP A 1 2320 ? 174.930 202.917 185.155 1.00 2.18  ? 2320 ASP A C     1 
ATOM   6909  O  O     . ASP A 1 2320 ? 175.739 203.594 184.516 1.00 1.99  ? 2320 ASP A O     1 
ATOM   6910  C  CB    . ASP A 1 2320 ? 174.608 201.823 187.427 1.00 1.62  ? 2320 ASP A CB    1 
ATOM   6911  C  CG    . ASP A 1 2320 ? 174.861 203.062 188.263 1.00 3.28  ? 2320 ASP A CG    1 
ATOM   6912  O  OD1   . ASP A 1 2320 ? 175.406 204.053 187.739 1.00 5.47  ? 2320 ASP A OD1   1 
ATOM   6913  O  OD2   . ASP A 1 2320 ? 174.505 203.044 189.459 1.00 3.08  ? 2320 ASP A OD2   1 
ATOM   6914  N  N     . ASP A 1 2321 ? 173.614 203.106 185.047 1.00 3.05  ? 2321 ASP A N     1 
ATOM   6915  C  CA    . ASP A 1 2321 ? 173.069 204.064 184.093 1.00 3.82  ? 2321 ASP A CA    1 
ATOM   6916  C  C     . ASP A 1 2321 ? 173.307 205.513 184.501 1.00 2.35  ? 2321 ASP A C     1 
ATOM   6917  O  O     . ASP A 1 2321 ? 173.113 206.411 183.676 1.00 6.83  ? 2321 ASP A O     1 
ATOM   6918  C  CB    . ASP A 1 2321 ? 171.574 203.800 183.893 1.00 7.51  ? 2321 ASP A CB    1 
ATOM   6919  C  CG    . ASP A 1 2321 ? 170.762 203.992 185.165 1.00 18.61 ? 2321 ASP A CG    1 
ATOM   6920  O  OD1   . ASP A 1 2321 ? 171.347 204.290 186.228 1.00 18.02 ? 2321 ASP A OD1   1 
ATOM   6921  O  OD2   . ASP A 1 2321 ? 169.525 203.833 185.101 1.00 19.22 ? 2321 ASP A OD2   1 
ATOM   6922  N  N     . ASN A 1 2322 ? 173.718 205.764 185.748 1.00 2.15  ? 2322 ASN A N     1 
ATOM   6923  C  CA    . ASN A 1 2322 ? 174.052 207.125 186.156 1.00 1.66  ? 2322 ASN A CA    1 
ATOM   6924  C  C     . ASN A 1 2322 ? 175.238 207.665 185.365 1.00 1.24  ? 2322 ASN A C     1 
ATOM   6925  O  O     . ASN A 1 2322 ? 175.245 208.838 184.974 1.00 1.18  ? 2322 ASN A O     1 
ATOM   6926  C  CB    . ASN A 1 2322 ? 174.349 207.178 187.655 1.00 2.04  ? 2322 ASN A CB    1 
ATOM   6927  C  CG    . ASN A 1 2322 ? 173.117 206.955 188.502 1.00 1.54  ? 2322 ASN A CG    1 
ATOM   6928  O  OD1   . ASN A 1 2322 ? 172.173 207.741 188.457 1.00 1.84  ? 2322 ASN A OD1   1 
ATOM   6929  N  ND2   . ASN A 1 2322 ? 173.119 205.883 189.281 1.00 2.39  ? 2322 ASN A ND2   1 
ATOM   6930  N  N     . LYS A 1 2323 ? 176.244 206.823 185.120 1.00 1.10  ? 2323 LYS A N     1 
ATOM   6931  C  CA    . LYS A 1 2323 ? 177.454 207.215 184.393 1.00 0.89  ? 2323 LYS A CA    1 
ATOM   6932  C  C     . LYS A 1 2323 ? 178.114 208.429 185.039 1.00 0.41  ? 2323 LYS A C     1 
ATOM   6933  O  O     . LYS A 1 2323 ? 178.564 209.355 184.364 1.00 0.55  ? 2323 LYS A O     1 
ATOM   6934  C  CB    . LYS A 1 2323 ? 177.152 207.478 182.918 1.00 1.08  ? 2323 LYS A CB    1 
ATOM   6935  C  CG    . LYS A 1 2323 ? 176.718 206.252 182.139 1.00 1.22  ? 2323 LYS A CG    1 
ATOM   6936  C  CD    . LYS A 1 2323 ? 176.307 206.622 180.727 1.00 1.89  ? 2323 LYS A CD    1 
ATOM   6937  C  CE    . LYS A 1 2323 ? 175.889 205.398 179.933 1.00 8.95  ? 2323 LYS A CE    1 
ATOM   6938  N  NZ    . LYS A 1 2323 ? 175.588 205.728 178.517 1.00 14.75 ? 2323 LYS A NZ    1 
ATOM   6939  N  N     . LEU A 1 2324 ? 178.163 208.428 186.368 1.00 0.57  ? 2324 LEU A N     1 
ATOM   6940  C  CA    . LEU A 1 2324 ? 178.673 209.554 187.134 1.00 0.43  ? 2324 LEU A CA    1 
ATOM   6941  C  C     . LEU A 1 2324 ? 179.703 209.063 188.138 1.00 0.27  ? 2324 LEU A C     1 
ATOM   6942  O  O     . LEU A 1 2324 ? 179.454 208.099 188.865 1.00 0.61  ? 2324 LEU A O     1 
ATOM   6943  C  CB    . LEU A 1 2324 ? 177.537 210.277 187.863 1.00 0.87  ? 2324 LEU A CB    1 
ATOM   6944  C  CG    . LEU A 1 2324 ? 176.712 211.280 187.059 1.00 0.65  ? 2324 LEU A CG    1 
ATOM   6945  C  CD1   . LEU A 1 2324 ? 175.477 211.680 187.842 1.00 0.98  ? 2324 LEU A CD1   1 
ATOM   6946  C  CD2   . LEU A 1 2324 ? 177.540 212.501 186.694 1.00 0.50  ? 2324 LEU A CD2   1 
ATOM   6947  N  N     . LEU A 1 2325 ? 180.854 209.724 188.172 1.00 0.24  ? 2325 LEU A N     1 
ATOM   6948  C  CA    . LEU A 1 2325 ? 181.830 209.545 189.240 1.00 0.15  ? 2325 LEU A CA    1 
ATOM   6949  C  C     . LEU A 1 2325 ? 181.566 210.627 190.277 1.00 0.24  ? 2325 LEU A C     1 
ATOM   6950  O  O     . LEU A 1 2325 ? 181.768 211.815 190.009 1.00 0.66  ? 2325 LEU A O     1 
ATOM   6951  C  CB    . LEU A 1 2325 ? 183.260 209.622 188.711 1.00 0.15  ? 2325 LEU A CB    1 
ATOM   6952  C  CG    . LEU A 1 2325 ? 184.361 209.554 189.774 1.00 0.10  ? 2325 LEU A CG    1 
ATOM   6953  C  CD1   . LEU A 1 2325 ? 184.437 208.170 190.396 1.00 0.08  ? 2325 LEU A CD1   1 
ATOM   6954  C  CD2   . LEU A 1 2325 ? 185.707 209.966 189.196 1.00 0.15  ? 2325 LEU A CD2   1 
ATOM   6955  N  N     . THR A 1 2326 ? 181.098 210.222 191.451 1.00 0.15  ? 2326 THR A N     1 
ATOM   6956  C  CA    . THR A 1 2326 ? 180.764 211.159 192.513 1.00 0.56  ? 2326 THR A CA    1 
ATOM   6957  C  C     . THR A 1 2326 ? 181.919 211.237 193.499 1.00 0.45  ? 2326 THR A C     1 
ATOM   6958  O  O     . THR A 1 2326 ? 182.427 210.208 193.955 1.00 0.66  ? 2326 THR A O     1 
ATOM   6959  C  CB    . THR A 1 2326 ? 179.476 210.752 193.231 1.00 0.57  ? 2326 THR A CB    1 
ATOM   6960  O  OG1   . THR A 1 2326 ? 179.649 209.467 193.836 1.00 2.00  ? 2326 THR A OG1   1 
ATOM   6961  C  CG2   . THR A 1 2326 ? 178.323 210.692 192.247 1.00 0.17  ? 2326 THR A CG2   1 
ATOM   6962  N  N     . LEU A 1 2327 ? 182.326 212.448 193.817 1.00 0.44  ? 2327 LEU A N     1 
ATOM   6963  C  CA    . LEU A 1 2327 ? 183.445 212.684 194.701 1.00 0.80  ? 2327 LEU A CA    1 
ATOM   6964  C  C     . LEU A 1 2327 ? 182.960 213.281 196.018 1.00 1.14  ? 2327 LEU A C     1 
ATOM   6965  O  O     . LEU A 1 2327 ? 181.937 213.972 196.051 1.00 1.69  ? 2327 LEU A O     1 
ATOM   6966  C  CB    . LEU A 1 2327 ? 184.455 213.629 194.040 1.00 2.60  ? 2327 LEU A CB    1 
ATOM   6967  C  CG    . LEU A 1 2327 ? 185.189 213.096 192.807 1.00 0.94  ? 2327 LEU A CG    1 
ATOM   6968  C  CD1   . LEU A 1 2327 ? 186.212 214.105 192.315 1.00 0.47  ? 2327 LEU A CD1   1 
ATOM   6969  C  CD2   . LEU A 1 2327 ? 185.843 211.755 193.090 1.00 0.18  ? 2327 LEU A CD2   1 
ATOM   6970  N  N     . PRO A 1 2328 ? 183.665 213.030 197.124 1.00 1.93  ? 2328 PRO A N     1 
ATOM   6971  C  CA    . PRO A 1 2328 ? 183.213 213.569 198.418 1.00 0.97  ? 2328 PRO A CA    1 
ATOM   6972  C  C     . PRO A 1 2328 ? 183.177 215.089 198.490 1.00 2.40  ? 2328 PRO A C     1 
ATOM   6973  O  O     . PRO A 1 2328 ? 182.501 215.627 199.375 1.00 6.57  ? 2328 PRO A O     1 
ATOM   6974  C  CB    . PRO A 1 2328 ? 184.218 212.974 199.415 1.00 0.90  ? 2328 PRO A CB    1 
ATOM   6975  C  CG    . PRO A 1 2328 ? 185.404 212.606 198.585 1.00 1.07  ? 2328 PRO A CG    1 
ATOM   6976  C  CD    . PRO A 1 2328 ? 184.816 212.128 197.293 1.00 1.31  ? 2328 PRO A CD    1 
ATOM   6977  N  N     . ASN A 1 2329 ? 183.869 215.805 197.603 1.00 1.43  ? 2329 ASN A N     1 
ATOM   6978  C  CA    . ASN A 1 2329 ? 183.744 217.258 197.578 1.00 1.50  ? 2329 ASN A CA    1 
ATOM   6979  C  C     . ASN A 1 2329 ? 182.464 217.732 196.901 1.00 1.37  ? 2329 ASN A C     1 
ATOM   6980  O  O     . ASN A 1 2329 ? 182.314 218.935 196.673 1.00 1.89  ? 2329 ASN A O     1 
ATOM   6981  C  CB    . ASN A 1 2329 ? 184.958 217.903 196.897 1.00 2.63  ? 2329 ASN A CB    1 
ATOM   6982  C  CG    . ASN A 1 2329 ? 185.079 217.542 195.421 1.00 2.23  ? 2329 ASN A CG    1 
ATOM   6983  O  OD1   . ASN A 1 2329 ? 184.303 216.752 194.889 1.00 3.17  ? 2329 ASN A OD1   1 
ATOM   6984  N  ND2   . ASN A 1 2329 ? 186.063 218.131 194.756 1.00 3.69  ? 2329 ASN A ND2   1 
ATOM   6985  N  N     . GLY A 1 2330 ? 181.546 216.822 196.573 1.00 1.22  ? 2330 GLY A N     1 
ATOM   6986  C  CA    . GLY A 1 2330 ? 180.301 217.171 195.928 1.00 1.01  ? 2330 GLY A CA    1 
ATOM   6987  C  C     . GLY A 1 2330 ? 180.349 217.194 194.416 1.00 1.69  ? 2330 GLY A C     1 
ATOM   6988  O  O     . GLY A 1 2330 ? 179.297 217.327 193.782 1.00 2.17  ? 2330 GLY A O     1 
ATOM   6989  N  N     . GLU A 1 2331 ? 181.530 217.063 193.823 1.00 1.94  ? 2331 GLU A N     1 
ATOM   6990  C  CA    . GLU A 1 2331 ? 181.674 217.112 192.377 1.00 1.85  ? 2331 GLU A CA    1 
ATOM   6991  C  C     . GLU A 1 2331 ? 181.201 215.806 191.748 1.00 1.53  ? 2331 GLU A C     1 
ATOM   6992  O  O     . GLU A 1 2331 ? 181.381 214.725 192.314 1.00 1.36  ? 2331 GLU A O     1 
ATOM   6993  C  CB    . GLU A 1 2331 ? 183.131 217.383 192.005 1.00 1.47  ? 2331 GLU A CB    1 
ATOM   6994  C  CG    . GLU A 1 2331 ? 183.318 218.252 190.783 1.00 3.79  ? 2331 GLU A CG    1 
ATOM   6995  C  CD    . GLU A 1 2331 ? 184.752 218.257 190.293 1.00 11.08 ? 2331 GLU A CD    1 
ATOM   6996  O  OE1   . GLU A 1 2331 ? 185.669 218.298 191.141 1.00 8.31  ? 2331 GLU A OE1   1 
ATOM   6997  O  OE2   . GLU A 1 2331 ? 184.961 218.222 189.063 1.00 18.23 ? 2331 GLU A OE2   1 
ATOM   6998  N  N     . ARG A 1 2332 ? 180.583 215.914 190.575 1.00 1.65  ? 2332 ARG A N     1 
ATOM   6999  C  CA    . ARG A 1 2332 ? 180.077 214.761 189.840 1.00 1.27  ? 2332 ARG A CA    1 
ATOM   7000  C  C     . ARG A 1 2332 ? 180.586 214.831 188.408 1.00 1.26  ? 2332 ARG A C     1 
ATOM   7001  O  O     . ARG A 1 2332 ? 180.294 215.791 187.690 1.00 2.37  ? 2332 ARG A O     1 
ATOM   7002  C  CB    . ARG A 1 2332 ? 178.546 214.716 189.878 1.00 1.63  ? 2332 ARG A CB    1 
ATOM   7003  C  CG    . ARG A 1 2332 ? 177.970 214.724 191.288 1.00 4.08  ? 2332 ARG A CG    1 
ATOM   7004  C  CD    . ARG A 1 2332 ? 176.523 215.174 191.314 1.00 3.00  ? 2332 ARG A CD    1 
ATOM   7005  N  NE    . ARG A 1 2332 ? 175.594 214.053 191.251 1.00 1.64  ? 2332 ARG A NE    1 
ATOM   7006  C  CZ    . ARG A 1 2332 ? 174.562 213.985 190.421 1.00 4.36  ? 2332 ARG A CZ    1 
ATOM   7007  N  NH1   . ARG A 1 2332 ? 174.291 214.964 189.574 1.00 2.79  ? 2332 ARG A NH1   1 
ATOM   7008  N  NH2   . ARG A 1 2332 ? 173.783 212.907 190.443 1.00 0.68  ? 2332 ARG A NH2   1 
ATOM   7009  N  N     . LEU A 1 2333 ? 181.340 213.816 187.997 1.00 1.07  ? 2333 LEU A N     1 
ATOM   7010  C  CA    . LEU A 1 2333 ? 181.941 213.768 186.670 1.00 0.67  ? 2333 LEU A CA    1 
ATOM   7011  C  C     . LEU A 1 2333 ? 181.159 212.792 185.800 1.00 0.53  ? 2333 LEU A C     1 
ATOM   7012  O  O     . LEU A 1 2333 ? 181.047 211.609 186.134 1.00 0.95  ? 2333 LEU A O     1 
ATOM   7013  C  CB    . LEU A 1 2333 ? 183.413 213.357 186.752 1.00 0.40  ? 2333 LEU A CB    1 
ATOM   7014  C  CG    . LEU A 1 2333 ? 184.424 214.357 187.326 1.00 0.72  ? 2333 LEU A CG    1 
ATOM   7015  C  CD1   . LEU A 1 2333 ? 184.374 214.407 188.846 1.00 1.30  ? 2333 LEU A CD1   1 
ATOM   7016  C  CD2   . LEU A 1 2333 ? 185.828 214.025 186.851 1.00 0.29  ? 2333 LEU A CD2   1 
ATOM   7017  N  N     . SER A 1 2334 ? 180.622 213.290 184.690 1.00 0.90  ? 2334 SER A N     1 
ATOM   7018  C  CA    . SER A 1 2334 ? 179.857 212.458 183.773 1.00 0.30  ? 2334 SER A CA    1 
ATOM   7019  C  C     . SER A 1 2334 ? 180.785 211.675 182.855 1.00 0.68  ? 2334 SER A C     1 
ATOM   7020  O  O     . SER A 1 2334 ? 181.774 212.207 182.347 1.00 2.38  ? 2334 SER A O     1 
ATOM   7021  C  CB    . SER A 1 2334 ? 178.907 213.315 182.937 1.00 0.69  ? 2334 SER A CB    1 
ATOM   7022  O  OG    . SER A 1 2334 ? 178.031 214.063 183.758 1.00 5.73  ? 2334 SER A OG    1 
ATOM   7023  N  N     . LEU A 1 2335 ? 180.459 210.408 182.643 1.00 0.63  ? 2335 LEU A N     1 
ATOM   7024  C  CA    . LEU A 1 2335 ? 181.234 209.580 181.731 1.00 0.47  ? 2335 LEU A CA    1 
ATOM   7025  C  C     . LEU A 1 2335 ? 180.874 209.926 180.291 1.00 1.52  ? 2335 LEU A C     1 
ATOM   7026  O  O     . LEU A 1 2335 ? 179.710 209.780 179.904 1.00 1.29  ? 2335 LEU A O     1 
ATOM   7027  C  CB    . LEU A 1 2335 ? 180.977 208.105 181.997 1.00 0.29  ? 2335 LEU A CB    1 
ATOM   7028  C  CG    . LEU A 1 2335 ? 182.064 207.144 181.517 1.00 0.43  ? 2335 LEU A CG    1 
ATOM   7029  C  CD1   . LEU A 1 2335 ? 183.358 207.381 182.280 1.00 0.16  ? 2335 LEU A CD1   1 
ATOM   7030  C  CD2   . LEU A 1 2335 ? 181.609 205.700 181.657 1.00 0.48  ? 2335 LEU A CD2   1 
ATOM   7031  N  N     . PRO A 1 2336 ? 181.824 210.384 179.475 1.00 0.59  ? 2336 PRO A N     1 
ATOM   7032  C  CA    . PRO A 1 2336 ? 181.497 210.707 178.088 1.00 0.40  ? 2336 PRO A CA    1 
ATOM   7033  C  C     . PRO A 1 2336 ? 181.221 209.446 177.291 1.00 0.74  ? 2336 PRO A C     1 
ATOM   7034  O  O     . PRO A 1 2336 ? 181.717 208.358 177.631 1.00 0.75  ? 2336 PRO A O     1 
ATOM   7035  C  CB    . PRO A 1 2336 ? 182.762 211.427 177.583 1.00 0.55  ? 2336 PRO A CB    1 
ATOM   7036  C  CG    . PRO A 1 2336 ? 183.576 211.724 178.803 1.00 0.34  ? 2336 PRO A CG    1 
ATOM   7037  C  CD    . PRO A 1 2336 ? 183.230 210.669 179.793 1.00 0.43  ? 2336 PRO A CD    1 
ATOM   7038  N  N     . PRO A 1 2337 ? 180.434 209.542 176.216 1.00 0.80  ? 2337 PRO A N     1 
ATOM   7039  C  CA    . PRO A 1 2337 ? 180.077 208.335 175.451 1.00 0.38  ? 2337 PRO A CA    1 
ATOM   7040  C  C     . PRO A 1 2337 ? 181.256 207.634 174.797 1.00 0.55  ? 2337 PRO A C     1 
ATOM   7041  O  O     . PRO A 1 2337 ? 181.146 206.444 174.481 1.00 1.04  ? 2337 PRO A O     1 
ATOM   7042  C  CB    . PRO A 1 2337 ? 179.094 208.870 174.401 1.00 0.59  ? 2337 PRO A CB    1 
ATOM   7043  C  CG    . PRO A 1 2337 ? 179.440 210.316 174.277 1.00 0.65  ? 2337 PRO A CG    1 
ATOM   7044  C  CD    . PRO A 1 2337 ? 179.786 210.744 175.667 1.00 1.03  ? 2337 PRO A CD    1 
ATOM   7045  N  N     . ASN A 1 2338 ? 182.374 208.321 174.582 1.00 0.53  ? 2338 ASN A N     1 
ATOM   7046  C  CA    . ASN A 1 2338 ? 183.529 207.717 173.930 1.00 0.26  ? 2338 ASN A CA    1 
ATOM   7047  C  C     . ASN A 1 2338 ? 184.425 206.953 174.895 1.00 0.23  ? 2338 ASN A C     1 
ATOM   7048  O  O     . ASN A 1 2338 ? 185.427 206.377 174.459 1.00 0.27  ? 2338 ASN A O     1 
ATOM   7049  C  CB    . ASN A 1 2338 ? 184.347 208.791 173.208 1.00 0.40  ? 2338 ASN A CB    1 
ATOM   7050  C  CG    . ASN A 1 2338 ? 185.080 209.709 174.166 1.00 0.86  ? 2338 ASN A CG    1 
ATOM   7051  O  OD1   . ASN A 1 2338 ? 184.479 210.295 175.065 1.00 1.00  ? 2338 ASN A OD1   1 
ATOM   7052  N  ND2   . ASN A 1 2338 ? 186.387 209.838 173.977 1.00 0.72  ? 2338 ASN A ND2   1 
ATOM   7053  N  N     . VAL A 1 2339 ? 184.093 206.928 176.181 1.00 0.21  ? 2339 VAL A N     1 
ATOM   7054  C  CA    . VAL A 1 2339 ? 184.921 206.301 177.203 1.00 0.17  ? 2339 VAL A CA    1 
ATOM   7055  C  C     . VAL A 1 2339 ? 184.347 204.932 177.536 1.00 0.07  ? 2339 VAL A C     1 
ATOM   7056  O  O     . VAL A 1 2339 ? 183.132 204.783 177.713 1.00 0.11  ? 2339 VAL A O     1 
ATOM   7057  C  CB    . VAL A 1 2339 ? 185.013 207.181 178.462 1.00 0.11  ? 2339 VAL A CB    1 
ATOM   7058  C  CG1   . VAL A 1 2339 ? 185.725 206.441 179.581 1.00 0.05  ? 2339 VAL A CG1   1 
ATOM   7059  C  CG2   . VAL A 1 2339 ? 185.727 208.481 178.146 1.00 0.09  ? 2339 VAL A CG2   1 
ATOM   7060  N  N     . ARG A 1 2340 ? 185.219 203.931 177.606 1.00 0.03  ? 2340 ARG A N     1 
ATOM   7061  C  CA    . ARG A 1 2340 ? 184.873 202.609 178.106 1.00 0.05  ? 2340 ARG A CA    1 
ATOM   7062  C  C     . ARG A 1 2340 ? 185.695 202.330 179.354 1.00 0.03  ? 2340 ARG A C     1 
ATOM   7063  O  O     . ARG A 1 2340 ? 186.908 202.555 179.365 1.00 0.04  ? 2340 ARG A O     1 
ATOM   7064  C  CB    . ARG A 1 2340 ? 185.136 201.528 177.053 1.00 0.07  ? 2340 ARG A CB    1 
ATOM   7065  C  CG    . ARG A 1 2340 ? 184.238 201.601 175.839 1.00 0.08  ? 2340 ARG A CG    1 
ATOM   7066  C  CD    . ARG A 1 2340 ? 182.774 201.460 176.207 1.00 0.13  ? 2340 ARG A CD    1 
ATOM   7067  N  NE    . ARG A 1 2340 ? 181.914 201.585 175.037 1.00 1.06  ? 2340 ARG A NE    1 
ATOM   7068  C  CZ    . ARG A 1 2340 ? 181.695 202.714 174.378 1.00 0.69  ? 2340 ARG A CZ    1 
ATOM   7069  N  NH1   . ARG A 1 2340 ? 182.215 203.863 174.780 1.00 0.19  ? 2340 ARG A NH1   1 
ATOM   7070  N  NH2   . ARG A 1 2340 ? 180.931 202.692 173.290 1.00 0.84  ? 2340 ARG A NH2   1 
ATOM   7071  N  N     . ILE A 1 2341 ? 185.039 201.851 180.403 1.00 0.03  ? 2341 ILE A N     1 
ATOM   7072  C  CA    . ILE A 1 2341 ? 185.718 201.406 181.612 1.00 0.03  ? 2341 ILE A CA    1 
ATOM   7073  C  C     . ILE A 1 2341 ? 185.871 199.896 181.525 1.00 0.04  ? 2341 ILE A C     1 
ATOM   7074  O  O     . ILE A 1 2341 ? 184.878 199.165 181.459 1.00 0.14  ? 2341 ILE A O     1 
ATOM   7075  C  CB    . ILE A 1 2341 ? 184.956 201.820 182.880 1.00 0.01  ? 2341 ILE A CB    1 
ATOM   7076  C  CG1   . ILE A 1 2341 ? 184.697 203.328 182.883 1.00 0.01  ? 2341 ILE A CG1   1 
ATOM   7077  C  CG2   . ILE A 1 2341 ? 185.733 201.418 184.120 1.00 0.02  ? 2341 ILE A CG2   1 
ATOM   7078  C  CD1   . ILE A 1 2341 ? 185.949 204.166 182.780 1.00 0.01  ? 2341 ILE A CD1   1 
ATOM   7079  N  N     . MET A 1 2342 ? 187.114 199.426 181.514 1.00 0.03  ? 2342 MET A N     1 
ATOM   7080  C  CA    . MET A 1 2342 ? 187.415 198.017 181.337 1.00 0.03  ? 2342 MET A CA    1 
ATOM   7081  C  C     . MET A 1 2342 ? 188.193 197.490 182.533 1.00 0.04  ? 2342 MET A C     1 
ATOM   7082  O  O     . MET A 1 2342 ? 188.975 198.212 183.156 1.00 0.03  ? 2342 MET A O     1 
ATOM   7083  C  CB    . MET A 1 2342 ? 188.213 197.776 180.055 1.00 0.02  ? 2342 MET A CB    1 
ATOM   7084  C  CG    . MET A 1 2342 ? 187.573 198.347 178.803 1.00 0.02  ? 2342 MET A CG    1 
ATOM   7085  S  SD    . MET A 1 2342 ? 188.302 197.673 177.301 1.00 7.99  ? 2342 MET A SD    1 
ATOM   7086  C  CE    . MET A 1 2342 ? 187.035 198.064 176.105 1.00 0.34  ? 2342 MET A CE    1 
ATOM   7087  N  N     . PHE A 1 2343 ? 187.964 196.217 182.848 1.00 0.04  ? 2343 PHE A N     1 
ATOM   7088  C  CA    . PHE A 1 2343 ? 188.657 195.565 183.988 1.00 0.03  ? 2343 PHE A CA    1 
ATOM   7089  C  C     . PHE A 1 2343 ? 189.260 194.266 183.496 1.00 0.03  ? 2343 PHE A C     1 
ATOM   7090  O  O     . PHE A 1 2343 ? 188.497 193.316 183.235 1.00 0.05  ? 2343 PHE A O     1 
ATOM   7091  C  CB    . PHE A 1 2343 ? 187.668 195.289 185.123 1.00 0.02  ? 2343 PHE A CB    1 
ATOM   7092  C  CG    . PHE A 1 2343 ? 186.990 196.505 185.738 1.00 0.04  ? 2343 PHE A CG    1 
ATOM   7093  C  CD1   . PHE A 1 2343 ? 185.837 197.039 185.175 1.00 0.06  ? 2343 PHE A CD1   1 
ATOM   7094  C  CD2   . PHE A 1 2343 ? 187.491 197.090 186.895 1.00 0.02  ? 2343 PHE A CD2   1 
ATOM   7095  C  CE1   . PHE A 1 2343 ? 185.217 198.140 185.743 1.00 0.03  ? 2343 PHE A CE1   1 
ATOM   7096  C  CE2   . PHE A 1 2343 ? 186.866 198.191 187.458 1.00 0.03  ? 2343 PHE A CE2   1 
ATOM   7097  C  CZ    . PHE A 1 2343 ? 185.732 198.712 186.881 1.00 0.03  ? 2343 PHE A CZ    1 
ATOM   7098  N  N     . GLU A 1 2344 ? 190.584 194.219 183.346 1.00 0.03  ? 2344 GLU A N     1 
ATOM   7099  C  CA    . GLU A 1 2344 ? 191.260 192.952 182.961 1.00 0.03  ? 2344 GLU A CA    1 
ATOM   7100  C  C     . GLU A 1 2344 ? 191.696 192.257 184.252 1.00 0.03  ? 2344 GLU A C     1 
ATOM   7101  O  O     . GLU A 1 2344 ? 192.592 192.787 184.937 1.00 0.06  ? 2344 GLU A O     1 
ATOM   7102  C  CB    . GLU A 1 2344 ? 192.440 193.203 182.027 1.00 0.04  ? 2344 GLU A CB    1 
ATOM   7103  C  CG    . GLU A 1 2344 ? 193.017 191.925 181.430 1.00 0.03  ? 2344 GLU A CG    1 
ATOM   7104  C  CD    . GLU A 1 2344 ? 194.411 192.158 180.891 1.00 0.03  ? 2344 GLU A CD    1 
ATOM   7105  O  OE1   . GLU A 1 2344 ? 194.571 193.050 180.034 1.00 0.05  ? 2344 GLU A OE1   1 
ATOM   7106  O  OE2   . GLU A 1 2344 ? 195.334 191.446 181.327 1.00 0.04  ? 2344 GLU A OE2   1 
ATOM   7107  N  N     . VAL A 1 2345 ? 191.077 191.124 184.573 1.00 0.07  ? 2345 VAL A N     1 
ATOM   7108  C  CA    . VAL A 1 2345 ? 191.361 190.456 185.873 1.00 0.13  ? 2345 VAL A CA    1 
ATOM   7109  C  C     . VAL A 1 2345 ? 191.526 188.945 185.669 1.00 0.11  ? 2345 VAL A C     1 
ATOM   7110  O  O     . VAL A 1 2345 ? 191.038 188.432 184.647 1.00 0.06  ? 2345 VAL A O     1 
ATOM   7111  C  CB    . VAL A 1 2345 ? 190.208 190.764 186.850 1.00 0.18  ? 2345 VAL A CB    1 
ATOM   7112  C  CG1   . VAL A 1 2345 ? 189.965 192.261 186.994 1.00 0.06  ? 2345 VAL A CG1   1 
ATOM   7113  C  CG2   . VAL A 1 2345 ? 188.922 190.051 186.451 1.00 0.08  ? 2345 VAL A CG2   1 
ATOM   7114  N  N     . GLN A 1 2346 ? 192.181 188.270 186.613 1.00 1.29  ? 2346 GLN A N     1 
ATOM   7115  C  CA    . GLN A 1 2346 ? 192.332 186.824 186.547 1.00 0.98  ? 2346 GLN A CA    1 
ATOM   7116  C  C     . GLN A 1 2346 ? 191.228 186.080 187.281 1.00 0.70  ? 2346 GLN A C     1 
ATOM   7117  O  O     . GLN A 1 2346 ? 191.009 184.896 187.004 1.00 0.77  ? 2346 GLN A O     1 
ATOM   7118  C  CB    . GLN A 1 2346 ? 193.692 186.393 187.108 1.00 0.67  ? 2346 GLN A CB    1 
ATOM   7119  C  CG    . GLN A 1 2346 ? 194.024 186.958 188.474 1.00 3.42  ? 2346 GLN A CG    1 
ATOM   7120  C  CD    . GLN A 1 2346 ? 195.247 186.307 189.090 1.00 7.18  ? 2346 GLN A CD    1 
ATOM   7121  O  OE1   . GLN A 1 2346 ? 195.735 185.289 188.600 1.00 5.72  ? 2346 GLN A OE1   1 
ATOM   7122  N  NE2   . GLN A 1 2346 ? 195.757 186.901 190.161 1.00 8.64  ? 2346 GLN A NE2   1 
ATOM   7123  N  N     . ASP A 1 2347 ? 190.528 186.744 188.194 1.00 1.30  ? 2347 ASP A N     1 
ATOM   7124  C  CA    . ASP A 1 2347 ? 189.456 186.121 188.957 1.00 2.16  ? 2347 ASP A CA    1 
ATOM   7125  C  C     . ASP A 1 2347 ? 188.582 187.224 189.532 1.00 2.49  ? 2347 ASP A C     1 
ATOM   7126  O  O     . ASP A 1 2347 ? 188.945 188.401 189.519 1.00 2.51  ? 2347 ASP A O     1 
ATOM   7127  C  CB    . ASP A 1 2347 ? 190.011 185.210 190.060 1.00 2.78  ? 2347 ASP A CB    1 
ATOM   7128  C  CG    . ASP A 1 2347 ? 190.863 185.962 191.067 1.00 6.99  ? 2347 ASP A CG    1 
ATOM   7129  O  OD1   . ASP A 1 2347 ? 190.301 186.712 191.892 1.00 8.71  ? 2347 ASP A OD1   1 
ATOM   7130  O  OD2   . ASP A 1 2347 ? 192.100 185.810 191.027 1.00 5.99  ? 2347 ASP A OD2   1 
ATOM   7131  N  N     . LEU A 1 2348 ? 187.416 186.829 190.034 1.00 4.89  ? 2348 LEU A N     1 
ATOM   7132  C  CA    . LEU A 1 2348 ? 186.480 187.744 190.673 1.00 2.66  ? 2348 LEU A CA    1 
ATOM   7133  C  C     . LEU A 1 2348 ? 185.986 187.172 191.990 1.00 4.78  ? 2348 LEU A C     1 
ATOM   7134  O  O     . LEU A 1 2348 ? 184.835 187.378 192.387 1.00 14.58 ? 2348 LEU A O     1 
ATOM   7135  C  CB    . LEU A 1 2348 ? 185.307 188.062 189.751 1.00 2.65  ? 2348 LEU A CB    1 
ATOM   7136  C  CG    . LEU A 1 2348 ? 185.571 189.062 188.623 1.00 3.45  ? 2348 LEU A CG    1 
ATOM   7137  C  CD1   . LEU A 1 2348 ? 184.317 189.273 187.800 1.00 1.96  ? 2348 LEU A CD1   1 
ATOM   7138  C  CD2   . LEU A 1 2348 ? 186.079 190.381 189.183 1.00 1.16  ? 2348 LEU A CD2   1 
ATOM   7139  N  N     . LYS A 1 2349 ? 186.854 186.452 192.701 1.00 6.06  ? 2349 LYS A N     1 
ATOM   7140  C  CA    . LYS A 1 2349 ? 186.451 185.779 193.928 1.00 6.11  ? 2349 LYS A CA    1 
ATOM   7141  C  C     . LYS A 1 2349 ? 186.217 186.732 195.093 1.00 5.57  ? 2349 LYS A C     1 
ATOM   7142  O  O     . LYS A 1 2349 ? 185.709 186.297 196.131 1.00 12.08 ? 2349 LYS A O     1 
ATOM   7143  C  CB    . LYS A 1 2349 ? 187.492 184.728 194.322 1.00 6.74  ? 2349 LYS A CB    1 
ATOM   7144  C  CG    . LYS A 1 2349 ? 188.908 185.247 194.425 1.00 5.93  ? 2349 LYS A CG    1 
ATOM   7145  C  CD    . LYS A 1 2349 ? 189.803 184.250 195.139 1.00 10.17 ? 2349 LYS A CD    1 
ATOM   7146  C  CE    . LYS A 1 2349 ? 189.265 183.914 196.520 1.00 10.50 ? 2349 LYS A CE    1 
ATOM   7147  N  NZ    . LYS A 1 2349 ? 190.235 183.116 197.315 1.00 17.34 ? 2349 LYS A NZ    1 
ATOM   7148  N  N     . TYR A 1 2350 ? 186.570 188.008 194.957 1.00 2.82  ? 2350 TYR A N     1 
ATOM   7149  C  CA    . TYR A 1 2350 ? 186.275 188.999 195.980 1.00 1.61  ? 2350 TYR A CA    1 
ATOM   7150  C  C     . TYR A 1 2350 ? 185.311 190.080 195.517 1.00 3.97  ? 2350 TYR A C     1 
ATOM   7151  O  O     . TYR A 1 2350 ? 184.894 190.901 196.340 1.00 9.17  ? 2350 TYR A O     1 
ATOM   7152  C  CB    . TYR A 1 2350 ? 187.570 189.653 196.487 1.00 2.73  ? 2350 TYR A CB    1 
ATOM   7153  C  CG    . TYR A 1 2350 ? 188.527 188.661 197.099 1.00 3.22  ? 2350 TYR A CG    1 
ATOM   7154  C  CD1   . TYR A 1 2350 ? 188.340 188.193 198.392 1.00 2.26  ? 2350 TYR A CD1   1 
ATOM   7155  C  CD2   . TYR A 1 2350 ? 189.609 188.176 196.377 1.00 3.94  ? 2350 TYR A CD2   1 
ATOM   7156  C  CE1   . TYR A 1 2350 ? 189.205 187.278 198.951 1.00 2.90  ? 2350 TYR A CE1   1 
ATOM   7157  C  CE2   . TYR A 1 2350 ? 190.481 187.262 196.929 1.00 2.81  ? 2350 TYR A CE2   1 
ATOM   7158  C  CZ    . TYR A 1 2350 ? 190.275 186.817 198.216 1.00 3.25  ? 2350 TYR A CZ    1 
ATOM   7159  O  OH    . TYR A 1 2350 ? 191.141 185.906 198.770 1.00 8.87  ? 2350 TYR A OH    1 
ATOM   7160  N  N     . ALA A 1 2351 ? 184.944 190.104 194.240 1.00 5.98  ? 2351 ALA A N     1 
ATOM   7161  C  CA    . ALA A 1 2351 ? 183.969 191.072 193.759 1.00 3.51  ? 2351 ALA A CA    1 
ATOM   7162  C  C     . ALA A 1 2351 ? 182.570 190.700 194.233 1.00 3.59  ? 2351 ALA A C     1 
ATOM   7163  O  O     . ALA A 1 2351 ? 182.210 189.522 194.297 1.00 4.62  ? 2351 ALA A O     1 
ATOM   7164  C  CB    . ALA A 1 2351 ? 184.004 191.148 192.234 1.00 2.22  ? 2351 ALA A CB    1 
ATOM   7165  N  N     . THR A 1 2352 ? 181.781 191.712 194.567 1.00 5.69  ? 2352 THR A N     1 
ATOM   7166  C  CA    . THR A 1 2352 ? 180.412 191.495 195.005 1.00 2.99  ? 2352 THR A CA    1 
ATOM   7167  C  C     . THR A 1 2352 ? 179.459 191.498 193.812 1.00 2.95  ? 2352 THR A C     1 
ATOM   7168  O  O     . THR A 1 2352 ? 179.828 191.828 192.683 1.00 2.50  ? 2352 THR A O     1 
ATOM   7169  C  CB    . THR A 1 2352 ? 179.994 192.556 196.024 1.00 3.86  ? 2352 THR A CB    1 
ATOM   7170  O  OG1   . THR A 1 2352 ? 180.061 193.854 195.422 1.00 9.17  ? 2352 THR A OG1   1 
ATOM   7171  C  CG2   . THR A 1 2352 ? 180.906 192.513 197.240 1.00 2.72  ? 2352 THR A CG2   1 
ATOM   7172  N  N     . LEU A 1 2353 ? 178.196 191.151 194.068 1.00 4.34  ? 2353 LEU A N     1 
ATOM   7173  C  CA    . LEU A 1 2353 ? 177.179 191.128 192.983 1.00 2.64  ? 2353 LEU A CA    1 
ATOM   7174  C  C     . LEU A 1 2353 ? 176.993 192.547 192.426 1.00 3.15  ? 2353 LEU A C     1 
ATOM   7175  O  O     . LEU A 1 2353 ? 176.817 192.687 191.197 1.00 2.05  ? 2353 LEU A O     1 
ATOM   7176  C  CB    . LEU A 1 2353 ? 175.874 190.560 193.538 1.00 3.08  ? 2353 LEU A CB    1 
ATOM   7177  C  CG    . LEU A 1 2353 ? 174.764 190.274 192.520 1.00 5.88  ? 2353 LEU A CG    1 
ATOM   7178  C  CD1   . LEU A 1 2353 ? 173.782 189.274 193.103 1.00 13.06 ? 2353 LEU A CD1   1 
ATOM   7179  C  CD2   . LEU A 1 2353 ? 174.034 191.544 192.121 1.00 10.79 ? 2353 LEU A CD2   1 
ATOM   7180  N  N     . ALA A 1 2354 ? 177.048 193.558 193.296 1.00 3.10  ? 2354 ALA A N     1 
ATOM   7181  C  CA    . ALA A 1 2354 ? 176.831 194.955 192.857 1.00 3.80  ? 2354 ALA A CA    1 
ATOM   7182  C  C     . ALA A 1 2354 ? 177.745 195.273 191.671 1.00 5.94  ? 2354 ALA A C     1 
ATOM   7183  O  O     . ALA A 1 2354 ? 177.272 195.898 190.700 1.00 4.58  ? 2354 ALA A O     1 
ATOM   7184  C  CB    . ALA A 1 2354 ? 177.078 195.892 194.011 1.00 3.71  ? 2354 ALA A CB    1 
ATOM   7185  N  N     . THR A 1 2355 ? 179.005 194.843 191.743 1.00 4.41  ? 2355 THR A N     1 
ATOM   7186  C  CA    . THR A 1 2355 ? 179.973 195.136 190.668 1.00 1.68  ? 2355 THR A CA    1 
ATOM   7187  C  C     . THR A 1 2355 ? 179.743 194.194 189.509 1.00 1.58  ? 2355 THR A C     1 
ATOM   7188  O  O     . THR A 1 2355 ? 179.714 194.678 188.358 1.00 2.09  ? 2355 THR A O     1 
ATOM   7189  C  CB    . THR A 1 2355 ? 181.393 195.019 191.222 1.00 1.10  ? 2355 THR A CB    1 
ATOM   7190  O  OG1   . THR A 1 2355 ? 181.471 195.974 192.274 1.00 3.26  ? 2355 THR A OG1   1 
ATOM   7191  C  CG2   . THR A 1 2355 ? 182.451 195.313 190.174 1.00 0.53  ? 2355 THR A CG2   1 
ATOM   7192  N  N     . VAL A 1 2356 ? 179.564 192.901 189.785 1.00 1.87  ? 2356 VAL A N     1 
ATOM   7193  C  CA    . VAL A 1 2356 ? 179.453 191.939 188.690 1.00 1.68  ? 2356 VAL A CA    1 
ATOM   7194  C  C     . VAL A 1 2356 ? 178.237 192.243 187.824 1.00 2.84  ? 2356 VAL A C     1 
ATOM   7195  O  O     . VAL A 1 2356 ? 178.301 192.169 186.592 1.00 3.71  ? 2356 VAL A O     1 
ATOM   7196  C  CB    . VAL A 1 2356 ? 179.417 190.502 189.243 1.00 3.25  ? 2356 VAL A CB    1 
ATOM   7197  C  CG1   . VAL A 1 2356 ? 179.191 189.499 188.125 1.00 2.67  ? 2356 VAL A CG1   1 
ATOM   7198  C  CG2   . VAL A 1 2356 ? 180.707 190.190 189.982 1.00 2.12  ? 2356 VAL A CG2   1 
ATOM   7199  N  N     . SER A 1 2357 ? 177.122 192.598 188.467 1.00 2.80  ? 2357 SER A N     1 
ATOM   7200  C  CA    . SER A 1 2357 ? 175.854 192.862 187.734 1.00 2.03  ? 2357 SER A CA    1 
ATOM   7201  C  C     . SER A 1 2357 ? 175.948 194.127 186.872 1.00 1.64  ? 2357 SER A C     1 
ATOM   7202  O  O     . SER A 1 2357 ? 175.167 194.233 185.905 1.00 2.09  ? 2357 SER A O     1 
ATOM   7203  C  CB    . SER A 1 2357 ? 174.703 192.968 188.700 1.00 2.55  ? 2357 SER A CB    1 
ATOM   7204  O  OG    . SER A 1 2357 ? 174.866 194.078 189.569 1.00 8.55  ? 2357 SER A OG    1 
ATOM   7205  N  N     . ARG A 1 2358 ? 176.860 195.042 187.196 1.00 1.60  ? 2358 ARG A N     1 
ATOM   7206  C  CA    . ARG A 1 2358 ? 176.916 196.338 186.468 1.00 1.92  ? 2358 ARG A CA    1 
ATOM   7207  C  C     . ARG A 1 2358 ? 177.891 196.285 185.284 1.00 1.66  ? 2358 ARG A C     1 
ATOM   7208  O  O     . ARG A 1 2358 ? 178.083 197.338 184.650 1.00 5.28  ? 2358 ARG A O     1 
ATOM   7209  C  CB    . ARG A 1 2358 ? 177.371 197.464 187.403 1.00 1.36  ? 2358 ARG A CB    1 
ATOM   7210  C  CG    . ARG A 1 2358 ? 176.364 198.010 188.402 1.00 1.22  ? 2358 ARG A CG    1 
ATOM   7211  C  CD    . ARG A 1 2358 ? 177.007 199.167 189.150 1.00 1.20  ? 2358 ARG A CD    1 
ATOM   7212  N  NE    . ARG A 1 2358 ? 176.080 199.929 189.993 1.00 1.86  ? 2358 ARG A NE    1 
ATOM   7213  C  CZ    . ARG A 1 2358 ? 175.437 199.457 191.051 1.00 0.98  ? 2358 ARG A CZ    1 
ATOM   7214  N  NH1   . ARG A 1 2358 ? 175.709 198.249 191.514 1.00 1.17  ? 2358 ARG A NH1   1 
ATOM   7215  N  NH2   . ARG A 1 2358 ? 174.529 200.203 191.650 1.00 1.33  ? 2358 ARG A NH2   1 
ATOM   7216  N  N     . CYS A 1 2359 ? 178.484 195.129 184.987 1.00 1.83  ? 2359 CYS A N     1 
ATOM   7217  C  CA    . CYS A 1 2359 ? 179.520 195.118 183.920 1.00 1.38  ? 2359 CYS A CA    1 
ATOM   7218  C  C     . CYS A 1 2359 ? 179.348 193.969 182.927 1.00 1.60  ? 2359 CYS A C     1 
ATOM   7219  O  O     . CYS A 1 2359 ? 179.071 192.838 183.378 1.00 9.11  ? 2359 CYS A O     1 
ATOM   7220  C  CB    . CYS A 1 2359 ? 180.920 194.961 184.505 1.00 1.22  ? 2359 CYS A CB    1 
ATOM   7221  S  SG    . CYS A 1 2359 ? 181.511 196.412 185.413 1.00 6.37  ? 2359 CYS A SG    1 
ATOM   7222  N  N     . GLY A 1 2360 ? 179.488 194.251 181.630 1.00 0.55  ? 2360 GLY A N     1 
ATOM   7223  C  CA    . GLY A 1 2360 ? 179.513 193.192 180.639 1.00 0.49  ? 2360 GLY A CA    1 
ATOM   7224  C  C     . GLY A 1 2360 ? 180.704 192.277 180.867 1.00 0.69  ? 2360 GLY A C     1 
ATOM   7225  O  O     . GLY A 1 2360 ? 181.803 192.726 181.197 1.00 0.45  ? 2360 GLY A O     1 
ATOM   7226  N  N     . MET A 1 2361 ? 180.479 190.981 180.703 1.00 1.40  ? 2361 MET A N     1 
ATOM   7227  C  CA    . MET A 1 2361 ? 181.486 189.977 181.008 1.00 0.57  ? 2361 MET A CA    1 
ATOM   7228  C  C     . MET A 1 2361 ? 181.915 189.266 179.737 1.00 0.22  ? 2361 MET A C     1 
ATOM   7229  O  O     . MET A 1 2361 ? 181.073 188.788 178.972 1.00 1.03  ? 2361 MET A O     1 
ATOM   7230  C  CB    . MET A 1 2361 ? 180.963 188.963 182.025 1.00 1.00  ? 2361 MET A CB    1 
ATOM   7231  C  CG    . MET A 1 2361 ? 180.673 189.544 183.390 1.00 2.25  ? 2361 MET A CG    1 
ATOM   7232  S  SD    . MET A 1 2361 ? 182.149 190.174 184.201 1.00 11.60 ? 2361 MET A SD    1 
ATOM   7233  C  CE    . MET A 1 2361 ? 181.425 190.974 185.624 1.00 5.50  ? 2361 MET A CE    1 
ATOM   7234  N  N     . VAL A 1 2362 ? 183.222 189.216 179.509 1.00 0.23  ? 2362 VAL A N     1 
ATOM   7235  C  CA    . VAL A 1 2362 ? 183.826 188.351 178.506 1.00 0.29  ? 2362 VAL A CA    1 
ATOM   7236  C  C     . VAL A 1 2362 ? 184.772 187.415 179.238 1.00 0.12  ? 2362 VAL A C     1 
ATOM   7237  O  O     . VAL A 1 2362 ? 185.760 187.864 179.831 1.00 0.09  ? 2362 VAL A O     1 
ATOM   7238  C  CB    . VAL A 1 2362 ? 184.567 189.142 177.417 1.00 0.13  ? 2362 VAL A CB    1 
ATOM   7239  C  CG1   . VAL A 1 2362 ? 185.055 188.201 176.331 1.00 0.20  ? 2362 VAL A CG1   1 
ATOM   7240  C  CG2   . VAL A 1 2362 ? 183.673 190.214 176.833 1.00 0.14  ? 2362 VAL A CG2   1 
ATOM   7241  N  N     . TRP A 1 2363 ? 184.469 186.123 179.208 1.00 0.19  ? 2363 TRP A N     1 
ATOM   7242  C  CA    . TRP A 1 2363 ? 185.253 185.120 179.912 1.00 0.12  ? 2363 TRP A CA    1 
ATOM   7243  C  C     . TRP A 1 2363 ? 186.311 184.549 178.983 1.00 0.05  ? 2363 TRP A C     1 
ATOM   7244  O  O     . TRP A 1 2363 ? 186.004 184.130 177.866 1.00 0.12  ? 2363 TRP A O     1 
ATOM   7245  C  CB    . TRP A 1 2363 ? 184.366 183.995 180.444 1.00 0.24  ? 2363 TRP A CB    1 
ATOM   7246  C  CG    . TRP A 1 2363 ? 185.135 182.760 180.800 1.00 0.08  ? 2363 TRP A CG    1 
ATOM   7247  C  CD1   . TRP A 1 2363 ? 185.255 181.627 180.054 1.00 0.12  ? 2363 TRP A CD1   1 
ATOM   7248  C  CD2   . TRP A 1 2363 ? 185.904 182.541 181.988 1.00 0.07  ? 2363 TRP A CD2   1 
ATOM   7249  N  NE1   . TRP A 1 2363 ? 186.044 180.713 180.703 1.00 0.18  ? 2363 TRP A NE1   1 
ATOM   7250  C  CE2   . TRP A 1 2363 ? 186.456 181.250 181.894 1.00 0.10  ? 2363 TRP A CE2   1 
ATOM   7251  C  CE3   . TRP A 1 2363 ? 186.173 183.309 183.124 1.00 0.08  ? 2363 TRP A CE3   1 
ATOM   7252  C  CZ2   . TRP A 1 2363 ? 187.261 180.708 182.892 1.00 0.11  ? 2363 TRP A CZ2   1 
ATOM   7253  C  CZ3   . TRP A 1 2363 ? 186.973 182.771 184.112 1.00 0.06  ? 2363 TRP A CZ3   1 
ATOM   7254  C  CH2   . TRP A 1 2363 ? 187.508 181.483 183.990 1.00 0.10  ? 2363 TRP A CH2   1 
ATOM   7255  N  N     . PHE A 1 2364 ? 187.551 184.536 179.449 1.00 0.05  ? 2364 PHE A N     1 
ATOM   7256  C  CA    . PHE A 1 2364 ? 188.649 183.898 178.746 1.00 0.06  ? 2364 PHE A CA    1 
ATOM   7257  C  C     . PHE A 1 2364 ? 189.026 182.634 179.503 1.00 0.11  ? 2364 PHE A C     1 
ATOM   7258  O  O     . PHE A 1 2364 ? 189.157 182.657 180.729 1.00 0.17  ? 2364 PHE A O     1 
ATOM   7259  C  CB    . PHE A 1 2364 ? 189.858 184.831 178.634 1.00 0.12  ? 2364 PHE A CB    1 
ATOM   7260  C  CG    . PHE A 1 2364 ? 189.662 185.981 177.684 1.00 0.01  ? 2364 PHE A CG    1 
ATOM   7261  C  CD1   . PHE A 1 2364 ? 188.743 186.981 177.962 1.00 0.02  ? 2364 PHE A CD1   1 
ATOM   7262  C  CD2   . PHE A 1 2364 ? 190.415 186.079 176.530 1.00 0.03  ? 2364 PHE A CD2   1 
ATOM   7263  C  CE1   . PHE A 1 2364 ? 188.570 188.036 177.103 1.00 0.02  ? 2364 PHE A CE1   1 
ATOM   7264  C  CE2   . PHE A 1 2364 ? 190.248 187.136 175.668 1.00 0.09  ? 2364 PHE A CE2   1 
ATOM   7265  C  CZ    . PHE A 1 2364 ? 189.322 188.116 175.953 1.00 0.02  ? 2364 PHE A CZ    1 
ATOM   7266  N  N     . SER A 1 2365 ? 189.168 181.534 178.780 1.00 0.86  ? 2365 SER A N     1 
ATOM   7267  C  CA    . SER A 1 2365 ? 189.698 180.309 179.350 1.00 1.38  ? 2365 SER A CA    1 
ATOM   7268  C  C     . SER A 1 2365 ? 191.133 180.115 178.885 1.00 2.98  ? 2365 SER A C     1 
ATOM   7269  O  O     . SER A 1 2365 ? 191.573 180.702 177.894 1.00 3.58  ? 2365 SER A O     1 
ATOM   7270  C  CB    . SER A 1 2365 ? 188.842 179.103 178.957 1.00 1.12  ? 2365 SER A CB    1 
ATOM   7271  O  OG    . SER A 1 2365 ? 188.915 178.851 177.567 1.00 3.92  ? 2365 SER A OG    1 
ATOM   7272  N  N     . GLU A 1 2366 ? 191.873 179.289 179.624 1.00 2.83  ? 2366 GLU A N     1 
ATOM   7273  C  CA    . GLU A 1 2366 ? 193.231 178.968 179.208 1.00 3.81  ? 2366 GLU A CA    1 
ATOM   7274  C  C     . GLU A 1 2366 ? 193.266 178.214 177.888 1.00 6.07  ? 2366 GLU A C     1 
ATOM   7275  O  O     . GLU A 1 2366 ? 194.321 178.169 177.247 1.00 15.46 ? 2366 GLU A O     1 
ATOM   7276  C  CB    . GLU A 1 2366 ? 193.938 178.163 180.299 1.00 6.47  ? 2366 GLU A CB    1 
ATOM   7277  C  CG    . GLU A 1 2366 ? 194.611 179.024 181.353 1.00 12.66 ? 2366 GLU A CG    1 
ATOM   7278  C  CD    . GLU A 1 2366 ? 195.453 178.218 182.325 1.00 22.53 ? 2366 GLU A CD    1 
ATOM   7279  O  OE1   . GLU A 1 2366 ? 194.901 177.318 182.991 1.00 21.73 ? 2366 GLU A OE1   1 
ATOM   7280  O  OE2   . GLU A 1 2366 ? 196.668 178.487 182.425 1.00 20.91 ? 2366 GLU A OE2   1 
ATOM   7281  N  N     . ASP A 1 2367 ? 192.145 177.629 177.468 1.00 5.17  ? 2367 ASP A N     1 
ATOM   7282  C  CA    . ASP A 1 2367 ? 192.075 176.977 176.167 1.00 3.90  ? 2367 ASP A CA    1 
ATOM   7283  C  C     . ASP A 1 2367 ? 191.950 177.982 175.030 1.00 3.51  ? 2367 ASP A C     1 
ATOM   7284  O  O     . ASP A 1 2367 ? 192.219 177.637 173.874 1.00 9.11  ? 2367 ASP A O     1 
ATOM   7285  C  CB    . ASP A 1 2367 ? 190.901 175.999 176.139 1.00 7.70  ? 2367 ASP A CB    1 
ATOM   7286  C  CG    . ASP A 1 2367 ? 191.122 174.802 177.041 1.00 19.06 ? 2367 ASP A CG    1 
ATOM   7287  O  OD1   . ASP A 1 2367 ? 192.293 174.419 177.245 1.00 20.58 ? 2367 ASP A OD1   1 
ATOM   7288  O  OD2   . ASP A 1 2367 ? 190.125 174.242 177.544 1.00 25.60 ? 2367 ASP A OD2   1 
ATOM   7289  N  N     . VAL A 1 2368 ? 191.544 179.215 175.333 1.00 4.01  ? 2368 VAL A N     1 
ATOM   7290  C  CA    . VAL A 1 2368 ? 191.437 180.246 174.303 1.00 2.30  ? 2368 VAL A CA    1 
ATOM   7291  C  C     . VAL A 1 2368 ? 192.804 180.535 173.698 1.00 2.66  ? 2368 VAL A C     1 
ATOM   7292  O  O     . VAL A 1 2368 ? 192.945 180.676 172.478 1.00 1.63  ? 2368 VAL A O     1 
ATOM   7293  C  CB    . VAL A 1 2368 ? 190.791 181.515 174.890 1.00 2.03  ? 2368 VAL A CB    1 
ATOM   7294  C  CG1   . VAL A 1 2368 ? 190.865 182.658 173.906 1.00 1.33  ? 2368 VAL A CG1   1 
ATOM   7295  C  CG2   . VAL A 1 2368 ? 189.349 181.238 175.273 1.00 4.57  ? 2368 VAL A CG2   1 
ATOM   7296  N  N     . LEU A 1 2369 ? 193.827 180.625 174.539 1.00 5.45  ? 2369 LEU A N     1 
ATOM   7297  C  CA    . LEU A 1 2369 ? 195.208 180.800 174.097 1.00 1.72  ? 2369 LEU A CA    1 
ATOM   7298  C  C     . LEU A 1 2369 ? 195.878 179.432 174.122 1.00 1.66  ? 2369 LEU A C     1 
ATOM   7299  O  O     . LEU A 1 2369 ? 196.220 178.917 175.187 1.00 6.43  ? 2369 LEU A O     1 
ATOM   7300  C  CB    . LEU A 1 2369 ? 195.932 181.800 174.990 1.00 1.47  ? 2369 LEU A CB    1 
ATOM   7301  C  CG    . LEU A 1 2369 ? 197.401 182.078 174.672 1.00 0.69  ? 2369 LEU A CG    1 
ATOM   7302  C  CD1   . LEU A 1 2369 ? 197.577 182.538 173.237 1.00 0.42  ? 2369 LEU A CD1   1 
ATOM   7303  C  CD2   . LEU A 1 2369 ? 197.948 183.098 175.640 1.00 0.32  ? 2369 LEU A CD2   1 
ATOM   7304  N  N     . SER A 1 2370 ? 196.058 178.841 172.946 1.00 1.61  ? 2370 SER A N     1 
ATOM   7305  C  CA    . SER A 1 2370 ? 196.682 177.533 172.849 1.00 2.57  ? 2370 SER A CA    1 
ATOM   7306  C  C     . SER A 1 2370 ? 198.204 177.654 172.907 1.00 3.25  ? 2370 SER A C     1 
ATOM   7307  O  O     . SER A 1 2370 ? 198.788 178.688 172.574 1.00 2.60  ? 2370 SER A O     1 
ATOM   7308  C  CB    . SER A 1 2370 ? 196.257 176.828 171.560 1.00 3.02  ? 2370 SER A CB    1 
ATOM   7309  O  OG    . SER A 1 2370 ? 196.867 177.418 170.428 1.00 2.00  ? 2370 SER A OG    1 
ATOM   7310  N  N     . THR A 1 2371 ? 198.845 176.569 173.346 1.00 2.95  ? 2371 THR A N     1 
ATOM   7311  C  CA    . THR A 1 2371 ? 200.302 176.555 173.434 1.00 2.35  ? 2371 THR A CA    1 
ATOM   7312  C  C     . THR A 1 2371 ? 200.944 176.665 172.057 1.00 3.52  ? 2371 THR A C     1 
ATOM   7313  O  O     . THR A 1 2371 ? 202.050 177.200 171.928 1.00 2.73  ? 2371 THR A O     1 
ATOM   7314  C  CB    . THR A 1 2371 ? 200.772 175.287 174.149 1.00 2.73  ? 2371 THR A CB    1 
ATOM   7315  O  OG1   . THR A 1 2371 ? 199.997 175.096 175.339 1.00 7.50  ? 2371 THR A OG1   1 
ATOM   7316  C  CG2   . THR A 1 2371 ? 202.232 175.399 174.531 1.00 2.65  ? 2371 THR A CG2   1 
ATOM   7317  N  N     . ASP A 1 2372 ? 200.261 176.179 171.020 1.00 6.62  ? 2372 ASP A N     1 
ATOM   7318  C  CA    . ASP A 1 2372 ? 200.745 176.361 169.656 1.00 3.75  ? 2372 ASP A CA    1 
ATOM   7319  C  C     . ASP A 1 2372 ? 200.801 177.839 169.287 1.00 3.29  ? 2372 ASP A C     1 
ATOM   7320  O  O     . ASP A 1 2372 ? 201.726 178.281 168.598 1.00 5.75  ? 2372 ASP A O     1 
ATOM   7321  C  CB    . ASP A 1 2372 ? 199.851 175.592 168.683 1.00 5.56  ? 2372 ASP A CB    1 
ATOM   7322  C  CG    . ASP A 1 2372 ? 200.327 175.688 167.249 1.00 16.89 ? 2372 ASP A CG    1 
ATOM   7323  O  OD1   . ASP A 1 2372 ? 201.555 175.748 167.030 1.00 25.17 ? 2372 ASP A OD1   1 
ATOM   7324  O  OD2   . ASP A 1 2372 ? 199.470 175.699 166.341 1.00 15.87 ? 2372 ASP A OD2   1 
ATOM   7325  N  N     . MET A 1 2373 ? 199.810 178.615 169.731 1.00 3.19  ? 2373 MET A N     1 
ATOM   7326  C  CA    . MET A 1 2373 ? 199.805 180.048 169.454 1.00 1.90  ? 2373 MET A CA    1 
ATOM   7327  C  C     . MET A 1 2373 ? 200.992 180.743 170.110 1.00 2.00  ? 2373 MET A C     1 
ATOM   7328  O  O     . MET A 1 2373 ? 201.638 181.598 169.494 1.00 2.13  ? 2373 MET A O     1 
ATOM   7329  C  CB    . MET A 1 2373 ? 198.493 180.662 169.938 1.00 3.05  ? 2373 MET A CB    1 
ATOM   7330  C  CG    . MET A 1 2373 ? 197.304 180.372 169.048 1.00 2.70  ? 2373 MET A CG    1 
ATOM   7331  S  SD    . MET A 1 2373 ? 195.741 180.538 169.927 1.00 4.45  ? 2373 MET A SD    1 
ATOM   7332  C  CE    . MET A 1 2373 ? 195.669 182.308 170.161 1.00 0.71  ? 2373 MET A CE    1 
ATOM   7333  N  N     . ILE A 1 2374 ? 201.291 180.386 171.361 1.00 2.90  ? 2374 ILE A N     1 
ATOM   7334  C  CA    . ILE A 1 2374 ? 202.427 180.977 172.062 1.00 1.57  ? 2374 ILE A CA    1 
ATOM   7335  C  C     . ILE A 1 2374 ? 203.732 180.604 171.373 1.00 2.56  ? 2374 ILE A C     1 
ATOM   7336  O  O     . ILE A 1 2374 ? 204.642 181.431 171.242 1.00 4.59  ? 2374 ILE A O     1 
ATOM   7337  C  CB    . ILE A 1 2374 ? 202.420 180.551 173.541 1.00 1.67  ? 2374 ILE A CB    1 
ATOM   7338  C  CG1   . ILE A 1 2374 ? 201.109 180.977 174.206 1.00 0.93  ? 2374 ILE A CG1   1 
ATOM   7339  C  CG2   . ILE A 1 2374 ? 203.621 181.134 174.276 1.00 1.26  ? 2374 ILE A CG2   1 
ATOM   7340  C  CD1   . ILE A 1 2374 ? 200.862 180.339 175.549 1.00 0.83  ? 2374 ILE A CD1   1 
ATOM   7341  N  N     . PHE A 1 2375 ? 203.845 179.353 170.922 1.00 1.82  ? 2375 PHE A N     1 
ATOM   7342  C  CA    . PHE A 1 2375 ? 205.044 178.928 170.207 1.00 1.77  ? 2375 PHE A CA    1 
ATOM   7343  C  C     . PHE A 1 2375 ? 205.212 179.698 168.904 1.00 3.24  ? 2375 PHE A C     1 
ATOM   7344  O  O     . PHE A 1 2375 ? 206.328 180.091 168.548 1.00 8.30  ? 2375 PHE A O     1 
ATOM   7345  C  CB    . PHE A 1 2375 ? 204.992 177.425 169.940 1.00 3.04  ? 2375 PHE A CB    1 
ATOM   7346  C  CG    . PHE A 1 2375 ? 205.162 176.587 171.172 1.00 2.55  ? 2375 PHE A CG    1 
ATOM   7347  C  CD1   . PHE A 1 2375 ? 205.653 177.141 172.341 1.00 2.13  ? 2375 PHE A CD1   1 
ATOM   7348  C  CD2   . PHE A 1 2375 ? 204.828 175.245 171.162 1.00 2.33  ? 2375 PHE A CD2   1 
ATOM   7349  C  CE1   . PHE A 1 2375 ? 205.807 176.374 173.472 1.00 3.11  ? 2375 PHE A CE1   1 
ATOM   7350  C  CE2   . PHE A 1 2375 ? 204.982 174.473 172.292 1.00 4.26  ? 2375 PHE A CE2   1 
ATOM   7351  C  CZ    . PHE A 1 2375 ? 205.474 175.036 173.447 1.00 3.31  ? 2375 PHE A CZ    1 
ATOM   7352  N  N     . ASN A 1 2376 ? 204.113 179.920 168.178 1.00 2.78  ? 2376 ASN A N     1 
ATOM   7353  C  CA    . ASN A 1 2376 ? 204.185 180.698 166.945 1.00 2.42  ? 2376 ASN A CA    1 
ATOM   7354  C  C     . ASN A 1 2376 ? 204.653 182.119 167.218 1.00 3.10  ? 2376 ASN A C     1 
ATOM   7355  O  O     . ASN A 1 2376 ? 205.464 182.670 166.465 1.00 4.14  ? 2376 ASN A O     1 
ATOM   7356  C  CB    . ASN A 1 2376 ? 202.822 180.722 166.253 1.00 3.10  ? 2376 ASN A CB    1 
ATOM   7357  C  CG    . ASN A 1 2376 ? 202.399 179.363 165.748 1.00 6.74  ? 2376 ASN A CG    1 
ATOM   7358  O  OD1   . ASN A 1 2376 ? 203.193 178.424 165.707 1.00 9.96  ? 2376 ASN A OD1   1 
ATOM   7359  N  ND2   . ASN A 1 2376 ? 201.133 179.247 165.366 1.00 6.55  ? 2376 ASN A ND2   1 
ATOM   7360  N  N     . ASN A 1 2377 ? 204.144 182.731 168.289 1.00 2.13  ? 2377 ASN A N     1 
ATOM   7361  C  CA    . ASN A 1 2377 ? 204.525 184.100 168.615 1.00 2.08  ? 2377 ASN A CA    1 
ATOM   7362  C  C     . ASN A 1 2377 ? 206.013 184.200 168.915 1.00 3.31  ? 2377 ASN A C     1 
ATOM   7363  O  O     . ASN A 1 2377 ? 206.684 185.131 168.458 1.00 4.66  ? 2377 ASN A O     1 
ATOM   7364  C  CB    . ASN A 1 2377 ? 203.699 184.598 169.801 1.00 2.03  ? 2377 ASN A CB    1 
ATOM   7365  C  CG    . ASN A 1 2377 ? 204.088 185.992 170.239 1.00 1.77  ? 2377 ASN A CG    1 
ATOM   7366  O  OD1   . ASN A 1 2377 ? 204.520 186.198 171.371 1.00 6.99  ? 2377 ASN A OD1   1 
ATOM   7367  N  ND2   . ASN A 1 2377 ? 203.933 186.961 169.347 1.00 1.65  ? 2377 ASN A ND2   1 
ATOM   7368  N  N     . PHE A 1 2378 ? 206.548 183.244 169.678 1.00 4.01  ? 2378 PHE A N     1 
ATOM   7369  C  CA    . PHE A 1 2378 ? 207.972 183.256 169.990 1.00 2.05  ? 2378 PHE A CA    1 
ATOM   7370  C  C     . PHE A 1 2378 ? 208.814 183.053 168.736 1.00 2.80  ? 2378 PHE A C     1 
ATOM   7371  O  O     . PHE A 1 2378 ? 209.847 183.708 168.561 1.00 3.38  ? 2378 PHE A O     1 
ATOM   7372  C  CB    . PHE A 1 2378 ? 208.281 182.188 171.039 1.00 2.16  ? 2378 PHE A CB    1 
ATOM   7373  C  CG    . PHE A 1 2378 ? 209.700 181.708 171.017 1.00 1.89  ? 2378 PHE A CG    1 
ATOM   7374  C  CD1   . PHE A 1 2378 ? 210.718 182.494 171.529 1.00 0.83  ? 2378 PHE A CD1   1 
ATOM   7375  C  CD2   . PHE A 1 2378 ? 210.019 180.469 170.487 1.00 2.50  ? 2378 PHE A CD2   1 
ATOM   7376  C  CE1   . PHE A 1 2378 ? 212.023 182.056 171.510 1.00 1.33  ? 2378 PHE A CE1   1 
ATOM   7377  C  CE2   . PHE A 1 2378 ? 211.324 180.027 170.465 1.00 2.97  ? 2378 PHE A CE2   1 
ATOM   7378  C  CZ    . PHE A 1 2378 ? 212.327 180.821 170.978 1.00 3.29  ? 2378 PHE A CZ    1 
ATOM   7379  N  N     . LEU A 1 2379 ? 208.390 182.148 167.853 1.00 2.83  ? 2379 LEU A N     1 
ATOM   7380  C  CA    . LEU A 1 2379 ? 209.147 181.902 166.630 1.00 4.35  ? 2379 LEU A CA    1 
ATOM   7381  C  C     . LEU A 1 2379 ? 209.035 183.068 165.656 1.00 6.14  ? 2379 LEU A C     1 
ATOM   7382  O  O     . LEU A 1 2379 ? 210.015 183.418 164.988 1.00 9.69  ? 2379 LEU A O     1 
ATOM   7383  C  CB    . LEU A 1 2379 ? 208.679 180.604 165.975 1.00 4.30  ? 2379 LEU A CB    1 
ATOM   7384  C  CG    . LEU A 1 2379 ? 209.178 179.329 166.654 1.00 4.04  ? 2379 LEU A CG    1 
ATOM   7385  C  CD1   . LEU A 1 2379 ? 208.649 178.101 165.949 1.00 7.12  ? 2379 LEU A CD1   1 
ATOM   7386  C  CD2   . LEU A 1 2379 ? 210.698 179.308 166.699 1.00 4.32  ? 2379 LEU A CD2   1 
ATOM   7387  N  N     . ALA A 1 2380 ? 207.852 183.677 165.553 1.00 4.83  ? 2380 ALA A N     1 
ATOM   7388  C  CA    . ALA A 1 2380 ? 207.688 184.818 164.657 1.00 2.50  ? 2380 ALA A CA    1 
ATOM   7389  C  C     . ALA A 1 2380 ? 208.559 185.988 165.094 1.00 3.98  ? 2380 ALA A C     1 
ATOM   7390  O  O     . ALA A 1 2380 ? 209.191 186.647 164.260 1.00 7.73  ? 2380 ALA A O     1 
ATOM   7391  C  CB    . ALA A 1 2380 ? 206.220 185.234 164.595 1.00 3.12  ? 2380 ALA A CB    1 
ATOM   7392  N  N     . ARG A 1 2381 ? 208.602 186.263 166.400 1.00 3.83  ? 2381 ARG A N     1 
ATOM   7393  C  CA    . ARG A 1 2381 ? 209.472 187.318 166.905 1.00 3.17  ? 2381 ARG A CA    1 
ATOM   7394  C  C     . ARG A 1 2381 ? 210.941 186.967 166.702 1.00 4.97  ? 2381 ARG A C     1 
ATOM   7395  O  O     . ARG A 1 2381 ? 211.754 187.838 166.372 1.00 5.84  ? 2381 ARG A O     1 
ATOM   7396  C  CB    . ARG A 1 2381 ? 209.181 187.581 168.382 1.00 2.41  ? 2381 ARG A CB    1 
ATOM   7397  C  CG    . ARG A 1 2381 ? 207.776 188.078 168.660 1.00 4.00  ? 2381 ARG A CG    1 
ATOM   7398  C  CD    . ARG A 1 2381 ? 207.468 188.064 170.147 1.00 2.74  ? 2381 ARG A CD    1 
ATOM   7399  N  NE    . ARG A 1 2381 ? 208.358 188.942 170.895 1.00 6.37  ? 2381 ARG A NE    1 
ATOM   7400  C  CZ    . ARG A 1 2381 ? 208.327 190.267 170.848 1.00 7.46  ? 2381 ARG A CZ    1 
ATOM   7401  N  NH1   . ARG A 1 2381 ? 207.429 190.915 170.124 1.00 7.45  ? 2381 ARG A NH1   1 
ATOM   7402  N  NH2   . ARG A 1 2381 ? 209.219 190.960 171.547 1.00 16.86 ? 2381 ARG A NH2   1 
ATOM   7403  N  N     . LEU A 1 2382 ? 211.298 185.695 166.899 1.00 3.44  ? 2382 LEU A N     1 
ATOM   7404  C  CA    . LEU A 1 2382 ? 212.683 185.277 166.716 1.00 4.91  ? 2382 LEU A CA    1 
ATOM   7405  C  C     . LEU A 1 2382 ? 213.137 185.447 165.273 1.00 8.42  ? 2382 LEU A C     1 
ATOM   7406  O  O     . LEU A 1 2382 ? 214.318 185.707 165.021 1.00 9.09  ? 2382 LEU A O     1 
ATOM   7407  C  CB    . LEU A 1 2382 ? 212.855 183.822 167.157 1.00 6.32  ? 2382 LEU A CB    1 
ATOM   7408  C  CG    . LEU A 1 2382 ? 214.289 183.290 167.200 1.00 8.86  ? 2382 LEU A CG    1 
ATOM   7409  C  CD1   . LEU A 1 2382 ? 215.125 184.071 168.199 1.00 6.13  ? 2382 LEU A CD1   1 
ATOM   7410  C  CD2   . LEU A 1 2382 ? 214.308 181.806 167.525 1.00 6.07  ? 2382 LEU A CD2   1 
ATOM   7411  N  N     . ARG A 1 2383 ? 212.219 185.313 164.318 1.00 4.91  ? 2383 ARG A N     1 
ATOM   7412  C  CA    . ARG A 1 2383 ? 212.550 185.431 162.906 1.00 4.95  ? 2383 ARG A CA    1 
ATOM   7413  C  C     . ARG A 1 2383 ? 212.484 186.860 162.385 1.00 5.75  ? 2383 ARG A C     1 
ATOM   7414  O  O     . ARG A 1 2383 ? 212.862 187.097 161.234 1.00 8.43  ? 2383 ARG A O     1 
ATOM   7415  C  CB    . ARG A 1 2383 ? 211.615 184.547 162.073 1.00 4.66  ? 2383 ARG A CB    1 
ATOM   7416  C  CG    . ARG A 1 2383 ? 211.903 183.065 162.196 1.00 7.28  ? 2383 ARG A CG    1 
ATOM   7417  C  CD    . ARG A 1 2383 ? 210.895 182.229 161.434 1.00 6.24  ? 2383 ARG A CD    1 
ATOM   7418  N  NE    . ARG A 1 2383 ? 211.413 180.897 161.146 1.00 7.70  ? 2383 ARG A NE    1 
ATOM   7419  C  CZ    . ARG A 1 2383 ? 210.880 179.770 161.599 1.00 7.43  ? 2383 ARG A CZ    1 
ATOM   7420  N  NH1   . ARG A 1 2383 ? 209.803 179.775 162.366 1.00 5.48  ? 2383 ARG A NH1   1 
ATOM   7421  N  NH2   . ARG A 1 2383 ? 211.446 178.611 161.278 1.00 8.07  ? 2383 ARG A NH2   1 
ATOM   7422  N  N     . SER A 1 2384 ? 212.019 187.806 163.186 1.00 5.99  ? 2384 SER A N     1 
ATOM   7423  C  CA    . SER A 1 2384 ? 211.846 189.166 162.691 1.00 5.75  ? 2384 SER A CA    1 
ATOM   7424  C  C     . SER A 1 2384 ? 212.551 190.219 163.534 1.00 9.48  ? 2384 SER A C     1 
ATOM   7425  O  O     . SER A 1 2384 ? 213.108 191.166 162.979 1.00 12.85 ? 2384 SER A O     1 
ATOM   7426  C  CB    . SER A 1 2384 ? 210.350 189.498 162.600 1.00 7.49  ? 2384 SER A CB    1 
ATOM   7427  O  OG    . SER A 1 2384 ? 209.652 188.515 161.856 1.00 16.79 ? 2384 SER A OG    1 
ATOM   7428  N  N     . ILE A 1 2385 ? 212.541 190.081 164.853 1.00 8.59  ? 2385 ILE A N     1 
ATOM   7429  C  CA    . ILE A 1 2385 ? 213.105 191.080 165.757 1.00 8.33  ? 2385 ILE A CA    1 
ATOM   7430  C  C     . ILE A 1 2385 ? 214.529 190.659 166.100 1.00 11.46 ? 2385 ILE A C     1 
ATOM   7431  O  O     . ILE A 1 2385 ? 214.717 189.598 166.712 1.00 10.44 ? 2385 ILE A O     1 
ATOM   7432  C  CB    . ILE A 1 2385 ? 212.258 191.239 167.027 1.00 8.76  ? 2385 ILE A CB    1 
ATOM   7433  C  CG1   . ILE A 1 2385 ? 210.788 191.449 166.660 1.00 5.35  ? 2385 ILE A CG1   1 
ATOM   7434  C  CG2   . ILE A 1 2385 ? 212.782 192.390 167.871 1.00 5.12  ? 2385 ILE A CG2   1 
ATOM   7435  C  CD1   . ILE A 1 2385 ? 209.865 191.513 167.852 1.00 5.26  ? 2385 ILE A CD1   1 
ATOM   7436  N  N     . PRO A 1 2386 ? 215.543 191.439 165.732 1.00 14.20 ? 2386 PRO A N     1 
ATOM   7437  C  CA    . PRO A 1 2386 ? 216.916 191.076 166.100 1.00 12.21 ? 2386 PRO A CA    1 
ATOM   7438  C  C     . PRO A 1 2386 ? 217.158 191.295 167.584 1.00 13.75 ? 2386 PRO A C     1 
ATOM   7439  O  O     . PRO A 1 2386 ? 216.678 192.264 168.176 1.00 25.14 ? 2386 PRO A O     1 
ATOM   7440  C  CB    . PRO A 1 2386 ? 217.776 192.015 165.245 1.00 16.66 ? 2386 PRO A CB    1 
ATOM   7441  C  CG    . PRO A 1 2386 ? 216.829 192.656 164.260 1.00 11.80 ? 2386 PRO A CG    1 
ATOM   7442  C  CD    . PRO A 1 2386 ? 215.496 192.662 164.922 1.00 8.28  ? 2386 PRO A CD    1 
ATOM   7443  N  N     . LEU A 1 2387 ? 217.907 190.372 168.186 1.00 12.43 ? 2387 LEU A N     1 
ATOM   7444  C  CA    . LEU A 1 2387 ? 218.214 190.468 169.606 1.00 9.63  ? 2387 LEU A CA    1 
ATOM   7445  C  C     . LEU A 1 2387 ? 219.328 191.461 169.907 1.00 15.20 ? 2387 LEU A C     1 
ATOM   7446  O  O     . LEU A 1 2387 ? 219.395 191.967 171.033 1.00 17.12 ? 2387 LEU A O     1 
ATOM   7447  C  CB    . LEU A 1 2387 ? 218.594 189.091 170.156 1.00 13.94 ? 2387 LEU A CB    1 
ATOM   7448  C  CG    . LEU A 1 2387 ? 217.523 188.001 170.096 1.00 12.04 ? 2387 LEU A CG    1 
ATOM   7449  C  CD1   . LEU A 1 2387 ? 218.157 186.631 170.249 1.00 9.29  ? 2387 LEU A CD1   1 
ATOM   7450  C  CD2   . LEU A 1 2387 ? 216.457 188.225 171.155 1.00 5.23  ? 2387 LEU A CD2   1 
ATOM   7451  N  N     . ASP A 1 2388 ? 220.200 191.747 168.936 1.00 21.61 ? 2388 ASP A N     1 
ATOM   7452  C  CA    . ASP A 1 2388 ? 221.324 192.645 169.191 1.00 18.04 ? 2388 ASP A CA    1 
ATOM   7453  C  C     . ASP A 1 2388 ? 220.850 194.062 169.489 1.00 25.47 ? 2388 ASP A C     1 
ATOM   7454  O  O     . ASP A 1 2388 ? 221.392 194.727 170.380 1.00 30.18 ? 2388 ASP A O     1 
ATOM   7455  C  CB    . ASP A 1 2388 ? 222.291 192.632 168.007 1.00 16.23 ? 2388 ASP A CB    1 
ATOM   7456  C  CG    . ASP A 1 2388 ? 221.625 193.011 166.700 1.00 30.47 ? 2388 ASP A CG    1 
ATOM   7457  O  OD1   . ASP A 1 2388 ? 220.710 192.284 166.267 1.00 32.82 ? 2388 ASP A OD1   1 
ATOM   7458  O  OD2   . ASP A 1 2388 ? 222.017 194.037 166.105 1.00 41.17 ? 2388 ASP A OD2   1 
ATOM   7459  N  N     . GLU A 1 2389 ? 219.843 194.540 168.764 1.00 23.88 ? 2389 GLU A N     1 
ATOM   7460  C  CA    . GLU A 1 2389 ? 219.295 195.871 168.996 1.00 31.17 ? 2389 GLU A CA    1 
ATOM   7461  C  C     . GLU A 1 2389 ? 217.911 196.009 168.372 1.00 24.66 ? 2389 GLU A C     1 
ATOM   7462  O  O     . GLU A 1 2389 ? 217.644 195.469 167.298 0.00 21.55 ? 2389 GLU A O     1 
ATOM   7463  C  CB    . GLU A 1 2389 ? 220.234 196.945 168.436 1.00 29.92 ? 2389 GLU A CB    1 
ATOM   7464  C  CG    . GLU A 1 2389 ? 219.726 198.378 168.574 1.00 29.77 ? 2389 GLU A CG    1 
ATOM   7465  C  CD    . GLU A 1 2389 ? 219.696 198.869 170.012 1.00 40.30 ? 2389 GLU A CD    1 
ATOM   7466  O  OE1   . GLU A 1 2389 ? 218.877 198.364 170.809 1.00 40.99 ? 2389 GLU A OE1   1 
ATOM   7467  O  OE2   . GLU A 1 2389 ? 220.499 199.766 170.348 1.00 38.91 ? 2389 GLU A OE2   1 
ATOM   7468  N  N     . SER A 1 2410 ? 220.636 190.830 158.658 1.00 20.88 ? 2410 SER A N     1 
ATOM   7469  C  CA    . SER A 1 2410 ? 221.458 191.068 159.838 1.00 19.98 ? 2410 SER A CA    1 
ATOM   7470  C  C     . SER A 1 2410 ? 222.156 189.790 160.275 1.00 22.24 ? 2410 SER A C     1 
ATOM   7471  O  O     . SER A 1 2410 ? 221.544 188.723 160.300 1.00 20.14 ? 2410 SER A O     1 
ATOM   7472  C  CB    . SER A 1 2410 ? 220.609 191.620 160.983 1.00 19.54 ? 2410 SER A CB    1 
ATOM   7473  O  OG    . SER A 1 2410 ? 221.377 191.756 162.167 1.00 19.95 ? 2410 SER A OG    1 
ATOM   7474  N  N     . PRO A 1 2411 ? 223.444 189.894 160.611 1.00 21.35 ? 2411 PRO A N     1 
ATOM   7475  C  CA    . PRO A 1 2411 ? 224.167 188.705 161.087 1.00 20.40 ? 2411 PRO A CA    1 
ATOM   7476  C  C     . PRO A 1 2411 ? 223.557 188.101 162.338 1.00 16.34 ? 2411 PRO A C     1 
ATOM   7477  O  O     . PRO A 1 2411 ? 223.573 186.873 162.495 1.00 20.64 ? 2411 PRO A O     1 
ATOM   7478  C  CB    . PRO A 1 2411 ? 225.584 189.237 161.340 1.00 14.98 ? 2411 PRO A CB    1 
ATOM   7479  C  CG    . PRO A 1 2411 ? 225.402 190.699 161.566 1.00 17.23 ? 2411 PRO A CG    1 
ATOM   7480  C  CD    . PRO A 1 2411 ? 224.274 191.108 160.668 1.00 15.68 ? 2411 PRO A CD    1 
ATOM   7481  N  N     . MET A 1 2412 ? 223.015 188.927 163.233 1.00 14.07 ? 2412 MET A N     1 
ATOM   7482  C  CA    . MET A 1 2412 ? 222.335 188.397 164.410 1.00 15.88 ? 2412 MET A CA    1 
ATOM   7483  C  C     . MET A 1 2412 ? 220.986 187.792 164.039 1.00 13.98 ? 2412 MET A C     1 
ATOM   7484  O  O     . MET A 1 2412 ? 220.632 186.709 164.518 1.00 12.70 ? 2412 MET A O     1 
ATOM   7485  C  CB    . MET A 1 2412 ? 222.164 189.499 165.454 1.00 16.45 ? 2412 MET A CB    1 
ATOM   7486  C  CG    . MET A 1 2412 ? 221.607 189.020 166.778 1.00 17.95 ? 2412 MET A CG    1 
ATOM   7487  S  SD    . MET A 1 2412 ? 222.601 187.705 167.505 1.00 26.27 ? 2412 MET A SD    1 
ATOM   7488  C  CE    . MET A 1 2412 ? 221.326 186.621 168.128 1.00 12.56 ? 2412 MET A CE    1 
ATOM   7489  N  N     . LEU A 1 2413 ? 220.221 188.477 163.184 1.00 14.74 ? 2413 LEU A N     1 
ATOM   7490  C  CA    . LEU A 1 2413 ? 218.946 187.939 162.721 1.00 12.58 ? 2413 LEU A CA    1 
ATOM   7491  C  C     . LEU A 1 2413 ? 219.138 186.657 161.922 1.00 12.66 ? 2413 LEU A C     1 
ATOM   7492  O  O     . LEU A 1 2413 ? 218.312 185.741 162.005 1.00 15.41 ? 2413 LEU A O     1 
ATOM   7493  C  CB    . LEU A 1 2413 ? 218.205 188.984 161.890 1.00 13.64 ? 2413 LEU A CB    1 
ATOM   7494  C  CG    . LEU A 1 2413 ? 216.683 188.852 161.831 1.00 11.53 ? 2413 LEU A CG    1 
ATOM   7495  C  CD1   . LEU A 1 2413 ? 216.030 189.343 163.105 1.00 10.99 ? 2413 LEU A CD1   1 
ATOM   7496  C  CD2   . LEU A 1 2413 ? 216.152 189.620 160.638 1.00 13.81 ? 2413 LEU A CD2   1 
ATOM   7497  N  N     . GLN A 1 2414 ? 220.213 186.577 161.137 1.00 15.28 ? 2414 GLN A N     1 
ATOM   7498  C  CA    . GLN A 1 2414 ? 220.478 185.363 160.373 1.00 14.69 ? 2414 GLN A CA    1 
ATOM   7499  C  C     . GLN A 1 2414 ? 220.710 184.172 161.293 1.00 15.75 ? 2414 GLN A C     1 
ATOM   7500  O  O     . GLN A 1 2414 ? 220.303 183.048 160.979 1.00 21.62 ? 2414 GLN A O     1 
ATOM   7501  C  CB    . GLN A 1 2414 ? 221.679 185.574 159.449 1.00 19.06 ? 2414 GLN A CB    1 
ATOM   7502  C  CG    . GLN A 1 2414 ? 221.816 184.569 158.296 1.00 19.65 ? 2414 GLN A CG    1 
ATOM   7503  C  CD    . GLN A 1 2414 ? 220.494 184.114 157.685 1.00 19.74 ? 2414 GLN A CD    1 
ATOM   7504  O  OE1   . GLN A 1 2414 ? 219.521 184.867 157.616 1.00 20.08 ? 2414 GLN A OE1   1 
ATOM   7505  N  NE2   . GLN A 1 2414 ? 220.459 182.865 157.240 1.00 23.19 ? 2414 GLN A NE2   1 
ATOM   7506  N  N     . ILE A 1 2415 ? 221.380 184.394 162.426 1.00 14.11 ? 2415 ILE A N     1 
ATOM   7507  C  CA    . ILE A 1 2415 ? 221.554 183.323 163.402 1.00 13.16 ? 2415 ILE A CA    1 
ATOM   7508  C  C     . ILE A 1 2415 ? 220.212 182.917 163.994 1.00 12.62 ? 2415 ILE A C     1 
ATOM   7509  O  O     . ILE A 1 2415 ? 219.913 181.725 164.131 1.00 16.96 ? 2415 ILE A O     1 
ATOM   7510  C  CB    . ILE A 1 2415 ? 222.551 183.747 164.494 1.00 17.19 ? 2415 ILE A CB    1 
ATOM   7511  C  CG1   . ILE A 1 2415 ? 223.968 183.795 163.926 1.00 11.93 ? 2415 ILE A CG1   1 
ATOM   7512  C  CG2   . ILE A 1 2415 ? 222.482 182.801 165.685 1.00 11.53 ? 2415 ILE A CG2   1 
ATOM   7513  C  CD1   . ILE A 1 2415 ? 225.006 184.215 164.932 1.00 10.34 ? 2415 ILE A CD1   1 
ATOM   7514  N  N     . GLN A 1 2416 ? 219.382 183.899 164.352 1.00 11.77 ? 2416 GLN A N     1 
ATOM   7515  C  CA    . GLN A 1 2416 ? 218.070 183.596 164.913 1.00 5.98  ? 2416 GLN A CA    1 
ATOM   7516  C  C     . GLN A 1 2416 ? 217.198 182.852 163.908 1.00 10.48 ? 2416 GLN A C     1 
ATOM   7517  O  O     . GLN A 1 2416 ? 216.492 181.905 164.272 1.00 10.42 ? 2416 GLN A O     1 
ATOM   7518  C  CB    . GLN A 1 2416 ? 217.382 184.881 165.368 1.00 7.63  ? 2416 GLN A CB    1 
ATOM   7519  C  CG    . GLN A 1 2416 ? 218.168 185.695 166.381 1.00 8.20  ? 2416 GLN A CG    1 
ATOM   7520  C  CD    . GLN A 1 2416 ? 217.628 187.103 166.545 1.00 7.88  ? 2416 GLN A CD    1 
ATOM   7521  O  OE1   . GLN A 1 2416 ? 218.378 188.042 166.798 1.00 13.46 ? 2416 GLN A OE1   1 
ATOM   7522  N  NE2   . GLN A 1 2416 ? 216.318 187.253 166.402 1.00 10.16 ? 2416 GLN A NE2   1 
ATOM   7523  N  N     . ARG A 1 2417 ? 217.234 183.268 162.640 1.00 13.61 ? 2417 ARG A N     1 
ATOM   7524  C  CA    . ARG A 1 2417 ? 216.406 182.625 161.626 1.00 11.88 ? 2417 ARG A CA    1 
ATOM   7525  C  C     . ARG A 1 2417 ? 216.814 181.174 161.411 1.00 10.82 ? 2417 ARG A C     1 
ATOM   7526  O  O     . ARG A 1 2417 ? 215.958 180.288 161.323 1.00 12.30 ? 2417 ARG A O     1 
ATOM   7527  C  CB    . ARG A 1 2417 ? 216.481 183.408 160.315 1.00 10.93 ? 2417 ARG A CB    1 
ATOM   7528  C  CG    . ARG A 1 2417 ? 215.747 184.732 160.359 1.00 11.31 ? 2417 ARG A CG    1 
ATOM   7529  C  CD    . ARG A 1 2417 ? 215.333 185.189 158.976 1.00 12.05 ? 2417 ARG A CD    1 
ATOM   7530  N  NE    . ARG A 1 2417 ? 214.472 186.363 159.037 1.00 11.31 ? 2417 ARG A NE    1 
ATOM   7531  C  CZ    . ARG A 1 2417 ? 214.682 187.483 158.359 1.00 9.78  ? 2417 ARG A CZ    1 
ATOM   7532  N  NH1   . ARG A 1 2417 ? 215.714 187.615 157.543 1.00 11.87 ? 2417 ARG A NH1   1 
ATOM   7533  N  NH2   . ARG A 1 2417 ? 213.834 188.497 158.505 1.00 9.46  ? 2417 ARG A NH2   1 
ATOM   7534  N  N     . ASP A 1 2418 ? 218.121 180.911 161.321 1.00 15.30 ? 2418 ASP A N     1 
ATOM   7535  C  CA    . ASP A 1 2418 ? 218.585 179.532 161.206 1.00 12.81 ? 2418 ASP A CA    1 
ATOM   7536  C  C     . ASP A 1 2418 ? 218.266 178.739 162.466 1.00 11.37 ? 2418 ASP A C     1 
ATOM   7537  O  O     . ASP A 1 2418 ? 217.897 177.562 162.387 1.00 10.20 ? 2418 ASP A O     1 
ATOM   7538  C  CB    . ASP A 1 2418 ? 220.085 179.500 160.915 1.00 16.11 ? 2418 ASP A CB    1 
ATOM   7539  C  CG    . ASP A 1 2418 ? 220.422 180.015 159.531 1.00 29.21 ? 2418 ASP A CG    1 
ATOM   7540  O  OD1   . ASP A 1 2418 ? 219.577 179.881 158.622 1.00 32.15 ? 2418 ASP A OD1   1 
ATOM   7541  O  OD2   . ASP A 1 2418 ? 221.537 180.547 159.349 1.00 31.99 ? 2418 ASP A OD2   1 
ATOM   7542  N  N     . ALA A 1 2419 ? 218.407 179.365 163.635 1.00 11.21 ? 2419 ALA A N     1 
ATOM   7543  C  CA    . ALA A 1 2419 ? 218.060 178.694 164.884 1.00 10.42 ? 2419 ALA A CA    1 
ATOM   7544  C  C     . ALA A 1 2419 ? 216.562 178.433 164.974 1.00 10.15 ? 2419 ALA A C     1 
ATOM   7545  O  O     . ALA A 1 2419 ? 216.136 177.415 165.532 1.00 13.37 ? 2419 ALA A O     1 
ATOM   7546  C  CB    . ALA A 1 2419 ? 218.536 179.525 166.074 1.00 9.32  ? 2419 ALA A CB    1 
ATOM   7547  N  N     . ALA A 1 2420 ? 215.747 179.346 164.437 1.00 10.64 ? 2420 ALA A N     1 
ATOM   7548  C  CA    . ALA A 1 2420 ? 214.302 179.142 164.434 1.00 9.78  ? 2420 ALA A CA    1 
ATOM   7549  C  C     . ALA A 1 2420 ? 213.920 177.916 163.617 1.00 9.25  ? 2420 ALA A C     1 
ATOM   7550  O  O     . ALA A 1 2420 ? 213.017 177.163 163.999 1.00 9.70  ? 2420 ALA A O     1 
ATOM   7551  C  CB    . ALA A 1 2420 ? 213.597 180.385 163.897 1.00 7.08  ? 2420 ALA A CB    1 
ATOM   7552  N  N     . THR A 1 2421 ? 214.597 177.702 162.485 1.00 7.75  ? 2421 THR A N     1 
ATOM   7553  C  CA    . THR A 1 2421 ? 214.333 176.519 161.675 1.00 8.73  ? 2421 THR A CA    1 
ATOM   7554  C  C     . THR A 1 2421 ? 214.667 175.246 162.437 1.00 11.25 ? 2421 THR A C     1 
ATOM   7555  O  O     . THR A 1 2421 ? 213.955 174.241 162.329 1.00 17.53 ? 2421 THR A O     1 
ATOM   7556  C  CB    . THR A 1 2421 ? 215.128 176.588 160.370 1.00 12.11 ? 2421 THR A CB    1 
ATOM   7557  O  OG1   . THR A 1 2421 ? 214.904 177.854 159.736 1.00 12.55 ? 2421 THR A OG1   1 
ATOM   7558  C  CG2   . THR A 1 2421 ? 214.705 175.475 159.428 1.00 14.44 ? 2421 THR A CG2   1 
ATOM   7559  N  N     . ILE A 1 2422 ? 215.752 175.269 163.213 1.00 8.28  ? 2422 ILE A N     1 
ATOM   7560  C  CA    . ILE A 1 2422 ? 216.139 174.103 164.000 1.00 9.65  ? 2422 ILE A CA    1 
ATOM   7561  C  C     . ILE A 1 2422 ? 215.134 173.845 165.118 1.00 9.47  ? 2422 ILE A C     1 
ATOM   7562  O  O     . ILE A 1 2422 ? 214.776 172.694 165.392 1.00 10.94 ? 2422 ILE A O     1 
ATOM   7563  C  CB    . ILE A 1 2422 ? 217.565 174.290 164.549 1.00 13.73 ? 2422 ILE A CB    1 
ATOM   7564  C  CG1   . ILE A 1 2422 ? 218.531 174.604 163.407 1.00 10.89 ? 2422 ILE A CG1   1 
ATOM   7565  C  CG2   . ILE A 1 2422 ? 218.017 173.051 165.305 1.00 13.46 ? 2422 ILE A CG2   1 
ATOM   7566  C  CD1   . ILE A 1 2422 ? 219.861 175.143 163.865 1.00 10.33 ? 2422 ILE A CD1   1 
ATOM   7567  N  N     . MET A 1 2423 ? 214.669 174.905 165.786 1.00 8.11  ? 2423 MET A N     1 
ATOM   7568  C  CA    . MET A 1 2423 ? 213.742 174.724 166.900 1.00 8.30  ? 2423 MET A CA    1 
ATOM   7569  C  C     . MET A 1 2423 ? 212.342 174.359 166.430 1.00 12.35 ? 2423 MET A C     1 
ATOM   7570  O  O     . MET A 1 2423 ? 211.562 173.792 167.203 1.00 18.46 ? 2423 MET A O     1 
ATOM   7571  C  CB    . MET A 1 2423 ? 213.666 175.989 167.757 1.00 9.33  ? 2423 MET A CB    1 
ATOM   7572  C  CG    . MET A 1 2423 ? 214.922 176.343 168.517 1.00 11.90 ? 2423 MET A CG    1 
ATOM   7573  S  SD    . MET A 1 2423 ? 214.765 177.968 169.282 1.00 20.84 ? 2423 MET A SD    1 
ATOM   7574  C  CE    . MET A 1 2423 ? 216.312 178.728 168.814 1.00 14.98 ? 2423 MET A CE    1 
ATOM   7575  N  N     . GLN A 1 2424 ? 212.005 174.676 165.181 1.00 11.68 ? 2424 GLN A N     1 
ATOM   7576  C  CA    . GLN A 1 2424 ? 210.632 174.542 164.693 1.00 11.73 ? 2424 GLN A CA    1 
ATOM   7577  C  C     . GLN A 1 2424 ? 210.039 173.150 164.878 1.00 10.95 ? 2424 GLN A C     1 
ATOM   7578  O  O     . GLN A 1 2424 ? 208.886 173.059 165.331 1.00 12.12 ? 2424 GLN A O     1 
ATOM   7579  C  CB    . GLN A 1 2424 ? 210.587 174.972 163.219 1.00 12.02 ? 2424 GLN A CB    1 
ATOM   7580  C  CG    . GLN A 1 2424 ? 209.199 174.993 162.610 1.00 11.02 ? 2424 GLN A CG    1 
ATOM   7581  C  CD    . GLN A 1 2424 ? 208.485 176.310 162.839 1.00 13.42 ? 2424 GLN A CD    1 
ATOM   7582  O  OE1   . GLN A 1 2424 ? 208.931 177.355 162.370 1.00 19.54 ? 2424 GLN A OE1   1 
ATOM   7583  N  NE2   . GLN A 1 2424 ? 207.370 176.266 163.557 1.00 9.28  ? 2424 GLN A NE2   1 
ATOM   7584  N  N     . PRO A 1 2425 ? 210.732 172.046 164.557 1.00 12.40 ? 2425 PRO A N     1 
ATOM   7585  C  CA    . PRO A 1 2425 ? 210.108 170.724 164.758 1.00 8.05  ? 2425 PRO A CA    1 
ATOM   7586  C  C     . PRO A 1 2425 ? 209.700 170.443 166.194 1.00 10.47 ? 2425 PRO A C     1 
ATOM   7587  O  O     . PRO A 1 2425 ? 208.673 169.793 166.423 1.00 18.30 ? 2425 PRO A O     1 
ATOM   7588  C  CB    . PRO A 1 2425 ? 211.198 169.753 164.282 1.00 7.72  ? 2425 PRO A CB    1 
ATOM   7589  C  CG    . PRO A 1 2425 ? 211.999 170.534 163.326 1.00 6.42  ? 2425 PRO A CG    1 
ATOM   7590  C  CD    . PRO A 1 2425 ? 212.034 171.922 163.877 1.00 8.41  ? 2425 PRO A CD    1 
ATOM   7591  N  N     . TYR A 1 2426 ? 210.474 170.911 167.171 1.00 11.76 ? 2426 TYR A N     1 
ATOM   7592  C  CA    . TYR A 1 2426 ? 210.176 170.641 168.571 1.00 7.97  ? 2426 TYR A CA    1 
ATOM   7593  C  C     . TYR A 1 2426 ? 209.099 171.549 169.144 1.00 9.49  ? 2426 TYR A C     1 
ATOM   7594  O  O     . TYR A 1 2426 ? 208.576 171.251 170.223 1.00 12.99 ? 2426 TYR A O     1 
ATOM   7595  C  CB    . TYR A 1 2426 ? 211.449 170.764 169.409 1.00 12.27 ? 2426 TYR A CB    1 
ATOM   7596  C  CG    . TYR A 1 2426 ? 212.611 169.983 168.853 1.00 9.20  ? 2426 TYR A CG    1 
ATOM   7597  C  CD1   . TYR A 1 2426 ? 213.575 170.595 168.064 1.00 10.01 ? 2426 TYR A CD1   1 
ATOM   7598  C  CD2   . TYR A 1 2426 ? 212.740 168.628 169.112 1.00 7.30  ? 2426 TYR A CD2   1 
ATOM   7599  C  CE1   . TYR A 1 2426 ? 214.634 169.876 167.552 1.00 10.19 ? 2426 TYR A CE1   1 
ATOM   7600  C  CE2   . TYR A 1 2426 ? 213.793 167.904 168.607 1.00 8.30  ? 2426 TYR A CE2   1 
ATOM   7601  C  CZ    . TYR A 1 2426 ? 214.736 168.530 167.827 1.00 13.22 ? 2426 TYR A CZ    1 
ATOM   7602  O  OH    . TYR A 1 2426 ? 215.786 167.799 167.327 1.00 21.45 ? 2426 TYR A OH    1 
ATOM   7603  N  N     . PHE A 1 2427 ? 208.751 172.633 168.458 1.00 11.10 ? 2427 PHE A N     1 
ATOM   7604  C  CA    . PHE A 1 2427 ? 207.743 173.568 168.934 1.00 10.00 ? 2427 PHE A CA    1 
ATOM   7605  C  C     . PHE A 1 2427 ? 206.395 173.372 168.257 1.00 9.53  ? 2427 PHE A C     1 
ATOM   7606  O  O     . PHE A 1 2427 ? 205.529 174.246 168.358 1.00 20.91 ? 2427 PHE A O     1 
ATOM   7607  C  CB    . PHE A 1 2427 ? 208.226 175.005 168.744 1.00 8.88  ? 2427 PHE A CB    1 
ATOM   7608  C  CG    . PHE A 1 2427 ? 209.129 175.480 169.838 1.00 7.51  ? 2427 PHE A CG    1 
ATOM   7609  C  CD1   . PHE A 1 2427 ? 208.615 175.826 171.074 1.00 4.89  ? 2427 PHE A CD1   1 
ATOM   7610  C  CD2   . PHE A 1 2427 ? 210.496 175.568 169.638 1.00 9.00  ? 2427 PHE A CD2   1 
ATOM   7611  C  CE1   . PHE A 1 2427 ? 209.442 176.259 172.084 1.00 6.49  ? 2427 PHE A CE1   1 
ATOM   7612  C  CE2   . PHE A 1 2427 ? 211.330 176.000 170.647 1.00 5.54  ? 2427 PHE A CE2   1 
ATOM   7613  C  CZ    . PHE A 1 2427 ? 210.802 176.348 171.871 1.00 2.99  ? 2427 PHE A CZ    1 
ATOM   7614  N  N     . THR A 1 2428 ? 206.205 172.260 167.558 1.00 13.66 ? 2428 THR A N     1 
ATOM   7615  C  CA    . THR A 1 2428 ? 204.900 171.924 167.017 1.00 16.24 ? 2428 THR A CA    1 
ATOM   7616  C  C     . THR A 1 2428 ? 204.010 171.351 168.115 1.00 17.10 ? 2428 THR A C     1 
ATOM   7617  O  O     . THR A 1 2428 ? 204.478 170.950 169.184 1.00 21.27 ? 2428 THR A O     1 
ATOM   7618  C  CB    . THR A 1 2428 ? 205.028 170.913 165.878 1.00 15.37 ? 2428 THR A CB    1 
ATOM   7619  O  OG1   . THR A 1 2428 ? 205.388 169.634 166.415 1.00 15.11 ? 2428 THR A OG1   1 
ATOM   7620  C  CG2   . THR A 1 2428 ? 206.091 171.359 164.885 1.00 11.20 ? 2428 THR A CG2   1 
ATOM   7621  N  N     . SER A 1 2429 ? 202.708 171.325 167.840 1.00 21.28 ? 2429 SER A N     1 
ATOM   7622  C  CA    . SER A 1 2429 ? 201.772 170.698 168.762 1.00 15.94 ? 2429 SER A CA    1 
ATOM   7623  C  C     . SER A 1 2429 ? 202.082 169.211 168.887 1.00 20.14 ? 2429 SER A C     1 
ATOM   7624  O  O     . SER A 1 2429 ? 202.394 168.541 167.898 1.00 24.58 ? 2429 SER A O     1 
ATOM   7625  C  CB    . SER A 1 2429 ? 200.334 170.906 168.283 1.00 24.19 ? 2429 SER A CB    1 
ATOM   7626  O  OG    . SER A 1 2429 ? 200.157 170.400 166.972 1.00 30.48 ? 2429 SER A OG    1 
ATOM   7627  N  N     . ASN A 1 2430 ? 201.996 168.698 170.116 1.00 18.30 ? 2430 ASN A N     1 
ATOM   7628  C  CA    . ASN A 1 2430 ? 202.418 167.334 170.444 1.00 15.04 ? 2430 ASN A CA    1 
ATOM   7629  C  C     . ASN A 1 2430 ? 203.899 167.120 170.149 1.00 16.80 ? 2430 ASN A C     1 
ATOM   7630  O  O     . ASN A 1 2430 ? 204.321 166.017 169.791 1.00 20.22 ? 2430 ASN A O     1 
ATOM   7631  C  CB    . ASN A 1 2430 ? 201.570 166.286 169.716 1.00 17.57 ? 2430 ASN A CB    1 
ATOM   7632  C  CG    . ASN A 1 2430 ? 200.124 166.299 170.158 1.00 25.11 ? 2430 ASN A CG    1 
ATOM   7633  O  OD1   . ASN A 1 2430 ? 199.737 167.078 171.027 1.00 21.56 ? 2430 ASN A OD1   1 
ATOM   7634  N  ND2   . ASN A 1 2430 ? 199.313 165.434 169.559 1.00 24.73 ? 2430 ASN A ND2   1 
ATOM   7635  N  N     . GLY A 1 2431 ? 204.696 168.176 170.290 1.00 13.97 ? 2431 GLY A N     1 
ATOM   7636  C  CA    . GLY A 1 2431 ? 206.131 168.089 170.143 1.00 9.44  ? 2431 GLY A CA    1 
ATOM   7637  C  C     . GLY A 1 2431 ? 206.821 167.825 171.468 1.00 11.35 ? 2431 GLY A C     1 
ATOM   7638  O  O     . GLY A 1 2431 ? 206.202 167.463 172.470 1.00 12.20 ? 2431 GLY A O     1 
ATOM   7639  N  N     . LEU A 1 2432 ? 208.142 168.006 171.457 1.00 10.82 ? 2432 LEU A N     1 
ATOM   7640  C  CA    . LEU A 1 2432 ? 208.933 167.768 172.659 1.00 5.70  ? 2432 LEU A CA    1 
ATOM   7641  C  C     . LEU A 1 2432 ? 208.549 168.730 173.777 1.00 6.14  ? 2432 LEU A C     1 
ATOM   7642  O  O     . LEU A 1 2432 ? 208.355 168.320 174.926 1.00 11.13 ? 2432 LEU A O     1 
ATOM   7643  C  CB    . LEU A 1 2432 ? 210.421 167.888 172.332 1.00 4.78  ? 2432 LEU A CB    1 
ATOM   7644  C  CG    . LEU A 1 2432 ? 211.387 167.826 173.515 1.00 5.37  ? 2432 LEU A CG    1 
ATOM   7645  C  CD1   . LEU A 1 2432 ? 211.390 166.438 174.132 1.00 11.70 ? 2432 LEU A CD1   1 
ATOM   7646  C  CD2   . LEU A 1 2432 ? 212.783 168.222 173.079 1.00 8.82  ? 2432 LEU A CD2   1 
ATOM   7647  N  N     . VAL A 1 2433 ? 208.424 170.018 173.454 1.00 6.96  ? 2433 VAL A N     1 
ATOM   7648  C  CA    . VAL A 1 2433 ? 208.158 171.017 174.484 1.00 3.68  ? 2433 VAL A CA    1 
ATOM   7649  C  C     . VAL A 1 2433 ? 206.751 170.851 175.044 1.00 5.49  ? 2433 VAL A C     1 
ATOM   7650  O  O     . VAL A 1 2433 ? 206.523 171.027 176.247 1.00 6.68  ? 2433 VAL A O     1 
ATOM   7651  C  CB    . VAL A 1 2433 ? 208.386 172.433 173.924 1.00 4.37  ? 2433 VAL A CB    1 
ATOM   7652  C  CG1   . VAL A 1 2433 ? 208.194 173.468 175.011 1.00 3.11  ? 2433 VAL A CG1   1 
ATOM   7653  C  CG2   . VAL A 1 2433 ? 209.771 172.543 173.314 1.00 6.14  ? 2433 VAL A CG2   1 
ATOM   7654  N  N     . THR A 1 2434 ? 205.784 170.520 174.186 1.00 10.88 ? 2434 THR A N     1 
ATOM   7655  C  CA    . THR A 1 2434 ? 204.416 170.317 174.652 1.00 6.25  ? 2434 THR A CA    1 
ATOM   7656  C  C     . THR A 1 2434 ? 204.330 169.128 175.602 1.00 6.40  ? 2434 THR A C     1 
ATOM   7657  O  O     . THR A 1 2434 ? 203.703 169.212 176.663 1.00 7.04  ? 2434 THR A O     1 
ATOM   7658  C  CB    . THR A 1 2434 ? 203.479 170.129 173.458 1.00 10.42 ? 2434 THR A CB    1 
ATOM   7659  O  OG1   . THR A 1 2434 ? 203.522 171.295 172.627 1.00 15.33 ? 2434 THR A OG1   1 
ATOM   7660  C  CG2   . THR A 1 2434 ? 202.050 169.909 173.926 1.00 8.20  ? 2434 THR A CG2   1 
ATOM   7661  N  N     . LYS A 1 2435 ? 204.959 168.007 175.236 1.00 6.67  ? 2435 LYS A N     1 
ATOM   7662  C  CA    . LYS A 1 2435 ? 204.934 166.834 176.103 1.00 5.67  ? 2435 LYS A CA    1 
ATOM   7663  C  C     . LYS A 1 2435 ? 205.690 167.084 177.400 1.00 6.46  ? 2435 LYS A C     1 
ATOM   7664  O  O     . LYS A 1 2435 ? 205.265 166.636 178.472 1.00 7.44  ? 2435 LYS A O     1 
ATOM   7665  C  CB    . LYS A 1 2435 ? 205.512 165.620 175.376 1.00 8.15  ? 2435 LYS A CB    1 
ATOM   7666  C  CG    . LYS A 1 2435 ? 204.677 165.135 174.208 1.00 10.54 ? 2435 LYS A CG    1 
ATOM   7667  C  CD    . LYS A 1 2435 ? 205.224 163.835 173.644 1.00 11.38 ? 2435 LYS A CD    1 
ATOM   7668  C  CE    . LYS A 1 2435 ? 206.498 164.061 172.857 1.00 19.74 ? 2435 LYS A CE    1 
ATOM   7669  N  NZ    . LYS A 1 2435 ? 206.976 162.805 172.214 1.00 26.56 ? 2435 LYS A NZ    1 
ATOM   7670  N  N     . ALA A 1 2436 ? 206.820 167.788 177.321 1.00 8.76  ? 2436 ALA A N     1 
ATOM   7671  C  CA    . ALA A 1 2436 ? 207.568 168.126 178.527 1.00 3.07  ? 2436 ALA A CA    1 
ATOM   7672  C  C     . ALA A 1 2436 ? 206.747 169.020 179.448 1.00 2.83  ? 2436 ALA A C     1 
ATOM   7673  O  O     . ALA A 1 2436 ? 206.769 168.849 180.672 1.00 6.07  ? 2436 ALA A O     1 
ATOM   7674  C  CB    . ALA A 1 2436 ? 208.885 168.802 178.154 1.00 3.67  ? 2436 ALA A CB    1 
ATOM   7675  N  N     . LEU A 1 2437 ? 206.022 169.982 178.875 1.00 2.81  ? 2437 LEU A N     1 
ATOM   7676  C  CA    . LEU A 1 2437 ? 205.212 170.890 179.680 1.00 3.47  ? 2437 LEU A CA    1 
ATOM   7677  C  C     . LEU A 1 2437 ? 204.108 170.142 180.417 1.00 5.34  ? 2437 LEU A C     1 
ATOM   7678  O  O     . LEU A 1 2437 ? 203.859 170.390 181.602 1.00 5.17  ? 2437 LEU A O     1 
ATOM   7679  C  CB    . LEU A 1 2437 ? 204.624 171.986 178.791 1.00 3.91  ? 2437 LEU A CB    1 
ATOM   7680  C  CG    . LEU A 1 2437 ? 203.931 173.151 179.496 1.00 6.61  ? 2437 LEU A CG    1 
ATOM   7681  C  CD1   . LEU A 1 2437 ? 204.900 173.865 180.423 1.00 8.67  ? 2437 LEU A CD1   1 
ATOM   7682  C  CD2   . LEU A 1 2437 ? 203.353 174.112 178.474 1.00 6.87  ? 2437 LEU A CD2   1 
ATOM   7683  N  N     . GLU A 1 2438 ? 203.439 169.212 179.731 1.00 5.68  ? 2438 GLU A N     1 
ATOM   7684  C  CA    . GLU A 1 2438 ? 202.368 168.447 180.363 1.00 10.37 ? 2438 GLU A CA    1 
ATOM   7685  C  C     . GLU A 1 2438 ? 202.899 167.602 181.514 1.00 7.60  ? 2438 GLU A C     1 
ATOM   7686  O  O     . GLU A 1 2438 ? 202.254 167.483 182.563 1.00 6.30  ? 2438 GLU A O     1 
ATOM   7687  C  CB    . GLU A 1 2438 ? 201.670 167.567 179.324 1.00 7.95  ? 2438 GLU A CB    1 
ATOM   7688  C  CG    . GLU A 1 2438 ? 200.918 168.344 178.258 1.00 18.79 ? 2438 GLU A CG    1 
ATOM   7689  C  CD    . GLU A 1 2438 ? 199.724 169.101 178.814 1.00 29.60 ? 2438 GLU A CD    1 
ATOM   7690  O  OE1   . GLU A 1 2438 ? 199.111 168.619 179.790 1.00 31.60 ? 2438 GLU A OE1   1 
ATOM   7691  O  OE2   . GLU A 1 2438 ? 199.402 170.180 178.277 1.00 34.40 ? 2438 GLU A OE2   1 
ATOM   7692  N  N     . HIS A 1 2439 ? 204.075 166.999 181.332 1.00 4.65  ? 2439 HIS A N     1 
ATOM   7693  C  CA    . HIS A 1 2439 ? 204.661 166.184 182.390 1.00 6.72  ? 2439 HIS A CA    1 
ATOM   7694  C  C     . HIS A 1 2439 ? 205.106 167.040 183.568 1.00 6.63  ? 2439 HIS A C     1 
ATOM   7695  O  O     . HIS A 1 2439 ? 205.021 166.612 184.725 1.00 6.03  ? 2439 HIS A O     1 
ATOM   7696  C  CB    . HIS A 1 2439 ? 205.837 165.382 181.838 1.00 9.28  ? 2439 HIS A CB    1 
ATOM   7697  C  CG    . HIS A 1 2439 ? 206.363 164.352 182.784 1.00 10.56 ? 2439 HIS A CG    1 
ATOM   7698  N  ND1   . HIS A 1 2439 ? 205.640 163.237 183.149 1.00 8.70  ? 2439 HIS A ND1   1 
ATOM   7699  C  CD2   . HIS A 1 2439 ? 207.544 164.265 183.442 1.00 14.87 ? 2439 HIS A CD2   1 
ATOM   7700  C  CE1   . HIS A 1 2439 ? 206.351 162.510 183.993 1.00 13.49 ? 2439 HIS A CE1   1 
ATOM   7701  N  NE2   . HIS A 1 2439 ? 207.511 163.111 184.185 1.00 11.13 ? 2439 HIS A NE2   1 
ATOM   7702  N  N     . ALA A 1 2440 ? 205.590 168.254 183.293 1.00 6.89  ? 2440 ALA A N     1 
ATOM   7703  C  CA    . ALA A 1 2440 ? 206.075 169.123 184.361 1.00 3.70  ? 2440 ALA A CA    1 
ATOM   7704  C  C     . ALA A 1 2440 ? 204.954 169.510 185.317 1.00 3.13  ? 2440 ALA A C     1 
ATOM   7705  O  O     . ALA A 1 2440 ? 205.178 169.636 186.526 1.00 4.59  ? 2440 ALA A O     1 
ATOM   7706  C  CB    . ALA A 1 2440 ? 206.731 170.367 183.764 1.00 3.87  ? 2440 ALA A CB    1 
ATOM   7707  N  N     . PHE A 1 2441 ? 203.741 169.713 184.794 1.00 3.98  ? 2441 PHE A N     1 
ATOM   7708  C  CA    . PHE A 1 2441 ? 202.616 170.066 185.655 1.00 5.14  ? 2441 PHE A CA    1 
ATOM   7709  C  C     . PHE A 1 2441 ? 202.279 168.947 186.631 1.00 5.08  ? 2441 PHE A C     1 
ATOM   7710  O  O     . PHE A 1 2441 ? 201.665 169.198 187.673 1.00 7.85  ? 2441 PHE A O     1 
ATOM   7711  C  CB    . PHE A 1 2441 ? 201.392 170.420 184.810 1.00 2.35  ? 2441 PHE A CB    1 
ATOM   7712  C  CG    . PHE A 1 2441 ? 201.365 171.850 184.351 1.00 2.89  ? 2441 PHE A CG    1 
ATOM   7713  C  CD1   . PHE A 1 2441 ? 200.800 172.834 185.144 1.00 3.09  ? 2441 PHE A CD1   1 
ATOM   7714  C  CD2   . PHE A 1 2441 ? 201.905 172.210 183.129 1.00 2.95  ? 2441 PHE A CD2   1 
ATOM   7715  C  CE1   . PHE A 1 2441 ? 200.776 174.150 184.727 1.00 2.05  ? 2441 PHE A CE1   1 
ATOM   7716  C  CE2   . PHE A 1 2441 ? 201.884 173.526 182.706 1.00 3.34  ? 2441 PHE A CE2   1 
ATOM   7717  C  CZ    . PHE A 1 2441 ? 201.316 174.497 183.507 1.00 5.70  ? 2441 PHE A CZ    1 
ATOM   7718  N  N     . GLN A 1 2442 ? 202.667 167.711 186.316 1.00 5.97  ? 2442 GLN A N     1 
ATOM   7719  C  CA    . GLN A 1 2442 ? 202.420 166.603 187.226 1.00 7.14  ? 2442 GLN A CA    1 
ATOM   7720  C  C     . GLN A 1 2442 ? 203.408 166.576 188.384 1.00 8.47  ? 2442 GLN A C     1 
ATOM   7721  O  O     . GLN A 1 2442 ? 203.148 165.910 189.389 1.00 15.12 ? 2442 GLN A O     1 
ATOM   7722  C  CB    . GLN A 1 2442 ? 202.469 165.280 186.463 1.00 8.46  ? 2442 GLN A CB    1 
ATOM   7723  C  CG    . GLN A 1 2442 ? 201.363 165.147 185.437 1.00 9.44  ? 2442 GLN A CG    1 
ATOM   7724  C  CD    . GLN A 1 2442 ? 199.989 165.164 186.068 1.00 22.94 ? 2442 GLN A CD    1 
ATOM   7725  O  OE1   . GLN A 1 2442 ? 199.240 166.131 185.921 1.00 28.40 ? 2442 GLN A OE1   1 
ATOM   7726  N  NE2   . GLN A 1 2442 ? 199.646 164.092 186.773 1.00 17.08 ? 2442 GLN A NE2   1 
ATOM   7727  N  N     . LEU A 1 2443 ? 204.523 167.288 188.269 1.00 8.29  ? 2443 LEU A N     1 
ATOM   7728  C  CA    . LEU A 1 2443 ? 205.555 167.269 189.290 1.00 6.22  ? 2443 LEU A CA    1 
ATOM   7729  C  C     . LEU A 1 2443 ? 205.277 168.314 190.365 1.00 6.10  ? 2443 LEU A C     1 
ATOM   7730  O  O     . LEU A 1 2443 ? 204.402 169.172 190.230 1.00 10.89 ? 2443 LEU A O     1 
ATOM   7731  C  CB    . LEU A 1 2443 ? 206.925 167.510 188.663 1.00 5.39  ? 2443 LEU A CB    1 
ATOM   7732  C  CG    . LEU A 1 2443 ? 207.285 166.475 187.605 1.00 8.81  ? 2443 LEU A CG    1 
ATOM   7733  C  CD1   . LEU A 1 2443 ? 208.587 166.819 186.901 1.00 10.33 ? 2443 LEU A CD1   1 
ATOM   7734  C  CD2   . LEU A 1 2443 ? 207.362 165.115 188.259 1.00 5.54  ? 2443 LEU A CD2   1 
ATOM   7735  N  N     . GLU A 1 2444 ? 206.038 168.225 191.450 1.00 5.80  ? 2444 GLU A N     1 
ATOM   7736  C  CA    . GLU A 1 2444 ? 205.932 169.181 192.541 1.00 7.62  ? 2444 GLU A CA    1 
ATOM   7737  C  C     . GLU A 1 2444 ? 206.973 170.278 192.372 1.00 6.20  ? 2444 GLU A C     1 
ATOM   7738  O  O     . GLU A 1 2444 ? 208.139 170.008 192.071 1.00 6.20  ? 2444 GLU A O     1 
ATOM   7739  C  CB    . GLU A 1 2444 ? 206.103 168.492 193.895 1.00 8.67  ? 2444 GLU A CB    1 
ATOM   7740  C  CG    . GLU A 1 2444 ? 204.991 167.517 194.232 1.00 16.93 ? 2444 GLU A CG    1 
ATOM   7741  C  CD    . GLU A 1 2444 ? 203.654 168.203 194.440 1.00 23.97 ? 2444 GLU A CD    1 
ATOM   7742  O  OE1   . GLU A 1 2444 ? 203.640 169.361 194.911 1.00 23.85 ? 2444 GLU A OE1   1 
ATOM   7743  O  OE2   . GLU A 1 2444 ? 202.613 167.586 194.131 1.00 26.58 ? 2444 GLU A OE2   1 
ATOM   7744  N  N     . HIS A 1 2445 ? 206.539 171.517 192.560 1.00 5.50  ? 2445 HIS A N     1 
ATOM   7745  C  CA    . HIS A 1 2445 ? 207.391 172.682 192.400 1.00 2.85  ? 2445 HIS A CA    1 
ATOM   7746  C  C     . HIS A 1 2445 ? 207.306 173.543 193.649 1.00 2.85  ? 2445 HIS A C     1 
ATOM   7747  O  O     . HIS A 1 2445 ? 206.289 173.553 194.346 1.00 3.44  ? 2445 HIS A O     1 
ATOM   7748  C  CB    . HIS A 1 2445 ? 206.988 173.491 191.163 1.00 2.56  ? 2445 HIS A CB    1 
ATOM   7749  C  CG    . HIS A 1 2445 ? 206.802 172.659 189.935 1.00 4.94  ? 2445 HIS A CG    1 
ATOM   7750  N  ND1   . HIS A 1 2445 ? 207.824 172.408 189.044 1.00 5.27  ? 2445 HIS A ND1   1 
ATOM   7751  C  CD2   . HIS A 1 2445 ? 205.719 172.006 189.455 1.00 4.30  ? 2445 HIS A CD2   1 
ATOM   7752  C  CE1   . HIS A 1 2445 ? 207.376 171.645 188.066 1.00 2.38  ? 2445 HIS A CE1   1 
ATOM   7753  N  NE2   . HIS A 1 2445 ? 206.102 171.384 188.292 1.00 4.27  ? 2445 HIS A NE2   1 
ATOM   7754  N  N     . ILE A 1 2446 ? 208.393 174.266 193.931 1.00 1.59  ? 2446 ILE A N     1 
ATOM   7755  C  CA    . ILE A 1 2446 ? 208.436 175.093 195.134 1.00 2.09  ? 2446 ILE A CA    1 
ATOM   7756  C  C     . ILE A 1 2446 ? 207.398 176.205 195.059 1.00 2.21  ? 2446 ILE A C     1 
ATOM   7757  O  O     . ILE A 1 2446 ? 206.903 176.675 196.090 1.00 3.28  ? 2446 ILE A O     1 
ATOM   7758  C  CB    . ILE A 1 2446 ? 209.863 175.641 195.358 1.00 2.79  ? 2446 ILE A CB    1 
ATOM   7759  C  CG1   . ILE A 1 2446 ? 210.112 175.892 196.846 1.00 3.24  ? 2446 ILE A CG1   1 
ATOM   7760  C  CG2   . ILE A 1 2446 ? 210.110 176.906 194.553 1.00 2.17  ? 2446 ILE A CG2   1 
ATOM   7761  C  CD1   . ILE A 1 2446 ? 209.954 174.662 197.704 1.00 2.31  ? 2446 ILE A CD1   1 
ATOM   7762  N  N     . MET A 1 2447 ? 207.039 176.631 193.852 1.00 2.97  ? 2447 MET A N     1 
ATOM   7763  C  CA    . MET A 1 2447 ? 205.970 177.591 193.638 1.00 2.09  ? 2447 MET A CA    1 
ATOM   7764  C  C     . MET A 1 2447 ? 204.954 176.990 192.679 1.00 2.09  ? 2447 MET A C     1 
ATOM   7765  O  O     . MET A 1 2447 ? 205.241 176.026 191.969 1.00 2.12  ? 2447 MET A O     1 
ATOM   7766  C  CB    . MET A 1 2447 ? 206.500 178.918 193.083 1.00 4.33  ? 2447 MET A CB    1 
ATOM   7767  C  CG    . MET A 1 2447 ? 207.251 179.748 194.099 1.00 4.30  ? 2447 MET A CG    1 
ATOM   7768  S  SD    . MET A 1 2447 ? 207.474 181.451 193.568 1.00 12.05 ? 2447 MET A SD    1 
ATOM   7769  C  CE    . MET A 1 2447 ? 208.385 182.093 194.960 1.00 0.94  ? 2447 MET A CE    1 
ATOM   7770  N  N     . ASP A 1 2448 ? 203.752 177.565 192.679 1.00 2.66  ? 2448 ASP A N     1 
ATOM   7771  C  CA    . ASP A 1 2448 ? 202.715 177.118 191.757 1.00 1.74  ? 2448 ASP A CA    1 
ATOM   7772  C  C     . ASP A 1 2448 ? 203.197 177.252 190.320 1.00 2.38  ? 2448 ASP A C     1 
ATOM   7773  O  O     . ASP A 1 2448 ? 203.811 178.255 189.947 1.00 5.06  ? 2448 ASP A O     1 
ATOM   7774  C  CB    . ASP A 1 2448 ? 201.436 177.922 191.969 1.00 3.07  ? 2448 ASP A CB    1 
ATOM   7775  C  CG    . ASP A 1 2448 ? 200.692 177.515 193.223 1.00 12.52 ? 2448 ASP A CG    1 
ATOM   7776  O  OD1   . ASP A 1 2448 ? 201.079 176.505 193.847 1.00 15.40 ? 2448 ASP A OD1   1 
ATOM   7777  O  OD2   . ASP A 1 2448 ? 199.721 178.209 193.588 1.00 13.85 ? 2448 ASP A OD2   1 
ATOM   7778  N  N     . LEU A 1 2449 ? 202.922 176.236 189.512 1.00 2.69  ? 2449 LEU A N     1 
ATOM   7779  C  CA    . LEU A 1 2449 ? 203.451 176.174 188.160 1.00 1.55  ? 2449 LEU A CA    1 
ATOM   7780  C  C     . LEU A 1 2449 ? 202.411 176.700 187.182 1.00 3.01  ? 2449 LEU A C     1 
ATOM   7781  O  O     . LEU A 1 2449 ? 201.251 176.278 187.213 1.00 4.68  ? 2449 LEU A O     1 
ATOM   7782  C  CB    . LEU A 1 2449 ? 203.832 174.739 187.798 1.00 2.24  ? 2449 LEU A CB    1 
ATOM   7783  C  CG    . LEU A 1 2449 ? 204.520 174.629 186.441 1.00 4.76  ? 2449 LEU A CG    1 
ATOM   7784  C  CD1   . LEU A 1 2449 ? 205.826 175.385 186.546 1.00 1.92  ? 2449 LEU A CD1   1 
ATOM   7785  C  CD2   . LEU A 1 2449 ? 204.739 173.198 185.997 1.00 3.89  ? 2449 LEU A CD2   1 
ATOM   7786  N  N     . THR A 1 2450 ? 202.823 177.629 186.323 1.00 2.06  ? 2450 THR A N     1 
ATOM   7787  C  CA    . THR A 1 2450 ? 201.972 178.130 185.256 1.00 1.24  ? 2450 THR A CA    1 
ATOM   7788  C  C     . THR A 1 2450 ? 202.685 177.971 183.920 1.00 1.37  ? 2450 THR A C     1 
ATOM   7789  O  O     . THR A 1 2450 ? 203.915 177.913 183.849 1.00 4.17  ? 2450 THR A O     1 
ATOM   7790  C  CB    . THR A 1 2450 ? 201.579 179.603 185.473 1.00 2.53  ? 2450 THR A CB    1 
ATOM   7791  O  OG1   . THR A 1 2450 ? 202.735 180.442 185.355 1.00 9.05  ? 2450 THR A OG1   1 
ATOM   7792  C  CG2   . THR A 1 2450 ? 200.939 179.795 186.840 1.00 1.72  ? 2450 THR A CG2   1 
ATOM   7793  N  N     . ARG A 1 2451 ? 201.884 177.889 182.855 1.00 1.77  ? 2451 ARG A N     1 
ATOM   7794  C  CA    . ARG A 1 2451 ? 202.429 177.616 181.530 1.00 2.02  ? 2451 ARG A CA    1 
ATOM   7795  C  C     . ARG A 1 2451 ? 203.378 178.717 181.074 1.00 0.88  ? 2451 ARG A C     1 
ATOM   7796  O  O     . ARG A 1 2451 ? 204.440 178.436 180.507 1.00 1.31  ? 2451 ARG A O     1 
ATOM   7797  C  CB    . ARG A 1 2451 ? 201.289 177.441 180.526 1.00 2.60  ? 2451 ARG A CB    1 
ATOM   7798  C  CG    . ARG A 1 2451 ? 201.734 177.470 179.074 1.00 1.74  ? 2451 ARG A CG    1 
ATOM   7799  C  CD    . ARG A 1 2451 ? 200.572 177.278 178.121 1.00 3.75  ? 2451 ARG A CD    1 
ATOM   7800  N  NE    . ARG A 1 2451 ? 199.521 178.271 178.311 1.00 2.64  ? 2451 ARG A NE    1 
ATOM   7801  C  CZ    . ARG A 1 2451 ? 198.466 178.401 177.519 1.00 2.26  ? 2451 ARG A CZ    1 
ATOM   7802  N  NH1   . ARG A 1 2451 ? 198.290 177.619 176.468 1.00 2.06  ? 2451 ARG A NH1   1 
ATOM   7803  N  NH2   . ARG A 1 2451 ? 197.568 179.344 177.785 1.00 3.05  ? 2451 ARG A NH2   1 
ATOM   7804  N  N     . LEU A 1 2452 ? 203.018 179.976 181.317 1.00 1.11  ? 2452 LEU A N     1 
ATOM   7805  C  CA    . LEU A 1 2452 ? 203.803 181.082 180.786 1.00 0.65  ? 2452 LEU A CA    1 
ATOM   7806  C  C     . LEU A 1 2452 ? 205.081 181.332 181.576 1.00 0.95  ? 2452 LEU A C     1 
ATOM   7807  O  O     . LEU A 1 2452 ? 206.036 181.891 181.026 1.00 0.99  ? 2452 LEU A O     1 
ATOM   7808  C  CB    . LEU A 1 2452 ? 202.946 182.343 180.728 1.00 0.82  ? 2452 LEU A CB    1 
ATOM   7809  C  CG    . LEU A 1 2452 ? 201.979 182.328 179.542 1.00 0.70  ? 2452 LEU A CG    1 
ATOM   7810  C  CD1   . LEU A 1 2452 ? 201.372 183.685 179.324 1.00 0.65  ? 2452 LEU A CD1   1 
ATOM   7811  C  CD2   . LEU A 1 2452 ? 202.693 181.861 178.284 1.00 0.62  ? 2452 LEU A CD2   1 
ATOM   7812  N  N     . ARG A 1 2453 ? 205.132 180.939 182.852 1.00 1.38  ? 2453 ARG A N     1 
ATOM   7813  C  CA    . ARG A 1 2453 ? 206.393 181.036 183.579 1.00 1.00  ? 2453 ARG A CA    1 
ATOM   7814  C  C     . ARG A 1 2453 ? 207.438 180.103 182.981 1.00 1.02  ? 2453 ARG A C     1 
ATOM   7815  O  O     . ARG A 1 2453 ? 208.608 180.477 182.840 1.00 2.52  ? 2453 ARG A O     1 
ATOM   7816  C  CB    . ARG A 1 2453 ? 206.193 180.740 185.066 1.00 0.91  ? 2453 ARG A CB    1 
ATOM   7817  C  CG    . ARG A 1 2453 ? 207.486 180.871 185.867 1.00 0.77  ? 2453 ARG A CG    1 
ATOM   7818  C  CD    . ARG A 1 2453 ? 207.281 180.873 187.375 1.00 0.72  ? 2453 ARG A CD    1 
ATOM   7819  N  NE    . ARG A 1 2453 ? 206.648 179.662 187.877 1.00 3.74  ? 2453 ARG A NE    1 
ATOM   7820  C  CZ    . ARG A 1 2453 ? 207.301 178.654 188.439 1.00 2.50  ? 2453 ARG A CZ    1 
ATOM   7821  N  NH1   . ARG A 1 2453 ? 208.620 178.639 188.510 1.00 1.49  ? 2453 ARG A NH1   1 
ATOM   7822  N  NH2   . ARG A 1 2453 ? 206.612 177.630 188.932 1.00 5.48  ? 2453 ARG A NH2   1 
ATOM   7823  N  N     . CYS A 1 2454 ? 207.030 178.888 182.611 1.00 1.50  ? 2454 CYS A N     1 
ATOM   7824  C  CA    . CYS A 1 2454 ? 207.949 177.956 181.965 1.00 1.41  ? 2454 CYS A CA    1 
ATOM   7825  C  C     . CYS A 1 2454 ? 208.367 178.460 180.594 1.00 0.91  ? 2454 CYS A C     1 
ATOM   7826  O  O     . CYS A 1 2454 ? 209.558 178.491 180.266 1.00 1.48  ? 2454 CYS A O     1 
ATOM   7827  C  CB    . CYS A 1 2454 ? 207.298 176.582 181.834 1.00 3.58  ? 2454 CYS A CB    1 
ATOM   7828  S  SG    . CYS A 1 2454 ? 206.589 175.951 183.337 1.00 12.23 ? 2454 CYS A SG    1 
ATOM   7829  N  N     . LEU A 1 2455 ? 207.390 178.845 179.770 1.00 1.09  ? 2455 LEU A N     1 
ATOM   7830  C  CA    . LEU A 1 2455 ? 207.691 179.267 178.408 1.00 0.82  ? 2455 LEU A CA    1 
ATOM   7831  C  C     . LEU A 1 2455 ? 208.453 180.584 178.397 1.00 0.54  ? 2455 LEU A C     1 
ATOM   7832  O  O     . LEU A 1 2455 ? 209.369 180.769 177.587 1.00 1.24  ? 2455 LEU A O     1 
ATOM   7833  C  CB    . LEU A 1 2455 ? 206.398 179.370 177.602 1.00 0.90  ? 2455 LEU A CB    1 
ATOM   7834  C  CG    . LEU A 1 2455 ? 205.696 178.030 177.362 1.00 0.99  ? 2455 LEU A CG    1 
ATOM   7835  C  CD1   . LEU A 1 2455 ? 204.525 178.190 176.409 1.00 1.32  ? 2455 LEU A CD1   1 
ATOM   7836  C  CD2   . LEU A 1 2455 ? 206.676 176.989 176.845 1.00 0.76  ? 2455 LEU A CD2   1 
ATOM   7837  N  N     . GLY A 1 2456 ? 208.096 181.509 179.289 1.00 0.79  ? 2456 GLY A N     1 
ATOM   7838  C  CA    . GLY A 1 2456 ? 208.864 182.736 179.411 1.00 0.99  ? 2456 GLY A CA    1 
ATOM   7839  C  C     . GLY A 1 2456 ? 210.315 182.471 179.761 1.00 1.26  ? 2456 GLY A C     1 
ATOM   7840  O  O     . GLY A 1 2456 ? 211.222 183.093 179.205 1.00 1.16  ? 2456 GLY A O     1 
ATOM   7841  N  N     . SER A 1 2457 ? 210.551 181.542 180.689 1.00 1.13  ? 2457 SER A N     1 
ATOM   7842  C  CA    . SER A 1 2457 ? 211.915 181.123 180.990 1.00 0.84  ? 2457 SER A CA    1 
ATOM   7843  C  C     . SER A 1 2457 ? 212.551 180.417 179.800 1.00 1.21  ? 2457 SER A C     1 
ATOM   7844  O  O     . SER A 1 2457 ? 213.717 180.664 179.476 1.00 1.87  ? 2457 SER A O     1 
ATOM   7845  C  CB    . SER A 1 2457 ? 211.924 180.216 182.219 1.00 0.53  ? 2457 SER A CB    1 
ATOM   7846  O  OG    . SER A 1 2457 ? 213.216 179.685 182.449 1.00 1.50  ? 2457 SER A OG    1 
ATOM   7847  N  N     . LEU A 1 2458 ? 211.799 179.536 179.136 1.00 1.10  ? 2458 LEU A N     1 
ATOM   7848  C  CA    . LEU A 1 2458 ? 212.351 178.778 178.018 1.00 0.99  ? 2458 LEU A CA    1 
ATOM   7849  C  C     . LEU A 1 2458 ? 212.747 179.690 176.866 1.00 1.53  ? 2458 LEU A C     1 
ATOM   7850  O  O     . LEU A 1 2458 ? 213.797 179.495 176.243 1.00 1.45  ? 2458 LEU A O     1 
ATOM   7851  C  CB    . LEU A 1 2458 ? 211.341 177.730 177.549 1.00 1.39  ? 2458 LEU A CB    1 
ATOM   7852  C  CG    . LEU A 1 2458 ? 211.731 176.951 176.291 1.00 1.85  ? 2458 LEU A CG    1 
ATOM   7853  C  CD1   . LEU A 1 2458 ? 212.925 176.051 176.568 1.00 1.27  ? 2458 LEU A CD1   1 
ATOM   7854  C  CD2   . LEU A 1 2458 ? 210.560 176.149 175.762 1.00 0.55  ? 2458 LEU A CD2   1 
ATOM   7855  N  N     . PHE A 1 2459 ? 211.919 180.690 176.565 1.00 4.10  ? 2459 PHE A N     1 
ATOM   7856  C  CA    . PHE A 1 2459 ? 212.218 181.584 175.451 1.00 1.67  ? 2459 PHE A CA    1 
ATOM   7857  C  C     . PHE A 1 2459 ? 213.388 182.505 175.768 1.00 1.93  ? 2459 PHE A C     1 
ATOM   7858  O  O     . PHE A 1 2459 ? 214.170 182.840 174.869 1.00 3.06  ? 2459 PHE A O     1 
ATOM   7859  C  CB    . PHE A 1 2459 ? 210.977 182.397 175.085 1.00 1.32  ? 2459 PHE A CB    1 
ATOM   7860  C  CG    . PHE A 1 2459 ? 209.797 181.556 174.683 1.00 0.92  ? 2459 PHE A CG    1 
ATOM   7861  C  CD1   . PHE A 1 2459 ? 209.979 180.305 174.121 1.00 1.38  ? 2459 PHE A CD1   1 
ATOM   7862  C  CD2   . PHE A 1 2459 ? 208.506 182.020 174.872 1.00 0.88  ? 2459 PHE A CD2   1 
ATOM   7863  C  CE1   . PHE A 1 2459 ? 208.895 179.532 173.755 1.00 1.59  ? 2459 PHE A CE1   1 
ATOM   7864  C  CE2   . PHE A 1 2459 ? 207.421 181.249 174.509 1.00 1.09  ? 2459 PHE A CE2   1 
ATOM   7865  C  CZ    . PHE A 1 2459 ? 207.615 180.005 173.950 1.00 1.48  ? 2459 PHE A CZ    1 
ATOM   7866  N  N     . SER A 1 2460 ? 213.525 182.929 177.026 1.00 3.15  ? 2460 SER A N     1 
ATOM   7867  C  CA    . SER A 1 2460 ? 214.676 183.739 177.412 1.00 1.31  ? 2460 SER A CA    1 
ATOM   7868  C  C     . SER A 1 2460 ? 215.974 182.960 177.254 1.00 1.82  ? 2460 SER A C     1 
ATOM   7869  O  O     . SER A 1 2460 ? 216.979 183.503 176.783 1.00 4.22  ? 2460 SER A O     1 
ATOM   7870  C  CB    . SER A 1 2460 ? 214.520 184.228 178.851 1.00 1.36  ? 2460 SER A CB    1 
ATOM   7871  O  OG    . SER A 1 2460 ? 213.381 185.055 178.990 1.00 3.45  ? 2460 SER A OG    1 
ATOM   7872  N  N     . MET A 1 2461 ? 215.973 181.686 177.648 1.00 2.39  ? 2461 MET A N     1 
ATOM   7873  C  CA    . MET A 1 2461 ? 217.176 180.870 177.534 1.00 1.30  ? 2461 MET A CA    1 
ATOM   7874  C  C     . MET A 1 2461 ? 217.556 180.637 176.078 1.00 2.53  ? 2461 MET A C     1 
ATOM   7875  O  O     . MET A 1 2461 ? 218.740 180.683 175.726 1.00 9.94  ? 2461 MET A O     1 
ATOM   7876  C  CB    . MET A 1 2461 ? 216.976 179.542 178.264 1.00 2.13  ? 2461 MET A CB    1 
ATOM   7877  C  CG    . MET A 1 2461 ? 216.677 179.704 179.746 1.00 1.18  ? 2461 MET A CG    1 
ATOM   7878  S  SD    . MET A 1 2461 ? 216.843 178.191 180.705 1.00 1.65  ? 2461 MET A SD    1 
ATOM   7879  C  CE    . MET A 1 2461 ? 218.469 177.651 180.204 1.00 1.27  ? 2461 MET A CE    1 
ATOM   7880  N  N     . LEU A 1 2462 ? 216.568 180.393 175.215 1.00 2.59  ? 2462 LEU A N     1 
ATOM   7881  C  CA    . LEU A 1 2462 ? 216.859 180.178 173.802 1.00 2.23  ? 2462 LEU A CA    1 
ATOM   7882  C  C     . LEU A 1 2462 ? 217.398 181.439 173.141 1.00 2.75  ? 2462 LEU A C     1 
ATOM   7883  O  O     . LEU A 1 2462 ? 218.238 181.353 172.239 1.00 4.08  ? 2462 LEU A O     1 
ATOM   7884  C  CB    . LEU A 1 2462 ? 215.611 179.682 173.076 1.00 1.56  ? 2462 LEU A CB    1 
ATOM   7885  C  CG    . LEU A 1 2462 ? 215.130 178.287 173.478 1.00 2.17  ? 2462 LEU A CG    1 
ATOM   7886  C  CD1   . LEU A 1 2462 ? 213.817 177.954 172.794 1.00 3.31  ? 2462 LEU A CD1   1 
ATOM   7887  C  CD2   . LEU A 1 2462 ? 216.184 177.237 173.165 1.00 3.16  ? 2462 LEU A CD2   1 
ATOM   7888  N  N     . HIS A 1 2463 ? 216.927 182.614 173.566 1.00 3.64  ? 2463 HIS A N     1 
ATOM   7889  C  CA    . HIS A 1 2463 ? 217.493 183.861 173.064 1.00 4.88  ? 2463 HIS A CA    1 
ATOM   7890  C  C     . HIS A 1 2463 ? 218.962 183.984 173.444 1.00 7.38  ? 2463 HIS A C     1 
ATOM   7891  O  O     . HIS A 1 2463 ? 219.778 184.475 172.656 1.00 10.33 ? 2463 HIS A O     1 
ATOM   7892  C  CB    . HIS A 1 2463 ? 216.701 185.053 173.599 1.00 5.04  ? 2463 HIS A CB    1 
ATOM   7893  C  CG    . HIS A 1 2463 ? 215.373 185.245 172.938 1.00 4.25  ? 2463 HIS A CG    1 
ATOM   7894  N  ND1   . HIS A 1 2463 ? 214.341 185.941 173.530 1.00 5.79  ? 2463 HIS A ND1   1 
ATOM   7895  C  CD2   . HIS A 1 2463 ? 214.905 184.828 171.738 1.00 4.38  ? 2463 HIS A CD2   1 
ATOM   7896  C  CE1   . HIS A 1 2463 ? 213.297 185.948 172.722 1.00 4.73  ? 2463 HIS A CE1   1 
ATOM   7897  N  NE2   . HIS A 1 2463 ? 213.612 185.279 171.628 1.00 6.94  ? 2463 HIS A NE2   1 
ATOM   7898  N  N     . GLN A 1 2464 ? 219.314 183.548 174.656 1.00 9.34  ? 2464 GLN A N     1 
ATOM   7899  C  CA    . GLN A 1 2464 ? 220.711 183.555 175.078 1.00 6.79  ? 2464 GLN A CA    1 
ATOM   7900  C  C     . GLN A 1 2464 ? 221.547 182.607 174.230 1.00 7.28  ? 2464 GLN A C     1 
ATOM   7901  O  O     . GLN A 1 2464 ? 222.710 182.896 173.926 1.00 8.05  ? 2464 GLN A O     1 
ATOM   7902  C  CB    . GLN A 1 2464 ? 220.806 183.183 176.559 1.00 7.62  ? 2464 GLN A CB    1 
ATOM   7903  C  CG    . GLN A 1 2464 ? 222.208 183.226 177.143 1.00 9.28  ? 2464 GLN A CG    1 
ATOM   7904  C  CD    . GLN A 1 2464 ? 222.906 184.547 176.904 1.00 7.78  ? 2464 GLN A CD    1 
ATOM   7905  O  OE1   . GLN A 1 2464 ? 222.366 185.611 177.205 1.00 10.67 ? 2464 GLN A OE1   1 
ATOM   7906  N  NE2   . GLN A 1 2464 ? 224.116 184.485 176.365 1.00 10.54 ? 2464 GLN A NE2   1 
ATOM   7907  N  N     . ALA A 1 2465 ? 220.974 181.465 173.842 1.00 7.24  ? 2465 ALA A N     1 
ATOM   7908  C  CA    . ALA A 1 2465 ? 221.689 180.531 172.982 1.00 4.49  ? 2465 ALA A CA    1 
ATOM   7909  C  C     . ALA A 1 2465 ? 222.010 181.163 171.634 1.00 8.49  ? 2465 ALA A C     1 
ATOM   7910  O  O     . ALA A 1 2465 ? 223.087 180.934 171.073 1.00 9.55  ? 2465 ALA A O     1 
ATOM   7911  C  CB    . ALA A 1 2465 ? 220.871 179.257 172.792 1.00 5.20  ? 2465 ALA A CB    1 
ATOM   7912  N  N     . CYS A 1 2466 ? 221.080 181.954 171.095 1.00 11.55 ? 2466 CYS A N     1 
ATOM   7913  C  CA    . CYS A 1 2466 ? 221.358 182.683 169.862 1.00 6.77  ? 2466 CYS A CA    1 
ATOM   7914  C  C     . CYS A 1 2466 ? 222.483 183.688 170.067 1.00 7.80  ? 2466 CYS A C     1 
ATOM   7915  O  O     . CYS A 1 2466 ? 223.336 183.862 169.190 1.00 11.12 ? 2466 CYS A O     1 
ATOM   7916  C  CB    . CYS A 1 2466 ? 220.090 183.377 169.368 1.00 7.56  ? 2466 CYS A CB    1 
ATOM   7917  S  SG    . CYS A 1 2466 ? 218.780 182.247 168.852 1.00 21.05 ? 2466 CYS A SG    1 
ATOM   7918  N  N     . ARG A 1 2467 ? 222.501 184.356 171.222 1.00 10.39 ? 2467 ARG A N     1 
ATOM   7919  C  CA    . ARG A 1 2467 ? 223.599 185.262 171.539 1.00 7.11  ? 2467 ARG A CA    1 
ATOM   7920  C  C     . ARG A 1 2467 ? 224.917 184.517 171.703 1.00 6.30  ? 2467 ARG A C     1 
ATOM   7921  O  O     . ARG A 1 2467 ? 225.979 185.068 171.393 1.00 10.69 ? 2467 ARG A O     1 
ATOM   7922  C  CB    . ARG A 1 2467 ? 223.276 186.054 172.805 1.00 6.49  ? 2467 ARG A CB    1 
ATOM   7923  C  CG    . ARG A 1 2467 ? 222.152 187.053 172.639 1.00 10.23 ? 2467 ARG A CG    1 
ATOM   7924  C  CD    . ARG A 1 2467 ? 221.767 187.670 173.968 1.00 11.85 ? 2467 ARG A CD    1 
ATOM   7925  N  NE    . ARG A 1 2467 ? 220.429 188.245 173.933 1.00 14.34 ? 2467 ARG A NE    1 
ATOM   7926  C  CZ    . ARG A 1 2467 ? 220.142 189.450 173.461 1.00 16.54 ? 2467 ARG A CZ    1 
ATOM   7927  N  NH1   . ARG A 1 2467 ? 221.083 190.250 172.987 1.00 9.11  ? 2467 ARG A NH1   1 
ATOM   7928  N  NH2   . ARG A 1 2467 ? 218.879 189.865 173.466 1.00 13.91 ? 2467 ARG A NH2   1 
ATOM   7929  N  N     . ASN A 1 2468 ? 224.873 183.274 172.188 1.00 6.67  ? 2468 ASN A N     1 
ATOM   7930  C  CA    . ASN A 1 2468 ? 226.096 182.487 172.323 1.00 7.90  ? 2468 ASN A CA    1 
ATOM   7931  C  C     . ASN A 1 2468 ? 226.740 182.233 170.967 1.00 8.59  ? 2468 ASN A C     1 
ATOM   7932  O  O     . ASN A 1 2468 ? 227.964 182.334 170.823 1.00 15.52 ? 2468 ASN A O     1 
ATOM   7933  C  CB    . ASN A 1 2468 ? 225.798 181.160 173.021 1.00 5.57  ? 2468 ASN A CB    1 
ATOM   7934  C  CG    . ASN A 1 2468 ? 225.464 181.332 174.486 1.00 7.08  ? 2468 ASN A CG    1 
ATOM   7935  O  OD1   . ASN A 1 2468 ? 225.622 182.414 175.049 1.00 10.01 ? 2468 ASN A OD1   1 
ATOM   7936  N  ND2   . ASN A 1 2468 ? 224.986 180.262 175.111 1.00 6.11  ? 2468 ASN A ND2   1 
ATOM   7937  N  N     . VAL A 1 2469 ? 225.930 181.901 169.960 1.00 9.98  ? 2469 VAL A N     1 
ATOM   7938  C  CA    . VAL A 1 2469 ? 226.462 181.628 168.628 1.00 9.07  ? 2469 VAL A CA    1 
ATOM   7939  C  C     . VAL A 1 2469 ? 227.076 182.887 168.031 1.00 10.12 ? 2469 VAL A C     1 
ATOM   7940  O  O     . VAL A 1 2469 ? 228.140 182.838 167.401 1.00 13.65 ? 2469 VAL A O     1 
ATOM   7941  C  CB    . VAL A 1 2469 ? 225.359 181.044 167.727 1.00 8.53  ? 2469 VAL A CB    1 
ATOM   7942  C  CG1   . VAL A 1 2469 ? 225.886 180.801 166.324 1.00 11.02 ? 2469 VAL A CG1   1 
ATOM   7943  C  CG2   . VAL A 1 2469 ? 224.817 179.760 168.331 1.00 8.42  ? 2469 VAL A CG2   1 
ATOM   7944  N  N     . ALA A 1 2470 ? 226.418 184.034 168.215 1.00 9.18  ? 2470 ALA A N     1 
ATOM   7945  C  CA    . ALA A 1 2470 ? 226.987 185.293 167.747 1.00 11.05 ? 2470 ALA A CA    1 
ATOM   7946  C  C     . ALA A 1 2470 ? 228.291 185.611 168.463 1.00 15.49 ? 2470 ALA A C     1 
ATOM   7947  O  O     . ALA A 1 2470 ? 229.260 186.060 167.839 1.00 20.63 ? 2470 ALA A O     1 
ATOM   7948  C  CB    . ALA A 1 2470 ? 225.981 186.426 167.939 1.00 10.57 ? 2470 ALA A CB    1 
ATOM   7949  N  N     . GLN A 1 2471 ? 228.334 185.384 169.777 1.00 15.49 ? 2471 GLN A N     1 
ATOM   7950  C  CA    . GLN A 1 2471 ? 229.553 185.639 170.534 1.00 17.55 ? 2471 GLN A CA    1 
ATOM   7951  C  C     . GLN A 1 2471 ? 230.670 184.702 170.093 1.00 18.80 ? 2471 GLN A C     1 
ATOM   7952  O  O     . GLN A 1 2471 ? 231.847 185.081 170.088 1.00 21.32 ? 2471 GLN A O     1 
ATOM   7953  C  CB    . GLN A 1 2471 ? 229.269 185.501 172.031 1.00 17.51 ? 2471 GLN A CB    1 
ATOM   7954  C  CG    . GLN A 1 2471 ? 230.398 185.930 172.958 1.00 13.21 ? 2471 GLN A CG    1 
ATOM   7955  C  CD    . GLN A 1 2471 ? 231.408 184.835 173.220 1.00 22.92 ? 2471 GLN A CD    1 
ATOM   7956  O  OE1   . GLN A 1 2471 ? 232.585 185.102 173.463 1.00 32.94 ? 2471 GLN A OE1   1 
ATOM   7957  N  NE2   . GLN A 1 2471 ? 230.959 183.589 173.143 1.00 22.74 ? 2471 GLN A NE2   1 
ATOM   7958  N  N     . TYR A 1 2472 ? 230.317 183.471 169.713 1.00 15.31 ? 2472 TYR A N     1 
ATOM   7959  C  CA    . TYR A 1 2472 ? 231.306 182.561 169.146 1.00 14.68 ? 2472 TYR A CA    1 
ATOM   7960  C  C     . TYR A 1 2472 ? 231.848 183.093 167.825 1.00 17.22 ? 2472 TYR A C     1 
ATOM   7961  O  O     . TYR A 1 2472 ? 233.051 182.996 167.555 1.00 21.21 ? 2472 TYR A O     1 
ATOM   7962  C  CB    . TYR A 1 2472 ? 230.693 181.167 168.978 1.00 11.44 ? 2472 TYR A CB    1 
ATOM   7963  C  CG    . TYR A 1 2472 ? 231.529 180.171 168.197 1.00 14.90 ? 2472 TYR A CG    1 
ATOM   7964  C  CD1   . TYR A 1 2472 ? 232.211 179.152 168.847 1.00 13.39 ? 2472 TYR A CD1   1 
ATOM   7965  C  CD2   . TYR A 1 2472 ? 231.582 180.207 166.808 1.00 15.76 ? 2472 TYR A CD2   1 
ATOM   7966  C  CE1   . TYR A 1 2472 ? 232.960 178.232 168.144 1.00 18.02 ? 2472 TYR A CE1   1 
ATOM   7967  C  CE2   . TYR A 1 2472 ? 232.329 179.292 166.098 1.00 21.18 ? 2472 TYR A CE2   1 
ATOM   7968  C  CZ    . TYR A 1 2472 ? 233.015 178.306 166.770 1.00 21.79 ? 2472 TYR A CZ    1 
ATOM   7969  O  OH    . TYR A 1 2472 ? 233.756 177.390 166.062 1.00 25.86 ? 2472 TYR A OH    1 
ATOM   7970  N  N     . ASN A 1 2473 ? 230.975 183.652 166.983 1.00 22.58 ? 2473 ASN A N     1 
ATOM   7971  C  CA    . ASN A 1 2473 ? 231.428 184.197 165.707 1.00 20.66 ? 2473 ASN A CA    1 
ATOM   7972  C  C     . ASN A 1 2473 ? 232.365 185.380 165.914 1.00 19.95 ? 2473 ASN A C     1 
ATOM   7973  O  O     . ASN A 1 2473 ? 233.278 185.604 165.112 1.00 21.84 ? 2473 ASN A O     1 
ATOM   7974  C  CB    . ASN A 1 2473 ? 230.230 184.596 164.846 1.00 14.72 ? 2473 ASN A CB    1 
ATOM   7975  C  CG    . ASN A 1 2473 ? 229.462 183.398 164.323 1.00 20.22 ? 2473 ASN A CG    1 
ATOM   7976  O  OD1   . ASN A 1 2473 ? 229.800 182.253 164.621 1.00 19.98 ? 2473 ASN A OD1   1 
ATOM   7977  N  ND2   . ASN A 1 2473 ? 228.425 183.655 163.537 1.00 19.23 ? 2473 ASN A ND2   1 
ATOM   7978  N  N     . ALA A 1 2474 ? 232.150 186.153 166.980 1.00 18.71 ? 2474 ALA A N     1 
ATOM   7979  C  CA    . ALA A 1 2474 ? 233.092 187.212 167.323 1.00 19.43 ? 2474 ALA A CA    1 
ATOM   7980  C  C     . ALA A 1 2474 ? 234.451 186.636 167.698 1.00 25.87 ? 2474 ALA A C     1 
ATOM   7981  O  O     . ALA A 1 2474 ? 235.493 187.168 167.296 1.00 26.75 ? 2474 ALA A O     1 
ATOM   7982  C  CB    . ALA A 1 2474 ? 232.532 188.062 168.463 1.00 14.78 ? 2474 ALA A CB    1 
ATOM   7983  N  N     . ASN A 1 2475 ? 234.463 185.544 168.469 1.00 22.11 ? 2475 ASN A N     1 
ATOM   7984  C  CA    . ASN A 1 2475 ? 235.713 184.882 168.818 1.00 21.64 ? 2475 ASN A CA    1 
ATOM   7985  C  C     . ASN A 1 2475 ? 236.371 184.217 167.619 1.00 22.45 ? 2475 ASN A C     1 
ATOM   7986  O  O     . ASN A 1 2475 ? 237.590 184.019 167.628 1.00 30.36 ? 2475 ASN A O     1 
ATOM   7987  C  CB    . ASN A 1 2475 ? 235.477 183.832 169.903 1.00 23.68 ? 2475 ASN A CB    1 
ATOM   7988  C  CG    . ASN A 1 2475 ? 234.840 184.407 171.146 1.00 27.00 ? 2475 ASN A CG    1 
ATOM   7989  O  OD1   . ASN A 1 2475 ? 234.699 185.621 171.284 1.00 20.26 ? 2475 ASN A OD1   1 
ATOM   7990  N  ND2   . ASN A 1 2475 ? 234.450 183.531 172.064 1.00 24.66 ? 2475 ASN A ND2   1 
ATOM   7991  N  N     . HIS A 1 2476 ? 235.598 183.870 166.595 1.00 17.01 ? 2476 HIS A N     1 
ATOM   7992  C  CA    . HIS A 1 2476 ? 236.104 183.195 165.400 1.00 21.33 ? 2476 HIS A CA    1 
ATOM   7993  C  C     . HIS A 1 2476 ? 235.670 183.982 164.171 1.00 26.68 ? 2476 HIS A C     1 
ATOM   7994  O  O     . HIS A 1 2476 ? 234.782 183.551 163.425 1.00 32.55 ? 2476 HIS A O     1 
ATOM   7995  C  CB    . HIS A 1 2476 ? 235.597 181.755 165.320 1.00 18.81 ? 2476 HIS A CB    1 
ATOM   7996  C  CG    . HIS A 1 2476 ? 235.899 180.931 166.532 1.00 17.74 ? 2476 HIS A CG    1 
ATOM   7997  N  ND1   . HIS A 1 2476 ? 235.263 181.123 167.739 1.00 20.85 ? 2476 HIS A ND1   1 
ATOM   7998  C  CD2   . HIS A 1 2476 ? 236.747 179.891 166.714 1.00 17.40 ? 2476 HIS A CD2   1 
ATOM   7999  C  CE1   . HIS A 1 2476 ? 235.720 180.250 168.619 1.00 24.90 ? 2476 HIS A CE1   1 
ATOM   8000  N  NE2   . HIS A 1 2476 ? 236.618 179.489 168.021 1.00 22.17 ? 2476 HIS A NE2   1 
ATOM   8001  N  N     . PRO A 1 2477 ? 236.269 185.151 163.934 1.00 24.90 ? 2477 PRO A N     1 
ATOM   8002  C  CA    . PRO A 1 2477 ? 235.909 185.919 162.732 1.00 21.95 ? 2477 PRO A CA    1 
ATOM   8003  C  C     . PRO A 1 2477 ? 236.238 185.190 161.446 1.00 29.36 ? 2477 PRO A C     1 
ATOM   8004  O  O     . PRO A 1 2477 ? 235.645 185.497 160.404 1.00 33.41 ? 2477 PRO A O     1 
ATOM   8005  C  CB    . PRO A 1 2477 ? 236.732 187.208 162.873 1.00 27.59 ? 2477 PRO A CB    1 
ATOM   8006  C  CG    . PRO A 1 2477 ? 237.149 187.256 164.308 1.00 21.20 ? 2477 PRO A CG    1 
ATOM   8007  C  CD    . PRO A 1 2477 ? 237.304 185.832 164.727 1.00 24.74 ? 2477 PRO A CD    1 
ATOM   8008  N  N     . ASP A 1 2478 ? 237.162 184.231 161.487 1.00 29.26 ? 2478 ASP A N     1 
ATOM   8009  C  CA    . ASP A 1 2478 ? 237.537 183.488 160.291 1.00 33.18 ? 2478 ASP A CA    1 
ATOM   8010  C  C     . ASP A 1 2478 ? 236.471 182.466 159.913 1.00 31.17 ? 2478 ASP A C     1 
ATOM   8011  O  O     . ASP A 1 2478 ? 235.975 182.460 158.782 1.00 39.99 ? 2478 ASP A O     1 
ATOM   8012  C  CB    . ASP A 1 2478 ? 238.892 182.808 160.508 1.00 31.25 ? 2478 ASP A CB    1 
ATOM   8013  C  CG    . ASP A 1 2478 ? 239.205 181.775 159.447 1.00 41.67 ? 2478 ASP A CG    1 
ATOM   8014  O  OD1   . ASP A 1 2478 ? 239.114 182.107 158.246 1.00 42.43 ? 2478 ASP A OD1   1 
ATOM   8015  O  OD2   . ASP A 1 2478 ? 239.551 180.634 159.815 1.00 43.84 ? 2478 ASP A OD2   1 
ATOM   8016  N  N     . PHE A 1 2479 ? 236.098 181.599 160.852 1.00 33.32 ? 2479 PHE A N     1 
ATOM   8017  C  CA    . PHE A 1 2479 ? 235.156 180.513 160.582 1.00 37.16 ? 2479 PHE A CA    1 
ATOM   8018  C  C     . PHE A 1 2479 ? 233.923 180.647 161.461 1.00 32.83 ? 2479 PHE A C     1 
ATOM   8019  O  O     . PHE A 1 2479 ? 233.916 180.160 162.606 1.00 32.99 ? 2479 PHE A O     1 
ATOM   8020  C  CB    . PHE A 1 2479 ? 235.821 179.156 160.804 1.00 29.88 ? 2479 PHE A CB    1 
ATOM   8021  C  CG    . PHE A 1 2479 ? 236.881 178.827 159.794 1.00 33.93 ? 2479 PHE A CG    1 
ATOM   8022  C  CD1   . PHE A 1 2479 ? 236.856 179.399 158.533 1.00 37.05 ? 2479 PHE A CD1   1 
ATOM   8023  C  CD2   . PHE A 1 2479 ? 237.902 177.946 160.106 1.00 36.45 ? 2479 PHE A CD2   1 
ATOM   8024  C  CE1   . PHE A 1 2479 ? 237.830 179.096 157.599 1.00 38.72 ? 2479 PHE A CE1   1 
ATOM   8025  C  CE2   . PHE A 1 2479 ? 238.880 177.640 159.177 1.00 33.04 ? 2479 PHE A CE2   1 
ATOM   8026  C  CZ    . PHE A 1 2479 ? 238.844 178.215 157.922 1.00 35.92 ? 2479 PHE A CZ    1 
ATOM   8027  N  N     . PRO A 1 2480 ? 232.861 181.290 160.982 1.00 29.98 ? 2480 PRO A N     1 
ATOM   8028  C  CA    . PRO A 1 2480 ? 231.609 181.311 161.741 1.00 26.07 ? 2480 PRO A CA    1 
ATOM   8029  C  C     . PRO A 1 2480 ? 230.978 179.928 161.790 1.00 25.95 ? 2480 PRO A C     1 
ATOM   8030  O  O     . PRO A 1 2480 ? 231.204 179.076 160.925 1.00 27.47 ? 2480 PRO A O     1 
ATOM   8031  C  CB    . PRO A 1 2480 ? 230.733 182.298 160.965 1.00 26.18 ? 2480 PRO A CB    1 
ATOM   8032  C  CG    . PRO A 1 2480 ? 231.280 182.269 159.578 1.00 28.65 ? 2480 PRO A CG    1 
ATOM   8033  C  CD    . PRO A 1 2480 ? 232.760 182.048 159.724 1.00 31.58 ? 2480 PRO A CD    1 
ATOM   8034  N  N     . MET A 1 2481 ? 230.181 179.714 162.833 1.00 20.33 ? 2481 MET A N     1 
ATOM   8035  C  CA    . MET A 1 2481 ? 229.566 178.414 163.061 1.00 21.36 ? 2481 MET A CA    1 
ATOM   8036  C  C     . MET A 1 2481 ? 228.718 178.000 161.865 1.00 23.18 ? 2481 MET A C     1 
ATOM   8037  O  O     . MET A 1 2481 ? 227.931 178.793 161.340 1.00 26.18 ? 2481 MET A O     1 
ATOM   8038  C  CB    . MET A 1 2481 ? 228.708 178.457 164.324 1.00 19.00 ? 2481 MET A CB    1 
ATOM   8039  C  CG    . MET A 1 2481 ? 228.114 177.121 164.719 1.00 18.55 ? 2481 MET A CG    1 
ATOM   8040  S  SD    . MET A 1 2481 ? 227.123 177.231 166.219 1.00 37.20 ? 2481 MET A SD    1 
ATOM   8041  C  CE    . MET A 1 2481 ? 228.398 177.459 167.451 1.00 20.06 ? 2481 MET A CE    1 
ATOM   8042  N  N     . GLN A 1 2482 ? 228.889 176.757 161.432 1.00 22.42 ? 2482 GLN A N     1 
ATOM   8043  C  CA    . GLN A 1 2482 ? 228.127 176.212 160.322 1.00 17.77 ? 2482 GLN A CA    1 
ATOM   8044  C  C     . GLN A 1 2482 ? 226.815 175.616 160.819 1.00 18.42 ? 2482 GLN A C     1 
ATOM   8045  O  O     . GLN A 1 2482 ? 226.616 175.390 162.014 1.00 24.56 ? 2482 GLN A O     1 
ATOM   8046  C  CB    . GLN A 1 2482 ? 228.947 175.163 159.572 1.00 18.07 ? 2482 GLN A CB    1 
ATOM   8047  C  CG    . GLN A 1 2482 ? 230.176 175.730 158.892 1.00 20.19 ? 2482 GLN A CG    1 
ATOM   8048  C  CD    . GLN A 1 2482 ? 229.878 177.008 158.136 1.00 21.00 ? 2482 GLN A CD    1 
ATOM   8049  O  OE1   . GLN A 1 2482 ? 229.059 177.023 157.217 1.00 26.11 ? 2482 GLN A OE1   1 
ATOM   8050  N  NE2   . GLN A 1 2482 ? 230.536 178.091 158.524 1.00 23.40 ? 2482 GLN A NE2   1 
ATOM   8051  N  N     . ILE A 1 2483 ? 225.912 175.354 159.871 1.00 18.04 ? 2483 ILE A N     1 
ATOM   8052  C  CA    . ILE A 1 2483 ? 224.585 174.853 160.219 1.00 16.25 ? 2483 ILE A CA    1 
ATOM   8053  C  C     . ILE A 1 2483 ? 224.682 173.511 160.928 1.00 21.48 ? 2483 ILE A C     1 
ATOM   8054  O  O     . ILE A 1 2483 ? 223.906 173.232 161.851 1.00 27.85 ? 2483 ILE A O     1 
ATOM   8055  C  CB    . ILE A 1 2483 ? 223.697 174.763 158.963 1.00 22.77 ? 2483 ILE A CB    1 
ATOM   8056  C  CG1   . ILE A 1 2483 ? 223.814 176.040 158.131 1.00 24.19 ? 2483 ILE A CG1   1 
ATOM   8057  C  CG2   . ILE A 1 2483 ? 222.250 174.525 159.352 1.00 19.04 ? 2483 ILE A CG2   1 
ATOM   8058  C  CD1   . ILE A 1 2483 ? 223.431 177.298 158.881 1.00 19.02 ? 2483 ILE A CD1   1 
ATOM   8059  N  N     . GLU A 1 2484 ? 225.624 172.662 160.517 1.00 18.52 ? 2484 GLU A N     1 
ATOM   8060  C  CA    . GLU A 1 2484 ? 225.794 171.368 161.170 1.00 15.32 ? 2484 GLU A CA    1 
ATOM   8061  C  C     . GLU A 1 2484 ? 226.169 171.543 162.638 1.00 20.04 ? 2484 GLU A C     1 
ATOM   8062  O  O     . GLU A 1 2484 ? 225.640 170.848 163.513 1.00 16.08 ? 2484 GLU A O     1 
ATOM   8063  C  CB    . GLU A 1 2484 ? 226.843 170.545 160.414 1.00 15.63 ? 2484 GLU A CB    1 
ATOM   8064  C  CG    . GLU A 1 2484 ? 227.109 169.148 160.956 1.00 22.74 ? 2484 GLU A CG    1 
ATOM   8065  C  CD    . GLU A 1 2484 ? 228.085 169.136 162.115 1.00 26.39 ? 2484 GLU A CD    1 
ATOM   8066  O  OE1   . GLU A 1 2484 ? 228.066 168.166 162.900 1.00 22.47 ? 2484 GLU A OE1   1 
ATOM   8067  O  OE2   . GLU A 1 2484 ? 228.875 170.095 162.240 1.00 28.84 ? 2484 GLU A OE2   1 
ATOM   8068  N  N     . GLN A 1 2485 ? 227.080 172.474 162.930 1.00 20.84 ? 2485 GLN A N     1 
ATOM   8069  C  CA    . GLN A 1 2485 ? 227.384 172.781 164.324 1.00 16.76 ? 2485 GLN A CA    1 
ATOM   8070  C  C     . GLN A 1 2485 ? 226.253 173.575 164.965 1.00 18.08 ? 2485 GLN A C     1 
ATOM   8071  O  O     . GLN A 1 2485 ? 225.925 173.359 166.137 1.00 18.27 ? 2485 GLN A O     1 
ATOM   8072  C  CB    . GLN A 1 2485 ? 228.701 173.548 164.430 1.00 20.54 ? 2485 GLN A CB    1 
ATOM   8073  C  CG    . GLN A 1 2485 ? 229.131 173.824 165.865 1.00 16.94 ? 2485 GLN A CG    1 
ATOM   8074  C  CD    . GLN A 1 2485 ? 230.464 174.536 165.956 1.00 22.00 ? 2485 GLN A CD    1 
ATOM   8075  O  OE1   . GLN A 1 2485 ? 230.965 174.800 167.048 1.00 25.94 ? 2485 GLN A OE1   1 
ATOM   8076  N  NE2   . GLN A 1 2485 ? 231.045 174.857 164.807 1.00 26.78 ? 2485 GLN A NE2   1 
ATOM   8077  N  N     . LEU A 1 2486 ? 225.646 174.497 164.210 1.00 17.85 ? 2486 LEU A N     1 
ATOM   8078  C  CA    . LEU A 1 2486 ? 224.513 175.253 164.733 1.00 14.46 ? 2486 LEU A CA    1 
ATOM   8079  C  C     . LEU A 1 2486 ? 223.348 174.336 165.071 1.00 14.59 ? 2486 LEU A C     1 
ATOM   8080  O  O     . LEU A 1 2486 ? 222.729 174.474 166.131 1.00 15.50 ? 2486 LEU A O     1 
ATOM   8081  C  CB    . LEU A 1 2486 ? 224.076 176.316 163.728 1.00 16.03 ? 2486 LEU A CB    1 
ATOM   8082  C  CG    . LEU A 1 2486 ? 222.970 177.261 164.206 1.00 17.09 ? 2486 LEU A CG    1 
ATOM   8083  C  CD1   . LEU A 1 2486 ? 223.367 177.947 165.502 1.00 11.24 ? 2486 LEU A CD1   1 
ATOM   8084  C  CD2   . LEU A 1 2486 ? 222.639 178.284 163.137 1.00 14.52 ? 2486 LEU A CD2   1 
ATOM   8085  N  N     . GLU A 1 2487 ? 223.039 173.388 164.184 1.00 13.77 ? 2487 GLU A N     1 
ATOM   8086  C  CA    . GLU A 1 2487 ? 222.003 172.409 164.489 1.00 15.54 ? 2487 GLU A CA    1 
ATOM   8087  C  C     . GLU A 1 2487 ? 222.389 171.585 165.704 1.00 13.49 ? 2487 GLU A C     1 
ATOM   8088  O  O     . GLU A 1 2487 ? 221.556 171.306 166.572 1.00 13.28 ? 2487 GLU A O     1 
ATOM   8089  C  CB    . GLU A 1 2487 ? 221.759 171.500 163.284 1.00 12.90 ? 2487 GLU A CB    1 
ATOM   8090  C  CG    . GLU A 1 2487 ? 220.537 170.613 163.417 1.00 17.59 ? 2487 GLU A CG    1 
ATOM   8091  C  CD    . GLU A 1 2487 ? 220.052 170.087 162.082 1.00 30.85 ? 2487 GLU A CD    1 
ATOM   8092  O  OE1   . GLU A 1 2487 ? 220.857 169.457 161.366 1.00 28.88 ? 2487 GLU A OE1   1 
ATOM   8093  O  OE2   . GLU A 1 2487 ? 218.867 170.302 161.750 1.00 35.59 ? 2487 GLU A OE2   1 
ATOM   8094  N  N     . ARG A 1 2488 ? 223.661 171.201 165.790 1.00 17.89 ? 2488 ARG A N     1 
ATOM   8095  C  CA    . ARG A 1 2488 ? 224.097 170.307 166.853 1.00 14.92 ? 2488 ARG A CA    1 
ATOM   8096  C  C     . ARG A 1 2488 ? 224.023 171.001 168.212 1.00 13.24 ? 2488 ARG A C     1 
ATOM   8097  O  O     . ARG A 1 2488 ? 223.752 170.359 169.234 1.00 15.77 ? 2488 ARG A O     1 
ATOM   8098  C  CB    . ARG A 1 2488 ? 225.513 169.817 166.541 1.00 17.31 ? 2488 ARG A CB    1 
ATOM   8099  C  CG    . ARG A 1 2488 ? 226.009 168.743 167.461 1.00 21.49 ? 2488 ARG A CG    1 
ATOM   8100  C  CD    . ARG A 1 2488 ? 227.379 168.197 167.108 1.00 20.26 ? 2488 ARG A CD    1 
ATOM   8101  N  NE    . ARG A 1 2488 ? 228.436 169.187 167.258 1.00 19.52 ? 2488 ARG A NE    1 
ATOM   8102  C  CZ    . ARG A 1 2488 ? 229.141 169.689 166.255 1.00 21.34 ? 2488 ARG A CZ    1 
ATOM   8103  N  NH1   . ARG A 1 2488 ? 228.906 169.338 165.004 1.00 20.48 ? 2488 ARG A NH1   1 
ATOM   8104  N  NH2   . ARG A 1 2488 ? 230.112 170.558 166.517 1.00 27.66 ? 2488 ARG A NH2   1 
ATOM   8105  N  N     . TYR A 1 2489 ? 224.251 172.317 168.235 1.00 13.33 ? 2489 TYR A N     1 
ATOM   8106  C  CA    . TYR A 1 2489 ? 224.189 173.083 169.478 1.00 6.35  ? 2489 TYR A CA    1 
ATOM   8107  C  C     . TYR A 1 2489 ? 222.753 173.334 169.930 1.00 9.42  ? 2489 TYR A C     1 
ATOM   8108  O  O     . TYR A 1 2489 ? 222.445 173.210 171.121 1.00 11.22 ? 2489 TYR A O     1 
ATOM   8109  C  CB    . TYR A 1 2489 ? 224.926 174.411 169.298 1.00 7.30  ? 2489 TYR A CB    1 
ATOM   8110  C  CG    . TYR A 1 2489 ? 224.959 175.283 170.533 1.00 6.23  ? 2489 TYR A CG    1 
ATOM   8111  C  CD1   . TYR A 1 2489 ? 225.469 174.810 171.733 1.00 7.17  ? 2489 TYR A CD1   1 
ATOM   8112  C  CD2   . TYR A 1 2489 ? 224.467 176.581 170.497 1.00 6.94  ? 2489 TYR A CD2   1 
ATOM   8113  C  CE1   . TYR A 1 2489 ? 225.494 175.610 172.860 1.00 7.75  ? 2489 TYR A CE1   1 
ATOM   8114  C  CE2   . TYR A 1 2489 ? 224.488 177.387 171.620 1.00 5.34  ? 2489 TYR A CE2   1 
ATOM   8115  C  CZ    . TYR A 1 2489 ? 225.002 176.896 172.797 1.00 6.94  ? 2489 TYR A CZ    1 
ATOM   8116  O  OH    . TYR A 1 2489 ? 225.023 177.695 173.916 1.00 9.79  ? 2489 TYR A OH    1 
ATOM   8117  N  N     . ILE A 1 2490 ? 221.866 173.700 169.002 1.00 11.02 ? 2490 ILE A N     1 
ATOM   8118  C  CA    . ILE A 1 2490 ? 220.539 174.184 169.382 1.00 5.85  ? 2490 ILE A CA    1 
ATOM   8119  C  C     . ILE A 1 2490 ? 219.709 173.066 170.004 1.00 4.93  ? 2490 ILE A C     1 
ATOM   8120  O  O     . ILE A 1 2490 ? 219.007 173.277 171.000 1.00 6.66  ? 2490 ILE A O     1 
ATOM   8121  C  CB    . ILE A 1 2490 ? 219.828 174.814 168.170 1.00 6.75  ? 2490 ILE A CB    1 
ATOM   8122  C  CG1   . ILE A 1 2490 ? 220.549 176.086 167.721 1.00 5.74  ? 2490 ILE A CG1   1 
ATOM   8123  C  CG2   . ILE A 1 2490 ? 218.383 175.139 168.503 1.00 8.93  ? 2490 ILE A CG2   1 
ATOM   8124  C  CD1   . ILE A 1 2490 ? 220.654 177.146 168.792 1.00 5.42  ? 2490 ILE A CD1   1 
ATOM   8125  N  N     . GLN A 1 2491 ? 219.769 171.863 169.426 1.00 4.26  ? 2491 GLN A N     1 
ATOM   8126  C  CA    . GLN A 1 2491 ? 218.941 170.765 169.919 1.00 5.10  ? 2491 GLN A CA    1 
ATOM   8127  C  C     . GLN A 1 2491 ? 219.290 170.405 171.356 1.00 9.26  ? 2491 GLN A C     1 
ATOM   8128  O  O     . GLN A 1 2491 ? 218.397 170.192 172.185 1.00 8.21  ? 2491 GLN A O     1 
ATOM   8129  C  CB    . GLN A 1 2491 ? 219.088 169.543 169.013 1.00 7.80  ? 2491 GLN A CB    1 
ATOM   8130  C  CG    . GLN A 1 2491 ? 219.091 169.864 167.538 1.00 11.21 ? 2491 GLN A CG    1 
ATOM   8131  C  CD    . GLN A 1 2491 ? 218.518 168.753 166.691 1.00 19.13 ? 2491 GLN A CD    1 
ATOM   8132  O  OE1   . GLN A 1 2491 ? 218.758 167.574 166.944 1.00 17.25 ? 2491 GLN A OE1   1 
ATOM   8133  N  NE2   . GLN A 1 2491 ? 217.751 169.126 165.674 1.00 25.67 ? 2491 GLN A NE2   1 
ATOM   8134  N  N     . ARG A 1 2492 ? 220.583 170.332 171.672 1.00 10.64 ? 2492 ARG A N     1 
ATOM   8135  C  CA    . ARG A 1 2492 ? 220.990 170.038 173.042 1.00 5.02  ? 2492 ARG A CA    1 
ATOM   8136  C  C     . ARG A 1 2492 ? 220.704 171.201 173.979 1.00 3.58  ? 2492 ARG A C     1 
ATOM   8137  O  O     . ARG A 1 2492 ? 220.288 170.988 175.124 1.00 4.53  ? 2492 ARG A O     1 
ATOM   8138  C  CB    . ARG A 1 2492 ? 222.465 169.656 173.076 1.00 6.18  ? 2492 ARG A CB    1 
ATOM   8139  C  CG    . ARG A 1 2492 ? 222.728 168.338 172.412 1.00 9.47  ? 2492 ARG A CG    1 
ATOM   8140  C  CD    . ARG A 1 2492 ? 224.189 167.976 172.443 1.00 12.80 ? 2492 ARG A CD    1 
ATOM   8141  N  NE    . ARG A 1 2492 ? 224.409 166.675 171.828 1.00 15.28 ? 2492 ARG A NE    1 
ATOM   8142  C  CZ    . ARG A 1 2492 ? 224.663 166.498 170.542 1.00 13.14 ? 2492 ARG A CZ    1 
ATOM   8143  N  NH1   . ARG A 1 2492 ? 224.598 167.499 169.690 1.00 9.97  ? 2492 ARG A NH1   1 
ATOM   8144  N  NH2   . ARG A 1 2492 ? 224.957 165.280 170.096 1.00 14.24 ? 2492 ARG A NH2   1 
ATOM   8145  N  N     . TYR A 1 2493 ? 220.911 172.436 173.521 1.00 2.29  ? 2493 TYR A N     1 
ATOM   8146  C  CA    . TYR A 1 2493 ? 220.591 173.573 174.375 1.00 2.49  ? 2493 TYR A CA    1 
ATOM   8147  C  C     . TYR A 1 2493 ? 219.096 173.644 174.650 1.00 5.22  ? 2493 TYR A C     1 
ATOM   8148  O  O     . TYR A 1 2493 ? 218.680 174.010 175.755 1.00 6.56  ? 2493 TYR A O     1 
ATOM   8149  C  CB    . TYR A 1 2493 ? 221.085 174.874 173.748 1.00 3.67  ? 2493 TYR A CB    1 
ATOM   8150  C  CG    . TYR A 1 2493 ? 221.084 176.034 174.719 1.00 5.18  ? 2493 TYR A CG    1 
ATOM   8151  C  CD1   . TYR A 1 2493 ? 219.917 176.738 174.991 1.00 5.04  ? 2493 TYR A CD1   1 
ATOM   8152  C  CD2   . TYR A 1 2493 ? 222.246 176.419 175.371 1.00 3.44  ? 2493 TYR A CD2   1 
ATOM   8153  C  CE1   . TYR A 1 2493 ? 219.910 177.789 175.878 1.00 4.41  ? 2493 TYR A CE1   1 
ATOM   8154  C  CE2   . TYR A 1 2493 ? 222.247 177.472 176.258 1.00 4.05  ? 2493 TYR A CE2   1 
ATOM   8155  C  CZ    . TYR A 1 2493 ? 221.076 178.154 176.509 1.00 6.44  ? 2493 TYR A CZ    1 
ATOM   8156  O  OH    . TYR A 1 2493 ? 221.070 179.206 177.394 1.00 11.33 ? 2493 TYR A OH    1 
ATOM   8157  N  N     . LEU A 1 2494 ? 218.276 173.298 173.656 1.00 6.87  ? 2494 LEU A N     1 
ATOM   8158  C  CA    . LEU A 1 2494 ? 216.833 173.276 173.866 1.00 3.54  ? 2494 LEU A CA    1 
ATOM   8159  C  C     . LEU A 1 2494 ? 216.450 172.286 174.956 1.00 2.93  ? 2494 LEU A C     1 
ATOM   8160  O  O     . LEU A 1 2494 ? 215.634 172.598 175.830 1.00 3.33  ? 2494 LEU A O     1 
ATOM   8161  C  CB    . LEU A 1 2494 ? 216.122 172.940 172.557 1.00 5.19  ? 2494 LEU A CB    1 
ATOM   8162  C  CG    . LEU A 1 2494 ? 214.620 172.675 172.636 1.00 2.62  ? 2494 LEU A CG    1 
ATOM   8163  C  CD1   . LEU A 1 2494 ? 213.864 173.925 173.058 1.00 2.08  ? 2494 LEU A CD1   1 
ATOM   8164  C  CD2   . LEU A 1 2494 ? 214.125 172.179 171.299 1.00 7.39  ? 2494 LEU A CD2   1 
ATOM   8165  N  N     . VAL A 1 2495 ? 217.039 171.088 174.927 1.00 4.90  ? 2495 VAL A N     1 
ATOM   8166  C  CA    . VAL A 1 2495 ? 216.807 170.117 175.994 1.00 3.59  ? 2495 VAL A CA    1 
ATOM   8167  C  C     . VAL A 1 2495 ? 217.309 170.665 177.323 1.00 3.36  ? 2495 VAL A C     1 
ATOM   8168  O  O     . VAL A 1 2495 ? 216.637 170.552 178.355 1.00 2.96  ? 2495 VAL A O     1 
ATOM   8169  C  CB    . VAL A 1 2495 ? 217.478 168.776 175.645 1.00 3.00  ? 2495 VAL A CB    1 
ATOM   8170  C  CG1   . VAL A 1 2495 ? 217.423 167.825 176.833 1.00 3.72  ? 2495 VAL A CG1   1 
ATOM   8171  C  CG2   . VAL A 1 2495 ? 216.821 168.158 174.426 1.00 3.96  ? 2495 VAL A CG2   1 
ATOM   8172  N  N     . TYR A 1 2496 ? 218.495 171.276 177.313 1.00 4.15  ? 2496 TYR A N     1 
ATOM   8173  C  CA    . TYR A 1 2496 ? 219.032 171.897 178.517 1.00 2.37  ? 2496 TYR A CA    1 
ATOM   8174  C  C     . TYR A 1 2496 ? 218.114 173.003 179.024 1.00 3.70  ? 2496 TYR A C     1 
ATOM   8175  O  O     . TYR A 1 2496 ? 217.849 173.097 180.227 1.00 3.44  ? 2496 TYR A O     1 
ATOM   8176  C  CB    . TYR A 1 2496 ? 220.434 172.435 178.223 1.00 2.70  ? 2496 TYR A CB    1 
ATOM   8177  C  CG    . TYR A 1 2496 ? 220.976 173.428 179.224 1.00 2.69  ? 2496 TYR A CG    1 
ATOM   8178  C  CD1   . TYR A 1 2496 ? 221.618 173.001 180.378 1.00 1.93  ? 2496 TYR A CD1   1 
ATOM   8179  C  CD2   . TYR A 1 2496 ? 220.871 174.794 179.002 1.00 3.12  ? 2496 TYR A CD2   1 
ATOM   8180  C  CE1   . TYR A 1 2496 ? 222.122 173.904 181.288 1.00 3.83  ? 2496 TYR A CE1   1 
ATOM   8181  C  CE2   . TYR A 1 2496 ? 221.370 175.703 179.906 1.00 2.60  ? 2496 TYR A CE2   1 
ATOM   8182  C  CZ    . TYR A 1 2496 ? 221.995 175.256 181.047 1.00 3.19  ? 2496 TYR A CZ    1 
ATOM   8183  O  OH    . TYR A 1 2496 ? 222.495 176.164 181.948 1.00 6.92  ? 2496 TYR A OH    1 
ATOM   8184  N  N     . ALA A 1 2497 ? 217.604 173.838 178.117 1.00 2.61  ? 2497 ALA A N     1 
ATOM   8185  C  CA    . ALA A 1 2497 ? 216.730 174.932 178.523 1.00 1.52  ? 2497 ALA A CA    1 
ATOM   8186  C  C     . ALA A 1 2497 ? 215.390 174.417 179.036 1.00 1.28  ? 2497 ALA A C     1 
ATOM   8187  O  O     . ALA A 1 2497 ? 214.812 174.999 179.960 1.00 1.15  ? 2497 ALA A O     1 
ATOM   8188  C  CB    . ALA A 1 2497 ? 216.527 175.902 177.360 1.00 3.45  ? 2497 ALA A CB    1 
ATOM   8189  N  N     . ILE A 1 2498 ? 214.885 173.330 178.449 1.00 2.00  ? 2498 ILE A N     1 
ATOM   8190  C  CA    . ILE A 1 2498 ? 213.606 172.768 178.881 1.00 1.56  ? 2498 ILE A CA    1 
ATOM   8191  C  C     . ILE A 1 2498 ? 213.693 172.279 180.321 1.00 1.34  ? 2498 ILE A C     1 
ATOM   8192  O  O     . ILE A 1 2498 ? 212.779 172.504 181.124 1.00 1.14  ? 2498 ILE A O     1 
ATOM   8193  C  CB    . ILE A 1 2498 ? 213.169 171.643 177.921 1.00 2.01  ? 2498 ILE A CB    1 
ATOM   8194  C  CG1   . ILE A 1 2498 ? 212.613 172.233 176.625 1.00 1.64  ? 2498 ILE A CG1   1 
ATOM   8195  C  CG2   . ILE A 1 2498 ? 212.148 170.729 178.579 1.00 1.48  ? 2498 ILE A CG2   1 
ATOM   8196  C  CD1   . ILE A 1 2498 ? 212.328 171.200 175.562 1.00 2.32  ? 2498 ILE A CD1   1 
ATOM   8197  N  N     . LEU A 1 2499 ? 214.788 171.602 180.670 1.00 1.78  ? 2499 LEU A N     1 
ATOM   8198  C  CA    . LEU A 1 2499 ? 214.929 171.059 182.019 1.00 1.81  ? 2499 LEU A CA    1 
ATOM   8199  C  C     . LEU A 1 2499 ? 214.945 172.162 183.070 1.00 1.41  ? 2499 LEU A C     1 
ATOM   8200  O  O     . LEU A 1 2499 ? 214.279 172.051 184.105 1.00 1.54  ? 2499 LEU A O     1 
ATOM   8201  C  CB    . LEU A 1 2499 ? 216.200 170.221 182.112 1.00 2.23  ? 2499 LEU A CB    1 
ATOM   8202  C  CG    . LEU A 1 2499 ? 216.127 168.798 181.569 1.00 3.16  ? 2499 LEU A CG    1 
ATOM   8203  C  CD1   . LEU A 1 2499 ? 217.519 168.223 181.478 1.00 3.50  ? 2499 LEU A CD1   1 
ATOM   8204  C  CD2   . LEU A 1 2499 ? 215.251 167.936 182.457 1.00 4.65  ? 2499 LEU A CD2   1 
ATOM   8205  N  N     . TRP A 1 2500 ? 215.695 173.235 182.821 1.00 0.88  ? 2500 TRP A N     1 
ATOM   8206  C  CA    . TRP A 1 2500 ? 215.804 174.300 183.809 1.00 0.78  ? 2500 TRP A CA    1 
ATOM   8207  C  C     . TRP A 1 2500 ? 214.575 175.196 183.840 1.00 0.91  ? 2500 TRP A C     1 
ATOM   8208  O  O     . TRP A 1 2500 ? 214.234 175.733 184.898 1.00 1.23  ? 2500 TRP A O     1 
ATOM   8209  C  CB    . TRP A 1 2500 ? 217.064 175.124 183.552 1.00 1.06  ? 2500 TRP A CB    1 
ATOM   8210  C  CG    . TRP A 1 2500 ? 218.296 174.412 183.989 1.00 0.75  ? 2500 TRP A CG    1 
ATOM   8211  C  CD1   . TRP A 1 2500 ? 219.230 173.822 183.192 1.00 0.70  ? 2500 TRP A CD1   1 
ATOM   8212  C  CD2   . TRP A 1 2500 ? 218.717 174.186 185.336 1.00 0.73  ? 2500 TRP A CD2   1 
ATOM   8213  N  NE1   . TRP A 1 2500 ? 220.215 173.255 183.959 1.00 1.68  ? 2500 TRP A NE1   1 
ATOM   8214  C  CE2   . TRP A 1 2500 ? 219.922 173.464 185.280 1.00 2.45  ? 2500 TRP A CE2   1 
ATOM   8215  C  CE3   . TRP A 1 2500 ? 218.193 174.528 186.586 1.00 0.86  ? 2500 TRP A CE3   1 
ATOM   8216  C  CZ2   . TRP A 1 2500 ? 220.614 173.078 186.425 1.00 2.12  ? 2500 TRP A CZ2   1 
ATOM   8217  C  CZ3   . TRP A 1 2500 ? 218.879 174.144 187.720 1.00 1.23  ? 2500 TRP A CZ3   1 
ATOM   8218  C  CH2   . TRP A 1 2500 ? 220.076 173.428 187.632 1.00 1.70  ? 2500 TRP A CH2   1 
ATOM   8219  N  N     . SER A 1 2501 ? 213.901 175.371 182.706 1.00 1.48  ? 2501 SER A N     1 
ATOM   8220  C  CA    . SER A 1 2501 ? 212.702 176.196 182.671 1.00 0.63  ? 2501 SER A CA    1 
ATOM   8221  C  C     . SER A 1 2501 ? 211.497 175.506 183.291 1.00 1.13  ? 2501 SER A C     1 
ATOM   8222  O  O     . SER A 1 2501 ? 210.581 176.189 183.757 1.00 3.99  ? 2501 SER A O     1 
ATOM   8223  C  CB    . SER A 1 2501 ? 212.384 176.595 181.231 1.00 0.72  ? 2501 SER A CB    1 
ATOM   8224  O  OG    . SER A 1 2501 ? 213.483 177.267 180.645 1.00 0.61  ? 2501 SER A OG    1 
ATOM   8225  N  N     . LEU A 1 2502 ? 211.477 174.173 183.309 1.00 0.75  ? 2502 LEU A N     1 
ATOM   8226  C  CA    . LEU A 1 2502 ? 210.329 173.422 183.789 1.00 1.19  ? 2502 LEU A CA    1 
ATOM   8227  C  C     . LEU A 1 2502 ? 210.563 172.732 185.123 1.00 2.66  ? 2502 LEU A C     1 
ATOM   8228  O  O     . LEU A 1 2502 ? 209.588 172.340 185.773 1.00 6.38  ? 2502 LEU A O     1 
ATOM   8229  C  CB    . LEU A 1 2502 ? 209.912 172.366 182.755 1.00 2.10  ? 2502 LEU A CB    1 
ATOM   8230  C  CG    . LEU A 1 2502 ? 208.983 172.768 181.605 1.00 2.79  ? 2502 LEU A CG    1 
ATOM   8231  C  CD1   . LEU A 1 2502 ? 209.524 173.945 180.804 1.00 1.36  ? 2502 LEU A CD1   1 
ATOM   8232  C  CD2   . LEU A 1 2502 ? 208.752 171.578 180.695 1.00 0.77  ? 2502 LEU A CD2   1 
ATOM   8233  N  N     . SER A 1 2503 ? 211.815 172.575 185.546 1.00 3.89  ? 2503 SER A N     1 
ATOM   8234  C  CA    . SER A 1 2503 ? 212.127 171.904 186.796 1.00 2.21  ? 2503 SER A CA    1 
ATOM   8235  C  C     . SER A 1 2503 ? 213.141 172.654 187.647 1.00 1.80  ? 2503 SER A C     1 
ATOM   8236  O  O     . SER A 1 2503 ? 213.471 172.182 188.740 1.00 4.32  ? 2503 SER A O     1 
ATOM   8237  C  CB    . SER A 1 2503 ? 212.644 170.482 186.526 1.00 2.68  ? 2503 SER A CB    1 
ATOM   8238  O  OG    . SER A 1 2503 ? 213.915 170.510 185.904 1.00 3.60  ? 2503 SER A OG    1 
ATOM   8239  N  N     . GLY A 1 2504 ? 213.636 173.805 187.188 1.00 1.49  ? 2504 GLY A N     1 
ATOM   8240  C  CA    . GLY A 1 2504 ? 214.570 174.587 187.981 1.00 2.13  ? 2504 GLY A CA    1 
ATOM   8241  C  C     . GLY A 1 2504 ? 213.999 175.075 189.294 1.00 0.68  ? 2504 GLY A C     1 
ATOM   8242  O  O     . GLY A 1 2504 ? 214.761 175.444 190.193 1.00 2.90  ? 2504 GLY A O     1 
ATOM   8243  N  N     . ASP A 1 2505 ? 212.677 175.088 189.428 1.00 0.56  ? 2505 ASP A N     1 
ATOM   8244  C  CA    . ASP A 1 2505 ? 212.009 175.459 190.666 1.00 0.97  ? 2505 ASP A CA    1 
ATOM   8245  C  C     . ASP A 1 2505 ? 211.582 174.244 191.480 1.00 2.21  ? 2505 ASP A C     1 
ATOM   8246  O  O     . ASP A 1 2505 ? 210.776 174.378 192.405 1.00 2.46  ? 2505 ASP A O     1 
ATOM   8247  C  CB    . ASP A 1 2505 ? 210.807 176.353 190.360 1.00 1.19  ? 2505 ASP A CB    1 
ATOM   8248  C  CG    . ASP A 1 2505 ? 209.629 175.583 189.808 1.00 6.00  ? 2505 ASP A CG    1 
ATOM   8249  O  OD1   . ASP A 1 2505 ? 209.841 174.624 189.034 1.00 2.81  ? 2505 ASP A OD1   1 
ATOM   8250  O  OD2   . ASP A 1 2505 ? 208.483 175.953 190.133 1.00 11.64 ? 2505 ASP A OD2   1 
ATOM   8251  N  N     . SER A 1 2506 ? 212.106 173.068 191.158 1.00 1.89  ? 2506 SER A N     1 
ATOM   8252  C  CA    . SER A 1 2506 ? 211.786 171.834 191.851 1.00 3.21  ? 2506 SER A CA    1 
ATOM   8253  C  C     . SER A 1 2506 ? 213.055 171.237 192.446 1.00 3.57  ? 2506 SER A C     1 
ATOM   8254  O  O     . SER A 1 2506 ? 214.172 171.635 192.114 1.00 6.28  ? 2506 SER A O     1 
ATOM   8255  C  CB    . SER A 1 2506 ? 211.107 170.836 190.902 1.00 4.48  ? 2506 SER A CB    1 
ATOM   8256  O  OG    . SER A 1 2506 ? 212.042 170.255 190.012 1.00 7.11  ? 2506 SER A OG    1 
ATOM   8257  N  N     . ARG A 1 2507 ? 212.869 170.270 193.341 1.00 4.64  ? 2507 ARG A N     1 
ATOM   8258  C  CA    . ARG A 1 2507 ? 213.999 169.626 193.990 1.00 3.98  ? 2507 ARG A CA    1 
ATOM   8259  C  C     . ARG A 1 2507 ? 214.734 168.709 193.015 1.00 5.12  ? 2507 ARG A C     1 
ATOM   8260  O  O     . ARG A 1 2507 ? 214.291 168.460 191.890 1.00 12.42 ? 2507 ARG A O     1 
ATOM   8261  C  CB    . ARG A 1 2507 ? 213.542 168.831 195.212 1.00 5.04  ? 2507 ARG A CB    1 
ATOM   8262  C  CG    . ARG A 1 2507 ? 212.396 169.457 195.975 1.00 8.13  ? 2507 ARG A CG    1 
ATOM   8263  C  CD    . ARG A 1 2507 ? 211.840 168.494 197.010 1.00 13.43 ? 2507 ARG A CD    1 
ATOM   8264  N  NE    . ARG A 1 2507 ? 211.278 167.293 196.405 1.00 12.14 ? 2507 ARG A NE    1 
ATOM   8265  C  CZ    . ARG A 1 2507 ? 209.984 167.009 196.373 1.00 17.97 ? 2507 ARG A CZ    1 
ATOM   8266  N  NH1   . ARG A 1 2507 ? 209.084 167.822 196.903 1.00 20.82 ? 2507 ARG A NH1   1 
ATOM   8267  N  NH2   . ARG A 1 2507 ? 209.579 165.882 195.795 1.00 17.81 ? 2507 ARG A NH2   1 
ATOM   8268  N  N     . LEU A 1 2508 ? 215.877 168.197 193.474 1.00 8.78  ? 2508 LEU A N     1 
ATOM   8269  C  CA    . LEU A 1 2508 ? 216.738 167.383 192.623 1.00 10.98 ? 2508 LEU A CA    1 
ATOM   8270  C  C     . LEU A 1 2508 ? 216.019 166.135 192.127 1.00 10.36 ? 2508 LEU A C     1 
ATOM   8271  O  O     . LEU A 1 2508 ? 216.174 165.743 190.964 1.00 7.81  ? 2508 LEU A O     1 
ATOM   8272  C  CB    . LEU A 1 2508 ? 218.011 167.004 193.380 1.00 8.50  ? 2508 LEU A CB    1 
ATOM   8273  C  CG    . LEU A 1 2508 ? 218.873 165.898 192.771 1.00 13.31 ? 2508 LEU A CG    1 
ATOM   8274  C  CD1   . LEU A 1 2508 ? 219.727 166.429 191.625 1.00 17.37 ? 2508 LEU A CD1   1 
ATOM   8275  C  CD2   . LEU A 1 2508 ? 219.738 165.253 193.835 1.00 13.71 ? 2508 LEU A CD2   1 
ATOM   8276  N  N     . LYS A 1 2509 ? 215.233 165.495 192.994 1.00 7.99  ? 2509 LYS A N     1 
ATOM   8277  C  CA    . LYS A 1 2509 ? 214.521 164.288 192.589 1.00 9.92  ? 2509 LYS A CA    1 
ATOM   8278  C  C     . LYS A 1 2509 ? 213.522 164.591 191.478 1.00 13.76 ? 2509 LYS A C     1 
ATOM   8279  O  O     . LYS A 1 2509 ? 213.362 163.800 190.542 1.00 12.83 ? 2509 LYS A O     1 
ATOM   8280  C  CB    . LYS A 1 2509 ? 213.834 163.658 193.803 1.00 14.17 ? 2509 LYS A CB    1 
ATOM   8281  C  CG    . LYS A 1 2509 ? 213.069 162.367 193.524 1.00 15.89 ? 2509 LYS A CG    1 
ATOM   8282  C  CD    . LYS A 1 2509 ? 211.596 162.608 193.236 1.00 17.80 ? 2509 LYS A CD    1 
ATOM   8283  C  CE    . LYS A 1 2509 ? 210.855 163.044 194.488 1.00 24.44 ? 2509 LYS A CE    1 
ATOM   8284  N  NZ    . LYS A 1 2509 ? 209.408 163.271 194.225 1.00 22.41 ? 2509 LYS A NZ    1 
ATOM   8285  N  N     . MET A 1 2510 ? 212.839 165.735 191.563 1.00 14.20 ? 2510 MET A N     1 
ATOM   8286  C  CA    . MET A 1 2510 ? 211.924 166.126 190.494 1.00 8.02  ? 2510 MET A CA    1 
ATOM   8287  C  C     . MET A 1 2510 ? 212.683 166.575 189.251 1.00 9.01  ? 2510 MET A C     1 
ATOM   8288  O  O     . MET A 1 2510 ? 212.244 166.316 188.125 1.00 12.06 ? 2510 MET A O     1 
ATOM   8289  C  CB    . MET A 1 2510 ? 210.984 167.224 190.985 1.00 6.41  ? 2510 MET A CB    1 
ATOM   8290  C  CG    . MET A 1 2510 ? 209.977 166.745 192.011 1.00 11.53 ? 2510 MET A CG    1 
ATOM   8291  S  SD    . MET A 1 2510 ? 208.980 165.374 191.402 1.00 18.75 ? 2510 MET A SD    1 
ATOM   8292  C  CE    . MET A 1 2510 ? 207.566 165.463 192.492 1.00 14.80 ? 2510 MET A CE    1 
ATOM   8293  N  N     . ARG A 1 2511 ? 213.820 167.252 189.432 1.00 7.43  ? 2511 ARG A N     1 
ATOM   8294  C  CA    . ARG A 1 2511 ? 214.661 167.594 188.289 1.00 5.90  ? 2511 ARG A CA    1 
ATOM   8295  C  C     . ARG A 1 2511 ? 215.160 166.342 187.590 1.00 10.93 ? 2511 ARG A C     1 
ATOM   8296  O  O     . ARG A 1 2511 ? 215.243 166.299 186.356 1.00 10.36 ? 2511 ARG A O     1 
ATOM   8297  C  CB    . ARG A 1 2511 ? 215.844 168.454 188.729 1.00 5.21  ? 2511 ARG A CB    1 
ATOM   8298  C  CG    . ARG A 1 2511 ? 215.483 169.822 189.240 1.00 5.23  ? 2511 ARG A CG    1 
ATOM   8299  C  CD    . ARG A 1 2511 ? 216.724 170.551 189.708 1.00 5.12  ? 2511 ARG A CD    1 
ATOM   8300  N  NE    . ARG A 1 2511 ? 216.440 171.918 190.124 1.00 2.02  ? 2511 ARG A NE    1 
ATOM   8301  C  CZ    . ARG A 1 2511 ? 217.335 172.731 190.666 1.00 3.26  ? 2511 ARG A CZ    1 
ATOM   8302  N  NH1   . ARG A 1 2511 ? 218.579 172.341 190.884 1.00 2.82  ? 2511 ARG A NH1   1 
ATOM   8303  N  NH2   . ARG A 1 2511 ? 216.971 173.966 190.998 1.00 3.29  ? 2511 ARG A NH2   1 
ATOM   8304  N  N     . ALA A 1 2512 ? 215.516 165.316 188.364 1.00 14.59 ? 2512 ALA A N     1 
ATOM   8305  C  CA    . ALA A 1 2512 ? 215.934 164.057 187.764 1.00 9.12  ? 2512 ALA A CA    1 
ATOM   8306  C  C     . ALA A 1 2512 ? 214.796 163.413 186.985 1.00 6.76  ? 2512 ALA A C     1 
ATOM   8307  O  O     . ALA A 1 2512 ? 214.979 163.030 185.826 1.00 5.60  ? 2512 ALA A O     1 
ATOM   8308  C  CB    . ALA A 1 2512 ? 216.454 163.108 188.842 1.00 9.20  ? 2512 ALA A CB    1 
ATOM   8309  N  N     . GLU A 1 2513 ? 213.603 163.333 187.585 1.00 10.01 ? 2513 GLU A N     1 
ATOM   8310  C  CA    . GLU A 1 2513 ? 212.522 162.553 186.987 1.00 10.15 ? 2513 GLU A CA    1 
ATOM   8311  C  C     . GLU A 1 2513 ? 212.105 163.127 185.639 1.00 10.83 ? 2513 GLU A C     1 
ATOM   8312  O  O     . GLU A 1 2513 ? 211.801 162.377 184.704 1.00 14.97 ? 2513 GLU A O     1 
ATOM   8313  C  CB    . GLU A 1 2513 ? 211.320 162.488 187.928 1.00 9.04  ? 2513 GLU A CB    1 
ATOM   8314  C  CG    . GLU A 1 2513 ? 210.383 161.328 187.616 1.00 18.06 ? 2513 GLU A CG    1 
ATOM   8315  C  CD    . GLU A 1 2513 ? 209.275 161.686 186.646 1.00 20.65 ? 2513 GLU A CD    1 
ATOM   8316  O  OE1   . GLU A 1 2513 ? 208.531 162.646 186.914 1.00 26.62 ? 2513 GLU A OE1   1 
ATOM   8317  O  OE2   . GLU A 1 2513 ? 209.145 160.998 185.613 1.00 23.16 ? 2513 GLU A OE2   1 
ATOM   8318  N  N     . LEU A 1 2514 ? 212.071 164.457 185.524 1.00 9.43  ? 2514 LEU A N     1 
ATOM   8319  C  CA    . LEU A 1 2514 ? 211.829 165.077 184.226 1.00 7.12  ? 2514 LEU A CA    1 
ATOM   8320  C  C     . LEU A 1 2514 ? 212.918 164.694 183.231 1.00 6.51  ? 2514 LEU A C     1 
ATOM   8321  O  O     . LEU A 1 2514 ? 212.678 164.657 182.020 1.00 8.28  ? 2514 LEU A O     1 
ATOM   8322  C  CB    . LEU A 1 2514 ? 211.747 166.598 184.381 1.00 8.72  ? 2514 LEU A CB    1 
ATOM   8323  C  CG    . LEU A 1 2514 ? 211.427 167.432 183.137 1.00 6.81  ? 2514 LEU A CG    1 
ATOM   8324  C  CD1   . LEU A 1 2514 ? 210.089 167.026 182.539 1.00 7.08  ? 2514 LEU A CD1   1 
ATOM   8325  C  CD2   . LEU A 1 2514 ? 211.441 168.915 183.462 1.00 2.89  ? 2514 LEU A CD2   1 
ATOM   8326  N  N     . GLY A 1 2515 ? 214.122 164.404 183.730 1.00 6.97  ? 2515 GLY A N     1 
ATOM   8327  C  CA    . GLY A 1 2515 ? 215.203 163.991 182.850 1.00 6.26  ? 2515 GLY A CA    1 
ATOM   8328  C  C     . GLY A 1 2515 ? 214.953 162.660 182.168 1.00 10.15 ? 2515 GLY A C     1 
ATOM   8329  O  O     . GLY A 1 2515 ? 215.154 162.528 180.959 1.00 9.71  ? 2515 GLY A O     1 
ATOM   8330  N  N     . GLU A 1 2516 ? 214.521 161.645 182.929 1.00 8.25  ? 2516 GLU A N     1 
ATOM   8331  C  CA    . GLU A 1 2516 ? 214.242 160.356 182.300 1.00 10.15 ? 2516 GLU A CA    1 
ATOM   8332  C  C     . GLU A 1 2516 ? 213.066 160.453 181.339 1.00 12.48 ? 2516 GLU A C     1 
ATOM   8333  O  O     . GLU A 1 2516 ? 213.085 159.839 180.267 1.00 15.88 ? 2516 GLU A O     1 
ATOM   8334  C  CB    . GLU A 1 2516 ? 213.984 159.248 183.330 1.00 18.30 ? 2516 GLU A CB    1 
ATOM   8335  C  CG    . GLU A 1 2516 ? 215.183 158.822 184.166 1.00 13.93 ? 2516 GLU A CG    1 
ATOM   8336  C  CD    . GLU A 1 2516 ? 215.387 159.683 185.381 1.00 19.27 ? 2516 GLU A CD    1 
ATOM   8337  O  OE1   . GLU A 1 2516 ? 214.536 160.554 185.611 1.00 25.80 ? 2516 GLU A OE1   1 
ATOM   8338  O  OE2   . GLU A 1 2516 ? 216.389 159.491 186.099 1.00 22.87 ? 2516 GLU A OE2   1 
ATOM   8339  N  N     . TYR A 1 2517 ? 212.033 161.216 181.703 1.00 9.59  ? 2517 TYR A N     1 
ATOM   8340  C  CA    . TYR A 1 2517 ? 210.884 161.349 180.814 1.00 12.79 ? 2517 TYR A CA    1 
ATOM   8341  C  C     . TYR A 1 2517 ? 211.287 161.977 179.489 1.00 13.39 ? 2517 TYR A C     1 
ATOM   8342  O  O     . TYR A 1 2517 ? 210.835 161.542 178.423 1.00 15.80 ? 2517 TYR A O     1 
ATOM   8343  C  CB    . TYR A 1 2517 ? 209.782 162.174 181.472 1.00 11.97 ? 2517 TYR A CB    1 
ATOM   8344  C  CG    . TYR A 1 2517 ? 208.633 162.438 180.532 1.00 12.07 ? 2517 TYR A CG    1 
ATOM   8345  C  CD1   . TYR A 1 2517 ? 207.817 161.401 180.099 1.00 12.95 ? 2517 TYR A CD1   1 
ATOM   8346  C  CD2   . TYR A 1 2517 ? 208.377 163.714 180.054 1.00 13.01 ? 2517 TYR A CD2   1 
ATOM   8347  C  CE1   . TYR A 1 2517 ? 206.774 161.629 179.234 1.00 11.63 ? 2517 TYR A CE1   1 
ATOM   8348  C  CE2   . TYR A 1 2517 ? 207.331 163.951 179.186 1.00 14.09 ? 2517 TYR A CE2   1 
ATOM   8349  C  CZ    . TYR A 1 2517 ? 206.532 162.906 178.779 1.00 12.38 ? 2517 TYR A CZ    1 
ATOM   8350  O  OH    . TYR A 1 2517 ? 205.489 163.135 177.916 1.00 12.75 ? 2517 TYR A OH    1 
ATOM   8351  N  N     . ILE A 1 2518 ? 212.128 163.012 179.534 1.00 10.71 ? 2518 ILE A N     1 
ATOM   8352  C  CA    . ILE A 1 2518 ? 212.654 163.589 178.302 1.00 10.28 ? 2518 ILE A CA    1 
ATOM   8353  C  C     . ILE A 1 2518 ? 213.477 162.554 177.551 1.00 12.34 ? 2518 ILE A C     1 
ATOM   8354  O  O     . ILE A 1 2518 ? 213.348 162.405 176.331 1.00 17.58 ? 2518 ILE A O     1 
ATOM   8355  C  CB    . ILE A 1 2518 ? 213.472 164.858 178.608 1.00 6.34  ? 2518 ILE A CB    1 
ATOM   8356  C  CG1   . ILE A 1 2518 ? 212.551 165.985 179.076 1.00 6.54  ? 2518 ILE A CG1   1 
ATOM   8357  C  CG2   . ILE A 1 2518 ? 214.267 165.295 177.389 1.00 7.34  ? 2518 ILE A CG2   1 
ATOM   8358  C  CD1   . ILE A 1 2518 ? 213.281 167.263 179.414 1.00 5.53  ? 2518 ILE A CD1   1 
ATOM   8359  N  N     . ARG A 1 2519 ? 214.310 161.801 178.273 1.00 11.19 ? 2519 ARG A N     1 
ATOM   8360  C  CA    . ARG A 1 2519 ? 215.160 160.798 177.639 1.00 11.30 ? 2519 ARG A CA    1 
ATOM   8361  C  C     . ARG A 1 2519 ? 214.343 159.760 176.882 1.00 16.17 ? 2519 ARG A C     1 
ATOM   8362  O  O     . ARG A 1 2519 ? 214.783 159.269 175.836 1.00 19.75 ? 2519 ARG A O     1 
ATOM   8363  C  CB    . ARG A 1 2519 ? 216.041 160.129 178.693 1.00 12.25 ? 2519 ARG A CB    1 
ATOM   8364  C  CG    . ARG A 1 2519 ? 216.916 159.007 178.168 1.00 14.57 ? 2519 ARG A CG    1 
ATOM   8365  C  CD    . ARG A 1 2519 ? 217.663 158.328 179.302 1.00 10.16 ? 2519 ARG A CD    1 
ATOM   8366  N  NE    . ARG A 1 2519 ? 218.674 159.203 179.882 1.00 8.96  ? 2519 ARG A NE    1 
ATOM   8367  C  CZ    . ARG A 1 2519 ? 219.786 159.585 179.268 1.00 13.36 ? 2519 ARG A CZ    1 
ATOM   8368  N  NH1   . ARG A 1 2519 ? 220.095 159.147 178.059 1.00 13.41 ? 2519 ARG A NH1   1 
ATOM   8369  N  NH2   . ARG A 1 2519 ? 220.611 160.426 179.885 1.00 10.33 ? 2519 ARG A NH2   1 
ATOM   8370  N  N     . ARG A 1 2520 ? 213.151 159.424 177.380 1.00 13.21 ? 2520 ARG A N     1 
ATOM   8371  C  CA    . ARG A 1 2520 ? 212.301 158.470 176.678 1.00 11.79 ? 2520 ARG A CA    1 
ATOM   8372  C  C     . ARG A 1 2520 ? 211.742 159.059 175.387 1.00 17.68 ? 2520 ARG A C     1 
ATOM   8373  O  O     . ARG A 1 2520 ? 211.784 158.411 174.335 1.00 20.08 ? 2520 ARG A O     1 
ATOM   8374  C  CB    . ARG A 1 2520 ? 211.164 158.010 177.592 1.00 11.88 ? 2520 ARG A CB    1 
ATOM   8375  C  CG    . ARG A 1 2520 ? 211.630 157.421 178.910 1.00 14.79 ? 2520 ARG A CG    1 
ATOM   8376  C  CD    . ARG A 1 2520 ? 210.588 156.506 179.528 1.00 13.27 ? 2520 ARG A CD    1 
ATOM   8377  N  NE    . ARG A 1 2520 ? 209.360 157.215 179.869 1.00 17.26 ? 2520 ARG A NE    1 
ATOM   8378  C  CZ    . ARG A 1 2520 ? 209.130 157.793 181.040 1.00 18.53 ? 2520 ARG A CZ    1 
ATOM   8379  N  NH1   . ARG A 1 2520 ? 210.034 157.785 182.006 1.00 18.10 ? 2520 ARG A NH1   1 
ATOM   8380  N  NH2   . ARG A 1 2520 ? 207.963 158.396 181.248 1.00 21.43 ? 2520 ARG A NH2   1 
ATOM   8381  N  N     . ILE A 1 2521 ? 211.234 160.288 175.438 1.00 16.30 ? 2521 ILE A N     1 
ATOM   8382  C  CA    . ILE A 1 2521 ? 210.448 160.806 174.323 1.00 13.14 ? 2521 ILE A CA    1 
ATOM   8383  C  C     . ILE A 1 2521 ? 211.272 161.613 173.322 1.00 12.04 ? 2521 ILE A C     1 
ATOM   8384  O  O     . ILE A 1 2521 ? 210.833 161.804 172.184 1.00 16.64 ? 2521 ILE A O     1 
ATOM   8385  C  CB    . ILE A 1 2521 ? 209.270 161.640 174.851 1.00 12.14 ? 2521 ILE A CB    1 
ATOM   8386  C  CG1   . ILE A 1 2521 ? 209.776 162.933 175.492 1.00 15.41 ? 2521 ILE A CG1   1 
ATOM   8387  C  CG2   . ILE A 1 2521 ? 208.450 160.833 175.840 1.00 12.55 ? 2521 ILE A CG2   1 
ATOM   8388  C  CD1   . ILE A 1 2521 ? 208.682 163.793 176.051 1.00 13.44 ? 2521 ILE A CD1   1 
ATOM   8389  N  N     . THR A 1 2522 ? 212.447 162.102 173.704 1.00 14.88 ? 2522 THR A N     1 
ATOM   8390  C  CA    . THR A 1 2522 ? 213.183 162.940 172.771 1.00 15.98 ? 2522 THR A CA    1 
ATOM   8391  C  C     . THR A 1 2522 ? 213.970 162.087 171.781 1.00 14.60 ? 2522 THR A C     1 
ATOM   8392  O  O     . THR A 1 2522 ? 214.248 160.907 172.012 1.00 14.02 ? 2522 THR A O     1 
ATOM   8393  C  CB    . THR A 1 2522 ? 214.147 163.881 173.494 1.00 15.88 ? 2522 THR A CB    1 
ATOM   8394  O  OG1   . THR A 1 2522 ? 214.705 164.798 172.545 1.00 14.19 ? 2522 THR A OG1   1 
ATOM   8395  C  CG2   . THR A 1 2522 ? 215.297 163.096 174.106 1.00 18.02 ? 2522 THR A CG2   1 
ATOM   8396  N  N     . THR A 1 2523 ? 214.322 162.709 170.660 1.00 16.02 ? 2523 THR A N     1 
ATOM   8397  C  CA    . THR A 1 2523 ? 215.259 162.137 169.708 1.00 13.17 ? 2523 THR A CA    1 
ATOM   8398  C  C     . THR A 1 2523 ? 216.574 162.900 169.672 1.00 13.39 ? 2523 THR A C     1 
ATOM   8399  O  O     . THR A 1 2523 ? 217.468 162.536 168.902 1.00 16.89 ? 2523 THR A O     1 
ATOM   8400  C  CB    . THR A 1 2523 ? 214.642 162.092 168.306 1.00 16.99 ? 2523 THR A CB    1 
ATOM   8401  O  OG1   . THR A 1 2523 ? 214.337 163.422 167.871 1.00 29.08 ? 2523 THR A OG1   1 
ATOM   8402  C  CG2   . THR A 1 2523 ? 213.370 161.266 168.317 1.00 14.91 ? 2523 THR A CG2   1 
ATOM   8403  N  N     . VAL A 1 2524 ? 216.705 163.949 170.473 1.00 13.75 ? 2524 VAL A N     1 
ATOM   8404  C  CA    . VAL A 1 2524 ? 217.976 164.673 170.583 1.00 11.28 ? 2524 VAL A CA    1 
ATOM   8405  C  C     . VAL A 1 2524 ? 218.999 163.777 171.269 1.00 13.40 ? 2524 VAL A C     1 
ATOM   8406  O  O     . VAL A 1 2524 ? 218.667 163.120 172.272 1.00 13.28 ? 2524 VAL A O     1 
ATOM   8407  C  CB    . VAL A 1 2524 ? 217.774 165.976 171.358 1.00 11.56 ? 2524 VAL A CB    1 
ATOM   8408  C  CG1   . VAL A 1 2524 ? 219.074 166.755 171.453 1.00 13.03 ? 2524 VAL A CG1   1 
ATOM   8409  C  CG2   . VAL A 1 2524 ? 216.692 166.816 170.704 1.00 12.17 ? 2524 VAL A CG2   1 
ATOM   8410  N  N     . PRO A 1 2525 ? 220.231 163.693 170.768 1.00 14.23 ? 2525 PRO A N     1 
ATOM   8411  C  CA    . PRO A 1 2525 ? 221.252 162.902 171.464 1.00 12.06 ? 2525 PRO A CA    1 
ATOM   8412  C  C     . PRO A 1 2525 ? 221.480 163.423 172.876 1.00 14.57 ? 2525 PRO A C     1 
ATOM   8413  O  O     . PRO A 1 2525 ? 221.472 164.628 173.125 1.00 21.87 ? 2525 PRO A O     1 
ATOM   8414  C  CB    . PRO A 1 2525 ? 222.496 163.081 170.587 1.00 8.35  ? 2525 PRO A CB    1 
ATOM   8415  C  CG    . PRO A 1 2525 ? 221.960 163.406 169.239 1.00 13.57 ? 2525 PRO A CG    1 
ATOM   8416  C  CD    . PRO A 1 2525 ? 220.705 164.194 169.468 1.00 11.84 ? 2525 PRO A CD    1 
ATOM   8417  N  N     . LEU A 1 2526 ? 221.689 162.495 173.796 1.00 11.99 ? 2526 LEU A N     1 
ATOM   8418  C  CA    . LEU A 1 2526 ? 221.785 162.774 175.218 1.00 12.16 ? 2526 LEU A CA    1 
ATOM   8419  C  C     . LEU A 1 2526 ? 223.026 162.107 175.788 1.00 17.73 ? 2526 LEU A C     1 
ATOM   8420  O  O     . LEU A 1 2526 ? 223.578 161.186 175.178 1.00 22.93 ? 2526 LEU A O     1 
ATOM   8421  C  CB    . LEU A 1 2526 ? 220.531 162.272 175.950 1.00 9.34  ? 2526 LEU A CB    1 
ATOM   8422  C  CG    . LEU A 1 2526 ? 219.226 162.982 175.590 1.00 6.99  ? 2526 LEU A CG    1 
ATOM   8423  C  CD1   . LEU A 1 2526 ? 218.118 162.516 176.500 1.00 8.46  ? 2526 LEU A CD1   1 
ATOM   8424  C  CD2   . LEU A 1 2526 ? 219.383 164.492 175.679 1.00 12.43 ? 2526 LEU A CD2   1 
ATOM   8425  N  N     . PRO A 1 2527 ? 223.511 162.572 176.940 1.00 15.81 ? 2527 PRO A N     1 
ATOM   8426  C  CA    . PRO A 1 2527 ? 224.656 161.907 177.570 1.00 13.83 ? 2527 PRO A CA    1 
ATOM   8427  C  C     . PRO A 1 2527 ? 224.347 160.447 177.872 1.00 18.75 ? 2527 PRO A C     1 
ATOM   8428  O  O     . PRO A 1 2527 ? 223.243 160.100 178.295 1.00 19.49 ? 2527 PRO A O     1 
ATOM   8429  C  CB    . PRO A 1 2527 ? 224.874 162.716 178.852 1.00 13.43 ? 2527 PRO A CB    1 
ATOM   8430  C  CG    . PRO A 1 2527 ? 224.295 164.051 178.551 1.00 9.16  ? 2527 PRO A CG    1 
ATOM   8431  C  CD    . PRO A 1 2527 ? 223.111 163.784 177.676 1.00 11.29 ? 2527 PRO A CD    1 
ATOM   8432  N  N     . THR A 1 2528 ? 225.345 159.594 177.657 1.00 18.05 ? 2528 THR A N     1 
ATOM   8433  C  CA    . THR A 1 2528 ? 225.186 158.152 177.762 1.00 19.64 ? 2528 THR A CA    1 
ATOM   8434  C  C     . THR A 1 2528 ? 225.625 157.603 179.113 1.00 25.18 ? 2528 THR A C     1 
ATOM   8435  O  O     . THR A 1 2528 ? 225.780 156.386 179.253 1.00 27.80 ? 2528 THR A O     1 
ATOM   8436  C  CB    . THR A 1 2528 ? 225.962 157.456 176.643 1.00 21.56 ? 2528 THR A CB    1 
ATOM   8437  O  OG1   . THR A 1 2528 ? 227.355 157.765 176.764 1.00 21.66 ? 2528 THR A OG1   1 
ATOM   8438  C  CG2   . THR A 1 2528 ? 225.461 157.913 175.282 1.00 16.88 ? 2528 THR A CG2   1 
ATOM   8439  N  N     . ALA A 1 2529 ? 225.836 158.467 180.101 1.00 29.55 ? 2529 ALA A N     1 
ATOM   8440  C  CA    . ALA A 1 2529 ? 226.232 158.002 181.419 1.00 18.30 ? 2529 ALA A CA    1 
ATOM   8441  C  C     . ALA A 1 2529 ? 225.121 157.145 182.021 1.00 25.48 ? 2529 ALA A C     1 
ATOM   8442  O  O     . ALA A 1 2529 ? 223.936 157.405 181.782 1.00 29.63 ? 2529 ALA A O     1 
ATOM   8443  C  CB    . ALA A 1 2529 ? 226.544 159.184 182.336 1.00 24.44 ? 2529 ALA A CB    1 
ATOM   8444  N  N     . PRO A 1 2530 ? 225.463 156.113 182.799 1.00 26.62 ? 2530 PRO A N     1 
ATOM   8445  C  CA    . PRO A 1 2530 ? 224.412 155.205 183.286 1.00 25.09 ? 2530 PRO A CA    1 
ATOM   8446  C  C     . PRO A 1 2530 ? 223.497 155.825 184.326 1.00 24.85 ? 2530 PRO A C     1 
ATOM   8447  O  O     . PRO A 1 2530 ? 222.274 155.657 184.236 1.00 27.72 ? 2530 PRO A O     1 
ATOM   8448  C  CB    . PRO A 1 2530 ? 225.218 154.031 183.858 1.00 23.95 ? 2530 PRO A CB    1 
ATOM   8449  C  CG    . PRO A 1 2530 ? 226.510 154.647 184.276 1.00 24.00 ? 2530 PRO A CG    1 
ATOM   8450  C  CD    . PRO A 1 2530 ? 226.805 155.694 183.240 1.00 26.84 ? 2530 PRO A CD    1 
ATOM   8451  N  N     . ASN A 1 2531 ? 224.044 156.542 185.311 1.00 20.80 ? 2531 ASN A N     1 
ATOM   8452  C  CA    . ASN A 1 2531 ? 223.251 157.003 186.446 1.00 24.14 ? 2531 ASN A CA    1 
ATOM   8453  C  C     . ASN A 1 2531 ? 223.438 158.491 186.732 1.00 20.43 ? 2531 ASN A C     1 
ATOM   8454  O  O     . ASN A 1 2531 ? 223.186 158.934 187.857 1.00 23.79 ? 2531 ASN A O     1 
ATOM   8455  C  CB    . ASN A 1 2531 ? 223.584 156.186 187.697 1.00 21.65 ? 2531 ASN A CB    1 
ATOM   8456  C  CG    . ASN A 1 2531 ? 223.600 154.693 187.430 1.00 31.91 ? 2531 ASN A CG    1 
ATOM   8457  O  OD1   . ASN A 1 2531 ? 224.631 154.036 187.572 1.00 31.19 ? 2531 ASN A OD1   1 
ATOM   8458  N  ND2   . ASN A 1 2531 ? 222.454 154.150 187.039 1.00 25.94 ? 2531 ASN A ND2   1 
ATOM   8459  N  N     . ILE A 1 2532 ? 223.866 159.270 185.749 1.00 17.71 ? 2532 ILE A N     1 
ATOM   8460  C  CA    . ILE A 1 2532 ? 224.091 160.703 185.916 1.00 11.19 ? 2532 ILE A CA    1 
ATOM   8461  C  C     . ILE A 1 2532 ? 222.897 161.444 185.326 1.00 11.93 ? 2532 ILE A C     1 
ATOM   8462  O  O     . ILE A 1 2532 ? 222.611 161.276 184.130 1.00 12.46 ? 2532 ILE A O     1 
ATOM   8463  C  CB    . ILE A 1 2532 ? 225.402 161.151 185.255 1.00 12.85 ? 2532 ILE A CB    1 
ATOM   8464  C  CG1   . ILE A 1 2532 ? 226.582 160.392 185.860 1.00 14.55 ? 2532 ILE A CG1   1 
ATOM   8465  C  CG2   . ILE A 1 2532 ? 225.598 162.648 185.427 1.00 11.57 ? 2532 ILE A CG2   1 
ATOM   8466  C  CD1   . ILE A 1 2532 ? 226.756 160.626 187.343 1.00 16.02 ? 2532 ILE A CD1   1 
ATOM   8467  N  N     . PRO A 1 2533 ? 222.181 162.251 186.107 1.00 8.96  ? 2533 PRO A N     1 
ATOM   8468  C  CA    . PRO A 1 2533 ? 221.033 162.983 185.558 1.00 8.63  ? 2533 PRO A CA    1 
ATOM   8469  C  C     . PRO A 1 2533 ? 221.460 163.962 184.476 1.00 8.40  ? 2533 PRO A C     1 
ATOM   8470  O  O     . PRO A 1 2533 ? 222.586 164.463 184.467 1.00 17.53 ? 2533 PRO A O     1 
ATOM   8471  C  CB    . PRO A 1 2533 ? 220.455 163.713 186.776 1.00 9.79  ? 2533 PRO A CB    1 
ATOM   8472  C  CG    . PRO A 1 2533 ? 221.535 163.714 187.792 1.00 6.26  ? 2533 PRO A CG    1 
ATOM   8473  C  CD    . PRO A 1 2533 ? 222.375 162.504 187.543 1.00 7.33  ? 2533 PRO A CD    1 
ATOM   8474  N  N     . ILE A 1 2534 ? 220.539 164.220 183.545 1.00 8.51  ? 2534 ILE A N     1 
ATOM   8475  C  CA    . ILE A 1 2534 ? 220.835 165.115 182.431 1.00 7.16  ? 2534 ILE A CA    1 
ATOM   8476  C  C     . ILE A 1 2534 ? 221.066 166.533 182.934 1.00 5.28  ? 2534 ILE A C     1 
ATOM   8477  O  O     . ILE A 1 2534 ? 221.869 167.284 182.367 1.00 5.73  ? 2534 ILE A O     1 
ATOM   8478  C  CB    . ILE A 1 2534 ? 219.697 165.059 181.393 1.00 6.36  ? 2534 ILE A CB    1 
ATOM   8479  C  CG1   . ILE A 1 2534 ? 219.587 163.655 180.809 1.00 8.36  ? 2534 ILE A CG1   1 
ATOM   8480  C  CG2   . ILE A 1 2534 ? 219.968 166.025 180.253 1.00 4.20  ? 2534 ILE A CG2   1 
ATOM   8481  C  CD1   . ILE A 1 2534 ? 218.342 163.441 179.982 1.00 12.46 ? 2534 ILE A CD1   1 
ATOM   8482  N  N     . ILE A 1 2535 ? 220.385 166.916 184.016 1.00 4.84  ? 2535 ILE A N     1 
ATOM   8483  C  CA    . ILE A 1 2535 ? 220.550 168.229 184.619 1.00 4.57  ? 2535 ILE A CA    1 
ATOM   8484  C  C     . ILE A 1 2535 ? 221.978 168.476 185.094 1.00 6.11  ? 2535 ILE A C     1 
ATOM   8485  O  O     . ILE A 1 2535 ? 222.330 169.614 185.413 1.00 6.97  ? 2535 ILE A O     1 
ATOM   8486  C  CB    . ILE A 1 2535 ? 219.544 168.391 185.782 1.00 7.68  ? 2535 ILE A CB    1 
ATOM   8487  C  CG1   . ILE A 1 2535 ? 219.250 169.866 186.052 1.00 6.74  ? 2535 ILE A CG1   1 
ATOM   8488  C  CG2   . ILE A 1 2535 ? 220.058 167.710 187.041 1.00 6.61  ? 2535 ILE A CG2   1 
ATOM   8489  C  CD1   . ILE A 1 2535 ? 218.283 170.478 185.074 1.00 2.24  ? 2535 ILE A CD1   1 
ATOM   8490  N  N     . ASP A 1 2536 ? 222.807 167.437 185.138 1.00 5.95  ? 2536 ASP A N     1 
ATOM   8491  C  CA    . ASP A 1 2536 ? 224.205 167.545 185.531 1.00 5.12  ? 2536 ASP A CA    1 
ATOM   8492  C  C     . ASP A 1 2536 ? 225.126 167.853 184.357 1.00 4.81  ? 2536 ASP A C     1 
ATOM   8493  O  O     . ASP A 1 2536 ? 226.349 167.835 184.522 1.00 6.00  ? 2536 ASP A O     1 
ATOM   8494  C  CB    . ASP A 1 2536 ? 224.660 166.250 186.213 1.00 6.09  ? 2536 ASP A CB    1 
ATOM   8495  C  CG    . ASP A 1 2536 ? 224.156 166.131 187.637 1.00 12.60 ? 2536 ASP A CG    1 
ATOM   8496  O  OD1   . ASP A 1 2536 ? 223.463 167.057 188.105 1.00 14.10 ? 2536 ASP A OD1   1 
ATOM   8497  O  OD2   . ASP A 1 2536 ? 224.449 165.108 188.287 1.00 17.31 ? 2536 ASP A OD2   1 
ATOM   8498  N  N     . TYR A 1 2537 ? 224.570 168.126 183.181 1.00 5.81  ? 2537 TYR A N     1 
ATOM   8499  C  CA    . TYR A 1 2537 ? 225.344 168.376 181.976 1.00 3.82  ? 2537 TYR A CA    1 
ATOM   8500  C  C     . TYR A 1 2537 ? 224.992 169.744 181.410 1.00 4.62  ? 2537 TYR A C     1 
ATOM   8501  O  O     . TYR A 1 2537 ? 223.825 170.147 181.418 1.00 7.71  ? 2537 TYR A O     1 
ATOM   8502  C  CB    . TYR A 1 2537 ? 225.074 167.304 180.914 1.00 4.45  ? 2537 TYR A CB    1 
ATOM   8503  C  CG    . TYR A 1 2537 ? 225.784 165.991 181.136 1.00 5.05  ? 2537 TYR A CG    1 
ATOM   8504  C  CD1   . TYR A 1 2537 ? 225.201 164.986 181.894 1.00 5.48  ? 2537 TYR A CD1   1 
ATOM   8505  C  CD2   . TYR A 1 2537 ? 227.026 165.747 180.569 1.00 6.88  ? 2537 TYR A CD2   1 
ATOM   8506  C  CE1   . TYR A 1 2537 ? 225.839 163.781 182.091 1.00 6.13  ? 2537 TYR A CE1   1 
ATOM   8507  C  CE2   . TYR A 1 2537 ? 227.674 164.543 180.763 1.00 5.10  ? 2537 TYR A CE2   1 
ATOM   8508  C  CZ    . TYR A 1 2537 ? 227.075 163.564 181.524 1.00 8.75  ? 2537 TYR A CZ    1 
ATOM   8509  O  OH    . TYR A 1 2537 ? 227.713 162.361 181.724 1.00 17.76 ? 2537 TYR A OH    1 
ATOM   8510  N  N     . GLU A 1 2538 ? 226.000 170.453 180.921 1.00 6.20  ? 2538 GLU A N     1 
ATOM   8511  C  CA    . GLU A 1 2538 ? 225.798 171.663 180.138 1.00 8.86  ? 2538 GLU A CA    1 
ATOM   8512  C  C     . GLU A 1 2538 ? 225.996 171.345 178.660 1.00 7.01  ? 2538 GLU A C     1 
ATOM   8513  O  O     . GLU A 1 2538 ? 226.307 170.215 178.277 1.00 8.63  ? 2538 GLU A O     1 
ATOM   8514  C  CB    . GLU A 1 2538 ? 226.749 172.774 180.582 1.00 6.49  ? 2538 GLU A CB    1 
ATOM   8515  C  CG    . GLU A 1 2538 ? 228.207 172.425 180.410 1.00 7.12  ? 2538 GLU A CG    1 
ATOM   8516  C  CD    . GLU A 1 2538 ? 229.078 173.645 180.244 1.00 13.71 ? 2538 GLU A CD    1 
ATOM   8517  O  OE1   . GLU A 1 2538 ? 229.965 173.623 179.363 1.00 14.87 ? 2538 GLU A OE1   1 
ATOM   8518  O  OE2   . GLU A 1 2538 ? 228.873 174.627 180.984 1.00 16.39 ? 2538 GLU A OE2   1 
ATOM   8519  N  N     . VAL A 1 2539 ? 225.821 172.364 177.826 1.00 5.23  ? 2539 VAL A N     1 
ATOM   8520  C  CA    . VAL A 1 2539 ? 226.002 172.240 176.385 1.00 5.33  ? 2539 VAL A CA    1 
ATOM   8521  C  C     . VAL A 1 2539 ? 227.116 173.188 175.974 1.00 6.30  ? 2539 VAL A C     1 
ATOM   8522  O  O     . VAL A 1 2539 ? 226.974 174.411 176.091 1.00 8.81  ? 2539 VAL A O     1 
ATOM   8523  C  CB    . VAL A 1 2539 ? 224.707 172.544 175.614 1.00 5.78  ? 2539 VAL A CB    1 
ATOM   8524  C  CG1   . VAL A 1 2539 ? 224.884 172.224 174.141 1.00 4.87  ? 2539 VAL A CG1   1 
ATOM   8525  C  CG2   . VAL A 1 2539 ? 223.541 171.761 176.198 1.00 2.78  ? 2539 VAL A CG2   1 
ATOM   8526  N  N     . SER A 1 2540 ? 228.224 172.628 175.500 1.00 8.62  ? 2540 SER A N     1 
ATOM   8527  C  CA    . SER A 1 2540 ? 229.318 173.442 174.998 1.00 9.64  ? 2540 SER A CA    1 
ATOM   8528  C  C     . SER A 1 2540 ? 228.961 174.011 173.628 1.00 11.38 ? 2540 SER A C     1 
ATOM   8529  O  O     . SER A 1 2540 ? 228.121 173.473 172.901 1.00 13.19 ? 2540 SER A O     1 
ATOM   8530  C  CB    . SER A 1 2540 ? 230.607 172.626 174.915 1.00 10.23 ? 2540 SER A CB    1 
ATOM   8531  O  OG    . SER A 1 2540 ? 230.458 171.518 174.044 1.00 20.57 ? 2540 SER A OG    1 
ATOM   8532  N  N     . ILE A 1 2541 ? 229.624 175.113 173.274 1.00 10.35 ? 2541 ILE A N     1 
ATOM   8533  C  CA    . ILE A 1 2541 ? 229.329 175.814 172.034 1.00 10.55 ? 2541 ILE A CA    1 
ATOM   8534  C  C     . ILE A 1 2541 ? 229.608 174.954 170.808 1.00 13.87 ? 2541 ILE A C     1 
ATOM   8535  O  O     . ILE A 1 2541 ? 229.123 175.261 169.716 1.00 15.79 ? 2541 ILE A O     1 
ATOM   8536  C  CB    . ILE A 1 2541 ? 230.122 177.141 171.982 1.00 12.86 ? 2541 ILE A CB    1 
ATOM   8537  C  CG1   . ILE A 1 2541 ? 229.602 178.048 170.866 1.00 17.22 ? 2541 ILE A CG1   1 
ATOM   8538  C  CG2   . ILE A 1 2541 ? 231.601 176.873 171.787 1.00 9.28  ? 2541 ILE A CG2   1 
ATOM   8539  C  CD1   . ILE A 1 2541 ? 228.192 178.539 171.085 1.00 10.40 ? 2541 ILE A CD1   1 
ATOM   8540  N  N     . SER A 1 2542 ? 230.360 173.868 170.966 1.00 15.24 ? 2542 SER A N     1 
ATOM   8541  C  CA    . SER A 1 2542 ? 230.615 172.919 169.892 1.00 11.48 ? 2542 SER A CA    1 
ATOM   8542  C  C     . SER A 1 2542 ? 229.497 171.892 169.734 1.00 15.93 ? 2542 SER A C     1 
ATOM   8543  O  O     . SER A 1 2542 ? 229.678 170.906 169.014 1.00 18.61 ? 2542 SER A O     1 
ATOM   8544  C  CB    . SER A 1 2542 ? 231.943 172.198 170.129 1.00 14.45 ? 2542 SER A CB    1 
ATOM   8545  O  OG    . SER A 1 2542 ? 231.843 171.297 171.218 1.00 16.24 ? 2542 SER A OG    1 
ATOM   8546  N  N     . GLY A 1 2543 ? 228.360 172.098 170.388 1.00 14.82 ? 2543 GLY A N     1 
ATOM   8547  C  CA    . GLY A 1 2543 ? 227.252 171.165 170.292 1.00 11.70 ? 2543 GLY A CA    1 
ATOM   8548  C  C     . GLY A 1 2543 ? 227.524 169.812 170.908 1.00 14.20 ? 2543 GLY A C     1 
ATOM   8549  O  O     . GLY A 1 2543 ? 227.040 168.794 170.399 1.00 17.15 ? 2543 GLY A O     1 
ATOM   8550  N  N     . GLU A 1 2544 ? 228.288 169.772 171.992 1.00 13.53 ? 2544 GLU A N     1 
ATOM   8551  C  CA    . GLU A 1 2544 ? 228.570 168.539 172.705 1.00 11.31 ? 2544 GLU A CA    1 
ATOM   8552  C  C     . GLU A 1 2544 ? 228.105 168.686 174.143 1.00 14.47 ? 2544 GLU A C     1 
ATOM   8553  O  O     . GLU A 1 2544 ? 228.260 169.754 174.745 1.00 17.32 ? 2544 GLU A O     1 
ATOM   8554  C  CB    . GLU A 1 2544 ? 230.066 168.195 172.677 1.00 9.82  ? 2544 GLU A CB    1 
ATOM   8555  C  CG    . GLU A 1 2544 ? 230.658 168.040 171.285 1.00 13.29 ? 2544 GLU A CG    1 
ATOM   8556  C  CD    . GLU A 1 2544 ? 229.908 167.042 170.424 1.00 21.38 ? 2544 GLU A CD    1 
ATOM   8557  O  OE1   . GLU A 1 2544 ? 229.553 165.956 170.926 1.00 23.93 ? 2544 GLU A OE1   1 
ATOM   8558  O  OE2   . GLU A 1 2544 ? 229.679 167.345 169.234 1.00 23.07 ? 2544 GLU A OE2   1 
ATOM   8559  N  N     . TRP A 1 2545 ? 227.520 167.627 174.686 1.00 10.57 ? 2545 TRP A N     1 
ATOM   8560  C  CA    . TRP A 1 2545 ? 227.262 167.587 176.115 1.00 9.48  ? 2545 TRP A CA    1 
ATOM   8561  C  C     . TRP A 1 2545 ? 228.589 167.556 176.860 1.00 12.51 ? 2545 TRP A C     1 
ATOM   8562  O  O     . TRP A 1 2545 ? 229.480 166.769 176.528 1.00 20.57 ? 2545 TRP A O     1 
ATOM   8563  C  CB    . TRP A 1 2545 ? 226.423 166.364 176.482 1.00 11.45 ? 2545 TRP A CB    1 
ATOM   8564  C  CG    . TRP A 1 2545 ? 225.001 166.444 176.031 1.00 9.81  ? 2545 TRP A CG    1 
ATOM   8565  C  CD1   . TRP A 1 2545 ? 224.444 165.789 174.974 1.00 9.11  ? 2545 TRP A CD1   1 
ATOM   8566  C  CD2   . TRP A 1 2545 ? 223.954 167.230 176.613 1.00 8.80  ? 2545 TRP A CD2   1 
ATOM   8567  N  NE1   . TRP A 1 2545 ? 223.114 166.107 174.868 1.00 8.28  ? 2545 TRP A NE1   1 
ATOM   8568  C  CE2   . TRP A 1 2545 ? 222.788 166.993 175.859 1.00 8.02  ? 2545 TRP A CE2   1 
ATOM   8569  C  CE3   . TRP A 1 2545 ? 223.887 168.105 177.702 1.00 9.10  ? 2545 TRP A CE3   1 
ATOM   8570  C  CZ2   . TRP A 1 2545 ? 221.570 167.602 176.157 1.00 7.51  ? 2545 TRP A CZ2   1 
ATOM   8571  C  CZ3   . TRP A 1 2545 ? 222.676 168.707 177.994 1.00 6.72  ? 2545 TRP A CZ3   1 
ATOM   8572  C  CH2   . TRP A 1 2545 ? 221.536 168.454 177.225 1.00 6.15  ? 2545 TRP A CH2   1 
ATOM   8573  N  N     . SER A 1 2546 ? 228.729 168.423 177.858 1.00 9.60  ? 2546 SER A N     1 
ATOM   8574  C  CA    . SER A 1 2546 ? 229.914 168.438 178.699 1.00 6.70  ? 2546 SER A CA    1 
ATOM   8575  C  C     . SER A 1 2546 ? 229.464 168.392 180.153 1.00 9.23  ? 2546 SER A C     1 
ATOM   8576  O  O     . SER A 1 2546 ? 228.575 169.162 180.550 1.00 10.76 ? 2546 SER A O     1 
ATOM   8577  C  CB    . SER A 1 2546 ? 230.781 169.675 178.438 1.00 10.67 ? 2546 SER A CB    1 
ATOM   8578  O  OG    . SER A 1 2546 ? 229.995 170.850 178.375 1.00 13.32 ? 2546 SER A OG    1 
ATOM   8579  N  N     . PRO A 1 2547 ? 230.029 167.502 180.966 1.00 8.25  ? 2547 PRO A N     1 
ATOM   8580  C  CA    . PRO A 1 2547 ? 229.605 167.418 182.367 1.00 6.18  ? 2547 PRO A CA    1 
ATOM   8581  C  C     . PRO A 1 2547 ? 229.903 168.706 183.119 1.00 5.94  ? 2547 PRO A C     1 
ATOM   8582  O  O     . PRO A 1 2547 ? 230.928 169.354 182.900 1.00 7.98  ? 2547 PRO A O     1 
ATOM   8583  C  CB    . PRO A 1 2547 ? 230.419 166.240 182.912 1.00 5.35  ? 2547 PRO A CB    1 
ATOM   8584  C  CG    . PRO A 1 2547 ? 231.604 166.156 182.015 1.00 6.21  ? 2547 PRO A CG    1 
ATOM   8585  C  CD    . PRO A 1 2547 ? 231.121 166.565 180.658 1.00 5.43  ? 2547 PRO A CD    1 
ATOM   8586  N  N     . TRP A 1 2548 ? 228.986 169.073 184.014 1.00 4.60  ? 2548 TRP A N     1 
ATOM   8587  C  CA    . TRP A 1 2548 ? 229.186 170.251 184.845 1.00 4.28  ? 2548 TRP A CA    1 
ATOM   8588  C  C     . TRP A 1 2548 ? 230.352 170.080 185.810 1.00 6.03  ? 2548 TRP A C     1 
ATOM   8589  O  O     . TRP A 1 2548 ? 230.900 171.079 186.285 1.00 6.86  ? 2548 TRP A O     1 
ATOM   8590  C  CB    . TRP A 1 2548 ? 227.912 170.561 185.629 1.00 3.91  ? 2548 TRP A CB    1 
ATOM   8591  C  CG    . TRP A 1 2548 ? 226.945 171.464 184.926 1.00 3.93  ? 2548 TRP A CG    1 
ATOM   8592  C  CD1   . TRP A 1 2548 ? 225.660 171.171 184.576 1.00 3.90  ? 2548 TRP A CD1   1 
ATOM   8593  C  CD2   . TRP A 1 2548 ? 227.177 172.814 184.504 1.00 3.66  ? 2548 TRP A CD2   1 
ATOM   8594  N  NE1   . TRP A 1 2548 ? 225.077 172.250 183.961 1.00 3.30  ? 2548 TRP A NE1   1 
ATOM   8595  C  CE2   . TRP A 1 2548 ? 225.987 173.272 183.903 1.00 3.74  ? 2548 TRP A CE2   1 
ATOM   8596  C  CE3   . TRP A 1 2548 ? 228.272 173.676 184.571 1.00 2.21  ? 2548 TRP A CE3   1 
ATOM   8597  C  CZ2   . TRP A 1 2548 ? 225.865 174.554 183.374 1.00 4.95  ? 2548 TRP A CZ2   1 
ATOM   8598  C  CZ3   . TRP A 1 2548 ? 228.148 174.946 184.046 1.00 2.96  ? 2548 TRP A CZ3   1 
ATOM   8599  C  CH2   . TRP A 1 2548 ? 226.955 175.372 183.453 1.00 4.48  ? 2548 TRP A CH2   1 
ATOM   8600  N  N     . GLN A 1 2549 ? 230.741 168.836 186.105 1.00 6.58  ? 2549 GLN A N     1 
ATOM   8601  C  CA    . GLN A 1 2549 ? 231.841 168.582 187.025 1.00 8.36  ? 2549 GLN A CA    1 
ATOM   8602  C  C     . GLN A 1 2549 ? 233.178 169.064 186.478 1.00 12.06 ? 2549 GLN A C     1 
ATOM   8603  O  O     . GLN A 1 2549 ? 234.108 169.288 187.260 1.00 15.96 ? 2549 GLN A O     1 
ATOM   8604  C  CB    . GLN A 1 2549 ? 231.916 167.090 187.346 1.00 8.62  ? 2549 GLN A CB    1 
ATOM   8605  C  CG    . GLN A 1 2549 ? 232.652 166.757 188.632 1.00 12.38 ? 2549 GLN A CG    1 
ATOM   8606  C  CD    . GLN A 1 2549 ? 231.900 167.213 189.865 1.00 14.88 ? 2549 GLN A CD    1 
ATOM   8607  O  OE1   . GLN A 1 2549 ? 230.772 166.786 190.111 1.00 19.96 ? 2549 GLN A OE1   1 
ATOM   8608  N  NE2   . GLN A 1 2549 ? 232.524 168.079 190.652 1.00 15.65 ? 2549 GLN A NE2   1 
ATOM   8609  N  N     . ALA A 1 2550 ? 233.297 169.229 185.159 1.00 10.36 ? 2550 ALA A N     1 
ATOM   8610  C  CA    . ALA A 1 2550 ? 234.529 169.748 184.580 1.00 6.69  ? 2550 ALA A CA    1 
ATOM   8611  C  C     . ALA A 1 2550 ? 234.783 171.198 184.968 1.00 10.65 ? 2550 ALA A C     1 
ATOM   8612  O  O     . ALA A 1 2550 ? 235.925 171.659 184.880 1.00 14.85 ? 2550 ALA A O     1 
ATOM   8613  C  CB    . ALA A 1 2550 ? 234.493 169.614 183.058 1.00 8.77  ? 2550 ALA A CB    1 
ATOM   8614  N  N     . LYS A 1 2551 ? 233.748 171.924 185.389 1.00 11.25 ? 2551 LYS A N     1 
ATOM   8615  C  CA    . LYS A 1 2551 ? 233.875 173.306 185.827 1.00 9.29  ? 2551 LYS A CA    1 
ATOM   8616  C  C     . LYS A 1 2551 ? 233.817 173.438 187.343 1.00 9.62  ? 2551 LYS A C     1 
ATOM   8617  O  O     . LYS A 1 2551 ? 233.531 174.525 187.856 1.00 15.33 ? 2551 LYS A O     1 
ATOM   8618  C  CB    . LYS A 1 2551 ? 232.792 174.165 185.175 1.00 7.76  ? 2551 LYS A CB    1 
ATOM   8619  C  CG    . LYS A 1 2551 ? 232.960 174.333 183.677 1.00 9.89  ? 2551 LYS A CG    1 
ATOM   8620  C  CD    . LYS A 1 2551 ? 231.974 175.341 183.119 1.00 12.64 ? 2551 LYS A CD    1 
ATOM   8621  C  CE    . LYS A 1 2551 ? 232.085 175.442 181.610 1.00 9.40  ? 2551 LYS A CE    1 
ATOM   8622  N  NZ    . LYS A 1 2551 ? 230.916 176.145 181.019 1.00 10.76 ? 2551 LYS A NZ    1 
ATOM   8623  N  N     . VAL A 1 2552 ? 234.081 172.357 188.069 1.00 12.40 ? 2552 VAL A N     1 
ATOM   8624  C  CA    . VAL A 1 2552 ? 234.072 172.377 189.529 1.00 10.15 ? 2552 VAL A CA    1 
ATOM   8625  C  C     . VAL A 1 2552 ? 235.431 171.874 190.000 1.00 16.28 ? 2552 VAL A C     1 
ATOM   8626  O  O     . VAL A 1 2552 ? 235.581 170.686 190.326 1.00 12.15 ? 2552 VAL A O     1 
ATOM   8627  C  CB    . VAL A 1 2552 ? 232.920 171.533 190.099 1.00 10.41 ? 2552 VAL A CB    1 
ATOM   8628  C  CG1   . VAL A 1 2552 ? 232.957 171.512 191.625 1.00 8.11  ? 2552 VAL A CG1   1 
ATOM   8629  C  CG2   . VAL A 1 2552 ? 231.584 172.048 189.605 1.00 9.88  ? 2552 VAL A CG2   1 
ATOM   8630  N  N     . PRO A 1 2553 ? 236.454 172.720 190.013 1.00 17.20 ? 2553 PRO A N     1 
ATOM   8631  C  CA    . PRO A 1 2553 ? 237.761 172.294 190.516 1.00 16.43 ? 2553 PRO A CA    1 
ATOM   8632  C  C     . PRO A 1 2553 ? 237.811 172.290 192.035 1.00 20.30 ? 2553 PRO A C     1 
ATOM   8633  O  O     . PRO A 1 2553 ? 237.094 173.028 192.713 1.00 22.26 ? 2553 PRO A O     1 
ATOM   8634  C  CB    . PRO A 1 2553 ? 238.712 173.349 189.940 1.00 16.11 ? 2553 PRO A CB    1 
ATOM   8635  C  CG    . PRO A 1 2553 ? 237.870 174.574 189.878 1.00 18.25 ? 2553 PRO A CG    1 
ATOM   8636  C  CD    . PRO A 1 2553 ? 236.487 174.104 189.508 1.00 9.06  ? 2553 PRO A CD    1 
ATOM   8637  N  N     . GLN A 1 2554 ? 238.676 171.431 192.566 1.00 22.40 ? 2554 GLN A N     1 
ATOM   8638  C  CA    . GLN A 1 2554 ? 238.956 171.410 194.001 1.00 16.68 ? 2554 GLN A CA    1 
ATOM   8639  C  C     . GLN A 1 2554 ? 239.971 172.509 194.284 1.00 21.24 ? 2554 GLN A C     1 
ATOM   8640  O  O     . GLN A 1 2554 ? 241.183 172.302 194.211 1.00 25.21 ? 2554 GLN A O     1 
ATOM   8641  C  CB    . GLN A 1 2554 ? 239.469 170.044 194.437 1.00 15.28 ? 2554 GLN A CB    1 
ATOM   8642  C  CG    . GLN A 1 2554 ? 239.696 169.930 195.934 1.00 23.91 ? 2554 GLN A CG    1 
ATOM   8643  C  CD    . GLN A 1 2554 ? 240.555 168.740 196.306 1.00 29.92 ? 2554 GLN A CD    1 
ATOM   8644  O  OE1   . GLN A 1 2554 ? 240.887 168.542 197.475 1.00 29.13 ? 2554 GLN A OE1   1 
ATOM   8645  N  NE2   . GLN A 1 2554 ? 240.922 167.941 195.312 1.00 27.74 ? 2554 GLN A NE2   1 
ATOM   8646  N  N     . ILE A 1 2555 ? 239.466 173.698 194.604 1.00 19.42 ? 2555 ILE A N     1 
ATOM   8647  C  CA    . ILE A 1 2555 ? 240.335 174.848 194.806 1.00 13.86 ? 2555 ILE A CA    1 
ATOM   8648  C  C     . ILE A 1 2555 ? 241.003 174.762 196.175 1.00 17.05 ? 2555 ILE A C     1 
ATOM   8649  O  O     . ILE A 1 2555 ? 240.561 174.043 197.075 1.00 15.80 ? 2555 ILE A O     1 
ATOM   8650  C  CB    . ILE A 1 2555 ? 239.557 176.166 194.664 1.00 15.51 ? 2555 ILE A CB    1 
ATOM   8651  C  CG1   . ILE A 1 2555 ? 238.472 176.254 195.737 1.00 14.23 ? 2555 ILE A CG1   1 
ATOM   8652  C  CG2   . ILE A 1 2555 ? 238.933 176.267 193.284 1.00 19.55 ? 2555 ILE A CG2   1 
ATOM   8653  C  CD1   . ILE A 1 2555 ? 237.817 177.604 195.826 1.00 11.53 ? 2555 ILE A CD1   1 
ATOM   8654  N  N     . GLU A 1 2556 ? 242.090 175.511 196.324 1.00 18.28 ? 2556 GLU A N     1 
ATOM   8655  C  CA    . GLU A 1 2556 ? 242.683 175.802 197.620 1.00 12.89 ? 2556 GLU A CA    1 
ATOM   8656  C  C     . GLU A 1 2556 ? 242.537 177.298 197.861 1.00 17.21 ? 2556 GLU A C     1 
ATOM   8657  O  O     . GLU A 1 2556 ? 242.979 178.107 197.038 1.00 23.19 ? 2556 GLU A O     1 
ATOM   8658  C  CB    . GLU A 1 2556 ? 244.151 175.377 197.678 1.00 9.03  ? 2556 GLU A CB    1 
ATOM   8659  C  CG    . GLU A 1 2556 ? 244.394 173.897 197.419 1.00 12.09 ? 2556 GLU A CG    1 
ATOM   8660  C  CD    . GLU A 1 2556 ? 243.644 172.991 198.378 1.00 20.61 ? 2556 GLU A CD    1 
ATOM   8661  O  OE1   . GLU A 1 2556 ? 243.798 173.154 199.606 1.00 30.70 ? 2556 GLU A OE1   1 
ATOM   8662  O  OE2   . GLU A 1 2556 ? 242.905 172.105 197.901 1.00 22.78 ? 2556 GLU A OE2   1 
ATOM   8663  N  N     . VAL A 1 2557 ? 241.912 177.660 198.969 1.00 13.11 ? 2557 VAL A N     1 
ATOM   8664  C  CA    . VAL A 1 2557 ? 241.569 179.045 199.264 1.00 4.64  ? 2557 VAL A CA    1 
ATOM   8665  C  C     . VAL A 1 2557 ? 242.719 179.694 200.023 1.00 11.70 ? 2557 VAL A C     1 
ATOM   8666  O  O     . VAL A 1 2557 ? 243.347 179.067 200.883 1.00 14.42 ? 2557 VAL A O     1 
ATOM   8667  C  CB    . VAL A 1 2557 ? 240.249 179.113 200.058 1.00 7.81  ? 2557 VAL A CB    1 
ATOM   8668  C  CG1   . VAL A 1 2557 ? 240.092 180.446 200.766 1.00 7.60  ? 2557 VAL A CG1   1 
ATOM   8669  C  CG2   . VAL A 1 2557 ? 239.069 178.856 199.137 1.00 11.09 ? 2557 VAL A CG2   1 
ATOM   8670  N  N     . GLU A 1 2558 ? 243.014 180.950 199.686 1.00 16.66 ? 2558 GLU A N     1 
ATOM   8671  C  CA    . GLU A 1 2558 ? 244.031 181.701 200.409 1.00 17.18 ? 2558 GLU A CA    1 
ATOM   8672  C  C     . GLU A 1 2558 ? 243.661 181.795 201.885 1.00 16.37 ? 2558 GLU A C     1 
ATOM   8673  O  O     . GLU A 1 2558 ? 242.496 181.998 202.236 1.00 13.40 ? 2558 GLU A O     1 
ATOM   8674  C  CB    . GLU A 1 2558 ? 244.182 183.099 199.810 1.00 16.30 ? 2558 GLU A CB    1 
ATOM   8675  C  CG    . GLU A 1 2558 ? 244.730 183.124 198.392 1.00 20.39 ? 2558 GLU A CG    1 
ATOM   8676  C  CD    . GLU A 1 2558 ? 246.167 182.647 198.306 1.00 26.48 ? 2558 GLU A CD    1 
ATOM   8677  O  OE1   . GLU A 1 2558 ? 246.929 182.859 199.274 1.00 28.45 ? 2558 GLU A OE1   1 
ATOM   8678  O  OE2   . GLU A 1 2558 ? 246.538 182.068 197.264 1.00 30.23 ? 2558 GLU A OE2   1 
ATOM   8679  N  N     . THR A 1 2559 ? 244.666 181.647 202.750 1.00 18.15 ? 2559 THR A N     1 
ATOM   8680  C  CA    . THR A 1 2559 ? 244.406 181.469 204.175 1.00 13.21 ? 2559 THR A CA    1 
ATOM   8681  C  C     . THR A 1 2559 ? 243.737 182.678 204.814 1.00 17.91 ? 2559 THR A C     1 
ATOM   8682  O  O     . THR A 1 2559 ? 243.110 182.534 205.867 1.00 17.89 ? 2559 THR A O     1 
ATOM   8683  C  CB    . THR A 1 2559 ? 245.707 181.143 204.916 1.00 13.56 ? 2559 THR A CB    1 
ATOM   8684  O  OG1   . THR A 1 2559 ? 245.411 180.803 206.276 1.00 20.25 ? 2559 THR A OG1   1 
ATOM   8685  C  CG2   . THR A 1 2559 ? 246.650 182.330 204.895 1.00 16.15 ? 2559 THR A CG2   1 
ATOM   8686  N  N     . HIS A 1 2560 ? 243.847 183.862 204.213 1.00 17.28 ? 2560 HIS A N     1 
ATOM   8687  C  CA    . HIS A 1 2560 ? 243.212 185.045 204.777 1.00 13.33 ? 2560 HIS A CA    1 
ATOM   8688  C  C     . HIS A 1 2560 ? 241.788 185.254 204.280 1.00 18.20 ? 2560 HIS A C     1 
ATOM   8689  O  O     . HIS A 1 2560 ? 241.103 186.158 204.773 1.00 22.69 ? 2560 HIS A O     1 
ATOM   8690  C  CB    . HIS A 1 2560 ? 244.047 186.294 204.476 1.00 18.43 ? 2560 HIS A CB    1 
ATOM   8691  C  CG    . HIS A 1 2560 ? 243.945 186.768 203.060 1.00 17.00 ? 2560 HIS A CG    1 
ATOM   8692  N  ND1   . HIS A 1 2560 ? 244.716 186.250 202.043 1.00 24.19 ? 2560 HIS A ND1   1 
ATOM   8693  C  CD2   . HIS A 1 2560 ? 243.170 187.723 202.494 1.00 17.07 ? 2560 HIS A CD2   1 
ATOM   8694  C  CE1   . HIS A 1 2560 ? 244.416 186.859 200.911 1.00 21.94 ? 2560 HIS A CE1   1 
ATOM   8695  N  NE2   . HIS A 1 2560 ? 243.481 187.759 201.157 1.00 18.97 ? 2560 HIS A NE2   1 
ATOM   8696  N  N     . LYS A 1 2561 ? 241.320 184.444 203.330 1.00 15.58 ? 2561 LYS A N     1 
ATOM   8697  C  CA    . LYS A 1 2561 ? 239.961 184.537 202.817 1.00 10.15 ? 2561 LYS A CA    1 
ATOM   8698  C  C     . LYS A 1 2561 ? 239.082 183.389 203.294 1.00 12.61 ? 2561 LYS A C     1 
ATOM   8699  O  O     . LYS A 1 2561 ? 238.067 183.086 202.656 1.00 17.22 ? 2561 LYS A O     1 
ATOM   8700  C  CB    . LYS A 1 2561 ? 239.970 184.585 201.289 1.00 15.51 ? 2561 LYS A CB    1 
ATOM   8701  C  CG    . LYS A 1 2561 ? 241.008 185.511 200.687 1.00 19.20 ? 2561 LYS A CG    1 
ATOM   8702  C  CD    . LYS A 1 2561 ? 241.006 185.402 199.170 1.00 18.67 ? 2561 LYS A CD    1 
ATOM   8703  C  CE    . LYS A 1 2561 ? 241.913 186.440 198.532 1.00 26.07 ? 2561 LYS A CE    1 
ATOM   8704  N  NZ    . LYS A 1 2561 ? 241.480 187.827 198.853 1.00 22.94 ? 2561 LYS A NZ    1 
ATOM   8705  N  N     . VAL A 1 2562 ? 239.449 182.744 204.399 1.00 13.99 ? 2562 VAL A N     1 
ATOM   8706  C  CA    . VAL A 1 2562 ? 238.736 181.562 204.868 1.00 11.82 ? 2562 VAL A CA    1 
ATOM   8707  C  C     . VAL A 1 2562 ? 237.335 181.963 205.310 1.00 14.59 ? 2562 VAL A C     1 
ATOM   8708  O  O     . VAL A 1 2562 ? 237.168 182.772 206.229 1.00 21.61 ? 2562 VAL A O     1 
ATOM   8709  C  CB    . VAL A 1 2562 ? 239.502 180.880 206.007 1.00 11.12 ? 2562 VAL A CB    1 
ATOM   8710  C  CG1   . VAL A 1 2562 ? 238.658 179.795 206.625 1.00 13.65 ? 2562 VAL A CG1   1 
ATOM   8711  C  CG2   . VAL A 1 2562 ? 240.808 180.310 205.501 1.00 13.29 ? 2562 VAL A CG2   1 
ATOM   8712  N  N     . ALA A 1 2563 ? 236.323 181.389 204.658 1.00 11.78 ? 2563 ALA A N     1 
ATOM   8713  C  CA    . ALA A 1 2563 ? 234.915 181.658 204.957 1.00 6.59  ? 2563 ALA A CA    1 
ATOM   8714  C  C     . ALA A 1 2563 ? 234.589 183.148 204.885 1.00 9.72  ? 2563 ALA A C     1 
ATOM   8715  O  O     . ALA A 1 2563 ? 233.766 183.652 205.654 1.00 11.81 ? 2563 ALA A O     1 
ATOM   8716  C  CB    . ALA A 1 2563 ? 234.515 181.086 206.319 1.00 6.34  ? 2563 ALA A CB    1 
ATOM   8717  N  N     . ALA A 1 2564 ? 235.234 183.864 203.969 1.00 13.36 ? 2564 ALA A N     1 
ATOM   8718  C  CA    . ALA A 1 2564 ? 234.922 185.267 203.770 1.00 11.22 ? 2564 ALA A CA    1 
ATOM   8719  C  C     . ALA A 1 2564 ? 233.602 185.407 203.010 1.00 18.47 ? 2564 ALA A C     1 
ATOM   8720  O  O     . ALA A 1 2564 ? 233.213 184.510 202.257 1.00 17.91 ? 2564 ALA A O     1 
ATOM   8721  C  CB    . ALA A 1 2564 ? 236.048 185.964 203.010 1.00 9.16  ? 2564 ALA A CB    1 
ATOM   8722  N  N     . PRO A 1 2565 ? 232.887 186.520 203.200 1.00 18.79 ? 2565 PRO A N     1 
ATOM   8723  C  CA    . PRO A 1 2565 ? 231.558 186.651 202.575 1.00 17.64 ? 2565 PRO A CA    1 
ATOM   8724  C  C     . PRO A 1 2565 ? 231.569 186.607 201.057 1.00 18.42 ? 2565 PRO A C     1 
ATOM   8725  O  O     . PRO A 1 2565 ? 230.553 186.244 200.453 1.00 27.05 ? 2565 PRO A O     1 
ATOM   8726  C  CB    . PRO A 1 2565 ? 231.068 188.010 203.096 1.00 15.79 ? 2565 PRO A CB    1 
ATOM   8727  C  CG    . PRO A 1 2565 ? 232.317 188.737 203.477 1.00 18.90 ? 2565 PRO A CG    1 
ATOM   8728  C  CD    . PRO A 1 2565 ? 233.195 187.679 204.052 1.00 14.47 ? 2565 PRO A CD    1 
ATOM   8729  N  N     . ASP A 1 2566 ? 232.677 186.972 200.416 1.00 13.72 ? 2566 ASP A N     1 
ATOM   8730  C  CA    . ASP A 1 2566 ? 232.742 187.048 198.963 1.00 15.70 ? 2566 ASP A CA    1 
ATOM   8731  C  C     . ASP A 1 2566 ? 233.251 185.758 198.327 1.00 13.95 ? 2566 ASP A C     1 
ATOM   8732  O  O     . ASP A 1 2566 ? 233.205 185.623 197.100 1.00 12.74 ? 2566 ASP A O     1 
ATOM   8733  C  CB    . ASP A 1 2566 ? 233.627 188.229 198.552 1.00 17.82 ? 2566 ASP A CB    1 
ATOM   8734  C  CG    . ASP A 1 2566 ? 233.624 188.476 197.058 1.00 23.17 ? 2566 ASP A CG    1 
ATOM   8735  O  OD1   . ASP A 1 2566 ? 232.614 189.001 196.548 1.00 26.89 ? 2566 ASP A OD1   1 
ATOM   8736  O  OD2   . ASP A 1 2566 ? 234.628 188.146 196.394 1.00 23.59 ? 2566 ASP A OD2   1 
ATOM   8737  N  N     . VAL A 1 2567 ? 233.708 184.797 199.125 1.00 11.92 ? 2567 VAL A N     1 
ATOM   8738  C  CA    . VAL A 1 2567 ? 234.348 183.588 198.618 1.00 5.08  ? 2567 VAL A CA    1 
ATOM   8739  C  C     . VAL A 1 2567 ? 233.303 182.495 198.460 1.00 4.06  ? 2567 VAL A C     1 
ATOM   8740  O  O     . VAL A 1 2567 ? 232.544 182.207 199.394 1.00 10.69 ? 2567 VAL A O     1 
ATOM   8741  C  CB    . VAL A 1 2567 ? 235.488 183.129 199.543 1.00 7.30  ? 2567 VAL A CB    1 
ATOM   8742  C  CG1   . VAL A 1 2567 ? 236.273 182.008 198.893 1.00 6.12  ? 2567 VAL A CG1   1 
ATOM   8743  C  CG2   . VAL A 1 2567 ? 236.403 184.291 199.858 1.00 10.05 ? 2567 VAL A CG2   1 
ATOM   8744  N  N     . VAL A 1 2568 ? 233.263 181.889 197.278 1.00 3.59  ? 2568 VAL A N     1 
ATOM   8745  C  CA    . VAL A 1 2568 ? 232.347 180.800 196.965 1.00 1.91  ? 2568 VAL A CA    1 
ATOM   8746  C  C     . VAL A 1 2568 ? 233.179 179.596 196.558 1.00 1.22  ? 2568 VAL A C     1 
ATOM   8747  O  O     . VAL A 1 2568 ? 233.975 179.676 195.615 1.00 3.08  ? 2568 VAL A O     1 
ATOM   8748  C  CB    . VAL A 1 2568 ? 231.364 181.182 195.846 1.00 2.39  ? 2568 VAL A CB    1 
ATOM   8749  C  CG1   . VAL A 1 2568 ? 230.368 180.059 195.600 1.00 0.58  ? 2568 VAL A CG1   1 
ATOM   8750  C  CG2   . VAL A 1 2568 ? 230.655 182.481 196.180 1.00 2.08  ? 2568 VAL A CG2   1 
ATOM   8751  N  N     . VAL A 1 2569 ? 233.003 178.487 197.267 1.00 1.25  ? 2569 VAL A N     1 
ATOM   8752  C  CA    . VAL A 1 2569 ? 233.665 177.240 196.897 1.00 1.38  ? 2569 VAL A CA    1 
ATOM   8753  C  C     . VAL A 1 2569 ? 232.847 176.590 195.790 1.00 1.64  ? 2569 VAL A C     1 
ATOM   8754  O  O     . VAL A 1 2569 ? 231.650 176.328 195.976 1.00 2.59  ? 2569 VAL A O     1 
ATOM   8755  C  CB    . VAL A 1 2569 ? 233.831 176.307 198.107 1.00 2.03  ? 2569 VAL A CB    1 
ATOM   8756  C  CG1   . VAL A 1 2569 ? 234.470 174.995 197.681 1.00 1.51  ? 2569 VAL A CG1   1 
ATOM   8757  C  CG2   . VAL A 1 2569 ? 234.660 176.986 199.183 1.00 1.33  ? 2569 VAL A CG2   1 
ATOM   8758  N  N     . PRO A 1 2570 ? 233.437 176.333 194.625 1.00 3.55  ? 2570 PRO A N     1 
ATOM   8759  C  CA    . PRO A 1 2570 ? 232.672 175.757 193.510 1.00 2.42  ? 2570 PRO A CA    1 
ATOM   8760  C  C     . PRO A 1 2570 ? 232.141 174.373 193.842 1.00 3.94  ? 2570 PRO A C     1 
ATOM   8761  O  O     . PRO A 1 2570 ? 232.891 173.474 194.227 1.00 4.79  ? 2570 PRO A O     1 
ATOM   8762  C  CB    . PRO A 1 2570 ? 233.696 175.713 192.371 1.00 2.53  ? 2570 PRO A CB    1 
ATOM   8763  C  CG    . PRO A 1 2570 ? 234.693 176.754 192.724 1.00 5.23  ? 2570 PRO A CG    1 
ATOM   8764  C  CD    . PRO A 1 2570 ? 234.794 176.723 194.215 1.00 5.08  ? 2570 PRO A CD    1 
ATOM   8765  N  N     . THR A 1 2571 ? 230.831 174.211 193.693 1.00 4.42  ? 2571 THR A N     1 
ATOM   8766  C  CA    . THR A 1 2571 ? 230.167 172.923 193.815 1.00 3.42  ? 2571 THR A CA    1 
ATOM   8767  C  C     . THR A 1 2571 ? 229.335 172.685 192.565 1.00 3.72  ? 2571 THR A C     1 
ATOM   8768  O  O     . THR A 1 2571 ? 229.218 173.551 191.695 1.00 6.14  ? 2571 THR A O     1 
ATOM   8769  C  CB    . THR A 1 2571 ? 229.284 172.846 195.071 1.00 5.19  ? 2571 THR A CB    1 
ATOM   8770  O  OG1   . THR A 1 2571 ? 228.166 173.732 194.935 1.00 5.62  ? 2571 THR A OG1   1 
ATOM   8771  C  CG2   . THR A 1 2571 ? 230.078 173.220 196.314 1.00 2.93  ? 2571 THR A CG2   1 
ATOM   8772  N  N     . LEU A 1 2572 ? 228.755 171.487 192.482 1.00 6.34  ? 2572 LEU A N     1 
ATOM   8773  C  CA    . LEU A 1 2572 ? 227.927 171.144 191.332 1.00 3.14  ? 2572 LEU A CA    1 
ATOM   8774  C  C     . LEU A 1 2572 ? 226.730 172.079 191.216 1.00 5.25  ? 2572 LEU A C     1 
ATOM   8775  O  O     . LEU A 1 2572 ? 226.362 172.494 190.112 1.00 9.67  ? 2572 LEU A O     1 
ATOM   8776  C  CB    . LEU A 1 2572 ? 227.464 169.691 191.437 1.00 7.07  ? 2572 LEU A CB    1 
ATOM   8777  C  CG    . LEU A 1 2572 ? 226.636 169.155 190.266 1.00 7.35  ? 2572 LEU A CG    1 
ATOM   8778  C  CD1   . LEU A 1 2572 ? 227.454 169.160 188.988 1.00 6.75  ? 2572 LEU A CD1   1 
ATOM   8779  C  CD2   . LEU A 1 2572 ? 226.101 167.765 190.565 1.00 10.90 ? 2572 LEU A CD2   1 
ATOM   8780  N  N     . ASP A 1 2573 ? 226.114 172.426 192.346 1.00 5.60  ? 2573 ASP A N     1 
ATOM   8781  C  CA    . ASP A 1 2573 ? 224.933 173.283 192.310 1.00 4.40  ? 2573 ASP A CA    1 
ATOM   8782  C  C     . ASP A 1 2573 ? 225.294 174.729 191.994 1.00 4.63  ? 2573 ASP A C     1 
ATOM   8783  O  O     . ASP A 1 2573 ? 224.559 175.410 191.269 1.00 7.75  ? 2573 ASP A O     1 
ATOM   8784  C  CB    . ASP A 1 2573 ? 224.182 173.193 193.638 1.00 5.24  ? 2573 ASP A CB    1 
ATOM   8785  C  CG    . ASP A 1 2573 ? 223.535 171.840 193.850 1.00 14.99 ? 2573 ASP A CG    1 
ATOM   8786  O  OD1   . ASP A 1 2573 ? 223.175 171.189 192.849 1.00 18.04 ? 2573 ASP A OD1   1 
ATOM   8787  O  OD2   . ASP A 1 2573 ? 223.383 171.424 195.016 1.00 17.62 ? 2573 ASP A OD2   1 
ATOM   8788  N  N     . THR A 1 2574 ? 226.413 175.220 192.532 1.00 3.39  ? 2574 THR A N     1 
ATOM   8789  C  CA    . THR A 1 2574 ? 226.756 176.629 192.354 1.00 2.69  ? 2574 THR A CA    1 
ATOM   8790  C  C     . THR A 1 2574 ? 227.052 176.959 190.895 1.00 2.06  ? 2574 THR A C     1 
ATOM   8791  O  O     . THR A 1 2574 ? 226.603 177.991 190.388 1.00 1.66  ? 2574 THR A O     1 
ATOM   8792  C  CB    . THR A 1 2574 ? 227.946 177.004 193.241 1.00 2.11  ? 2574 THR A CB    1 
ATOM   8793  O  OG1   . THR A 1 2574 ? 229.002 176.054 193.064 1.00 5.40  ? 2574 THR A OG1   1 
ATOM   8794  C  CG2   . THR A 1 2574 ? 227.532 177.036 194.702 1.00 1.00  ? 2574 THR A CG2   1 
ATOM   8795  N  N     . VAL A 1 2575 ? 227.806 176.101 190.206 1.00 2.89  ? 2575 VAL A N     1 
ATOM   8796  C  CA    . VAL A 1 2575 ? 228.157 176.382 188.817 1.00 2.96  ? 2575 VAL A CA    1 
ATOM   8797  C  C     . VAL A 1 2575 ? 226.928 176.293 187.916 1.00 2.86  ? 2575 VAL A C     1 
ATOM   8798  O  O     . VAL A 1 2575 ? 226.808 177.038 186.938 1.00 4.99  ? 2575 VAL A O     1 
ATOM   8799  C  CB    . VAL A 1 2575 ? 229.290 175.450 188.343 1.00 4.79  ? 2575 VAL A CB    1 
ATOM   8800  C  CG1   . VAL A 1 2575 ? 230.493 175.582 189.257 1.00 4.59  ? 2575 VAL A CG1   1 
ATOM   8801  C  CG2   . VAL A 1 2575 ? 228.822 174.004 188.278 1.00 6.88  ? 2575 VAL A CG2   1 
ATOM   8802  N  N     . ARG A 1 2576 ? 226.002 175.381 188.221 1.00 3.01  ? 2576 ARG A N     1 
ATOM   8803  C  CA    . ARG A 1 2576 ? 224.777 175.280 187.434 1.00 2.34  ? 2576 ARG A CA    1 
ATOM   8804  C  C     . ARG A 1 2576 ? 223.865 176.471 187.689 1.00 1.90  ? 2576 ARG A C     1 
ATOM   8805  O  O     . ARG A 1 2576 ? 223.329 177.070 186.749 1.00 1.69  ? 2576 ARG A O     1 
ATOM   8806  C  CB    . ARG A 1 2576 ? 224.047 173.974 187.750 1.00 3.05  ? 2576 ARG A CB    1 
ATOM   8807  C  CG    . ARG A 1 2576 ? 224.815 172.739 187.362 1.00 4.68  ? 2576 ARG A CG    1 
ATOM   8808  C  CD    . ARG A 1 2576 ? 224.035 171.463 187.628 1.00 4.48  ? 2576 ARG A CD    1 
ATOM   8809  N  NE    . ARG A 1 2576 ? 223.416 171.436 188.946 1.00 4.68  ? 2576 ARG A NE    1 
ATOM   8810  C  CZ    . ARG A 1 2576 ? 222.925 170.342 189.512 1.00 10.79 ? 2576 ARG A CZ    1 
ATOM   8811  N  NH1   . ARG A 1 2576 ? 222.967 169.169 188.901 1.00 8.04  ? 2576 ARG A NH1   1 
ATOM   8812  N  NH2   . ARG A 1 2576 ? 222.381 170.426 190.722 1.00 8.95  ? 2576 ARG A NH2   1 
ATOM   8813  N  N     . HIS A 1 2577 ? 223.672 176.824 188.960 1.00 2.04  ? 2577 HIS A N     1 
ATOM   8814  C  CA    . HIS A 1 2577 ? 222.801 177.944 189.294 1.00 1.48  ? 2577 HIS A CA    1 
ATOM   8815  C  C     . HIS A 1 2577 ? 223.367 179.258 188.774 1.00 1.57  ? 2577 HIS A C     1 
ATOM   8816  O  O     . HIS A 1 2577 ? 222.614 180.123 188.314 1.00 3.53  ? 2577 HIS A O     1 
ATOM   8817  C  CB    . HIS A 1 2577 ? 222.587 178.005 190.806 1.00 1.85  ? 2577 HIS A CB    1 
ATOM   8818  C  CG    . HIS A 1 2577 ? 221.718 176.910 191.338 1.00 1.79  ? 2577 HIS A CG    1 
ATOM   8819  N  ND1   . HIS A 1 2577 ? 221.634 176.612 192.681 1.00 3.79  ? 2577 HIS A ND1   1 
ATOM   8820  C  CD2   . HIS A 1 2577 ? 220.899 176.035 190.707 1.00 1.58  ? 2577 HIS A CD2   1 
ATOM   8821  C  CE1   . HIS A 1 2577 ? 220.796 175.606 192.855 1.00 1.89  ? 2577 HIS A CE1   1 
ATOM   8822  N  NE2   . HIS A 1 2577 ? 220.338 175.236 191.673 1.00 1.36  ? 2577 HIS A NE2   1 
ATOM   8823  N  N     . GLU A 1 2578 ? 224.689 179.427 188.844 1.00 1.53  ? 2578 GLU A N     1 
ATOM   8824  C  CA    . GLU A 1 2578 ? 225.311 180.653 188.351 1.00 1.58  ? 2578 GLU A CA    1 
ATOM   8825  C  C     . GLU A 1 2578 ? 225.118 180.800 186.847 1.00 1.94  ? 2578 GLU A C     1 
ATOM   8826  O  O     . GLU A 1 2578 ? 224.832 181.898 186.355 1.00 2.60  ? 2578 GLU A O     1 
ATOM   8827  C  CB    . GLU A 1 2578 ? 226.797 180.666 188.719 1.00 4.12  ? 2578 GLU A CB    1 
ATOM   8828  C  CG    . GLU A 1 2578 ? 227.520 181.983 188.474 1.00 7.63  ? 2578 GLU A CG    1 
ATOM   8829  C  CD    . GLU A 1 2578 ? 227.992 182.149 187.040 1.00 18.21 ? 2578 GLU A CD    1 
ATOM   8830  O  OE1   . GLU A 1 2578 ? 228.269 181.127 186.380 1.00 20.09 ? 2578 GLU A OE1   1 
ATOM   8831  O  OE2   . GLU A 1 2578 ? 228.087 183.305 186.573 1.00 18.08 ? 2578 GLU A OE2   1 
ATOM   8832  N  N     . ALA A 1 2579 ? 225.272 179.705 186.101 1.00 2.47  ? 2579 ALA A N     1 
ATOM   8833  C  CA    . ALA A 1 2579 ? 225.056 179.753 184.659 1.00 1.03  ? 2579 ALA A CA    1 
ATOM   8834  C  C     . ALA A 1 2579 ? 223.605 180.074 184.324 1.00 1.12  ? 2579 ALA A C     1 
ATOM   8835  O  O     . ALA A 1 2579 ? 223.333 180.865 183.415 1.00 1.33  ? 2579 ALA A O     1 
ATOM   8836  C  CB    . ALA A 1 2579 ? 225.472 178.428 184.024 1.00 0.76  ? 2579 ALA A CB    1 
ATOM   8837  N  N     . LEU A 1 2580 ? 222.660 179.463 185.044 1.00 1.05  ? 2580 LEU A N     1 
ATOM   8838  C  CA    . LEU A 1 2580 ? 221.249 179.757 184.816 1.00 0.76  ? 2580 LEU A CA    1 
ATOM   8839  C  C     . LEU A 1 2580 ? 220.920 181.199 185.178 1.00 0.92  ? 2580 LEU A C     1 
ATOM   8840  O  O     . LEU A 1 2580 ? 220.179 181.875 184.455 1.00 1.08  ? 2580 LEU A O     1 
ATOM   8841  C  CB    . LEU A 1 2580 ? 220.376 178.791 185.615 1.00 0.63  ? 2580 LEU A CB    1 
ATOM   8842  C  CG    . LEU A 1 2580 ? 218.866 178.955 185.433 1.00 1.24  ? 2580 LEU A CG    1 
ATOM   8843  C  CD1   . LEU A 1 2580 ? 218.453 178.558 184.024 1.00 1.38  ? 2580 LEU A CD1   1 
ATOM   8844  C  CD2   . LEU A 1 2580 ? 218.104 178.151 186.466 1.00 1.16  ? 2580 LEU A CD2   1 
ATOM   8845  N  N     . LEU A 1 2581 ? 221.458 181.686 186.298 1.00 1.40  ? 2581 LEU A N     1 
ATOM   8846  C  CA    . LEU A 1 2581 ? 221.247 183.079 186.677 1.00 1.07  ? 2581 LEU A CA    1 
ATOM   8847  C  C     . LEU A 1 2581 ? 221.854 184.022 185.651 1.00 1.11  ? 2581 LEU A C     1 
ATOM   8848  O  O     . LEU A 1 2581 ? 221.287 185.080 185.357 1.00 1.61  ? 2581 LEU A O     1 
ATOM   8849  C  CB    . LEU A 1 2581 ? 221.838 183.344 188.059 1.00 1.10  ? 2581 LEU A CB    1 
ATOM   8850  C  CG    . LEU A 1 2581 ? 221.026 182.877 189.263 1.00 1.35  ? 2581 LEU A CG    1 
ATOM   8851  C  CD1   . LEU A 1 2581 ? 221.615 183.445 190.536 1.00 0.66  ? 2581 LEU A CD1   1 
ATOM   8852  C  CD2   . LEU A 1 2581 ? 219.573 183.285 189.117 1.00 0.83  ? 2581 LEU A CD2   1 
ATOM   8853  N  N     . TYR A 1 2582 ? 223.011 183.655 185.096 1.00 0.87  ? 2582 TYR A N     1 
ATOM   8854  C  CA    . TYR A 1 2582 ? 223.652 184.482 184.081 1.00 1.56  ? 2582 TYR A CA    1 
ATOM   8855  C  C     . TYR A 1 2582 ? 222.742 184.683 182.877 1.00 3.50  ? 2582 TYR A C     1 
ATOM   8856  O  O     . TYR A 1 2582 ? 222.619 185.800 182.364 1.00 8.97  ? 2582 TYR A O     1 
ATOM   8857  C  CB    . TYR A 1 2582 ? 224.973 183.841 183.653 1.00 2.28  ? 2582 TYR A CB    1 
ATOM   8858  C  CG    . TYR A 1 2582 ? 225.842 184.707 182.775 1.00 5.11  ? 2582 TYR A CG    1 
ATOM   8859  C  CD1   . TYR A 1 2582 ? 225.625 184.786 181.405 1.00 6.00  ? 2582 TYR A CD1   1 
ATOM   8860  C  CD2   . TYR A 1 2582 ? 226.893 185.435 183.314 1.00 11.03 ? 2582 TYR A CD2   1 
ATOM   8861  C  CE1   . TYR A 1 2582 ? 226.422 185.573 180.602 1.00 6.08  ? 2582 TYR A CE1   1 
ATOM   8862  C  CE2   . TYR A 1 2582 ? 227.698 186.220 182.519 1.00 6.87  ? 2582 TYR A CE2   1 
ATOM   8863  C  CZ    . TYR A 1 2582 ? 227.457 186.287 181.164 1.00 11.74 ? 2582 TYR A CZ    1 
ATOM   8864  O  OH    . TYR A 1 2582 ? 228.259 187.073 180.367 1.00 25.69 ? 2582 TYR A OH    1 
ATOM   8865  N  N     . THR A 1 2583 ? 222.091 183.614 182.419 1.00 2.57  ? 2583 THR A N     1 
ATOM   8866  C  CA    . THR A 1 2583 ? 221.236 183.707 181.241 1.00 1.99  ? 2583 THR A CA    1 
ATOM   8867  C  C     . THR A 1 2583 ? 220.071 184.661 181.478 1.00 2.45  ? 2583 THR A C     1 
ATOM   8868  O  O     . THR A 1 2583 ? 219.824 185.569 180.677 1.00 8.27  ? 2583 THR A O     1 
ATOM   8869  C  CB    . THR A 1 2583 ? 220.731 182.316 180.857 1.00 3.78  ? 2583 THR A CB    1 
ATOM   8870  O  OG1   . THR A 1 2583 ? 221.798 181.565 180.267 1.00 3.93  ? 2583 THR A OG1   1 
ATOM   8871  C  CG2   . THR A 1 2583 ? 219.576 182.413 179.873 1.00 3.40  ? 2583 THR A CG2   1 
ATOM   8872  N  N     . TRP A 1 2584 ? 219.346 184.472 182.583 1.00 1.25  ? 2584 TRP A N     1 
ATOM   8873  C  CA    . TRP A 1 2584 ? 218.206 185.335 182.874 1.00 1.01  ? 2584 TRP A CA    1 
ATOM   8874  C  C     . TRP A 1 2584 ? 218.645 186.774 183.123 1.00 1.91  ? 2584 TRP A C     1 
ATOM   8875  O  O     . TRP A 1 2584 ? 218.003 187.715 182.645 1.00 1.99  ? 2584 TRP A O     1 
ATOM   8876  C  CB    . TRP A 1 2584 ? 217.434 184.793 184.075 1.00 0.77  ? 2584 TRP A CB    1 
ATOM   8877  C  CG    . TRP A 1 2584 ? 216.826 183.438 183.865 1.00 1.23  ? 2584 TRP A CG    1 
ATOM   8878  C  CD1   . TRP A 1 2584 ? 216.583 182.822 182.673 1.00 1.49  ? 2584 TRP A CD1   1 
ATOM   8879  C  CD2   . TRP A 1 2584 ? 216.381 182.534 184.881 1.00 0.92  ? 2584 TRP A CD2   1 
ATOM   8880  N  NE1   . TRP A 1 2584 ? 216.017 181.590 182.884 1.00 0.67  ? 2584 TRP A NE1   1 
ATOM   8881  C  CE2   . TRP A 1 2584 ? 215.882 181.389 184.231 1.00 0.90  ? 2584 TRP A CE2   1 
ATOM   8882  C  CE3   . TRP A 1 2584 ? 216.356 182.581 186.279 1.00 0.61  ? 2584 TRP A CE3   1 
ATOM   8883  C  CZ2   . TRP A 1 2584 ? 215.361 180.301 184.930 1.00 2.45  ? 2584 TRP A CZ2   1 
ATOM   8884  C  CZ3   . TRP A 1 2584 ? 215.839 181.500 186.971 1.00 0.66  ? 2584 TRP A CZ3   1 
ATOM   8885  C  CH2   . TRP A 1 2584 ? 215.348 180.377 186.294 1.00 0.78  ? 2584 TRP A CH2   1 
ATOM   8886  N  N     . LEU A 1 2585 ? 219.735 186.964 183.872 1.00 2.34  ? 2585 LEU A N     1 
ATOM   8887  C  CA    . LEU A 1 2585 ? 220.195 188.313 184.186 1.00 1.28  ? 2585 LEU A CA    1 
ATOM   8888  C  C     . LEU A 1 2585 ? 220.684 189.043 182.942 1.00 3.65  ? 2585 LEU A C     1 
ATOM   8889  O  O     . LEU A 1 2585 ? 220.413 190.237 182.773 1.00 2.85  ? 2585 LEU A O     1 
ATOM   8890  C  CB    . LEU A 1 2585 ? 221.301 188.258 185.238 1.00 0.96  ? 2585 LEU A CB    1 
ATOM   8891  C  CG    . LEU A 1 2585 ? 220.864 188.024 186.683 1.00 0.65  ? 2585 LEU A CG    1 
ATOM   8892  C  CD1   . LEU A 1 2585 ? 222.008 187.433 187.487 1.00 0.73  ? 2585 LEU A CD1   1 
ATOM   8893  C  CD2   . LEU A 1 2585 ? 220.384 189.318 187.301 1.00 0.38  ? 2585 LEU A CD2   1 
ATOM   8894  N  N     . ALA A 1 2586 ? 221.409 188.345 182.063 1.00 3.68  ? 2586 ALA A N     1 
ATOM   8895  C  CA    . ALA A 1 2586 ? 221.940 188.987 180.865 1.00 2.70  ? 2586 ALA A CA    1 
ATOM   8896  C  C     . ALA A 1 2586 ? 220.827 189.443 179.933 1.00 2.87  ? 2586 ALA A C     1 
ATOM   8897  O  O     . ALA A 1 2586 ? 221.019 190.377 179.147 1.00 3.64  ? 2586 ALA A O     1 
ATOM   8898  C  CB    . ALA A 1 2586 ? 222.893 188.040 180.136 1.00 2.94  ? 2586 ALA A CB    1 
ATOM   8899  N  N     . GLU A 1 2587 ? 219.667 188.802 180.003 1.00 3.69  ? 2587 GLU A N     1 
ATOM   8900  C  CA    . GLU A 1 2587 ? 218.509 189.193 179.215 1.00 3.49  ? 2587 GLU A CA    1 
ATOM   8901  C  C     . GLU A 1 2587 ? 217.627 190.207 179.929 1.00 2.37  ? 2587 GLU A C     1 
ATOM   8902  O  O     . GLU A 1 2587 ? 216.578 190.577 179.392 1.00 6.64  ? 2587 GLU A O     1 
ATOM   8903  C  CB    . GLU A 1 2587 ? 217.682 187.955 178.847 1.00 4.01  ? 2587 GLU A CB    1 
ATOM   8904  C  CG    . GLU A 1 2587 ? 218.402 186.918 177.978 1.00 6.49  ? 2587 GLU A CG    1 
ATOM   8905  C  CD    . GLU A 1 2587 ? 218.765 187.404 176.576 1.00 16.40 ? 2587 GLU A CD    1 
ATOM   8906  O  OE1   . GLU A 1 2587 ? 218.695 188.618 176.296 1.00 14.39 ? 2587 GLU A OE1   1 
ATOM   8907  O  OE2   . GLU A 1 2587 ? 219.133 186.551 175.741 1.00 16.33 ? 2587 GLU A OE2   1 
ATOM   8908  N  N     . HIS A 1 2588 ? 218.023 190.653 181.122 1.00 1.12  ? 2588 HIS A N     1 
ATOM   8909  C  CA    . HIS A 1 2588 ? 217.263 191.596 181.942 1.00 0.87  ? 2588 HIS A CA    1 
ATOM   8910  C  C     . HIS A 1 2588 ? 215.898 191.043 182.337 1.00 0.86  ? 2588 HIS A C     1 
ATOM   8911  O  O     . HIS A 1 2588 ? 214.975 191.804 182.636 1.00 1.54  ? 2588 HIS A O     1 
ATOM   8912  C  CB    . HIS A 1 2588 ? 217.116 192.947 181.235 1.00 0.39  ? 2588 HIS A CB    1 
ATOM   8913  C  CG    . HIS A 1 2588 ? 218.401 193.465 180.672 1.00 0.51  ? 2588 HIS A CG    1 
ATOM   8914  N  ND1   . HIS A 1 2588 ? 219.553 193.566 181.419 1.00 1.05  ? 2588 HIS A ND1   1 
ATOM   8915  C  CD2   . HIS A 1 2588 ? 218.725 193.881 179.425 1.00 0.30  ? 2588 HIS A CD2   1 
ATOM   8916  C  CE1   . HIS A 1 2588 ? 220.528 194.036 180.663 1.00 0.47  ? 2588 HIS A CE1   1 
ATOM   8917  N  NE2   . HIS A 1 2588 ? 220.051 194.236 179.449 1.00 0.42  ? 2588 HIS A NE2   1 
ATOM   8918  N  N     . LYS A 1 2589 ? 215.768 189.726 182.341 1.00 1.35  ? 2589 LYS A N     1 
ATOM   8919  C  CA    . LYS A 1 2589 ? 214.536 189.055 182.728 1.00 1.15  ? 2589 LYS A CA    1 
ATOM   8920  C  C     . LYS A 1 2589 ? 214.425 189.015 184.248 1.00 0.47  ? 2589 LYS A C     1 
ATOM   8921  O  O     . LYS A 1 2589 ? 215.353 188.550 184.917 1.00 1.05  ? 2589 LYS A O     1 
ATOM   8922  C  CB    . LYS A 1 2589 ? 214.514 187.636 182.158 1.00 1.62  ? 2589 LYS A CB    1 
ATOM   8923  C  CG    . LYS A 1 2589 ? 213.259 186.835 182.460 1.00 2.18  ? 2589 LYS A CG    1 
ATOM   8924  C  CD    . LYS A 1 2589 ? 212.182 187.079 181.415 1.00 4.10  ? 2589 LYS A CD    1 
ATOM   8925  C  CE    . LYS A 1 2589 ? 211.112 185.998 181.461 1.00 3.16  ? 2589 LYS A CE    1 
ATOM   8926  N  NZ    . LYS A 1 2589 ? 210.011 186.263 180.498 1.00 5.47  ? 2589 LYS A NZ    1 
ATOM   8927  N  N     . PRO A 1 2590 ? 213.329 189.504 184.826 1.00 0.34  ? 2590 PRO A N     1 
ATOM   8928  C  CA    . PRO A 1 2590 ? 213.158 189.394 186.279 1.00 0.19  ? 2590 PRO A CA    1 
ATOM   8929  C  C     . PRO A 1 2590 ? 213.125 187.937 186.715 1.00 0.20  ? 2590 PRO A C     1 
ATOM   8930  O  O     . PRO A 1 2590 ? 212.569 187.079 186.029 1.00 0.50  ? 2590 PRO A O     1 
ATOM   8931  C  CB    . PRO A 1 2590 ? 211.817 190.091 186.533 1.00 0.12  ? 2590 PRO A CB    1 
ATOM   8932  C  CG    . PRO A 1 2590 ? 211.105 190.015 185.229 1.00 0.17  ? 2590 PRO A CG    1 
ATOM   8933  C  CD    . PRO A 1 2590 ? 212.166 190.129 184.181 1.00 0.22  ? 2590 PRO A CD    1 
ATOM   8934  N  N     . LEU A 1 2591 ? 213.726 187.660 187.868 1.00 0.16  ? 2591 LEU A N     1 
ATOM   8935  C  CA    . LEU A 1 2591 ? 213.832 186.288 188.338 1.00 0.08  ? 2591 LEU A CA    1 
ATOM   8936  C  C     . LEU A 1 2591 ? 213.685 186.273 189.852 1.00 0.07  ? 2591 LEU A C     1 
ATOM   8937  O  O     . LEU A 1 2591 ? 213.884 187.287 190.525 1.00 0.03  ? 2591 LEU A O     1 
ATOM   8938  C  CB    . LEU A 1 2591 ? 215.158 185.650 187.896 1.00 0.22  ? 2591 LEU A CB    1 
ATOM   8939  C  CG    . LEU A 1 2591 ? 216.482 186.242 188.394 1.00 0.08  ? 2591 LEU A CG    1 
ATOM   8940  C  CD1   . LEU A 1 2591 ? 216.868 185.676 189.760 1.00 0.06  ? 2591 LEU A CD1   1 
ATOM   8941  C  CD2   . LEU A 1 2591 ? 217.603 186.053 187.387 1.00 0.31  ? 2591 LEU A CD2   1 
ATOM   8942  N  N     . VAL A 1 2592 ? 213.327 185.108 190.380 1.00 0.05  ? 2592 VAL A N     1 
ATOM   8943  C  CA    . VAL A 1 2592 ? 213.223 184.892 191.815 1.00 0.03  ? 2592 VAL A CA    1 
ATOM   8944  C  C     . VAL A 1 2592 ? 214.001 183.637 192.178 1.00 0.03  ? 2592 VAL A C     1 
ATOM   8945  O  O     . VAL A 1 2592 ? 213.811 182.583 191.562 1.00 0.04  ? 2592 VAL A O     1 
ATOM   8946  C  CB    . VAL A 1 2592 ? 211.755 184.782 192.277 1.00 0.04  ? 2592 VAL A CB    1 
ATOM   8947  C  CG1   . VAL A 1 2592 ? 211.662 184.055 193.604 1.00 0.06  ? 2592 VAL A CG1   1 
ATOM   8948  C  CG2   . VAL A 1 2592 ? 211.145 186.162 192.405 1.00 0.02  ? 2592 VAL A CG2   1 
ATOM   8949  N  N     . LEU A 1 2593 ? 214.882 183.756 193.165 1.00 0.04  ? 2593 LEU A N     1 
ATOM   8950  C  CA    . LEU A 1 2593 ? 215.528 182.610 193.788 1.00 0.04  ? 2593 LEU A CA    1 
ATOM   8951  C  C     . LEU A 1 2593 ? 214.732 182.222 195.025 1.00 0.04  ? 2593 LEU A C     1 
ATOM   8952  O  O     . LEU A 1 2593 ? 214.476 183.063 195.891 1.00 0.09  ? 2593 LEU A O     1 
ATOM   8953  C  CB    . LEU A 1 2593 ? 216.976 182.923 194.168 1.00 0.05  ? 2593 LEU A CB    1 
ATOM   8954  C  CG    . LEU A 1 2593 ? 217.922 183.428 193.079 1.00 0.07  ? 2593 LEU A CG    1 
ATOM   8955  C  CD1   . LEU A 1 2593 ? 218.062 184.935 193.155 1.00 0.07  ? 2593 LEU A CD1   1 
ATOM   8956  C  CD2   . LEU A 1 2593 ? 219.277 182.760 193.204 1.00 0.21  ? 2593 LEU A CD2   1 
ATOM   8957  N  N     . CYS A 1 2594 ? 214.333 180.959 195.101 1.00 0.07  ? 2594 CYS A N     1 
ATOM   8958  C  CA    . CYS A 1 2594 ? 213.555 180.457 196.222 1.00 0.13  ? 2594 CYS A CA    1 
ATOM   8959  C  C     . CYS A 1 2594 ? 214.308 179.320 196.895 1.00 0.14  ? 2594 CYS A C     1 
ATOM   8960  O  O     . CYS A 1 2594 ? 214.878 178.456 196.222 1.00 0.31  ? 2594 CYS A O     1 
ATOM   8961  C  CB    . CYS A 1 2594 ? 212.170 179.981 195.776 1.00 0.16  ? 2594 CYS A CB    1 
ATOM   8962  S  SG    . CYS A 1 2594 ? 211.037 179.630 197.134 1.00 0.80  ? 2594 CYS A SG    1 
ATOM   8963  N  N     . GLY A 1 2595 ? 214.309 179.328 198.223 1.00 0.15  ? 2595 GLY A N     1 
ATOM   8964  C  CA    . GLY A 1 2595 ? 214.974 178.304 198.986 1.00 0.09  ? 2595 GLY A CA    1 
ATOM   8965  C  C     . GLY A 1 2595 ? 214.932 178.575 200.472 1.00 0.10  ? 2595 GLY A C     1 
ATOM   8966  O  O     . GLY A 1 2595 ? 214.511 179.644 200.921 1.00 0.37  ? 2595 GLY A O     1 
ATOM   8967  N  N     . PRO A 1 2596 ? 215.369 177.600 201.269 1.00 0.47  ? 2596 PRO A N     1 
ATOM   8968  C  CA    . PRO A 1 2596 ? 215.383 177.797 202.715 1.00 0.17  ? 2596 PRO A CA    1 
ATOM   8969  C  C     . PRO A 1 2596 ? 216.374 178.879 203.098 1.00 0.16  ? 2596 PRO A C     1 
ATOM   8970  O  O     . PRO A 1 2596 ? 217.386 179.089 202.406 1.00 0.16  ? 2596 PRO A O     1 
ATOM   8971  C  CB    . PRO A 1 2596 ? 215.816 176.421 203.256 1.00 0.22  ? 2596 PRO A CB    1 
ATOM   8972  C  CG    . PRO A 1 2596 ? 215.638 175.476 202.122 1.00 0.41  ? 2596 PRO A CG    1 
ATOM   8973  C  CD    . PRO A 1 2596 ? 215.879 176.274 200.892 1.00 0.60  ? 2596 PRO A CD    1 
ATOM   8974  N  N     . PRO A 1 2597 ? 216.126 179.598 204.194 1.00 0.18  ? 2597 PRO A N     1 
ATOM   8975  C  CA    . PRO A 1 2597 ? 217.027 180.694 204.588 1.00 0.23  ? 2597 PRO A CA    1 
ATOM   8976  C  C     . PRO A 1 2597 ? 218.443 180.196 204.823 1.00 0.28  ? 2597 PRO A C     1 
ATOM   8977  O  O     . PRO A 1 2597 ? 218.680 179.301 205.638 1.00 1.62  ? 2597 PRO A O     1 
ATOM   8978  C  CB    . PRO A 1 2597 ? 216.389 181.230 205.876 1.00 0.16  ? 2597 PRO A CB    1 
ATOM   8979  C  CG    . PRO A 1 2597 ? 215.456 180.149 206.332 1.00 0.15  ? 2597 PRO A CG    1 
ATOM   8980  C  CD    . PRO A 1 2597 ? 214.974 179.476 205.099 1.00 0.22  ? 2597 PRO A CD    1 
ATOM   8981  N  N     . GLY A 1 2598 ? 219.389 180.782 204.097 1.00 0.14  ? 2598 GLY A N     1 
ATOM   8982  C  CA    . GLY A 1 2598 ? 220.777 180.387 204.173 1.00 0.19  ? 2598 GLY A CA    1 
ATOM   8983  C  C     . GLY A 1 2598 ? 221.224 179.366 203.154 1.00 0.18  ? 2598 GLY A C     1 
ATOM   8984  O  O     . GLY A 1 2598 ? 222.318 178.809 203.302 1.00 0.20  ? 2598 GLY A O     1 
ATOM   8985  N  N     . SER A 1 2599 ? 220.424 179.101 202.121 1.00 0.18  ? 2599 SER A N     1 
ATOM   8986  C  CA    . SER A 1 2599 ? 220.763 178.076 201.142 1.00 0.34  ? 2599 SER A CA    1 
ATOM   8987  C  C     . SER A 1 2599 ? 221.727 178.565 200.071 1.00 0.28  ? 2599 SER A C     1 
ATOM   8988  O  O     . SER A 1 2599 ? 222.183 177.755 199.258 1.00 0.30  ? 2599 SER A O     1 
ATOM   8989  C  CB    . SER A 1 2599 ? 219.493 177.535 200.478 1.00 0.20  ? 2599 SER A CB    1 
ATOM   8990  O  OG    . SER A 1 2599 ? 218.796 178.555 199.785 1.00 0.16  ? 2599 SER A OG    1 
ATOM   8991  N  N     . GLY A 1 2600 ? 222.050 179.849 200.051 1.00 0.13  ? 2600 GLY A N     1 
ATOM   8992  C  CA    . GLY A 1 2600 ? 222.974 180.399 199.094 1.00 0.17  ? 2600 GLY A CA    1 
ATOM   8993  C  C     . GLY A 1 2600 ? 222.369 181.243 197.991 1.00 0.27  ? 2600 GLY A C     1 
ATOM   8994  O  O     . GLY A 1 2600 ? 223.003 181.395 196.944 1.00 1.66  ? 2600 GLY A O     1 
ATOM   8995  N  N     . LYS A 1 2601 ? 221.169 181.790 198.192 1.00 0.22  ? 2601 LYS A N     1 
ATOM   8996  C  CA    . LYS A 1 2601 ? 220.521 182.569 197.142 1.00 0.21  ? 2601 LYS A CA    1 
ATOM   8997  C  C     . LYS A 1 2601 ? 221.248 183.885 196.898 1.00 0.70  ? 2601 LYS A C     1 
ATOM   8998  O  O     . LYS A 1 2601 ? 221.541 184.239 195.750 1.00 0.71  ? 2601 LYS A O     1 
ATOM   8999  C  CB    . LYS A 1 2601 ? 219.058 182.813 197.508 1.00 0.14  ? 2601 LYS A CB    1 
ATOM   9000  C  CG    . LYS A 1 2601 ? 218.236 181.536 197.599 1.00 0.10  ? 2601 LYS A CG    1 
ATOM   9001  C  CD    . LYS A 1 2601 ? 216.805 181.815 198.017 1.00 0.06  ? 2601 LYS A CD    1 
ATOM   9002  C  CE    . LYS A 1 2601 ? 216.744 182.439 199.399 1.00 0.08  ? 2601 LYS A CE    1 
ATOM   9003  N  NZ    . LYS A 1 2601 ? 217.284 181.536 200.450 1.00 0.05  ? 2601 LYS A NZ    1 
ATOM   9004  N  N     . THR A 1 2602 ? 221.550 184.627 197.967 1.00 1.18  ? 2602 THR A N     1 
ATOM   9005  C  CA    . THR A 1 2602 ? 222.322 185.855 197.812 1.00 0.99  ? 2602 THR A CA    1 
ATOM   9006  C  C     . THR A 1 2602 ? 223.727 185.555 197.310 1.00 1.06  ? 2602 THR A C     1 
ATOM   9007  O  O     . THR A 1 2602 ? 224.269 186.293 196.480 1.00 1.26  ? 2602 THR A O     1 
ATOM   9008  C  CB    . THR A 1 2602 ? 222.379 186.617 199.137 1.00 1.24  ? 2602 THR A CB    1 
ATOM   9009  O  OG1   . THR A 1 2602 ? 221.059 186.751 199.673 1.00 9.14  ? 2602 THR A OG1   1 
ATOM   9010  C  CG2   . THR A 1 2602 ? 222.981 187.995 198.932 1.00 0.98  ? 2602 THR A CG2   1 
ATOM   9011  N  N     . MET A 1 2603 ? 224.329 184.473 197.804 1.00 0.58  ? 2603 MET A N     1 
ATOM   9012  C  CA    . MET A 1 2603 ? 225.673 184.101 197.378 1.00 0.47  ? 2603 MET A CA    1 
ATOM   9013  C  C     . MET A 1 2603 ? 225.711 183.777 195.890 1.00 0.81  ? 2603 MET A C     1 
ATOM   9014  O  O     . MET A 1 2603 ? 226.614 184.216 195.171 1.00 0.94  ? 2603 MET A O     1 
ATOM   9015  C  CB    . MET A 1 2603 ? 226.161 182.912 198.205 1.00 0.40  ? 2603 MET A CB    1 
ATOM   9016  C  CG    . MET A 1 2603 ? 227.590 182.517 197.935 1.00 0.40  ? 2603 MET A CG    1 
ATOM   9017  S  SD    . MET A 1 2603 ? 227.935 180.804 198.359 1.00 0.22  ? 2603 MET A SD    1 
ATOM   9018  C  CE    . MET A 1 2603 ? 226.845 179.938 197.235 1.00 0.30  ? 2603 MET A CE    1 
ATOM   9019  N  N     . THR A 1 2604 ? 224.731 183.010 195.408 1.00 0.55  ? 2604 THR A N     1 
ATOM   9020  C  CA    . THR A 1 2604 ? 224.704 182.654 193.994 1.00 0.80  ? 2604 THR A CA    1 
ATOM   9021  C  C     . THR A 1 2604 ? 224.426 183.871 193.118 1.00 0.80  ? 2604 THR A C     1 
ATOM   9022  O  O     . THR A 1 2604 ? 225.061 184.045 192.073 1.00 1.29  ? 2604 THR A O     1 
ATOM   9023  C  CB    . THR A 1 2604 ? 223.663 181.564 193.746 1.00 1.22  ? 2604 THR A CB    1 
ATOM   9024  O  OG1   . THR A 1 2604 ? 223.895 180.470 194.641 1.00 2.05  ? 2604 THR A OG1   1 
ATOM   9025  C  CG2   . THR A 1 2604 ? 223.753 181.063 192.319 1.00 0.86  ? 2604 THR A CG2   1 
ATOM   9026  N  N     . LEU A 1 2605 ? 223.485 184.723 193.529 1.00 0.67  ? 2605 LEU A N     1 
ATOM   9027  C  CA    . LEU A 1 2605 ? 223.149 185.899 192.734 1.00 0.61  ? 2605 LEU A CA    1 
ATOM   9028  C  C     . LEU A 1 2605 ? 224.338 186.845 192.615 1.00 0.97  ? 2605 LEU A C     1 
ATOM   9029  O  O     . LEU A 1 2605 ? 224.652 187.330 191.524 1.00 1.53  ? 2605 LEU A O     1 
ATOM   9030  C  CB    . LEU A 1 2605 ? 221.951 186.623 193.343 1.00 1.80  ? 2605 LEU A CB    1 
ATOM   9031  C  CG    . LEU A 1 2605 ? 221.683 188.011 192.756 1.00 1.06  ? 2605 LEU A CG    1 
ATOM   9032  C  CD1   . LEU A 1 2605 ? 221.211 187.912 191.313 1.00 0.37  ? 2605 LEU A CD1   1 
ATOM   9033  C  CD2   . LEU A 1 2605 ? 220.689 188.768 193.605 1.00 0.62  ? 2605 LEU A CD2   1 
ATOM   9034  N  N     . PHE A 1 2606 ? 225.015 187.114 193.732 1.00 1.19  ? 2606 PHE A N     1 
ATOM   9035  C  CA    . PHE A 1 2606 ? 226.161 188.017 193.695 1.00 1.25  ? 2606 PHE A CA    1 
ATOM   9036  C  C     . PHE A 1 2606 ? 227.347 187.388 192.979 1.00 1.50  ? 2606 PHE A C     1 
ATOM   9037  O  O     . PHE A 1 2606 ? 228.141 188.102 192.358 1.00 3.15  ? 2606 PHE A O     1 
ATOM   9038  C  CB    . PHE A 1 2606 ? 226.554 188.447 195.111 1.00 1.17  ? 2606 PHE A CB    1 
ATOM   9039  C  CG    . PHE A 1 2606 ? 225.560 189.366 195.778 1.00 1.70  ? 2606 PHE A CG    1 
ATOM   9040  C  CD1   . PHE A 1 2606 ? 224.319 189.614 195.212 1.00 2.01  ? 2606 PHE A CD1   1 
ATOM   9041  C  CD2   . PHE A 1 2606 ? 225.870 189.979 196.977 1.00 3.23  ? 2606 PHE A CD2   1 
ATOM   9042  C  CE1   . PHE A 1 2606 ? 223.412 190.454 195.829 1.00 1.54  ? 2606 PHE A CE1   1 
ATOM   9043  C  CE2   . PHE A 1 2606 ? 224.967 190.822 197.598 1.00 6.42  ? 2606 PHE A CE2   1 
ATOM   9044  C  CZ    . PHE A 1 2606 ? 223.738 191.059 197.022 1.00 1.84  ? 2606 PHE A CZ    1 
ATOM   9045  N  N     . SER A 1 2607 ? 227.489 186.064 193.055 1.00 1.84  ? 2607 SER A N     1 
ATOM   9046  C  CA    . SER A 1 2607 ? 228.534 185.391 192.293 1.00 1.68  ? 2607 SER A CA    1 
ATOM   9047  C  C     . SER A 1 2607 ? 228.294 185.521 190.795 1.00 3.41  ? 2607 SER A C     1 
ATOM   9048  O  O     . SER A 1 2607 ? 229.235 185.746 190.027 1.00 9.76  ? 2607 SER A O     1 
ATOM   9049  C  CB    . SER A 1 2607 ? 228.615 183.921 192.704 1.00 1.98  ? 2607 SER A CB    1 
ATOM   9050  O  OG    . SER A 1 2607 ? 229.602 183.231 191.960 1.00 12.41 ? 2607 SER A OG    1 
ATOM   9051  N  N     . ALA A 1 2608 ? 227.039 185.386 190.362 1.00 2.52  ? 2608 ALA A N     1 
ATOM   9052  C  CA    . ALA A 1 2608 ? 226.720 185.530 188.947 1.00 2.18  ? 2608 ALA A CA    1 
ATOM   9053  C  C     . ALA A 1 2608 ? 226.868 186.972 188.478 1.00 2.65  ? 2608 ALA A C     1 
ATOM   9054  O  O     . ALA A 1 2608 ? 227.235 187.211 187.323 1.00 3.18  ? 2608 ALA A O     1 
ATOM   9055  C  CB    . ALA A 1 2608 ? 225.304 185.024 188.675 1.00 1.71  ? 2608 ALA A CB    1 
ATOM   9056  N  N     . LEU A 1 2609 ? 226.589 187.940 189.354 1.00 2.31  ? 2609 LEU A N     1 
ATOM   9057  C  CA    . LEU A 1 2609 ? 226.713 189.342 188.972 1.00 3.35  ? 2609 LEU A CA    1 
ATOM   9058  C  C     . LEU A 1 2609 ? 228.165 189.745 188.753 1.00 6.28  ? 2609 LEU A C     1 
ATOM   9059  O  O     . LEU A 1 2609 ? 228.435 190.685 187.997 1.00 5.71  ? 2609 LEU A O     1 
ATOM   9060  C  CB    . LEU A 1 2609 ? 226.070 190.231 190.035 1.00 2.45  ? 2609 LEU A CB    1 
ATOM   9061  C  CG    . LEU A 1 2609 ? 224.543 190.218 190.066 1.00 1.52  ? 2609 LEU A CG    1 
ATOM   9062  C  CD1   . LEU A 1 2609 ? 224.027 190.940 191.293 1.00 1.03  ? 2609 LEU A CD1   1 
ATOM   9063  C  CD2   . LEU A 1 2609 ? 223.985 190.838 188.799 1.00 1.90  ? 2609 LEU A CD2   1 
ATOM   9064  N  N     . ARG A 1 2610 ? 229.108 189.062 189.406 1.00 8.09  ? 2610 ARG A N     1 
ATOM   9065  C  CA    . ARG A 1 2610 ? 230.520 189.381 189.213 1.00 5.48  ? 2610 ARG A CA    1 
ATOM   9066  C  C     . ARG A 1 2610 ? 230.965 189.075 187.790 1.00 9.36  ? 2610 ARG A C     1 
ATOM   9067  O  O     . ARG A 1 2610 ? 231.780 189.807 187.218 1.00 17.13 ? 2610 ARG A O     1 
ATOM   9068  C  CB    . ARG A 1 2610 ? 231.374 188.622 190.228 1.00 7.83  ? 2610 ARG A CB    1 
ATOM   9069  C  CG    . ARG A 1 2610 ? 231.098 189.034 191.662 1.00 5.62  ? 2610 ARG A CG    1 
ATOM   9070  C  CD    . ARG A 1 2610 ? 231.844 188.183 192.671 1.00 8.41  ? 2610 ARG A CD    1 
ATOM   9071  N  NE    . ARG A 1 2610 ? 231.259 188.330 193.999 1.00 9.98  ? 2610 ARG A NE    1 
ATOM   9072  C  CZ    . ARG A 1 2610 ? 230.868 187.322 194.765 1.00 8.19  ? 2610 ARG A CZ    1 
ATOM   9073  N  NH1   . ARG A 1 2610 ? 231.026 186.064 194.389 1.00 10.40 ? 2610 ARG A NH1   1 
ATOM   9074  N  NH2   . ARG A 1 2610 ? 230.306 187.583 195.941 1.00 9.07  ? 2610 ARG A NH2   1 
ATOM   9075  N  N     . ALA A 1 2611 ? 230.439 188.004 187.202 1.00 5.62  ? 2611 ALA A N     1 
ATOM   9076  C  CA    . ALA A 1 2611 ? 230.719 187.674 185.812 1.00 8.70  ? 2611 ALA A CA    1 
ATOM   9077  C  C     . ALA A 1 2611 ? 229.898 188.501 184.835 1.00 8.33  ? 2611 ALA A C     1 
ATOM   9078  O  O     . ALA A 1 2611 ? 230.011 188.293 183.622 1.00 16.28 ? 2611 ALA A O     1 
ATOM   9079  C  CB    . ALA A 1 2611 ? 230.465 186.185 185.561 1.00 7.83  ? 2611 ALA A CB    1 
ATOM   9080  N  N     . LEU A 1 2612 ? 229.080 189.427 185.328 1.00 5.77  ? 2612 LEU A N     1 
ATOM   9081  C  CA    . LEU A 1 2612 ? 228.198 190.240 184.496 1.00 8.32  ? 2612 LEU A CA    1 
ATOM   9082  C  C     . LEU A 1 2612 ? 228.427 191.703 184.849 1.00 6.23  ? 2612 LEU A C     1 
ATOM   9083  O  O     . LEU A 1 2612 ? 227.640 192.309 185.589 1.00 9.54  ? 2612 LEU A O     1 
ATOM   9084  C  CB    . LEU A 1 2612 ? 226.739 189.824 184.680 1.00 6.02  ? 2612 LEU A CB    1 
ATOM   9085  C  CG    . LEU A 1 2612 ? 225.788 190.041 183.505 1.00 7.05  ? 2612 LEU A CG    1 
ATOM   9086  C  CD1   . LEU A 1 2612 ? 226.344 189.413 182.249 1.00 6.15  ? 2612 LEU A CD1   1 
ATOM   9087  C  CD2   . LEU A 1 2612 ? 224.445 189.421 183.832 1.00 10.84 ? 2612 LEU A CD2   1 
ATOM   9088  N  N     . PRO A 1 2613 ? 229.502 192.305 184.334 1.00 8.96  ? 2613 PRO A N     1 
ATOM   9089  C  CA    . PRO A 1 2613 ? 229.749 193.725 184.608 1.00 9.24  ? 2613 PRO A CA    1 
ATOM   9090  C  C     . PRO A 1 2613 ? 228.697 194.609 183.961 1.00 22.98 ? 2613 PRO A C     1 
ATOM   9091  O  O     . PRO A 1 2613 ? 227.793 194.110 183.282 1.00 24.68 ? 2613 PRO A O     1 
ATOM   9092  C  CB    . PRO A 1 2613 ? 231.139 193.963 184.005 1.00 6.40  ? 2613 PRO A CB    1 
ATOM   9093  C  CG    . PRO A 1 2613 ? 231.253 192.944 182.933 1.00 10.43 ? 2613 PRO A CG    1 
ATOM   9094  C  CD    . PRO A 1 2613 ? 230.511 191.733 183.425 1.00 11.97 ? 2613 PRO A CD    1 
ATOM   9095  N  N     . ASP A 1 2614 ? 228.811 195.919 184.163 1.00 16.71 ? 2614 ASP A N     1 
ATOM   9096  C  CA    . ASP A 1 2614 ? 227.820 196.892 183.717 1.00 12.70 ? 2614 ASP A CA    1 
ATOM   9097  C  C     . ASP A 1 2614 ? 226.461 196.668 184.372 1.00 9.31  ? 2614 ASP A C     1 
ATOM   9098  O  O     . ASP A 1 2614 ? 225.423 196.994 183.788 1.00 13.10 ? 2614 ASP A O     1 
ATOM   9099  C  CB    . ASP A 1 2614 ? 227.678 196.890 182.188 1.00 14.68 ? 2614 ASP A CB    1 
ATOM   9100  C  CG    . ASP A 1 2614 ? 228.908 197.433 181.492 1.00 28.55 ? 2614 ASP A CG    1 
ATOM   9101  O  OD1   . ASP A 1 2614 ? 229.601 198.286 182.086 1.00 31.08 ? 2614 ASP A OD1   1 
ATOM   9102  O  OD2   . ASP A 1 2614 ? 229.184 197.006 180.351 1.00 28.22 ? 2614 ASP A OD2   1 
ATOM   9103  N  N     . MET A 1 2615 ? 226.450 196.112 185.582 1.00 7.93  ? 2615 MET A N     1 
ATOM   9104  C  CA    . MET A 1 2615 ? 225.224 195.888 186.338 1.00 6.35  ? 2615 MET A CA    1 
ATOM   9105  C  C     . MET A 1 2615 ? 225.493 196.150 187.812 1.00 6.21  ? 2615 MET A C     1 
ATOM   9106  O  O     . MET A 1 2615 ? 226.355 195.501 188.412 1.00 10.03 ? 2615 MET A O     1 
ATOM   9107  C  CB    . MET A 1 2615 ? 224.688 194.469 186.120 1.00 5.76  ? 2615 MET A CB    1 
ATOM   9108  C  CG    . MET A 1 2615 ? 223.763 194.361 184.918 1.00 10.48 ? 2615 MET A CG    1 
ATOM   9109  S  SD    . MET A 1 2615 ? 223.379 192.682 184.395 1.00 22.84 ? 2615 MET A SD    1 
ATOM   9110  C  CE    . MET A 1 2615 ? 222.375 192.100 185.753 1.00 2.27  ? 2615 MET A CE    1 
ATOM   9111  N  N     . GLU A 1 2616 ? 224.762 197.101 188.383 1.00 5.54  ? 2616 GLU A N     1 
ATOM   9112  C  CA    . GLU A 1 2616 ? 224.876 197.464 189.790 1.00 4.55  ? 2616 GLU A CA    1 
ATOM   9113  C  C     . GLU A 1 2616 ? 223.695 196.888 190.558 1.00 2.11  ? 2616 GLU A C     1 
ATOM   9114  O  O     . GLU A 1 2616 ? 222.543 197.051 190.146 1.00 5.42  ? 2616 GLU A O     1 
ATOM   9115  C  CB    . GLU A 1 2616 ? 224.919 198.983 189.963 1.00 9.87  ? 2616 GLU A CB    1 
ATOM   9116  C  CG    . GLU A 1 2616 ? 225.114 199.427 191.405 1.00 15.97 ? 2616 GLU A CG    1 
ATOM   9117  C  CD    . GLU A 1 2616 ? 225.202 200.934 191.561 1.00 23.01 ? 2616 GLU A CD    1 
ATOM   9118  O  OE1   . GLU A 1 2616 ? 225.090 201.651 190.547 1.00 24.34 ? 2616 GLU A OE1   1 
ATOM   9119  O  OE2   . GLU A 1 2616 ? 225.381 201.400 192.706 1.00 29.09 ? 2616 GLU A OE2   1 
ATOM   9120  N  N     . VAL A 1 2617 ? 223.982 196.228 191.675 1.00 1.12  ? 2617 VAL A N     1 
ATOM   9121  C  CA    . VAL A 1 2617 ? 222.958 195.607 192.507 1.00 0.83  ? 2617 VAL A CA    1 
ATOM   9122  C  C     . VAL A 1 2617 ? 222.678 196.509 193.701 1.00 0.35  ? 2617 VAL A C     1 
ATOM   9123  O  O     . VAL A 1 2617 ? 223.604 197.051 194.318 1.00 0.79  ? 2617 VAL A O     1 
ATOM   9124  C  CB    . VAL A 1 2617 ? 223.378 194.192 192.951 1.00 0.73  ? 2617 VAL A CB    1 
ATOM   9125  C  CG1   . VAL A 1 2617 ? 224.660 194.226 193.769 1.00 1.35  ? 2617 VAL A CG1   1 
ATOM   9126  C  CG2   . VAL A 1 2617 ? 222.256 193.520 193.732 1.00 0.63  ? 2617 VAL A CG2   1 
ATOM   9127  N  N     . VAL A 1 2618 ? 221.399 196.704 194.001 1.00 0.49  ? 2618 VAL A N     1 
ATOM   9128  C  CA    . VAL A 1 2618 ? 220.960 197.463 195.165 1.00 0.51  ? 2618 VAL A CA    1 
ATOM   9129  C  C     . VAL A 1 2618 ? 220.026 196.572 195.966 1.00 0.26  ? 2618 VAL A C     1 
ATOM   9130  O  O     . VAL A 1 2618 ? 218.956 196.188 195.478 1.00 0.52  ? 2618 VAL A O     1 
ATOM   9131  C  CB    . VAL A 1 2618 ? 220.269 198.777 194.768 1.00 0.41  ? 2618 VAL A CB    1 
ATOM   9132  C  CG1   . VAL A 1 2618 ? 219.548 199.377 195.959 1.00 0.45  ? 2618 VAL A CG1   1 
ATOM   9133  C  CG2   . VAL A 1 2618 ? 221.281 199.754 194.204 1.00 0.42  ? 2618 VAL A CG2   1 
ATOM   9134  N  N     . GLY A 1 2619 ? 220.424 196.249 197.191 1.00 0.21  ? 2619 GLY A N     1 
ATOM   9135  C  CA    . GLY A 1 2619 ? 219.664 195.326 198.010 1.00 0.45  ? 2619 GLY A CA    1 
ATOM   9136  C  C     . GLY A 1 2619 ? 218.529 195.961 198.785 1.00 0.34  ? 2619 GLY A C     1 
ATOM   9137  O  O     . GLY A 1 2619 ? 218.745 196.871 199.588 1.00 0.50  ? 2619 GLY A O     1 
ATOM   9138  N  N     . LEU A 1 2620 ? 217.312 195.486 198.547 1.00 0.74  ? 2620 LEU A N     1 
ATOM   9139  C  CA    . LEU A 1 2620 ? 216.134 195.895 199.298 1.00 0.68  ? 2620 LEU A CA    1 
ATOM   9140  C  C     . LEU A 1 2620 ? 215.666 194.722 200.145 1.00 0.66  ? 2620 LEU A C     1 
ATOM   9141  O  O     . LEU A 1 2620 ? 215.630 193.584 199.667 1.00 1.81  ? 2620 LEU A O     1 
ATOM   9142  C  CB    . LEU A 1 2620 ? 215.010 196.360 198.370 1.00 0.32  ? 2620 LEU A CB    1 
ATOM   9143  C  CG    . LEU A 1 2620 ? 215.238 197.646 197.576 1.00 0.51  ? 2620 LEU A CG    1 
ATOM   9144  C  CD1   . LEU A 1 2620 ? 215.880 197.349 196.229 1.00 0.98  ? 2620 LEU A CD1   1 
ATOM   9145  C  CD2   . LEU A 1 2620 ? 213.932 198.397 197.400 1.00 0.40  ? 2620 LEU A CD2   1 
ATOM   9146  N  N     . ASN A 1 2621 ? 215.319 194.997 201.394 1.00 0.75  ? 2621 ASN A N     1 
ATOM   9147  C  CA    . ASN A 1 2621 ? 214.927 193.965 202.348 1.00 1.05  ? 2621 ASN A CA    1 
ATOM   9148  C  C     . ASN A 1 2621 ? 213.451 194.151 202.675 1.00 0.79  ? 2621 ASN A C     1 
ATOM   9149  O  O     . ASN A 1 2621 ? 213.078 195.047 203.435 1.00 5.81  ? 2621 ASN A O     1 
ATOM   9150  C  CB    . ASN A 1 2621 ? 215.799 194.030 203.594 1.00 2.12  ? 2621 ASN A CB    1 
ATOM   9151  C  CG    . ASN A 1 2621 ? 217.246 193.730 203.293 1.00 5.56  ? 2621 ASN A CG    1 
ATOM   9152  O  OD1   . ASN A 1 2621 ? 218.049 194.639 203.095 1.00 2.97  ? 2621 ASN A OD1   1 
ATOM   9153  N  ND2   . ASN A 1 2621 ? 217.590 192.448 203.248 1.00 5.16  ? 2621 ASN A ND2   1 
ATOM   9154  N  N     . PHE A 1 2622 ? 212.615 193.300 202.093 1.00 0.63  ? 2622 PHE A N     1 
ATOM   9155  C  CA    . PHE A 1 2622 ? 211.179 193.397 202.294 1.00 0.46  ? 2622 PHE A CA    1 
ATOM   9156  C  C     . PHE A 1 2622 ? 210.800 192.869 203.671 1.00 0.88  ? 2622 PHE A C     1 
ATOM   9157  O  O     . PHE A 1 2622 ? 211.412 191.932 204.188 1.00 1.29  ? 2622 PHE A O     1 
ATOM   9158  C  CB    . PHE A 1 2622 ? 210.430 192.619 201.212 1.00 0.36  ? 2622 PHE A CB    1 
ATOM   9159  C  CG    . PHE A 1 2622 ? 210.346 193.331 199.889 1.00 0.57  ? 2622 PHE A CG    1 
ATOM   9160  C  CD1   . PHE A 1 2622 ? 211.191 194.388 199.592 1.00 0.36  ? 2622 PHE A CD1   1 
ATOM   9161  C  CD2   . PHE A 1 2622 ? 209.426 192.932 198.934 1.00 0.25  ? 2622 PHE A CD2   1 
ATOM   9162  C  CE1   . PHE A 1 2622 ? 211.115 195.033 198.376 1.00 0.27  ? 2622 PHE A CE1   1 
ATOM   9163  C  CE2   . PHE A 1 2622 ? 209.345 193.576 197.717 1.00 0.12  ? 2622 PHE A CE2   1 
ATOM   9164  C  CZ    . PHE A 1 2622 ? 210.190 194.628 197.439 1.00 0.13  ? 2622 PHE A CZ    1 
ATOM   9165  N  N     . SER A 1 2623 ? 209.793 193.487 204.264 1.00 0.71  ? 2623 SER A N     1 
ATOM   9166  C  CA    . SER A 1 2623 ? 209.185 193.015 205.497 1.00 0.75  ? 2623 SER A CA    1 
ATOM   9167  C  C     . SER A 1 2623 ? 207.697 192.802 205.242 1.00 0.56  ? 2623 SER A C     1 
ATOM   9168  O  O     . SER A 1 2623 ? 207.219 192.916 204.112 1.00 0.67  ? 2623 SER A O     1 
ATOM   9169  C  CB    . SER A 1 2623 ? 209.442 194.002 206.637 1.00 1.17  ? 2623 SER A CB    1 
ATOM   9170  O  OG    . SER A 1 2623 ? 208.748 195.219 206.426 1.00 1.54  ? 2623 SER A OG    1 
ATOM   9171  N  N     . SER A 1 2624 ? 206.960 192.483 206.305 1.00 0.81  ? 2624 SER A N     1 
ATOM   9172  C  CA    . SER A 1 2624 ? 205.510 192.388 206.176 1.00 1.04  ? 2624 SER A CA    1 
ATOM   9173  C  C     . SER A 1 2624 ? 204.890 193.747 205.877 1.00 0.82  ? 2624 SER A C     1 
ATOM   9174  O  O     . SER A 1 2624 ? 203.838 193.819 205.236 1.00 1.86  ? 2624 SER A O     1 
ATOM   9175  C  CB    . SER A 1 2624 ? 204.905 191.788 207.444 1.00 2.14  ? 2624 SER A CB    1 
ATOM   9176  O  OG    . SER A 1 2624 ? 205.238 192.555 208.586 1.00 5.90  ? 2624 SER A OG    1 
ATOM   9177  N  N     . ALA A 1 2625 ? 205.536 194.826 206.309 1.00 0.73  ? 2625 ALA A N     1 
ATOM   9178  C  CA    . ALA A 1 2625 ? 205.024 196.177 206.138 1.00 0.62  ? 2625 ALA A CA    1 
ATOM   9179  C  C     . ALA A 1 2625 ? 205.602 196.883 204.918 1.00 1.23  ? 2625 ALA A C     1 
ATOM   9180  O  O     . ALA A 1 2625 ? 205.407 198.093 204.769 1.00 2.34  ? 2625 ALA A O     1 
ATOM   9181  C  CB    . ALA A 1 2625 ? 205.298 197.006 207.394 1.00 1.62  ? 2625 ALA A CB    1 
ATOM   9182  N  N     . THR A 1 2626 ? 206.312 196.166 204.052 1.00 1.27  ? 2626 THR A N     1 
ATOM   9183  C  CA    . THR A 1 2626 ? 206.911 196.793 202.882 1.00 0.95  ? 2626 THR A CA    1 
ATOM   9184  C  C     . THR A 1 2626 ? 205.832 197.210 201.888 1.00 0.93  ? 2626 THR A C     1 
ATOM   9185  O  O     . THR A 1 2626 ? 204.968 196.410 201.518 1.00 1.18  ? 2626 THR A O     1 
ATOM   9186  C  CB    . THR A 1 2626 ? 207.908 195.841 202.220 1.00 0.66  ? 2626 THR A CB    1 
ATOM   9187  O  OG1   . THR A 1 2626 ? 209.086 195.749 203.027 1.00 1.07  ? 2626 THR A OG1   1 
ATOM   9188  C  CG2   . THR A 1 2626 ? 208.296 196.339 200.835 1.00 0.49  ? 2626 THR A CG2   1 
ATOM   9189  N  N     . THR A 1 2627 ? 205.887 198.465 201.460 1.00 1.65  ? 2627 THR A N     1 
ATOM   9190  C  CA    . THR A 1 2627 ? 204.966 199.025 200.481 1.00 1.10  ? 2627 THR A CA    1 
ATOM   9191  C  C     . THR A 1 2627 ? 205.762 199.421 199.243 1.00 1.15  ? 2627 THR A C     1 
ATOM   9192  O  O     . THR A 1 2627 ? 206.998 199.363 199.267 1.00 1.68  ? 2627 THR A O     1 
ATOM   9193  C  CB    . THR A 1 2627 ? 204.220 200.228 201.068 1.00 2.90  ? 2627 THR A CB    1 
ATOM   9194  O  OG1   . THR A 1 2627 ? 205.129 201.319 201.247 1.00 6.72  ? 2627 THR A OG1   1 
ATOM   9195  C  CG2   . THR A 1 2627 ? 203.594 199.869 202.405 1.00 2.18  ? 2627 THR A CG2   1 
ATOM   9196  N  N     . PRO A 1 2628 ? 205.113 199.810 198.141 1.00 2.12  ? 2628 PRO A N     1 
ATOM   9197  C  CA    . PRO A 1 2628 ? 205.880 200.297 196.985 1.00 1.36  ? 2628 PRO A CA    1 
ATOM   9198  C  C     . PRO A 1 2628 ? 206.751 201.497 197.301 1.00 1.41  ? 2628 PRO A C     1 
ATOM   9199  O  O     . PRO A 1 2628 ? 207.699 201.769 196.557 1.00 1.13  ? 2628 PRO A O     1 
ATOM   9200  C  CB    . PRO A 1 2628 ? 204.784 200.652 195.974 1.00 0.67  ? 2628 PRO A CB    1 
ATOM   9201  C  CG    . PRO A 1 2628 ? 203.696 199.710 196.291 1.00 0.45  ? 2628 PRO A CG    1 
ATOM   9202  C  CD    . PRO A 1 2628 ? 203.698 199.590 197.789 1.00 0.72  ? 2628 PRO A CD    1 
ATOM   9203  N  N     . GLU A 1 2629 ? 206.463 202.214 198.387 1.00 2.13  ? 2629 GLU A N     1 
ATOM   9204  C  CA    . GLU A 1 2629 ? 207.217 203.416 198.714 1.00 2.04  ? 2629 GLU A CA    1 
ATOM   9205  C  C     . GLU A 1 2629 ? 208.674 203.090 199.032 1.00 3.52  ? 2629 GLU A C     1 
ATOM   9206  O  O     . GLU A 1 2629 ? 209.556 203.932 198.832 1.00 4.24  ? 2629 GLU A O     1 
ATOM   9207  C  CB    . GLU A 1 2629 ? 206.546 204.130 199.886 1.00 3.31  ? 2629 GLU A CB    1 
ATOM   9208  C  CG    . GLU A 1 2629 ? 207.197 205.428 200.289 1.00 11.98 ? 2629 GLU A CG    1 
ATOM   9209  C  CD    . GLU A 1 2629 ? 207.086 206.478 199.197 1.00 17.79 ? 2629 GLU A CD    1 
ATOM   9210  O  OE1   . GLU A 1 2629 ? 206.142 206.401 198.385 1.00 16.67 ? 2629 GLU A OE1   1 
ATOM   9211  O  OE2   . GLU A 1 2629 ? 207.935 207.387 199.146 1.00 27.46 ? 2629 GLU A OE2   1 
ATOM   9212  N  N     . LEU A 1 2630 ? 208.945 201.876 199.523 1.00 1.41  ? 2630 LEU A N     1 
ATOM   9213  C  CA    . LEU A 1 2630 ? 210.326 201.441 199.710 1.00 0.95  ? 2630 LEU A CA    1 
ATOM   9214  C  C     . LEU A 1 2630 ? 211.072 201.382 198.385 1.00 1.80  ? 2630 LEU A C     1 
ATOM   9215  O  O     . LEU A 1 2630 ? 212.245 201.765 198.307 1.00 3.32  ? 2630 LEU A O     1 
ATOM   9216  C  CB    . LEU A 1 2630 ? 210.363 200.076 200.396 1.00 2.75  ? 2630 LEU A CB    1 
ATOM   9217  C  CG    . LEU A 1 2630 ? 211.757 199.551 200.750 1.00 0.84  ? 2630 LEU A CG    1 
ATOM   9218  C  CD1   . LEU A 1 2630 ? 212.301 200.243 201.984 1.00 3.56  ? 2630 LEU A CD1   1 
ATOM   9219  C  CD2   . LEU A 1 2630 ? 211.744 198.041 200.931 1.00 0.39  ? 2630 LEU A CD2   1 
ATOM   9220  N  N     . LEU A 1 2631 ? 210.414 200.887 197.337 1.00 1.37  ? 2631 LEU A N     1 
ATOM   9221  C  CA    . LEU A 1 2631 ? 211.020 200.898 196.011 1.00 0.76  ? 2631 LEU A CA    1 
ATOM   9222  C  C     . LEU A 1 2631 ? 211.228 202.323 195.515 1.00 1.12  ? 2631 LEU A C     1 
ATOM   9223  O  O     . LEU A 1 2631 ? 212.233 202.617 194.858 1.00 1.12  ? 2631 LEU A O     1 
ATOM   9224  C  CB    . LEU A 1 2631 ? 210.151 200.112 195.030 1.00 1.09  ? 2631 LEU A CB    1 
ATOM   9225  C  CG    . LEU A 1 2631 ? 210.048 198.595 195.209 1.00 0.50  ? 2631 LEU A CG    1 
ATOM   9226  C  CD1   . LEU A 1 2631 ? 208.971 198.025 194.311 1.00 0.20  ? 2631 LEU A CD1   1 
ATOM   9227  C  CD2   . LEU A 1 2631 ? 211.368 197.915 194.933 1.00 1.24  ? 2631 LEU A CD2   1 
ATOM   9228  N  N     . LEU A 1 2632 ? 210.289 203.220 195.825 1.00 1.52  ? 2632 LEU A N     1 
ATOM   9229  C  CA    . LEU A 1 2632 ? 210.358 204.585 195.316 1.00 0.98  ? 2632 LEU A CA    1 
ATOM   9230  C  C     . LEU A 1 2632 ? 211.516 205.358 195.936 1.00 1.94  ? 2632 LEU A C     1 
ATOM   9231  O  O     . LEU A 1 2632 ? 212.152 206.175 195.260 1.00 2.45  ? 2632 LEU A O     1 
ATOM   9232  C  CB    . LEU A 1 2632 ? 209.031 205.300 195.564 1.00 1.48  ? 2632 LEU A CB    1 
ATOM   9233  C  CG    . LEU A 1 2632 ? 207.845 204.700 194.806 1.00 1.13  ? 2632 LEU A CG    1 
ATOM   9234  C  CD1   . LEU A 1 2632 ? 206.533 205.291 195.287 1.00 2.24  ? 2632 LEU A CD1   1 
ATOM   9235  C  CD2   . LEU A 1 2632 ? 208.011 204.899 193.311 1.00 0.31  ? 2632 LEU A CD2   1 
ATOM   9236  N  N     . LYS A 1 2633 ? 211.796 205.128 197.221 1.00 3.13  ? 2633 LYS A N     1 
ATOM   9237  C  CA    . LYS A 1 2633 ? 212.962 205.751 197.841 1.00 1.89  ? 2633 LYS A CA    1 
ATOM   9238  C  C     . LYS A 1 2633 ? 214.253 205.280 197.188 1.00 2.07  ? 2633 LYS A C     1 
ATOM   9239  O  O     . LYS A 1 2633 ? 215.179 206.073 196.985 1.00 4.10  ? 2633 LYS A O     1 
ATOM   9240  C  CB    . LYS A 1 2633 ? 212.993 205.464 199.340 1.00 2.31  ? 2633 LYS A CB    1 
ATOM   9241  C  CG    . LYS A 1 2633 ? 211.822 206.000 200.128 1.00 3.22  ? 2633 LYS A CG    1 
ATOM   9242  C  CD    . LYS A 1 2633 ? 211.824 207.514 200.118 1.00 9.43  ? 2633 LYS A CD    1 
ATOM   9243  C  CE    . LYS A 1 2633 ? 210.779 208.073 201.055 1.00 14.12 ? 2633 LYS A CE    1 
ATOM   9244  N  NZ    . LYS A 1 2633 ? 209.400 207.831 200.606 1.00 18.10 ? 2633 LYS A NZ    1 
ATOM   9245  N  N     . THR A 1 2634 ? 214.334 203.990 196.856 1.00 1.71  ? 2634 THR A N     1 
ATOM   9246  C  CA    . THR A 1 2634 ? 215.496 203.478 196.140 1.00 1.33  ? 2634 THR A CA    1 
ATOM   9247  C  C     . THR A 1 2634 ? 215.632 204.139 194.773 1.00 1.25  ? 2634 THR A C     1 
ATOM   9248  O  O     . THR A 1 2634 ? 216.745 204.438 194.326 1.00 2.93  ? 2634 THR A O     1 
ATOM   9249  C  CB    . THR A 1 2634 ? 215.393 201.958 196.005 1.00 1.13  ? 2634 THR A CB    1 
ATOM   9250  O  OG1   . THR A 1 2634 ? 215.390 201.367 197.308 1.00 1.29  ? 2634 THR A OG1   1 
ATOM   9251  C  CG2   . THR A 1 2634 ? 216.559 201.404 195.215 1.00 0.88  ? 2634 THR A CG2   1 
ATOM   9252  N  N     . PHE A 1 2635 ? 214.508 204.383 194.098 1.00 0.80  ? 2635 PHE A N     1 
ATOM   9253  C  CA    . PHE A 1 2635 ? 214.548 205.102 192.829 1.00 1.00  ? 2635 PHE A CA    1 
ATOM   9254  C  C     . PHE A 1 2635 ? 215.034 206.533 193.023 1.00 2.23  ? 2635 PHE A C     1 
ATOM   9255  O  O     . PHE A 1 2635 ? 215.789 207.057 192.197 1.00 5.52  ? 2635 PHE A O     1 
ATOM   9256  C  CB    . PHE A 1 2635 ? 213.168 205.089 192.173 1.00 1.14  ? 2635 PHE A CB    1 
ATOM   9257  C  CG    . PHE A 1 2635 ? 212.740 203.737 191.679 1.00 0.80  ? 2635 PHE A CG    1 
ATOM   9258  C  CD1   . PHE A 1 2635 ? 213.680 202.784 191.328 1.00 0.49  ? 2635 PHE A CD1   1 
ATOM   9259  C  CD2   . PHE A 1 2635 ? 211.396 203.422 191.560 1.00 0.58  ? 2635 PHE A CD2   1 
ATOM   9260  C  CE1   . PHE A 1 2635 ? 213.288 201.544 190.872 1.00 0.51  ? 2635 PHE A CE1   1 
ATOM   9261  C  CE2   . PHE A 1 2635 ? 210.999 202.182 191.104 1.00 0.41  ? 2635 PHE A CE2   1 
ATOM   9262  C  CZ    . PHE A 1 2635 ? 211.947 201.241 190.759 1.00 0.43  ? 2635 PHE A CZ    1 
ATOM   9263  N  N     . ASP A 1 2636 ? 214.612 207.183 194.111 1.00 2.75  ? 2636 ASP A N     1 
ATOM   9264  C  CA    . ASP A 1 2636 ? 215.005 208.569 194.345 1.00 2.32  ? 2636 ASP A CA    1 
ATOM   9265  C  C     . ASP A 1 2636 ? 216.505 208.708 194.557 1.00 5.50  ? 2636 ASP A C     1 
ATOM   9266  O  O     . ASP A 1 2636 ? 217.091 209.729 194.182 1.00 9.14  ? 2636 ASP A O     1 
ATOM   9267  C  CB    . ASP A 1 2636 ? 214.255 209.130 195.552 1.00 2.65  ? 2636 ASP A CB    1 
ATOM   9268  C  CG    . ASP A 1 2636 ? 212.834 209.517 195.224 1.00 12.85 ? 2636 ASP A CG    1 
ATOM   9269  O  OD1   . ASP A 1 2636 ? 212.593 210.007 194.100 1.00 16.69 ? 2636 ASP A OD1   1 
ATOM   9270  O  OD2   . ASP A 1 2636 ? 211.955 209.333 196.092 1.00 21.01 ? 2636 ASP A OD2   1 
ATOM   9271  N  N     . HIS A 1 2637 ? 217.141 207.702 195.152 1.00 2.48  ? 2637 HIS A N     1 
ATOM   9272  C  CA    . HIS A 1 2637 ? 218.557 207.785 195.478 1.00 1.95  ? 2637 HIS A CA    1 
ATOM   9273  C  C     . HIS A 1 2637 ? 219.456 207.358 194.322 1.00 3.34  ? 2637 HIS A C     1 
ATOM   9274  O  O     . HIS A 1 2637 ? 220.502 207.973 194.094 1.00 2.92  ? 2637 HIS A O     1 
ATOM   9275  C  CB    . HIS A 1 2637 ? 218.857 206.932 196.712 1.00 1.91  ? 2637 HIS A CB    1 
ATOM   9276  C  CG    . HIS A 1 2637 ? 220.290 206.969 197.137 1.00 5.52  ? 2637 HIS A CG    1 
ATOM   9277  N  ND1   . HIS A 1 2637 ? 221.228 206.072 196.671 1.00 5.67  ? 2637 HIS A ND1   1 
ATOM   9278  C  CD2   . HIS A 1 2637 ? 220.949 207.796 197.982 1.00 5.70  ? 2637 HIS A CD2   1 
ATOM   9279  C  CE1   . HIS A 1 2637 ? 222.401 206.343 197.212 1.00 7.64  ? 2637 HIS A CE1   1 
ATOM   9280  N  NE2   . HIS A 1 2637 ? 222.260 207.386 198.012 1.00 6.21  ? 2637 HIS A NE2   1 
ATOM   9281  N  N     . TYR A 1 2638 ? 219.068 206.320 193.584 1.00 3.37  ? 2638 TYR A N     1 
ATOM   9282  C  CA    . TYR A 1 2638 ? 219.911 205.756 192.543 1.00 2.10  ? 2638 TYR A CA    1 
ATOM   9283  C  C     . TYR A 1 2638 ? 219.504 206.148 191.131 1.00 3.03  ? 2638 TYR A C     1 
ATOM   9284  O  O     . TYR A 1 2638 ? 220.266 205.886 190.195 1.00 4.12  ? 2638 TYR A O     1 
ATOM   9285  C  CB    . TYR A 1 2638 ? 219.922 204.225 192.643 1.00 1.94  ? 2638 TYR A CB    1 
ATOM   9286  C  CG    . TYR A 1 2638 ? 220.541 203.686 193.906 1.00 2.51  ? 2638 TYR A CG    1 
ATOM   9287  C  CD1   . TYR A 1 2638 ? 221.910 203.467 193.990 1.00 3.71  ? 2638 TYR A CD1   1 
ATOM   9288  C  CD2   . TYR A 1 2638 ? 219.760 203.387 195.013 1.00 1.60  ? 2638 TYR A CD2   1 
ATOM   9289  C  CE1   . TYR A 1 2638 ? 222.483 202.972 195.144 1.00 3.15  ? 2638 TYR A CE1   1 
ATOM   9290  C  CE2   . TYR A 1 2638 ? 220.324 202.892 196.169 1.00 2.24  ? 2638 TYR A CE2   1 
ATOM   9291  C  CZ    . TYR A 1 2638 ? 221.684 202.686 196.229 1.00 3.12  ? 2638 TYR A CZ    1 
ATOM   9292  O  OH    . TYR A 1 2638 ? 222.250 202.192 197.381 1.00 12.05 ? 2638 TYR A OH    1 
ATOM   9293  N  N     . CYS A 1 2639 ? 218.343 206.764 190.949 1.00 2.78  ? 2639 CYS A N     1 
ATOM   9294  C  CA    . CYS A 1 2639 ? 217.810 207.019 189.622 1.00 1.47  ? 2639 CYS A CA    1 
ATOM   9295  C  C     . CYS A 1 2639 ? 217.334 208.461 189.523 1.00 1.17  ? 2639 CYS A C     1 
ATOM   9296  O  O     . CYS A 1 2639 ? 217.102 209.133 190.530 1.00 1.63  ? 2639 CYS A O     1 
ATOM   9297  C  CB    . CYS A 1 2639 ? 216.659 206.057 189.293 1.00 1.39  ? 2639 CYS A CB    1 
ATOM   9298  S  SG    . CYS A 1 2639 ? 217.125 204.312 189.258 1.00 5.27  ? 2639 CYS A SG    1 
ATOM   9299  N  N     . GLU A 1 2640 ? 217.199 208.933 188.290 1.00 1.97  ? 2640 GLU A N     1 
ATOM   9300  C  CA    . GLU A 1 2640 ? 216.687 210.267 188.017 1.00 2.81  ? 2640 GLU A CA    1 
ATOM   9301  C  C     . GLU A 1 2640 ? 215.471 210.182 187.104 1.00 1.80  ? 2640 GLU A C     1 
ATOM   9302  O  O     . GLU A 1 2640 ? 215.381 209.310 186.238 1.00 1.16  ? 2640 GLU A O     1 
ATOM   9303  C  CB    . GLU A 1 2640 ? 217.760 211.164 187.379 1.00 2.54  ? 2640 GLU A CB    1 
ATOM   9304  C  CG    . GLU A 1 2640 ? 218.211 210.726 185.997 1.00 9.39  ? 2640 GLU A CG    1 
ATOM   9305  C  CD    . GLU A 1 2640 ? 219.314 211.604 185.436 1.00 25.04 ? 2640 GLU A CD    1 
ATOM   9306  O  OE1   . GLU A 1 2640 ? 219.743 212.544 186.136 1.00 21.27 ? 2640 GLU A OE1   1 
ATOM   9307  O  OE2   . GLU A 1 2640 ? 219.747 211.357 184.290 1.00 27.26 ? 2640 GLU A OE2   1 
ATOM   9308  N  N     . TYR A 1 2641 ? 214.528 211.091 187.326 1.00 3.56  ? 2641 TYR A N     1 
ATOM   9309  C  CA    . TYR A 1 2641 ? 213.397 211.284 186.427 1.00 1.71  ? 2641 TYR A CA    1 
ATOM   9310  C  C     . TYR A 1 2641 ? 213.760 212.371 185.427 1.00 1.61  ? 2641 TYR A C     1 
ATOM   9311  O  O     . TYR A 1 2641 ? 214.134 213.479 185.823 1.00 5.80  ? 2641 TYR A O     1 
ATOM   9312  C  CB    . TYR A 1 2641 ? 212.139 211.676 187.201 1.00 1.56  ? 2641 TYR A CB    1 
ATOM   9313  C  CG    . TYR A 1 2641 ? 211.626 210.630 188.162 1.00 1.53  ? 2641 TYR A CG    1 
ATOM   9314  C  CD1   . TYR A 1 2641 ? 212.133 210.534 189.450 1.00 2.33  ? 2641 TYR A CD1   1 
ATOM   9315  C  CD2   . TYR A 1 2641 ? 210.617 209.753 187.788 1.00 0.83  ? 2641 TYR A CD2   1 
ATOM   9316  C  CE1   . TYR A 1 2641 ? 211.662 209.585 190.335 1.00 1.87  ? 2641 TYR A CE1   1 
ATOM   9317  C  CE2   . TYR A 1 2641 ? 210.138 208.800 188.667 1.00 1.15  ? 2641 TYR A CE2   1 
ATOM   9318  C  CZ    . TYR A 1 2641 ? 210.664 208.720 189.938 1.00 1.80  ? 2641 TYR A CZ    1 
ATOM   9319  O  OH    . TYR A 1 2641 ? 210.192 207.776 190.815 1.00 2.93  ? 2641 TYR A OH    1 
ATOM   9320  N  N     . ARG A 1 2642 ? 213.665 212.059 184.138 1.00 1.75  ? 2642 ARG A N     1 
ATOM   9321  C  CA    . ARG A 1 2642 ? 213.960 213.025 183.092 1.00 3.36  ? 2642 ARG A CA    1 
ATOM   9322  C  C     . ARG A 1 2642 ? 212.786 213.133 182.127 1.00 5.43  ? 2642 ARG A C     1 
ATOM   9323  O  O     . ARG A 1 2642 ? 212.162 212.128 181.772 1.00 4.19  ? 2642 ARG A O     1 
ATOM   9324  C  CB    . ARG A 1 2642 ? 215.259 212.661 182.347 1.00 3.66  ? 2642 ARG A CB    1 
ATOM   9325  C  CG    . ARG A 1 2642 ? 215.175 211.503 181.364 1.00 3.62  ? 2642 ARG A CG    1 
ATOM   9326  C  CD    . ARG A 1 2642 ? 216.414 211.471 180.472 1.00 3.72  ? 2642 ARG A CD    1 
ATOM   9327  N  NE    . ARG A 1 2642 ? 216.338 210.458 179.424 1.00 5.87  ? 2642 ARG A NE    1 
ATOM   9328  C  CZ    . ARG A 1 2642 ? 216.499 209.157 179.623 1.00 6.56  ? 2642 ARG A CZ    1 
ATOM   9329  N  NH1   . ARG A 1 2642 ? 216.774 208.667 180.820 1.00 9.62  ? 2642 ARG A NH1   1 
ATOM   9330  N  NH2   . ARG A 1 2642 ? 216.387 208.325 178.591 1.00 4.16  ? 2642 ARG A NH2   1 
ATOM   9331  N  N     . ARG A 1 2643 ? 212.475 214.365 181.734 1.00 12.44 ? 2643 ARG A N     1 
ATOM   9332  C  CA    . ARG A 1 2643 ? 211.442 214.644 180.747 1.00 7.61  ? 2643 ARG A CA    1 
ATOM   9333  C  C     . ARG A 1 2643 ? 211.996 214.376 179.353 1.00 6.71  ? 2643 ARG A C     1 
ATOM   9334  O  O     . ARG A 1 2643 ? 213.016 214.952 178.961 1.00 8.24  ? 2643 ARG A O     1 
ATOM   9335  C  CB    . ARG A 1 2643 ? 210.960 216.090 180.872 1.00 7.82  ? 2643 ARG A CB    1 
ATOM   9336  C  CG    . ARG A 1 2643 ? 209.894 216.519 179.863 1.00 16.91 ? 2643 ARG A CG    1 
ATOM   9337  C  CD    . ARG A 1 2643 ? 208.555 215.808 180.010 1.00 19.64 ? 2643 ARG A CD    1 
ATOM   9338  N  NE    . ARG A 1 2643 ? 207.884 216.120 181.268 1.00 21.45 ? 2643 ARG A NE    1 
ATOM   9339  C  CZ    . ARG A 1 2643 ? 206.830 215.463 181.735 1.00 23.04 ? 2643 ARG A CZ    1 
ATOM   9340  N  NH1   . ARG A 1 2643 ? 206.269 214.481 181.049 1.00 17.83 ? 2643 ARG A NH1   1 
ATOM   9341  N  NH2   . ARG A 1 2643 ? 206.317 215.811 182.912 1.00 16.85 ? 2643 ARG A NH2   1 
ATOM   9342  N  N     . THR A 1 2644 ? 211.329 213.498 178.617 1.00 6.91  ? 2644 THR A N     1 
ATOM   9343  C  CA    . THR A 1 2644 ? 211.651 213.162 177.242 1.00 6.76  ? 2644 THR A CA    1 
ATOM   9344  C  C     . THR A 1 2644 ? 210.443 213.456 176.363 1.00 9.43  ? 2644 THR A C     1 
ATOM   9345  O  O     . THR A 1 2644 ? 209.321 213.586 176.866 1.00 12.73 ? 2644 THR A O     1 
ATOM   9346  C  CB    . THR A 1 2644 ? 212.050 211.683 177.106 1.00 8.84  ? 2644 THR A CB    1 
ATOM   9347  O  OG1   . THR A 1 2644 ? 210.882 210.857 177.191 1.00 11.77 ? 2644 THR A OG1   1 
ATOM   9348  C  CG2   . THR A 1 2644 ? 213.040 211.283 178.191 1.00 6.78  ? 2644 THR A CG2   1 
ATOM   9349  N  N     . PRO A 1 2645 ? 210.634 213.586 175.047 1.00 10.74 ? 2645 PRO A N     1 
ATOM   9350  C  CA    . PRO A 1 2645 ? 209.479 213.844 174.171 1.00 11.09 ? 2645 PRO A CA    1 
ATOM   9351  C  C     . PRO A 1 2645 ? 208.408 212.772 174.245 1.00 8.87  ? 2645 PRO A C     1 
ATOM   9352  O  O     . PRO A 1 2645 ? 207.240 213.058 173.953 1.00 10.29 ? 2645 PRO A O     1 
ATOM   9353  C  CB    . PRO A 1 2645 ? 210.111 213.912 172.774 1.00 8.99  ? 2645 PRO A CB    1 
ATOM   9354  C  CG    . PRO A 1 2645 ? 211.513 214.325 173.024 1.00 8.66  ? 2645 PRO A CG    1 
ATOM   9355  C  CD    . PRO A 1 2645 ? 211.905 213.653 174.304 1.00 6.08  ? 2645 PRO A CD    1 
ATOM   9356  N  N     . ASN A 1 2646 ? 208.765 211.547 174.621 1.00 8.58  ? 2646 ASN A N     1 
ATOM   9357  C  CA    . ASN A 1 2646 ? 207.812 210.451 174.715 1.00 8.53  ? 2646 ASN A CA    1 
ATOM   9358  C  C     . ASN A 1 2646 ? 207.280 210.234 176.125 1.00 9.33  ? 2646 ASN A C     1 
ATOM   9359  O  O     . ASN A 1 2646 ? 206.483 209.314 176.333 1.00 14.19 ? 2646 ASN A O     1 
ATOM   9360  C  CB    . ASN A 1 2646 ? 208.447 209.158 174.197 1.00 7.01  ? 2646 ASN A CB    1 
ATOM   9361  C  CG    . ASN A 1 2646 ? 208.396 209.052 172.691 1.00 15.81 ? 2646 ASN A CG    1 
ATOM   9362  O  OD1   . ASN A 1 2646 ? 209.216 209.640 171.987 1.00 15.50 ? 2646 ASN A OD1   1 
ATOM   9363  N  ND2   . ASN A 1 2646 ? 207.422 208.308 172.184 1.00 15.63 ? 2646 ASN A ND2   1 
ATOM   9364  N  N     . GLY A 1 2647 ? 207.693 211.046 177.090 1.00 6.72  ? 2647 GLY A N     1 
ATOM   9365  C  CA    . GLY A 1 2647 ? 207.230 210.938 178.456 1.00 2.71  ? 2647 GLY A CA    1 
ATOM   9366  C  C     . GLY A 1 2647 ? 208.378 210.911 179.438 1.00 3.51  ? 2647 GLY A C     1 
ATOM   9367  O  O     . GLY A 1 2647 ? 209.547 211.060 179.084 1.00 3.58  ? 2647 GLY A O     1 
ATOM   9368  N  N     . VAL A 1 2648 ? 208.025 210.712 180.702 1.00 1.88  ? 2648 VAL A N     1 
ATOM   9369  C  CA    . VAL A 1 2648 ? 209.009 210.665 181.776 1.00 1.26  ? 2648 VAL A CA    1 
ATOM   9370  C  C     . VAL A 1 2648 ? 209.683 209.300 181.779 1.00 1.04  ? 2648 VAL A C     1 
ATOM   9371  O  O     . VAL A 1 2648 ? 209.015 208.262 181.727 1.00 1.10  ? 2648 VAL A O     1 
ATOM   9372  C  CB    . VAL A 1 2648 ? 208.351 210.964 183.132 1.00 2.33  ? 2648 VAL A CB    1 
ATOM   9373  C  CG1   . VAL A 1 2648 ? 209.374 210.889 184.252 1.00 0.93  ? 2648 VAL A CG1   1 
ATOM   9374  C  CG2   . VAL A 1 2648 ? 207.689 212.329 183.105 1.00 1.27  ? 2648 VAL A CG2   1 
ATOM   9375  N  N     . VAL A 1 2649 ? 211.012 209.300 181.834 1.00 1.26  ? 2649 VAL A N     1 
ATOM   9376  C  CA    . VAL A 1 2649 ? 211.809 208.081 181.864 1.00 0.73  ? 2649 VAL A CA    1 
ATOM   9377  C  C     . VAL A 1 2649 ? 212.607 208.063 183.159 1.00 1.29  ? 2649 VAL A C     1 
ATOM   9378  O  O     . VAL A 1 2649 ? 213.255 209.056 183.507 1.00 2.62  ? 2649 VAL A O     1 
ATOM   9379  C  CB    . VAL A 1 2649 ? 212.740 207.979 180.642 1.00 1.72  ? 2649 VAL A CB    1 
ATOM   9380  C  CG1   . VAL A 1 2649 ? 213.798 206.914 180.863 1.00 2.43  ? 2649 VAL A CG1   1 
ATOM   9381  C  CG2   . VAL A 1 2649 ? 211.936 207.679 179.394 1.00 2.06  ? 2649 VAL A CG2   1 
ATOM   9382  N  N     . LEU A 1 2650 ? 212.542 206.947 183.879 1.00 1.21  ? 2650 LEU A N     1 
ATOM   9383  C  CA    . LEU A 1 2650 ? 213.333 206.738 185.085 1.00 0.39  ? 2650 LEU A CA    1 
ATOM   9384  C  C     . LEU A 1 2650 ? 214.495 205.812 184.748 1.00 0.32  ? 2650 LEU A C     1 
ATOM   9385  O  O     . LEU A 1 2650 ? 214.282 204.660 184.359 1.00 0.60  ? 2650 LEU A O     1 
ATOM   9386  C  CB    . LEU A 1 2650 ? 212.477 206.148 186.204 1.00 0.45  ? 2650 LEU A CB    1 
ATOM   9387  C  CG    . LEU A 1 2650 ? 213.143 205.962 187.568 1.00 0.25  ? 2650 LEU A CG    1 
ATOM   9388  C  CD1   . LEU A 1 2650 ? 213.460 207.307 188.193 1.00 0.45  ? 2650 LEU A CD1   1 
ATOM   9389  C  CD2   . LEU A 1 2650 ? 212.254 205.139 188.482 1.00 0.24  ? 2650 LEU A CD2   1 
ATOM   9390  N  N     . ALA A 1 2651 ? 215.714 206.318 184.895 1.00 0.47  ? 2651 ALA A N     1 
ATOM   9391  C  CA    . ALA A 1 2651 ? 216.921 205.582 184.560 1.00 0.66  ? 2651 ALA A CA    1 
ATOM   9392  C  C     . ALA A 1 2651 ? 217.947 205.762 185.668 1.00 1.05  ? 2651 ALA A C     1 
ATOM   9393  O  O     . ALA A 1 2651 ? 217.919 206.771 186.382 1.00 1.37  ? 2651 ALA A O     1 
ATOM   9394  C  CB    . ALA A 1 2651 ? 217.513 206.050 183.221 1.00 0.45  ? 2651 ALA A CB    1 
ATOM   9395  N  N     . PRO A 1 2652 ? 218.859 204.804 185.835 1.00 1.47  ? 2652 PRO A N     1 
ATOM   9396  C  CA    . PRO A 1 2652 ? 219.893 204.945 186.866 1.00 1.93  ? 2652 PRO A CA    1 
ATOM   9397  C  C     . PRO A 1 2652 ? 220.765 206.165 186.619 1.00 2.68  ? 2652 PRO A C     1 
ATOM   9398  O  O     . PRO A 1 2652 ? 221.020 206.557 185.478 1.00 2.20  ? 2652 PRO A O     1 
ATOM   9399  C  CB    . PRO A 1 2652 ? 220.702 203.648 186.741 1.00 2.14  ? 2652 PRO A CB    1 
ATOM   9400  C  CG    . PRO A 1 2652 ? 219.793 202.697 186.064 1.00 1.46  ? 2652 PRO A CG    1 
ATOM   9401  C  CD    . PRO A 1 2652 ? 218.952 203.509 185.142 1.00 0.99  ? 2652 PRO A CD    1 
ATOM   9402  N  N     . VAL A 1 2653 ? 221.224 206.767 187.718 1.00 5.81  ? 2653 VAL A N     1 
ATOM   9403  C  CA    . VAL A 1 2653 ? 222.064 207.959 187.632 1.00 3.40  ? 2653 VAL A CA    1 
ATOM   9404  C  C     . VAL A 1 2653 ? 223.347 207.647 186.874 1.00 4.55  ? 2653 VAL A C     1 
ATOM   9405  O  O     . VAL A 1 2653 ? 223.775 208.409 185.999 1.00 8.96  ? 2653 VAL A O     1 
ATOM   9406  C  CB    . VAL A 1 2653 ? 222.353 208.510 189.039 1.00 5.65  ? 2653 VAL A CB    1 
ATOM   9407  C  CG1   . VAL A 1 2653 ? 223.510 209.495 189.004 1.00 5.21  ? 2653 VAL A CG1   1 
ATOM   9408  C  CG2   . VAL A 1 2653 ? 221.108 209.165 189.612 1.00 3.61  ? 2653 VAL A CG2   1 
ATOM   9409  N  N     . GLN A 1 2654 ? 223.968 206.514 187.187 1.00 7.40  ? 2654 GLN A N     1 
ATOM   9410  C  CA    . GLN A 1 2654 ? 225.166 206.097 186.475 1.00 8.00  ? 2654 GLN A CA    1 
ATOM   9411  C  C     . GLN A 1 2654 ? 224.805 205.628 185.069 1.00 4.50  ? 2654 GLN A C     1 
ATOM   9412  O  O     . GLN A 1 2654 ? 223.914 204.792 184.891 1.00 5.66  ? 2654 GLN A O     1 
ATOM   9413  C  CB    . GLN A 1 2654 ? 225.871 204.988 187.250 1.00 9.15  ? 2654 GLN A CB    1 
ATOM   9414  C  CG    . GLN A 1 2654 ? 227.321 204.773 186.865 1.00 17.75 ? 2654 GLN A CG    1 
ATOM   9415  C  CD    . GLN A 1 2654 ? 227.932 203.579 187.570 1.00 25.21 ? 2654 GLN A CD    1 
ATOM   9416  O  OE1   . GLN A 1 2654 ? 229.103 203.256 187.368 1.00 28.95 ? 2654 GLN A OE1   1 
ATOM   9417  N  NE2   . GLN A 1 2654 ? 227.138 202.916 188.402 1.00 16.11 ? 2654 GLN A NE2   1 
ATOM   9418  N  N     . LEU A 1 2655 ? 225.499 206.168 184.073 1.00 10.75 ? 2655 LEU A N     1 
ATOM   9419  C  CA    . LEU A 1 2655 ? 225.214 205.870 182.678 1.00 10.09 ? 2655 LEU A CA    1 
ATOM   9420  C  C     . LEU A 1 2655 ? 225.874 204.565 182.252 1.00 10.44 ? 2655 LEU A C     1 
ATOM   9421  O  O     . LEU A 1 2655 ? 226.935 204.186 182.758 1.00 8.01  ? 2655 LEU A O     1 
ATOM   9422  C  CB    . LEU A 1 2655 ? 225.689 207.004 181.771 1.00 9.12  ? 2655 LEU A CB    1 
ATOM   9423  C  CG    . LEU A 1 2655 ? 225.198 208.427 182.046 1.00 13.10 ? 2655 LEU A CG    1 
ATOM   9424  C  CD1   . LEU A 1 2655 ? 225.388 209.281 180.808 1.00 10.67 ? 2655 LEU A CD1   1 
ATOM   9425  C  CD2   . LEU A 1 2655 ? 223.738 208.441 182.485 1.00 9.63  ? 2655 LEU A CD2   1 
ATOM   9426  N  N     . GLY A 1 2656 ? 225.229 203.877 181.313 1.00 10.44 ? 2656 GLY A N     1 
ATOM   9427  C  CA    . GLY A 1 2656 ? 225.761 202.635 180.796 1.00 6.20  ? 2656 GLY A CA    1 
ATOM   9428  C  C     . GLY A 1 2656 ? 225.630 201.453 181.722 1.00 7.88  ? 2656 GLY A C     1 
ATOM   9429  O  O     . GLY A 1 2656 ? 226.160 200.382 181.414 1.00 16.52 ? 2656 GLY A O     1 
ATOM   9430  N  N     . LYS A 1 2657 ? 224.937 201.609 182.843 1.00 8.93  ? 2657 LYS A N     1 
ATOM   9431  C  CA    . LYS A 1 2657 ? 224.787 200.560 183.837 1.00 5.71  ? 2657 LYS A CA    1 
ATOM   9432  C  C     . LYS A 1 2657 ? 223.327 200.153 183.949 1.00 3.80  ? 2657 LYS A C     1 
ATOM   9433  O  O     . LYS A 1 2657 ? 222.430 201.002 183.922 1.00 4.75  ? 2657 LYS A O     1 
ATOM   9434  C  CB    . LYS A 1 2657 ? 225.296 201.020 185.205 1.00 7.10  ? 2657 LYS A CB    1 
ATOM   9435  C  CG    . LYS A 1 2657 ? 226.764 201.378 185.242 1.00 7.67  ? 2657 LYS A CG    1 
ATOM   9436  C  CD    . LYS A 1 2657 ? 227.620 200.142 185.064 1.00 14.71 ? 2657 LYS A CD    1 
ATOM   9437  C  CE    . LYS A 1 2657 ? 229.098 200.474 185.093 1.00 20.76 ? 2657 LYS A CE    1 
ATOM   9438  N  NZ    . LYS A 1 2657 ? 229.526 200.921 186.444 1.00 23.83 ? 2657 LYS A NZ    1 
ATOM   9439  N  N     . TRP A 1 2658 ? 223.095 198.853 184.068 1.00 5.58  ? 2658 TRP A N     1 
ATOM   9440  C  CA    . TRP A 1 2658 ? 221.779 198.315 184.374 1.00 1.18  ? 2658 TRP A CA    1 
ATOM   9441  C  C     . TRP A 1 2658 ? 221.696 198.130 185.883 1.00 1.98  ? 2658 TRP A C     1 
ATOM   9442  O  O     . TRP A 1 2658 ? 222.538 197.449 186.473 1.00 6.59  ? 2658 TRP A O     1 
ATOM   9443  C  CB    . TRP A 1 2658 ? 221.541 196.994 183.648 1.00 1.52  ? 2658 TRP A CB    1 
ATOM   9444  C  CG    . TRP A 1 2658 ? 220.908 197.164 182.306 1.00 0.32  ? 2658 TRP A CG    1 
ATOM   9445  C  CD1   . TRP A 1 2658 ? 221.521 197.561 181.159 1.00 0.22  ? 2658 TRP A CD1   1 
ATOM   9446  C  CD2   . TRP A 1 2658 ? 219.530 196.957 181.976 1.00 0.29  ? 2658 TRP A CD2   1 
ATOM   9447  N  NE1   . TRP A 1 2658 ? 220.616 197.605 180.130 1.00 0.50  ? 2658 TRP A NE1   1 
ATOM   9448  C  CE2   . TRP A 1 2658 ? 219.385 197.242 180.606 1.00 0.26  ? 2658 TRP A CE2   1 
ATOM   9449  C  CE3   . TRP A 1 2658 ? 218.407 196.556 182.704 1.00 0.25  ? 2658 TRP A CE3   1 
ATOM   9450  C  CZ2   . TRP A 1 2658 ? 218.164 197.138 179.948 1.00 0.18  ? 2658 TRP A CZ2   1 
ATOM   9451  C  CZ3   . TRP A 1 2658 ? 217.197 196.456 182.052 1.00 0.23  ? 2658 TRP A CZ3   1 
ATOM   9452  C  CH2   . TRP A 1 2658 ? 217.083 196.745 180.687 1.00 0.18  ? 2658 TRP A CH2   1 
ATOM   9453  N  N     . LEU A 1 2659 ? 220.696 198.738 186.503 1.00 1.95  ? 2659 LEU A N     1 
ATOM   9454  C  CA    . LEU A 1 2659 ? 220.579 198.736 187.952 1.00 0.93  ? 2659 LEU A CA    1 
ATOM   9455  C  C     . LEU A 1 2659 ? 219.641 197.610 188.367 1.00 0.55  ? 2659 LEU A C     1 
ATOM   9456  O  O     . LEU A 1 2659 ? 218.511 197.522 187.874 1.00 0.73  ? 2659 LEU A O     1 
ATOM   9457  C  CB    . LEU A 1 2659 ? 220.078 200.093 188.443 1.00 0.55  ? 2659 LEU A CB    1 
ATOM   9458  C  CG    . LEU A 1 2659 ? 220.039 200.428 189.933 1.00 2.72  ? 2659 LEU A CG    1 
ATOM   9459  C  CD1   . LEU A 1 2659 ? 220.155 201.924 190.071 1.00 9.10  ? 2659 LEU A CD1   1 
ATOM   9460  C  CD2   . LEU A 1 2659 ? 218.791 199.952 190.604 1.00 2.40  ? 2659 LEU A CD2   1 
ATOM   9461  N  N     . VAL A 1 2660 ? 220.111 196.751 189.266 1.00 0.68  ? 2660 VAL A N     1 
ATOM   9462  C  CA    . VAL A 1 2660 ? 219.392 195.550 189.675 1.00 0.36  ? 2660 VAL A CA    1 
ATOM   9463  C  C     . VAL A 1 2660 ? 218.830 195.780 191.069 1.00 0.36  ? 2660 VAL A C     1 
ATOM   9464  O  O     . VAL A 1 2660 ? 219.589 195.984 192.024 1.00 0.56  ? 2660 VAL A O     1 
ATOM   9465  C  CB    . VAL A 1 2660 ? 220.302 194.311 189.650 1.00 0.47  ? 2660 VAL A CB    1 
ATOM   9466  C  CG1   . VAL A 1 2660 ? 219.497 193.048 189.902 1.00 0.31  ? 2660 VAL A CG1   1 
ATOM   9467  C  CG2   . VAL A 1 2660 ? 221.045 194.224 188.330 1.00 0.36  ? 2660 VAL A CG2   1 
ATOM   9468  N  N     . LEU A 1 2661 ? 217.505 195.743 191.191 1.00 0.54  ? 2661 LEU A N     1 
ATOM   9469  C  CA    . LEU A 1 2661 ? 216.847 195.811 192.492 1.00 0.33  ? 2661 LEU A CA    1 
ATOM   9470  C  C     . LEU A 1 2661 ? 216.730 194.396 193.038 1.00 0.30  ? 2661 LEU A C     1 
ATOM   9471  O  O     . LEU A 1 2661 ? 215.960 193.584 192.516 1.00 0.26  ? 2661 LEU A O     1 
ATOM   9472  C  CB    . LEU A 1 2661 ? 215.468 196.461 192.403 1.00 0.72  ? 2661 LEU A CB    1 
ATOM   9473  C  CG    . LEU A 1 2661 ? 215.339 197.980 192.282 1.00 0.79  ? 2661 LEU A CG    1 
ATOM   9474  C  CD1   . LEU A 1 2661 ? 215.766 198.440 190.920 1.00 2.69  ? 2661 LEU A CD1   1 
ATOM   9475  C  CD2   . LEU A 1 2661 ? 213.926 198.436 192.573 1.00 1.65  ? 2661 LEU A CD2   1 
ATOM   9476  N  N     . PHE A 1 2662 ? 217.486 194.102 194.088 1.00 0.49  ? 2662 PHE A N     1 
ATOM   9477  C  CA    . PHE A 1 2662 ? 217.457 192.798 194.730 1.00 0.34  ? 2662 PHE A CA    1 
ATOM   9478  C  C     . PHE A 1 2662 ? 216.540 192.862 195.946 1.00 0.47  ? 2662 PHE A C     1 
ATOM   9479  O  O     . PHE A 1 2662 ? 216.821 193.591 196.903 1.00 0.91  ? 2662 PHE A O     1 
ATOM   9480  C  CB    . PHE A 1 2662 ? 218.864 192.359 195.131 1.00 0.44  ? 2662 PHE A CB    1 
ATOM   9481  C  CG    . PHE A 1 2662 ? 218.906 191.033 195.828 1.00 1.06  ? 2662 PHE A CG    1 
ATOM   9482  C  CD1   . PHE A 1 2662 ? 218.049 190.012 195.457 1.00 1.09  ? 2662 PHE A CD1   1 
ATOM   9483  C  CD2   . PHE A 1 2662 ? 219.802 190.809 196.859 1.00 1.03  ? 2662 PHE A CD2   1 
ATOM   9484  C  CE1   . PHE A 1 2662 ? 218.086 188.797 196.097 1.00 0.94  ? 2662 PHE A CE1   1 
ATOM   9485  C  CE2   . PHE A 1 2662 ? 219.844 189.593 197.503 1.00 1.66  ? 2662 PHE A CE2   1 
ATOM   9486  C  CZ    . PHE A 1 2662 ? 218.987 188.585 197.123 1.00 1.73  ? 2662 PHE A CZ    1 
ATOM   9487  N  N     . CYS A 1 2663 ? 215.450 192.102 195.903 1.00 0.52  ? 2663 CYS A N     1 
ATOM   9488  C  CA    . CYS A 1 2663 ? 214.486 192.022 196.994 1.00 0.68  ? 2663 CYS A CA    1 
ATOM   9489  C  C     . CYS A 1 2663 ? 214.630 190.665 197.670 1.00 1.10  ? 2663 CYS A C     1 
ATOM   9490  O  O     . CYS A 1 2663 ? 214.376 189.629 197.049 1.00 0.86  ? 2663 CYS A O     1 
ATOM   9491  C  CB    . CYS A 1 2663 ? 213.064 192.235 196.474 1.00 0.96  ? 2663 CYS A CB    1 
ATOM   9492  S  SG    . CYS A 1 2663 ? 212.890 193.669 195.381 1.00 1.45  ? 2663 CYS A SG    1 
ATOM   9493  N  N     . ASP A 1 2664 ? 215.027 190.677 198.944 1.00 1.35  ? 2664 ASP A N     1 
ATOM   9494  C  CA    . ASP A 1 2664 ? 215.445 189.468 199.646 1.00 1.93  ? 2664 ASP A CA    1 
ATOM   9495  C  C     . ASP A 1 2664 ? 214.292 188.669 200.240 1.00 4.89  ? 2664 ASP A C     1 
ATOM   9496  O  O     . ASP A 1 2664 ? 214.451 187.466 200.477 1.00 5.61  ? 2664 ASP A O     1 
ATOM   9497  C  CB    . ASP A 1 2664 ? 216.424 189.830 200.767 1.00 3.05  ? 2664 ASP A CB    1 
ATOM   9498  C  CG    . ASP A 1 2664 ? 217.234 188.641 201.245 1.00 12.28 ? 2664 ASP A CG    1 
ATOM   9499  O  OD1   . ASP A 1 2664 ? 217.165 187.570 200.607 1.00 13.81 ? 2664 ASP A OD1   1 
ATOM   9500  O  OD2   . ASP A 1 2664 ? 217.941 188.777 202.265 1.00 16.96 ? 2664 ASP A OD2   1 
ATOM   9501  N  N     . GLU A 1 2665 ? 213.153 189.296 200.502 1.00 1.16  ? 2665 GLU A N     1 
ATOM   9502  C  CA    . GLU A 1 2665 ? 212.015 188.640 201.140 1.00 0.85  ? 2665 GLU A CA    1 
ATOM   9503  C  C     . GLU A 1 2665 ? 210.728 188.984 200.405 1.00 1.24  ? 2665 GLU A C     1 
ATOM   9504  O  O     . GLU A 1 2665 ? 209.728 189.394 200.997 1.00 1.39  ? 2665 GLU A O     1 
ATOM   9505  C  CB    . GLU A 1 2665 ? 211.928 189.028 202.612 1.00 1.32  ? 2665 GLU A CB    1 
ATOM   9506  C  CG    . GLU A 1 2665 ? 213.189 188.758 203.422 1.00 1.77  ? 2665 GLU A CG    1 
ATOM   9507  C  CD    . GLU A 1 2665 ? 213.388 187.284 203.737 1.00 3.67  ? 2665 GLU A CD    1 
ATOM   9508  O  OE1   . GLU A 1 2665 ? 212.486 186.476 203.439 1.00 5.49  ? 2665 GLU A OE1   1 
ATOM   9509  O  OE2   . GLU A 1 2665 ? 214.453 186.932 204.285 1.00 7.07  ? 2665 GLU A OE2   1 
ATOM   9510  N  N     . ILE A 1 2666 ? 210.751 188.811 199.081 1.00 0.72  ? 2666 ILE A N     1 
ATOM   9511  C  CA    . ILE A 1 2666 ? 209.723 189.359 198.203 1.00 0.35  ? 2666 ILE A CA    1 
ATOM   9512  C  C     . ILE A 1 2666 ? 208.321 188.838 198.509 1.00 0.32  ? 2666 ILE A C     1 
ATOM   9513  O  O     . ILE A 1 2666 ? 207.338 189.439 198.068 1.00 0.33  ? 2666 ILE A O     1 
ATOM   9514  C  CB    . ILE A 1 2666 ? 210.113 189.087 196.732 1.00 0.31  ? 2666 ILE A CB    1 
ATOM   9515  C  CG1   . ILE A 1 2666 ? 209.413 190.073 195.792 1.00 0.16  ? 2666 ILE A CG1   1 
ATOM   9516  C  CG2   . ILE A 1 2666 ? 209.825 187.642 196.351 1.00 0.17  ? 2666 ILE A CG2   1 
ATOM   9517  C  CD1   . ILE A 1 2666 ? 210.048 190.167 194.426 1.00 0.19  ? 2666 ILE A CD1   1 
ATOM   9518  N  N     . ASN A 1 2667 ? 208.191 187.748 199.262 1.00 0.68  ? 2667 ASN A N     1 
ATOM   9519  C  CA    . ASN A 1 2667 ? 206.879 187.179 199.542 1.00 0.41  ? 2667 ASN A CA    1 
ATOM   9520  C  C     . ASN A 1 2667 ? 206.435 187.367 200.993 1.00 0.51  ? 2667 ASN A C     1 
ATOM   9521  O  O     . ASN A 1 2667 ? 205.414 186.800 201.390 1.00 0.75  ? 2667 ASN A O     1 
ATOM   9522  C  CB    . ASN A 1 2667 ? 206.857 185.697 199.155 1.00 0.22  ? 2667 ASN A CB    1 
ATOM   9523  C  CG    . ASN A 1 2667 ? 207.808 184.862 199.976 1.00 0.63  ? 2667 ASN A CG    1 
ATOM   9524  O  OD1   . ASN A 1 2667 ? 208.825 185.351 200.460 1.00 4.61  ? 2667 ASN A OD1   1 
ATOM   9525  N  ND2   . ASN A 1 2667 ? 207.509 183.578 200.092 1.00 0.36  ? 2667 ASN A ND2   1 
ATOM   9526  N  N     . LEU A 1 2668 ? 207.181 188.132 201.793 1.00 0.58  ? 2668 LEU A N     1 
ATOM   9527  C  CA    . LEU A 1 2668 ? 206.719 188.574 203.110 1.00 0.77  ? 2668 LEU A CA    1 
ATOM   9528  C  C     . LEU A 1 2668 ? 205.682 189.695 203.156 1.00 0.46  ? 2668 LEU A C     1 
ATOM   9529  O  O     . LEU A 1 2668 ? 204.906 189.726 204.119 1.00 0.64  ? 2668 LEU A O     1 
ATOM   9530  C  CB    . LEU A 1 2668 ? 207.888 188.988 204.008 1.00 1.09  ? 2668 LEU A CB    1 
ATOM   9531  C  CG    . LEU A 1 2668 ? 208.781 187.843 204.469 1.00 2.36  ? 2668 LEU A CG    1 
ATOM   9532  C  CD1   . LEU A 1 2668 ? 209.951 188.366 205.273 1.00 3.81  ? 2668 LEU A CD1   1 
ATOM   9533  C  CD2   . LEU A 1 2668 ? 207.941 186.897 205.296 1.00 4.10  ? 2668 LEU A CD2   1 
ATOM   9534  N  N     . PRO A 1 2669 ? 205.644 190.652 202.218 1.00 0.71  ? 2669 PRO A N     1 
ATOM   9535  C  CA    . PRO A 1 2669 ? 204.725 191.786 202.387 1.00 0.73  ? 2669 PRO A CA    1 
ATOM   9536  C  C     . PRO A 1 2669 ? 203.291 191.336 202.628 1.00 0.61  ? 2669 PRO A C     1 
ATOM   9537  O  O     . PRO A 1 2669 ? 202.823 190.355 202.047 1.00 0.88  ? 2669 PRO A O     1 
ATOM   9538  C  CB    . PRO A 1 2669 ? 204.861 192.549 201.068 1.00 0.34  ? 2669 PRO A CB    1 
ATOM   9539  C  CG    . PRO A 1 2669 ? 206.230 192.257 200.635 1.00 0.38  ? 2669 PRO A CG    1 
ATOM   9540  C  CD    . PRO A 1 2669 ? 206.480 190.837 201.017 1.00 0.44  ? 2669 PRO A CD    1 
ATOM   9541  N  N     . ASP A 1 2670 ? 202.611 192.057 203.518 1.00 1.01  ? 2670 ASP A N     1 
ATOM   9542  C  CA    . ASP A 1 2670 ? 201.289 191.653 203.980 1.00 1.61  ? 2670 ASP A CA    1 
ATOM   9543  C  C     . ASP A 1 2670 ? 200.315 191.500 202.822 1.00 2.53  ? 2670 ASP A C     1 
ATOM   9544  O  O     . ASP A 1 2670 ? 200.213 192.369 201.952 1.00 1.75  ? 2670 ASP A O     1 
ATOM   9545  C  CB    . ASP A 1 2670 ? 200.739 192.671 204.981 1.00 1.28  ? 2670 ASP A CB    1 
ATOM   9546  C  CG    . ASP A 1 2670 ? 201.362 192.540 206.355 1.00 7.82  ? 2670 ASP A CG    1 
ATOM   9547  O  OD1   . ASP A 1 2670 ? 201.464 193.566 207.060 1.00 6.86  ? 2670 ASP A OD1   1 
ATOM   9548  O  OD2   . ASP A 1 2670 ? 201.741 191.414 206.737 1.00 11.92 ? 2670 ASP A OD2   1 
ATOM   9549  N  N     . MET A 1 2671 ? 199.599 190.384 202.822 1.00 1.69  ? 2671 MET A N     1 
ATOM   9550  C  CA    . MET A 1 2671 ? 198.481 190.172 201.921 1.00 1.03  ? 2671 MET A CA    1 
ATOM   9551  C  C     . MET A 1 2671 ? 197.218 190.700 202.585 1.00 2.23  ? 2671 MET A C     1 
ATOM   9552  O  O     . MET A 1 2671 ? 196.905 190.322 203.718 1.00 6.83  ? 2671 MET A O     1 
ATOM   9553  C  CB    . MET A 1 2671 ? 198.335 188.685 201.595 1.00 1.81  ? 2671 MET A CB    1 
ATOM   9554  C  CG    . MET A 1 2671 ? 197.275 188.372 200.565 1.00 1.79  ? 2671 MET A CG    1 
ATOM   9555  S  SD    . MET A 1 2671 ? 197.643 186.896 199.601 1.00 20.88 ? 2671 MET A SD    1 
ATOM   9556  C  CE    . MET A 1 2671 ? 199.036 187.454 198.629 1.00 0.98  ? 2671 MET A CE    1 
ATOM   9557  N  N     . ASP A 1 2672 ? 196.504 191.583 201.892 1.00 1.12  ? 2672 ASP A N     1 
ATOM   9558  C  CA    . ASP A 1 2672 ? 195.276 192.130 202.444 1.00 1.26  ? 2672 ASP A CA    1 
ATOM   9559  C  C     . ASP A 1 2672 ? 194.186 191.056 202.468 1.00 1.83  ? 2672 ASP A C     1 
ATOM   9560  O  O     . ASP A 1 2672 ? 194.383 189.916 202.038 1.00 1.38  ? 2672 ASP A O     1 
ATOM   9561  C  CB    . ASP A 1 2672 ? 194.843 193.370 201.661 1.00 1.73  ? 2672 ASP A CB    1 
ATOM   9562  C  CG    . ASP A 1 2672 ? 194.481 193.071 200.210 1.00 1.52  ? 2672 ASP A CG    1 
ATOM   9563  O  OD1   . ASP A 1 2672 ? 194.564 191.906 199.772 1.00 1.77  ? 2672 ASP A OD1   1 
ATOM   9564  O  OD2   . ASP A 1 2672 ? 194.105 194.023 199.500 1.00 3.18  ? 2672 ASP A OD2   1 
ATOM   9565  N  N     . LYS A 1 2673 ? 193.010 191.429 202.977 1.00 2.05  ? 2673 LYS A N     1 
ATOM   9566  C  CA    . LYS A 1 2673 ? 191.917 190.471 203.089 1.00 2.98  ? 2673 LYS A CA    1 
ATOM   9567  C  C     . LYS A 1 2673 ? 191.376 190.036 201.734 1.00 1.78  ? 2673 LYS A C     1 
ATOM   9568  O  O     . LYS A 1 2673 ? 190.599 189.078 201.675 1.00 3.93  ? 2673 LYS A O     1 
ATOM   9569  C  CB    . LYS A 1 2673 ? 190.787 191.053 203.943 1.00 2.26  ? 2673 LYS A CB    1 
ATOM   9570  C  CG    . LYS A 1 2673 ? 190.221 192.356 203.423 1.00 3.16  ? 2673 LYS A CG    1 
ATOM   9571  C  CD    . LYS A 1 2673 ? 188.988 192.781 204.200 1.00 5.38  ? 2673 LYS A CD    1 
ATOM   9572  C  CE    . LYS A 1 2673 ? 189.331 193.201 205.614 1.00 12.42 ? 2673 LYS A CE    1 
ATOM   9573  N  NZ    . LYS A 1 2673 ? 188.158 193.800 206.304 1.00 15.90 ? 2673 LYS A NZ    1 
ATOM   9574  N  N     . TYR A 1 2674 ? 191.767 190.706 200.651 1.00 1.99  ? 2674 TYR A N     1 
ATOM   9575  C  CA    . TYR A 1 2674 ? 191.332 190.356 199.307 1.00 1.19  ? 2674 TYR A CA    1 
ATOM   9576  C  C     . TYR A 1 2674 ? 192.443 189.716 198.482 1.00 1.85  ? 2674 TYR A C     1 
ATOM   9577  O  O     . TYR A 1 2674 ? 192.394 189.751 197.249 1.00 2.17  ? 2674 TYR A O     1 
ATOM   9578  C  CB    . TYR A 1 2674 ? 190.776 191.591 198.603 1.00 1.21  ? 2674 TYR A CB    1 
ATOM   9579  C  CG    . TYR A 1 2674 ? 189.827 192.386 199.467 1.00 1.95  ? 2674 TYR A CG    1 
ATOM   9580  C  CD1   . TYR A 1 2674 ? 188.577 191.883 199.802 1.00 1.88  ? 2674 TYR A CD1   1 
ATOM   9581  C  CD2   . TYR A 1 2674 ? 190.181 193.636 199.954 1.00 1.41  ? 2674 TYR A CD2   1 
ATOM   9582  C  CE1   . TYR A 1 2674 ? 187.707 192.603 200.592 1.00 1.28  ? 2674 TYR A CE1   1 
ATOM   9583  C  CE2   . TYR A 1 2674 ? 189.314 194.365 200.742 1.00 1.87  ? 2674 TYR A CE2   1 
ATOM   9584  C  CZ    . TYR A 1 2674 ? 188.079 193.843 201.059 1.00 1.59  ? 2674 TYR A CZ    1 
ATOM   9585  O  OH    . TYR A 1 2674 ? 187.215 194.564 201.846 1.00 5.23  ? 2674 TYR A OH    1 
ATOM   9586  N  N     . GLY A 1 2675 ? 193.447 189.141 199.138 1.00 2.97  ? 2675 GLY A N     1 
ATOM   9587  C  CA    . GLY A 1 2675 ? 194.454 188.350 198.454 1.00 1.99  ? 2675 GLY A CA    1 
ATOM   9588  C  C     . GLY A 1 2675 ? 195.437 189.121 197.602 1.00 1.45  ? 2675 GLY A C     1 
ATOM   9589  O  O     . GLY A 1 2675 ? 195.972 188.565 196.640 1.00 1.28  ? 2675 GLY A O     1 
ATOM   9590  N  N     . THR A 1 2676 ? 195.709 190.379 197.936 1.00 1.38  ? 2676 THR A N     1 
ATOM   9591  C  CA    . THR A 1 2676 ? 196.583 191.226 197.135 1.00 1.03  ? 2676 THR A CA    1 
ATOM   9592  C  C     . THR A 1 2676 ? 197.722 191.770 197.985 1.00 0.53  ? 2676 THR A C     1 
ATOM   9593  O  O     . THR A 1 2676 ? 197.497 192.256 199.097 1.00 0.53  ? 2676 THR A O     1 
ATOM   9594  C  CB    . THR A 1 2676 ? 195.801 192.387 196.511 1.00 1.10  ? 2676 THR A CB    1 
ATOM   9595  O  OG1   . THR A 1 2676 ? 194.745 191.870 195.694 1.00 1.52  ? 2676 THR A OG1   1 
ATOM   9596  C  CG2   . THR A 1 2676 ? 196.716 193.254 195.658 1.00 0.84  ? 2676 THR A CG2   1 
ATOM   9597  N  N     . GLN A 1 2677 ? 198.940 191.682 197.458 1.00 0.91  ? 2677 GLN A N     1 
ATOM   9598  C  CA    . GLN A 1 2677 ? 200.095 192.379 198.008 1.00 0.43  ? 2677 GLN A CA    1 
ATOM   9599  C  C     . GLN A 1 2677 ? 200.376 193.591 197.127 1.00 0.32  ? 2677 GLN A C     1 
ATOM   9600  O  O     . GLN A 1 2677 ? 200.614 193.442 195.924 1.00 0.91  ? 2677 GLN A O     1 
ATOM   9601  C  CB    . GLN A 1 2677 ? 201.315 191.461 198.072 1.00 0.20  ? 2677 GLN A CB    1 
ATOM   9602  C  CG    . GLN A 1 2677 ? 201.209 190.341 199.092 1.00 0.22  ? 2677 GLN A CG    1 
ATOM   9603  C  CD    . GLN A 1 2677 ? 202.232 189.246 198.859 1.00 0.42  ? 2677 GLN A CD    1 
ATOM   9604  O  OE1   . GLN A 1 2677 ? 202.173 188.529 197.863 1.00 0.59  ? 2677 GLN A OE1   1 
ATOM   9605  N  NE2   . GLN A 1 2677 ? 203.180 189.116 199.779 1.00 0.35  ? 2677 GLN A NE2   1 
ATOM   9606  N  N     . ARG A 1 2678 ? 200.340 194.783 197.725 1.00 0.09  ? 2678 ARG A N     1 
ATOM   9607  C  CA    . ARG A 1 2678 ? 200.433 196.009 196.937 1.00 0.09  ? 2678 ARG A CA    1 
ATOM   9608  C  C     . ARG A 1 2678 ? 201.775 196.117 196.220 1.00 0.12  ? 2678 ARG A C     1 
ATOM   9609  O  O     . ARG A 1 2678 ? 201.826 196.486 195.042 1.00 0.11  ? 2678 ARG A O     1 
ATOM   9610  C  CB    . ARG A 1 2678 ? 200.203 197.230 197.827 1.00 0.19  ? 2678 ARG A CB    1 
ATOM   9611  C  CG    . ARG A 1 2678 ? 200.284 198.551 197.079 1.00 0.28  ? 2678 ARG A CG    1 
ATOM   9612  C  CD    . ARG A 1 2678 ? 200.036 199.738 197.990 1.00 0.60  ? 2678 ARG A CD    1 
ATOM   9613  N  NE    . ARG A 1 2678 ? 198.700 199.724 198.572 1.00 2.15  ? 2678 ARG A NE    1 
ATOM   9614  C  CZ    . ARG A 1 2678 ? 198.264 200.605 199.461 1.00 2.06  ? 2678 ARG A CZ    1 
ATOM   9615  N  NH1   . ARG A 1 2678 ? 199.035 201.586 199.898 1.00 1.71  ? 2678 ARG A NH1   1 
ATOM   9616  N  NH2   . ARG A 1 2678 ? 197.023 200.497 199.926 1.00 3.34  ? 2678 ARG A NH2   1 
ATOM   9617  N  N     . VAL A 1 2679 ? 202.870 195.799 196.911 1.00 0.12  ? 2679 VAL A N     1 
ATOM   9618  C  CA    . VAL A 1 2679 ? 204.189 195.925 196.298 1.00 0.14  ? 2679 VAL A CA    1 
ATOM   9619  C  C     . VAL A 1 2679 ? 204.354 194.916 195.164 1.00 0.05  ? 2679 VAL A C     1 
ATOM   9620  O  O     . VAL A 1 2679 ? 204.996 195.207 194.151 1.00 0.01  ? 2679 VAL A O     1 
ATOM   9621  C  CB    . VAL A 1 2679 ? 205.296 195.797 197.364 1.00 0.16  ? 2679 VAL A CB    1 
ATOM   9622  C  CG1   . VAL A 1 2679 ? 205.394 194.378 197.895 1.00 0.07  ? 2679 VAL A CG1   1 
ATOM   9623  C  CG2   . VAL A 1 2679 ? 206.634 196.254 196.803 1.00 0.04  ? 2679 VAL A CG2   1 
ATOM   9624  N  N     . ILE A 1 2680 ? 203.770 193.724 195.309 1.00 0.03  ? 2680 ILE A N     1 
ATOM   9625  C  CA    . ILE A 1 2680 ? 203.848 192.729 194.245 1.00 0.04  ? 2680 ILE A CA    1 
ATOM   9626  C  C     . ILE A 1 2680 ? 203.107 193.211 193.004 1.00 0.03  ? 2680 ILE A C     1 
ATOM   9627  O  O     . ILE A 1 2680 ? 203.597 193.068 191.879 1.00 0.05  ? 2680 ILE A O     1 
ATOM   9628  C  CB    . ILE A 1 2680 ? 203.316 191.371 194.740 1.00 0.08  ? 2680 ILE A CB    1 
ATOM   9629  C  CG1   . ILE A 1 2680 ? 204.116 190.901 195.956 1.00 0.05  ? 2680 ILE A CG1   1 
ATOM   9630  C  CG2   . ILE A 1 2680 ? 203.378 190.333 193.630 1.00 0.02  ? 2680 ILE A CG2   1 
ATOM   9631  C  CD1   . ILE A 1 2680 ? 205.594 190.788 195.702 1.00 0.07  ? 2680 ILE A CD1   1 
ATOM   9632  N  N     . SER A 1 2681 ? 201.921 193.796 193.188 1.00 0.04  ? 2681 SER A N     1 
ATOM   9633  C  CA    . SER A 1 2681 ? 201.217 194.399 192.062 1.00 0.07  ? 2681 SER A CA    1 
ATOM   9634  C  C     . SER A 1 2681 ? 202.040 195.522 191.447 1.00 0.03  ? 2681 SER A C     1 
ATOM   9635  O  O     . SER A 1 2681 ? 202.050 195.699 190.224 1.00 0.10  ? 2681 SER A O     1 
ATOM   9636  C  CB    . SER A 1 2681 ? 199.851 194.921 192.508 1.00 0.11  ? 2681 SER A CB    1 
ATOM   9637  O  OG    . SER A 1 2681 ? 199.019 193.872 192.960 1.00 0.41  ? 2681 SER A OG    1 
ATOM   9638  N  N     . PHE A 1 2682 ? 202.735 196.290 192.285 1.00 0.04  ? 2682 PHE A N     1 
ATOM   9639  C  CA    . PHE A 1 2682 ? 203.589 197.360 191.786 1.00 0.02  ? 2682 PHE A CA    1 
ATOM   9640  C  C     . PHE A 1 2682 ? 204.748 196.809 190.964 1.00 0.05  ? 2682 PHE A C     1 
ATOM   9641  O  O     . PHE A 1 2682 ? 205.091 197.364 189.913 1.00 0.03  ? 2682 PHE A O     1 
ATOM   9642  C  CB    . PHE A 1 2682 ? 204.097 198.199 192.959 1.00 0.04  ? 2682 PHE A CB    1 
ATOM   9643  C  CG    . PHE A 1 2682 ? 204.834 199.434 192.550 1.00 0.05  ? 2682 PHE A CG    1 
ATOM   9644  C  CD1   . PHE A 1 2682 ? 204.149 200.560 192.133 1.00 0.06  ? 2682 PHE A CD1   1 
ATOM   9645  C  CD2   . PHE A 1 2682 ? 206.214 199.481 192.603 1.00 0.09  ? 2682 PHE A CD2   1 
ATOM   9646  C  CE1   . PHE A 1 2682 ? 204.827 201.701 191.763 1.00 0.08  ? 2682 PHE A CE1   1 
ATOM   9647  C  CE2   . PHE A 1 2682 ? 206.896 200.622 192.233 1.00 0.05  ? 2682 PHE A CE2   1 
ATOM   9648  C  CZ    . PHE A 1 2682 ? 206.202 201.731 191.814 1.00 0.03  ? 2682 PHE A CZ    1 
ATOM   9649  N  N     . ILE A 1 2683 ? 205.340 195.707 191.411 1.00 0.02  ? 2683 ILE A N     1 
ATOM   9650  C  CA    . ILE A 1 2683 ? 206.476 195.105 190.654 1.00 0.03  ? 2683 ILE A CA    1 
ATOM   9651  C  C     . ILE A 1 2683 ? 205.931 194.498 189.351 1.00 0.05  ? 2683 ILE A C     1 
ATOM   9652  O  O     . ILE A 1 2683 ? 206.605 194.636 188.311 1.00 0.01  ? 2683 ILE A O     1 
ATOM   9653  C  CB    . ILE A 1 2683 ? 207.260 194.090 191.507 1.00 0.02  ? 2683 ILE A CB    1 
ATOM   9654  C  CG1   . ILE A 1 2683 ? 207.806 194.738 192.781 1.00 0.02  ? 2683 ILE A CG1   1 
ATOM   9655  C  CG2   . ILE A 1 2683 ? 208.369 193.428 190.690 1.00 0.01  ? 2683 ILE A CG2   1 
ATOM   9656  C  CD1   . ILE A 1 2683 ? 208.474 193.769 193.738 1.00 0.02  ? 2683 ILE A CD1   1 
ATOM   9657  N  N     . ARG A 1 2684 ? 204.751 193.877 189.409 1.00 0.01  ? 2684 ARG A N     1 
ATOM   9658  C  CA    . ARG A 1 2684 ? 204.147 193.254 188.203 1.00 0.03  ? 2684 ARG A CA    1 
ATOM   9659  C  C     . ARG A 1 2684 ? 203.914 194.359 187.166 1.00 0.06  ? 2684 ARG A C     1 
ATOM   9660  O  O     . ARG A 1 2684 ? 204.211 194.129 185.976 1.00 0.06  ? 2684 ARG A O     1 
ATOM   9661  C  CB    . ARG A 1 2684 ? 202.849 192.516 188.551 1.00 0.07  ? 2684 ARG A CB    1 
ATOM   9662  C  CG    . ARG A 1 2684 ? 202.202 191.809 187.368 1.00 0.08  ? 2684 ARG A CG    1 
ATOM   9663  C  CD    . ARG A 1 2684 ? 200.743 192.201 187.214 1.00 0.10  ? 2684 ARG A CD    1 
ATOM   9664  N  NE    . ARG A 1 2684 ? 200.147 191.703 185.970 1.00 2.79  ? 2684 ARG A NE    1 
ATOM   9665  C  CZ    . ARG A 1 2684 ? 198.903 191.944 185.575 1.00 0.38  ? 2684 ARG A CZ    1 
ATOM   9666  N  NH1   . ARG A 1 2684 ? 198.115 192.716 186.299 1.00 0.19  ? 2684 ARG A NH1   1 
ATOM   9667  N  NH2   . ARG A 1 2684 ? 198.454 191.411 184.453 1.00 0.13  ? 2684 ARG A NH2   1 
ATOM   9668  N  N     . GLN A 1 2685 ? 203.425 195.513 187.614 1.00 0.04  ? 2685 GLN A N     1 
ATOM   9669  C  CA    . GLN A 1 2685 ? 203.195 196.658 186.699 1.00 0.05  ? 2685 GLN A CA    1 
ATOM   9670  C  C     . GLN A 1 2685 ? 204.530 197.067 186.058 1.00 0.10  ? 2685 GLN A C     1 
ATOM   9671  O  O     . GLN A 1 2685 ? 204.557 197.236 184.823 1.00 0.25  ? 2685 GLN A O     1 
ATOM   9672  C  CB    . GLN A 1 2685 ? 202.523 197.793 187.473 1.00 0.06  ? 2685 GLN A CB    1 
ATOM   9673  C  CG    . GLN A 1 2685 ? 202.297 199.068 186.667 1.00 0.05  ? 2685 GLN A CG    1 
ATOM   9674  C  CD    . GLN A 1 2685 ? 201.695 200.180 187.497 1.00 0.07  ? 2685 GLN A CD    1 
ATOM   9675  O  OE1   . GLN A 1 2685 ? 202.262 200.608 188.508 1.00 0.19  ? 2685 GLN A OE1   1 
ATOM   9676  N  NE2   . GLN A 1 2685 ? 200.530 200.654 187.082 1.00 0.07  ? 2685 GLN A NE2   1 
ATOM   9677  N  N     . MET A 1 2686 ? 205.597 197.196 186.851 1.00 0.10  ? 2686 MET A N     1 
ATOM   9678  C  CA    . MET A 1 2686 ? 206.860 197.666 186.288 1.00 0.23  ? 2686 MET A CA    1 
ATOM   9679  C  C     . MET A 1 2686 ? 207.475 196.655 185.329 1.00 0.37  ? 2686 MET A C     1 
ATOM   9680  O  O     . MET A 1 2686 ? 208.249 197.037 184.445 1.00 4.68  ? 2686 MET A O     1 
ATOM   9681  C  CB    . MET A 1 2686 ? 207.869 198.001 187.386 1.00 0.31  ? 2686 MET A CB    1 
ATOM   9682  C  CG    . MET A 1 2686 ? 207.532 199.224 188.204 1.00 0.24  ? 2686 MET A CG    1 
ATOM   9683  S  SD    . MET A 1 2686 ? 208.759 199.484 189.493 1.00 11.49 ? 2686 MET A SD    1 
ATOM   9684  C  CE    . MET A 1 2686 ? 208.492 198.049 190.518 1.00 0.07  ? 2686 MET A CE    1 
ATOM   9685  N  N     . VAL A 1 2687 ? 207.163 195.372 185.484 1.00 0.41  ? 2687 VAL A N     1 
ATOM   9686  C  CA    . VAL A 1 2687 ? 207.754 194.373 184.603 1.00 0.79  ? 2687 VAL A CA    1 
ATOM   9687  C  C     . VAL A 1 2687 ? 206.946 194.235 183.320 1.00 0.94  ? 2687 VAL A C     1 
ATOM   9688  O  O     . VAL A 1 2687 ? 207.500 194.312 182.217 1.00 6.75  ? 2687 VAL A O     1 
ATOM   9689  C  CB    . VAL A 1 2687 ? 207.886 193.031 185.343 1.00 2.02  ? 2687 VAL A CB    1 
ATOM   9690  C  CG1   . VAL A 1 2687 ? 208.222 191.928 184.361 1.00 1.68  ? 2687 VAL A CG1   1 
ATOM   9691  C  CG2   . VAL A 1 2687 ? 208.955 193.136 186.422 1.00 0.26  ? 2687 VAL A CG2   1 
ATOM   9692  N  N     . GLU A 1 2688 ? 205.628 194.049 183.454 1.00 0.88  ? 2688 GLU A N     1 
ATOM   9693  C  CA    . GLU A 1 2688 ? 204.739 193.776 182.329 1.00 0.94  ? 2688 GLU A CA    1 
ATOM   9694  C  C     . GLU A 1 2688 ? 204.413 195.036 181.529 1.00 1.00  ? 2688 GLU A C     1 
ATOM   9695  O  O     . GLU A 1 2688 ? 204.361 194.988 180.295 1.00 1.51  ? 2688 GLU A O     1 
ATOM   9696  C  CB    . GLU A 1 2688 ? 203.482 193.065 182.854 1.00 0.97  ? 2688 GLU A CB    1 
ATOM   9697  C  CG    . GLU A 1 2688 ? 202.542 192.481 181.792 1.00 2.66  ? 2688 GLU A CG    1 
ATOM   9698  C  CD    . GLU A 1 2688 ? 201.596 193.475 181.256 1.00 7.23  ? 2688 GLU A CD    1 
ATOM   9699  O  OE1   . GLU A 1 2688 ? 201.281 194.390 182.035 1.00 15.47 ? 2688 GLU A OE1   1 
ATOM   9700  O  OE2   . GLU A 1 2688 ? 201.162 193.348 180.089 1.00 10.50 ? 2688 GLU A OE2   1 
ATOM   9701  N  N     . HIS A 1 2689 ? 204.187 196.169 182.203 1.00 0.40  ? 2689 HIS A N     1 
ATOM   9702  C  CA    . HIS A 1 2689 ? 203.989 197.463 181.550 1.00 0.33  ? 2689 HIS A CA    1 
ATOM   9703  C  C     . HIS A 1 2689 ? 205.264 198.294 181.425 1.00 0.32  ? 2689 HIS A C     1 
ATOM   9704  O  O     . HIS A 1 2689 ? 205.237 199.342 180.772 1.00 0.40  ? 2689 HIS A O     1 
ATOM   9705  C  CB    . HIS A 1 2689 ? 202.931 198.295 182.295 1.00 0.43  ? 2689 HIS A CB    1 
ATOM   9706  C  CG    . HIS A 1 2689 ? 201.565 197.683 182.292 1.00 0.42  ? 2689 HIS A CG    1 
ATOM   9707  N  ND1   . HIS A 1 2689 ? 201.047 197.040 181.190 1.00 0.47  ? 2689 HIS A ND1   1 
ATOM   9708  C  CD2   . HIS A 1 2689 ? 200.627 197.579 183.261 1.00 1.31  ? 2689 HIS A CD2   1 
ATOM   9709  C  CE1   . HIS A 1 2689 ? 199.839 196.594 181.469 1.00 0.85  ? 2689 HIS A CE1   1 
ATOM   9710  N  NE2   . HIS A 1 2689 ? 199.566 196.896 182.724 1.00 2.15  ? 2689 HIS A NE2   1 
ATOM   9711  N  N     . GLY A 1 2690 ? 206.377 197.864 182.013 1.00 0.44  ? 2690 GLY A N     1 
ATOM   9712  C  CA    . GLY A 1 2690 ? 207.601 198.632 181.864 1.00 0.23  ? 2690 GLY A CA    1 
ATOM   9713  C  C     . GLY A 1 2690 ? 207.623 199.968 182.573 1.00 0.12  ? 2690 GLY A C     1 
ATOM   9714  O  O     . GLY A 1 2690 ? 208.410 200.842 182.199 1.00 0.16  ? 2690 GLY A O     1 
ATOM   9715  N  N     . GLY A 1 2691 ? 206.798 200.153 183.595 1.00 0.22  ? 2691 GLY A N     1 
ATOM   9716  C  CA    . GLY A 1 2691 ? 206.786 201.418 184.300 1.00 0.15  ? 2691 GLY A CA    1 
ATOM   9717  C  C     . GLY A 1 2691 ? 205.735 201.452 185.384 1.00 0.06  ? 2691 GLY A C     1 
ATOM   9718  O  O     . GLY A 1 2691 ? 205.217 200.416 185.805 1.00 0.10  ? 2691 GLY A O     1 
ATOM   9719  N  N     . PHE A 1 2692 ? 205.430 202.665 185.836 1.00 0.04  ? 2692 PHE A N     1 
ATOM   9720  C  CA    . PHE A 1 2692 ? 204.454 202.893 186.890 1.00 0.04  ? 2692 PHE A CA    1 
ATOM   9721  C  C     . PHE A 1 2692 ? 203.960 204.327 186.775 1.00 0.03  ? 2692 PHE A C     1 
ATOM   9722  O  O     . PHE A 1 2692 ? 204.428 205.099 185.934 1.00 0.04  ? 2692 PHE A O     1 
ATOM   9723  C  CB    . PHE A 1 2692 ? 205.053 202.618 188.272 1.00 0.06  ? 2692 PHE A CB    1 
ATOM   9724  C  CG    . PHE A 1 2692 ? 206.156 203.561 188.648 1.00 0.06  ? 2692 PHE A CG    1 
ATOM   9725  C  CD1   . PHE A 1 2692 ? 207.452 203.343 188.214 1.00 0.08  ? 2692 PHE A CD1   1 
ATOM   9726  C  CD2   . PHE A 1 2692 ? 205.895 204.666 189.438 1.00 0.06  ? 2692 PHE A CD2   1 
ATOM   9727  C  CE1   . PHE A 1 2692 ? 208.466 204.210 188.563 1.00 0.15  ? 2692 PHE A CE1   1 
ATOM   9728  C  CE2   . PHE A 1 2692 ? 206.902 205.536 189.787 1.00 0.13  ? 2692 PHE A CE2   1 
ATOM   9729  C  CZ    . PHE A 1 2692 ? 208.189 205.307 189.350 1.00 0.09  ? 2692 PHE A CZ    1 
ATOM   9730  N  N     . TYR A 1 2693 ? 203.012 204.681 187.633 1.00 0.05  ? 2693 TYR A N     1 
ATOM   9731  C  CA    . TYR A 1 2693 ? 202.465 206.029 187.684 1.00 0.09  ? 2693 TYR A CA    1 
ATOM   9732  C  C     . TYR A 1 2693 ? 203.083 206.800 188.842 1.00 0.27  ? 2693 TYR A C     1 
ATOM   9733  O  O     . TYR A 1 2693 ? 203.120 206.309 189.973 1.00 0.25  ? 2693 TYR A O     1 
ATOM   9734  C  CB    . TYR A 1 2693 ? 200.944 206.007 187.832 1.00 0.04  ? 2693 TYR A CB    1 
ATOM   9735  C  CG    . TYR A 1 2693 ? 200.199 205.800 186.537 1.00 0.03  ? 2693 TYR A CG    1 
ATOM   9736  C  CD1   . TYR A 1 2693 ? 200.028 206.844 185.638 1.00 0.03  ? 2693 TYR A CD1   1 
ATOM   9737  C  CD2   . TYR A 1 2693 ? 199.659 204.565 186.217 1.00 0.03  ? 2693 TYR A CD2   1 
ATOM   9738  C  CE1   . TYR A 1 2693 ? 199.346 206.659 184.455 1.00 0.07  ? 2693 TYR A CE1   1 
ATOM   9739  C  CE2   . TYR A 1 2693 ? 198.974 204.370 185.037 1.00 0.04  ? 2693 TYR A CE2   1 
ATOM   9740  C  CZ    . TYR A 1 2693 ? 198.820 205.418 184.160 1.00 0.07  ? 2693 TYR A CZ    1 
ATOM   9741  O  OH    . TYR A 1 2693 ? 198.136 205.220 182.983 1.00 0.05  ? 2693 TYR A OH    1 
ATOM   9742  N  N     . ARG A 1 2694 ? 203.561 208.006 188.553 1.00 0.92  ? 2694 ARG A N     1 
ATOM   9743  C  CA    . ARG A 1 2694 ? 204.026 208.927 189.583 1.00 0.88  ? 2694 ARG A CA    1 
ATOM   9744  C  C     . ARG A 1 2694 ? 202.805 209.616 190.179 1.00 1.35  ? 2694 ARG A C     1 
ATOM   9745  O  O     . ARG A 1 2694 ? 202.126 210.389 189.497 1.00 1.85  ? 2694 ARG A O     1 
ATOM   9746  C  CB    . ARG A 1 2694 ? 205.008 209.935 188.992 1.00 1.10  ? 2694 ARG A CB    1 
ATOM   9747  C  CG    . ARG A 1 2694 ? 205.815 210.707 190.024 1.00 2.23  ? 2694 ARG A CG    1 
ATOM   9748  C  CD    . ARG A 1 2694 ? 206.199 212.090 189.516 1.00 2.14  ? 2694 ARG A CD    1 
ATOM   9749  N  NE    . ARG A 1 2694 ? 207.434 212.097 188.745 1.00 2.52  ? 2694 ARG A NE    1 
ATOM   9750  C  CZ    . ARG A 1 2694 ? 207.613 212.779 187.621 1.00 3.14  ? 2694 ARG A CZ    1 
ATOM   9751  N  NH1   . ARG A 1 2694 ? 206.637 213.488 187.080 1.00 1.74  ? 2694 ARG A NH1   1 
ATOM   9752  N  NH2   . ARG A 1 2694 ? 208.801 212.748 187.027 1.00 4.65  ? 2694 ARG A NH2   1 
ATOM   9753  N  N     . THR A 1 2695 ? 202.517 209.334 191.452 1.00 1.62  ? 2695 THR A N     1 
ATOM   9754  C  CA    . THR A 1 2695 ? 201.261 209.777 192.047 1.00 1.62  ? 2695 THR A CA    1 
ATOM   9755  C  C     . THR A 1 2695 ? 201.216 211.276 192.305 1.00 2.58  ? 2695 THR A C     1 
ATOM   9756  O  O     . THR A 1 2695 ? 200.123 211.824 192.484 1.00 4.22  ? 2695 THR A O     1 
ATOM   9757  C  CB    . THR A 1 2695 ? 200.995 209.022 193.353 1.00 2.11  ? 2695 THR A CB    1 
ATOM   9758  O  OG1   . THR A 1 2695 ? 202.064 209.257 194.278 1.00 10.31 ? 2695 THR A OG1   1 
ATOM   9759  C  CG2   . THR A 1 2695 ? 200.878 207.531 193.089 1.00 1.83  ? 2695 THR A CG2   1 
ATOM   9760  N  N     . SER A 1 2696 ? 202.365 211.952 192.337 1.00 3.44  ? 2696 SER A N     1 
ATOM   9761  C  CA    . SER A 1 2696 ? 202.363 213.389 192.598 1.00 3.29  ? 2696 SER A CA    1 
ATOM   9762  C  C     . SER A 1 2696 ? 201.708 214.165 191.460 1.00 3.61  ? 2696 SER A C     1 
ATOM   9763  O  O     . SER A 1 2696 ? 200.966 215.122 191.704 1.00 9.24  ? 2696 SER A O     1 
ATOM   9764  C  CB    . SER A 1 2696 ? 203.790 213.885 192.835 1.00 7.25  ? 2696 SER A CB    1 
ATOM   9765  O  OG    . SER A 1 2696 ? 204.548 213.855 191.641 1.00 9.77  ? 2696 SER A OG    1 
ATOM   9766  N  N     . ASP A 1 2697 ? 201.972 213.775 190.214 1.00 2.21  ? 2697 ASP A N     1 
ATOM   9767  C  CA    . ASP A 1 2697 ? 201.426 214.474 189.056 1.00 2.10  ? 2697 ASP A CA    1 
ATOM   9768  C  C     . ASP A 1 2697 ? 200.588 213.573 188.158 1.00 1.97  ? 2697 ASP A C     1 
ATOM   9769  O  O     . ASP A 1 2697 ? 200.190 214.006 187.071 1.00 2.94  ? 2697 ASP A O     1 
ATOM   9770  C  CB    . ASP A 1 2697 ? 202.552 215.118 188.241 1.00 4.10  ? 2697 ASP A CB    1 
ATOM   9771  C  CG    . ASP A 1 2697 ? 203.566 214.109 187.745 1.00 6.25  ? 2697 ASP A CG    1 
ATOM   9772  O  OD1   . ASP A 1 2697 ? 203.471 212.926 188.130 1.00 4.07  ? 2697 ASP A OD1   1 
ATOM   9773  O  OD2   . ASP A 1 2697 ? 204.458 214.497 186.964 1.00 12.75 ? 2697 ASP A OD2   1 
ATOM   9774  N  N     . GLN A 1 2698 ? 200.318 212.336 188.579 1.00 2.02  ? 2698 GLN A N     1 
ATOM   9775  C  CA    . GLN A 1 2698 ? 199.486 211.402 187.815 1.00 1.39  ? 2698 GLN A CA    1 
ATOM   9776  C  C     . GLN A 1 2698 ? 200.066 211.145 186.426 1.00 1.43  ? 2698 GLN A C     1 
ATOM   9777  O  O     . GLN A 1 2698 ? 199.339 211.070 185.434 1.00 5.75  ? 2698 GLN A O     1 
ATOM   9778  C  CB    . GLN A 1 2698 ? 198.046 211.908 187.714 1.00 1.20  ? 2698 GLN A CB    1 
ATOM   9779  C  CG    . GLN A 1 2698 ? 197.119 211.395 188.788 1.00 0.33  ? 2698 GLN A CG    1 
ATOM   9780  C  CD    . GLN A 1 2698 ? 197.579 211.744 190.183 1.00 0.74  ? 2698 GLN A CD    1 
ATOM   9781  O  OE1   . GLN A 1 2698 ? 197.757 212.914 190.516 1.00 2.24  ? 2698 GLN A OE1   1 
ATOM   9782  N  NE2   . GLN A 1 2698 ? 197.768 210.727 191.013 1.00 2.37  ? 2698 GLN A NE2   1 
ATOM   9783  N  N     . THR A 1 2699 ? 201.384 211.008 186.355 1.00 1.85  ? 2699 THR A N     1 
ATOM   9784  C  CA    . THR A 1 2699 ? 202.099 210.891 185.091 1.00 0.98  ? 2699 THR A CA    1 
ATOM   9785  C  C     . THR A 1 2699 ? 202.736 209.514 184.993 1.00 0.32  ? 2699 THR A C     1 
ATOM   9786  O  O     . THR A 1 2699 ? 203.332 209.031 185.961 1.00 0.19  ? 2699 THR A O     1 
ATOM   9787  C  CB    . THR A 1 2699 ? 203.167 211.984 184.965 1.00 2.16  ? 2699 THR A CB    1 
ATOM   9788  O  OG1   . THR A 1 2699 ? 202.530 213.257 184.803 1.00 6.33  ? 2699 THR A OG1   1 
ATOM   9789  C  CG2   . THR A 1 2699 ? 204.075 211.726 183.773 1.00 1.71  ? 2699 THR A CG2   1 
ATOM   9790  N  N     . TRP A 1 2700 ? 202.601 208.885 183.830 1.00 0.18  ? 2700 TRP A N     1 
ATOM   9791  C  CA    . TRP A 1 2700 ? 203.240 207.598 183.599 1.00 0.11  ? 2700 TRP A CA    1 
ATOM   9792  C  C     . TRP A 1 2700 ? 204.750 207.768 183.500 1.00 0.13  ? 2700 TRP A C     1 
ATOM   9793  O  O     . TRP A 1 2700 ? 205.245 208.654 182.798 1.00 0.33  ? 2700 TRP A O     1 
ATOM   9794  C  CB    . TRP A 1 2700 ? 202.695 206.949 182.330 1.00 0.07  ? 2700 TRP A CB    1 
ATOM   9795  C  CG    . TRP A 1 2700 ? 203.358 205.651 182.003 1.00 0.06  ? 2700 TRP A CG    1 
ATOM   9796  C  CD1   . TRP A 1 2700 ? 204.323 205.437 181.065 1.00 0.04  ? 2700 TRP A CD1   1 
ATOM   9797  C  CD2   . TRP A 1 2700 ? 203.116 204.384 182.624 1.00 0.04  ? 2700 TRP A CD2   1 
ATOM   9798  N  NE1   . TRP A 1 2700 ? 204.691 204.117 181.058 1.00 0.04  ? 2700 TRP A NE1   1 
ATOM   9799  C  CE2   . TRP A 1 2700 ? 203.965 203.448 182.006 1.00 0.04  ? 2700 TRP A CE2   1 
ATOM   9800  C  CE3   . TRP A 1 2700 ? 202.261 203.950 183.640 1.00 0.02  ? 2700 TRP A CE3   1 
ATOM   9801  C  CZ2   . TRP A 1 2700 ? 203.982 202.103 182.368 1.00 0.08  ? 2700 TRP A CZ2   1 
ATOM   9802  C  CZ3   . TRP A 1 2700 ? 202.281 202.619 183.997 1.00 0.02  ? 2700 TRP A CZ3   1 
ATOM   9803  C  CH2   . TRP A 1 2700 ? 203.135 201.711 183.364 1.00 0.06  ? 2700 TRP A CH2   1 
ATOM   9804  N  N     . VAL A 1 2701 ? 205.481 206.911 184.205 1.00 0.08  ? 2701 VAL A N     1 
ATOM   9805  C  CA    . VAL A 1 2701 ? 206.937 206.909 184.200 1.00 0.21  ? 2701 VAL A CA    1 
ATOM   9806  C  C     . VAL A 1 2701 ? 207.398 205.598 183.583 1.00 0.07  ? 2701 VAL A C     1 
ATOM   9807  O  O     . VAL A 1 2701 ? 206.931 204.526 183.979 1.00 0.08  ? 2701 VAL A O     1 
ATOM   9808  C  CB    . VAL A 1 2701 ? 207.514 207.078 185.618 1.00 0.16  ? 2701 VAL A CB    1 
ATOM   9809  C  CG1   . VAL A 1 2701 ? 209.024 206.921 185.599 1.00 0.13  ? 2701 VAL A CG1   1 
ATOM   9810  C  CG2   . VAL A 1 2701 ? 207.120 208.427 186.195 1.00 0.28  ? 2701 VAL A CG2   1 
ATOM   9811  N  N     . LYS A 1 2702 ? 208.297 205.685 182.612 1.00 0.18  ? 2702 LYS A N     1 
ATOM   9812  C  CA    . LYS A 1 2702 ? 208.844 204.513 181.948 1.00 0.21  ? 2702 LYS A CA    1 
ATOM   9813  C  C     . LYS A 1 2702 ? 210.218 204.181 182.516 1.00 0.29  ? 2702 LYS A C     1 
ATOM   9814  O  O     . LYS A 1 2702 ? 211.071 205.059 182.660 1.00 0.21  ? 2702 LYS A O     1 
ATOM   9815  C  CB    . LYS A 1 2702 ? 208.945 204.735 180.440 1.00 0.36  ? 2702 LYS A CB    1 
ATOM   9816  C  CG    . LYS A 1 2702 ? 209.407 203.515 179.671 1.00 1.67  ? 2702 LYS A CG    1 
ATOM   9817  C  CD    . LYS A 1 2702 ? 209.408 203.770 178.175 1.00 3.22  ? 2702 LYS A CD    1 
ATOM   9818  C  CE    . LYS A 1 2702 ? 209.878 202.547 177.409 1.00 8.16  ? 2702 LYS A CE    1 
ATOM   9819  N  NZ    . LYS A 1 2702 ? 209.887 202.781 175.940 1.00 19.38 ? 2702 LYS A NZ    1 
ATOM   9820  N  N     . LEU A 1 2703 ? 210.420 202.908 182.837 1.00 0.63  ? 2703 LEU A N     1 
ATOM   9821  C  CA    . LEU A 1 2703 ? 211.701 202.445 183.344 1.00 0.28  ? 2703 LEU A CA    1 
ATOM   9822  C  C     . LEU A 1 2703 ? 212.684 202.216 182.205 1.00 0.23  ? 2703 LEU A C     1 
ATOM   9823  O  O     . LEU A 1 2703 ? 212.313 201.794 181.107 1.00 0.94  ? 2703 LEU A O     1 
ATOM   9824  C  CB    . LEU A 1 2703 ? 211.530 201.150 184.138 1.00 0.50  ? 2703 LEU A CB    1 
ATOM   9825  C  CG    . LEU A 1 2703 ? 210.742 201.201 185.444 1.00 0.47  ? 2703 LEU A CG    1 
ATOM   9826  C  CD1   . LEU A 1 2703 ? 210.690 199.819 186.066 1.00 1.86  ? 2703 LEU A CD1   1 
ATOM   9827  C  CD2   . LEU A 1 2703 ? 211.355 202.202 186.410 1.00 0.44  ? 2703 LEU A CD2   1 
ATOM   9828  N  N     . GLU A 1 2704 ? 213.953 202.506 182.477 1.00 0.20  ? 2704 GLU A N     1 
ATOM   9829  C  CA    . GLU A 1 2704 ? 215.031 202.226 181.540 1.00 0.34  ? 2704 GLU A CA    1 
ATOM   9830  C  C     . GLU A 1 2704 ? 216.235 201.728 182.323 1.00 0.39  ? 2704 GLU A C     1 
ATOM   9831  O  O     . GLU A 1 2704 ? 216.619 202.339 183.324 1.00 0.45  ? 2704 GLU A O     1 
ATOM   9832  C  CB    . GLU A 1 2704 ? 215.395 203.467 180.715 1.00 0.97  ? 2704 GLU A CB    1 
ATOM   9833  C  CG    . GLU A 1 2704 ? 216.743 203.379 180.018 1.00 4.59  ? 2704 GLU A CG    1 
ATOM   9834  C  CD    . GLU A 1 2704 ? 217.244 204.726 179.535 1.00 13.76 ? 2704 GLU A CD    1 
ATOM   9835  O  OE1   . GLU A 1 2704 ? 216.568 205.344 178.687 1.00 18.01 ? 2704 GLU A OE1   1 
ATOM   9836  O  OE2   . GLU A 1 2704 ? 218.315 205.167 180.000 1.00 13.85 ? 2704 GLU A OE2   1 
ATOM   9837  N  N     . ARG A 1 2705 ? 216.815 200.615 181.867 1.00 0.36  ? 2705 ARG A N     1 
ATOM   9838  C  CA    . ARG A 1 2705 ? 217.998 200.013 182.488 1.00 0.22  ? 2705 ARG A CA    1 
ATOM   9839  C  C     . ARG A 1 2705 ? 217.769 199.689 183.963 1.00 0.25  ? 2705 ARG A C     1 
ATOM   9840  O  O     . ARG A 1 2705 ? 218.645 199.890 184.805 1.00 0.51  ? 2705 ARG A O     1 
ATOM   9841  C  CB    . ARG A 1 2705 ? 219.232 200.900 182.313 1.00 0.39  ? 2705 ARG A CB    1 
ATOM   9842  C  CG    . ARG A 1 2705 ? 219.691 201.055 180.874 1.00 0.32  ? 2705 ARG A CG    1 
ATOM   9843  C  CD    . ARG A 1 2705 ? 220.882 201.992 180.762 1.00 1.74  ? 2705 ARG A CD    1 
ATOM   9844  N  NE    . ARG A 1 2705 ? 220.567 203.353 181.183 1.00 1.50  ? 2705 ARG A NE    1 
ATOM   9845  C  CZ    . ARG A 1 2705 ? 221.151 203.980 182.193 1.00 2.48  ? 2705 ARG A CZ    1 
ATOM   9846  N  NH1   . ARG A 1 2705 ? 222.075 203.388 182.933 1.00 2.77  ? 2705 ARG A NH1   1 
ATOM   9847  N  NH2   . ARG A 1 2705 ? 220.798 205.230 182.473 1.00 3.85  ? 2705 ARG A NH2   1 
ATOM   9848  N  N     . ILE A 1 2706 ? 216.583 199.178 184.280 1.00 0.18  ? 2706 ILE A N     1 
ATOM   9849  C  CA    . ILE A 1 2706 ? 216.241 198.751 185.632 1.00 0.17  ? 2706 ILE A CA    1 
ATOM   9850  C  C     . ILE A 1 2706 ? 215.630 197.359 185.555 1.00 0.15  ? 2706 ILE A C     1 
ATOM   9851  O  O     . ILE A 1 2706 ? 214.620 197.161 184.871 1.00 0.60  ? 2706 ILE A O     1 
ATOM   9852  C  CB    . ILE A 1 2706 ? 215.279 199.736 186.320 1.00 0.31  ? 2706 ILE A CB    1 
ATOM   9853  C  CG1   . ILE A 1 2706 ? 215.966 201.086 186.544 1.00 0.28  ? 2706 ILE A CG1   1 
ATOM   9854  C  CG2   . ILE A 1 2706 ? 214.754 199.158 187.618 1.00 0.19  ? 2706 ILE A CG2   1 
ATOM   9855  C  CD1   . ILE A 1 2706 ? 215.033 202.192 186.970 1.00 0.43  ? 2706 ILE A CD1   1 
ATOM   9856  N  N     . GLN A 1 2707 ? 216.239 196.401 186.246 1.00 0.26  ? 2707 GLN A N     1 
ATOM   9857  C  CA    . GLN A 1 2707 ? 215.729 195.041 186.324 1.00 0.13  ? 2707 GLN A CA    1 
ATOM   9858  C  C     . GLN A 1 2707 ? 215.572 194.634 187.783 1.00 0.19  ? 2707 GLN A C     1 
ATOM   9859  O  O     . GLN A 1 2707 ? 216.134 195.254 188.689 1.00 0.33  ? 2707 GLN A O     1 
ATOM   9860  C  CB    . GLN A 1 2707 ? 216.642 194.043 185.599 1.00 0.19  ? 2707 GLN A CB    1 
ATOM   9861  C  CG    . GLN A 1 2707 ? 218.112 194.148 185.951 1.00 0.26  ? 2707 GLN A CG    1 
ATOM   9862  C  CD    . GLN A 1 2707 ? 218.981 193.296 185.051 1.00 0.74  ? 2707 GLN A CD    1 
ATOM   9863  O  OE1   . GLN A 1 2707 ? 219.820 193.809 184.313 1.00 6.84  ? 2707 GLN A OE1   1 
ATOM   9864  N  NE2   . GLN A 1 2707 ? 218.785 191.987 185.105 1.00 0.41  ? 2707 GLN A NE2   1 
ATOM   9865  N  N     . PHE A 1 2708 ? 214.800 193.573 188.000 1.00 0.49  ? 2708 PHE A N     1 
ATOM   9866  C  CA    . PHE A 1 2708 ? 214.434 193.127 189.336 1.00 0.10  ? 2708 PHE A CA    1 
ATOM   9867  C  C     . PHE A 1 2708 ? 214.858 191.681 189.550 1.00 0.09  ? 2708 PHE A C     1 
ATOM   9868  O  O     . PHE A 1 2708 ? 214.698 190.837 188.665 1.00 0.14  ? 2708 PHE A O     1 
ATOM   9869  C  CB    . PHE A 1 2708 ? 212.925 193.267 189.561 1.00 0.12  ? 2708 PHE A CB    1 
ATOM   9870  C  CG    . PHE A 1 2708 ? 212.405 194.651 189.312 1.00 0.50  ? 2708 PHE A CG    1 
ATOM   9871  C  CD1   . PHE A 1 2708 ? 211.981 195.030 188.050 1.00 0.50  ? 2708 PHE A CD1   1 
ATOM   9872  C  CD2   . PHE A 1 2708 ? 212.349 195.578 190.338 1.00 0.93  ? 2708 PHE A CD2   1 
ATOM   9873  C  CE1   . PHE A 1 2708 ? 211.509 196.304 187.815 1.00 0.50  ? 2708 PHE A CE1   1 
ATOM   9874  C  CE2   . PHE A 1 2708 ? 211.874 196.854 190.108 1.00 1.02  ? 2708 PHE A CE2   1 
ATOM   9875  C  CZ    . PHE A 1 2708 ? 211.455 197.215 188.846 1.00 0.48  ? 2708 PHE A CZ    1 
ATOM   9876  N  N     . VAL A 1 2709 ? 215.410 191.409 190.727 1.00 0.16  ? 2709 VAL A N     1 
ATOM   9877  C  CA    . VAL A 1 2709 ? 215.711 190.056 191.174 1.00 0.03  ? 2709 VAL A CA    1 
ATOM   9878  C  C     . VAL A 1 2709 ? 215.083 189.872 192.545 1.00 0.08  ? 2709 VAL A C     1 
ATOM   9879  O  O     . VAL A 1 2709 ? 215.243 190.723 193.426 1.00 0.21  ? 2709 VAL A O     1 
ATOM   9880  C  CB    . VAL A 1 2709 ? 217.227 189.784 191.227 1.00 0.07  ? 2709 VAL A CB    1 
ATOM   9881  C  CG1   . VAL A 1 2709 ? 217.506 188.461 191.919 1.00 0.06  ? 2709 VAL A CG1   1 
ATOM   9882  C  CG2   . VAL A 1 2709 ? 217.814 189.779 189.830 1.00 0.08  ? 2709 VAL A CG2   1 
ATOM   9883  N  N     . GLY A 1 2710 ? 214.365 188.770 192.724 1.00 0.11  ? 2710 GLY A N     1 
ATOM   9884  C  CA    . GLY A 1 2710 ? 213.724 188.455 193.984 1.00 0.06  ? 2710 GLY A CA    1 
ATOM   9885  C  C     . GLY A 1 2710 ? 214.387 187.274 194.663 1.00 0.05  ? 2710 GLY A C     1 
ATOM   9886  O  O     . GLY A 1 2710 ? 214.899 186.368 194.005 1.00 0.04  ? 2710 GLY A O     1 
ATOM   9887  N  N     . ALA A 1 2711 ? 214.400 187.305 195.988 1.00 0.27  ? 2711 ALA A N     1 
ATOM   9888  C  CA    . ALA A 1 2711 ? 214.754 186.154 196.801 1.00 0.16  ? 2711 ALA A CA    1 
ATOM   9889  C  C     . ALA A 1 2711 ? 213.656 185.957 197.830 1.00 0.20  ? 2711 ALA A C     1 
ATOM   9890  O  O     . ALA A 1 2711 ? 212.991 186.912 198.233 1.00 0.38  ? 2711 ALA A O     1 
ATOM   9891  C  CB    . ALA A 1 2711 ? 216.111 186.323 197.492 1.00 0.14  ? 2711 ALA A CB    1 
ATOM   9892  N  N     . CYS A 1 2712 ? 213.452 184.711 198.235 1.00 0.27  ? 2712 CYS A N     1 
ATOM   9893  C  CA    . CYS A 1 2712 ? 212.367 184.411 199.156 1.00 0.38  ? 2712 CYS A CA    1 
ATOM   9894  C  C     . CYS A 1 2712 ? 212.544 182.998 199.687 1.00 0.34  ? 2712 CYS A C     1 
ATOM   9895  O  O     . CYS A 1 2712 ? 213.291 182.188 199.134 1.00 0.23  ? 2712 CYS A O     1 
ATOM   9896  C  CB    . CYS A 1 2712 ? 211.002 184.559 198.481 1.00 0.23  ? 2712 CYS A CB    1 
ATOM   9897  S  SG    . CYS A 1 2712 ? 210.739 183.446 197.100 1.00 0.58  ? 2712 CYS A SG    1 
ATOM   9898  N  N     . ASN A 1 2713 ? 211.854 182.726 200.764 1.00 0.90  ? 2713 ASN A N     1 
ATOM   9899  C  CA    . ASN A 1 2713 ? 211.672 181.394 201.304 1.00 0.79  ? 2713 ASN A CA    1 
ATOM   9900  C  C     . ASN A 1 2713 ? 210.441 180.756 200.677 1.00 1.10  ? 2713 ASN A C     1 
ATOM   9901  O  O     . ASN A 1 2713 ? 209.593 181.454 200.114 1.00 1.54  ? 2713 ASN A O     1 
ATOM   9902  C  CB    . ASN A 1 2713 ? 211.540 181.467 202.822 1.00 2.55  ? 2713 ASN A CB    1 
ATOM   9903  C  CG    . ASN A 1 2713 ? 212.833 181.886 203.498 1.00 0.71  ? 2713 ASN A CG    1 
ATOM   9904  O  OD1   . ASN A 1 2713 ? 212.840 182.261 204.668 1.00 1.59  ? 2713 ASN A OD1   1 
ATOM   9905  N  ND2   . ASN A 1 2713 ? 213.935 181.819 202.761 1.00 0.11  ? 2713 ASN A ND2   1 
ATOM   9906  N  N     . PRO A 1 2714 ? 210.322 179.431 200.728 1.00 2.29  ? 2714 PRO A N     1 
ATOM   9907  C  CA    . PRO A 1 2714 ? 209.156 178.764 200.134 1.00 1.34  ? 2714 PRO A CA    1 
ATOM   9908  C  C     . PRO A 1 2714 ? 207.859 179.294 200.717 1.00 1.16  ? 2714 PRO A C     1 
ATOM   9909  O  O     . PRO A 1 2714 ? 207.784 179.596 201.917 1.00 4.89  ? 2714 PRO A O     1 
ATOM   9910  C  CB    . PRO A 1 2714 ? 209.375 177.292 200.501 1.00 2.68  ? 2714 PRO A CB    1 
ATOM   9911  C  CG    . PRO A 1 2714 ? 210.853 177.162 200.560 1.00 2.18  ? 2714 PRO A CG    1 
ATOM   9912  C  CD    . PRO A 1 2714 ? 211.358 178.461 201.128 1.00 1.31  ? 2714 PRO A CD    1 
ATOM   9913  N  N     . PRO A 1 2715 ? 206.817 179.429 199.893 1.00 1.83  ? 2715 PRO A N     1 
ATOM   9914  C  CA    . PRO A 1 2715 ? 205.568 180.041 200.377 1.00 1.46  ? 2715 PRO A CA    1 
ATOM   9915  C  C     . PRO A 1 2715 ? 204.899 179.264 201.494 1.00 2.29  ? 2715 PRO A C     1 
ATOM   9916  O  O     . PRO A 1 2715 ? 204.063 179.834 202.207 1.00 3.69  ? 2715 PRO A O     1 
ATOM   9917  C  CB    . PRO A 1 2715 ? 204.690 180.088 199.119 1.00 1.25  ? 2715 PRO A CB    1 
ATOM   9918  C  CG    . PRO A 1 2715 ? 205.264 179.051 198.215 1.00 0.78  ? 2715 PRO A CG    1 
ATOM   9919  C  CD    . PRO A 1 2715 ? 206.736 179.065 198.469 1.00 1.46  ? 2715 PRO A CD    1 
ATOM   9920  N  N     . THR A 1 2716 ? 205.232 177.987 201.669 1.00 2.84  ? 2716 THR A N     1 
ATOM   9921  C  CA    . THR A 1 2716 ? 204.680 177.201 202.764 1.00 4.62  ? 2716 THR A CA    1 
ATOM   9922  C  C     . THR A 1 2716 ? 205.264 177.577 204.120 1.00 5.42  ? 2716 THR A C     1 
ATOM   9923  O  O     . THR A 1 2716 ? 204.699 177.183 205.145 1.00 10.99 ? 2716 THR A O     1 
ATOM   9924  C  CB    . THR A 1 2716 ? 204.905 175.711 202.499 1.00 6.42  ? 2716 THR A CB    1 
ATOM   9925  O  OG1   . THR A 1 2716 ? 206.304 175.459 202.325 1.00 10.56 ? 2716 THR A OG1   1 
ATOM   9926  C  CG2   . THR A 1 2716 ? 204.159 175.280 201.246 1.00 4.74  ? 2716 THR A CG2   1 
ATOM   9927  N  N     . ASP A 1 2717 ? 206.366 178.322 204.154 1.00 3.42  ? 2717 ASP A N     1 
ATOM   9928  C  CA    . ASP A 1 2717 ? 206.961 178.722 205.418 1.00 4.45  ? 2717 ASP A CA    1 
ATOM   9929  C  C     . ASP A 1 2717 ? 206.088 179.764 206.118 1.00 4.55  ? 2717 ASP A C     1 
ATOM   9930  O  O     . ASP A 1 2717 ? 205.368 180.521 205.463 1.00 3.18  ? 2717 ASP A O     1 
ATOM   9931  C  CB    . ASP A 1 2717 ? 208.363 179.281 205.193 1.00 6.04  ? 2717 ASP A CB    1 
ATOM   9932  C  CG    . ASP A 1 2717 ? 209.310 178.255 204.608 1.00 9.87  ? 2717 ASP A CG    1 
ATOM   9933  O  OD1   . ASP A 1 2717 ? 208.872 177.112 204.362 1.00 7.12  ? 2717 ASP A OD1   1 
ATOM   9934  O  OD2   . ASP A 1 2717 ? 210.494 178.589 204.397 1.00 14.86 ? 2717 ASP A OD2   1 
ATOM   9935  N  N     . PRO A 1 2718 ? 206.124 179.812 207.450 1.00 6.32  ? 2718 PRO A N     1 
ATOM   9936  C  CA    . PRO A 1 2718 ? 205.283 180.773 208.179 1.00 4.62  ? 2718 PRO A CA    1 
ATOM   9937  C  C     . PRO A 1 2718 ? 205.629 182.212 207.824 1.00 2.61  ? 2718 PRO A C     1 
ATOM   9938  O  O     . PRO A 1 2718 ? 206.798 182.575 207.682 1.00 4.55  ? 2718 PRO A O     1 
ATOM   9939  C  CB    . PRO A 1 2718 ? 205.580 180.456 209.649 1.00 4.03  ? 2718 PRO A CB    1 
ATOM   9940  C  CG    . PRO A 1 2718 ? 206.920 179.801 209.627 1.00 4.15  ? 2718 PRO A CG    1 
ATOM   9941  C  CD    . PRO A 1 2718 ? 206.930 178.991 208.370 1.00 3.84  ? 2718 PRO A CD    1 
ATOM   9942  N  N     . GLY A 1 2719 ? 204.590 183.035 207.687 1.00 1.70  ? 2719 GLY A N     1 
ATOM   9943  C  CA    . GLY A 1 2719 ? 204.738 184.412 207.276 1.00 0.78  ? 2719 GLY A CA    1 
ATOM   9944  C  C     . GLY A 1 2719 ? 204.863 184.621 205.782 1.00 1.22  ? 2719 GLY A C     1 
ATOM   9945  O  O     . GLY A 1 2719 ? 204.800 185.768 205.326 1.00 1.40  ? 2719 GLY A O     1 
ATOM   9946  N  N     . ARG A 1 2720 ? 205.027 183.554 205.008 1.00 1.09  ? 2720 ARG A N     1 
ATOM   9947  C  CA    . ARG A 1 2720 ? 205.222 183.653 203.570 1.00 0.94  ? 2720 ARG A CA    1 
ATOM   9948  C  C     . ARG A 1 2720 ? 203.903 183.431 202.845 1.00 1.00  ? 2720 ARG A C     1 
ATOM   9949  O  O     . ARG A 1 2720 ? 203.131 182.533 203.192 1.00 3.84  ? 2720 ARG A O     1 
ATOM   9950  C  CB    . ARG A 1 2720 ? 206.262 182.640 203.087 1.00 1.49  ? 2720 ARG A CB    1 
ATOM   9951  C  CG    . ARG A 1 2720 ? 207.726 183.054 203.251 1.00 0.94  ? 2720 ARG A CG    1 
ATOM   9952  C  CD    . ARG A 1 2720 ? 208.102 183.398 204.675 1.00 2.05  ? 2720 ARG A CD    1 
ATOM   9953  N  NE    . ARG A 1 2720 ? 209.485 183.847 204.777 1.00 5.07  ? 2720 ARG A NE    1 
ATOM   9954  C  CZ    . ARG A 1 2720 ? 210.054 184.268 205.898 1.00 3.75  ? 2720 ARG A CZ    1 
ATOM   9955  N  NH1   . ARG A 1 2720 ? 209.382 184.325 207.034 1.00 4.01  ? 2720 ARG A NH1   1 
ATOM   9956  N  NH2   . ARG A 1 2720 ? 211.327 184.651 205.874 1.00 3.07  ? 2720 ARG A NH2   1 
ATOM   9957  N  N     . LYS A 1 2721 ? 203.645 184.258 201.847 1.00 1.23  ? 2721 LYS A N     1 
ATOM   9958  C  CA    . LYS A 1 2721 ? 202.445 184.129 201.041 1.00 1.74  ? 2721 LYS A CA    1 
ATOM   9959  C  C     . LYS A 1 2721 ? 202.794 183.683 199.627 1.00 0.76  ? 2721 LYS A C     1 
ATOM   9960  O  O     . LYS A 1 2721 ? 203.860 184.024 199.109 1.00 0.41  ? 2721 LYS A O     1 
ATOM   9961  C  CB    . LYS A 1 2721 ? 201.667 185.450 200.976 1.00 1.60  ? 2721 LYS A CB    1 
ATOM   9962  C  CG    . LYS A 1 2721 ? 200.740 185.702 202.156 1.00 2.69  ? 2721 LYS A CG    1 
ATOM   9963  C  CD    . LYS A 1 2721 ? 201.489 186.075 203.422 1.00 2.83  ? 2721 LYS A CD    1 
ATOM   9964  C  CE    . LYS A 1 2721 ? 202.123 187.446 203.315 1.00 1.32  ? 2721 LYS A CE    1 
ATOM   9965  N  NZ    . LYS A 1 2721 ? 202.797 187.834 204.583 1.00 1.09  ? 2721 LYS A NZ    1 
ATOM   9966  N  N     . PRO A 1 2722 ? 201.926 182.903 198.984 1.00 2.49  ? 2722 PRO A N     1 
ATOM   9967  C  CA    . PRO A 1 2722 ? 202.155 182.557 197.577 1.00 0.46  ? 2722 PRO A CA    1 
ATOM   9968  C  C     . PRO A 1 2722 ? 202.130 183.796 196.696 1.00 0.33  ? 2722 PRO A C     1 
ATOM   9969  O  O     . PRO A 1 2722 ? 201.326 184.709 196.893 1.00 0.44  ? 2722 PRO A O     1 
ATOM   9970  C  CB    . PRO A 1 2722 ? 200.999 181.607 197.250 1.00 0.31  ? 2722 PRO A CB    1 
ATOM   9971  C  CG    . PRO A 1 2722 ? 199.953 181.917 198.263 1.00 0.68  ? 2722 PRO A CG    1 
ATOM   9972  C  CD    . PRO A 1 2722 ? 200.693 182.293 199.507 1.00 1.18  ? 2722 PRO A CD    1 
ATOM   9973  N  N     . LEU A 1 2723 ? 203.025 183.820 195.716 1.00 0.35  ? 2723 LEU A N     1 
ATOM   9974  C  CA    . LEU A 1 2723 ? 203.070 184.928 194.778 1.00 0.18  ? 2723 LEU A CA    1 
ATOM   9975  C  C     . LEU A 1 2723 ? 201.922 184.826 193.781 1.00 0.24  ? 2723 LEU A C     1 
ATOM   9976  O  O     . LEU A 1 2723 ? 201.484 183.734 193.411 1.00 0.24  ? 2723 LEU A O     1 
ATOM   9977  C  CB    . LEU A 1 2723 ? 204.412 184.949 194.048 1.00 0.15  ? 2723 LEU A CB    1 
ATOM   9978  C  CG    . LEU A 1 2723 ? 205.601 185.438 194.881 1.00 0.14  ? 2723 LEU A CG    1 
ATOM   9979  C  CD1   . LEU A 1 2723 ? 206.896 185.356 194.091 1.00 0.08  ? 2723 LEU A CD1   1 
ATOM   9980  C  CD2   . LEU A 1 2723 ? 205.362 186.856 195.376 1.00 0.08  ? 2723 LEU A CD2   1 
ATOM   9981  N  N     . SER A 1 2724 ? 201.424 185.986 193.358 1.00 0.41  ? 2724 SER A N     1 
ATOM   9982  C  CA    . SER A 1 2724 ? 200.342 186.031 192.385 1.00 0.40  ? 2724 SER A CA    1 
ATOM   9983  C  C     . SER A 1 2724 ? 200.770 185.382 191.074 1.00 0.35  ? 2724 SER A C     1 
ATOM   9984  O  O     . SER A 1 2724 ? 201.890 185.585 190.597 1.00 0.31  ? 2724 SER A O     1 
ATOM   9985  C  CB    . SER A 1 2724 ? 199.913 187.479 192.144 1.00 0.37  ? 2724 SER A CB    1 
ATOM   9986  O  OG    . SER A 1 2724 ? 198.981 187.574 191.084 1.00 3.17  ? 2724 SER A OG    1 
ATOM   9987  N  N     . HIS A 1 2725 ? 199.856 184.624 190.461 1.00 0.81  ? 2725 HIS A N     1 
ATOM   9988  C  CA    . HIS A 1 2725 ? 200.171 183.926 189.183 1.00 0.46  ? 2725 HIS A CA    1 
ATOM   9989  C  C     . HIS A 1 2725 ? 200.402 184.955 188.068 1.00 0.19  ? 2725 HIS A C     1 
ATOM   9990  O  O     . HIS A 1 2725 ? 201.128 184.643 187.104 1.00 0.12  ? 2725 HIS A O     1 
ATOM   9991  C  CB    . HIS A 1 2725 ? 199.073 182.911 188.843 1.00 1.83  ? 2725 HIS A CB    1 
ATOM   9992  C  CG    . HIS A 1 2725 ? 199.044 181.724 189.742 1.00 2.21  ? 2725 HIS A CG    1 
ATOM   9993  N  ND1   . HIS A 1 2725 ? 198.538 180.504 189.351 1.00 3.69  ? 2725 HIS A ND1   1 
ATOM   9994  C  CD2   . HIS A 1 2725 ? 199.443 181.569 191.010 1.00 3.13  ? 2725 HIS A CD2   1 
ATOM   9995  C  CE1   . HIS A 1 2725 ? 198.641 179.646 190.355 1.00 3.42  ? 2725 HIS A CE1   1 
ATOM   9996  N  NE2   . HIS A 1 2725 ? 199.190 180.273 191.372 1.00 3.89  ? 2725 HIS A NE2   1 
ATOM   9997  N  N     . ARG A 1 2726 ? 199.811 186.146 188.200 1.00 0.16  ? 2726 ARG A N     1 
ATOM   9998  C  CA    . ARG A 1 2726 ? 199.991 187.217 187.185 1.00 0.34  ? 2726 ARG A CA    1 
ATOM   9999  C  C     . ARG A 1 2726 ? 201.406 187.810 187.306 1.00 0.20  ? 2726 ARG A C     1 
ATOM   10000 O  O     . ARG A 1 2726 ? 201.881 188.405 186.320 1.00 0.59  ? 2726 ARG A O     1 
ATOM   10001 C  CB    . ARG A 1 2726 ? 198.896 188.279 187.325 1.00 0.54  ? 2726 ARG A CB    1 
ATOM   10002 C  CG    . ARG A 1 2726 ? 197.756 188.174 186.324 1.00 0.15  ? 2726 ARG A CG    1 
ATOM   10003 C  CD    . ARG A 1 2726 ? 196.774 189.313 186.526 1.00 0.25  ? 2726 ARG A CD    1 
ATOM   10004 N  NE    . ARG A 1 2726 ? 195.967 189.580 185.330 1.00 0.12  ? 2726 ARG A NE    1 
ATOM   10005 C  CZ    . ARG A 1 2726 ? 195.059 190.539 185.245 1.00 0.09  ? 2726 ARG A CZ    1 
ATOM   10006 N  NH1   . ARG A 1 2726 ? 194.784 191.283 186.301 1.00 0.82  ? 2726 ARG A NH1   1 
ATOM   10007 N  NH2   . ARG A 1 2726 ? 194.432 190.752 184.104 1.00 0.07  ? 2726 ARG A NH2   1 
ATOM   10008 N  N     . PHE A 1 2727 ? 202.048 187.650 188.464 1.00 0.13  ? 2727 PHE A N     1 
ATOM   10009 C  CA    . PHE A 1 2727 ? 203.443 188.130 188.646 1.00 0.09  ? 2727 PHE A CA    1 
ATOM   10010 C  C     . PHE A 1 2727 ? 204.413 187.019 188.264 1.00 0.12  ? 2727 PHE A C     1 
ATOM   10011 O  O     . PHE A 1 2727 ? 205.518 187.334 187.783 1.00 0.13  ? 2727 PHE A O     1 
ATOM   10012 C  CB    . PHE A 1 2727 ? 203.644 188.571 190.099 1.00 0.04  ? 2727 PHE A CB    1 
ATOM   10013 C  CG    . PHE A 1 2727 ? 205.088 188.785 190.532 1.00 0.07  ? 2727 PHE A CG    1 
ATOM   10014 C  CD1   . PHE A 1 2727 ? 205.834 187.739 191.062 1.00 0.04  ? 2727 PHE A CD1   1 
ATOM   10015 C  CD2   . PHE A 1 2727 ? 205.690 190.034 190.418 1.00 0.03  ? 2727 PHE A CD2   1 
ATOM   10016 C  CE1   . PHE A 1 2727 ? 207.148 187.937 191.458 1.00 0.04  ? 2727 PHE A CE1   1 
ATOM   10017 C  CE2   . PHE A 1 2727 ? 207.003 190.224 190.818 1.00 0.03  ? 2727 PHE A CE2   1 
ATOM   10018 C  CZ    . PHE A 1 2727 ? 207.727 189.177 191.337 1.00 0.02  ? 2727 PHE A CZ    1 
ATOM   10019 N  N     . LEU A 1 2728 ? 204.012 185.759 188.450 1.00 0.05  ? 2728 LEU A N     1 
ATOM   10020 C  CA    . LEU A 1 2728 ? 204.942 184.661 188.213 1.00 0.08  ? 2728 LEU A CA    1 
ATOM   10021 C  C     . LEU A 1 2728 ? 205.151 184.380 186.729 1.00 0.31  ? 2728 LEU A C     1 
ATOM   10022 O  O     . LEU A 1 2728 ? 206.182 183.811 186.358 1.00 0.43  ? 2728 LEU A O     1 
ATOM   10023 C  CB    . LEU A 1 2728 ? 204.458 183.399 188.928 1.00 0.30  ? 2728 LEU A CB    1 
ATOM   10024 C  CG    . LEU A 1 2728 ? 204.529 183.403 190.458 1.00 0.20  ? 2728 LEU A CG    1 
ATOM   10025 C  CD1   . LEU A 1 2728 ? 204.078 182.074 191.027 1.00 0.37  ? 2728 LEU A CD1   1 
ATOM   10026 C  CD2   . LEU A 1 2728 ? 205.937 183.729 190.925 1.00 0.10  ? 2728 LEU A CD2   1 
ATOM   10027 N  N     . ARG A 1 2729 ? 204.198 184.755 185.867 1.00 0.88  ? 2729 ARG A N     1 
ATOM   10028 C  CA    . ARG A 1 2729 ? 204.362 184.481 184.440 1.00 0.32  ? 2729 ARG A CA    1 
ATOM   10029 C  C     . ARG A 1 2729 ? 205.556 185.223 183.858 1.00 0.45  ? 2729 ARG A C     1 
ATOM   10030 O  O     . ARG A 1 2729 ? 206.104 184.806 182.833 1.00 1.03  ? 2729 ARG A O     1 
ATOM   10031 C  CB    . ARG A 1 2729 ? 203.094 184.841 183.664 1.00 0.64  ? 2729 ARG A CB    1 
ATOM   10032 C  CG    . ARG A 1 2729 ? 202.747 186.320 183.654 1.00 1.34  ? 2729 ARG A CG    1 
ATOM   10033 C  CD    . ARG A 1 2729 ? 201.460 186.561 182.889 1.00 2.24  ? 2729 ARG A CD    1 
ATOM   10034 N  NE    . ARG A 1 2729 ? 201.565 186.273 181.462 1.00 4.86  ? 2729 ARG A NE    1 
ATOM   10035 C  CZ    . ARG A 1 2729 ? 202.013 187.132 180.558 1.00 3.67  ? 2729 ARG A CZ    1 
ATOM   10036 N  NH1   . ARG A 1 2729 ? 202.327 188.372 180.879 1.00 9.72  ? 2729 ARG A NH1   1 
ATOM   10037 N  NH2   . ARG A 1 2729 ? 202.122 186.748 179.291 1.00 6.81  ? 2729 ARG A NH2   1 
ATOM   10038 N  N     . HIS A 1 2730 ? 205.971 186.316 184.490 1.00 0.34  ? 2730 HIS A N     1 
ATOM   10039 C  CA    . HIS A 1 2730 ? 207.118 187.087 184.041 1.00 0.35  ? 2730 HIS A CA    1 
ATOM   10040 C  C     . HIS A 1 2730 ? 208.418 186.671 184.705 1.00 0.38  ? 2730 HIS A C     1 
ATOM   10041 O  O     . HIS A 1 2730 ? 209.490 187.041 184.216 1.00 0.78  ? 2730 HIS A O     1 
ATOM   10042 C  CB    . HIS A 1 2730 ? 206.886 188.575 184.307 1.00 0.26  ? 2730 HIS A CB    1 
ATOM   10043 C  CG    . HIS A 1 2730 ? 205.646 189.106 183.670 1.00 0.80  ? 2730 HIS A CG    1 
ATOM   10044 N  ND1   . HIS A 1 2730 ? 204.456 189.229 184.352 1.00 0.63  ? 2730 HIS A ND1   1 
ATOM   10045 C  CD2   . HIS A 1 2730 ? 205.407 189.530 182.410 1.00 0.75  ? 2730 HIS A CD2   1 
ATOM   10046 C  CE1   . HIS A 1 2730 ? 203.537 189.712 183.538 1.00 0.94  ? 2730 HIS A CE1   1 
ATOM   10047 N  NE2   . HIS A 1 2730 ? 204.089 189.904 182.354 1.00 1.06  ? 2730 HIS A NE2   1 
ATOM   10048 N  N     . VAL A 1 2731 ? 208.353 185.917 185.792 1.00 0.34  ? 2731 VAL A N     1 
ATOM   10049 C  CA    . VAL A 1 2731 ? 209.476 185.733 186.697 1.00 0.27  ? 2731 VAL A CA    1 
ATOM   10050 C  C     . VAL A 1 2731 ? 209.795 184.246 186.787 1.00 0.19  ? 2731 VAL A C     1 
ATOM   10051 O  O     . VAL A 1 2731 ? 209.140 183.501 187.516 1.00 0.78  ? 2731 VAL A O     1 
ATOM   10052 C  CB    . VAL A 1 2731 ? 209.168 186.318 188.087 1.00 0.21  ? 2731 VAL A CB    1 
ATOM   10053 C  CG1   . VAL A 1 2731 ? 210.345 186.138 189.000 1.00 0.14  ? 2731 VAL A CG1   1 
ATOM   10054 C  CG2   . VAL A 1 2731 ? 208.792 187.789 187.974 1.00 0.13  ? 2731 VAL A CG2   1 
ATOM   10055 N  N     . PRO A 1 2732 ? 210.800 183.773 186.051 1.00 0.13  ? 2732 PRO A N     1 
ATOM   10056 C  CA    . PRO A 1 2732 ? 211.280 182.403 186.260 1.00 0.18  ? 2732 PRO A CA    1 
ATOM   10057 C  C     . PRO A 1 2732 ? 211.824 182.216 187.668 1.00 0.13  ? 2732 PRO A C     1 
ATOM   10058 O  O     . PRO A 1 2732 ? 212.416 183.122 188.258 1.00 0.27  ? 2732 PRO A O     1 
ATOM   10059 C  CB    . PRO A 1 2732 ? 212.385 182.246 185.206 1.00 0.18  ? 2732 PRO A CB    1 
ATOM   10060 C  CG    . PRO A 1 2732 ? 212.754 183.634 184.826 1.00 0.25  ? 2732 PRO A CG    1 
ATOM   10061 C  CD    . PRO A 1 2732 ? 211.490 184.421 184.927 1.00 0.28  ? 2732 PRO A CD    1 
ATOM   10062 N  N     . VAL A 1 2733 ? 211.613 181.020 188.207 1.00 0.11  ? 2733 VAL A N     1 
ATOM   10063 C  CA    . VAL A 1 2733 ? 211.985 180.691 189.576 1.00 0.11  ? 2733 VAL A CA    1 
ATOM   10064 C  C     . VAL A 1 2733 ? 212.990 179.550 189.545 1.00 0.12  ? 2733 VAL A C     1 
ATOM   10065 O  O     . VAL A 1 2733 ? 212.757 178.527 188.893 1.00 0.19  ? 2733 VAL A O     1 
ATOM   10066 C  CB    . VAL A 1 2733 ? 210.756 180.317 190.425 1.00 0.10  ? 2733 VAL A CB    1 
ATOM   10067 C  CG1   . VAL A 1 2733 ? 211.184 179.828 191.798 1.00 0.11  ? 2733 VAL A CG1   1 
ATOM   10068 C  CG2   . VAL A 1 2733 ? 209.815 181.499 190.544 1.00 0.10  ? 2733 VAL A CG2   1 
ATOM   10069 N  N     . VAL A 1 2734 ? 214.107 179.735 190.238 1.00 0.16  ? 2734 VAL A N     1 
ATOM   10070 C  CA    . VAL A 1 2734 ? 215.097 178.690 190.453 1.00 0.27  ? 2734 VAL A CA    1 
ATOM   10071 C  C     . VAL A 1 2734 ? 215.065 178.309 191.927 1.00 0.19  ? 2734 VAL A C     1 
ATOM   10072 O  O     . VAL A 1 2734 ? 214.984 179.183 192.798 1.00 0.13  ? 2734 VAL A O     1 
ATOM   10073 C  CB    . VAL A 1 2734 ? 216.508 179.132 190.008 1.00 0.40  ? 2734 VAL A CB    1 
ATOM   10074 C  CG1   . VAL A 1 2734 ? 217.011 180.302 190.841 1.00 2.04  ? 2734 VAL A CG1   1 
ATOM   10075 C  CG2   . VAL A 1 2734 ? 217.478 177.966 190.094 1.00 0.37  ? 2734 VAL A CG2   1 
ATOM   10076 N  N     . TYR A 1 2735 ? 215.085 177.010 192.202 1.00 0.41  ? 2735 TYR A N     1 
ATOM   10077 C  CA    . TYR A 1 2735 ? 215.053 176.505 193.567 1.00 0.36  ? 2735 TYR A CA    1 
ATOM   10078 C  C     . TYR A 1 2735 ? 216.476 176.230 194.038 1.00 0.41  ? 2735 TYR A C     1 
ATOM   10079 O  O     . TYR A 1 2735 ? 217.185 175.408 193.447 1.00 0.89  ? 2735 TYR A O     1 
ATOM   10080 C  CB    . TYR A 1 2735 ? 214.208 175.237 193.662 1.00 0.64  ? 2735 TYR A CB    1 
ATOM   10081 C  CG    . TYR A 1 2735 ? 214.119 174.673 195.061 1.00 1.13  ? 2735 TYR A CG    1 
ATOM   10082 C  CD1   . TYR A 1 2735 ? 213.709 175.464 196.126 1.00 1.22  ? 2735 TYR A CD1   1 
ATOM   10083 C  CD2   . TYR A 1 2735 ? 214.461 173.354 195.319 1.00 0.82  ? 2735 TYR A CD2   1 
ATOM   10084 C  CE1   . TYR A 1 2735 ? 213.629 174.954 197.403 1.00 1.93  ? 2735 TYR A CE1   1 
ATOM   10085 C  CE2   . TYR A 1 2735 ? 214.385 172.834 196.595 1.00 1.86  ? 2735 TYR A CE2   1 
ATOM   10086 C  CZ    . TYR A 1 2735 ? 213.969 173.639 197.633 1.00 5.10  ? 2735 TYR A CZ    1 
ATOM   10087 O  OH    . TYR A 1 2735 ? 213.892 173.124 198.905 1.00 12.45 ? 2735 TYR A OH    1 
ATOM   10088 N  N     . VAL A 1 2736 ? 216.887 176.911 195.098 1.00 0.19  ? 2736 VAL A N     1 
ATOM   10089 C  CA    . VAL A 1 2736 ? 218.199 176.718 195.697 1.00 0.46  ? 2736 VAL A CA    1 
ATOM   10090 C  C     . VAL A 1 2736 ? 217.983 176.014 197.027 1.00 0.37  ? 2736 VAL A C     1 
ATOM   10091 O  O     . VAL A 1 2736 ? 217.484 176.613 197.987 1.00 0.32  ? 2736 VAL A O     1 
ATOM   10092 C  CB    . VAL A 1 2736 ? 218.951 178.043 195.873 1.00 0.59  ? 2736 VAL A CB    1 
ATOM   10093 C  CG1   . VAL A 1 2736 ? 220.306 177.801 196.515 1.00 0.25  ? 2736 VAL A CG1   1 
ATOM   10094 C  CG2   . VAL A 1 2736 ? 219.106 178.745 194.531 1.00 0.47  ? 2736 VAL A CG2   1 
ATOM   10095 N  N     . ASP A 1 2737 ? 218.345 174.740 197.083 1.00 0.49  ? 2737 ASP A N     1 
ATOM   10096 C  CA    . ASP A 1 2737 ? 218.200 173.947 198.290 1.00 1.13  ? 2737 ASP A CA    1 
ATOM   10097 C  C     . ASP A 1 2737 ? 219.463 174.037 199.142 1.00 0.55  ? 2737 ASP A C     1 
ATOM   10098 O  O     . ASP A 1 2737 ? 220.491 174.574 198.728 1.00 0.68  ? 2737 ASP A O     1 
ATOM   10099 C  CB    . ASP A 1 2737 ? 217.896 172.493 197.935 1.00 1.28  ? 2737 ASP A CB    1 
ATOM   10100 C  CG    . ASP A 1 2737 ? 217.206 171.751 199.059 1.00 4.81  ? 2737 ASP A CG    1 
ATOM   10101 O  OD1   . ASP A 1 2737 ? 216.888 172.383 200.088 1.00 3.14  ? 2737 ASP A OD1   1 
ATOM   10102 O  OD2   . ASP A 1 2737 ? 216.982 170.531 198.915 1.00 14.41 ? 2737 ASP A OD2   1 
ATOM   10103 N  N     . TYR A 1 2738 ? 219.369 173.506 200.353 1.00 0.94  ? 2738 TYR A N     1 
ATOM   10104 C  CA    . TYR A 1 2738 ? 220.542 173.399 201.200 1.00 0.77  ? 2738 TYR A CA    1 
ATOM   10105 C  C     . TYR A 1 2738 ? 221.545 172.442 200.563 1.00 1.23  ? 2738 TYR A C     1 
ATOM   10106 O  O     . TYR A 1 2738 ? 221.148 171.420 199.991 1.00 1.46  ? 2738 TYR A O     1 
ATOM   10107 C  CB    . TYR A 1 2738 ? 220.158 172.903 202.595 1.00 0.47  ? 2738 TYR A CB    1 
ATOM   10108 C  CG    . TYR A 1 2738 ? 219.595 173.983 203.483 1.00 0.36  ? 2738 TYR A CG    1 
ATOM   10109 C  CD1   . TYR A 1 2738 ? 220.067 175.284 203.403 1.00 0.41  ? 2738 TYR A CD1   1 
ATOM   10110 C  CD2   . TYR A 1 2738 ? 218.585 173.705 204.393 1.00 0.25  ? 2738 TYR A CD2   1 
ATOM   10111 C  CE1   . TYR A 1 2738 ? 219.555 176.279 204.208 1.00 0.30  ? 2738 TYR A CE1   1 
ATOM   10112 C  CE2   . TYR A 1 2738 ? 218.067 174.692 205.202 1.00 0.32  ? 2738 TYR A CE2   1 
ATOM   10113 C  CZ    . TYR A 1 2738 ? 218.557 175.978 205.106 1.00 0.35  ? 2738 TYR A CZ    1 
ATOM   10114 O  OH    . TYR A 1 2738 ? 218.043 176.970 205.906 1.00 0.30  ? 2738 TYR A OH    1 
ATOM   10115 N  N     . PRO A 1 2739 ? 222.839 172.752 200.613 1.00 1.78  ? 2739 PRO A N     1 
ATOM   10116 C  CA    . PRO A 1 2739 ? 223.839 171.788 200.148 1.00 1.26  ? 2739 PRO A CA    1 
ATOM   10117 C  C     . PRO A 1 2739 ? 223.752 170.496 200.945 1.00 1.91  ? 2739 PRO A C     1 
ATOM   10118 O  O     . PRO A 1 2739 ? 223.492 170.501 202.150 1.00 2.62  ? 2739 PRO A O     1 
ATOM   10119 C  CB    . PRO A 1 2739 ? 225.168 172.513 200.386 1.00 0.72  ? 2739 PRO A CB    1 
ATOM   10120 C  CG    . PRO A 1 2739 ? 224.814 173.958 200.377 1.00 0.67  ? 2739 PRO A CG    1 
ATOM   10121 C  CD    . PRO A 1 2739 ? 223.438 174.049 200.967 1.00 1.26  ? 2739 PRO A CD    1 
ATOM   10122 N  N     . GLY A 1 2740 ? 223.968 169.377 200.255 1.00 1.95  ? 2740 GLY A N     1 
ATOM   10123 C  CA    . GLY A 1 2740 ? 223.908 168.091 200.885 1.00 3.37  ? 2740 GLY A CA    1 
ATOM   10124 C  C     . GLY A 1 2740 ? 225.132 167.824 201.738 1.00 4.68  ? 2740 GLY A C     1 
ATOM   10125 O  O     . GLY A 1 2740 ? 226.064 168.635 201.808 1.00 4.13  ? 2740 GLY A O     1 
ATOM   10126 N  N     . PRO A 1 2741 ? 225.133 166.670 202.412 1.00 4.84  ? 2741 PRO A N     1 
ATOM   10127 C  CA    . PRO A 1 2741 ? 226.279 166.332 203.273 1.00 4.72  ? 2741 PRO A CA    1 
ATOM   10128 C  C     . PRO A 1 2741 ? 227.602 166.284 202.530 1.00 4.97  ? 2741 PRO A C     1 
ATOM   10129 O  O     . PRO A 1 2741 ? 228.632 166.687 203.084 1.00 5.23  ? 2741 PRO A O     1 
ATOM   10130 C  CB    . PRO A 1 2741 ? 225.890 164.958 203.837 1.00 7.78  ? 2741 PRO A CB    1 
ATOM   10131 C  CG    . PRO A 1 2741 ? 224.398 164.921 203.739 1.00 10.02 ? 2741 PRO A CG    1 
ATOM   10132 C  CD    . PRO A 1 2741 ? 224.078 165.647 202.472 1.00 8.66  ? 2741 PRO A CD    1 
ATOM   10133 N  N     . ALA A 1 2742 ? 227.605 165.804 201.284 1.00 4.19  ? 2742 ALA A N     1 
ATOM   10134 C  CA    . ALA A 1 2742 ? 228.843 165.757 200.515 1.00 3.07  ? 2742 ALA A CA    1 
ATOM   10135 C  C     . ALA A 1 2742 ? 229.235 167.141 200.018 1.00 2.35  ? 2742 ALA A C     1 
ATOM   10136 O  O     . ALA A 1 2742 ? 230.424 167.474 199.964 1.00 2.07  ? 2742 ALA A O     1 
ATOM   10137 C  CB    . ALA A 1 2742 ? 228.703 164.783 199.346 1.00 3.19  ? 2742 ALA A CB    1 
ATOM   10138 N  N     . SER A 1 2743 ? 228.250 167.956 199.637 1.00 5.18  ? 2743 SER A N     1 
ATOM   10139 C  CA    . SER A 1 2743 ? 228.541 169.325 199.224 1.00 1.37  ? 2743 SER A CA    1 
ATOM   10140 C  C     . SER A 1 2743 ? 229.084 170.145 200.389 1.00 2.45  ? 2743 SER A C     1 
ATOM   10141 O  O     . SER A 1 2743 ? 230.015 170.938 200.215 1.00 3.20  ? 2743 SER A O     1 
ATOM   10142 C  CB    . SER A 1 2743 ? 227.286 169.968 198.638 1.00 1.91  ? 2743 SER A CB    1 
ATOM   10143 O  OG    . SER A 1 2743 ? 227.550 171.274 198.160 1.00 8.15  ? 2743 SER A OG    1 
ATOM   10144 N  N     . LEU A 1 2744 ? 228.513 169.964 201.582 1.00 2.67  ? 2744 LEU A N     1 
ATOM   10145 C  CA    . LEU A 1 2744 ? 229.020 170.658 202.762 1.00 0.98  ? 2744 LEU A CA    1 
ATOM   10146 C  C     . LEU A 1 2744 ? 230.446 170.236 203.078 1.00 1.51  ? 2744 LEU A C     1 
ATOM   10147 O  O     . LEU A 1 2744 ? 231.281 171.069 203.450 1.00 1.46  ? 2744 LEU A O     1 
ATOM   10148 C  CB    . LEU A 1 2744 ? 228.107 170.394 203.957 1.00 1.28  ? 2744 LEU A CB    1 
ATOM   10149 C  CG    . LEU A 1 2744 ? 226.727 171.049 203.908 1.00 1.37  ? 2744 LEU A CG    1 
ATOM   10150 C  CD1   . LEU A 1 2744 ? 225.916 170.668 205.132 1.00 1.25  ? 2744 LEU A CD1   1 
ATOM   10151 C  CD2   . LEU A 1 2744 ? 226.852 172.557 203.785 1.00 0.90  ? 2744 LEU A CD2   1 
ATOM   10152 N  N     . THR A 1 2745 ? 230.746 168.943 202.935 1.00 1.99  ? 2745 THR A N     1 
ATOM   10153 C  CA    . THR A 1 2745 ? 232.103 168.464 203.166 1.00 1.51  ? 2745 THR A CA    1 
ATOM   10154 C  C     . THR A 1 2745 ? 233.079 169.089 202.180 1.00 3.12  ? 2745 THR A C     1 
ATOM   10155 O  O     . THR A 1 2745 ? 234.212 169.424 202.542 1.00 4.83  ? 2745 THR A O     1 
ATOM   10156 C  CB    . THR A 1 2745 ? 232.141 166.939 203.071 1.00 1.26  ? 2745 THR A CB    1 
ATOM   10157 O  OG1   . THR A 1 2745 ? 231.276 166.378 204.067 1.00 1.84  ? 2745 THR A OG1   1 
ATOM   10158 C  CG2   . THR A 1 2745 ? 233.550 166.417 203.282 1.00 1.07  ? 2745 THR A CG2   1 
ATOM   10159 N  N     . GLN A 1 2746 ? 232.658 169.255 200.926 1.00 4.71  ? 2746 GLN A N     1 
ATOM   10160 C  CA    . GLN A 1 2746 ? 233.523 169.880 199.932 1.00 2.96  ? 2746 GLN A CA    1 
ATOM   10161 C  C     . GLN A 1 2746 ? 233.722 171.365 200.220 1.00 3.12  ? 2746 GLN A C     1 
ATOM   10162 O  O     . GLN A 1 2746 ? 234.836 171.881 200.090 1.00 3.40  ? 2746 GLN A O     1 
ATOM   10163 C  CB    . GLN A 1 2746 ? 232.941 169.671 198.534 1.00 4.09  ? 2746 GLN A CB    1 
ATOM   10164 C  CG    . GLN A 1 2746 ? 233.724 170.342 197.421 1.00 5.67  ? 2746 GLN A CG    1 
ATOM   10165 C  CD    . GLN A 1 2746 ? 234.897 169.503 196.943 1.00 20.27 ? 2746 GLN A CD    1 
ATOM   10166 O  OE1   . GLN A 1 2746 ? 235.169 168.432 197.484 1.00 14.60 ? 2746 GLN A OE1   1 
ATOM   10167 N  NE2   . GLN A 1 2746 ? 235.595 169.989 195.922 1.00 15.29 ? 2746 GLN A NE2   1 
ATOM   10168 N  N     . ILE A 1 2747 ? 232.656 172.067 200.614 1.00 1.60  ? 2747 ILE A N     1 
ATOM   10169 C  CA    . ILE A 1 2747 ? 232.756 173.503 200.862 1.00 1.06  ? 2747 ILE A CA    1 
ATOM   10170 C  C     . ILE A 1 2747 ? 233.659 173.780 202.057 1.00 1.56  ? 2747 ILE A C     1 
ATOM   10171 O  O     . ILE A 1 2747 ? 234.697 174.438 201.938 1.00 1.66  ? 2747 ILE A O     1 
ATOM   10172 C  CB    . ILE A 1 2747 ? 231.361 174.118 201.073 1.00 1.34  ? 2747 ILE A CB    1 
ATOM   10173 C  CG1   . ILE A 1 2747 ? 230.537 174.055 199.785 1.00 2.32  ? 2747 ILE A CG1   1 
ATOM   10174 C  CG2   . ILE A 1 2747 ? 231.473 175.546 201.577 1.00 0.30  ? 2747 ILE A CG2   1 
ATOM   10175 C  CD1   . ILE A 1 2747 ? 229.050 174.100 200.017 1.00 0.72  ? 2747 ILE A CD1   1 
ATOM   10176 N  N     . TYR A 1 2748 ? 233.273 173.278 203.226 1.00 1.16  ? 2748 TYR A N     1 
ATOM   10177 C  CA    . TYR A 1 2748 ? 233.961 173.610 204.462 1.00 0.82  ? 2748 TYR A CA    1 
ATOM   10178 C  C     . TYR A 1 2748 ? 235.172 172.731 204.730 1.00 1.05  ? 2748 TYR A C     1 
ATOM   10179 O  O     . TYR A 1 2748 ? 235.987 173.076 205.591 1.00 3.00  ? 2748 TYR A O     1 
ATOM   10180 C  CB    . TYR A 1 2748 ? 232.969 173.550 205.622 1.00 0.46  ? 2748 TYR A CB    1 
ATOM   10181 C  CG    . TYR A 1 2748 ? 231.854 174.546 205.429 1.00 0.23  ? 2748 TYR A CG    1 
ATOM   10182 C  CD1   . TYR A 1 2748 ? 232.066 175.897 205.655 1.00 0.39  ? 2748 TYR A CD1   1 
ATOM   10183 C  CD2   . TYR A 1 2748 ? 230.605 174.144 204.979 1.00 0.22  ? 2748 TYR A CD2   1 
ATOM   10184 C  CE1   . TYR A 1 2748 ? 231.061 176.818 205.465 1.00 0.26  ? 2748 TYR A CE1   1 
ATOM   10185 C  CE2   . TYR A 1 2748 ? 229.592 175.060 204.783 1.00 0.34  ? 2748 TYR A CE2   1 
ATOM   10186 C  CZ    . TYR A 1 2748 ? 229.828 176.398 205.027 1.00 0.28  ? 2748 TYR A CZ    1 
ATOM   10187 O  OH    . TYR A 1 2748 ? 228.828 177.319 204.840 1.00 0.20  ? 2748 TYR A OH    1 
ATOM   10188 N  N     . GLY A 1 2749 ? 235.319 171.617 204.013 1.00 1.26  ? 2749 GLY A N     1 
ATOM   10189 C  CA    . GLY A 1 2749 ? 236.603 170.941 203.982 1.00 1.27  ? 2749 GLY A CA    1 
ATOM   10190 C  C     . GLY A 1 2749 ? 237.664 171.766 203.286 1.00 2.36  ? 2749 GLY A C     1 
ATOM   10191 O  O     . GLY A 1 2749 ? 238.832 171.746 203.685 1.00 5.51  ? 2749 GLY A O     1 
ATOM   10192 N  N     . THR A 1 2750 ? 237.280 172.493 202.236 1.00 4.53  ? 2750 THR A N     1 
ATOM   10193 C  CA    . THR A 1 2750 ? 238.194 173.433 201.597 1.00 4.30  ? 2750 THR A CA    1 
ATOM   10194 C  C     . THR A 1 2750 ? 238.569 174.560 202.550 1.00 2.86  ? 2750 THR A C     1 
ATOM   10195 O  O     . THR A 1 2750 ? 239.739 174.949 202.641 1.00 6.42  ? 2750 THR A O     1 
ATOM   10196 C  CB    . THR A 1 2750 ? 237.558 173.992 200.322 1.00 2.61  ? 2750 THR A CB    1 
ATOM   10197 O  OG1   . THR A 1 2750 ? 237.340 172.927 199.389 1.00 7.69  ? 2750 THR A OG1   1 
ATOM   10198 C  CG2   . THR A 1 2750 ? 238.452 175.043 199.684 1.00 3.92  ? 2750 THR A CG2   1 
ATOM   10199 N  N     . PHE A 1 2751 ? 237.583 175.096 203.276 1.00 2.23  ? 2751 PHE A N     1 
ATOM   10200 C  CA    . PHE A 1 2751 ? 237.858 176.160 204.235 1.00 3.35  ? 2751 PHE A CA    1 
ATOM   10201 C  C     . PHE A 1 2751 ? 238.735 175.667 205.379 1.00 7.13  ? 2751 PHE A C     1 
ATOM   10202 O  O     . PHE A 1 2751 ? 239.672 176.360 205.793 1.00 7.43  ? 2751 PHE A O     1 
ATOM   10203 C  CB    . PHE A 1 2751 ? 236.544 176.725 204.776 1.00 1.96  ? 2751 PHE A CB    1 
ATOM   10204 C  CG    . PHE A 1 2751 ? 235.864 177.674 203.838 1.00 2.41  ? 2751 PHE A CG    1 
ATOM   10205 C  CD1   . PHE A 1 2751 ? 236.602 178.477 202.987 1.00 3.62  ? 2751 PHE A CD1   1 
ATOM   10206 C  CD2   . PHE A 1 2751 ? 234.484 177.760 203.803 1.00 1.54  ? 2751 PHE A CD2   1 
ATOM   10207 C  CE1   . PHE A 1 2751 ? 235.978 179.349 202.125 1.00 3.50  ? 2751 PHE A CE1   1 
ATOM   10208 C  CE2   . PHE A 1 2751 ? 233.855 178.633 202.941 1.00 1.73  ? 2751 PHE A CE2   1 
ATOM   10209 C  CZ    . PHE A 1 2751 ? 234.603 179.428 202.102 1.00 2.24  ? 2751 PHE A CZ    1 
ATOM   10210 N  N     . ASN A 1 2752 ? 238.445 174.474 205.905 1.00 2.52  ? 2752 ASN A N     1 
ATOM   10211 C  CA    . ASN A 1 2752 ? 239.217 173.953 207.029 1.00 3.41  ? 2752 ASN A CA    1 
ATOM   10212 C  C     . ASN A 1 2752 ? 240.662 173.679 206.631 1.00 6.92  ? 2752 ASN A C     1 
ATOM   10213 O  O     . ASN A 1 2752 ? 241.583 173.913 207.421 1.00 8.66  ? 2752 ASN A O     1 
ATOM   10214 C  CB    . ASN A 1 2752 ? 238.555 172.692 207.583 1.00 3.23  ? 2752 ASN A CB    1 
ATOM   10215 C  CG    . ASN A 1 2752 ? 237.347 172.998 208.446 1.00 1.08  ? 2752 ASN A CG    1 
ATOM   10216 O  OD1   . ASN A 1 2752 ? 237.005 174.158 208.670 1.00 1.71  ? 2752 ASN A OD1   1 
ATOM   10217 N  ND2   . ASN A 1 2752 ? 236.686 171.957 208.925 1.00 2.57  ? 2752 ASN A ND2   1 
ATOM   10218 N  N     . ARG A 1 2753 ? 240.881 173.180 205.412 1.00 7.52  ? 2753 ARG A N     1 
ATOM   10219 C  CA    . ARG A 1 2753 ? 242.246 172.967 204.940 1.00 9.15  ? 2753 ARG A CA    1 
ATOM   10220 C  C     . ARG A 1 2753 ? 243.019 174.279 204.885 1.00 8.92  ? 2753 ARG A C     1 
ATOM   10221 O  O     . ARG A 1 2753 ? 244.200 174.329 205.249 1.00 11.88 ? 2753 ARG A O     1 
ATOM   10222 C  CB    . ARG A 1 2753 ? 242.228 172.301 203.565 1.00 5.61  ? 2753 ARG A CB    1 
ATOM   10223 C  CG    . ARG A 1 2753 ? 242.064 170.793 203.603 1.00 11.94 ? 2753 ARG A CG    1 
ATOM   10224 C  CD    . ARG A 1 2753 ? 242.375 170.170 202.253 1.00 10.73 ? 2753 ARG A CD    1 
ATOM   10225 N  NE    . ARG A 1 2753 ? 241.791 170.928 201.153 1.00 10.98 ? 2753 ARG A NE    1 
ATOM   10226 C  CZ    . ARG A 1 2753 ? 240.575 170.725 200.662 1.00 10.65 ? 2753 ARG A CZ    1 
ATOM   10227 N  NH1   . ARG A 1 2753 ? 239.782 169.787 201.149 1.00 6.72  ? 2753 ARG A NH1   1 
ATOM   10228 N  NH2   . ARG A 1 2753 ? 240.146 171.485 199.660 1.00 7.66  ? 2753 ARG A NH2   1 
ATOM   10229 N  N     . ALA A 1 2754 ? 242.373 175.351 204.426 1.00 4.99  ? 2754 ALA A N     1 
ATOM   10230 C  CA    . ALA A 1 2754 ? 243.038 176.648 204.369 1.00 7.90  ? 2754 ALA A CA    1 
ATOM   10231 C  C     . ALA A 1 2754 ? 243.287 177.210 205.764 1.00 11.07 ? 2754 ALA A C     1 
ATOM   10232 O  O     . ALA A 1 2754 ? 244.367 177.745 206.040 1.00 13.64 ? 2754 ALA A O     1 
ATOM   10233 C  CB    . ALA A 1 2754 ? 242.207 177.621 203.536 1.00 7.03  ? 2754 ALA A CB    1 
ATOM   10234 N  N     . MET A 1 2755 ? 242.299 177.100 206.654 1.00 14.94 ? 2755 MET A N     1 
ATOM   10235 C  CA    . MET A 1 2755 ? 242.426 177.688 207.985 1.00 8.36  ? 2755 MET A CA    1 
ATOM   10236 C  C     . MET A 1 2755 ? 243.374 176.882 208.868 1.00 8.81  ? 2755 MET A C     1 
ATOM   10237 O  O     . MET A 1 2755 ? 244.015 177.439 209.766 1.00 16.92 ? 2755 MET A O     1 
ATOM   10238 C  CB    . MET A 1 2755 ? 241.037 177.832 208.611 1.00 5.82  ? 2755 MET A CB    1 
ATOM   10239 C  CG    . MET A 1 2755 ? 240.993 178.000 210.117 1.00 8.74  ? 2755 MET A CG    1 
ATOM   10240 S  SD    . MET A 1 2755 ? 239.473 177.313 210.799 1.00 14.00 ? 2755 MET A SD    1 
ATOM   10241 C  CE    . MET A 1 2755 ? 239.958 175.626 211.120 1.00 6.15  ? 2755 MET A CE    1 
ATOM   10242 N  N     . LEU A 1 2756 ? 243.496 175.580 208.619 1.00 8.29  ? 2756 LEU A N     1 
ATOM   10243 C  CA    . LEU A 1 2756 ? 244.460 174.778 209.365 1.00 6.53  ? 2756 LEU A CA    1 
ATOM   10244 C  C     . LEU A 1 2756 ? 245.864 174.828 208.775 1.00 11.80 ? 2756 LEU A C     1 
ATOM   10245 O  O     . LEU A 1 2756 ? 246.716 174.039 209.197 1.00 13.50 ? 2756 LEU A O     1 
ATOM   10246 C  CB    . LEU A 1 2756 ? 243.977 173.331 209.468 1.00 6.84  ? 2756 LEU A CB    1 
ATOM   10247 C  CG    . LEU A 1 2756 ? 242.800 173.094 210.419 1.00 9.57  ? 2756 LEU A CG    1 
ATOM   10248 C  CD1   . LEU A 1 2756 ? 242.678 171.631 210.770 1.00 9.10  ? 2756 LEU A CD1   1 
ATOM   10249 C  CD2   . LEU A 1 2756 ? 242.995 173.904 211.687 1.00 9.22  ? 2756 LEU A CD2   1 
ATOM   10250 N  N     . ARG A 1 2757 ? 246.127 175.708 207.806 1.00 15.99 ? 2757 ARG A N     1 
ATOM   10251 C  CA    . ARG A 1 2757 ? 247.505 175.983 207.417 1.00 12.75 ? 2757 ARG A CA    1 
ATOM   10252 C  C     . ARG A 1 2757 ? 248.160 177.012 208.328 1.00 13.07 ? 2757 ARG A C     1 
ATOM   10253 O  O     . ARG A 1 2757 ? 249.376 177.207 208.245 1.00 14.08 ? 2757 ARG A O     1 
ATOM   10254 C  CB    . ARG A 1 2757 ? 247.584 176.455 205.963 1.00 15.33 ? 2757 ARG A CB    1 
ATOM   10255 C  CG    . ARG A 1 2757 ? 247.269 175.382 204.937 1.00 16.27 ? 2757 ARG A CG    1 
ATOM   10256 C  CD    . ARG A 1 2757 ? 247.686 175.808 203.538 1.00 15.47 ? 2757 ARG A CD    1 
ATOM   10257 N  NE    . ARG A 1 2757 ? 246.733 176.714 202.908 1.00 17.47 ? 2757 ARG A NE    1 
ATOM   10258 C  CZ    . ARG A 1 2757 ? 245.705 176.324 202.169 1.00 16.87 ? 2757 ARG A CZ    1 
ATOM   10259 N  NH1   . ARG A 1 2757 ? 245.448 175.043 201.959 1.00 18.66 ? 2757 ARG A NH1   1 
ATOM   10260 N  NH2   . ARG A 1 2757 ? 244.916 177.243 201.621 1.00 16.35 ? 2757 ARG A NH2   1 
ATOM   10261 N  N     . LEU A 1 2758 ? 247.383 177.680 209.185 1.00 13.94 ? 2758 LEU A N     1 
ATOM   10262 C  CA    . LEU A 1 2758 ? 247.969 178.561 210.189 1.00 12.38 ? 2758 LEU A CA    1 
ATOM   10263 C  C     . LEU A 1 2758 ? 248.841 177.774 211.158 1.00 17.81 ? 2758 LEU A C     1 
ATOM   10264 O  O     . LEU A 1 2758 ? 249.943 178.206 211.514 1.00 23.47 ? 2758 LEU A O     1 
ATOM   10265 C  CB    . LEU A 1 2758 ? 246.870 179.309 210.943 1.00 12.05 ? 2758 LEU A CB    1 
ATOM   10266 C  CG    . LEU A 1 2758 ? 245.993 180.280 210.152 1.00 14.46 ? 2758 LEU A CG    1 
ATOM   10267 C  CD1   . LEU A 1 2758 ? 244.937 180.900 211.048 1.00 10.93 ? 2758 LEU A CD1   1 
ATOM   10268 C  CD2   . LEU A 1 2758 ? 246.848 181.361 209.514 1.00 9.94  ? 2758 LEU A CD2   1 
ATOM   10269 N  N     . ILE A 1 2759 ? 248.365 176.610 211.587 1.00 13.68 ? 2759 ILE A N     1 
ATOM   10270 C  CA    . ILE A 1 2759 ? 249.130 175.742 212.476 1.00 13.67 ? 2759 ILE A CA    1 
ATOM   10271 C  C     . ILE A 1 2759 ? 249.527 174.501 211.685 1.00 16.80 ? 2759 ILE A C     1 
ATOM   10272 O  O     . ILE A 1 2759 ? 248.707 173.587 211.520 1.00 22.81 ? 2759 ILE A O     1 
ATOM   10273 C  CB    . ILE A 1 2759 ? 248.326 175.367 213.729 1.00 17.08 ? 2759 ILE A CB    1 
ATOM   10274 C  CG1   . ILE A 1 2759 ? 247.680 176.608 214.351 1.00 16.61 ? 2759 ILE A CG1   1 
ATOM   10275 C  CG2   . ILE A 1 2759 ? 249.220 174.681 214.742 1.00 17.91 ? 2759 ILE A CG2   1 
ATOM   10276 C  CD1   . ILE A 1 2759 ? 248.666 177.633 214.849 1.00 15.71 ? 2759 ILE A CD1   1 
ATOM   10277 N  N     . PRO A 1 2760 ? 250.759 174.429 211.176 1.00 21.10 ? 2760 PRO A N     1 
ATOM   10278 C  CA    . PRO A 1 2760 ? 251.155 173.264 210.367 1.00 16.87 ? 2760 PRO A CA    1 
ATOM   10279 C  C     . PRO A 1 2760 ? 251.050 171.936 211.097 1.00 21.74 ? 2760 PRO A C     1 
ATOM   10280 O  O     . PRO A 1 2760 ? 250.854 170.896 210.454 1.00 24.92 ? 2760 PRO A O     1 
ATOM   10281 C  CB    . PRO A 1 2760 ? 252.607 173.594 209.996 1.00 20.30 ? 2760 PRO A CB    1 
ATOM   10282 C  CG    . PRO A 1 2760 ? 252.635 175.080 209.958 1.00 19.26 ? 2760 PRO A CG    1 
ATOM   10283 C  CD    . PRO A 1 2760 ? 251.747 175.518 211.091 1.00 18.45 ? 2760 PRO A CD    1 
ATOM   10284 N  N     . SER A 1 2761 ? 251.180 171.935 212.422 1.00 16.12 ? 2761 SER A N     1 
ATOM   10285 C  CA    . SER A 1 2761 ? 251.051 170.702 213.188 1.00 16.84 ? 2761 SER A CA    1 
ATOM   10286 C  C     . SER A 1 2761 ? 249.619 170.185 213.250 1.00 16.56 ? 2761 SER A C     1 
ATOM   10287 O  O     . SER A 1 2761 ? 249.409 169.066 213.726 1.00 17.50 ? 2761 SER A O     1 
ATOM   10288 C  CB    . SER A 1 2761 ? 251.587 170.908 214.606 1.00 24.17 ? 2761 SER A CB    1 
ATOM   10289 O  OG    . SER A 1 2761 ? 250.780 171.815 215.333 1.00 26.87 ? 2761 SER A OG    1 
ATOM   10290 N  N     . LEU A 1 2762 ? 248.636 170.964 212.798 1.00 19.10 ? 2762 LEU A N     1 
ATOM   10291 C  CA    . LEU A 1 2762 ? 247.239 170.552 212.839 1.00 14.40 ? 2762 LEU A CA    1 
ATOM   10292 C  C     . LEU A 1 2762 ? 246.664 170.272 211.455 1.00 15.10 ? 2762 LEU A C     1 
ATOM   10293 O  O     . LEU A 1 2762 ? 245.440 170.173 211.315 1.00 16.07 ? 2762 LEU A O     1 
ATOM   10294 C  CB    . LEU A 1 2762 ? 246.397 171.614 213.551 1.00 17.22 ? 2762 LEU A CB    1 
ATOM   10295 C  CG    . LEU A 1 2762 ? 246.615 171.738 215.061 1.00 15.73 ? 2762 LEU A CG    1 
ATOM   10296 C  CD1   . LEU A 1 2762 ? 245.675 172.773 215.654 1.00 13.40 ? 2762 LEU A CD1   1 
ATOM   10297 C  CD2   . LEU A 1 2762 ? 246.443 170.392 215.745 1.00 14.48 ? 2762 LEU A CD2   1 
ATOM   10298 N  N     . ARG A 1 2763 ? 247.512 170.136 210.433 1.00 20.15 ? 2763 ARG A N     1 
ATOM   10299 C  CA    . ARG A 1 2763 ? 247.021 169.896 209.076 1.00 16.82 ? 2763 ARG A CA    1 
ATOM   10300 C  C     . ARG A 1 2763 ? 246.280 168.568 208.975 1.00 14.01 ? 2763 ARG A C     1 
ATOM   10301 O  O     . ARG A 1 2763 ? 245.285 168.458 208.250 1.00 14.55 ? 2763 ARG A O     1 
ATOM   10302 C  CB    . ARG A 1 2763 ? 248.188 169.934 208.089 1.00 18.27 ? 2763 ARG A CB    1 
ATOM   10303 C  CG    . ARG A 1 2763 ? 247.785 169.834 206.625 1.00 25.44 ? 2763 ARG A CG    1 
ATOM   10304 C  CD    . ARG A 1 2763 ? 249.006 169.896 205.715 1.00 26.29 ? 2763 ARG A CD    1 
ATOM   10305 N  NE    . ARG A 1 2763 ? 249.691 171.182 205.787 1.00 26.71 ? 2763 ARG A NE    1 
ATOM   10306 C  CZ    . ARG A 1 2763 ? 249.350 172.249 205.079 1.00 31.13 ? 2763 ARG A CZ    1 
ATOM   10307 N  NH1   . ARG A 1 2763 ? 248.355 172.211 204.208 1.00 32.78 ? 2763 ARG A NH1   1 
ATOM   10308 N  NH2   . ARG A 1 2763 ? 250.033 173.379 205.239 1.00 31.64 ? 2763 ARG A NH2   1 
ATOM   10309 N  N     . THR A 1 2764 ? 246.754 167.549 209.693 1.00 14.07 ? 2764 THR A N     1 
ATOM   10310 C  CA    . THR A 1 2764 ? 246.172 166.214 209.582 1.00 12.63 ? 2764 THR A CA    1 
ATOM   10311 C  C     . THR A 1 2764 ? 244.717 166.186 210.036 1.00 10.52 ? 2764 THR A C     1 
ATOM   10312 O  O     . THR A 1 2764 ? 243.920 165.394 209.519 1.00 17.60 ? 2764 THR A O     1 
ATOM   10313 C  CB    . THR A 1 2764 ? 247.009 165.218 210.390 1.00 19.33 ? 2764 THR A CB    1 
ATOM   10314 O  OG1   . THR A 1 2764 ? 248.347 165.195 209.881 1.00 26.28 ? 2764 THR A OG1   1 
ATOM   10315 C  CG2   . THR A 1 2764 ? 246.431 163.817 210.304 1.00 15.79 ? 2764 THR A CG2   1 
ATOM   10316 N  N     . TYR A 1 2765 ? 244.343 167.046 210.981 1.00 11.45 ? 2765 TYR A N     1 
ATOM   10317 C  CA    . TYR A 1 2765 ? 243.002 167.020 211.550 1.00 10.33 ? 2765 TYR A CA    1 
ATOM   10318 C  C     . TYR A 1 2765 ? 241.981 167.810 210.733 1.00 6.62  ? 2765 TYR A C     1 
ATOM   10319 O  O     . TYR A 1 2765 ? 240.912 168.133 211.262 1.00 6.02  ? 2765 TYR A O     1 
ATOM   10320 C  CB    . TYR A 1 2765 ? 243.035 167.538 212.990 1.00 6.89  ? 2765 TYR A CB    1 
ATOM   10321 C  CG    . TYR A 1 2765 ? 243.973 166.775 213.894 1.00 7.37  ? 2765 TYR A CG    1 
ATOM   10322 C  CD1   . TYR A 1 2765 ? 243.636 165.517 214.369 1.00 8.83  ? 2765 TYR A CD1   1 
ATOM   10323 C  CD2   . TYR A 1 2765 ? 245.194 167.314 214.276 1.00 8.38  ? 2765 TYR A CD2   1 
ATOM   10324 C  CE1   . TYR A 1 2765 ? 244.488 164.813 215.195 1.00 9.18  ? 2765 TYR A CE1   1 
ATOM   10325 C  CE2   . TYR A 1 2765 ? 246.052 166.620 215.102 1.00 8.39  ? 2765 TYR A CE2   1 
ATOM   10326 C  CZ    . TYR A 1 2765 ? 245.693 165.369 215.560 1.00 9.98  ? 2765 TYR A CZ    1 
ATOM   10327 O  OH    . TYR A 1 2765 ? 246.543 164.670 216.384 1.00 19.83 ? 2765 TYR A OH    1 
ATOM   10328 N  N     . ALA A 1 2766 ? 242.271 168.121 209.469 1.00 7.99  ? 2766 ALA A N     1 
ATOM   10329 C  CA    . ALA A 1 2766 ? 241.327 168.892 208.663 1.00 6.13  ? 2766 ALA A CA    1 
ATOM   10330 C  C     . ALA A 1 2766 ? 240.072 168.084 208.351 1.00 5.47  ? 2766 ALA A C     1 
ATOM   10331 O  O     . ALA A 1 2766 ? 238.950 168.578 208.511 1.00 5.77  ? 2766 ALA A O     1 
ATOM   10332 C  CB    . ALA A 1 2766 ? 241.997 169.364 207.374 1.00 5.44  ? 2766 ALA A CB    1 
ATOM   10333 N  N     . GLU A 1 2767 ? 240.242 166.844 207.891 1.00 6.96  ? 2767 GLU A N     1 
ATOM   10334 C  CA    . GLU A 1 2767 ? 239.083 166.018 207.560 1.00 3.66  ? 2767 GLU A CA    1 
ATOM   10335 C  C     . GLU A 1 2767 ? 238.220 165.687 208.772 1.00 3.11  ? 2767 GLU A C     1 
ATOM   10336 O  O     . GLU A 1 2767 ? 236.992 165.862 208.688 1.00 3.53  ? 2767 GLU A O     1 
ATOM   10337 C  CB    . GLU A 1 2767 ? 239.544 164.750 206.831 1.00 8.17  ? 2767 GLU A CB    1 
ATOM   10338 C  CG    . GLU A 1 2767 ? 239.796 164.943 205.349 1.00 12.78 ? 2767 GLU A CG    1 
ATOM   10339 C  CD    . GLU A 1 2767 ? 240.611 163.817 204.746 1.00 28.46 ? 2767 GLU A CD    1 
ATOM   10340 O  OE1   . GLU A 1 2767 ? 240.769 163.794 203.507 1.00 31.81 ? 2767 GLU A OE1   1 
ATOM   10341 O  OE2   . GLU A 1 2767 ? 241.094 162.955 205.509 1.00 23.90 ? 2767 GLU A OE2   1 
ATOM   10342 N  N     . PRO A 1 2768 ? 238.759 165.205 209.901 1.00 6.68  ? 2768 PRO A N     1 
ATOM   10343 C  CA    . PRO A 1 2768 ? 237.888 164.974 211.068 1.00 2.82  ? 2768 PRO A CA    1 
ATOM   10344 C  C     . PRO A 1 2768 ? 237.223 166.235 211.593 1.00 1.84  ? 2768 PRO A C     1 
ATOM   10345 O  O     . PRO A 1 2768 ? 236.095 166.162 212.095 1.00 2.17  ? 2768 PRO A O     1 
ATOM   10346 C  CB    . PRO A 1 2768 ? 238.839 164.363 212.107 1.00 2.41  ? 2768 PRO A CB    1 
ATOM   10347 C  CG    . PRO A 1 2768 ? 240.197 164.731 211.657 1.00 4.35  ? 2768 PRO A CG    1 
ATOM   10348 C  CD    . PRO A 1 2768 ? 240.139 164.761 210.168 1.00 5.04  ? 2768 PRO A CD    1 
ATOM   10349 N  N     . LEU A 1 2769 ? 237.888 167.388 211.501 1.00 2.10  ? 2769 LEU A N     1 
ATOM   10350 C  CA    . LEU A 1 2769 ? 237.266 168.632 211.940 1.00 2.30  ? 2769 LEU A CA    1 
ATOM   10351 C  C     . LEU A 1 2769 ? 236.053 168.972 211.084 1.00 2.67  ? 2769 LEU A C     1 
ATOM   10352 O  O     . LEU A 1 2769 ? 235.010 169.383 211.607 1.00 3.98  ? 2769 LEU A O     1 
ATOM   10353 C  CB    . LEU A 1 2769 ? 238.283 169.772 211.904 1.00 2.87  ? 2769 LEU A CB    1 
ATOM   10354 C  CG    . LEU A 1 2769 ? 237.783 171.133 212.391 1.00 1.65  ? 2769 LEU A CG    1 
ATOM   10355 C  CD1   . LEU A 1 2769 ? 237.606 171.127 213.900 1.00 0.72  ? 2769 LEU A CD1   1 
ATOM   10356 C  CD2   . LEU A 1 2769 ? 238.726 172.239 211.957 1.00 1.71  ? 2769 LEU A CD2   1 
ATOM   10357 N  N     . THR A 1 2770 ? 236.172 168.808 209.764 1.00 2.01  ? 2770 THR A N     1 
ATOM   10358 C  CA    . THR A 1 2770 ? 235.032 169.034 208.882 1.00 1.33  ? 2770 THR A CA    1 
ATOM   10359 C  C     . THR A 1 2770 ? 233.922 168.025 209.146 1.00 1.51  ? 2770 THR A C     1 
ATOM   10360 O  O     . THR A 1 2770 ? 232.741 168.389 209.186 1.00 0.98  ? 2770 THR A O     1 
ATOM   10361 C  CB    . THR A 1 2770 ? 235.476 168.969 207.420 1.00 1.88  ? 2770 THR A CB    1 
ATOM   10362 O  OG1   . THR A 1 2770 ? 236.523 169.919 207.192 1.00 1.76  ? 2770 THR A OG1   1 
ATOM   10363 C  CG2   . THR A 1 2770 ? 234.311 169.275 206.491 1.00 0.71  ? 2770 THR A CG2   1 
ATOM   10364 N  N     . ALA A 1 2771 ? 234.285 166.754 209.332 1.00 1.48  ? 2771 ALA A N     1 
ATOM   10365 C  CA    . ALA A 1 2771 ? 233.282 165.719 209.560 1.00 1.83  ? 2771 ALA A CA    1 
ATOM   10366 C  C     . ALA A 1 2771 ? 232.510 165.970 210.847 1.00 2.31  ? 2771 ALA A C     1 
ATOM   10367 O  O     . ALA A 1 2771 ? 231.284 165.811 210.886 1.00 2.70  ? 2771 ALA A O     1 
ATOM   10368 C  CB    . ALA A 1 2771 ? 233.947 164.344 209.590 1.00 2.56  ? 2771 ALA A CB    1 
ATOM   10369 N  N     . ALA A 1 2772 ? 233.210 166.366 211.912 1.00 1.49  ? 2772 ALA A N     1 
ATOM   10370 C  CA    . ALA A 1 2772 ? 232.532 166.717 213.154 1.00 1.23  ? 2772 ALA A CA    1 
ATOM   10371 C  C     . ALA A 1 2772 ? 231.623 167.924 212.961 1.00 0.56  ? 2772 ALA A C     1 
ATOM   10372 O  O     . ALA A 1 2772 ? 230.513 167.969 213.503 1.00 0.66  ? 2772 ALA A O     1 
ATOM   10373 C  CB    . ALA A 1 2772 ? 233.559 166.981 214.255 1.00 1.02  ? 2772 ALA A CB    1 
ATOM   10374 N  N     . MET A 1 2773 ? 232.081 168.912 212.192 1.00 1.06  ? 2773 MET A N     1 
ATOM   10375 C  CA    . MET A 1 2773 ? 231.262 170.088 211.916 1.00 0.57  ? 2773 MET A CA    1 
ATOM   10376 C  C     . MET A 1 2773 ? 229.974 169.706 211.199 1.00 0.79  ? 2773 MET A C     1 
ATOM   10377 O  O     . MET A 1 2773 ? 228.883 170.141 211.582 1.00 0.66  ? 2773 MET A O     1 
ATOM   10378 C  CB    . MET A 1 2773 ? 232.059 171.085 211.078 1.00 0.58  ? 2773 MET A CB    1 
ATOM   10379 C  CG    . MET A 1 2773 ? 232.880 172.067 211.876 1.00 0.52  ? 2773 MET A CG    1 
ATOM   10380 S  SD    . MET A 1 2773 ? 233.708 173.252 210.805 1.00 7.16  ? 2773 MET A SD    1 
ATOM   10381 C  CE    . MET A 1 2773 ? 234.155 174.513 211.981 1.00 0.64  ? 2773 MET A CE    1 
ATOM   10382 N  N     . VAL A 1 2774 ? 230.085 168.883 210.155 1.00 2.17  ? 2774 VAL A N     1 
ATOM   10383 C  CA    . VAL A 1 2774 ? 228.910 168.501 209.377 1.00 1.02  ? 2774 VAL A CA    1 
ATOM   10384 C  C     . VAL A 1 2774 ? 227.970 167.640 210.212 1.00 0.98  ? 2774 VAL A C     1 
ATOM   10385 O  O     . VAL A 1 2774 ? 226.746 167.805 210.158 1.00 2.20  ? 2774 VAL A O     1 
ATOM   10386 C  CB    . VAL A 1 2774 ? 229.339 167.790 208.080 1.00 1.28  ? 2774 VAL A CB    1 
ATOM   10387 C  CG1   . VAL A 1 2774 ? 228.131 167.236 207.344 1.00 1.91  ? 2774 VAL A CG1   1 
ATOM   10388 C  CG2   . VAL A 1 2774 ? 230.113 168.743 207.185 1.00 0.66  ? 2774 VAL A CG2   1 
ATOM   10389 N  N     . GLU A 1 2775 ? 228.520 166.714 210.999 1.00 0.74  ? 2775 GLU A N     1 
ATOM   10390 C  CA    . GLU A 1 2775 ? 227.673 165.819 211.782 1.00 1.42  ? 2775 GLU A CA    1 
ATOM   10391 C  C     . GLU A 1 2775 ? 226.868 166.586 212.824 1.00 1.82  ? 2775 GLU A C     1 
ATOM   10392 O  O     . GLU A 1 2775 ? 225.650 166.405 212.937 1.00 2.40  ? 2775 GLU A O     1 
ATOM   10393 C  CB    . GLU A 1 2775 ? 228.518 164.735 212.449 1.00 4.37  ? 2775 GLU A CB    1 
ATOM   10394 C  CG    . GLU A 1 2775 ? 227.681 163.726 213.214 1.00 3.60  ? 2775 GLU A CG    1 
ATOM   10395 C  CD    . GLU A 1 2775 ? 228.506 162.625 213.831 1.00 11.78 ? 2775 GLU A CD    1 
ATOM   10396 O  OE1   . GLU A 1 2775 ? 229.743 162.651 213.679 1.00 14.99 ? 2775 GLU A OE1   1 
ATOM   10397 O  OE2   . GLU A 1 2775 ? 227.917 161.724 214.465 1.00 18.48 ? 2775 GLU A OE2   1 
ATOM   10398 N  N     . PHE A 1 2776 ? 227.529 167.449 213.599 1.00 0.71  ? 2776 PHE A N     1 
ATOM   10399 C  CA    . PHE A 1 2776 ? 226.811 168.184 214.633 1.00 0.67  ? 2776 PHE A CA    1 
ATOM   10400 C  C     . PHE A 1 2776 ? 225.824 169.175 214.028 1.00 0.88  ? 2776 PHE A C     1 
ATOM   10401 O  O     . PHE A 1 2776 ? 224.721 169.358 214.557 1.00 1.21  ? 2776 PHE A O     1 
ATOM   10402 C  CB    . PHE A 1 2776 ? 227.783 168.904 215.566 1.00 0.78  ? 2776 PHE A CB    1 
ATOM   10403 C  CG    . PHE A 1 2776 ? 227.102 169.584 216.712 1.00 1.03  ? 2776 PHE A CG    1 
ATOM   10404 C  CD1   . PHE A 1 2776 ? 226.666 168.853 217.804 1.00 2.23  ? 2776 PHE A CD1   1 
ATOM   10405 C  CD2   . PHE A 1 2776 ? 226.857 170.946 216.682 1.00 0.47  ? 2776 PHE A CD2   1 
ATOM   10406 C  CE1   . PHE A 1 2776 ? 226.017 169.472 218.851 1.00 2.64  ? 2776 PHE A CE1   1 
ATOM   10407 C  CE2   . PHE A 1 2776 ? 226.211 171.567 217.726 1.00 0.91  ? 2776 PHE A CE2   1 
ATOM   10408 C  CZ    . PHE A 1 2776 ? 225.789 170.829 218.812 1.00 2.02  ? 2776 PHE A CZ    1 
ATOM   10409 N  N     . TYR A 1 2777 ? 226.205 169.833 212.931 1.00 1.01  ? 2777 TYR A N     1 
ATOM   10410 C  CA    . TYR A 1 2777 ? 225.294 170.771 212.283 1.00 0.78  ? 2777 TYR A CA    1 
ATOM   10411 C  C     . TYR A 1 2777 ? 224.051 170.061 211.762 1.00 0.96  ? 2777 TYR A C     1 
ATOM   10412 O  O     . TYR A 1 2777 ? 222.932 170.567 211.905 1.00 1.17  ? 2777 TYR A O     1 
ATOM   10413 C  CB    . TYR A 1 2777 ? 226.007 171.499 211.146 1.00 0.59  ? 2777 TYR A CB    1 
ATOM   10414 C  CG    . TYR A 1 2777 ? 225.068 172.061 210.108 1.00 0.65  ? 2777 TYR A CG    1 
ATOM   10415 C  CD1   . TYR A 1 2777 ? 224.311 173.194 210.372 1.00 0.71  ? 2777 TYR A CD1   1 
ATOM   10416 C  CD2   . TYR A 1 2777 ? 224.929 171.457 208.866 1.00 0.78  ? 2777 TYR A CD2   1 
ATOM   10417 C  CE1   . TYR A 1 2777 ? 223.447 173.708 209.433 1.00 0.82  ? 2777 TYR A CE1   1 
ATOM   10418 C  CE2   . TYR A 1 2777 ? 224.068 171.968 207.918 1.00 0.64  ? 2777 TYR A CE2   1 
ATOM   10419 C  CZ    . TYR A 1 2777 ? 223.330 173.094 208.208 1.00 0.60  ? 2777 TYR A CZ    1 
ATOM   10420 O  OH    . TYR A 1 2777 ? 222.468 173.609 207.270 1.00 3.45  ? 2777 TYR A OH    1 
ATOM   10421 N  N     . THR A 1 2778 ? 224.229 168.892 211.142 1.00 1.00  ? 2778 THR A N     1 
ATOM   10422 C  CA    . THR A 1 2778 ? 223.085 168.133 210.648 1.00 1.14  ? 2778 THR A CA    1 
ATOM   10423 C  C     . THR A 1 2778 ? 222.202 167.660 211.795 1.00 1.18  ? 2778 THR A C     1 
ATOM   10424 O  O     . THR A 1 2778 ? 220.970 167.729 211.712 1.00 1.51  ? 2778 THR A O     1 
ATOM   10425 C  CB    . THR A 1 2778 ? 223.561 166.943 209.814 1.00 1.00  ? 2778 THR A CB    1 
ATOM   10426 O  OG1   . THR A 1 2778 ? 224.413 167.406 208.761 1.00 1.18  ? 2778 THR A OG1   1 
ATOM   10427 C  CG2   . THR A 1 2778 ? 222.378 166.208 209.208 1.00 4.63  ? 2778 THR A CG2   1 
ATOM   10428 N  N     . MET A 1 2779 ? 222.817 167.178 212.878 1.00 1.58  ? 2779 MET A N     1 
ATOM   10429 C  CA    . MET A 1 2779 ? 222.047 166.723 214.030 1.00 0.97  ? 2779 MET A CA    1 
ATOM   10430 C  C     . MET A 1 2779 ? 221.260 167.866 214.657 1.00 1.68  ? 2779 MET A C     1 
ATOM   10431 O  O     . MET A 1 2779 ? 220.091 167.695 215.021 1.00 3.57  ? 2779 MET A O     1 
ATOM   10432 C  CB    . MET A 1 2779 ? 222.979 166.084 215.059 1.00 0.92  ? 2779 MET A CB    1 
ATOM   10433 C  CG    . MET A 1 2779 ? 223.444 164.690 214.683 1.00 1.84  ? 2779 MET A CG    1 
ATOM   10434 S  SD    . MET A 1 2779 ? 224.953 164.202 215.538 1.00 16.87 ? 2779 MET A SD    1 
ATOM   10435 C  CE    . MET A 1 2779 ? 224.591 164.747 217.201 1.00 5.57  ? 2779 MET A CE    1 
ATOM   10436 N  N     . SER A 1 2780 ? 221.884 169.037 214.793 1.00 1.27  ? 2780 SER A N     1 
ATOM   10437 C  CA    . SER A 1 2780 ? 221.191 170.184 215.369 1.00 1.34  ? 2780 SER A CA    1 
ATOM   10438 C  C     . SER A 1 2780 ? 220.052 170.650 214.473 1.00 1.78  ? 2780 SER A C     1 
ATOM   10439 O  O     . SER A 1 2780 ? 218.978 171.018 214.963 1.00 3.69  ? 2780 SER A O     1 
ATOM   10440 C  CB    . SER A 1 2780 ? 222.178 171.323 215.619 1.00 2.45  ? 2780 SER A CB    1 
ATOM   10441 O  OG    . SER A 1 2780 ? 223.254 170.898 216.434 1.00 3.03  ? 2780 SER A OG    1 
ATOM   10442 N  N     . GLN A 1 2781 ? 220.270 170.643 213.157 1.00 1.89  ? 2781 GLN A N     1 
ATOM   10443 C  CA    . GLN A 1 2781 ? 219.235 171.080 212.229 1.00 1.39  ? 2781 GLN A CA    1 
ATOM   10444 C  C     . GLN A 1 2781 ? 218.031 170.144 212.272 1.00 2.31  ? 2781 GLN A C     1 
ATOM   10445 O  O     . GLN A 1 2781 ? 216.886 170.586 212.131 1.00 3.16  ? 2781 GLN A O     1 
ATOM   10446 C  CB    . GLN A 1 2781 ? 219.813 171.172 210.818 1.00 1.60  ? 2781 GLN A CB    1 
ATOM   10447 C  CG    . GLN A 1 2781 ? 218.866 171.739 209.781 1.00 1.82  ? 2781 GLN A CG    1 
ATOM   10448 C  CD    . GLN A 1 2781 ? 219.508 171.841 208.415 1.00 4.95  ? 2781 GLN A CD    1 
ATOM   10449 O  OE1   . GLN A 1 2781 ? 220.043 170.862 207.896 1.00 10.03 ? 2781 GLN A OE1   1 
ATOM   10450 N  NE2   . GLN A 1 2781 ? 219.461 173.029 207.825 1.00 2.63  ? 2781 GLN A NE2   1 
ATOM   10451 N  N     . GLU A 1 2782 ? 218.274 168.847 212.460 1.00 2.90  ? 2782 GLU A N     1 
ATOM   10452 C  CA    . GLU A 1 2782 ? 217.181 167.897 212.620 1.00 2.51  ? 2782 GLU A CA    1 
ATOM   10453 C  C     . GLU A 1 2782 ? 216.535 168.016 213.994 1.00 4.09  ? 2782 GLU A C     1 
ATOM   10454 O  O     . GLU A 1 2782 ? 215.305 167.988 214.110 1.00 4.75  ? 2782 GLU A O     1 
ATOM   10455 C  CB    . GLU A 1 2782 ? 217.699 166.474 212.375 1.00 2.13  ? 2782 GLU A CB    1 
ATOM   10456 C  CG    . GLU A 1 2782 ? 216.680 165.344 212.540 1.00 9.10  ? 2782 GLU A CG    1 
ATOM   10457 C  CD    . GLU A 1 2782 ? 216.429 164.954 213.985 1.00 17.80 ? 2782 GLU A CD    1 
ATOM   10458 O  OE1   . GLU A 1 2782 ? 217.412 164.736 214.726 1.00 19.20 ? 2782 GLU A OE1   1 
ATOM   10459 O  OE2   . GLU A 1 2782 ? 215.248 164.862 214.379 1.00 21.23 ? 2782 GLU A OE2   1 
ATOM   10460 N  N     . ARG A 1 2783 ? 217.349 168.150 215.044 1.00 3.13  ? 2783 ARG A N     1 
ATOM   10461 C  CA    . ARG A 1 2783 ? 216.829 168.159 216.408 1.00 2.83  ? 2783 ARG A CA    1 
ATOM   10462 C  C     . ARG A 1 2783 ? 215.937 169.368 216.666 1.00 2.92  ? 2783 ARG A C     1 
ATOM   10463 O  O     . ARG A 1 2783 ? 214.884 169.243 217.301 1.00 8.44  ? 2783 ARG A O     1 
ATOM   10464 C  CB    . ARG A 1 2783 ? 217.990 168.122 217.402 1.00 4.03  ? 2783 ARG A CB    1 
ATOM   10465 C  CG    . ARG A 1 2783 ? 217.598 168.289 218.859 1.00 3.38  ? 2783 ARG A CG    1 
ATOM   10466 C  CD    . ARG A 1 2783 ? 216.957 167.043 219.438 1.00 3.05  ? 2783 ARG A CD    1 
ATOM   10467 N  NE    . ARG A 1 2783 ? 216.753 167.154 220.879 1.00 6.69  ? 2783 ARG A NE    1 
ATOM   10468 C  CZ    . ARG A 1 2783 ? 215.872 167.957 221.462 1.00 9.55  ? 2783 ARG A CZ    1 
ATOM   10469 N  NH1   . ARG A 1 2783 ? 215.057 168.725 220.756 1.00 7.95  ? 2783 ARG A NH1   1 
ATOM   10470 N  NH2   . ARG A 1 2783 ? 215.803 167.987 222.790 1.00 8.37  ? 2783 ARG A NH2   1 
ATOM   10471 N  N     . PHE A 1 2784 ? 216.337 170.544 216.191 1.00 2.27  ? 2784 PHE A N     1 
ATOM   10472 C  CA    . PHE A 1 2784 ? 215.610 171.783 216.441 1.00 1.95  ? 2784 PHE A CA    1 
ATOM   10473 C  C     . PHE A 1 2784 ? 215.102 172.342 215.123 1.00 3.06  ? 2784 PHE A C     1 
ATOM   10474 O  O     . PHE A 1 2784 ? 215.886 172.565 214.195 1.00 9.15  ? 2784 PHE A O     1 
ATOM   10475 C  CB    . PHE A 1 2784 ? 216.497 172.800 217.160 1.00 2.12  ? 2784 PHE A CB    1 
ATOM   10476 C  CG    . PHE A 1 2784 ? 217.212 172.238 218.351 1.00 1.70  ? 2784 PHE A CG    1 
ATOM   10477 C  CD1   . PHE A 1 2784 ? 216.510 171.885 219.489 1.00 1.74  ? 2784 PHE A CD1   1 
ATOM   10478 C  CD2   . PHE A 1 2784 ? 218.582 172.054 218.333 1.00 2.60  ? 2784 PHE A CD2   1 
ATOM   10479 C  CE1   . PHE A 1 2784 ? 217.160 171.364 220.586 1.00 2.30  ? 2784 PHE A CE1   1 
ATOM   10480 C  CE2   . PHE A 1 2784 ? 219.237 171.533 219.430 1.00 2.92  ? 2784 PHE A CE2   1 
ATOM   10481 C  CZ    . PHE A 1 2784 ? 218.527 171.191 220.558 1.00 1.90  ? 2784 PHE A CZ    1 
ATOM   10482 N  N     . THR A 1 2785 ? 213.794 172.570 215.045 1.00 2.57  ? 2785 THR A N     1 
ATOM   10483 C  CA    . THR A 1 2785 ? 213.136 173.025 213.831 1.00 2.81  ? 2785 THR A CA    1 
ATOM   10484 C  C     . THR A 1 2785 ? 212.202 174.181 214.163 1.00 3.35  ? 2785 THR A C     1 
ATOM   10485 O  O     . THR A 1 2785 ? 211.972 174.506 215.331 1.00 3.46  ? 2785 THR A O     1 
ATOM   10486 C  CB    . THR A 1 2785 ? 212.352 171.887 213.155 1.00 4.47  ? 2785 THR A CB    1 
ATOM   10487 O  OG1   . THR A 1 2785 ? 211.296 171.451 214.019 1.00 4.49  ? 2785 THR A OG1   1 
ATOM   10488 C  CG2   . THR A 1 2785 ? 213.265 170.710 212.848 1.00 1.83  ? 2785 THR A CG2   1 
ATOM   10489 N  N     . GLN A 1 2786 ? 211.657 174.800 213.114 1.00 4.90  ? 2786 GLN A N     1 
ATOM   10490 C  CA    . GLN A 1 2786 ? 210.741 175.920 213.301 1.00 3.99  ? 2786 GLN A CA    1 
ATOM   10491 C  C     . GLN A 1 2786 ? 209.455 175.509 214.002 1.00 6.05  ? 2786 GLN A C     1 
ATOM   10492 O  O     . GLN A 1 2786 ? 208.729 176.378 214.495 1.00 9.43  ? 2786 GLN A O     1 
ATOM   10493 C  CB    . GLN A 1 2786 ? 210.404 176.568 211.957 1.00 6.59  ? 2786 GLN A CB    1 
ATOM   10494 C  CG    . GLN A 1 2786 ? 211.500 177.445 211.389 1.00 11.57 ? 2786 GLN A CG    1 
ATOM   10495 C  CD    . GLN A 1 2786 ? 211.000 178.353 210.281 1.00 14.26 ? 2786 GLN A CD    1 
ATOM   10496 O  OE1   . GLN A 1 2786 ? 211.370 178.193 209.120 1.00 21.52 ? 2786 GLN A OE1   1 
ATOM   10497 N  NE2   . GLN A 1 2786 ? 210.159 179.316 210.639 1.00 10.89 ? 2786 GLN A NE2   1 
ATOM   10498 N  N     . ASP A 1 2787 ? 209.150 174.210 214.047 1.00 6.27  ? 2787 ASP A N     1 
ATOM   10499 C  CA    . ASP A 1 2787 ? 207.955 173.756 214.749 1.00 5.00  ? 2787 ASP A CA    1 
ATOM   10500 C  C     . ASP A 1 2787 ? 208.052 174.038 216.242 1.00 8.57  ? 2787 ASP A C     1 
ATOM   10501 O  O     . ASP A 1 2787 ? 207.070 174.455 216.867 1.00 7.65  ? 2787 ASP A O     1 
ATOM   10502 C  CB    . ASP A 1 2787 ? 207.732 172.265 214.496 1.00 6.04  ? 2787 ASP A CB    1 
ATOM   10503 C  CG    . ASP A 1 2787 ? 207.654 171.929 213.021 1.00 23.05 ? 2787 ASP A CG    1 
ATOM   10504 O  OD1   . ASP A 1 2787 ? 206.604 172.203 212.401 1.00 21.23 ? 2787 ASP A OD1   1 
ATOM   10505 O  OD2   . ASP A 1 2787 ? 208.642 171.390 212.479 1.00 27.17 ? 2787 ASP A OD2   1 
ATOM   10506 N  N     . THR A 1 2788 ? 209.228 173.818 216.833 1.00 5.74  ? 2788 THR A N     1 
ATOM   10507 C  CA    . THR A 1 2788 ? 209.402 174.070 218.259 1.00 4.40  ? 2788 THR A CA    1 
ATOM   10508 C  C     . THR A 1 2788 ? 209.440 175.567 218.545 1.00 5.41  ? 2788 THR A C     1 
ATOM   10509 O  O     . THR A 1 2788 ? 208.618 176.086 219.308 1.00 5.92  ? 2788 THR A O     1 
ATOM   10510 C  CB    . THR A 1 2788 ? 210.677 173.386 218.762 1.00 6.57  ? 2788 THR A CB    1 
ATOM   10511 O  OG1   . THR A 1 2788 ? 210.465 171.973 218.838 1.00 17.88 ? 2788 THR A OG1   1 
ATOM   10512 C  CG2   . THR A 1 2788 ? 211.045 173.899 220.143 1.00 4.56  ? 2788 THR A CG2   1 
ATOM   10513 N  N     . GLN A 1 2789 ? 210.387 176.276 217.941 1.00 5.59  ? 2789 GLN A N     1 
ATOM   10514 C  CA    . GLN A 1 2789 ? 210.520 177.712 218.120 1.00 5.69  ? 2789 GLN A CA    1 
ATOM   10515 C  C     . GLN A 1 2789 ? 210.705 178.390 216.772 1.00 5.67  ? 2789 GLN A C     1 
ATOM   10516 O  O     . GLN A 1 2789 ? 211.322 177.823 215.866 1.00 6.72  ? 2789 GLN A O     1 
ATOM   10517 C  CB    . GLN A 1 2789 ? 211.703 178.052 219.038 1.00 2.62  ? 2789 GLN A CB    1 
ATOM   10518 C  CG    . GLN A 1 2789 ? 211.578 177.478 220.436 1.00 2.26  ? 2789 GLN A CG    1 
ATOM   10519 C  CD    . GLN A 1 2789 ? 210.593 178.243 221.300 1.00 5.08  ? 2789 GLN A CD    1 
ATOM   10520 O  OE1   . GLN A 1 2789 ? 210.157 179.338 220.950 1.00 5.06  ? 2789 GLN A OE1   1 
ATOM   10521 N  NE2   . GLN A 1 2789 ? 210.232 177.661 222.436 1.00 3.22  ? 2789 GLN A NE2   1 
ATOM   10522 N  N     . PRO A 1 2790 ? 210.185 179.611 216.614 1.00 7.72  ? 2790 PRO A N     1 
ATOM   10523 C  CA    . PRO A 1 2790 ? 210.254 180.282 215.307 1.00 4.22  ? 2790 PRO A CA    1 
ATOM   10524 C  C     . PRO A 1 2790 ? 211.657 180.652 214.868 1.00 3.19  ? 2790 PRO A C     1 
ATOM   10525 O  O     . PRO A 1 2790 ? 211.849 180.937 213.681 1.00 8.61  ? 2790 PRO A O     1 
ATOM   10526 C  CB    . PRO A 1 2790 ? 209.397 181.535 215.518 1.00 4.69  ? 2790 PRO A CB    1 
ATOM   10527 C  CG    . PRO A 1 2790 ? 209.521 181.808 216.972 1.00 8.24  ? 2790 PRO A CG    1 
ATOM   10528 C  CD    . PRO A 1 2790 ? 209.521 180.454 217.622 1.00 4.74  ? 2790 PRO A CD    1 
ATOM   10529 N  N     . HIS A 1 2791 ? 212.631 180.682 215.774 1.00 2.86  ? 2791 HIS A N     1 
ATOM   10530 C  CA    . HIS A 1 2791 ? 213.994 181.070 215.442 1.00 1.66  ? 2791 HIS A CA    1 
ATOM   10531 C  C     . HIS A 1 2791 ? 214.943 179.882 215.379 1.00 1.74  ? 2791 HIS A C     1 
ATOM   10532 O  O     . HIS A 1 2791 ? 216.163 180.074 215.358 1.00 5.42  ? 2791 HIS A O     1 
ATOM   10533 C  CB    . HIS A 1 2791 ? 214.505 182.109 216.444 1.00 1.50  ? 2791 HIS A CB    1 
ATOM   10534 C  CG    . HIS A 1 2791 ? 214.627 181.596 217.843 1.00 1.24  ? 2791 HIS A CG    1 
ATOM   10535 N  ND1   . HIS A 1 2791 ? 213.538 181.413 218.668 1.00 1.74  ? 2791 HIS A ND1   1 
ATOM   10536 C  CD2   . HIS A 1 2791 ? 215.711 181.235 218.568 1.00 0.98  ? 2791 HIS A CD2   1 
ATOM   10537 C  CE1   . HIS A 1 2791 ? 213.946 180.957 219.838 1.00 1.14  ? 2791 HIS A CE1   1 
ATOM   10538 N  NE2   . HIS A 1 2791 ? 215.261 180.840 219.803 1.00 0.53  ? 2791 HIS A NE2   1 
ATOM   10539 N  N     . TYR A 1 2792 ? 214.417 178.658 215.349 1.00 2.23  ? 2792 TYR A N     1 
ATOM   10540 C  CA    . TYR A 1 2792 ? 215.247 177.459 215.242 1.00 2.53  ? 2792 TYR A CA    1 
ATOM   10541 C  C     . TYR A 1 2792 ? 215.492 177.140 213.767 1.00 3.28  ? 2792 TYR A C     1 
ATOM   10542 O  O     . TYR A 1 2792 ? 215.007 176.153 213.213 1.00 5.93  ? 2792 TYR A O     1 
ATOM   10543 C  CB    . TYR A 1 2792 ? 214.590 176.289 215.964 1.00 2.30  ? 2792 TYR A CB    1 
ATOM   10544 C  CG    . TYR A 1 2792 ? 214.691 176.326 217.473 1.00 2.24  ? 2792 TYR A CG    1 
ATOM   10545 C  CD1   . TYR A 1 2792 ? 215.226 177.426 218.134 1.00 1.74  ? 2792 TYR A CD1   1 
ATOM   10546 C  CD2   . TYR A 1 2792 ? 214.243 175.259 218.239 1.00 1.79  ? 2792 TYR A CD2   1 
ATOM   10547 C  CE1   . TYR A 1 2792 ? 215.316 177.456 219.512 1.00 1.03  ? 2792 TYR A CE1   1 
ATOM   10548 C  CE2   . TYR A 1 2792 ? 214.328 175.280 219.614 1.00 2.01  ? 2792 TYR A CE2   1 
ATOM   10549 C  CZ    . TYR A 1 2792 ? 214.864 176.378 220.248 1.00 2.55  ? 2792 TYR A CZ    1 
ATOM   10550 O  OH    . TYR A 1 2792 ? 214.946 176.394 221.619 1.00 2.66  ? 2792 TYR A OH    1 
ATOM   10551 N  N     . ILE A 1 2793 ? 216.260 178.015 213.125 1.00 3.26  ? 2793 ILE A N     1 
ATOM   10552 C  CA    . ILE A 1 2793 ? 216.672 177.840 211.738 1.00 2.38  ? 2793 ILE A CA    1 
ATOM   10553 C  C     . ILE A 1 2793 ? 218.182 177.681 211.731 1.00 2.18  ? 2793 ILE A C     1 
ATOM   10554 O  O     . ILE A 1 2793 ? 218.915 178.595 212.127 1.00 4.14  ? 2793 ILE A O     1 
ATOM   10555 C  CB    . ILE A 1 2793 ? 216.243 179.012 210.842 1.00 4.89  ? 2793 ILE A CB    1 
ATOM   10556 C  CG1   . ILE A 1 2793 ? 214.721 179.137 210.780 1.00 3.34  ? 2793 ILE A CG1   1 
ATOM   10557 C  CG2   . ILE A 1 2793 ? 216.823 178.853 209.445 1.00 5.00  ? 2793 ILE A CG2   1 
ATOM   10558 C  CD1   . ILE A 1 2793 ? 214.140 180.003 211.855 1.00 8.29  ? 2793 ILE A CD1   1 
ATOM   10559 N  N     . TYR A 1 2794 ? 218.650 176.528 211.273 1.00 1.81  ? 2794 TYR A N     1 
ATOM   10560 C  CA    . TYR A 1 2794 ? 220.070 176.262 211.125 1.00 1.05  ? 2794 TYR A CA    1 
ATOM   10561 C  C     . TYR A 1 2794 ? 220.380 176.071 209.649 1.00 1.06  ? 2794 TYR A C     1 
ATOM   10562 O  O     . TYR A 1 2794 ? 219.697 175.308 208.959 1.00 3.28  ? 2794 TYR A O     1 
ATOM   10563 C  CB    . TYR A 1 2794 ? 220.487 175.041 211.944 1.00 1.22  ? 2794 TYR A CB    1 
ATOM   10564 C  CG    . TYR A 1 2794 ? 220.306 175.245 213.431 1.00 2.82  ? 2794 TYR A CG    1 
ATOM   10565 C  CD1   . TYR A 1 2794 ? 221.242 175.954 214.171 1.00 2.51  ? 2794 TYR A CD1   1 
ATOM   10566 C  CD2   . TYR A 1 2794 ? 219.192 174.747 214.089 1.00 1.83  ? 2794 TYR A CD2   1 
ATOM   10567 C  CE1   . TYR A 1 2794 ? 221.079 176.151 215.527 1.00 2.40  ? 2794 TYR A CE1   1 
ATOM   10568 C  CE2   . TYR A 1 2794 ? 219.020 174.938 215.444 1.00 1.46  ? 2794 TYR A CE2   1 
ATOM   10569 C  CZ    . TYR A 1 2794 ? 219.967 175.640 216.158 1.00 4.13  ? 2794 TYR A CZ    1 
ATOM   10570 O  OH    . TYR A 1 2794 ? 219.800 175.832 217.509 1.00 9.18  ? 2794 TYR A OH    1 
ATOM   10571 N  N     . SER A 1 2795 ? 221.395 176.773 209.174 1.00 0.90  ? 2795 SER A N     1 
ATOM   10572 C  CA    . SER A 1 2795 ? 221.729 176.817 207.760 1.00 0.58  ? 2795 SER A CA    1 
ATOM   10573 C  C     . SER A 1 2795 ? 223.244 176.780 207.607 1.00 0.63  ? 2795 SER A C     1 
ATOM   10574 O  O     . SER A 1 2795 ? 223.962 176.828 208.612 1.00 0.79  ? 2795 SER A O     1 
ATOM   10575 C  CB    . SER A 1 2795 ? 221.138 178.075 207.120 1.00 0.51  ? 2795 SER A CB    1 
ATOM   10576 O  OG    . SER A 1 2795 ? 221.687 179.249 207.685 1.00 0.66  ? 2795 SER A OG    1 
ATOM   10577 N  N     . PRO A 1 2796 ? 223.772 176.689 206.381 1.00 0.73  ? 2796 PRO A N     1 
ATOM   10578 C  CA    . PRO A 1 2796 ? 225.226 176.823 206.198 1.00 0.68  ? 2796 PRO A CA    1 
ATOM   10579 C  C     . PRO A 1 2796 ? 225.787 178.155 206.668 1.00 0.28  ? 2796 PRO A C     1 
ATOM   10580 O  O     . PRO A 1 2796 ? 227.014 178.302 206.715 1.00 0.37  ? 2796 PRO A O     1 
ATOM   10581 C  CB    . PRO A 1 2796 ? 225.403 176.645 204.686 1.00 0.29  ? 2796 PRO A CB    1 
ATOM   10582 C  CG    . PRO A 1 2796 ? 224.279 175.765 204.305 1.00 0.37  ? 2796 PRO A CG    1 
ATOM   10583 C  CD    . PRO A 1 2796 ? 223.121 176.208 205.148 1.00 0.25  ? 2796 PRO A CD    1 
ATOM   10584 N  N     . ARG A 1 2797 ? 224.937 179.123 207.013 1.00 0.39  ? 2797 ARG A N     1 
ATOM   10585 C  CA    . ARG A 1 2797 ? 225.423 180.355 207.624 1.00 1.22  ? 2797 ARG A CA    1 
ATOM   10586 C  C     . ARG A 1 2797 ? 226.104 180.070 208.957 1.00 1.60  ? 2797 ARG A C     1 
ATOM   10587 O  O     . ARG A 1 2797 ? 227.128 180.682 209.282 1.00 2.51  ? 2797 ARG A O     1 
ATOM   10588 C  CB    . ARG A 1 2797 ? 224.269 181.339 207.805 1.00 0.68  ? 2797 ARG A CB    1 
ATOM   10589 C  CG    . ARG A 1 2797 ? 224.127 182.318 206.661 1.00 0.83  ? 2797 ARG A CG    1 
ATOM   10590 C  CD    . ARG A 1 2797 ? 223.226 183.479 207.024 1.00 2.20  ? 2797 ARG A CD    1 
ATOM   10591 N  NE    . ARG A 1 2797 ? 221.852 183.059 207.266 1.00 5.06  ? 2797 ARG A NE    1 
ATOM   10592 C  CZ    . ARG A 1 2797 ? 220.821 183.410 206.508 1.00 3.21  ? 2797 ARG A CZ    1 
ATOM   10593 N  NH1   . ARG A 1 2797 ? 220.982 184.155 205.427 1.00 2.92  ? 2797 ARG A NH1   1 
ATOM   10594 N  NH2   . ARG A 1 2797 ? 219.602 182.999 206.841 1.00 0.91  ? 2797 ARG A NH2   1 
ATOM   10595 N  N     . GLU A 1 2798 ? 225.547 179.145 209.741 1.00 1.27  ? 2798 GLU A N     1 
ATOM   10596 C  CA    . GLU A 1 2798 ? 226.205 178.718 210.972 1.00 1.13  ? 2798 GLU A CA    1 
ATOM   10597 C  C     . GLU A 1 2798 ? 227.528 178.025 210.681 1.00 0.72  ? 2798 GLU A C     1 
ATOM   10598 O  O     . GLU A 1 2798 ? 228.500 178.194 211.426 1.00 1.11  ? 2798 GLU A O     1 
ATOM   10599 C  CB    . GLU A 1 2798 ? 225.278 177.799 211.770 1.00 0.98  ? 2798 GLU A CB    1 
ATOM   10600 C  CG    . GLU A 1 2798 ? 224.314 178.539 212.683 1.00 1.42  ? 2798 GLU A CG    1 
ATOM   10601 C  CD    . GLU A 1 2798 ? 223.373 179.452 211.926 1.00 8.90  ? 2798 GLU A CD    1 
ATOM   10602 O  OE1   . GLU A 1 2798 ? 222.513 178.940 211.182 1.00 4.50  ? 2798 GLU A OE1   1 
ATOM   10603 O  OE2   . GLU A 1 2798 ? 223.503 180.686 212.071 1.00 17.30 ? 2798 GLU A OE2   1 
ATOM   10604 N  N     . MET A 1 2799 ? 227.585 177.237 209.605 1.00 1.07  ? 2799 MET A N     1 
ATOM   10605 C  CA    . MET A 1 2799 ? 228.844 176.612 209.212 1.00 0.52  ? 2799 MET A CA    1 
ATOM   10606 C  C     . MET A 1 2799 ? 229.886 177.659 208.834 1.00 0.66  ? 2799 MET A C     1 
ATOM   10607 O  O     . MET A 1 2799 ? 231.063 177.527 209.184 1.00 0.87  ? 2799 MET A O     1 
ATOM   10608 C  CB    . MET A 1 2799 ? 228.609 175.645 208.054 1.00 0.41  ? 2799 MET A CB    1 
ATOM   10609 C  CG    . MET A 1 2799 ? 227.740 174.446 208.397 1.00 1.07  ? 2799 MET A CG    1 
ATOM   10610 S  SD    . MET A 1 2799 ? 228.567 173.251 209.460 1.00 11.93 ? 2799 MET A SD    1 
ATOM   10611 C  CE    . MET A 1 2799 ? 229.961 172.789 208.439 1.00 0.28  ? 2799 MET A CE    1 
ATOM   10612 N  N     . THR A 1 2800 ? 229.471 178.704 208.117 1.00 0.71  ? 2800 THR A N     1 
ATOM   10613 C  CA    . THR A 1 2800 ? 230.394 179.776 207.760 1.00 0.56  ? 2800 THR A CA    1 
ATOM   10614 C  C     . THR A 1 2800 ? 230.886 180.512 209.001 1.00 0.72  ? 2800 THR A C     1 
ATOM   10615 O  O     . THR A 1 2800 ? 232.077 180.819 209.125 1.00 1.15  ? 2800 THR A O     1 
ATOM   10616 C  CB    . THR A 1 2800 ? 229.721 180.742 206.784 1.00 0.84  ? 2800 THR A CB    1 
ATOM   10617 O  OG1   . THR A 1 2800 ? 229.264 180.019 205.637 1.00 0.80  ? 2800 THR A OG1   1 
ATOM   10618 C  CG2   . THR A 1 2800 ? 230.691 181.824 206.339 1.00 1.23  ? 2800 THR A CG2   1 
ATOM   10619 N  N     . ARG A 1 2801 ? 229.978 180.799 209.937 1.00 0.64  ? 2801 ARG A N     1 
ATOM   10620 C  CA    . ARG A 1 2801 ? 230.379 181.432 211.190 1.00 0.58  ? 2801 ARG A CA    1 
ATOM   10621 C  C     . ARG A 1 2801 ? 231.244 180.498 212.026 1.00 0.92  ? 2801 ARG A C     1 
ATOM   10622 O  O     . ARG A 1 2801 ? 232.150 180.948 212.736 1.00 0.98  ? 2801 ARG A O     1 
ATOM   10623 C  CB    . ARG A 1 2801 ? 229.141 181.866 211.974 1.00 0.78  ? 2801 ARG A CB    1 
ATOM   10624 C  CG    . ARG A 1 2801 ? 228.477 183.118 211.434 1.00 6.97  ? 2801 ARG A CG    1 
ATOM   10625 C  CD    . ARG A 1 2801 ? 226.995 183.143 211.754 1.00 9.72  ? 2801 ARG A CD    1 
ATOM   10626 N  NE    . ARG A 1 2801 ? 226.300 184.202 211.029 1.00 19.73 ? 2801 ARG A NE    1 
ATOM   10627 C  CZ    . ARG A 1 2801 ? 224.991 184.234 210.823 1.00 13.53 ? 2801 ARG A CZ    1 
ATOM   10628 N  NH1   . ARG A 1 2801 ? 224.197 183.275 211.272 1.00 11.60 ? 2801 ARG A NH1   1 
ATOM   10629 N  NH2   . ARG A 1 2801 ? 224.464 185.252 210.150 1.00 9.37  ? 2801 ARG A NH2   1 
ATOM   10630 N  N     . TRP A 1 2802 ? 230.975 179.193 211.953 1.00 0.55  ? 2802 TRP A N     1 
ATOM   10631 C  CA    . TRP A 1 2802 ? 231.755 178.216 212.705 1.00 0.44  ? 2802 TRP A CA    1 
ATOM   10632 C  C     . TRP A 1 2802 ? 233.211 178.226 212.264 1.00 0.59  ? 2802 TRP A C     1 
ATOM   10633 O  O     . TRP A 1 2802 ? 234.127 178.240 213.094 1.00 1.08  ? 2802 TRP A O     1 
ATOM   10634 C  CB    . TRP A 1 2802 ? 231.150 176.826 212.513 1.00 0.73  ? 2802 TRP A CB    1 
ATOM   10635 C  CG    . TRP A 1 2802 ? 231.435 175.857 213.609 1.00 0.44  ? 2802 TRP A CG    1 
ATOM   10636 C  CD1   . TRP A 1 2802 ? 232.420 175.937 214.547 1.00 0.29  ? 2802 TRP A CD1   1 
ATOM   10637 C  CD2   . TRP A 1 2802 ? 230.742 174.632 213.859 1.00 0.49  ? 2802 TRP A CD2   1 
ATOM   10638 N  NE1   . TRP A 1 2802 ? 232.372 174.847 215.377 1.00 0.23  ? 2802 TRP A NE1   1 
ATOM   10639 C  CE2   . TRP A 1 2802 ? 231.350 174.030 214.975 1.00 0.35  ? 2802 TRP A CE2   1 
ATOM   10640 C  CE3   . TRP A 1 2802 ? 229.658 173.991 213.252 1.00 0.67  ? 2802 TRP A CE3   1 
ATOM   10641 C  CZ2   . TRP A 1 2802 ? 230.910 172.818 215.496 1.00 0.60  ? 2802 TRP A CZ2   1 
ATOM   10642 C  CZ3   . TRP A 1 2802 ? 229.226 172.789 213.771 1.00 0.42  ? 2802 TRP A CZ3   1 
ATOM   10643 C  CH2   . TRP A 1 2802 ? 229.851 172.214 214.880 1.00 0.39  ? 2802 TRP A CH2   1 
ATOM   10644 N  N     . VAL A 1 2803 ? 233.441 178.220 210.952 1.00 1.25  ? 2803 VAL A N     1 
ATOM   10645 C  CA    . VAL A 1 2803 ? 234.803 178.212 210.430 1.00 1.09  ? 2803 VAL A CA    1 
ATOM   10646 C  C     . VAL A 1 2803 ? 235.476 179.555 210.681 1.00 1.08  ? 2803 VAL A C     1 
ATOM   10647 O  O     . VAL A 1 2803 ? 236.652 179.617 211.057 1.00 2.08  ? 2803 VAL A O     1 
ATOM   10648 C  CB    . VAL A 1 2803 ? 234.789 177.846 208.934 1.00 1.01  ? 2803 VAL A CB    1 
ATOM   10649 C  CG1   . VAL A 1 2803 ? 236.171 177.993 208.335 1.00 1.69  ? 2803 VAL A CG1   1 
ATOM   10650 C  CG2   . VAL A 1 2803 ? 234.269 176.433 208.745 1.00 1.02  ? 2803 VAL A CG2   1 
ATOM   10651 N  N     . ARG A 1 2804 ? 234.738 180.650 210.481 1.00 1.11  ? 2804 ARG A N     1 
ATOM   10652 C  CA    . ARG A 1 2804 ? 235.275 181.977 210.767 1.00 2.61  ? 2804 ARG A CA    1 
ATOM   10653 C  C     . ARG A 1 2804 ? 235.632 182.134 212.240 1.00 3.42  ? 2804 ARG A C     1 
ATOM   10654 O  O     . ARG A 1 2804 ? 236.679 182.698 212.572 1.00 4.62  ? 2804 ARG A O     1 
ATOM   10655 C  CB    . ARG A 1 2804 ? 234.275 183.051 210.337 1.00 3.84  ? 2804 ARG A CB    1 
ATOM   10656 C  CG    . ARG A 1 2804 ? 234.909 184.388 209.986 1.00 10.28 ? 2804 ARG A CG    1 
ATOM   10657 C  CD    . ARG A 1 2804 ? 235.813 184.321 208.768 1.00 10.00 ? 2804 ARG A CD    1 
ATOM   10658 N  NE    . ARG A 1 2804 ? 236.868 185.324 208.846 1.00 17.40 ? 2804 ARG A NE    1 
ATOM   10659 C  CZ    . ARG A 1 2804 ? 237.801 185.513 207.922 1.00 22.76 ? 2804 ARG A CZ    1 
ATOM   10660 N  NH1   . ARG A 1 2804 ? 237.828 184.796 206.811 1.00 14.36 ? 2804 ARG A NH1   1 
ATOM   10661 N  NH2   . ARG A 1 2804 ? 238.727 186.447 208.117 1.00 23.90 ? 2804 ARG A NH2   1 
ATOM   10662 N  N     . GLY A 1 2805 ? 234.774 181.642 213.136 1.00 3.02  ? 2805 GLY A N     1 
ATOM   10663 C  CA    . GLY A 1 2805 ? 235.051 181.770 214.557 1.00 2.22  ? 2805 GLY A CA    1 
ATOM   10664 C  C     . GLY A 1 2805 ? 236.321 181.051 214.970 1.00 2.26  ? 2805 GLY A C     1 
ATOM   10665 O  O     . GLY A 1 2805 ? 237.134 181.586 215.727 1.00 6.16  ? 2805 GLY A O     1 
ATOM   10666 N  N     . ILE A 1 2806 ? 236.506 179.825 214.479 1.00 1.75  ? 2806 ILE A N     1 
ATOM   10667 C  CA    . ILE A 1 2806 ? 237.737 179.091 214.759 1.00 3.46  ? 2806 ILE A CA    1 
ATOM   10668 C  C     . ILE A 1 2806 ? 238.931 179.801 214.139 1.00 4.13  ? 2806 ILE A C     1 
ATOM   10669 O  O     . ILE A 1 2806 ? 240.003 179.898 214.748 1.00 4.01  ? 2806 ILE A O     1 
ATOM   10670 C  CB    . ILE A 1 2806 ? 237.619 177.638 214.264 1.00 0.99  ? 2806 ILE A CB    1 
ATOM   10671 C  CG1   . ILE A 1 2806 ? 236.470 176.923 214.973 1.00 1.07  ? 2806 ILE A CG1   1 
ATOM   10672 C  CG2   . ILE A 1 2806 ? 238.931 176.896 214.458 1.00 0.54  ? 2806 ILE A CG2   1 
ATOM   10673 C  CD1   . ILE A 1 2806 ? 236.382 175.453 214.660 1.00 0.91  ? 2806 ILE A CD1   1 
ATOM   10674 N  N     . PHE A 1 2807 ? 238.764 180.309 212.917 1.00 3.57  ? 2807 PHE A N     1 
ATOM   10675 C  CA    . PHE A 1 2807 ? 239.857 180.980 212.226 1.00 3.64  ? 2807 PHE A CA    1 
ATOM   10676 C  C     . PHE A 1 2807 ? 240.305 182.235 212.967 1.00 5.73  ? 2807 PHE A C     1 
ATOM   10677 O  O     . PHE A 1 2807 ? 241.507 182.505 213.072 1.00 10.08 ? 2807 PHE A O     1 
ATOM   10678 C  CB    . PHE A 1 2807 ? 239.433 181.310 210.795 1.00 3.33  ? 2807 PHE A CB    1 
ATOM   10679 C  CG    . PHE A 1 2807 ? 240.408 182.166 210.058 1.00 10.34 ? 2807 PHE A CG    1 
ATOM   10680 C  CD1   . PHE A 1 2807 ? 241.557 181.618 209.519 1.00 7.46  ? 2807 PHE A CD1   1 
ATOM   10681 C  CD2   . PHE A 1 2807 ? 240.164 183.515 209.875 1.00 12.85 ? 2807 PHE A CD2   1 
ATOM   10682 C  CE1   . PHE A 1 2807 ? 242.456 182.403 208.838 1.00 9.48  ? 2807 PHE A CE1   1 
ATOM   10683 C  CE2   . PHE A 1 2807 ? 241.056 184.301 209.186 1.00 10.92 ? 2807 PHE A CE2   1 
ATOM   10684 C  CZ    . PHE A 1 2807 ? 242.205 183.747 208.668 1.00 9.52  ? 2807 PHE A CZ    1 
ATOM   10685 N  N     . GLU A 1 2808 ? 239.354 183.013 213.489 1.00 5.38  ? 2808 GLU A N     1 
ATOM   10686 C  CA    . GLU A 1 2808 ? 239.711 184.213 214.238 1.00 5.94  ? 2808 GLU A CA    1 
ATOM   10687 C  C     . GLU A 1 2808 ? 240.465 183.877 215.518 1.00 7.65  ? 2808 GLU A C     1 
ATOM   10688 O  O     . GLU A 1 2808 ? 241.343 184.638 215.937 1.00 10.75 ? 2808 GLU A O     1 
ATOM   10689 C  CB    . GLU A 1 2808 ? 238.456 185.025 214.554 1.00 6.04  ? 2808 GLU A CB    1 
ATOM   10690 C  CG    . GLU A 1 2808 ? 237.746 185.545 213.318 1.00 13.32 ? 2808 GLU A CG    1 
ATOM   10691 C  CD    . GLU A 1 2808 ? 236.301 185.910 213.582 1.00 20.36 ? 2808 GLU A CD    1 
ATOM   10692 O  OE1   . GLU A 1 2808 ? 235.858 185.792 214.744 1.00 16.41 ? 2808 GLU A OE1   1 
ATOM   10693 O  OE2   . GLU A 1 2808 ? 235.606 186.308 212.624 1.00 18.38 ? 2808 GLU A OE2   1 
ATOM   10694 N  N     . ALA A 1 2809 ? 240.142 182.748 216.147 1.00 5.47  ? 2809 ALA A N     1 
ATOM   10695 C  CA    . ALA A 1 2809 ? 240.829 182.316 217.353 1.00 3.03  ? 2809 ALA A CA    1 
ATOM   10696 C  C     . ALA A 1 2809 ? 242.154 181.622 217.068 1.00 6.53  ? 2809 ALA A C     1 
ATOM   10697 O  O     . ALA A 1 2809 ? 242.866 181.273 218.017 1.00 16.15 ? 2809 ALA A O     1 
ATOM   10698 C  CB    . ALA A 1 2809 ? 239.928 181.383 218.165 1.00 3.07  ? 2809 ALA A CB    1 
ATOM   10699 N  N     . LEU A 1 2810 ? 242.499 181.407 215.797 1.00 5.89  ? 2810 LEU A N     1 
ATOM   10700 C  CA    . LEU A 1 2810 ? 243.730 180.722 215.436 1.00 4.32  ? 2810 LEU A CA    1 
ATOM   10701 C  C     . LEU A 1 2810 ? 244.770 181.620 214.780 1.00 11.93 ? 2810 LEU A C     1 
ATOM   10702 O  O     . LEU A 1 2810 ? 245.945 181.243 214.748 1.00 17.14 ? 2810 LEU A O     1 
ATOM   10703 C  CB    . LEU A 1 2810 ? 243.428 179.549 214.491 1.00 5.62  ? 2810 LEU A CB    1 
ATOM   10704 C  CG    . LEU A 1 2810 ? 242.934 178.235 215.099 1.00 3.43  ? 2810 LEU A CG    1 
ATOM   10705 C  CD1   . LEU A 1 2810 ? 242.600 177.239 214.005 1.00 4.44  ? 2810 LEU A CD1   1 
ATOM   10706 C  CD2   . LEU A 1 2810 ? 243.964 177.653 216.044 1.00 10.03 ? 2810 LEU A CD2   1 
ATOM   10707 N  N     . ARG A 1 2811 ? 244.376 182.786 214.260 1.00 7.69  ? 2811 ARG A N     1 
ATOM   10708 C  CA    . ARG A 1 2811 ? 245.332 183.661 213.579 1.00 11.54 ? 2811 ARG A CA    1 
ATOM   10709 C  C     . ARG A 1 2811 ? 246.498 184.099 214.455 1.00 13.15 ? 2811 ARG A C     1 
ATOM   10710 O  O     . ARG A 1 2811 ? 247.652 183.975 214.008 1.00 19.48 ? 2811 ARG A O     1 
ATOM   10711 C  CB    . ARG A 1 2811 ? 244.610 184.885 213.009 1.00 12.89 ? 2811 ARG A CB    1 
ATOM   10712 C  CG    . ARG A 1 2811 ? 243.667 184.596 211.877 1.00 15.21 ? 2811 ARG A CG    1 
ATOM   10713 C  CD    . ARG A 1 2811 ? 242.984 185.868 211.423 1.00 19.53 ? 2811 ARG A CD    1 
ATOM   10714 N  NE    . ARG A 1 2811 ? 242.065 186.388 212.426 1.00 19.97 ? 2811 ARG A NE    1 
ATOM   10715 C  CZ    . ARG A 1 2811 ? 241.433 187.549 212.328 1.00 23.44 ? 2811 ARG A CZ    1 
ATOM   10716 N  NH1   . ARG A 1 2811 ? 241.596 188.336 211.278 1.00 20.75 ? 2811 ARG A NH1   1 
ATOM   10717 N  NH2   . ARG A 1 2811 ? 240.613 187.926 213.305 1.00 22.76 ? 2811 ARG A NH2   1 
ATOM   10718 N  N     . PRO A 1 2812 ? 246.299 184.618 215.678 1.00 14.42 ? 2812 PRO A N     1 
ATOM   10719 C  CA    . PRO A 1 2812 ? 247.449 185.127 216.434 1.00 13.78 ? 2812 PRO A CA    1 
ATOM   10720 C  C     . PRO A 1 2812 ? 248.202 184.040 217.185 1.00 11.76 ? 2812 PRO A C     1 
ATOM   10721 O  O     . PRO A 1 2812 ? 249.011 184.342 218.068 1.00 24.61 ? 2812 PRO A O     1 
ATOM   10722 C  CB    . PRO A 1 2812 ? 246.802 186.124 217.397 1.00 15.53 ? 2812 PRO A CB    1 
ATOM   10723 C  CG    . PRO A 1 2812 ? 245.499 185.487 217.706 1.00 14.45 ? 2812 PRO A CG    1 
ATOM   10724 C  CD    . PRO A 1 2812 ? 245.041 184.839 216.419 1.00 8.53  ? 2812 PRO A CD    1 
ATOM   10725 N  N     . LEU A 1 2813 ? 247.949 182.780 216.849 1.00 14.56 ? 2813 LEU A N     1 
ATOM   10726 C  CA    . LEU A 1 2813 ? 248.527 181.649 217.562 1.00 15.89 ? 2813 LEU A CA    1 
ATOM   10727 C  C     . LEU A 1 2813 ? 249.656 181.035 216.748 1.00 22.12 ? 2813 LEU A C     1 
ATOM   10728 O  O     . LEU A 1 2813 ? 249.467 180.683 215.579 1.00 25.20 ? 2813 LEU A O     1 
ATOM   10729 C  CB    . LEU A 1 2813 ? 247.463 180.594 217.863 1.00 15.75 ? 2813 LEU A CB    1 
ATOM   10730 C  CG    . LEU A 1 2813 ? 246.362 181.007 218.840 1.00 12.47 ? 2813 LEU A CG    1 
ATOM   10731 C  CD1   . LEU A 1 2813 ? 245.607 179.786 219.338 1.00 9.15  ? 2813 LEU A CD1   1 
ATOM   10732 C  CD2   . LEU A 1 2813 ? 246.946 181.792 219.999 1.00 14.33 ? 2813 LEU A CD2   1 
ATOM   10733 N  N     . GLU A 1 2814 ? 250.829 180.911 217.369 1.00 21.35 ? 2814 GLU A N     1 
ATOM   10734 C  CA    . GLU A 1 2814 ? 251.957 180.269 216.705 1.00 23.19 ? 2814 GLU A CA    1 
ATOM   10735 C  C     . GLU A 1 2814 ? 251.820 178.752 216.686 1.00 23.40 ? 2814 GLU A C     1 
ATOM   10736 O  O     . GLU A 1 2814 ? 252.269 178.109 215.732 1.00 22.91 ? 2814 GLU A O     1 
ATOM   10737 C  CB    . GLU A 1 2814 ? 253.271 180.685 217.377 1.00 26.39 ? 2814 GLU A CB    1 
ATOM   10738 C  CG    . GLU A 1 2814 ? 253.602 179.965 218.682 1.00 31.73 ? 2814 GLU A CG    1 
ATOM   10739 C  CD    . GLU A 1 2814 ? 252.557 180.174 219.765 1.00 34.28 ? 2814 GLU A CD    1 
ATOM   10740 O  OE1   . GLU A 1 2814 ? 251.858 181.210 219.735 1.00 31.54 ? 2814 GLU A OE1   1 
ATOM   10741 O  OE2   . GLU A 1 2814 ? 252.432 179.300 220.648 1.00 36.80 ? 2814 GLU A OE2   1 
ATOM   10742 N  N     . THR A 1 2815 ? 251.205 178.167 217.713 1.00 20.16 ? 2815 THR A N     1 
ATOM   10743 C  CA    . THR A 1 2815 ? 251.014 176.726 217.765 1.00 20.55 ? 2815 THR A CA    1 
ATOM   10744 C  C     . THR A 1 2815 ? 249.876 176.416 218.724 1.00 16.84 ? 2815 THR A C     1 
ATOM   10745 O  O     . THR A 1 2815 ? 249.507 177.237 219.568 1.00 19.40 ? 2815 THR A O     1 
ATOM   10746 C  CB    . THR A 1 2815 ? 252.291 175.994 218.193 1.00 20.98 ? 2815 THR A CB    1 
ATOM   10747 O  OG1   . THR A 1 2815 ? 252.177 174.604 217.868 1.00 24.35 ? 2815 THR A OG1   1 
ATOM   10748 C  CG2   . THR A 1 2815 ? 252.516 176.141 219.690 1.00 18.47 ? 2815 THR A CG2   1 
ATOM   10749 N  N     . LEU A 1 2816 ? 249.325 175.208 218.582 1.00 14.27 ? 2816 LEU A N     1 
ATOM   10750 C  CA    . LEU A 1 2816 ? 248.199 174.772 219.390 1.00 9.22  ? 2816 LEU A CA    1 
ATOM   10751 C  C     . LEU A 1 2816 ? 248.119 173.258 219.344 1.00 7.64  ? 2816 LEU A C     1 
ATOM   10752 O  O     . LEU A 1 2816 ? 248.241 172.682 218.254 1.00 23.87 ? 2816 LEU A O     1 
ATOM   10753 C  CB    . LEU A 1 2816 ? 246.888 175.381 218.888 1.00 9.64  ? 2816 LEU A CB    1 
ATOM   10754 C  CG    . LEU A 1 2816 ? 245.675 175.327 219.819 1.00 9.29  ? 2816 LEU A CG    1 
ATOM   10755 C  CD1   . LEU A 1 2816 ? 245.834 176.295 220.980 1.00 3.42  ? 2816 LEU A CD1   1 
ATOM   10756 C  CD2   . LEU A 1 2816 ? 244.407 175.624 219.043 1.00 7.77  ? 2816 LEU A CD2   1 
ATOM   10757 N  N     . PRO A 1 2817 ? 247.929 172.586 220.474 1.00 13.47 ? 2817 PRO A N     1 
ATOM   10758 C  CA    . PRO A 1 2817 ? 247.673 171.142 220.440 1.00 10.56 ? 2817 PRO A CA    1 
ATOM   10759 C  C     . PRO A 1 2817 ? 246.280 170.855 219.903 1.00 11.40 ? 2817 PRO A C     1 
ATOM   10760 O  O     . PRO A 1 2817 ? 245.426 171.735 219.795 1.00 17.14 ? 2817 PRO A O     1 
ATOM   10761 C  CB    . PRO A 1 2817 ? 247.819 170.714 221.901 1.00 8.52  ? 2817 PRO A CB    1 
ATOM   10762 C  CG    . PRO A 1 2817 ? 247.548 171.949 222.686 1.00 12.56 ? 2817 PRO A CG    1 
ATOM   10763 C  CD    . PRO A 1 2817 ? 248.008 173.108 221.849 1.00 11.79 ? 2817 PRO A CD    1 
ATOM   10764 N  N     . VAL A 1 2818 ? 246.059 169.587 219.553 1.00 11.28 ? 2818 VAL A N     1 
ATOM   10765 C  CA    . VAL A 1 2818 ? 244.778 169.198 218.973 1.00 10.00 ? 2818 VAL A CA    1 
ATOM   10766 C  C     . VAL A 1 2818 ? 243.655 169.371 219.990 1.00 8.00  ? 2818 VAL A C     1 
ATOM   10767 O  O     . VAL A 1 2818 ? 242.525 169.725 219.631 1.00 8.75  ? 2818 VAL A O     1 
ATOM   10768 C  CB    . VAL A 1 2818 ? 244.849 167.760 218.424 1.00 9.72  ? 2818 VAL A CB    1 
ATOM   10769 C  CG1   . VAL A 1 2818 ? 245.074 166.751 219.543 1.00 9.76  ? 2818 VAL A CG1   1 
ATOM   10770 C  CG2   . VAL A 1 2818 ? 243.594 167.432 217.628 1.00 6.46  ? 2818 VAL A CG2   1 
ATOM   10771 N  N     . GLU A 1 2819 ? 243.943 169.133 221.271 1.00 9.08  ? 2819 GLU A N     1 
ATOM   10772 C  CA    . GLU A 1 2819 ? 242.949 169.380 222.310 1.00 8.46  ? 2819 GLU A CA    1 
ATOM   10773 C  C     . GLU A 1 2819 ? 242.565 170.853 222.375 1.00 9.98  ? 2819 GLU A C     1 
ATOM   10774 O  O     . GLU A 1 2819 ? 241.411 171.179 222.669 1.00 7.85  ? 2819 GLU A O     1 
ATOM   10775 C  CB    . GLU A 1 2819 ? 243.468 168.899 223.664 1.00 10.65 ? 2819 GLU A CB    1 
ATOM   10776 C  CG    . GLU A 1 2819 ? 243.637 167.389 223.775 1.00 15.92 ? 2819 GLU A CG    1 
ATOM   10777 C  CD    . GLU A 1 2819 ? 244.946 166.894 223.190 1.00 20.29 ? 2819 GLU A CD    1 
ATOM   10778 O  OE1   . GLU A 1 2819 ? 245.762 167.730 222.749 1.00 16.26 ? 2819 GLU A OE1   1 
ATOM   10779 O  OE2   . GLU A 1 2819 ? 245.155 165.663 223.163 1.00 29.54 ? 2819 GLU A OE2   1 
ATOM   10780 N  N     . GLY A 1 2820 ? 243.516 171.751 222.109 1.00 8.19  ? 2820 GLY A N     1 
ATOM   10781 C  CA    . GLY A 1 2820 ? 243.184 173.160 222.009 1.00 4.56  ? 2820 GLY A CA    1 
ATOM   10782 C  C     . GLY A 1 2820 ? 242.286 173.471 220.830 1.00 4.97  ? 2820 GLY A C     1 
ATOM   10783 O  O     . GLY A 1 2820 ? 241.437 174.363 220.909 1.00 5.28  ? 2820 GLY A O     1 
ATOM   10784 N  N     . LEU A 1 2821 ? 242.468 172.755 219.718 1.00 7.61  ? 2821 LEU A N     1 
ATOM   10785 C  CA    . LEU A 1 2821 ? 241.588 172.928 218.566 1.00 3.59  ? 2821 LEU A CA    1 
ATOM   10786 C  C     . LEU A 1 2821 ? 240.163 172.502 218.888 1.00 2.40  ? 2821 LEU A C     1 
ATOM   10787 O  O     . LEU A 1 2821 ? 239.203 173.174 218.495 1.00 2.67  ? 2821 LEU A O     1 
ATOM   10788 C  CB    . LEU A 1 2821 ? 242.126 172.139 217.374 1.00 4.55  ? 2821 LEU A CB    1 
ATOM   10789 C  CG    . LEU A 1 2821 ? 241.291 172.199 216.094 1.00 3.71  ? 2821 LEU A CG    1 
ATOM   10790 C  CD1   . LEU A 1 2821 ? 241.214 173.625 215.569 1.00 1.76  ? 2821 LEU A CD1   1 
ATOM   10791 C  CD2   . LEU A 1 2821 ? 241.851 171.261 215.041 1.00 3.49  ? 2821 LEU A CD2   1 
ATOM   10792 N  N     . ILE A 1 2822 ? 240.005 171.388 219.605 1.00 1.63  ? 2822 ILE A N     1 
ATOM   10793 C  CA    . ILE A 1 2822 ? 238.669 170.899 219.935 1.00 1.64  ? 2822 ILE A CA    1 
ATOM   10794 C  C     . ILE A 1 2822 ? 237.951 171.877 220.854 1.00 2.92  ? 2822 ILE A C     1 
ATOM   10795 O  O     . ILE A 1 2822 ? 236.736 172.077 220.739 1.00 1.85  ? 2822 ILE A O     1 
ATOM   10796 C  CB    . ILE A 1 2822 ? 238.750 169.493 220.556 1.00 3.17  ? 2822 ILE A CB    1 
ATOM   10797 C  CG1   . ILE A 1 2822 ? 239.529 168.548 219.643 1.00 3.54  ? 2822 ILE A CG1   1 
ATOM   10798 C  CG2   . ILE A 1 2822 ? 237.358 168.945 220.820 1.00 5.41  ? 2822 ILE A CG2   1 
ATOM   10799 C  CD1   . ILE A 1 2822 ? 239.037 168.536 218.217 1.00 4.18  ? 2822 ILE A CD1   1 
ATOM   10800 N  N     . ARG A 1 2823 ? 238.684 172.496 221.782 1.00 4.69  ? 2823 ARG A N     1 
ATOM   10801 C  CA    . ARG A 1 2823 ? 238.061 173.453 222.691 1.00 2.23  ? 2823 ARG A CA    1 
ATOM   10802 C  C     . ARG A 1 2823 ? 237.507 174.652 221.933 1.00 1.68  ? 2823 ARG A C     1 
ATOM   10803 O  O     . ARG A 1 2823 ? 236.396 175.114 222.218 1.00 1.75  ? 2823 ARG A O     1 
ATOM   10804 C  CB    . ARG A 1 2823 ? 239.061 173.897 223.757 1.00 4.47  ? 2823 ARG A CB    1 
ATOM   10805 C  CG    . ARG A 1 2823 ? 238.401 174.518 224.971 1.00 3.27  ? 2823 ARG A CG    1 
ATOM   10806 C  CD    . ARG A 1 2823 ? 239.379 174.738 226.108 1.00 3.40  ? 2823 ARG A CD    1 
ATOM   10807 N  NE    . ARG A 1 2823 ? 238.688 175.120 227.334 1.00 11.46 ? 2823 ARG A NE    1 
ATOM   10808 C  CZ    . ARG A 1 2823 ? 237.937 174.306 228.063 1.00 8.59  ? 2823 ARG A CZ    1 
ATOM   10809 N  NH1   . ARG A 1 2823 ? 237.816 173.023 227.765 1.00 6.43  ? 2823 ARG A NH1   1 
ATOM   10810 N  NH2   . ARG A 1 2823 ? 237.296 174.789 229.122 1.00 5.11  ? 2823 ARG A NH2   1 
ATOM   10811 N  N     . ILE A 1 2824 ? 238.265 175.171 220.965 1.00 1.58  ? 2824 ILE A N     1 
ATOM   10812 C  CA    . ILE A 1 2824 ? 237.750 176.239 220.112 1.00 1.43  ? 2824 ILE A CA    1 
ATOM   10813 C  C     . ILE A 1 2824 ? 236.555 175.741 219.311 1.00 1.59  ? 2824 ILE A C     1 
ATOM   10814 O  O     . ILE A 1 2824 ? 235.543 176.439 219.176 1.00 1.58  ? 2824 ILE A O     1 
ATOM   10815 C  CB    . ILE A 1 2824 ? 238.862 176.774 219.189 1.00 1.46  ? 2824 ILE A CB    1 
ATOM   10816 C  CG1   . ILE A 1 2824 ? 240.082 177.197 220.006 1.00 1.50  ? 2824 ILE A CG1   1 
ATOM   10817 C  CG2   . ILE A 1 2824 ? 238.349 177.934 218.350 1.00 1.61  ? 2824 ILE A CG2   1 
ATOM   10818 C  CD1   . ILE A 1 2824 ? 241.267 177.610 219.160 1.00 5.03  ? 2824 ILE A CD1   1 
ATOM   10819 N  N     . TRP A 1 2825 ? 236.655 174.526 218.772 1.00 2.00  ? 2825 TRP A N     1 
ATOM   10820 C  CA    . TRP A 1 2825 ? 235.551 173.945 218.018 1.00 0.67  ? 2825 TRP A CA    1 
ATOM   10821 C  C     . TRP A 1 2825 ? 234.319 173.762 218.896 1.00 1.17  ? 2825 TRP A C     1 
ATOM   10822 O  O     . TRP A 1 2825 ? 233.193 174.039 218.466 1.00 1.50  ? 2825 TRP A O     1 
ATOM   10823 C  CB    . TRP A 1 2825 ? 235.994 172.614 217.412 1.00 0.87  ? 2825 TRP A CB    1 
ATOM   10824 C  CG    . TRP A 1 2825 ? 234.918 171.884 216.689 1.00 0.97  ? 2825 TRP A CG    1 
ATOM   10825 C  CD1   . TRP A 1 2825 ? 234.574 172.023 215.379 1.00 0.41  ? 2825 TRP A CD1   1 
ATOM   10826 C  CD2   . TRP A 1 2825 ? 234.047 170.889 217.231 1.00 1.05  ? 2825 TRP A CD2   1 
ATOM   10827 N  NE1   . TRP A 1 2825 ? 233.539 171.179 215.072 1.00 0.44  ? 2825 TRP A NE1   1 
ATOM   10828 C  CE2   . TRP A 1 2825 ? 233.197 170.471 216.192 1.00 0.41  ? 2825 TRP A CE2   1 
ATOM   10829 C  CE3   . TRP A 1 2825 ? 233.903 170.311 218.496 1.00 1.09  ? 2825 TRP A CE3   1 
ATOM   10830 C  CZ2   . TRP A 1 2825 ? 232.213 169.505 216.377 1.00 0.70  ? 2825 TRP A CZ2   1 
ATOM   10831 C  CZ3   . TRP A 1 2825 ? 232.927 169.354 218.678 1.00 1.41  ? 2825 TRP A CZ3   1 
ATOM   10832 C  CH2   . TRP A 1 2825 ? 232.096 168.959 217.624 1.00 1.87  ? 2825 TRP A CH2   1 
ATOM   10833 N  N     . ALA A 1 2826 ? 234.510 173.290 220.129 1.00 2.50  ? 2826 ALA A N     1 
ATOM   10834 C  CA    . ALA A 1 2826 ? 233.385 173.139 221.045 1.00 1.03  ? 2826 ALA A CA    1 
ATOM   10835 C  C     . ALA A 1 2826 ? 232.836 174.492 221.479 1.00 0.47  ? 2826 ALA A C     1 
ATOM   10836 O  O     . ALA A 1 2826 ? 231.619 174.660 221.612 1.00 0.54  ? 2826 ALA A O     1 
ATOM   10837 C  CB    . ALA A 1 2826 ? 233.807 172.318 222.261 1.00 0.61  ? 2826 ALA A CB    1 
ATOM   10838 N  N     . HIS A 1 2827 ? 233.719 175.463 221.712 1.00 0.59  ? 2827 HIS A N     1 
ATOM   10839 C  CA    . HIS A 1 2827 ? 233.271 176.781 222.144 1.00 0.40  ? 2827 HIS A CA    1 
ATOM   10840 C  C     . HIS A 1 2827 ? 232.409 177.452 221.085 1.00 0.34  ? 2827 HIS A C     1 
ATOM   10841 O  O     . HIS A 1 2827 ? 231.351 178.010 221.397 1.00 0.24  ? 2827 HIS A O     1 
ATOM   10842 C  CB    . HIS A 1 2827 ? 234.474 177.657 222.486 1.00 0.42  ? 2827 HIS A CB    1 
ATOM   10843 C  CG    . HIS A 1 2827 ? 234.123 179.088 222.741 1.00 0.45  ? 2827 HIS A CG    1 
ATOM   10844 N  ND1   . HIS A 1 2827 ? 233.535 179.513 223.911 1.00 0.36  ? 2827 HIS A ND1   1 
ATOM   10845 C  CD2   . HIS A 1 2827 ? 234.279 180.192 221.975 1.00 0.63  ? 2827 HIS A CD2   1 
ATOM   10846 C  CE1   . HIS A 1 2827 ? 233.338 180.817 223.854 1.00 0.40  ? 2827 HIS A CE1   1 
ATOM   10847 N  NE2   . HIS A 1 2827 ? 233.782 181.254 222.689 1.00 0.48  ? 2827 HIS A NE2   1 
ATOM   10848 N  N     . GLU A 1 2828 ? 232.841 177.401 219.824 1.00 0.55  ? 2828 GLU A N     1 
ATOM   10849 C  CA    . GLU A 1 2828 ? 232.075 178.032 218.757 1.00 0.29  ? 2828 GLU A CA    1 
ATOM   10850 C  C     . GLU A 1 2828 ? 230.750 177.321 218.520 1.00 0.24  ? 2828 GLU A C     1 
ATOM   10851 O  O     . GLU A 1 2828 ? 229.761 177.967 218.158 1.00 0.55  ? 2828 GLU A O     1 
ATOM   10852 C  CB    . GLU A 1 2828 ? 232.907 178.079 217.476 1.00 1.48  ? 2828 GLU A CB    1 
ATOM   10853 C  CG    . GLU A 1 2828 ? 234.137 178.964 217.585 1.00 1.56  ? 2828 GLU A CG    1 
ATOM   10854 C  CD    . GLU A 1 2828 ? 233.789 180.437 217.711 1.00 8.45  ? 2828 GLU A CD    1 
ATOM   10855 O  OE1   . GLU A 1 2828 ? 232.648 180.815 217.378 1.00 9.93  ? 2828 GLU A OE1   1 
ATOM   10856 O  OE2   . GLU A 1 2828 ? 234.655 181.216 218.157 1.00 8.28  ? 2828 GLU A OE2   1 
ATOM   10857 N  N     . ALA A 1 2829 ? 230.710 176.003 218.719 1.00 0.31  ? 2829 ALA A N     1 
ATOM   10858 C  CA    . ALA A 1 2829 ? 229.450 175.277 218.606 1.00 0.46  ? 2829 ALA A CA    1 
ATOM   10859 C  C     . ALA A 1 2829 ? 228.445 175.751 219.650 1.00 0.32  ? 2829 ALA A C     1 
ATOM   10860 O  O     . ALA A 1 2829 ? 227.258 175.917 219.348 1.00 0.41  ? 2829 ALA A O     1 
ATOM   10861 C  CB    . ALA A 1 2829 ? 229.697 173.775 218.735 1.00 0.52  ? 2829 ALA A CB    1 
ATOM   10862 N  N     . LEU A 1 2830 ? 228.902 175.978 220.883 1.00 0.34  ? 2830 LEU A N     1 
ATOM   10863 C  CA    . LEU A 1 2830 ? 228.005 176.468 221.926 1.00 0.51  ? 2830 LEU A CA    1 
ATOM   10864 C  C     . LEU A 1 2830 ? 227.480 177.859 221.595 1.00 0.29  ? 2830 LEU A C     1 
ATOM   10865 O  O     . LEU A 1 2830 ? 226.301 178.155 221.812 1.00 0.74  ? 2830 LEU A O     1 
ATOM   10866 C  CB    . LEU A 1 2830 ? 228.723 176.473 223.274 1.00 0.84  ? 2830 LEU A CB    1 
ATOM   10867 C  CG    . LEU A 1 2830 ? 229.074 175.107 223.863 1.00 0.82  ? 2830 LEU A CG    1 
ATOM   10868 C  CD1   . LEU A 1 2830 ? 230.192 175.243 224.881 1.00 0.30  ? 2830 LEU A CD1   1 
ATOM   10869 C  CD2   . LEU A 1 2830 ? 227.851 174.460 224.485 1.00 2.00  ? 2830 LEU A CD2   1 
ATOM   10870 N  N     . ARG A 1 2831 ? 228.342 178.724 221.061 1.00 0.25  ? 2831 ARG A N     1 
ATOM   10871 C  CA    . ARG A 1 2831 ? 227.924 180.081 220.735 1.00 0.34  ? 2831 ARG A CA    1 
ATOM   10872 C  C     . ARG A 1 2831 ? 226.940 180.111 219.574 1.00 0.70  ? 2831 ARG A C     1 
ATOM   10873 O  O     . ARG A 1 2831 ? 226.068 180.985 219.526 1.00 1.75  ? 2831 ARG A O     1 
ATOM   10874 C  CB    . ARG A 1 2831 ? 229.148 180.940 220.423 1.00 0.50  ? 2831 ARG A CB    1 
ATOM   10875 C  CG    . ARG A 1 2831 ? 230.121 181.087 221.584 1.00 0.32  ? 2831 ARG A CG    1 
ATOM   10876 C  CD    . ARG A 1 2831 ? 229.592 182.031 222.662 1.00 0.60  ? 2831 ARG A CD    1 
ATOM   10877 N  NE    . ARG A 1 2831 ? 228.601 181.394 223.523 1.00 0.53  ? 2831 ARG A NE    1 
ATOM   10878 C  CZ    . ARG A 1 2831 ? 228.864 180.432 224.395 1.00 0.39  ? 2831 ARG A CZ    1 
ATOM   10879 N  NH1   . ARG A 1 2831 ? 230.099 180.006 224.607 1.00 0.18  ? 2831 ARG A NH1   1 
ATOM   10880 N  NH2   . ARG A 1 2831 ? 227.863 179.879 225.071 1.00 0.69  ? 2831 ARG A NH2   1 
ATOM   10881 N  N     . LEU A 1 2832 ? 227.054 179.172 218.637 1.00 0.65  ? 2832 LEU A N     1 
ATOM   10882 C  CA    . LEU A 1 2832 ? 226.225 179.172 217.440 1.00 0.61  ? 2832 LEU A CA    1 
ATOM   10883 C  C     . LEU A 1 2832 ? 224.956 178.347 217.575 1.00 0.50  ? 2832 LEU A C     1 
ATOM   10884 O  O     . LEU A 1 2832 ? 223.961 178.657 216.915 1.00 1.68  ? 2832 LEU A O     1 
ATOM   10885 C  CB    . LEU A 1 2832 ? 227.022 178.648 216.244 1.00 1.23  ? 2832 LEU A CB    1 
ATOM   10886 C  CG    . LEU A 1 2832 ? 228.103 179.578 215.697 1.00 0.59  ? 2832 LEU A CG    1 
ATOM   10887 C  CD1   . LEU A 1 2832 ? 228.872 178.869 214.616 1.00 0.45  ? 2832 LEU A CD1   1 
ATOM   10888 C  CD2   . LEU A 1 2832 ? 227.492 180.861 215.168 1.00 1.08  ? 2832 LEU A CD2   1 
ATOM   10889 N  N     . PHE A 1 2833 ? 224.964 177.306 218.402 1.00 0.46  ? 2833 PHE A N     1 
ATOM   10890 C  CA    . PHE A 1 2833 ? 223.832 176.398 218.491 1.00 0.46  ? 2833 PHE A CA    1 
ATOM   10891 C  C     . PHE A 1 2833 ? 223.102 176.449 219.820 1.00 0.55  ? 2833 PHE A C     1 
ATOM   10892 O  O     . PHE A 1 2833 ? 221.888 176.244 219.845 1.00 1.43  ? 2833 PHE A O     1 
ATOM   10893 C  CB    . PHE A 1 2833 ? 224.289 174.956 218.229 1.00 0.46  ? 2833 PHE A CB    1 
ATOM   10894 C  CG    . PHE A 1 2833 ? 224.856 174.740 216.858 1.00 0.27  ? 2833 PHE A CG    1 
ATOM   10895 C  CD1   . PHE A 1 2833 ? 224.025 174.451 215.791 1.00 0.45  ? 2833 PHE A CD1   1 
ATOM   10896 C  CD2   . PHE A 1 2833 ? 226.216 174.829 216.635 1.00 0.29  ? 2833 PHE A CD2   1 
ATOM   10897 C  CE1   . PHE A 1 2833 ? 224.541 174.251 214.530 1.00 0.44  ? 2833 PHE A CE1   1 
ATOM   10898 C  CE2   . PHE A 1 2833 ? 226.739 174.633 215.374 1.00 0.57  ? 2833 PHE A CE2   1 
ATOM   10899 C  CZ    . PHE A 1 2833 ? 225.899 174.342 214.320 1.00 0.53  ? 2833 PHE A CZ    1 
ATOM   10900 N  N     . GLN A 1 2834 ? 223.800 176.729 220.917 1.00 0.61  ? 2834 GLN A N     1 
ATOM   10901 C  CA    . GLN A 1 2834 ? 223.177 176.693 222.233 1.00 0.47  ? 2834 GLN A CA    1 
ATOM   10902 C  C     . GLN A 1 2834 ? 222.628 178.043 222.678 1.00 0.62  ? 2834 GLN A C     1 
ATOM   10903 O  O     . GLN A 1 2834 ? 221.680 178.081 223.468 1.00 1.47  ? 2834 GLN A O     1 
ATOM   10904 C  CB    . GLN A 1 2834 ? 224.181 176.182 223.269 1.00 0.46  ? 2834 GLN A CB    1 
ATOM   10905 C  CG    . GLN A 1 2834 ? 223.548 175.601 224.516 1.00 1.15  ? 2834 GLN A CG    1 
ATOM   10906 C  CD    . GLN A 1 2834 ? 224.565 175.326 225.602 1.00 2.84  ? 2834 GLN A CD    1 
ATOM   10907 O  OE1   . GLN A 1 2834 ? 225.254 176.233 226.062 1.00 5.60  ? 2834 GLN A OE1   1 
ATOM   10908 N  NE2   . GLN A 1 2834 ? 224.665 174.071 226.016 1.00 3.07  ? 2834 GLN A NE2   1 
ATOM   10909 N  N     . ASP A 1 2835 ? 223.187 179.150 222.185 1.00 0.57  ? 2835 ASP A N     1 
ATOM   10910 C  CA    . ASP A 1 2835 ? 222.820 180.467 222.695 1.00 0.63  ? 2835 ASP A CA    1 
ATOM   10911 C  C     . ASP A 1 2835 ? 221.405 180.882 222.314 1.00 0.36  ? 2835 ASP A C     1 
ATOM   10912 O  O     . ASP A 1 2835 ? 220.841 181.767 222.963 1.00 0.43  ? 2835 ASP A O     1 
ATOM   10913 C  CB    . ASP A 1 2835 ? 223.816 181.518 222.206 1.00 0.82  ? 2835 ASP A CB    1 
ATOM   10914 C  CG    . ASP A 1 2835 ? 225.146 181.444 222.929 1.00 1.77  ? 2835 ASP A CG    1 
ATOM   10915 O  OD1   . ASP A 1 2835 ? 225.300 180.575 223.812 1.00 0.72  ? 2835 ASP A OD1   1 
ATOM   10916 O  OD2   . ASP A 1 2835 ? 226.040 182.256 222.617 1.00 3.41  ? 2835 ASP A OD2   1 
ATOM   10917 N  N     . ARG A 1 2836 ? 220.824 180.276 221.283 1.00 0.46  ? 2836 ARG A N     1 
ATOM   10918 C  CA    . ARG A 1 2836 ? 219.465 180.593 220.872 1.00 0.58  ? 2836 ARG A CA    1 
ATOM   10919 C  C     . ARG A 1 2836 ? 218.421 179.686 221.505 1.00 0.65  ? 2836 ARG A C     1 
ATOM   10920 O  O     . ARG A 1 2836 ? 217.223 179.940 221.342 1.00 1.04  ? 2836 ARG A O     1 
ATOM   10921 C  CB    . ARG A 1 2836 ? 219.342 180.505 219.349 1.00 0.62  ? 2836 ARG A CB    1 
ATOM   10922 C  CG    . ARG A 1 2836 ? 219.352 179.080 218.824 1.00 0.59  ? 2836 ARG A CG    1 
ATOM   10923 C  CD    . ARG A 1 2836 ? 219.253 179.058 217.322 1.00 1.65  ? 2836 ARG A CD    1 
ATOM   10924 N  NE    . ARG A 1 2836 ? 220.447 179.614 216.699 1.00 5.70  ? 2836 ARG A NE    1 
ATOM   10925 C  CZ    . ARG A 1 2836 ? 220.550 179.907 215.412 1.00 2.56  ? 2836 ARG A CZ    1 
ATOM   10926 N  NH1   . ARG A 1 2836 ? 219.540 179.720 214.578 1.00 2.28  ? 2836 ARG A NH1   1 
ATOM   10927 N  NH2   . ARG A 1 2836 ? 221.693 180.402 214.948 1.00 4.56  ? 2836 ARG A NH2   1 
ATOM   10928 N  N     . LEU A 1 2837 ? 218.839 178.642 222.214 1.00 0.59  ? 2837 LEU A N     1 
ATOM   10929 C  CA    . LEU A 1 2837 ? 217.896 177.665 222.738 1.00 0.81  ? 2837 LEU A CA    1 
ATOM   10930 C  C     . LEU A 1 2837 ? 217.121 178.236 223.920 1.00 1.86  ? 2837 LEU A C     1 
ATOM   10931 O  O     . LEU A 1 2837 ? 217.645 179.028 224.706 1.00 2.97  ? 2837 LEU A O     1 
ATOM   10932 C  CB    . LEU A 1 2837 ? 218.632 176.391 223.138 1.00 1.33  ? 2837 LEU A CB    1 
ATOM   10933 C  CG    . LEU A 1 2837 ? 219.321 175.678 221.971 1.00 1.31  ? 2837 LEU A CG    1 
ATOM   10934 C  CD1   . LEU A 1 2837 ? 220.056 174.447 222.451 1.00 1.15  ? 2837 LEU A CD1   1 
ATOM   10935 C  CD2   . LEU A 1 2837 ? 218.317 175.319 220.882 1.00 0.92  ? 2837 LEU A CD2   1 
ATOM   10936 N  N     . VAL A 1 2838 ? 215.862 177.825 224.036 1.00 2.64  ? 2838 VAL A N     1 
ATOM   10937 C  CA    . VAL A 1 2838 ? 214.948 178.379 225.029 1.00 2.41  ? 2838 VAL A CA    1 
ATOM   10938 C  C     . VAL A 1 2838 ? 214.908 177.494 226.268 1.00 5.29  ? 2838 VAL A C     1 
ATOM   10939 O  O     . VAL A 1 2838 ? 214.923 177.992 227.398 1.00 10.09 ? 2838 VAL A O     1 
ATOM   10940 C  CB    . VAL A 1 2838 ? 213.540 178.554 224.433 1.00 3.30  ? 2838 VAL A CB    1 
ATOM   10941 C  CG1   . VAL A 1 2838 ? 212.586 179.116 225.472 1.00 3.84  ? 2838 VAL A CG1   1 
ATOM   10942 C  CG2   . VAL A 1 2838 ? 213.592 179.444 223.202 1.00 1.16  ? 2838 VAL A CG2   1 
ATOM   10943 N  N     . GLU A 1 2839 ? 214.854 176.183 226.069 1.00 6.93  ? 2839 GLU A N     1 
ATOM   10944 C  CA    . GLU A 1 2839 ? 214.628 175.238 227.151 1.00 7.66  ? 2839 GLU A CA    1 
ATOM   10945 C  C     . GLU A 1 2839 ? 215.934 174.623 227.638 1.00 6.85  ? 2839 GLU A C     1 
ATOM   10946 O  O     . GLU A 1 2839 ? 216.892 174.461 226.878 1.00 8.03  ? 2839 GLU A O     1 
ATOM   10947 C  CB    . GLU A 1 2839 ? 213.661 174.135 226.710 1.00 7.69  ? 2839 GLU A CB    1 
ATOM   10948 C  CG    . GLU A 1 2839 ? 212.186 174.550 226.586 1.00 9.80  ? 2839 GLU A CG    1 
ATOM   10949 C  CD    . GLU A 1 2839 ? 211.667 175.463 227.702 1.00 20.91 ? 2839 GLU A CD    1 
ATOM   10950 O  OE1   . GLU A 1 2839 ? 212.232 175.485 228.817 1.00 26.12 ? 2839 GLU A OE1   1 
ATOM   10951 O  OE2   . GLU A 1 2839 ? 210.674 176.175 227.453 1.00 25.35 ? 2839 GLU A OE2   1 
ATOM   10952 N  N     . ASP A 1 2840 ? 215.954 174.277 228.928 1.00 13.94 ? 2840 ASP A N     1 
ATOM   10953 C  CA    . ASP A 1 2840 ? 217.135 173.659 229.525 1.00 8.18  ? 2840 ASP A CA    1 
ATOM   10954 C  C     . ASP A 1 2840 ? 217.387 172.265 228.970 1.00 9.13  ? 2840 ASP A C     1 
ATOM   10955 O  O     . ASP A 1 2840 ? 218.542 171.833 228.884 1.00 12.07 ? 2840 ASP A O     1 
ATOM   10956 C  CB    . ASP A 1 2840 ? 216.982 173.602 231.044 1.00 11.47 ? 2840 ASP A CB    1 
ATOM   10957 C  CG    . ASP A 1 2840 ? 217.578 174.813 231.734 1.00 20.09 ? 2840 ASP A CG    1 
ATOM   10958 O  OD1   . ASP A 1 2840 ? 218.336 175.560 231.082 1.00 17.27 ? 2840 ASP A OD1   1 
ATOM   10959 O  OD2   . ASP A 1 2840 ? 217.288 175.017 232.931 1.00 23.24 ? 2840 ASP A OD2   1 
ATOM   10960 N  N     . GLU A 1 2841 ? 216.327 171.539 228.610 1.00 9.19  ? 2841 GLU A N     1 
ATOM   10961 C  CA    . GLU A 1 2841 ? 216.507 170.246 227.960 1.00 9.79  ? 2841 GLU A CA    1 
ATOM   10962 C  C     . GLU A 1 2841 ? 217.212 170.400 226.621 1.00 8.97  ? 2841 GLU A C     1 
ATOM   10963 O  O     . GLU A 1 2841 ? 218.102 169.610 226.283 1.00 9.57  ? 2841 GLU A O     1 
ATOM   10964 C  CB    . GLU A 1 2841 ? 215.152 169.563 227.774 1.00 7.90  ? 2841 GLU A CB    1 
ATOM   10965 C  CG    . GLU A 1 2841 ? 215.230 168.187 227.139 1.00 13.91 ? 2841 GLU A CG    1 
ATOM   10966 C  CD    . GLU A 1 2841 ? 215.949 167.174 228.005 1.00 27.24 ? 2841 GLU A CD    1 
ATOM   10967 O  OE1   . GLU A 1 2841 ? 215.965 167.343 229.243 1.00 22.46 ? 2841 GLU A OE1   1 
ATOM   10968 O  OE2   . GLU A 1 2841 ? 216.499 166.202 227.446 1.00 37.32 ? 2841 GLU A OE2   1 
ATOM   10969 N  N     . GLU A 1 2842 ? 216.827 171.415 225.845 1.00 4.32  ? 2842 GLU A N     1 
ATOM   10970 C  CA    . GLU A 1 2842 ? 217.462 171.649 224.553 1.00 4.32  ? 2842 GLU A CA    1 
ATOM   10971 C  C     . GLU A 1 2842 ? 218.933 172.006 224.722 1.00 3.22  ? 2842 GLU A C     1 
ATOM   10972 O  O     . GLU A 1 2842 ? 219.789 171.509 223.983 1.00 2.69  ? 2842 GLU A O     1 
ATOM   10973 C  CB    . GLU A 1 2842 ? 216.719 172.755 223.808 1.00 3.99  ? 2842 GLU A CB    1 
ATOM   10974 C  CG    . GLU A 1 2842 ? 215.287 172.405 223.463 1.00 3.98  ? 2842 GLU A CG    1 
ATOM   10975 C  CD    . GLU A 1 2842 ? 214.438 173.627 223.187 1.00 9.74  ? 2842 GLU A CD    1 
ATOM   10976 O  OE1   . GLU A 1 2842 ? 214.945 174.755 223.353 1.00 7.12  ? 2842 GLU A OE1   1 
ATOM   10977 O  OE2   . GLU A 1 2842 ? 213.260 173.461 222.808 1.00 12.90 ? 2842 GLU A OE2   1 
ATOM   10978 N  N     . ARG A 1 2843 ? 219.244 172.861 225.699 1.00 5.06  ? 2843 ARG A N     1 
ATOM   10979 C  CA    . ARG A 1 2843 ? 220.631 173.218 225.965 1.00 5.98  ? 2843 ARG A CA    1 
ATOM   10980 C  C     . ARG A 1 2843 ? 221.422 172.030 226.496 1.00 4.00  ? 2843 ARG A C     1 
ATOM   10981 O  O     . ARG A 1 2843 ? 222.612 171.892 226.190 1.00 2.17  ? 2843 ARG A O     1 
ATOM   10982 C  CB    . ARG A 1 2843 ? 220.689 174.391 226.945 1.00 2.69  ? 2843 ARG A CB    1 
ATOM   10983 C  CG    . ARG A 1 2843 ? 219.915 175.612 226.475 1.00 3.32  ? 2843 ARG A CG    1 
ATOM   10984 C  CD    . ARG A 1 2843 ? 220.197 176.837 227.324 1.00 6.01  ? 2843 ARG A CD    1 
ATOM   10985 N  NE    . ARG A 1 2843 ? 219.287 176.931 228.459 1.00 9.23  ? 2843 ARG A NE    1 
ATOM   10986 C  CZ    . ARG A 1 2843 ? 218.265 177.771 228.538 1.00 9.97  ? 2843 ARG A CZ    1 
ATOM   10987 N  NH1   . ARG A 1 2843 ? 217.994 178.623 227.563 1.00 6.63  ? 2843 ARG A NH1   1 
ATOM   10988 N  NH2   . ARG A 1 2843 ? 217.490 177.753 229.620 1.00 12.90 ? 2843 ARG A NH2   1 
ATOM   10989 N  N     . ARG A 1 2844 ? 220.784 171.171 227.293 1.00 5.33  ? 2844 ARG A N     1 
ATOM   10990 C  CA    . ARG A 1 2844 ? 221.455 169.968 227.775 1.00 3.98  ? 2844 ARG A CA    1 
ATOM   10991 C  C     . ARG A 1 2844 ? 221.794 169.027 226.626 1.00 3.14  ? 2844 ARG A C     1 
ATOM   10992 O  O     . ARG A 1 2844 ? 222.890 168.458 226.585 1.00 2.21  ? 2844 ARG A O     1 
ATOM   10993 C  CB    . ARG A 1 2844 ? 220.581 169.264 228.813 1.00 8.32  ? 2844 ARG A CB    1 
ATOM   10994 C  CG    . ARG A 1 2844 ? 221.359 168.577 229.918 1.00 8.96  ? 2844 ARG A CG    1 
ATOM   10995 C  CD    . ARG A 1 2844 ? 220.429 167.965 230.954 1.00 17.66 ? 2844 ARG A CD    1 
ATOM   10996 N  NE    . ARG A 1 2844 ? 219.602 168.969 231.613 1.00 21.25 ? 2844 ARG A NE    1 
ATOM   10997 C  CZ    . ARG A 1 2844 ? 218.291 169.087 231.449 1.00 22.01 ? 2844 ARG A CZ    1 
ATOM   10998 N  NH1   . ARG A 1 2844 ? 217.617 168.276 230.650 1.00 19.64 ? 2844 ARG A NH1   1 
ATOM   10999 N  NH2   . ARG A 1 2844 ? 217.641 170.046 232.101 1.00 16.64 ? 2844 ARG A NH2   1 
ATOM   11000 N  N     . TRP A 1 2845 ? 220.863 168.852 225.685 1.00 4.09  ? 2845 TRP A N     1 
ATOM   11001 C  CA    . TRP A 1 2845 ? 221.122 167.989 224.536 1.00 2.18  ? 2845 TRP A CA    1 
ATOM   11002 C  C     . TRP A 1 2845 ? 222.284 168.513 223.703 1.00 2.96  ? 2845 TRP A C     1 
ATOM   11003 O  O     . TRP A 1 2845 ? 223.158 167.744 223.288 1.00 4.85  ? 2845 TRP A O     1 
ATOM   11004 C  CB    . TRP A 1 2845 ? 219.864 167.864 223.678 1.00 2.06  ? 2845 TRP A CB    1 
ATOM   11005 C  CG    . TRP A 1 2845 ? 220.036 166.986 222.474 1.00 2.62  ? 2845 TRP A CG    1 
ATOM   11006 C  CD1   . TRP A 1 2845 ? 219.725 165.662 222.379 1.00 4.26  ? 2845 TRP A CD1   1 
ATOM   11007 C  CD2   . TRP A 1 2845 ? 220.556 167.367 221.195 1.00 3.19  ? 2845 TRP A CD2   1 
ATOM   11008 N  NE1   . TRP A 1 2845 ? 220.021 165.195 221.124 1.00 3.49  ? 2845 TRP A NE1   1 
ATOM   11009 C  CE2   . TRP A 1 2845 ? 220.531 166.222 220.376 1.00 3.53  ? 2845 TRP A CE2   1 
ATOM   11010 C  CE3   . TRP A 1 2845 ? 221.041 168.565 220.663 1.00 2.48  ? 2845 TRP A CE3   1 
ATOM   11011 C  CZ2   . TRP A 1 2845 ? 220.974 166.238 219.055 1.00 2.80  ? 2845 TRP A CZ2   1 
ATOM   11012 C  CZ3   . TRP A 1 2845 ? 221.482 168.580 219.354 1.00 4.58  ? 2845 TRP A CZ3   1 
ATOM   11013 C  CH2   . TRP A 1 2845 ? 221.443 167.424 218.565 1.00 4.01  ? 2845 TRP A CH2   1 
ATOM   11014 N  N     . THR A 1 2846 ? 222.305 169.823 223.443 1.00 3.33  ? 2846 THR A N     1 
ATOM   11015 C  CA    . THR A 1 2846 ? 223.384 170.409 222.658 1.00 2.44  ? 2846 THR A CA    1 
ATOM   11016 C  C     . THR A 1 2846 ? 224.724 170.245 223.360 1.00 2.69  ? 2846 THR A C     1 
ATOM   11017 O  O     . THR A 1 2846 ? 225.732 169.918 222.726 1.00 3.18  ? 2846 THR A O     1 
ATOM   11018 C  CB    . THR A 1 2846 ? 223.088 171.886 222.392 1.00 3.85  ? 2846 THR A CB    1 
ATOM   11019 O  OG1   . THR A 1 2846 ? 221.912 171.995 221.582 1.00 7.01  ? 2846 THR A OG1   1 
ATOM   11020 C  CG2   . THR A 1 2846 ? 224.250 172.555 221.675 1.00 1.30  ? 2846 THR A CG2   1 
ATOM   11021 N  N     . ASP A 1 2847 ? 224.748 170.456 224.677 1.00 4.00  ? 2847 ASP A N     1 
ATOM   11022 C  CA    . ASP A 1 2847 ? 225.984 170.311 225.435 1.00 4.43  ? 2847 ASP A CA    1 
ATOM   11023 C  C     . ASP A 1 2847 ? 226.500 168.877 225.389 1.00 5.93  ? 2847 ASP A C     1 
ATOM   11024 O  O     . ASP A 1 2847 ? 227.708 168.647 225.263 1.00 6.37  ? 2847 ASP A O     1 
ATOM   11025 C  CB    . ASP A 1 2847 ? 225.754 170.758 226.878 1.00 6.59  ? 2847 ASP A CB    1 
ATOM   11026 C  CG    . ASP A 1 2847 ? 227.036 171.141 227.580 1.00 18.52 ? 2847 ASP A CG    1 
ATOM   11027 O  OD1   . ASP A 1 2847 ? 227.742 172.044 227.085 1.00 16.56 ? 2847 ASP A OD1   1 
ATOM   11028 O  OD2   . ASP A 1 2847 ? 227.338 170.536 228.630 1.00 22.98 ? 2847 ASP A OD2   1 
ATOM   11029 N  N     . GLU A 1 2848 ? 225.597 167.900 225.488 1.00 8.07  ? 2848 GLU A N     1 
ATOM   11030 C  CA    . GLU A 1 2848 ? 226.018 166.502 225.492 1.00 4.66  ? 2848 GLU A CA    1 
ATOM   11031 C  C     . GLU A 1 2848 ? 226.526 166.064 224.123 1.00 6.96  ? 2848 GLU A C     1 
ATOM   11032 O  O     . GLU A 1 2848 ? 227.575 165.418 224.022 1.00 10.45 ? 2848 GLU A O     1 
ATOM   11033 C  CB    . GLU A 1 2848 ? 224.862 165.612 225.944 1.00 5.84  ? 2848 GLU A CB    1 
ATOM   11034 C  CG    . GLU A 1 2848 ? 225.044 164.141 225.616 1.00 17.36 ? 2848 GLU A CG    1 
ATOM   11035 C  CD    . GLU A 1 2848 ? 226.173 163.504 226.404 1.00 23.35 ? 2848 GLU A CD    1 
ATOM   11036 O  OE1   . GLU A 1 2848 ? 227.195 163.136 225.788 1.00 18.97 ? 2848 GLU A OE1   1 
ATOM   11037 O  OE2   . GLU A 1 2848 ? 226.037 163.373 227.638 1.00 21.86 ? 2848 GLU A OE2   1 
ATOM   11038 N  N     . ASN A 1 2849 ? 225.804 166.414 223.058 1.00 7.95  ? 2849 ASN A N     1 
ATOM   11039 C  CA    . ASN A 1 2849 ? 226.148 165.917 221.733 1.00 4.56  ? 2849 ASN A CA    1 
ATOM   11040 C  C     . ASN A 1 2849 ? 227.378 166.600 221.149 1.00 5.60  ? 2849 ASN A C     1 
ATOM   11041 O  O     . ASN A 1 2849 ? 227.983 166.060 220.219 1.00 7.14  ? 2849 ASN A O     1 
ATOM   11042 C  CB    . ASN A 1 2849 ? 224.952 166.070 220.797 1.00 4.52  ? 2849 ASN A CB    1 
ATOM   11043 C  CG    . ASN A 1 2849 ? 223.913 164.987 221.012 1.00 8.87  ? 2849 ASN A CG    1 
ATOM   11044 O  OD1   . ASN A 1 2849 ? 222.953 165.171 221.757 1.00 6.03  ? 2849 ASN A OD1   1 
ATOM   11045 N  ND2   . ASN A 1 2849 ? 224.108 163.843 220.367 1.00 10.33 ? 2849 ASN A ND2   1 
ATOM   11046 N  N     . ILE A 1 2850 ? 227.758 167.769 221.668 1.00 5.01  ? 2850 ILE A N     1 
ATOM   11047 C  CA    . ILE A 1 2850 ? 229.041 168.355 221.294 1.00 3.85  ? 2850 ILE A CA    1 
ATOM   11048 C  C     . ILE A 1 2850 ? 230.178 167.445 221.738 1.00 7.93  ? 2850 ILE A C     1 
ATOM   11049 O  O     . ILE A 1 2850 ? 231.137 167.209 220.993 1.00 9.79  ? 2850 ILE A O     1 
ATOM   11050 C  CB    . ILE A 1 2850 ? 229.173 169.772 221.885 1.00 4.53  ? 2850 ILE A CB    1 
ATOM   11051 C  CG1   . ILE A 1 2850 ? 228.334 170.764 221.083 1.00 3.60  ? 2850 ILE A CG1   1 
ATOM   11052 C  CG2   . ILE A 1 2850 ? 230.619 170.225 221.900 1.00 2.87  ? 2850 ILE A CG2   1 
ATOM   11053 C  CD1   . ILE A 1 2850 ? 228.278 172.143 221.681 1.00 2.17  ? 2850 ILE A CD1   1 
ATOM   11054 N  N     . ASP A 1 2851 ? 230.082 166.910 222.957 1.00 10.15 ? 2851 ASP A N     1 
ATOM   11055 C  CA    . ASP A 1 2851 ? 231.078 165.959 223.438 1.00 9.22  ? 2851 ASP A CA    1 
ATOM   11056 C  C     . ASP A 1 2851 ? 231.044 164.662 222.640 1.00 11.14 ? 2851 ASP A C     1 
ATOM   11057 O  O     . ASP A 1 2851 ? 232.094 164.087 222.333 1.00 15.64 ? 2851 ASP A O     1 
ATOM   11058 C  CB    . ASP A 1 2851 ? 230.856 165.684 224.925 1.00 10.76 ? 2851 ASP A CB    1 
ATOM   11059 C  CG    . ASP A 1 2851 ? 230.991 166.933 225.774 1.00 15.28 ? 2851 ASP A CG    1 
ATOM   11060 O  OD1   . ASP A 1 2851 ? 232.078 167.545 225.770 1.00 19.77 ? 2851 ASP A OD1   1 
ATOM   11061 O  OD2   . ASP A 1 2851 ? 230.005 167.307 226.439 1.00 19.26 ? 2851 ASP A OD2   1 
ATOM   11062 N  N     . THR A 1 2852 ? 229.845 164.182 222.303 1.00 5.86  ? 2852 THR A N     1 
ATOM   11063 C  CA    . THR A 1 2852 ? 229.725 162.926 221.568 1.00 6.66  ? 2852 THR A CA    1 
ATOM   11064 C  C     . THR A 1 2852 ? 230.354 163.030 220.184 1.00 9.92  ? 2852 THR A C     1 
ATOM   11065 O  O     . THR A 1 2852 ? 231.123 162.155 219.771 1.00 11.47 ? 2852 THR A O     1 
ATOM   11066 C  CB    . THR A 1 2852 ? 228.252 162.527 221.455 1.00 7.93  ? 2852 THR A CB    1 
ATOM   11067 O  OG1   . THR A 1 2852 ? 227.696 162.357 222.764 1.00 13.95 ? 2852 THR A OG1   1 
ATOM   11068 C  CG2   . THR A 1 2852 ? 228.110 161.232 220.674 1.00 10.79 ? 2852 THR A CG2   1 
ATOM   11069 N  N     . VAL A 1 2853 ? 230.036 164.100 219.451 1.00 7.29  ? 2853 VAL A N     1 
ATOM   11070 C  CA    . VAL A 1 2853 ? 230.550 164.256 218.095 1.00 5.71  ? 2853 VAL A CA    1 
ATOM   11071 C  C     . VAL A 1 2853 ? 232.066 164.415 218.106 1.00 6.45  ? 2853 VAL A C     1 
ATOM   11072 O  O     . VAL A 1 2853 ? 232.769 163.827 217.277 1.00 12.02 ? 2853 VAL A O     1 
ATOM   11073 C  CB    . VAL A 1 2853 ? 229.856 165.441 217.396 1.00 6.98  ? 2853 VAL A CB    1 
ATOM   11074 C  CG1   . VAL A 1 2853 ? 230.560 165.787 216.098 1.00 3.43  ? 2853 VAL A CG1   1 
ATOM   11075 C  CG2   . VAL A 1 2853 ? 228.393 165.120 217.136 1.00 1.93  ? 2853 VAL A CG2   1 
ATOM   11076 N  N     . ALA A 1 2854 ? 232.592 165.202 219.046 1.00 6.40  ? 2854 ALA A N     1 
ATOM   11077 C  CA    . ALA A 1 2854 ? 234.024 165.491 219.062 1.00 5.62  ? 2854 ALA A CA    1 
ATOM   11078 C  C     . ALA A 1 2854 ? 234.853 164.232 219.287 1.00 10.06 ? 2854 ALA A C     1 
ATOM   11079 O  O     . ALA A 1 2854 ? 235.869 164.024 218.617 1.00 16.97 ? 2854 ALA A O     1 
ATOM   11080 C  CB    . ALA A 1 2854 ? 234.336 166.530 220.136 1.00 4.11  ? 2854 ALA A CB    1 
ATOM   11081 N  N     . LEU A 1 2855 ? 234.445 163.386 220.234 1.00 11.76 ? 2855 LEU A N     1 
ATOM   11082 C  CA    . LEU A 1 2855 ? 235.224 162.184 220.520 1.00 13.78 ? 2855 LEU A CA    1 
ATOM   11083 C  C     . LEU A 1 2855 ? 235.043 161.122 219.445 1.00 14.02 ? 2855 LEU A C     1 
ATOM   11084 O  O     . LEU A 1 2855 ? 235.926 160.278 219.259 1.00 22.49 ? 2855 LEU A O     1 
ATOM   11085 C  CB    . LEU A 1 2855 ? 234.860 161.626 221.897 1.00 16.01 ? 2855 LEU A CB    1 
ATOM   11086 C  CG    . LEU A 1 2855 ? 235.577 162.230 223.111 1.00 19.30 ? 2855 LEU A CG    1 
ATOM   11087 C  CD1   . LEU A 1 2855 ? 237.067 161.935 223.036 1.00 22.86 ? 2855 LEU A CD1   1 
ATOM   11088 C  CD2   . LEU A 1 2855 ? 235.343 163.728 223.242 1.00 13.03 ? 2855 LEU A CD2   1 
ATOM   11089 N  N     . LYS A 1 2856 ? 233.915 161.141 218.736 1.00 7.19  ? 2856 LYS A N     1 
ATOM   11090 C  CA    . LYS A 1 2856 ? 233.729 160.204 217.634 1.00 8.51  ? 2856 LYS A CA    1 
ATOM   11091 C  C     . LYS A 1 2856 ? 234.727 160.469 216.514 1.00 8.44  ? 2856 LYS A C     1 
ATOM   11092 O  O     . LYS A 1 2856 ? 235.273 159.530 215.923 1.00 11.88 ? 2856 LYS A O     1 
ATOM   11093 C  CB    . LYS A 1 2856 ? 232.293 160.282 217.116 1.00 7.08  ? 2856 LYS A CB    1 
ATOM   11094 C  CG    . LYS A 1 2856 ? 232.076 159.593 215.782 1.00 7.57  ? 2856 LYS A CG    1 
ATOM   11095 C  CD    . LYS A 1 2856 ? 230.690 159.875 215.241 1.00 12.06 ? 2856 LYS A CD    1 
ATOM   11096 C  CE    . LYS A 1 2856 ? 230.534 159.345 213.827 1.00 11.30 ? 2856 LYS A CE    1 
ATOM   11097 N  NZ    . LYS A 1 2856 ? 229.155 159.564 213.310 1.00 13.10 ? 2856 LYS A NZ    1 
ATOM   11098 N  N     . HIS A 1 2857 ? 234.985 161.742 216.213 1.00 6.32  ? 2857 HIS A N     1 
ATOM   11099 C  CA    . HIS A 1 2857 ? 235.918 162.104 215.154 1.00 6.34  ? 2857 HIS A CA    1 
ATOM   11100 C  C     . HIS A 1 2857 ? 237.327 162.383 215.655 1.00 8.07  ? 2857 HIS A C     1 
ATOM   11101 O  O     . HIS A 1 2857 ? 238.261 162.399 214.847 1.00 9.73  ? 2857 HIS A O     1 
ATOM   11102 C  CB    . HIS A 1 2857 ? 235.407 163.329 214.388 1.00 4.87  ? 2857 HIS A CB    1 
ATOM   11103 C  CG    . HIS A 1 2857 ? 234.051 163.141 213.789 1.00 6.17  ? 2857 HIS A CG    1 
ATOM   11104 N  ND1   . HIS A 1 2857 ? 233.859 162.573 212.549 1.00 5.93  ? 2857 HIS A ND1   1 
ATOM   11105 C  CD2   . HIS A 1 2857 ? 232.818 163.442 214.259 1.00 7.29  ? 2857 HIS A CD2   1 
ATOM   11106 C  CE1   . HIS A 1 2857 ? 232.567 162.531 212.281 1.00 7.74  ? 2857 HIS A CE1   1 
ATOM   11107 N  NE2   . HIS A 1 2857 ? 231.913 163.055 213.301 1.00 6.52  ? 2857 HIS A NE2   1 
ATOM   11108 N  N     . PHE A 1 2858 ? 237.510 162.600 216.956 1.00 10.23 ? 2858 PHE A N     1 
ATOM   11109 C  CA    . PHE A 1 2858 ? 238.827 162.867 217.533 1.00 9.82  ? 2858 PHE A CA    1 
ATOM   11110 C  C     . PHE A 1 2858 ? 239.070 161.928 218.707 1.00 17.01 ? 2858 PHE A C     1 
ATOM   11111 O  O     . PHE A 1 2858 ? 238.944 162.329 219.871 1.00 23.00 ? 2858 PHE A O     1 
ATOM   11112 C  CB    . PHE A 1 2858 ? 238.954 164.328 217.966 1.00 5.07  ? 2858 PHE A CB    1 
ATOM   11113 C  CG    . PHE A 1 2858 ? 239.020 165.294 216.822 1.00 4.76  ? 2858 PHE A CG    1 
ATOM   11114 C  CD1   . PHE A 1 2858 ? 240.234 165.616 216.239 1.00 3.87  ? 2858 PHE A CD1   1 
ATOM   11115 C  CD2   . PHE A 1 2858 ? 237.867 165.876 216.322 1.00 3.76  ? 2858 PHE A CD2   1 
ATOM   11116 C  CE1   . PHE A 1 2858 ? 240.296 166.501 215.186 1.00 2.98  ? 2858 PHE A CE1   1 
ATOM   11117 C  CE2   . PHE A 1 2858 ? 237.925 166.763 215.269 1.00 1.88  ? 2858 PHE A CE2   1 
ATOM   11118 C  CZ    . PHE A 1 2858 ? 239.140 167.076 214.700 1.00 1.46  ? 2858 PHE A CZ    1 
ATOM   11119 N  N     . PRO A 1 2859 ? 239.405 160.672 218.443 1.00 19.92 ? 2859 PRO A N     1 
ATOM   11120 C  CA    . PRO A 1 2859 ? 239.850 159.778 219.513 1.00 19.71 ? 2859 PRO A CA    1 
ATOM   11121 C  C     . PRO A 1 2859 ? 241.250 160.172 219.970 1.00 20.92 ? 2859 PRO A C     1 
ATOM   11122 O  O     . PRO A 1 2859 ? 241.888 161.059 219.407 1.00 28.90 ? 2859 PRO A O     1 
ATOM   11123 C  CB    . PRO A 1 2859 ? 239.853 158.400 218.847 1.00 18.65 ? 2859 PRO A CB    1 
ATOM   11124 C  CG    . PRO A 1 2859 ? 238.914 158.519 217.715 1.00 14.30 ? 2859 PRO A CG    1 
ATOM   11125 C  CD    . PRO A 1 2859 ? 239.074 159.922 217.218 1.00 18.88 ? 2859 PRO A CD    1 
ATOM   11126 N  N     . ASN A 1 2860 ? 241.723 159.484 221.009 1.00 15.44 ? 2860 ASN A N     1 
ATOM   11127 C  CA    . ASN A 1 2860 ? 243.097 159.625 221.490 1.00 21.10 ? 2860 ASN A CA    1 
ATOM   11128 C  C     . ASN A 1 2860 ? 243.415 161.071 221.865 1.00 22.64 ? 2860 ASN A C     1 
ATOM   11129 O  O     . ASN A 1 2860 ? 244.515 161.567 221.622 1.00 29.23 ? 2860 ASN A O     1 
ATOM   11130 C  CB    . ASN A 1 2860 ? 244.093 159.101 220.455 1.00 19.31 ? 2860 ASN A CB    1 
ATOM   11131 C  CG    . ASN A 1 2860 ? 243.624 157.821 219.795 1.00 25.09 ? 2860 ASN A CG    1 
ATOM   11132 O  OD1   . ASN A 1 2860 ? 243.426 157.772 218.582 1.00 26.61 ? 2860 ASN A OD1   1 
ATOM   11133 N  ND2   . ASN A 1 2860 ? 243.430 156.779 220.595 1.00 22.11 ? 2860 ASN A ND2   1 
ATOM   11134 N  N     . ILE A 1 2861 ? 242.440 161.751 222.462 1.00 19.70 ? 2861 ILE A N     1 
ATOM   11135 C  CA    . ILE A 1 2861 ? 242.616 163.109 222.956 1.00 17.14 ? 2861 ILE A CA    1 
ATOM   11136 C  C     . ILE A 1 2861 ? 242.238 163.126 224.428 1.00 19.63 ? 2861 ILE A C     1 
ATOM   11137 O  O     . ILE A 1 2861 ? 241.456 162.292 224.897 1.00 26.07 ? 2861 ILE A O     1 
ATOM   11138 C  CB    . ILE A 1 2861 ? 241.772 164.137 222.174 1.00 19.49 ? 2861 ILE A CB    1 
ATOM   11139 C  CG1   . ILE A 1 2861 ? 240.281 163.830 222.332 1.00 20.29 ? 2861 ILE A CG1   1 
ATOM   11140 C  CG2   . ILE A 1 2861 ? 242.168 164.149 220.709 1.00 21.44 ? 2861 ILE A CG2   1 
ATOM   11141 C  CD1   . ILE A 1 2861 ? 239.379 164.916 221.797 1.00 24.77 ? 2861 ILE A CD1   1 
ATOM   11142 N  N     . ASP A 1 2862 ? 242.798 164.082 225.161 1.00 20.35 ? 2862 ASP A N     1 
ATOM   11143 C  CA    . ASP A 1 2862 ? 242.517 164.207 226.589 1.00 21.40 ? 2862 ASP A CA    1 
ATOM   11144 C  C     . ASP A 1 2862 ? 241.191 164.948 226.723 1.00 21.09 ? 2862 ASP A C     1 
ATOM   11145 O  O     . ASP A 1 2862 ? 241.115 166.157 226.497 1.00 22.01 ? 2862 ASP A O     1 
ATOM   11146 C  CB    . ASP A 1 2862 ? 243.663 164.921 227.300 1.00 14.26 ? 2862 ASP A CB    1 
ATOM   11147 C  CG    . ASP A 1 2862 ? 243.306 165.377 228.711 1.00 26.37 ? 2862 ASP A CG    1 
ATOM   11148 O  OD1   . ASP A 1 2862 ? 242.309 164.890 229.287 1.00 22.58 ? 2862 ASP A OD1   1 
ATOM   11149 O  OD2   . ASP A 1 2862 ? 244.044 166.223 229.256 1.00 36.54 ? 2862 ASP A OD2   1 
ATOM   11150 N  N     . ARG A 1 2863 ? 240.146 164.211 227.105 1.00 21.47 ? 2863 ARG A N     1 
ATOM   11151 C  CA    . ARG A 1 2863 ? 238.794 164.763 227.145 1.00 20.92 ? 2863 ARG A CA    1 
ATOM   11152 C  C     . ARG A 1 2863 ? 238.703 165.968 228.073 1.00 24.77 ? 2863 ARG A C     1 
ATOM   11153 O  O     . ARG A 1 2863 ? 238.102 166.990 227.724 1.00 23.74 ? 2863 ARG A O     1 
ATOM   11154 C  CB    . ARG A 1 2863 ? 237.810 163.678 227.586 1.00 15.56 ? 2863 ARG A CB    1 
ATOM   11155 C  CG    . ARG A 1 2863 ? 236.347 164.091 227.591 1.00 26.07 ? 2863 ARG A CG    1 
ATOM   11156 C  CD    . ARG A 1 2863 ? 235.465 162.903 227.960 1.00 28.60 ? 2863 ARG A CD    1 
ATOM   11157 N  NE    . ARG A 1 2863 ? 234.053 163.249 228.071 1.00 24.59 ? 2863 ARG A NE    1 
ATOM   11158 C  CZ    . ARG A 1 2863 ? 233.192 163.260 227.063 1.00 26.91 ? 2863 ARG A CZ    1 
ATOM   11159 N  NH1   . ARG A 1 2863 ? 233.560 162.935 225.835 1.00 28.42 ? 2863 ARG A NH1   1 
ATOM   11160 N  NH2   . ARG A 1 2863 ? 231.926 163.594 227.294 1.00 26.67 ? 2863 ARG A NH2   1 
ATOM   11161 N  N     . GLU A 1 2864 ? 239.296 165.866 229.266 1.00 25.23 ? 2864 GLU A N     1 
ATOM   11162 C  CA    . GLU A 1 2864 ? 239.117 166.907 230.273 1.00 20.07 ? 2864 GLU A CA    1 
ATOM   11163 C  C     . GLU A 1 2864 ? 239.728 168.231 229.828 1.00 23.25 ? 2864 GLU A C     1 
ATOM   11164 O  O     . GLU A 1 2864 ? 239.098 169.287 229.960 1.00 26.27 ? 2864 GLU A O     1 
ATOM   11165 C  CB    . GLU A 1 2864 ? 239.708 166.441 231.607 1.00 24.66 ? 2864 GLU A CB    1 
ATOM   11166 C  CG    . GLU A 1 2864 ? 239.757 167.495 232.712 1.00 27.43 ? 2864 GLU A CG    1 
ATOM   11167 C  CD    . GLU A 1 2864 ? 241.045 168.298 232.714 1.00 32.41 ? 2864 GLU A CD    1 
ATOM   11168 O  OE1   . GLU A 1 2864 ? 241.940 167.992 231.898 1.00 30.05 ? 2864 GLU A OE1   1 
ATOM   11169 O  OE2   . GLU A 1 2864 ? 241.164 169.229 233.537 1.00 33.93 ? 2864 GLU A OE2   1 
ATOM   11170 N  N     . LYS A 1 2865 ? 240.947 168.199 229.286 1.00 20.80 ? 2865 LYS A N     1 
ATOM   11171 C  CA    . LYS A 1 2865 ? 241.615 169.433 228.890 1.00 19.49 ? 2865 LYS A CA    1 
ATOM   11172 C  C     . LYS A 1 2865 ? 240.970 170.074 227.669 1.00 21.55 ? 2865 LYS A C     1 
ATOM   11173 O  O     . LYS A 1 2865 ? 241.111 171.288 227.477 1.00 31.54 ? 2865 LYS A O     1 
ATOM   11174 C  CB    . LYS A 1 2865 ? 243.103 169.158 228.638 1.00 18.87 ? 2865 LYS A CB    1 
ATOM   11175 C  CG    . LYS A 1 2865 ? 243.985 170.394 228.429 1.00 26.23 ? 2865 LYS A CG    1 
ATOM   11176 C  CD    . LYS A 1 2865 ? 244.138 170.786 226.964 1.00 20.05 ? 2865 LYS A CD    1 
ATOM   11177 C  CE    . LYS A 1 2865 ? 245.073 171.981 226.819 1.00 25.75 ? 2865 LYS A CE    1 
ATOM   11178 N  NZ    . LYS A 1 2865 ? 245.223 172.418 225.403 1.00 15.30 ? 2865 LYS A NZ    1 
ATOM   11179 N  N     . ALA A 1 2866 ? 240.250 169.306 226.866 1.00 19.24 ? 2866 ALA A N     1 
ATOM   11180 C  CA    . ALA A 1 2866 ? 239.599 169.823 225.673 1.00 15.28 ? 2866 ALA A CA    1 
ATOM   11181 C  C     . ALA A 1 2866 ? 238.122 170.124 225.858 1.00 15.11 ? 2866 ALA A C     1 
ATOM   11182 O  O     . ALA A 1 2866 ? 237.602 171.010 225.177 1.00 17.44 ? 2866 ALA A O     1 
ATOM   11183 C  CB    . ALA A 1 2866 ? 239.756 168.832 224.509 1.00 15.93 ? 2866 ALA A CB    1 
ATOM   11184 N  N     . MET A 1 2867 ? 237.430 169.428 226.761 1.00 19.24 ? 2867 MET A N     1 
ATOM   11185 C  CA    . MET A 1 2867 ? 235.980 169.536 226.840 1.00 11.95 ? 2867 MET A CA    1 
ATOM   11186 C  C     . MET A 1 2867 ? 235.487 169.867 228.246 1.00 14.57 ? 2867 MET A C     1 
ATOM   11187 O  O     . MET A 1 2867 ? 234.345 169.545 228.584 1.00 20.21 ? 2867 MET A O     1 
ATOM   11188 C  CB    . MET A 1 2867 ? 235.329 168.248 226.338 1.00 17.37 ? 2867 MET A CB    1 
ATOM   11189 C  CG    . MET A 1 2867 ? 235.525 168.032 224.847 1.00 19.86 ? 2867 MET A CG    1 
ATOM   11190 S  SD    . MET A 1 2867 ? 234.790 169.348 223.868 1.00 34.54 ? 2867 MET A SD    1 
ATOM   11191 C  CE    . MET A 1 2867 ? 233.506 168.467 223.005 1.00 15.18 ? 2867 MET A CE    1 
ATOM   11192 N  N     . SER A 1 2868 ? 236.319 170.502 229.069 1.00 14.03 ? 2868 SER A N     1 
ATOM   11193 C  CA    . SER A 1 2868 ? 235.887 170.977 230.379 1.00 9.70  ? 2868 SER A CA    1 
ATOM   11194 C  C     . SER A 1 2868 ? 234.690 171.901 230.234 1.00 13.41 ? 2868 SER A C     1 
ATOM   11195 O  O     . SER A 1 2868 ? 234.765 172.925 229.549 1.00 19.18 ? 2868 SER A O     1 
ATOM   11196 C  CB    . SER A 1 2868 ? 237.035 171.708 231.079 1.00 12.26 ? 2868 SER A CB    1 
ATOM   11197 O  OG    . SER A 1 2868 ? 238.119 170.837 231.342 1.00 21.04 ? 2868 SER A OG    1 
ATOM   11198 N  N     . ARG A 1 2869 ? 233.586 171.541 230.890 1.00 15.92 ? 2869 ARG A N     1 
ATOM   11199 C  CA    . ARG A 1 2869 ? 232.288 172.154 230.604 1.00 15.98 ? 2869 ARG A CA    1 
ATOM   11200 C  C     . ARG A 1 2869 ? 232.268 173.675 230.694 1.00 22.65 ? 2869 ARG A C     1 
ATOM   11201 O  O     . ARG A 1 2869 ? 231.647 174.307 229.825 1.00 33.44 ? 2869 ARG A O     1 
ATOM   11202 C  CB    . ARG A 1 2869 ? 231.223 171.515 231.505 1.00 20.51 ? 2869 ARG A CB    1 
ATOM   11203 C  CG    . ARG A 1 2869 ? 230.799 170.095 231.086 1.00 20.09 ? 2869 ARG A CG    1 
ATOM   11204 C  CD    . ARG A 1 2869 ? 230.281 170.032 229.637 1.00 24.96 ? 2869 ARG A CD    1 
ATOM   11205 N  NE    . ARG A 1 2869 ? 231.324 170.102 228.618 1.00 23.05 ? 2869 ARG A NE    1 
ATOM   11206 C  CZ    . ARG A 1 2869 ? 231.100 170.165 227.312 1.00 16.05 ? 2869 ARG A CZ    1 
ATOM   11207 N  NH1   . ARG A 1 2869 ? 229.873 170.202 226.823 1.00 13.66 ? 2869 ARG A NH1   1 
ATOM   11208 N  NH2   . ARG A 1 2869 ? 232.133 170.199 226.478 1.00 14.18 ? 2869 ARG A NH2   1 
ATOM   11209 N  N     . PRO A 1 2870 ? 232.897 174.327 231.678 1.00 18.85 ? 2870 PRO A N     1 
ATOM   11210 C  CA    . PRO A 1 2870 ? 232.974 175.793 231.610 1.00 11.33 ? 2870 PRO A CA    1 
ATOM   11211 C  C     . PRO A 1 2870 ? 233.940 176.254 230.527 1.00 6.55  ? 2870 PRO A C     1 
ATOM   11212 O  O     . PRO A 1 2870 ? 235.094 176.584 230.813 1.00 9.11  ? 2870 PRO A O     1 
ATOM   11213 C  CB    . PRO A 1 2870 ? 233.456 176.186 233.012 1.00 8.10  ? 2870 PRO A CB    1 
ATOM   11214 C  CG    . PRO A 1 2870 ? 234.190 174.992 233.499 1.00 11.67 ? 2870 PRO A CG    1 
ATOM   11215 C  CD    . PRO A 1 2870 ? 233.469 173.808 232.934 1.00 10.93 ? 2870 PRO A CD    1 
ATOM   11216 N  N     . ILE A 1 2871 ? 233.482 176.268 229.277 1.00 4.05  ? 2871 ILE A N     1 
ATOM   11217 C  CA    . ILE A 1 2871 ? 234.301 176.707 228.150 1.00 4.84  ? 2871 ILE A CA    1 
ATOM   11218 C  C     . ILE A 1 2871 ? 234.130 178.213 228.001 1.00 2.22  ? 2871 ILE A C     1 
ATOM   11219 O  O     . ILE A 1 2871 ? 233.078 178.688 227.567 1.00 4.27  ? 2871 ILE A O     1 
ATOM   11220 C  CB    . ILE A 1 2871 ? 233.924 175.983 226.853 1.00 5.10  ? 2871 ILE A CB    1 
ATOM   11221 C  CG1   . ILE A 1 2871 ? 233.737 174.487 227.096 1.00 5.27  ? 2871 ILE A CG1   1 
ATOM   11222 C  CG2   . ILE A 1 2871 ? 234.990 176.219 225.797 1.00 3.67  ? 2871 ILE A CG2   1 
ATOM   11223 C  CD1   . ILE A 1 2871 ? 233.515 173.690 225.837 1.00 5.49  ? 2871 ILE A CD1   1 
ATOM   11224 N  N     . LEU A 1 2872 ? 235.170 178.967 228.345 1.00 2.36  ? 2872 LEU A N     1 
ATOM   11225 C  CA    . LEU A 1 2872 ? 235.133 180.419 228.276 1.00 2.01  ? 2872 LEU A CA    1 
ATOM   11226 C  C     . LEU A 1 2872 ? 236.342 180.918 227.504 1.00 1.27  ? 2872 LEU A C     1 
ATOM   11227 O  O     . LEU A 1 2872 ? 237.468 180.475 227.749 1.00 1.51  ? 2872 LEU A O     1 
ATOM   11228 C  CB    . LEU A 1 2872 ? 235.101 181.044 229.674 1.00 5.09  ? 2872 LEU A CB    1 
ATOM   11229 C  CG    . LEU A 1 2872 ? 233.999 180.534 230.602 1.00 2.90  ? 2872 LEU A CG    1 
ATOM   11230 C  CD1   . LEU A 1 2872 ? 234.251 180.987 232.028 1.00 4.04  ? 2872 LEU A CD1   1 
ATOM   11231 C  CD2   . LEU A 1 2872 ? 232.637 180.996 230.116 1.00 1.44  ? 2872 LEU A CD2   1 
ATOM   11232 N  N     . TYR A 1 2873 ? 236.104 181.835 226.574 1.00 1.68  ? 2873 TYR A N     1 
ATOM   11233 C  CA    . TYR A 1 2873 ? 237.156 182.453 225.785 1.00 1.03  ? 2873 TYR A CA    1 
ATOM   11234 C  C     . TYR A 1 2873 ? 237.035 183.963 225.900 1.00 0.67  ? 2873 TYR A C     1 
ATOM   11235 O  O     . TYR A 1 2873 ? 235.928 184.506 225.907 1.00 0.77  ? 2873 TYR A O     1 
ATOM   11236 C  CB    . TYR A 1 2873 ? 237.076 182.025 224.317 1.00 0.45  ? 2873 TYR A CB    1 
ATOM   11237 C  CG    . TYR A 1 2873 ? 237.750 180.706 224.034 1.00 0.38  ? 2873 TYR A CG    1 
ATOM   11238 C  CD1   . TYR A 1 2873 ? 237.136 179.506 224.361 1.00 0.73  ? 2873 TYR A CD1   1 
ATOM   11239 C  CD2   . TYR A 1 2873 ? 239.000 180.660 223.440 1.00 0.54  ? 2873 TYR A CD2   1 
ATOM   11240 C  CE1   . TYR A 1 2873 ? 237.749 178.299 224.105 1.00 0.48  ? 2873 TYR A CE1   1 
ATOM   11241 C  CE2   . TYR A 1 2873 ? 239.618 179.458 223.178 1.00 0.69  ? 2873 TYR A CE2   1 
ATOM   11242 C  CZ    . TYR A 1 2873 ? 238.991 178.282 223.514 1.00 0.55  ? 2873 TYR A CZ    1 
ATOM   11243 O  OH    . TYR A 1 2873 ? 239.610 177.085 223.253 1.00 2.50  ? 2873 TYR A OH    1 
ATOM   11244 N  N     . SER A 1 2874 ? 238.177 184.635 226.004 1.00 0.65  ? 2874 SER A N     1 
ATOM   11245 C  CA    . SER A 1 2874 ? 238.174 186.081 226.159 1.00 1.33  ? 2874 SER A CA    1 
ATOM   11246 C  C     . SER A 1 2874 ? 239.506 186.642 225.694 1.00 1.80  ? 2874 SER A C     1 
ATOM   11247 O  O     . SER A 1 2874 ? 240.533 185.961 225.735 1.00 2.12  ? 2874 SER A O     1 
ATOM   11248 C  CB    . SER A 1 2874 ? 237.908 186.484 227.616 1.00 0.72  ? 2874 SER A CB    1 
ATOM   11249 O  OG    . SER A 1 2874 ? 237.722 187.881 227.732 1.00 0.81  ? 2874 SER A OG    1 
ATOM   11250 N  N     . ASN A 1 2875 ? 239.471 187.898 225.250 1.00 2.04  ? 2875 ASN A N     1 
ATOM   11251 C  CA    . ASN A 1 2875 ? 240.673 188.679 224.997 1.00 3.24  ? 2875 ASN A CA    1 
ATOM   11252 C  C     . ASN A 1 2875 ? 240.850 189.783 226.033 1.00 7.61  ? 2875 ASN A C     1 
ATOM   11253 O  O     . ASN A 1 2875 ? 241.527 190.779 225.769 1.00 11.21 ? 2875 ASN A O     1 
ATOM   11254 C  CB    . ASN A 1 2875 ? 240.646 189.263 223.583 1.00 2.51  ? 2875 ASN A CB    1 
ATOM   11255 C  CG    . ASN A 1 2875 ? 239.354 189.989 223.276 1.00 4.36  ? 2875 ASN A CG    1 
ATOM   11256 O  OD1   . ASN A 1 2875 ? 238.489 190.133 224.137 1.00 7.37  ? 2875 ASN A OD1   1 
ATOM   11257 N  ND2   . ASN A 1 2875 ? 239.214 190.447 222.039 1.00 6.14  ? 2875 ASN A ND2   1 
ATOM   11258 N  N     . TRP A 1 2876 ? 240.237 189.624 227.207 1.00 2.37  ? 2876 TRP A N     1 
ATOM   11259 C  CA    . TRP A 1 2876 ? 240.301 190.650 228.240 1.00 3.09  ? 2876 TRP A CA    1 
ATOM   11260 C  C     . TRP A 1 2876 ? 241.534 190.514 229.124 1.00 9.05  ? 2876 TRP A C     1 
ATOM   11261 O  O     . TRP A 1 2876 ? 242.022 191.519 229.650 1.00 10.94 ? 2876 TRP A O     1 
ATOM   11262 C  CB    . TRP A 1 2876 ? 239.040 190.601 229.100 1.00 1.85  ? 2876 TRP A CB    1 
ATOM   11263 C  CG    . TRP A 1 2876 ? 237.835 191.173 228.432 1.00 1.78  ? 2876 TRP A CG    1 
ATOM   11264 C  CD1   . TRP A 1 2876 ? 237.810 191.945 227.310 1.00 2.10  ? 2876 TRP A CD1   1 
ATOM   11265 C  CD2   . TRP A 1 2876 ? 236.475 191.030 228.851 1.00 1.03  ? 2876 TRP A CD2   1 
ATOM   11266 N  NE1   . TRP A 1 2876 ? 236.518 192.286 226.999 1.00 0.96  ? 2876 TRP A NE1   1 
ATOM   11267 C  CE2   . TRP A 1 2876 ? 235.678 191.738 227.932 1.00 0.86  ? 2876 TRP A CE2   1 
ATOM   11268 C  CE3   . TRP A 1 2876 ? 235.852 190.369 229.913 1.00 0.85  ? 2876 TRP A CE3   1 
ATOM   11269 C  CZ2   . TRP A 1 2876 ? 234.294 191.805 228.042 1.00 0.95  ? 2876 TRP A CZ2   1 
ATOM   11270 C  CZ3   . TRP A 1 2876 ? 234.478 190.437 230.020 1.00 1.12  ? 2876 TRP A CZ3   1 
ATOM   11271 C  CH2   . TRP A 1 2876 ? 233.713 191.151 229.090 1.00 0.90  ? 2876 TRP A CH2   1 
ATOM   11272 N  N     . LEU A 1 2877 ? 242.043 189.297 229.306 1.00 6.52  ? 2877 LEU A N     1 
ATOM   11273 C  CA    . LEU A 1 2877 ? 243.192 189.059 230.169 1.00 6.01  ? 2877 LEU A CA    1 
ATOM   11274 C  C     . LEU A 1 2877 ? 244.495 188.950 229.394 1.00 13.04 ? 2877 LEU A C     1 
ATOM   11275 O  O     . LEU A 1 2877 ? 245.537 188.658 229.990 1.00 20.47 ? 2877 LEU A O     1 
ATOM   11276 C  CB    . LEU A 1 2877 ? 242.979 187.796 231.006 1.00 6.35  ? 2877 LEU A CB    1 
ATOM   11277 C  CG    . LEU A 1 2877 ? 241.715 187.722 231.866 1.00 8.68  ? 2877 LEU A CG    1 
ATOM   11278 C  CD1   . LEU A 1 2877 ? 241.907 186.725 232.993 1.00 6.16  ? 2877 LEU A CD1   1 
ATOM   11279 C  CD2   . LEU A 1 2877 ? 241.340 189.086 232.417 1.00 4.34  ? 2877 LEU A CD2   1 
ATOM   11280 N  N     . SER A 1 2878 ? 244.464 189.178 228.086 1.00 13.84 ? 2878 SER A N     1 
ATOM   11281 C  CA    . SER A 1 2878 ? 245.653 189.089 227.253 1.00 12.26 ? 2878 SER A CA    1 
ATOM   11282 C  C     . SER A 1 2878 ? 245.385 189.842 225.958 1.00 14.55 ? 2878 SER A C     1 
ATOM   11283 O  O     . SER A 1 2878 ? 244.318 190.431 225.768 1.00 20.09 ? 2878 SER A O     1 
ATOM   11284 C  CB    . SER A 1 2878 ? 246.034 187.631 226.988 1.00 16.80 ? 2878 SER A CB    1 
ATOM   11285 O  OG    . SER A 1 2878 ? 244.941 186.913 226.440 1.00 17.64 ? 2878 SER A OG    1 
ATOM   11286 N  N     . LYS A 1 2879 ? 246.372 189.820 225.064 1.00 13.90 ? 2879 LYS A N     1 
ATOM   11287 C  CA    . LYS A 1 2879 ? 246.196 190.420 223.747 1.00 15.76 ? 2879 LYS A CA    1 
ATOM   11288 C  C     . LYS A 1 2879 ? 245.342 189.548 222.839 1.00 13.48 ? 2879 LYS A C     1 
ATOM   11289 O  O     . LYS A 1 2879 ? 244.668 190.067 221.943 1.00 12.32 ? 2879 LYS A O     1 
ATOM   11290 C  CB    . LYS A 1 2879 ? 247.556 190.667 223.095 1.00 16.12 ? 2879 LYS A CB    1 
ATOM   11291 C  CG    . LYS A 1 2879 ? 248.433 189.430 223.020 1.00 19.66 ? 2879 LYS A CG    1 
ATOM   11292 C  CD    . LYS A 1 2879 ? 249.748 189.717 222.316 1.00 25.77 ? 2879 LYS A CD    1 
ATOM   11293 C  CE    . LYS A 1 2879 ? 250.614 188.471 222.238 1.00 26.28 ? 2879 LYS A CE    1 
ATOM   11294 N  NZ    . LYS A 1 2879 ? 250.848 187.869 223.579 1.00 24.84 ? 2879 LYS A NZ    1 
ATOM   11295 N  N     . ASP A 1 2880 ? 245.350 188.239 223.058 1.00 13.74 ? 2880 ASP A N     1 
ATOM   11296 C  CA    . ASP A 1 2880 ? 244.742 187.276 222.155 1.00 9.21  ? 2880 ASP A CA    1 
ATOM   11297 C  C     . ASP A 1 2880 ? 243.445 186.733 222.737 1.00 6.17  ? 2880 ASP A C     1 
ATOM   11298 O  O     . ASP A 1 2880 ? 243.184 186.817 223.940 1.00 11.37 ? 2880 ASP A O     1 
ATOM   11299 C  CB    . ASP A 1 2880 ? 245.714 186.128 221.867 1.00 9.22  ? 2880 ASP A CB    1 
ATOM   11300 C  CG    . ASP A 1 2880 ? 246.778 186.507 220.866 1.00 16.52 ? 2880 ASP A CG    1 
ATOM   11301 O  OD1   . ASP A 1 2880 ? 246.775 187.670 220.413 1.00 22.54 ? 2880 ASP A OD1   1 
ATOM   11302 O  OD2   . ASP A 1 2880 ? 247.621 185.648 220.538 1.00 18.60 ? 2880 ASP A OD2   1 
ATOM   11303 N  N     . TYR A 1 2881 ? 242.631 186.164 221.852 1.00 3.83  ? 2881 TYR A N     1 
ATOM   11304 C  CA    . TYR A 1 2881 ? 241.368 185.531 222.223 1.00 1.50  ? 2881 TYR A CA    1 
ATOM   11305 C  C     . TYR A 1 2881 ? 241.675 184.084 222.586 1.00 2.41  ? 2881 TYR A C     1 
ATOM   11306 O  O     . TYR A 1 2881 ? 241.632 183.183 221.750 1.00 4.38  ? 2881 TYR A O     1 
ATOM   11307 C  CB    . TYR A 1 2881 ? 240.366 185.646 221.082 1.00 3.10  ? 2881 TYR A CB    1 
ATOM   11308 C  CG    . TYR A 1 2881 ? 238.964 185.194 221.408 1.00 2.19  ? 2881 TYR A CG    1 
ATOM   11309 C  CD1   . TYR A 1 2881 ? 238.145 185.949 222.235 1.00 1.38  ? 2881 TYR A CD1   1 
ATOM   11310 C  CD2   . TYR A 1 2881 ? 238.442 184.031 220.855 1.00 1.00  ? 2881 TYR A CD2   1 
ATOM   11311 C  CE1   . TYR A 1 2881 ? 236.858 185.549 222.525 1.00 0.97  ? 2881 TYR A CE1   1 
ATOM   11312 C  CE2   . TYR A 1 2881 ? 237.154 183.624 221.136 1.00 1.01  ? 2881 TYR A CE2   1 
ATOM   11313 C  CZ    . TYR A 1 2881 ? 236.366 184.388 221.970 1.00 1.10  ? 2881 TYR A CZ    1 
ATOM   11314 O  OH    . TYR A 1 2881 ? 235.083 183.987 222.256 1.00 1.75  ? 2881 TYR A OH    1 
ATOM   11315 N  N     . ILE A 1 2882 ? 241.991 183.868 223.855 1.00 5.18  ? 2882 ILE A N     1 
ATOM   11316 C  CA    . ILE A 1 2882 ? 242.445 182.571 224.353 1.00 3.72  ? 2882 ILE A CA    1 
ATOM   11317 C  C     . ILE A 1 2882 ? 241.513 182.162 225.484 1.00 1.63  ? 2882 ILE A C     1 
ATOM   11318 O  O     . ILE A 1 2882 ? 240.777 183.001 226.031 1.00 2.20  ? 2882 ILE A O     1 
ATOM   11319 C  CB    . ILE A 1 2882 ? 243.921 182.619 224.810 1.00 3.08  ? 2882 ILE A CB    1 
ATOM   11320 C  CG1   . ILE A 1 2882 ? 244.074 183.534 226.026 1.00 3.27  ? 2882 ILE A CG1   1 
ATOM   11321 C  CG2   . ILE A 1 2882 ? 244.818 183.053 223.661 1.00 3.93  ? 2882 ILE A CG2   1 
ATOM   11322 C  CD1   . ILE A 1 2882 ? 245.457 183.521 226.626 1.00 4.70  ? 2882 ILE A CD1   1 
ATOM   11323 N  N     . PRO A 1 2883 ? 241.492 180.876 225.847 1.00 1.71  ? 2883 PRO A N     1 
ATOM   11324 C  CA    . PRO A 1 2883 ? 240.616 180.444 226.942 1.00 1.52  ? 2883 PRO A CA    1 
ATOM   11325 C  C     . PRO A 1 2883 ? 240.968 181.127 228.257 1.00 2.22  ? 2883 PRO A C     1 
ATOM   11326 O  O     . PRO A 1 2883 ? 242.135 181.390 228.557 1.00 3.49  ? 2883 PRO A O     1 
ATOM   11327 C  CB    . PRO A 1 2883 ? 240.859 178.931 227.011 1.00 1.76  ? 2883 PRO A CB    1 
ATOM   11328 C  CG    . PRO A 1 2883 ? 242.200 178.743 226.407 1.00 0.76  ? 2883 PRO A CG    1 
ATOM   11329 C  CD    . PRO A 1 2883 ? 242.263 179.745 225.303 1.00 1.18  ? 2883 PRO A CD    1 
ATOM   11330 N  N     . VAL A 1 2884 ? 239.934 181.408 229.046 1.00 1.84  ? 2884 VAL A N     1 
ATOM   11331 C  CA    . VAL A 1 2884 ? 240.060 182.152 230.294 1.00 2.31  ? 2884 VAL A CA    1 
ATOM   11332 C  C     . VAL A 1 2884 ? 239.425 181.343 231.417 1.00 3.58  ? 2884 VAL A C     1 
ATOM   11333 O  O     . VAL A 1 2884 ? 238.378 180.713 231.226 1.00 1.73  ? 2884 VAL A O     1 
ATOM   11334 C  CB    . VAL A 1 2884 ? 239.416 183.554 230.186 1.00 1.64  ? 2884 VAL A CB    1 
ATOM   11335 C  CG1   . VAL A 1 2884 ? 237.942 183.453 229.819 1.00 0.93  ? 2884 VAL A CG1   1 
ATOM   11336 C  CG2   . VAL A 1 2884 ? 239.596 184.337 231.475 1.00 2.10  ? 2884 VAL A CG2   1 
ATOM   11337 N  N     . ASP A 1 2885 ? 240.073 181.339 232.579 1.00 4.55  ? 2885 ASP A N     1 
ATOM   11338 C  CA    . ASP A 1 2885 ? 239.503 180.689 233.750 1.00 5.75  ? 2885 ASP A CA    1 
ATOM   11339 C  C     . ASP A 1 2885 ? 238.315 181.484 234.278 1.00 5.05  ? 2885 ASP A C     1 
ATOM   11340 O  O     . ASP A 1 2885 ? 238.304 182.718 234.230 1.00 4.48  ? 2885 ASP A O     1 
ATOM   11341 C  CB    . ASP A 1 2885 ? 240.556 180.536 234.846 1.00 5.35  ? 2885 ASP A CB    1 
ATOM   11342 C  CG    . ASP A 1 2885 ? 240.145 179.541 235.911 1.00 16.96 ? 2885 ASP A CG    1 
ATOM   11343 O  OD1   . ASP A 1 2885 ? 239.375 179.920 236.818 1.00 14.32 ? 2885 ASP A OD1   1 
ATOM   11344 O  OD2   . ASP A 1 2885 ? 240.587 178.376 235.836 1.00 22.78 ? 2885 ASP A OD2   1 
ATOM   11345 N  N     . GLN A 1 2886 ? 237.312 180.766 234.787 1.00 3.58  ? 2886 GLN A N     1 
ATOM   11346 C  CA    . GLN A 1 2886 ? 236.098 181.420 235.267 1.00 5.03  ? 2886 GLN A CA    1 
ATOM   11347 C  C     . GLN A 1 2886 ? 236.387 182.331 236.454 1.00 7.46  ? 2886 GLN A C     1 
ATOM   11348 O  O     . GLN A 1 2886 ? 235.883 183.457 236.523 1.00 5.49  ? 2886 GLN A O     1 
ATOM   11349 C  CB    . GLN A 1 2886 ? 235.048 180.372 235.636 1.00 5.43  ? 2886 GLN A CB    1 
ATOM   11350 C  CG    . GLN A 1 2886 ? 233.695 180.962 235.980 1.00 4.69  ? 2886 GLN A CG    1 
ATOM   11351 C  CD    . GLN A 1 2886 ? 232.640 179.907 236.211 1.00 6.65  ? 2886 GLN A CD    1 
ATOM   11352 O  OE1   . GLN A 1 2886 ? 232.768 179.070 237.102 1.00 15.19 ? 2886 GLN A OE1   1 
ATOM   11353 N  NE2   . GLN A 1 2886 ? 231.582 179.942 235.410 1.00 8.56  ? 2886 GLN A NE2   1 
ATOM   11354 N  N     . GLU A 1 2887 ? 237.197 181.858 237.404 1.00 9.46  ? 2887 GLU A N     1 
ATOM   11355 C  CA    . GLU A 1 2887 ? 237.507 182.673 238.575 1.00 7.07  ? 2887 GLU A CA    1 
ATOM   11356 C  C     . GLU A 1 2887 ? 238.385 183.863 238.209 1.00 7.84  ? 2887 GLU A C     1 
ATOM   11357 O  O     . GLU A 1 2887 ? 238.206 184.960 238.748 1.00 7.05  ? 2887 GLU A O     1 
ATOM   11358 C  CB    . GLU A 1 2887 ? 238.170 181.817 239.652 1.00 6.84  ? 2887 GLU A CB    1 
ATOM   11359 C  CG    . GLU A 1 2887 ? 237.259 180.743 240.221 1.00 12.16 ? 2887 GLU A CG    1 
ATOM   11360 C  CD    . GLU A 1 2887 ? 235.857 181.256 240.493 1.00 15.95 ? 2887 GLU A CD    1 
ATOM   11361 O  OE1   . GLU A 1 2887 ? 235.716 182.234 241.259 1.00 19.72 ? 2887 GLU A OE1   1 
ATOM   11362 O  OE2   . GLU A 1 2887 ? 234.896 180.681 239.943 1.00 14.17 ? 2887 GLU A OE2   1 
ATOM   11363 N  N     . GLU A 1 2888 ? 239.341 183.666 237.299 1.00 8.39  ? 2888 GLU A N     1 
ATOM   11364 C  CA    . GLU A 1 2888 ? 240.145 184.789 236.825 1.00 5.62  ? 2888 GLU A CA    1 
ATOM   11365 C  C     . GLU A 1 2888 ? 239.277 185.819 236.116 1.00 5.78  ? 2888 GLU A C     1 
ATOM   11366 O  O     . GLU A 1 2888 ? 239.464 187.028 236.292 1.00 9.21  ? 2888 GLU A O     1 
ATOM   11367 C  CB    . GLU A 1 2888 ? 241.253 184.291 235.896 1.00 5.43  ? 2888 GLU A CB    1 
ATOM   11368 C  CG    . GLU A 1 2888 ? 242.303 183.423 236.573 1.00 12.40 ? 2888 GLU A CG    1 
ATOM   11369 C  CD    . GLU A 1 2888 ? 243.135 184.183 237.587 1.00 25.24 ? 2888 GLU A CD    1 
ATOM   11370 O  OE1   . GLU A 1 2888 ? 243.361 185.395 237.385 1.00 28.15 ? 2888 GLU A OE1   1 
ATOM   11371 O  OE2   . GLU A 1 2888 ? 243.563 183.569 238.588 1.00 28.25 ? 2888 GLU A OE2   1 
ATOM   11372 N  N     . LEU A 1 2889 ? 238.321 185.357 235.308 1.00 5.19  ? 2889 LEU A N     1 
ATOM   11373 C  CA    . LEU A 1 2889 ? 237.408 186.270 234.629 1.00 4.38  ? 2889 LEU A CA    1 
ATOM   11374 C  C     . LEU A 1 2889 ? 236.524 187.012 235.625 1.00 3.89  ? 2889 LEU A C     1 
ATOM   11375 O  O     . LEU A 1 2889 ? 236.236 188.200 235.441 1.00 4.50  ? 2889 LEU A O     1 
ATOM   11376 C  CB    . LEU A 1 2889 ? 236.554 185.501 233.621 1.00 1.90  ? 2889 LEU A CB    1 
ATOM   11377 C  CG    . LEU A 1 2889 ? 235.562 186.313 232.789 1.00 1.12  ? 2889 LEU A CG    1 
ATOM   11378 C  CD1   . LEU A 1 2889 ? 236.274 187.077 231.685 1.00 0.87  ? 2889 LEU A CD1   1 
ATOM   11379 C  CD2   . LEU A 1 2889 ? 234.481 185.415 232.217 1.00 0.78  ? 2889 LEU A CD2   1 
ATOM   11380 N  N     . ARG A 1 2890 ? 236.076 186.325 236.679 1.00 5.94  ? 2890 ARG A N     1 
ATOM   11381 C  CA    . ARG A 1 2890 ? 235.198 186.957 237.659 1.00 4.46  ? 2890 ARG A CA    1 
ATOM   11382 C  C     . ARG A 1 2890 ? 235.896 188.113 238.361 1.00 5.42  ? 2890 ARG A C     1 
ATOM   11383 O  O     . ARG A 1 2890 ? 235.291 189.168 238.585 1.00 8.96  ? 2890 ARG A O     1 
ATOM   11384 C  CB    . ARG A 1 2890 ? 234.719 185.922 238.675 1.00 6.18  ? 2890 ARG A CB    1 
ATOM   11385 C  CG    . ARG A 1 2890 ? 233.461 186.329 239.422 1.00 4.87  ? 2890 ARG A CG    1 
ATOM   11386 C  CD    . ARG A 1 2890 ? 233.216 185.435 240.620 1.00 5.95  ? 2890 ARG A CD    1 
ATOM   11387 N  NE    . ARG A 1 2890 ? 233.240 184.024 240.258 1.00 9.32  ? 2890 ARG A NE    1 
ATOM   11388 C  CZ    . ARG A 1 2890 ? 232.179 183.334 239.861 1.00 11.09 ? 2890 ARG A CZ    1 
ATOM   11389 N  NH1   . ARG A 1 2890 ? 230.986 183.895 239.760 1.00 8.50  ? 2890 ARG A NH1   1 
ATOM   11390 N  NH2   . ARG A 1 2890 ? 232.322 182.048 239.551 1.00 7.02  ? 2890 ARG A NH2   1 
ATOM   11391 N  N     . ASP A 1 2891 ? 237.169 187.934 238.721 1.00 6.73  ? 2891 ASP A N     1 
ATOM   11392 C  CA    . ASP A 1 2891 ? 237.918 189.015 239.354 1.00 4.20  ? 2891 ASP A CA    1 
ATOM   11393 C  C     . ASP A 1 2891 ? 238.071 190.203 238.416 1.00 6.41  ? 2891 ASP A C     1 
ATOM   11394 O  O     . ASP A 1 2891 ? 237.932 191.358 238.838 1.00 12.65 ? 2891 ASP A O     1 
ATOM   11395 C  CB    . ASP A 1 2891 ? 239.288 188.512 239.803 1.00 8.01  ? 2891 ASP A CB    1 
ATOM   11396 C  CG    . ASP A 1 2891 ? 239.196 187.414 240.838 1.00 16.52 ? 2891 ASP A CG    1 
ATOM   11397 O  OD1   . ASP A 1 2891 ? 240.137 186.600 240.925 1.00 23.94 ? 2891 ASP A OD1   1 
ATOM   11398 O  OD2   . ASP A 1 2891 ? 238.184 187.366 241.564 1.00 16.55 ? 2891 ASP A OD2   1 
ATOM   11399 N  N     . TYR A 1 2892 ? 238.361 189.940 237.139 1.00 8.46  ? 2892 TYR A N     1 
ATOM   11400 C  CA    . TYR A 1 2892 ? 238.542 191.025 236.180 1.00 3.53  ? 2892 TYR A CA    1 
ATOM   11401 C  C     . TYR A 1 2892 ? 237.253 191.810 235.978 1.00 2.80  ? 2892 TYR A C     1 
ATOM   11402 O  O     . TYR A 1 2892 ? 237.279 193.042 235.891 1.00 5.23  ? 2892 TYR A O     1 
ATOM   11403 C  CB    . TYR A 1 2892 ? 239.049 190.467 234.852 1.00 5.25  ? 2892 TYR A CB    1 
ATOM   11404 C  CG    . TYR A 1 2892 ? 239.239 191.515 233.782 1.00 3.24  ? 2892 TYR A CG    1 
ATOM   11405 C  CD1   . TYR A 1 2892 ? 240.375 192.310 233.759 1.00 2.29  ? 2892 TYR A CD1   1 
ATOM   11406 C  CD2   . TYR A 1 2892 ? 238.281 191.711 232.796 1.00 1.82  ? 2892 TYR A CD2   1 
ATOM   11407 C  CE1   . TYR A 1 2892 ? 240.551 193.273 232.787 1.00 3.58  ? 2892 TYR A CE1   1 
ATOM   11408 C  CE2   . TYR A 1 2892 ? 238.449 192.667 231.825 1.00 1.53  ? 2892 TYR A CE2   1 
ATOM   11409 C  CZ    . TYR A 1 2892 ? 239.586 193.445 231.821 1.00 4.74  ? 2892 TYR A CZ    1 
ATOM   11410 O  OH    . TYR A 1 2892 ? 239.752 194.401 230.846 1.00 8.49  ? 2892 TYR A OH    1 
ATOM   11411 N  N     . VAL A 1 2893 ? 236.115 191.117 235.898 1.00 2.70  ? 2893 VAL A N     1 
ATOM   11412 C  CA    . VAL A 1 2893 ? 234.846 191.803 235.678 1.00 3.72  ? 2893 VAL A CA    1 
ATOM   11413 C  C     . VAL A 1 2893 ? 234.470 192.633 236.900 1.00 3.51  ? 2893 VAL A C     1 
ATOM   11414 O  O     . VAL A 1 2893 ? 233.935 193.741 236.773 1.00 3.92  ? 2893 VAL A O     1 
ATOM   11415 C  CB    . VAL A 1 2893 ? 233.745 190.792 235.302 1.00 4.08  ? 2893 VAL A CB    1 
ATOM   11416 C  CG1   . VAL A 1 2893 ? 232.386 191.475 235.231 1.00 2.54  ? 2893 VAL A CG1   1 
ATOM   11417 C  CG2   . VAL A 1 2893 ? 234.067 190.134 233.975 1.00 2.21  ? 2893 VAL A CG2   1 
ATOM   11418 N  N     . LYS A 1 2894 ? 234.753 192.123 238.103 1.00 5.68  ? 2894 LYS A N     1 
ATOM   11419 C  CA    . LYS A 1 2894 ? 234.529 192.917 239.309 1.00 3.92  ? 2894 LYS A CA    1 
ATOM   11420 C  C     . LYS A 1 2894 ? 235.402 194.164 239.318 1.00 4.19  ? 2894 LYS A C     1 
ATOM   11421 O  O     . LYS A 1 2894 ? 234.941 195.249 239.688 1.00 6.16  ? 2894 LYS A O     1 
ATOM   11422 C  CB    . LYS A 1 2894 ? 234.789 192.082 240.564 1.00 8.34  ? 2894 LYS A CB    1 
ATOM   11423 C  CG    . LYS A 1 2894 ? 233.792 190.970 240.796 1.00 11.13 ? 2894 LYS A CG    1 
ATOM   11424 C  CD    . LYS A 1 2894 ? 234.091 190.208 242.071 1.00 20.64 ? 2894 LYS A CD    1 
ATOM   11425 C  CE    . LYS A 1 2894 ? 233.095 189.079 242.283 1.00 18.30 ? 2894 LYS A CE    1 
ATOM   11426 N  NZ    . LYS A 1 2894 ? 233.378 188.311 243.524 1.00 23.26 ? 2894 LYS A NZ    1 
ATOM   11427 N  N     . ALA A 1 2895 ? 236.666 194.029 238.915 1.00 5.07  ? 2895 ALA A N     1 
ATOM   11428 C  CA    . ALA A 1 2895 ? 237.548 195.188 238.854 1.00 3.35  ? 2895 ALA A CA    1 
ATOM   11429 C  C     . ALA A 1 2895 ? 237.047 196.212 237.843 1.00 4.47  ? 2895 ALA A C     1 
ATOM   11430 O  O     . ALA A 1 2895 ? 237.088 197.421 238.101 1.00 5.21  ? 2895 ALA A O     1 
ATOM   11431 C  CB    . ALA A 1 2895 ? 238.971 194.746 238.511 1.00 2.22  ? 2895 ALA A CB    1 
ATOM   11432 N  N     . ARG A 1 2896 ? 236.569 195.749 236.686 1.00 4.73  ? 2896 ARG A N     1 
ATOM   11433 C  CA    . ARG A 1 2896 ? 236.077 196.675 235.672 1.00 3.61  ? 2896 ARG A CA    1 
ATOM   11434 C  C     . ARG A 1 2896 ? 234.710 197.235 236.039 1.00 2.97  ? 2896 ARG A C     1 
ATOM   11435 O  O     . ARG A 1 2896 ? 234.399 198.378 235.686 1.00 5.62  ? 2896 ARG A O     1 
ATOM   11436 C  CB    . ARG A 1 2896 ? 236.026 195.987 234.306 1.00 2.94  ? 2896 ARG A CB    1 
ATOM   11437 C  CG    . ARG A 1 2896 ? 237.384 195.544 233.781 1.00 1.87  ? 2896 ARG A CG    1 
ATOM   11438 C  CD    . ARG A 1 2896 ? 238.429 196.638 233.932 1.00 4.82  ? 2896 ARG A CD    1 
ATOM   11439 N  NE    . ARG A 1 2896 ? 238.135 197.812 233.121 1.00 4.41  ? 2896 ARG A NE    1 
ATOM   11440 C  CZ    . ARG A 1 2896 ? 238.666 199.011 233.324 1.00 4.12  ? 2896 ARG A CZ    1 
ATOM   11441 N  NH1   . ARG A 1 2896 ? 239.495 199.239 234.329 1.00 3.49  ? 2896 ARG A NH1   1 
ATOM   11442 N  NH2   . ARG A 1 2896 ? 238.352 200.008 232.501 1.00 4.01  ? 2896 ARG A NH2   1 
ATOM   11443 N  N     . LEU A 1 2897 ? 233.883 196.455 236.739 1.00 2.15  ? 2897 LEU A N     1 
ATOM   11444 C  CA    . LEU A 1 2897 ? 232.588 196.963 237.181 1.00 3.03  ? 2897 LEU A CA    1 
ATOM   11445 C  C     . LEU A 1 2897 ? 232.748 198.094 238.185 1.00 3.24  ? 2897 LEU A C     1 
ATOM   11446 O  O     . LEU A 1 2897 ? 231.927 199.019 238.215 1.00 3.90  ? 2897 LEU A O     1 
ATOM   11447 C  CB    . LEU A 1 2897 ? 231.752 195.832 237.785 1.00 1.87  ? 2897 LEU A CB    1 
ATOM   11448 C  CG    . LEU A 1 2897 ? 230.879 195.032 236.817 1.00 2.03  ? 2897 LEU A CG    1 
ATOM   11449 C  CD1   . LEU A 1 2897 ? 230.205 193.881 237.539 1.00 2.11  ? 2897 LEU A CD1   1 
ATOM   11450 C  CD2   . LEU A 1 2897 ? 229.849 195.925 236.142 1.00 0.84  ? 2897 LEU A CD2   1 
ATOM   11451 N  N     . LYS A 1 2898 ? 233.795 198.040 239.011 1.00 4.10  ? 2898 LYS A N     1 
ATOM   11452 C  CA    . LYS A 1 2898 ? 234.072 199.123 239.947 1.00 4.57  ? 2898 LYS A CA    1 
ATOM   11453 C  C     . LYS A 1 2898 ? 234.307 200.436 239.209 1.00 8.33  ? 2898 LYS A C     1 
ATOM   11454 O  O     . LYS A 1 2898 ? 233.773 201.483 239.591 1.00 14.08 ? 2898 LYS A O     1 
ATOM   11455 C  CB    . LYS A 1 2898 ? 235.282 198.761 240.807 1.00 6.09  ? 2898 LYS A CB    1 
ATOM   11456 C  CG    . LYS A 1 2898 ? 235.607 199.765 241.894 1.00 10.37 ? 2898 LYS A CG    1 
ATOM   11457 C  CD    . LYS A 1 2898 ? 236.768 199.283 242.746 1.00 17.10 ? 2898 LYS A CD    1 
ATOM   11458 C  CE    . LYS A 1 2898 ? 237.109 200.284 243.835 1.00 24.01 ? 2898 LYS A CE    1 
ATOM   11459 N  NZ    . LYS A 1 2898 ? 238.246 199.819 244.671 1.00 24.87 ? 2898 LYS A NZ    1 
ATOM   11460 N  N     . VAL A 1 2899 ? 235.105 200.395 238.142 1.00 4.20  ? 2899 VAL A N     1 
ATOM   11461 C  CA    . VAL A 1 2899 ? 235.336 201.589 237.337 1.00 3.07  ? 2899 VAL A CA    1 
ATOM   11462 C  C     . VAL A 1 2899 ? 234.060 201.999 236.611 1.00 4.37  ? 2899 VAL A C     1 
ATOM   11463 O  O     . VAL A 1 2899 ? 233.773 203.192 236.455 1.00 7.35  ? 2899 VAL A O     1 
ATOM   11464 C  CB    . VAL A 1 2899 ? 236.500 201.347 236.360 1.00 1.47  ? 2899 VAL A CB    1 
ATOM   11465 C  CG1   . VAL A 1 2899 ? 236.800 202.598 235.567 1.00 1.41  ? 2899 VAL A CG1   1 
ATOM   11466 C  CG2   . VAL A 1 2899 ? 237.734 200.883 237.114 1.00 1.33  ? 2899 VAL A CG2   1 
ATOM   11467 N  N     . PHE A 1 2900 ? 233.275 201.017 236.161 1.00 3.79  ? 2900 PHE A N     1 
ATOM   11468 C  CA    . PHE A 1 2900 ? 232.038 201.310 235.442 1.00 3.10  ? 2900 PHE A CA    1 
ATOM   11469 C  C     . PHE A 1 2900 ? 231.041 202.051 236.327 1.00 4.77  ? 2900 PHE A C     1 
ATOM   11470 O  O     . PHE A 1 2900 ? 230.297 202.914 235.847 1.00 2.74  ? 2900 PHE A O     1 
ATOM   11471 C  CB    . PHE A 1 2900 ? 231.435 200.009 234.910 1.00 1.27  ? 2900 PHE A CB    1 
ATOM   11472 C  CG    . PHE A 1 2900 ? 230.182 200.197 234.106 1.00 0.67  ? 2900 PHE A CG    1 
ATOM   11473 C  CD1   . PHE A 1 2900 ? 230.231 200.750 232.836 1.00 0.52  ? 2900 PHE A CD1   1 
ATOM   11474 C  CD2   . PHE A 1 2900 ? 228.957 199.793 234.606 1.00 0.55  ? 2900 PHE A CD2   1 
ATOM   11475 C  CE1   . PHE A 1 2900 ? 229.079 200.909 232.089 1.00 0.46  ? 2900 PHE A CE1   1 
ATOM   11476 C  CE2   . PHE A 1 2900 ? 227.802 199.952 233.865 1.00 0.46  ? 2900 PHE A CE2   1 
ATOM   11477 C  CZ    . PHE A 1 2900 ? 227.863 200.512 232.604 1.00 0.31  ? 2900 PHE A CZ    1 
ATOM   11478 N  N     . TYR A 1 2901 ? 231.006 201.724 237.621 1.00 4.82  ? 2901 TYR A N     1 
ATOM   11479 C  CA    . TYR A 1 2901 ? 230.097 202.409 238.536 1.00 6.00  ? 2901 TYR A CA    1 
ATOM   11480 C  C     . TYR A 1 2901 ? 230.448 203.886 238.666 1.00 7.68  ? 2901 TYR A C     1 
ATOM   11481 O  O     . TYR A 1 2901 ? 229.556 204.738 238.740 1.00 9.84  ? 2901 TYR A O     1 
ATOM   11482 C  CB    . TYR A 1 2901 ? 230.123 201.737 239.908 1.00 6.18  ? 2901 TYR A CB    1 
ATOM   11483 C  CG    . TYR A 1 2901 ? 229.691 200.290 239.902 1.00 6.46  ? 2901 TYR A CG    1 
ATOM   11484 C  CD1   . TYR A 1 2901 ? 228.768 199.821 238.976 1.00 5.01  ? 2901 TYR A CD1   1 
ATOM   11485 C  CD2   . TYR A 1 2901 ? 230.207 199.391 240.825 1.00 4.07  ? 2901 TYR A CD2   1 
ATOM   11486 C  CE1   . TYR A 1 2901 ? 228.374 198.500 238.970 1.00 3.96  ? 2901 TYR A CE1   1 
ATOM   11487 C  CE2   . TYR A 1 2901 ? 229.820 198.069 240.826 1.00 2.32  ? 2901 TYR A CE2   1 
ATOM   11488 C  CZ    . TYR A 1 2901 ? 228.903 197.627 239.898 1.00 3.36  ? 2901 TYR A CZ    1 
ATOM   11489 O  OH    . TYR A 1 2901 ? 228.516 196.307 239.899 1.00 6.57  ? 2901 TYR A OH    1 
ATOM   11490 N  N     . GLU A 1 2902 ? 231.741 204.207 238.694 1.00 8.23  ? 2902 GLU A N     1 
ATOM   11491 C  CA    . GLU A 1 2902 ? 232.201 205.572 238.917 1.00 7.77  ? 2902 GLU A CA    1 
ATOM   11492 C  C     . GLU A 1 2902 ? 232.207 206.429 237.657 1.00 8.41  ? 2902 GLU A C     1 
ATOM   11493 O  O     . GLU A 1 2902 ? 232.372 207.648 237.764 1.00 19.54 ? 2902 GLU A O     1 
ATOM   11494 C  CB    . GLU A 1 2902 ? 233.607 205.548 239.518 1.00 8.90  ? 2902 GLU A CB    1 
ATOM   11495 C  CG    . GLU A 1 2902 ? 233.664 204.975 240.924 1.00 15.35 ? 2902 GLU A CG    1 
ATOM   11496 C  CD    . GLU A 1 2902 ? 235.069 204.947 241.487 1.00 26.23 ? 2902 GLU A CD    1 
ATOM   11497 O  OE1   . GLU A 1 2902 ? 236.019 205.257 240.738 1.00 26.80 ? 2902 GLU A OE1   1 
ATOM   11498 O  OE2   . GLU A 1 2902 ? 235.225 204.620 242.682 1.00 32.32 ? 2902 GLU A OE2   1 
ATOM   11499 N  N     . GLU A 1 2903 ? 232.033 205.842 236.477 1.00 7.57  ? 2903 GLU A N     1 
ATOM   11500 C  CA    . GLU A 1 2903 ? 232.105 206.598 235.233 1.00 7.10  ? 2903 GLU A CA    1 
ATOM   11501 C  C     . GLU A 1 2903 ? 230.800 206.644 234.454 1.00 11.52 ? 2903 GLU A C     1 
ATOM   11502 O  O     . GLU A 1 2903 ? 230.463 207.691 233.898 1.00 19.72 ? 2903 GLU A O     1 
ATOM   11503 C  CB    . GLU A 1 2903 ? 233.203 206.029 234.326 1.00 6.96  ? 2903 GLU A CB    1 
ATOM   11504 C  CG    . GLU A 1 2903 ? 234.614 206.276 234.824 1.00 11.03 ? 2903 GLU A CG    1 
ATOM   11505 C  CD    . GLU A 1 2903 ? 235.668 205.697 233.903 1.00 21.10 ? 2903 GLU A CD    1 
ATOM   11506 O  OE1   . GLU A 1 2903 ? 235.348 205.418 232.727 1.00 27.01 ? 2903 GLU A OE1   1 
ATOM   11507 O  OE2   . GLU A 1 2903 ? 236.824 205.532 234.346 1.00 22.54 ? 2903 GLU A OE2   1 
ATOM   11508 N  N     . GLU A 1 2904 ? 230.055 205.542 234.385 1.00 10.81 ? 2904 GLU A N     1 
ATOM   11509 C  CA    . GLU A 1 2904 ? 228.887 205.463 233.518 1.00 7.79  ? 2904 GLU A CA    1 
ATOM   11510 C  C     . GLU A 1 2904 ? 227.584 205.299 234.289 1.00 10.76 ? 2904 GLU A C     1 
ATOM   11511 O  O     . GLU A 1 2904 ? 226.675 206.121 234.150 1.00 17.36 ? 2904 GLU A O     1 
ATOM   11512 C  CB    . GLU A 1 2904 ? 229.058 204.306 232.527 1.00 4.71  ? 2904 GLU A CB    1 
ATOM   11513 C  CG    . GLU A 1 2904 ? 230.164 204.514 231.516 1.00 9.11  ? 2904 GLU A CG    1 
ATOM   11514 C  CD    . GLU A 1 2904 ? 229.873 205.654 230.563 1.00 17.62 ? 2904 GLU A CD    1 
ATOM   11515 O  OE1   . GLU A 1 2904 ? 228.802 205.633 229.921 1.00 14.58 ? 2904 GLU A OE1   1 
ATOM   11516 O  OE2   . GLU A 1 2904 ? 230.715 206.568 230.455 1.00 17.80 ? 2904 GLU A OE2   1 
ATOM   11517 N  N     . LEU A 1 2905 ? 227.467 204.255 235.107 1.00 8.19  ? 2905 LEU A N     1 
ATOM   11518 C  CA    . LEU A 1 2905 ? 226.192 203.917 235.729 1.00 7.34  ? 2905 LEU A CA    1 
ATOM   11519 C  C     . LEU A 1 2905 ? 226.465 203.371 237.121 1.00 6.14  ? 2905 LEU A C     1 
ATOM   11520 O  O     . LEU A 1 2905 ? 227.025 202.280 237.261 1.00 10.61 ? 2905 LEU A O     1 
ATOM   11521 C  CB    . LEU A 1 2905 ? 225.428 202.901 234.886 1.00 7.53  ? 2905 LEU A CB    1 
ATOM   11522 C  CG    . LEU A 1 2905 ? 223.903 202.980 234.913 1.00 5.81  ? 2905 LEU A CG    1 
ATOM   11523 C  CD1   . LEU A 1 2905 ? 223.436 204.396 234.632 1.00 5.55  ? 2905 LEU A CD1   1 
ATOM   11524 C  CD2   . LEU A 1 2905 ? 223.309 201.999 233.916 1.00 7.26  ? 2905 LEU A CD2   1 
ATOM   11525 N  N     . ASP A 1 2906 ? 226.058 204.116 238.144 1.00 8.45  ? 2906 ASP A N     1 
ATOM   11526 C  CA    . ASP A 1 2906 ? 226.239 203.673 239.527 1.00 9.37  ? 2906 ASP A CA    1 
ATOM   11527 C  C     . ASP A 1 2906 ? 225.043 202.829 239.973 1.00 8.99  ? 2906 ASP A C     1 
ATOM   11528 O  O     . ASP A 1 2906 ? 224.279 203.182 240.868 1.00 12.10 ? 2906 ASP A O     1 
ATOM   11529 C  CB    . ASP A 1 2906 ? 226.460 204.869 240.444 1.00 11.40 ? 2906 ASP A CB    1 
ATOM   11530 C  CG    . ASP A 1 2906 ? 226.794 204.454 241.861 1.00 18.42 ? 2906 ASP A CG    1 
ATOM   11531 O  OD1   . ASP A 1 2906 ? 227.933 204.000 242.095 1.00 21.28 ? 2906 ASP A OD1   1 
ATOM   11532 O  OD2   . ASP A 1 2906 ? 225.922 204.584 242.745 1.00 29.58 ? 2906 ASP A OD2   1 
ATOM   11533 N  N     . VAL A 1 2907 ? 224.890 201.694 239.306 1.00 7.72  ? 2907 VAL A N     1 
ATOM   11534 C  CA    . VAL A 1 2907 ? 223.909 200.681 239.666 1.00 6.53  ? 2907 VAL A CA    1 
ATOM   11535 C  C     . VAL A 1 2907 ? 224.658 199.394 239.985 1.00 6.75  ? 2907 VAL A C     1 
ATOM   11536 O  O     . VAL A 1 2907 ? 225.088 198.674 239.084 1.00 12.62 ? 2907 VAL A O     1 
ATOM   11537 C  CB    . VAL A 1 2907 ? 222.880 200.461 238.541 1.00 6.93  ? 2907 VAL A CB    1 
ATOM   11538 C  CG1   . VAL A 1 2907 ? 221.796 199.506 238.999 1.00 5.05  ? 2907 VAL A CG1   1 
ATOM   11539 C  CG2   . VAL A 1 2907 ? 222.277 201.787 238.096 1.00 7.86  ? 2907 VAL A CG2   1 
ATOM   11540 N  N     . PRO A 1 2908 ? 224.848 199.079 241.265 1.00 5.73  ? 2908 PRO A N     1 
ATOM   11541 C  CA    . PRO A 1 2908 ? 225.604 197.871 241.623 1.00 6.26  ? 2908 PRO A CA    1 
ATOM   11542 C  C     . PRO A 1 2908 ? 224.934 196.611 241.096 1.00 7.59  ? 2908 PRO A C     1 
ATOM   11543 O  O     . PRO A 1 2908 ? 223.708 196.491 241.086 1.00 13.71 ? 2908 PRO A O     1 
ATOM   11544 C  CB    . PRO A 1 2908 ? 225.618 197.902 243.156 1.00 8.70  ? 2908 PRO A CB    1 
ATOM   11545 C  CG    . PRO A 1 2908 ? 225.369 199.333 243.510 1.00 5.91  ? 2908 PRO A CG    1 
ATOM   11546 C  CD    . PRO A 1 2908 ? 224.442 199.846 242.453 1.00 5.95  ? 2908 PRO A CD    1 
ATOM   11547 N  N     . LEU A 1 2909 ? 225.759 195.663 240.662 1.00 5.71  ? 2909 LEU A N     1 
ATOM   11548 C  CA    . LEU A 1 2909 ? 225.288 194.407 240.098 1.00 2.59  ? 2909 LEU A CA    1 
ATOM   11549 C  C     . LEU A 1 2909 ? 225.908 193.241 240.850 1.00 2.82  ? 2909 LEU A C     1 
ATOM   11550 O  O     . LEU A 1 2909 ? 227.094 193.270 241.190 1.00 4.60  ? 2909 LEU A O     1 
ATOM   11551 C  CB    . LEU A 1 2909 ? 225.632 194.296 238.608 1.00 2.95  ? 2909 LEU A CB    1 
ATOM   11552 C  CG    . LEU A 1 2909 ? 225.153 195.416 237.687 1.00 4.26  ? 2909 LEU A CG    1 
ATOM   11553 C  CD1   . LEU A 1 2909 ? 225.883 195.349 236.359 1.00 3.12  ? 2909 LEU A CD1   1 
ATOM   11554 C  CD2   . LEU A 1 2909 ? 223.652 195.330 237.483 1.00 2.59  ? 2909 LEU A CD2   1 
ATOM   11555 N  N     . VAL A 1 2910 ? 225.101 192.220 241.105 1.00 2.97  ? 2910 VAL A N     1 
ATOM   11556 C  CA    . VAL A 1 2910 ? 225.584 190.973 241.684 1.00 3.76  ? 2910 VAL A CA    1 
ATOM   11557 C  C     . VAL A 1 2910 ? 226.062 190.080 240.550 1.00 3.14  ? 2910 VAL A C     1 
ATOM   11558 O  O     . VAL A 1 2910 ? 225.331 189.845 239.582 1.00 7.32  ? 2910 VAL A O     1 
ATOM   11559 C  CB    . VAL A 1 2910 ? 224.484 190.283 242.507 1.00 4.82  ? 2910 VAL A CB    1 
ATOM   11560 C  CG1   . VAL A 1 2910 ? 224.969 188.935 243.017 1.00 3.32  ? 2910 VAL A CG1   1 
ATOM   11561 C  CG2   . VAL A 1 2910 ? 224.044 191.171 243.658 1.00 3.04  ? 2910 VAL A CG2   1 
ATOM   11562 N  N     . LEU A 1 2911 ? 227.293 189.591 240.660 1.00 2.11  ? 2911 LEU A N     1 
ATOM   11563 C  CA    . LEU A 1 2911 ? 227.914 188.814 239.594 1.00 2.68  ? 2911 LEU A CA    1 
ATOM   11564 C  C     . LEU A 1 2911 ? 227.687 187.330 239.852 1.00 4.73  ? 2911 LEU A C     1 
ATOM   11565 O  O     . LEU A 1 2911 ? 228.234 186.769 240.806 1.00 18.36 ? 2911 LEU A O     1 
ATOM   11566 C  CB    . LEU A 1 2911 ? 229.404 189.120 239.498 1.00 5.07  ? 2911 LEU A CB    1 
ATOM   11567 C  CG    . LEU A 1 2911 ? 229.797 190.336 238.663 1.00 5.58  ? 2911 LEU A CG    1 
ATOM   11568 C  CD1   . LEU A 1 2911 ? 231.292 190.353 238.445 1.00 6.88  ? 2911 LEU A CD1   1 
ATOM   11569 C  CD2   . LEU A 1 2911 ? 229.063 190.349 237.344 1.00 4.77  ? 2911 LEU A CD2   1 
ATOM   11570 N  N     . PHE A 1 2912 ? 226.885 186.697 239.007 1.00 1.49  ? 2912 PHE A N     1 
ATOM   11571 C  CA    . PHE A 1 2912 ? 226.742 185.251 239.005 1.00 2.14  ? 2912 PHE A CA    1 
ATOM   11572 C  C     . PHE A 1 2912 ? 227.265 184.685 237.690 1.00 3.23  ? 2912 PHE A C     1 
ATOM   11573 O  O     . PHE A 1 2912 ? 227.642 185.419 236.774 1.00 3.01  ? 2912 PHE A O     1 
ATOM   11574 C  CB    . PHE A 1 2912 ? 225.286 184.834 239.265 1.00 1.87  ? 2912 PHE A CB    1 
ATOM   11575 C  CG    . PHE A 1 2912 ? 224.283 185.454 238.335 1.00 1.74  ? 2912 PHE A CG    1 
ATOM   11576 C  CD1   . PHE A 1 2912 ? 223.749 186.700 238.604 1.00 1.42  ? 2912 PHE A CD1   1 
ATOM   11577 C  CD2   . PHE A 1 2912 ? 223.839 184.771 237.217 1.00 2.20  ? 2912 PHE A CD2   1 
ATOM   11578 C  CE1   . PHE A 1 2912 ? 222.811 187.265 237.765 1.00 0.76  ? 2912 PHE A CE1   1 
ATOM   11579 C  CE2   . PHE A 1 2912 ? 222.901 185.333 236.374 1.00 1.62  ? 2912 PHE A CE2   1 
ATOM   11580 C  CZ    . PHE A 1 2912 ? 222.388 186.580 236.650 1.00 1.24  ? 2912 PHE A CZ    1 
ATOM   11581 N  N     . ASN A 1 2913 ? 227.292 183.352 237.616 1.00 3.24  ? 2913 ASN A N     1 
ATOM   11582 C  CA    . ASN A 1 2913 ? 228.006 182.675 236.537 1.00 1.33  ? 2913 ASN A CA    1 
ATOM   11583 C  C     . ASN A 1 2913 ? 227.411 182.992 235.170 1.00 3.80  ? 2913 ASN A C     1 
ATOM   11584 O  O     . ASN A 1 2913 ? 228.148 183.175 234.195 1.00 2.94  ? 2913 ASN A O     1 
ATOM   11585 C  CB    . ASN A 1 2913 ? 228.016 181.168 236.783 1.00 1.80  ? 2913 ASN A CB    1 
ATOM   11586 C  CG    . ASN A 1 2913 ? 229.054 180.753 237.804 1.00 2.43  ? 2913 ASN A CG    1 
ATOM   11587 O  OD1   . ASN A 1 2913 ? 229.849 181.570 238.264 1.00 3.95  ? 2913 ASN A OD1   1 
ATOM   11588 N  ND2   . ASN A 1 2913 ? 229.052 179.478 238.167 1.00 1.82  ? 2913 ASN A ND2   1 
ATOM   11589 N  N     . GLU A 1 2914 ? 226.082 183.053 235.072 1.00 4.32  ? 2914 GLU A N     1 
ATOM   11590 C  CA    . GLU A 1 2914 ? 225.454 183.325 233.782 1.00 2.79  ? 2914 GLU A CA    1 
ATOM   11591 C  C     . GLU A 1 2914 ? 225.797 184.716 233.264 1.00 2.81  ? 2914 GLU A C     1 
ATOM   11592 O  O     . GLU A 1 2914 ? 225.864 184.918 232.047 1.00 5.94  ? 2914 GLU A O     1 
ATOM   11593 C  CB    . GLU A 1 2914 ? 223.940 183.154 233.882 1.00 4.14  ? 2914 GLU A CB    1 
ATOM   11594 C  CG    . GLU A 1 2914 ? 223.479 181.716 233.967 1.00 10.22 ? 2914 GLU A CG    1 
ATOM   11595 C  CD    . GLU A 1 2914 ? 222.173 181.565 234.722 1.00 19.05 ? 2914 GLU A CD    1 
ATOM   11596 O  OE1   . GLU A 1 2914 ? 221.211 182.300 234.410 1.00 9.62  ? 2914 GLU A OE1   1 
ATOM   11597 O  OE2   . GLU A 1 2914 ? 222.108 180.710 235.631 1.00 15.51 ? 2914 GLU A OE2   1 
ATOM   11598 N  N     . VAL A 1 2915 ? 226.014 185.682 234.160 1.00 2.31  ? 2915 VAL A N     1 
ATOM   11599 C  CA    . VAL A 1 2915 ? 226.396 187.024 233.725 1.00 1.41  ? 2915 VAL A CA    1 
ATOM   11600 C  C     . VAL A 1 2915 ? 227.755 186.994 233.038 1.00 0.93  ? 2915 VAL A C     1 
ATOM   11601 O  O     . VAL A 1 2915 ? 227.956 187.633 231.999 1.00 2.16  ? 2915 VAL A O     1 
ATOM   11602 C  CB    . VAL A 1 2915 ? 226.385 188.003 234.916 1.00 1.80  ? 2915 VAL A CB    1 
ATOM   11603 C  CG1   . VAL A 1 2915 ? 227.185 189.248 234.587 1.00 2.46  ? 2915 VAL A CG1   1 
ATOM   11604 C  CG2   . VAL A 1 2915 ? 224.969 188.380 235.275 1.00 1.05  ? 2915 VAL A CG2   1 
ATOM   11605 N  N     . LEU A 1 2916 ? 228.706 186.245 233.603 1.00 1.00  ? 2916 LEU A N     1 
ATOM   11606 C  CA    . LEU A 1 2916 ? 230.039 186.162 233.014 1.00 0.86  ? 2916 LEU A CA    1 
ATOM   11607 C  C     . LEU A 1 2916 ? 229.990 185.568 231.613 1.00 0.98  ? 2916 LEU A C     1 
ATOM   11608 O  O     . LEU A 1 2916 ? 230.696 186.027 230.709 1.00 0.81  ? 2916 LEU A O     1 
ATOM   11609 C  CB    . LEU A 1 2916 ? 230.958 185.337 233.913 1.00 0.88  ? 2916 LEU A CB    1 
ATOM   11610 C  CG    . LEU A 1 2916 ? 231.204 185.866 235.323 1.00 1.60  ? 2916 LEU A CG    1 
ATOM   11611 C  CD1   . LEU A 1 2916 ? 232.086 184.907 236.101 1.00 4.21  ? 2916 LEU A CD1   1 
ATOM   11612 C  CD2   . LEU A 1 2916 ? 231.824 187.252 235.278 1.00 1.97  ? 2916 LEU A CD2   1 
ATOM   11613 N  N     . ASP A 1 2917 ? 229.173 184.533 231.418 1.00 1.22  ? 2917 ASP A N     1 
ATOM   11614 C  CA    . ASP A 1 2917 ? 229.002 183.978 230.081 1.00 1.18  ? 2917 ASP A CA    1 
ATOM   11615 C  C     . ASP A 1 2917 ? 228.301 184.981 229.168 1.00 0.74  ? 2917 ASP A C     1 
ATOM   11616 O  O     . ASP A 1 2917 ? 228.671 185.131 227.999 1.00 0.26  ? 2917 ASP A O     1 
ATOM   11617 C  CB    . ASP A 1 2917 ? 228.227 182.659 230.163 1.00 1.73  ? 2917 ASP A CB    1 
ATOM   11618 C  CG    . ASP A 1 2917 ? 228.192 181.899 228.839 1.00 9.27  ? 2917 ASP A CG    1 
ATOM   11619 O  OD1   . ASP A 1 2917 ? 228.739 182.387 227.829 1.00 8.27  ? 2917 ASP A OD1   1 
ATOM   11620 O  OD2   . ASP A 1 2917 ? 227.617 180.791 228.813 1.00 12.56 ? 2917 ASP A OD2   1 
ATOM   11621 N  N     . HIS A 1 2918 ? 227.305 185.698 229.698 1.00 0.61  ? 2918 HIS A N     1 
ATOM   11622 C  CA    . HIS A 1 2918 ? 226.554 186.647 228.881 1.00 1.08  ? 2918 HIS A CA    1 
ATOM   11623 C  C     . HIS A 1 2918 ? 227.422 187.812 228.417 1.00 0.41  ? 2918 HIS A C     1 
ATOM   11624 O  O     . HIS A 1 2918 ? 227.347 188.217 227.251 1.00 0.23  ? 2918 HIS A O     1 
ATOM   11625 C  CB    . HIS A 1 2918 ? 225.339 187.165 229.650 1.00 0.67  ? 2918 HIS A CB    1 
ATOM   11626 C  CG    . HIS A 1 2918 ? 224.250 186.152 229.807 1.00 1.32  ? 2918 HIS A CG    1 
ATOM   11627 N  ND1   . HIS A 1 2918 ? 223.177 186.340 230.651 1.00 3.03  ? 2918 HIS A ND1   1 
ATOM   11628 C  CD2   . HIS A 1 2918 ? 224.072 184.940 229.235 1.00 2.50  ? 2918 HIS A CD2   1 
ATOM   11629 C  CE1   . HIS A 1 2918 ? 222.381 185.289 230.586 1.00 1.78  ? 2918 HIS A CE1   1 
ATOM   11630 N  NE2   . HIS A 1 2918 ? 222.901 184.424 229.734 1.00 3.07  ? 2918 HIS A NE2   1 
ATOM   11631 N  N     . VAL A 1 2919 ? 228.243 188.369 229.309 1.00 0.43  ? 2919 VAL A N     1 
ATOM   11632 C  CA    . VAL A 1 2919 ? 229.071 189.505 228.915 1.00 0.66  ? 2919 VAL A CA    1 
ATOM   11633 C  C     . VAL A 1 2919 ? 230.092 189.086 227.868 1.00 0.26  ? 2919 VAL A C     1 
ATOM   11634 O  O     . VAL A 1 2919 ? 230.432 189.871 226.976 1.00 0.22  ? 2919 VAL A O     1 
ATOM   11635 C  CB    . VAL A 1 2919 ? 229.736 190.162 230.143 1.00 0.43  ? 2919 VAL A CB    1 
ATOM   11636 C  CG1   . VAL A 1 2919 ? 228.680 190.667 231.108 1.00 0.38  ? 2919 VAL A CG1   1 
ATOM   11637 C  CG2   . VAL A 1 2919 ? 230.687 189.205 230.839 1.00 0.70  ? 2919 VAL A CG2   1 
ATOM   11638 N  N     . LEU A 1 2920 ? 230.595 187.852 227.947 1.00 0.26  ? 2920 LEU A N     1 
ATOM   11639 C  CA    . LEU A 1 2920 ? 231.500 187.354 226.917 1.00 0.21  ? 2920 LEU A CA    1 
ATOM   11640 C  C     . LEU A 1 2920 ? 230.791 187.221 225.573 1.00 0.28  ? 2920 LEU A C     1 
ATOM   11641 O  O     . LEU A 1 2920 ? 231.374 187.524 224.527 1.00 0.43  ? 2920 LEU A O     1 
ATOM   11642 C  CB    . LEU A 1 2920 ? 232.099 186.017 227.350 1.00 0.18  ? 2920 LEU A CB    1 
ATOM   11643 C  CG    . LEU A 1 2920 ? 233.167 186.076 228.446 1.00 0.35  ? 2920 LEU A CG    1 
ATOM   11644 C  CD1   . LEU A 1 2920 ? 233.767 184.705 228.686 1.00 0.37  ? 2920 LEU A CD1   1 
ATOM   11645 C  CD2   . LEU A 1 2920 ? 234.251 187.086 228.106 1.00 0.33  ? 2920 LEU A CD2   1 
ATOM   11646 N  N     . ARG A 1 2921 ? 229.535 186.766 225.581 1.00 0.19  ? 2921 ARG A N     1 
ATOM   11647 C  CA    . ARG A 1 2921 ? 228.775 186.652 224.340 1.00 0.21  ? 2921 ARG A CA    1 
ATOM   11648 C  C     . ARG A 1 2921 ? 228.504 188.017 223.722 1.00 0.28  ? 2921 ARG A C     1 
ATOM   11649 O  O     . ARG A 1 2921 ? 228.581 188.173 222.498 1.00 0.50  ? 2921 ARG A O     1 
ATOM   11650 C  CB    . ARG A 1 2921 ? 227.461 185.911 224.589 1.00 0.64  ? 2921 ARG A CB    1 
ATOM   11651 C  CG    . ARG A 1 2921 ? 227.623 184.493 225.096 1.00 0.58  ? 2921 ARG A CG    1 
ATOM   11652 C  CD    . ARG A 1 2921 ? 226.291 183.930 225.550 1.00 1.63  ? 2921 ARG A CD    1 
ATOM   11653 N  NE    . ARG A 1 2921 ? 226.442 182.659 226.248 1.00 2.53  ? 2921 ARG A NE    1 
ATOM   11654 C  CZ    . ARG A 1 2921 ? 225.431 181.921 226.682 1.00 1.94  ? 2921 ARG A CZ    1 
ATOM   11655 N  NH1   . ARG A 1 2921 ? 224.175 182.295 226.502 1.00 1.66  ? 2921 ARG A NH1   1 
ATOM   11656 N  NH2   . ARG A 1 2921 ? 225.685 180.774 227.306 1.00 2.44  ? 2921 ARG A NH2   1 
ATOM   11657 N  N     . ILE A 1 2922 ? 228.171 189.012 224.545 1.00 0.28  ? 2922 ILE A N     1 
ATOM   11658 C  CA    . ILE A 1 2922 ? 227.951 190.360 224.031 1.00 0.22  ? 2922 ILE A CA    1 
ATOM   11659 C  C     . ILE A 1 2922 ? 229.257 190.950 223.509 1.00 0.35  ? 2922 ILE A C     1 
ATOM   11660 O  O     . ILE A 1 2922 ? 229.270 191.663 222.499 1.00 0.58  ? 2922 ILE A O     1 
ATOM   11661 C  CB    . ILE A 1 2922 ? 227.314 191.245 225.118 1.00 0.17  ? 2922 ILE A CB    1 
ATOM   11662 C  CG1   . ILE A 1 2922 ? 225.952 190.683 225.533 1.00 0.15  ? 2922 ILE A CG1   1 
ATOM   11663 C  CG2   . ILE A 1 2922 ? 227.175 192.682 224.638 1.00 0.10  ? 2922 ILE A CG2   1 
ATOM   11664 C  CD1   . ILE A 1 2922 ? 225.345 191.372 226.730 1.00 0.30  ? 2922 ILE A CD1   1 
ATOM   11665 N  N     . ASP A 1 2923 ? 230.372 190.653 224.178 1.00 0.29  ? 2923 ASP A N     1 
ATOM   11666 C  CA    . ASP A 1 2923 ? 231.664 191.178 223.751 1.00 0.57  ? 2923 ASP A CA    1 
ATOM   11667 C  C     . ASP A 1 2923 ? 232.047 190.657 222.372 1.00 0.89  ? 2923 ASP A C     1 
ATOM   11668 O  O     . ASP A 1 2923 ? 232.671 191.372 221.581 1.00 2.29  ? 2923 ASP A O     1 
ATOM   11669 C  CB    . ASP A 1 2923 ? 232.735 190.821 224.782 1.00 0.57  ? 2923 ASP A CB    1 
ATOM   11670 C  CG    . ASP A 1 2923 ? 234.096 191.376 224.424 1.00 2.02  ? 2923 ASP A CG    1 
ATOM   11671 O  OD1   . ASP A 1 2923 ? 234.264 192.608 224.469 1.00 2.55  ? 2923 ASP A OD1   1 
ATOM   11672 O  OD2   . ASP A 1 2923 ? 234.998 190.581 224.095 1.00 7.67  ? 2923 ASP A OD2   1 
ATOM   11673 N  N     . ARG A 1 2924 ? 231.685 189.408 222.069 1.00 0.95  ? 2924 ARG A N     1 
ATOM   11674 C  CA    . ARG A 1 2924 ? 231.996 188.833 220.763 1.00 0.98  ? 2924 ARG A CA    1 
ATOM   11675 C  C     . ARG A 1 2924 ? 231.301 189.591 219.638 1.00 0.80  ? 2924 ARG A C     1 
ATOM   11676 O  O     . ARG A 1 2924 ? 231.907 189.878 218.600 1.00 3.18  ? 2924 ARG A O     1 
ATOM   11677 C  CB    . ARG A 1 2924 ? 231.600 187.359 220.745 1.00 0.70  ? 2924 ARG A CB    1 
ATOM   11678 C  CG    . ARG A 1 2924 ? 232.550 186.459 221.497 1.00 1.16  ? 2924 ARG A CG    1 
ATOM   11679 C  CD    . ARG A 1 2924 ? 232.065 185.025 221.505 1.00 1.72  ? 2924 ARG A CD    1 
ATOM   11680 N  NE    . ARG A 1 2924 ? 231.561 184.601 220.205 1.00 3.85  ? 2924 ARG A NE    1 
ATOM   11681 C  CZ    . ARG A 1 2924 ? 232.096 183.634 219.474 1.00 2.76  ? 2924 ARG A CZ    1 
ATOM   11682 N  NH1   . ARG A 1 2924 ? 233.200 183.012 219.853 1.00 2.37  ? 2924 ARG A NH1   1 
ATOM   11683 N  NH2   . ARG A 1 2924 ? 231.513 183.288 218.331 1.00 4.01  ? 2924 ARG A NH2   1 
ATOM   11684 N  N     . ILE A 1 2925 ? 230.025 189.925 219.830 1.00 0.90  ? 2925 ILE A N     1 
ATOM   11685 C  CA    . ILE A 1 2925 ? 229.249 190.555 218.766 1.00 1.27  ? 2925 ILE A CA    1 
ATOM   11686 C  C     . ILE A 1 2925 ? 229.713 191.988 218.523 1.00 0.87  ? 2925 ILE A C     1 
ATOM   11687 O  O     . ILE A 1 2925 ? 229.767 192.447 217.378 1.00 1.29  ? 2925 ILE A O     1 
ATOM   11688 C  CB    . ILE A 1 2925 ? 227.747 190.481 219.093 1.00 1.55  ? 2925 ILE A CB    1 
ATOM   11689 C  CG1   . ILE A 1 2925 ? 227.369 189.051 219.483 1.00 1.24  ? 2925 ILE A CG1   1 
ATOM   11690 C  CG2   . ILE A 1 2925 ? 226.915 190.942 217.915 1.00 0.29  ? 2925 ILE A CG2   1 
ATOM   11691 C  CD1   . ILE A 1 2925 ? 227.787 188.009 218.474 1.00 0.81  ? 2925 ILE A CD1   1 
ATOM   11692 N  N     . PHE A 1 2926 ? 230.054 192.718 219.588 1.00 1.69  ? 2926 PHE A N     1 
ATOM   11693 C  CA    . PHE A 1 2926 ? 230.572 194.073 219.429 1.00 1.22  ? 2926 PHE A CA    1 
ATOM   11694 C  C     . PHE A 1 2926 ? 231.914 194.127 218.713 1.00 2.33  ? 2926 PHE A C     1 
ATOM   11695 O  O     . PHE A 1 2926 ? 232.312 195.210 218.275 1.00 6.50  ? 2926 PHE A O     1 
ATOM   11696 C  CB    . PHE A 1 2926 ? 230.701 194.770 220.786 1.00 0.85  ? 2926 PHE A CB    1 
ATOM   11697 C  CG    . PHE A 1 2926 ? 229.390 195.132 221.414 1.00 0.57  ? 2926 PHE A CG    1 
ATOM   11698 C  CD1   . PHE A 1 2926 ? 228.222 195.124 220.672 1.00 0.38  ? 2926 PHE A CD1   1 
ATOM   11699 C  CD2   . PHE A 1 2926 ? 229.329 195.515 222.743 1.00 0.10  ? 2926 PHE A CD2   1 
ATOM   11700 C  CE1   . PHE A 1 2926 ? 227.020 195.473 221.248 1.00 0.33  ? 2926 PHE A CE1   1 
ATOM   11701 C  CE2   . PHE A 1 2926 ? 228.131 195.864 223.322 1.00 0.08  ? 2926 PHE A CE2   1 
ATOM   11702 C  CZ    . PHE A 1 2926 ? 226.975 195.845 222.574 1.00 0.13  ? 2926 PHE A CZ    1 
ATOM   11703 N  N     . ARG A 1 2927 ? 232.620 193.005 218.589 1.00 2.66  ? 2927 ARG A N     1 
ATOM   11704 C  CA    . ARG A 1 2927 ? 233.904 192.966 217.904 1.00 2.84  ? 2927 ARG A CA    1 
ATOM   11705 C  C     . ARG A 1 2927 ? 233.793 192.431 216.482 1.00 3.01  ? 2927 ARG A C     1 
ATOM   11706 O  O     . ARG A 1 2927 ? 234.819 192.191 215.839 1.00 6.76  ? 2927 ARG A O     1 
ATOM   11707 C  CB    . ARG A 1 2927 ? 234.904 192.134 218.711 1.00 3.53  ? 2927 ARG A CB    1 
ATOM   11708 C  CG    . ARG A 1 2927 ? 235.196 192.703 220.088 1.00 3.69  ? 2927 ARG A CG    1 
ATOM   11709 C  CD    . ARG A 1 2927 ? 236.280 191.918 220.806 1.00 4.17  ? 2927 ARG A CD    1 
ATOM   11710 N  NE    . ARG A 1 2927 ? 235.771 190.685 221.396 1.00 5.50  ? 2927 ARG A NE    1 
ATOM   11711 C  CZ    . ARG A 1 2927 ? 236.071 189.469 220.965 1.00 10.36 ? 2927 ARG A CZ    1 
ATOM   11712 N  NH1   . ARG A 1 2927 ? 236.880 189.282 219.934 1.00 8.89  ? 2927 ARG A NH1   1 
ATOM   11713 N  NH2   . ARG A 1 2927 ? 235.549 188.414 221.582 1.00 4.80  ? 2927 ARG A NH2   1 
ATOM   11714 N  N     . GLN A 1 2928 ? 232.574 192.243 215.975 1.00 3.77  ? 2928 GLN A N     1 
ATOM   11715 C  CA    . GLN A 1 2928 ? 232.327 191.797 214.615 1.00 3.28  ? 2928 GLN A CA    1 
ATOM   11716 C  C     . GLN A 1 2928 ? 231.690 192.915 213.797 1.00 1.99  ? 2928 GLN A C     1 
ATOM   11717 O  O     . GLN A 1 2928 ? 230.902 193.703 214.327 1.00 2.13  ? 2928 GLN A O     1 
ATOM   11718 C  CB    . GLN A 1 2928 ? 231.402 190.573 214.585 1.00 3.21  ? 2928 GLN A CB    1 
ATOM   11719 C  CG    . GLN A 1 2928 ? 232.052 189.266 215.011 1.00 4.56  ? 2928 GLN A CG    1 
ATOM   11720 C  CD    . GLN A 1 2928 ? 233.351 188.988 214.280 1.00 12.72 ? 2928 GLN A CD    1 
ATOM   11721 O  OE1   . GLN A 1 2928 ? 233.351 188.660 213.095 1.00 15.37 ? 2928 GLN A OE1   1 
ATOM   11722 N  NE2   . GLN A 1 2928 ? 234.465 189.110 214.989 1.00 11.04 ? 2928 GLN A NE2   1 
ATOM   11723 N  N     . PRO A 1 2929 ? 232.021 193.021 212.510 1.00 4.13  ? 2929 PRO A N     1 
ATOM   11724 C  CA    . PRO A 1 2929 ? 231.337 194.001 211.657 1.00 2.05  ? 2929 PRO A CA    1 
ATOM   11725 C  C     . PRO A 1 2929 ? 229.861 193.669 211.504 1.00 1.87  ? 2929 PRO A C     1 
ATOM   11726 O  O     . PRO A 1 2929 ? 229.470 192.504 211.409 1.00 3.28  ? 2929 PRO A O     1 
ATOM   11727 C  CB    . PRO A 1 2929 ? 232.082 193.887 210.321 1.00 3.38  ? 2929 PRO A CB    1 
ATOM   11728 C  CG    . PRO A 1 2929 ? 232.662 192.512 210.336 1.00 3.57  ? 2929 PRO A CG    1 
ATOM   11729 C  CD    . PRO A 1 2929 ? 233.038 192.258 211.767 1.00 4.51  ? 2929 PRO A CD    1 
ATOM   11730 N  N     . GLN A 1 2930 ? 229.040 194.721 211.464 1.00 2.74  ? 2930 GLN A N     1 
ATOM   11731 C  CA    . GLN A 1 2930 ? 227.581 194.592 211.492 1.00 2.29  ? 2930 GLN A CA    1 
ATOM   11732 C  C     . GLN A 1 2930 ? 227.135 193.679 212.630 1.00 1.64  ? 2930 GLN A C     1 
ATOM   11733 O  O     . GLN A 1 2930 ? 226.258 192.829 212.470 1.00 2.52  ? 2930 GLN A O     1 
ATOM   11734 C  CB    . GLN A 1 2930 ? 227.033 194.102 210.151 1.00 1.77  ? 2930 GLN A CB    1 
ATOM   11735 C  CG    . GLN A 1 2930 ? 226.654 195.220 209.202 1.00 4.30  ? 2930 GLN A CG    1 
ATOM   11736 C  CD    . GLN A 1 2930 ? 226.031 194.713 207.917 1.00 5.68  ? 2930 GLN A CD    1 
ATOM   11737 O  OE1   . GLN A 1 2930 ? 224.893 195.046 207.591 1.00 4.57  ? 2930 GLN A OE1   1 
ATOM   11738 N  NE2   . GLN A 1 2930 ? 226.779 193.904 207.178 1.00 3.84  ? 2930 GLN A NE2   1 
ATOM   11739 N  N     . GLY A 1 2931 ? 227.744 193.864 213.796 1.00 1.10  ? 2931 GLY A N     1 
ATOM   11740 C  CA    . GLY A 1 2931 ? 227.455 193.004 214.921 1.00 0.60  ? 2931 GLY A CA    1 
ATOM   11741 C  C     . GLY A 1 2931 ? 226.207 193.448 215.647 1.00 0.25  ? 2931 GLY A C     1 
ATOM   11742 O  O     . GLY A 1 2931 ? 226.239 194.379 216.453 1.00 0.14  ? 2931 GLY A O     1 
ATOM   11743 N  N     . HIS A 1 2932 ? 225.101 192.772 215.368 1.00 0.30  ? 2932 HIS A N     1 
ATOM   11744 C  CA    . HIS A 1 2932 ? 223.803 193.110 215.923 1.00 0.09  ? 2932 HIS A CA    1 
ATOM   11745 C  C     . HIS A 1 2932 ? 223.344 192.025 216.886 1.00 0.06  ? 2932 HIS A C     1 
ATOM   11746 O  O     . HIS A 1 2932 ? 223.583 190.834 216.676 1.00 0.19  ? 2932 HIS A O     1 
ATOM   11747 C  CB    . HIS A 1 2932 ? 222.776 193.304 214.809 1.00 0.22  ? 2932 HIS A CB    1 
ATOM   11748 C  CG    . HIS A 1 2932 ? 223.161 194.345 213.808 1.00 0.34  ? 2932 HIS A CG    1 
ATOM   11749 N  ND1   . HIS A 1 2932 ? 223.786 195.522 214.162 1.00 0.17  ? 2932 HIS A ND1   1 
ATOM   11750 C  CD2   . HIS A 1 2932 ? 223.031 194.379 212.462 1.00 0.49  ? 2932 HIS A CD2   1 
ATOM   11751 C  CE1   . HIS A 1 2932 ? 224.011 196.241 213.079 1.00 0.15  ? 2932 HIS A CE1   1 
ATOM   11752 N  NE2   . HIS A 1 2932 ? 223.563 195.571 212.034 1.00 0.33  ? 2932 HIS A NE2   1 
ATOM   11753 N  N     . LEU A 1 2933 ? 222.681 192.453 217.951 1.00 0.14  ? 2933 LEU A N     1 
ATOM   11754 C  CA    . LEU A 1 2933 ? 222.298 191.577 219.045 1.00 0.13  ? 2933 LEU A CA    1 
ATOM   11755 C  C     . LEU A 1 2933 ? 220.789 191.584 219.217 1.00 0.09  ? 2933 LEU A C     1 
ATOM   11756 O  O     . LEU A 1 2933 ? 220.154 192.640 219.171 1.00 0.14  ? 2933 LEU A O     1 
ATOM   11757 C  CB    . LEU A 1 2933 ? 222.967 192.013 220.348 1.00 0.12  ? 2933 LEU A CB    1 
ATOM   11758 C  CG    . LEU A 1 2933 ? 224.322 191.383 220.648 1.00 1.59  ? 2933 LEU A CG    1 
ATOM   11759 C  CD1   . LEU A 1 2933 ? 224.927 192.007 221.885 1.00 1.94  ? 2933 LEU A CD1   1 
ATOM   11760 C  CD2   . LEU A 1 2933 ? 224.165 189.889 220.823 1.00 1.92  ? 2933 LEU A CD2   1 
ATOM   11761 N  N     . LEU A 1 2934 ? 220.225 190.400 219.414 1.00 0.15  ? 2934 LEU A N     1 
ATOM   11762 C  CA    . LEU A 1 2934 ? 218.820 190.230 219.775 1.00 0.12  ? 2934 LEU A CA    1 
ATOM   11763 C  C     . LEU A 1 2934 ? 218.804 189.536 221.135 1.00 0.09  ? 2934 LEU A C     1 
ATOM   11764 O  O     . LEU A 1 2934 ? 218.865 188.308 221.222 1.00 0.08  ? 2934 LEU A O     1 
ATOM   11765 C  CB    . LEU A 1 2934 ? 218.057 189.437 218.712 1.00 0.18  ? 2934 LEU A CB    1 
ATOM   11766 C  CG    . LEU A 1 2934 ? 216.587 189.143 219.019 1.00 0.26  ? 2934 LEU A CG    1 
ATOM   11767 C  CD1   . LEU A 1 2934 ? 215.842 190.423 219.356 1.00 0.35  ? 2934 LEU A CD1   1 
ATOM   11768 C  CD2   . LEU A 1 2934 ? 215.925 188.421 217.858 1.00 0.72  ? 2934 LEU A CD2   1 
ATOM   11769 N  N     . LEU A 1 2935 ? 218.734 190.331 222.195 1.00 0.19  ? 2935 LEU A N     1 
ATOM   11770 C  CA    . LEU A 1 2935 ? 218.713 189.820 223.559 1.00 0.16  ? 2935 LEU A CA    1 
ATOM   11771 C  C     . LEU A 1 2935 ? 217.269 189.596 223.985 1.00 0.14  ? 2935 LEU A C     1 
ATOM   11772 O  O     . LEU A 1 2935 ? 216.487 190.546 224.066 1.00 0.41  ? 2935 LEU A O     1 
ATOM   11773 C  CB    . LEU A 1 2935 ? 219.408 190.795 224.508 1.00 0.34  ? 2935 LEU A CB    1 
ATOM   11774 C  CG    . LEU A 1 2935 ? 220.890 191.078 224.263 1.00 0.24  ? 2935 LEU A CG    1 
ATOM   11775 C  CD1   . LEU A 1 2935 ? 221.515 191.711 225.492 1.00 0.13  ? 2935 LEU A CD1   1 
ATOM   11776 C  CD2   . LEU A 1 2935 ? 221.635 189.813 223.869 1.00 0.30  ? 2935 LEU A CD2   1 
ATOM   11777 N  N     . ILE A 1 2936 ? 216.915 188.345 224.261 1.00 0.21  ? 2936 ILE A N     1 
ATOM   11778 C  CA    . ILE A 1 2936 ? 215.553 187.979 224.629 1.00 0.40  ? 2936 ILE A CA    1 
ATOM   11779 C  C     . ILE A 1 2936 ? 215.566 187.477 226.065 1.00 0.58  ? 2936 ILE A C     1 
ATOM   11780 O  O     . ILE A 1 2936 ? 216.315 186.553 226.403 1.00 0.74  ? 2936 ILE A O     1 
ATOM   11781 C  CB    . ILE A 1 2936 ? 214.967 186.928 223.677 1.00 0.80  ? 2936 ILE A CB    1 
ATOM   11782 C  CG1   . ILE A 1 2936 ? 215.052 187.425 222.231 1.00 0.55  ? 2936 ILE A CG1   1 
ATOM   11783 C  CG2   . ILE A 1 2936 ? 213.528 186.610 224.054 1.00 0.77  ? 2936 ILE A CG2   1 
ATOM   11784 C  CD1   . ILE A 1 2936 ? 214.508 186.454 221.219 1.00 0.84  ? 2936 ILE A CD1   1 
ATOM   11785 N  N     . GLY A 1 2937 ? 214.740 188.084 226.904 1.00 0.80  ? 2937 GLY A N     1 
ATOM   11786 C  CA    . GLY A 1 2937 ? 214.659 187.684 228.295 1.00 0.91  ? 2937 GLY A CA    1 
ATOM   11787 C  C     . GLY A 1 2937 ? 213.655 188.541 229.030 1.00 1.71  ? 2937 GLY A C     1 
ATOM   11788 O  O     . GLY A 1 2937 ? 213.144 189.535 228.504 1.00 5.37  ? 2937 GLY A O     1 
ATOM   11789 N  N     . VAL A 1 2938 ? 213.381 188.132 230.268 1.00 1.77  ? 2938 VAL A N     1 
ATOM   11790 C  CA    . VAL A 1 2938 ? 212.431 188.854 231.101 1.00 1.54  ? 2938 VAL A CA    1 
ATOM   11791 C  C     . VAL A 1 2938 ? 212.995 190.231 231.450 1.00 0.98  ? 2938 VAL A C     1 
ATOM   11792 O  O     . VAL A 1 2938 ? 214.213 190.426 231.546 1.00 1.86  ? 2938 VAL A O     1 
ATOM   11793 C  CB    . VAL A 1 2938 ? 212.117 188.035 232.366 1.00 1.66  ? 2938 VAL A CB    1 
ATOM   11794 C  CG1   . VAL A 1 2938 ? 211.038 188.705 233.207 1.00 1.88  ? 2938 VAL A CG1   1 
ATOM   11795 C  CG2   . VAL A 1 2938 ? 211.702 186.623 231.988 1.00 2.53  ? 2938 VAL A CG2   1 
ATOM   11796 N  N     . SER A 1 2939 ? 212.099 191.199 231.621 1.00 0.92  ? 2939 SER A N     1 
ATOM   11797 C  CA    . SER A 1 2939 ? 212.509 192.537 232.021 1.00 0.80  ? 2939 SER A CA    1 
ATOM   11798 C  C     . SER A 1 2939 ? 213.150 192.507 233.400 1.00 0.83  ? 2939 SER A C     1 
ATOM   11799 O  O     . SER A 1 2939 ? 212.760 191.723 234.269 1.00 1.95  ? 2939 SER A O     1 
ATOM   11800 C  CB    . SER A 1 2939 ? 211.311 193.484 232.019 1.00 2.39  ? 2939 SER A CB    1 
ATOM   11801 O  OG    . SER A 1 2939 ? 210.783 193.638 230.716 1.00 10.30 ? 2939 SER A OG    1 
ATOM   11802 N  N     . GLY A 1 2940 ? 214.148 193.362 233.597 1.00 0.76  ? 2940 GLY A N     1 
ATOM   11803 C  CA    . GLY A 1 2940 ? 214.845 193.413 234.864 1.00 0.73  ? 2940 GLY A CA    1 
ATOM   11804 C  C     . GLY A 1 2940 ? 215.900 192.353 235.053 1.00 0.96  ? 2940 GLY A C     1 
ATOM   11805 O  O     . GLY A 1 2940 ? 216.379 192.166 236.176 1.00 3.28  ? 2940 GLY A O     1 
ATOM   11806 N  N     . ALA A 1 2941 ? 216.278 191.648 233.992 1.00 0.80  ? 2941 ALA A N     1 
ATOM   11807 C  CA    . ALA A 1 2941 ? 217.309 190.626 234.060 1.00 0.59  ? 2941 ALA A CA    1 
ATOM   11808 C  C     . ALA A 1 2941 ? 218.695 191.165 233.739 1.00 1.06  ? 2941 ALA A C     1 
ATOM   11809 O  O     . ALA A 1 2941 ? 219.663 190.399 233.757 1.00 2.03  ? 2941 ALA A O     1 
ATOM   11810 C  CB    . ALA A 1 2941 ? 216.969 189.472 233.113 1.00 0.58  ? 2941 ALA A CB    1 
ATOM   11811 N  N     . GLY A 1 2942 ? 218.815 192.457 233.450 1.00 0.60  ? 2942 GLY A N     1 
ATOM   11812 C  CA    . GLY A 1 2942 ? 220.104 193.056 233.182 1.00 0.80  ? 2942 GLY A CA    1 
ATOM   11813 C  C     . GLY A 1 2942 ? 220.524 193.103 231.732 1.00 0.26  ? 2942 GLY A C     1 
ATOM   11814 O  O     . GLY A 1 2942 ? 221.706 193.330 231.460 1.00 0.40  ? 2942 GLY A O     1 
ATOM   11815 N  N     . LYS A 1 2943 ? 219.599 192.895 230.792 1.00 0.36  ? 2943 LYS A N     1 
ATOM   11816 C  CA    . LYS A 1 2943 ? 219.969 192.889 229.379 1.00 0.42  ? 2943 LYS A CA    1 
ATOM   11817 C  C     . LYS A 1 2943 ? 220.528 194.240 228.948 1.00 0.39  ? 2943 LYS A C     1 
ATOM   11818 O  O     . LYS A 1 2943 ? 221.562 194.311 228.278 1.00 0.27  ? 2943 LYS A O     1 
ATOM   11819 C  CB    . LYS A 1 2943 ? 218.762 192.509 228.520 1.00 0.26  ? 2943 LYS A CB    1 
ATOM   11820 C  CG    . LYS A 1 2943 ? 218.308 191.071 228.682 1.00 0.36  ? 2943 LYS A CG    1 
ATOM   11821 C  CD    . LYS A 1 2943 ? 217.188 190.725 227.711 1.00 0.32  ? 2943 LYS A CD    1 
ATOM   11822 C  CE    . LYS A 1 2943 ? 216.008 191.669 227.862 1.00 0.49  ? 2943 LYS A CE    1 
ATOM   11823 N  NZ    . LYS A 1 2943 ? 215.474 191.688 229.250 1.00 0.51  ? 2943 LYS A NZ    1 
ATOM   11824 N  N     . THR A 1 2944 ? 219.859 195.328 229.335 1.00 0.26  ? 2944 THR A N     1 
ATOM   11825 C  CA    . THR A 1 2944 ? 220.343 196.652 228.963 1.00 0.24  ? 2944 THR A CA    1 
ATOM   11826 C  C     . THR A 1 2944 ? 221.618 197.006 229.717 1.00 0.39  ? 2944 THR A C     1 
ATOM   11827 O  O     . THR A 1 2944 ? 222.564 197.542 229.128 1.00 0.35  ? 2944 THR A O     1 
ATOM   11828 C  CB    . THR A 1 2944 ? 219.264 197.702 229.221 1.00 0.45  ? 2944 THR A CB    1 
ATOM   11829 O  OG1   . THR A 1 2944 ? 218.026 197.266 228.650 1.00 0.65  ? 2944 THR A OG1   1 
ATOM   11830 C  CG2   . THR A 1 2944 ? 219.657 199.030 228.603 1.00 0.54  ? 2944 THR A CG2   1 
ATOM   11831 N  N     . THR A 1 2945 ? 221.661 196.716 231.018 1.00 0.42  ? 2945 THR A N     1 
ATOM   11832 C  CA    . THR A 1 2945 ? 222.813 197.098 231.828 1.00 0.21  ? 2945 THR A CA    1 
ATOM   11833 C  C     . THR A 1 2945 ? 224.072 196.371 231.377 1.00 0.19  ? 2945 THR A C     1 
ATOM   11834 O  O     . THR A 1 2945 ? 225.142 196.980 231.267 1.00 1.10  ? 2945 THR A O     1 
ATOM   11835 C  CB    . THR A 1 2945 ? 222.532 196.819 233.305 1.00 0.24  ? 2945 THR A CB    1 
ATOM   11836 O  OG1   . THR A 1 2945 ? 221.324 197.481 233.695 1.00 0.48  ? 2945 THR A OG1   1 
ATOM   11837 C  CG2   . THR A 1 2945 ? 223.675 197.319 234.167 1.00 0.12  ? 2945 THR A CG2   1 
ATOM   11838 N  N     . LEU A 1 2946 ? 223.966 195.069 231.108 1.00 0.14  ? 2946 LEU A N     1 
ATOM   11839 C  CA    . LEU A 1 2946 ? 225.125 194.325 230.634 1.00 0.12  ? 2946 LEU A CA    1 
ATOM   11840 C  C     . LEU A 1 2946 ? 225.576 194.823 229.268 1.00 0.09  ? 2946 LEU A C     1 
ATOM   11841 O  O     . LEU A 1 2946 ? 226.780 194.906 228.999 1.00 0.10  ? 2946 LEU A O     1 
ATOM   11842 C  CB    . LEU A 1 2946 ? 224.810 192.831 230.591 1.00 0.17  ? 2946 LEU A CB    1 
ATOM   11843 C  CG    . LEU A 1 2946 ? 224.710 192.132 231.947 1.00 0.16  ? 2946 LEU A CG    1 
ATOM   11844 C  CD1   . LEU A 1 2946 ? 224.658 190.627 231.767 1.00 0.23  ? 2946 LEU A CD1   1 
ATOM   11845 C  CD2   . LEU A 1 2946 ? 225.865 192.529 232.853 1.00 0.14  ? 2946 LEU A CD2   1 
ATOM   11846 N  N     . SER A 1 2947 ? 224.626 195.164 228.396 1.00 0.10  ? 2947 SER A N     1 
ATOM   11847 C  CA    . SER A 1 2947 ? 224.982 195.693 227.085 1.00 0.09  ? 2947 SER A CA    1 
ATOM   11848 C  C     . SER A 1 2947 ? 225.743 197.007 227.207 1.00 0.08  ? 2947 SER A C     1 
ATOM   11849 O  O     . SER A 1 2947 ? 226.739 197.220 226.507 1.00 0.07  ? 2947 SER A O     1 
ATOM   11850 C  CB    . SER A 1 2947 ? 223.726 195.875 226.233 1.00 0.10  ? 2947 SER A CB    1 
ATOM   11851 O  OG    . SER A 1 2947 ? 223.063 194.643 226.036 1.00 1.07  ? 2947 SER A OG    1 
ATOM   11852 N  N     . ARG A 1 2948 ? 225.292 197.899 228.091 1.00 0.09  ? 2948 ARG A N     1 
ATOM   11853 C  CA    . ARG A 1 2948 ? 226.010 199.151 228.303 1.00 0.12  ? 2948 ARG A CA    1 
ATOM   11854 C  C     . ARG A 1 2948 ? 227.385 198.903 228.908 1.00 0.10  ? 2948 ARG A C     1 
ATOM   11855 O  O     . ARG A 1 2948 ? 228.359 199.574 228.549 1.00 0.16  ? 2948 ARG A O     1 
ATOM   11856 C  CB    . ARG A 1 2948 ? 225.188 200.087 229.189 1.00 0.13  ? 2948 ARG A CB    1 
ATOM   11857 C  CG    . ARG A 1 2948 ? 223.873 200.511 228.571 1.00 0.78  ? 2948 ARG A CG    1 
ATOM   11858 C  CD    . ARG A 1 2948 ? 222.976 201.222 229.567 1.00 2.35  ? 2948 ARG A CD    1 
ATOM   11859 N  NE    . ARG A 1 2948 ? 223.496 202.530 229.945 1.00 4.41  ? 2948 ARG A NE    1 
ATOM   11860 C  CZ    . ARG A 1 2948 ? 222.815 203.432 230.638 1.00 6.08  ? 2948 ARG A CZ    1 
ATOM   11861 N  NH1   . ARG A 1 2948 ? 221.578 203.202 231.043 1.00 5.63  ? 2948 ARG A NH1   1 
ATOM   11862 N  NH2   . ARG A 1 2948 ? 223.388 204.596 230.929 1.00 5.53  ? 2948 ARG A NH2   1 
ATOM   11863 N  N     . PHE A 1 2949 ? 227.483 197.949 229.833 1.00 0.09  ? 2949 PHE A N     1 
ATOM   11864 C  CA    . PHE A 1 2949 ? 228.761 197.654 230.469 1.00 0.10  ? 2949 PHE A CA    1 
ATOM   11865 C  C     . PHE A 1 2949 ? 229.762 197.084 229.471 1.00 0.11  ? 2949 PHE A C     1 
ATOM   11866 O  O     . PHE A 1 2949 ? 230.939 197.461 229.480 1.00 0.19  ? 2949 PHE A O     1 
ATOM   11867 C  CB    . PHE A 1 2949 ? 228.543 196.695 231.639 1.00 0.08  ? 2949 PHE A CB    1 
ATOM   11868 C  CG    . PHE A 1 2949 ? 229.800 196.060 232.151 1.00 0.06  ? 2949 PHE A CG    1 
ATOM   11869 C  CD1   . PHE A 1 2949 ? 230.783 196.827 232.752 1.00 0.10  ? 2949 PHE A CD1   1 
ATOM   11870 C  CD2   . PHE A 1 2949 ? 229.995 194.696 232.043 1.00 0.07  ? 2949 PHE A CD2   1 
ATOM   11871 C  CE1   . PHE A 1 2949 ? 231.936 196.249 233.229 1.00 0.12  ? 2949 PHE A CE1   1 
ATOM   11872 C  CE2   . PHE A 1 2949 ? 231.150 194.108 232.519 1.00 0.16  ? 2949 PHE A CE2   1 
ATOM   11873 C  CZ    . PHE A 1 2949 ? 232.120 194.886 233.118 1.00 0.25  ? 2949 PHE A CZ    1 
ATOM   11874 N  N     . VAL A 1 2950 ? 229.319 196.164 228.613 1.00 0.12  ? 2950 VAL A N     1 
ATOM   11875 C  CA    . VAL A 1 2950 ? 230.206 195.619 227.591 1.00 0.13  ? 2950 VAL A CA    1 
ATOM   11876 C  C     . VAL A 1 2950 ? 230.522 196.678 226.540 1.00 0.08  ? 2950 VAL A C     1 
ATOM   11877 O  O     . VAL A 1 2950 ? 231.642 196.741 226.020 1.00 0.24  ? 2950 VAL A O     1 
ATOM   11878 C  CB    . VAL A 1 2950 ? 229.589 194.351 226.971 1.00 0.14  ? 2950 VAL A CB    1 
ATOM   11879 C  CG1   . VAL A 1 2950 ? 230.445 193.844 225.827 1.00 0.19  ? 2950 VAL A CG1   1 
ATOM   11880 C  CG2   . VAL A 1 2950 ? 229.438 193.274 228.027 1.00 0.09  ? 2950 VAL A CG2   1 
ATOM   11881 N  N     . ALA A 1 2951 ? 229.546 197.527 226.215 1.00 0.05  ? 2951 ALA A N     1 
ATOM   11882 C  CA    . ALA A 1 2951 ? 229.790 198.613 225.271 1.00 0.16  ? 2951 ALA A CA    1 
ATOM   11883 C  C     . ALA A 1 2951 ? 230.839 199.579 225.803 1.00 0.66  ? 2951 ALA A C     1 
ATOM   11884 O  O     . ALA A 1 2951 ? 231.655 200.105 225.037 1.00 1.10  ? 2951 ALA A O     1 
ATOM   11885 C  CB    . ALA A 1 2951 ? 228.488 199.351 224.966 1.00 0.15  ? 2951 ALA A CB    1 
ATOM   11886 N  N     . TRP A 1 2952 ? 230.828 199.832 227.113 1.00 0.51  ? 2952 TRP A N     1 
ATOM   11887 C  CA    . TRP A 1 2952 ? 231.838 200.696 227.711 1.00 0.39  ? 2952 TRP A CA    1 
ATOM   11888 C  C     . TRP A 1 2952 ? 233.203 200.019 227.748 1.00 0.68  ? 2952 TRP A C     1 
ATOM   11889 O  O     . TRP A 1 2952 ? 234.233 200.700 227.695 1.00 1.37  ? 2952 TRP A O     1 
ATOM   11890 C  CB    . TRP A 1 2952 ? 231.391 201.113 229.114 1.00 0.46  ? 2952 TRP A CB    1 
ATOM   11891 C  CG    . TRP A 1 2952 ? 232.471 201.679 229.984 1.00 1.07  ? 2952 TRP A CG    1 
ATOM   11892 C  CD1   . TRP A 1 2952 ? 232.867 202.980 230.052 1.00 1.04  ? 2952 TRP A CD1   1 
ATOM   11893 C  CD2   . TRP A 1 2952 ? 233.279 200.965 230.925 1.00 0.70  ? 2952 TRP A CD2   1 
ATOM   11894 N  NE1   . TRP A 1 2952 ? 233.876 203.120 230.970 1.00 0.95  ? 2952 TRP A NE1   1 
ATOM   11895 C  CE2   . TRP A 1 2952 ? 234.148 201.898 231.520 1.00 0.76  ? 2952 TRP A CE2   1 
ATOM   11896 C  CE3   . TRP A 1 2952 ? 233.355 199.625 231.318 1.00 0.70  ? 2952 TRP A CE3   1 
ATOM   11897 C  CZ2   . TRP A 1 2952 ? 235.082 201.536 232.488 1.00 1.67  ? 2952 TRP A CZ2   1 
ATOM   11898 C  CZ3   . TRP A 1 2952 ? 234.283 199.268 232.277 1.00 1.17  ? 2952 TRP A CZ3   1 
ATOM   11899 C  CH2   . TRP A 1 2952 ? 235.133 200.219 232.851 1.00 1.71  ? 2952 TRP A CH2   1 
ATOM   11900 N  N     . MET A 1 2953 ? 233.231 198.686 227.825 1.00 0.65  ? 2953 MET A N     1 
ATOM   11901 C  CA    . MET A 1 2953 ? 234.499 197.965 227.821 1.00 0.73  ? 2953 MET A CA    1 
ATOM   11902 C  C     . MET A 1 2953 ? 235.130 197.928 226.436 1.00 1.70  ? 2953 MET A C     1 
ATOM   11903 O  O     . MET A 1 2953 ? 236.355 197.820 226.316 1.00 6.84  ? 2953 MET A O     1 
ATOM   11904 C  CB    . MET A 1 2953 ? 234.299 196.541 228.336 1.00 1.83  ? 2953 MET A CB    1 
ATOM   11905 C  CG    . MET A 1 2953 ? 234.101 196.433 229.837 1.00 2.13  ? 2953 MET A CG    1 
ATOM   11906 S  SD    . MET A 1 2953 ? 233.969 194.717 230.351 1.00 24.58 ? 2953 MET A SD    1 
ATOM   11907 C  CE    . MET A 1 2953 ? 235.696 194.243 230.374 1.00 2.47  ? 2953 MET A CE    1 
ATOM   11908 N  N     . ASN A 1 2954 ? 234.321 197.998 225.383 1.00 2.17  ? 2954 ASN A N     1 
ATOM   11909 C  CA    . ASN A 1 2954 ? 234.810 197.932 224.014 1.00 1.86  ? 2954 ASN A CA    1 
ATOM   11910 C  C     . ASN A 1 2954 ? 234.940 199.305 223.369 1.00 3.38  ? 2954 ASN A C     1 
ATOM   11911 O  O     . ASN A 1 2954 ? 235.207 199.389 222.167 1.00 9.62  ? 2954 ASN A O     1 
ATOM   11912 C  CB    . ASN A 1 2954 ? 233.896 197.040 223.175 1.00 1.39  ? 2954 ASN A CB    1 
ATOM   11913 C  CG    . ASN A 1 2954 ? 234.072 195.572 223.489 1.00 2.82  ? 2954 ASN A CG    1 
ATOM   11914 O  OD1   . ASN A 1 2954 ? 235.123 194.992 223.227 1.00 6.79  ? 2954 ASN A OD1   1 
ATOM   11915 N  ND2   . ASN A 1 2954 ? 233.046 194.964 224.066 1.00 3.26  ? 2954 ASN A ND2   1 
ATOM   11916 N  N     . GLY A 1 2955 ? 234.758 200.379 224.135 1.00 1.98  ? 2955 GLY A N     1 
ATOM   11917 C  CA    . GLY A 1 2955 ? 234.860 201.717 223.598 1.00 0.64  ? 2955 GLY A CA    1 
ATOM   11918 C  C     . GLY A 1 2955 ? 233.675 202.175 222.784 1.00 0.90  ? 2955 GLY A C     1 
ATOM   11919 O  O     . GLY A 1 2955 ? 233.784 203.180 222.072 1.00 2.26  ? 2955 GLY A O     1 
ATOM   11920 N  N     . LEU A 1 2956 ? 232.549 201.476 222.862 1.00 2.17  ? 2956 LEU A N     1 
ATOM   11921 C  CA    . LEU A 1 2956 ? 231.361 201.826 222.098 1.00 0.60  ? 2956 LEU A CA    1 
ATOM   11922 C  C     . LEU A 1 2956 ? 230.511 202.809 222.888 1.00 1.12  ? 2956 LEU A C     1 
ATOM   11923 O  O     . LEU A 1 2956 ? 230.245 202.598 224.075 1.00 4.07  ? 2956 LEU A O     1 
ATOM   11924 C  CB    . LEU A 1 2956 ? 230.539 200.579 221.763 1.00 0.84  ? 2956 LEU A CB    1 
ATOM   11925 C  CG    . LEU A 1 2956 ? 230.890 199.741 220.529 1.00 0.72  ? 2956 LEU A CG    1 
ATOM   11926 C  CD1   . LEU A 1 2956 ? 232.329 199.260 220.556 1.00 1.39  ? 2956 LEU A CD1   1 
ATOM   11927 C  CD2   . LEU A 1 2956 ? 229.932 198.563 220.399 1.00 0.22  ? 2956 LEU A CD2   1 
ATOM   11928 N  N     . SER A 1 2957 ? 230.093 203.884 222.231 1.00 1.00  ? 2957 SER A N     1 
ATOM   11929 C  CA    . SER A 1 2957 ? 229.142 204.804 222.829 1.00 0.68  ? 2957 SER A CA    1 
ATOM   11930 C  C     . SER A 1 2957 ? 227.753 204.183 222.825 1.00 0.78  ? 2957 SER A C     1 
ATOM   11931 O  O     . SER A 1 2957 ? 227.365 203.500 221.874 1.00 0.97  ? 2957 SER A O     1 
ATOM   11932 C  CB    . SER A 1 2957 ? 229.131 206.131 222.074 1.00 2.06  ? 2957 SER A CB    1 
ATOM   11933 O  OG    . SER A 1 2957 ? 230.414 206.730 222.088 1.00 13.59 ? 2957 SER A OG    1 
ATOM   11934 N  N     . VAL A 1 2958 ? 227.009 204.411 223.897 1.00 2.21  ? 2958 VAL A N     1 
ATOM   11935 C  CA    . VAL A 1 2958 ? 225.663 203.875 224.037 1.00 1.22  ? 2958 VAL A CA    1 
ATOM   11936 C  C     . VAL A 1 2958 ? 224.680 204.950 223.604 1.00 1.15  ? 2958 VAL A C     1 
ATOM   11937 O  O     . VAL A 1 2958 ? 224.682 206.061 224.144 1.00 1.62  ? 2958 VAL A O     1 
ATOM   11938 C  CB    . VAL A 1 2958 ? 225.381 203.419 225.477 1.00 0.74  ? 2958 VAL A CB    1 
ATOM   11939 C  CG1   . VAL A 1 2958 ? 223.893 203.198 225.675 1.00 0.73  ? 2958 VAL A CG1   1 
ATOM   11940 C  CG2   . VAL A 1 2958 ? 226.155 202.156 225.793 1.00 0.64  ? 2958 VAL A CG2   1 
ATOM   11941 N  N     . TYR A 1 2959 ? 223.847 204.627 222.620 1.00 1.51  ? 2959 TYR A N     1 
ATOM   11942 C  CA    . TYR A 1 2959 ? 222.755 205.491 222.202 1.00 0.87  ? 2959 TYR A CA    1 
ATOM   11943 C  C     . TYR A 1 2959 ? 221.434 204.797 222.493 1.00 0.81  ? 2959 TYR A C     1 
ATOM   11944 O  O     . TYR A 1 2959 ? 221.216 203.660 222.064 1.00 1.00  ? 2959 TYR A O     1 
ATOM   11945 C  CB    . TYR A 1 2959 ? 222.846 205.843 220.715 1.00 0.80  ? 2959 TYR A CB    1 
ATOM   11946 C  CG    . TYR A 1 2959 ? 221.893 206.943 220.308 1.00 2.04  ? 2959 TYR A CG    1 
ATOM   11947 C  CD1   . TYR A 1 2959 ? 220.558 206.668 220.034 1.00 2.10  ? 2959 TYR A CD1   1 
ATOM   11948 C  CD2   . TYR A 1 2959 ? 222.323 208.259 220.208 1.00 2.06  ? 2959 TYR A CD2   1 
ATOM   11949 C  CE1   . TYR A 1 2959 ? 219.684 207.667 219.671 1.00 2.67  ? 2959 TYR A CE1   1 
ATOM   11950 C  CE2   . TYR A 1 2959 ? 221.455 209.264 219.842 1.00 3.13  ? 2959 TYR A CE2   1 
ATOM   11951 C  CZ    . TYR A 1 2959 ? 220.136 208.963 219.574 1.00 5.14  ? 2959 TYR A CZ    1 
ATOM   11952 O  OH    . TYR A 1 2959 ? 219.264 209.961 219.209 1.00 7.36  ? 2959 TYR A OH    1 
ATOM   11953 N  N     . GLN A 1 2960 ? 220.563 205.484 223.220 1.00 0.65  ? 2960 GLN A N     1 
ATOM   11954 C  CA    . GLN A 1 2960 ? 219.201 205.035 223.455 1.00 1.59  ? 2960 GLN A CA    1 
ATOM   11955 C  C     . GLN A 1 2960 ? 218.250 206.155 223.072 1.00 2.67  ? 2960 GLN A C     1 
ATOM   11956 O  O     . GLN A 1 2960 ? 218.462 207.313 223.445 1.00 7.48  ? 2960 GLN A O     1 
ATOM   11957 C  CB    . GLN A 1 2960 ? 218.984 204.631 224.922 1.00 1.23  ? 2960 GLN A CB    1 
ATOM   11958 C  CG    . GLN A 1 2960 ? 219.868 203.489 225.389 1.00 1.60  ? 2960 GLN A CG    1 
ATOM   11959 C  CD    . GLN A 1 2960 ? 219.643 203.132 226.844 1.00 4.05  ? 2960 GLN A CD    1 
ATOM   11960 O  OE1   . GLN A 1 2960 ? 218.556 202.705 227.231 1.00 4.46  ? 2960 GLN A OE1   1 
ATOM   11961 N  NE2   . GLN A 1 2960 ? 220.674 203.303 227.661 1.00 7.36  ? 2960 GLN A NE2   1 
ATOM   11962 N  N     . ILE A 1 2961 ? 217.212 205.816 222.310 1.00 1.82  ? 2961 ILE A N     1 
ATOM   11963 C  CA    . ILE A 1 2961 ? 216.215 206.812 221.944 1.00 3.17  ? 2961 ILE A CA    1 
ATOM   11964 C  C     . ILE A 1 2961 ? 215.393 207.171 223.173 1.00 6.95  ? 2961 ILE A C     1 
ATOM   11965 O  O     . ILE A 1 2961 ? 215.066 206.310 224.002 1.00 8.20  ? 2961 ILE A O     1 
ATOM   11966 C  CB    . ILE A 1 2961 ? 215.348 206.316 220.776 1.00 2.31  ? 2961 ILE A CB    1 
ATOM   11967 C  CG1   . ILE A 1 2961 ? 214.328 205.271 221.229 1.00 3.30  ? 2961 ILE A CG1   1 
ATOM   11968 C  CG2   . ILE A 1 2961 ? 216.218 205.786 219.652 1.00 5.17  ? 2961 ILE A CG2   1 
ATOM   11969 C  CD1   . ILE A 1 2961 ? 213.362 204.868 220.143 1.00 6.55  ? 2961 ILE A CD1   1 
ATOM   11970 N  N     . LYS A 1 2962 ? 215.094 208.460 223.320 1.00 9.74  ? 2962 LYS A N     1 
ATOM   11971 C  CA    . LYS A 1 2962 ? 214.482 208.982 224.538 1.00 6.00  ? 2962 LYS A CA    1 
ATOM   11972 C  C     . LYS A 1 2962 ? 212.980 209.140 224.302 1.00 7.85  ? 2962 LYS A C     1 
ATOM   11973 O  O     . LYS A 1 2962 ? 212.453 210.233 224.083 1.00 7.96  ? 2962 LYS A O     1 
ATOM   11974 C  CB    . LYS A 1 2962 ? 215.142 210.295 224.929 1.00 8.61  ? 2962 LYS A CB    1 
ATOM   11975 C  CG    . LYS A 1 2962 ? 216.626 210.142 225.211 1.00 12.72 ? 2962 LYS A CG    1 
ATOM   11976 C  CD    . LYS A 1 2962 ? 216.900 209.341 226.468 1.00 20.05 ? 2962 LYS A CD    1 
ATOM   11977 C  CE    . LYS A 1 2962 ? 218.396 209.201 226.703 1.00 13.94 ? 2962 LYS A CE    1 
ATOM   11978 N  NZ    . LYS A 1 2962 ? 219.041 210.495 227.046 1.00 18.64 ? 2962 LYS A NZ    1 
ATOM   11979 N  N     . VAL A 1 2963 ? 212.286 208.002 224.344 1.00 6.45  ? 2963 VAL A N     1 
ATOM   11980 C  CA    . VAL A 1 2963 ? 210.867 207.999 224.016 1.00 7.88  ? 2963 VAL A CA    1 
ATOM   11981 C  C     . VAL A 1 2963 ? 210.063 208.684 225.114 1.00 10.38 ? 2963 VAL A C     1 
ATOM   11982 O  O     . VAL A 1 2963 ? 210.485 208.807 226.270 1.00 6.99  ? 2963 VAL A O     1 
ATOM   11983 C  CB    . VAL A 1 2963 ? 210.350 206.573 223.768 1.00 7.60  ? 2963 VAL A CB    1 
ATOM   11984 C  CG1   . VAL A 1 2963 ? 211.056 205.951 222.590 1.00 8.34  ? 2963 VAL A CG1   1 
ATOM   11985 C  CG2   . VAL A 1 2963 ? 210.538 205.721 225.011 1.00 12.73 ? 2963 VAL A CG2   1 
ATOM   11986 N  N     . HIS A 1 2964 ? 208.877 209.138 224.728 1.00 10.48 ? 2964 HIS A N     1 
ATOM   11987 C  CA    . HIS A 1 2964 ? 207.907 209.720 225.635 1.00 9.07  ? 2964 HIS A CA    1 
ATOM   11988 C  C     . HIS A 1 2964 ? 206.531 209.520 225.015 1.00 11.30 ? 2964 HIS A C     1 
ATOM   11989 O  O     . HIS A 1 2964 ? 206.391 208.883 223.968 1.00 13.95 ? 2964 HIS A O     1 
ATOM   11990 C  CB    . HIS A 1 2964 ? 208.229 211.192 225.918 1.00 9.12  ? 2964 HIS A CB    1 
ATOM   11991 C  CG    . HIS A 1 2964 ? 208.481 212.007 224.688 1.00 9.95  ? 2964 HIS A CG    1 
ATOM   11992 N  ND1   . HIS A 1 2964 ? 207.483 212.690 224.028 1.00 11.45 ? 2964 HIS A ND1   1 
ATOM   11993 C  CD2   . HIS A 1 2964 ? 209.624 212.260 224.008 1.00 8.34  ? 2964 HIS A CD2   1 
ATOM   11994 C  CE1   . HIS A 1 2964 ? 207.999 213.320 222.988 1.00 8.64  ? 2964 HIS A CE1   1 
ATOM   11995 N  NE2   . HIS A 1 2964 ? 209.295 213.077 222.954 1.00 8.94  ? 2964 HIS A NE2   1 
ATOM   11996 N  N     . ARG A 1 2965 ? 205.505 210.059 225.674 1.00 14.19 ? 2965 ARG A N     1 
ATOM   11997 C  CA    . ARG A 1 2965 ? 204.145 209.858 225.188 1.00 16.14 ? 2965 ARG A CA    1 
ATOM   11998 C  C     . ARG A 1 2965 ? 203.912 210.503 223.828 1.00 11.40 ? 2965 ARG A C     1 
ATOM   11999 O  O     . ARG A 1 2965 ? 203.035 210.056 223.083 1.00 12.28 ? 2965 ARG A O     1 
ATOM   12000 C  CB    . ARG A 1 2965 ? 203.135 210.406 226.194 1.00 15.84 ? 2965 ARG A CB    1 
ATOM   12001 C  CG    . ARG A 1 2965 ? 203.379 211.850 226.595 1.00 19.25 ? 2965 ARG A CG    1 
ATOM   12002 C  CD    . ARG A 1 2965 ? 202.322 212.303 227.578 1.00 25.91 ? 2965 ARG A CD    1 
ATOM   12003 N  NE    . ARG A 1 2965 ? 200.986 212.097 227.033 1.00 21.13 ? 2965 ARG A NE    1 
ATOM   12004 C  CZ    . ARG A 1 2965 ? 200.083 211.283 227.560 1.00 25.01 ? 2965 ARG A CZ    1 
ATOM   12005 N  NH1   . ARG A 1 2965 ? 200.341 210.579 228.651 1.00 24.37 ? 2965 ARG A NH1   1 
ATOM   12006 N  NH2   . ARG A 1 2965 ? 198.896 211.163 226.973 1.00 22.57 ? 2965 ARG A NH2   1 
ATOM   12007 N  N     . LYS A 1 2966 ? 204.678 211.538 223.485 1.00 11.96 ? 2966 LYS A N     1 
ATOM   12008 C  CA    . LYS A 1 2966 ? 204.520 212.248 222.223 1.00 13.29 ? 2966 LYS A CA    1 
ATOM   12009 C  C     . LYS A 1 2966 ? 205.613 211.912 221.215 1.00 13.92 ? 2966 LYS A C     1 
ATOM   12010 O  O     . LYS A 1 2966 ? 205.769 212.631 220.223 1.00 15.53 ? 2966 LYS A O     1 
ATOM   12011 C  CB    . LYS A 1 2966 ? 204.480 213.757 222.470 1.00 11.67 ? 2966 LYS A CB    1 
ATOM   12012 C  CG    . LYS A 1 2966 ? 203.343 214.260 223.368 1.00 14.13 ? 2966 LYS A CG    1 
ATOM   12013 C  CD    . LYS A 1 2966 ? 201.959 214.187 222.715 1.00 14.24 ? 2966 LYS A CD    1 
ATOM   12014 C  CE    . LYS A 1 2966 ? 201.210 212.901 223.048 1.00 22.43 ? 2966 LYS A CE    1 
ATOM   12015 N  NZ    . LYS A 1 2966 ? 199.828 212.908 222.489 1.00 26.74 ? 2966 LYS A NZ    1 
ATOM   12016 N  N     . TYR A 1 2967 ? 206.378 210.849 221.447 1.00 14.54 ? 2967 TYR A N     1 
ATOM   12017 C  CA    . TYR A 1 2967 ? 207.437 210.460 220.524 1.00 7.91  ? 2967 TYR A CA    1 
ATOM   12018 C  C     . TYR A 1 2967 ? 206.833 209.775 219.303 1.00 9.41  ? 2967 TYR A C     1 
ATOM   12019 O  O     . TYR A 1 2967 ? 206.121 208.776 219.428 1.00 9.78  ? 2967 TYR A O     1 
ATOM   12020 C  CB    . TYR A 1 2967 ? 208.422 209.533 221.233 1.00 6.96  ? 2967 TYR A CB    1 
ATOM   12021 C  CG    . TYR A 1 2967 ? 209.711 209.272 220.493 1.00 6.30  ? 2967 TYR A CG    1 
ATOM   12022 C  CD1   . TYR A 1 2967 ? 209.809 208.240 219.568 1.00 3.67  ? 2967 TYR A CD1   1 
ATOM   12023 C  CD2   . TYR A 1 2967 ? 210.840 210.041 220.740 1.00 4.79  ? 2967 TYR A CD2   1 
ATOM   12024 C  CE1   . TYR A 1 2967 ? 210.991 207.992 218.901 1.00 4.12  ? 2967 TYR A CE1   1 
ATOM   12025 C  CE2   . TYR A 1 2967 ? 212.025 209.801 220.079 1.00 4.61  ? 2967 TYR A CE2   1 
ATOM   12026 C  CZ    . TYR A 1 2967 ? 212.096 208.776 219.160 1.00 3.05  ? 2967 TYR A CZ    1 
ATOM   12027 O  OH    . TYR A 1 2967 ? 213.277 208.539 218.504 1.00 2.28  ? 2967 TYR A OH    1 
ATOM   12028 N  N     . THR A 1 2968 ? 207.115 210.314 218.118 1.00 11.71 ? 2968 THR A N     1 
ATOM   12029 C  CA    . THR A 1 2968 ? 206.469 209.877 216.888 1.00 12.46 ? 2968 THR A CA    1 
ATOM   12030 C  C     . THR A 1 2968 ? 207.503 209.363 215.892 1.00 7.81  ? 2968 THR A C     1 
ATOM   12031 O  O     . THR A 1 2968 ? 208.692 209.232 216.201 1.00 5.40  ? 2968 THR A O     1 
ATOM   12032 C  CB    . THR A 1 2968 ? 205.643 211.010 216.267 1.00 12.70 ? 2968 THR A CB    1 
ATOM   12033 O  OG1   . THR A 1 2968 ? 206.525 211.986 215.704 1.00 15.79 ? 2968 THR A OG1   1 
ATOM   12034 C  CG2   . THR A 1 2968 ? 204.754 211.664 217.309 1.00 9.53  ? 2968 THR A CG2   1 
ATOM   12035 N  N     . GLY A 1 2969 ? 207.026 209.066 214.681 1.00 10.22 ? 2969 GLY A N     1 
ATOM   12036 C  CA    . GLY A 1 2969 ? 207.880 208.450 213.678 1.00 5.06  ? 2969 GLY A CA    1 
ATOM   12037 C  C     . GLY A 1 2969 ? 208.989 209.361 213.187 1.00 8.75  ? 2969 GLY A C     1 
ATOM   12038 O  O     . GLY A 1 2969 ? 210.118 208.915 212.972 1.00 14.85 ? 2969 GLY A O     1 
ATOM   12039 N  N     . GLU A 1 2970 ? 208.684 210.645 212.987 1.00 9.14  ? 2970 GLU A N     1 
ATOM   12040 C  CA    . GLU A 1 2970 ? 209.719 211.566 212.529 1.00 7.41  ? 2970 GLU A CA    1 
ATOM   12041 C  C     . GLU A 1 2970 ? 210.687 211.918 213.652 1.00 8.50  ? 2970 GLU A C     1 
ATOM   12042 O  O     . GLU A 1 2970 ? 211.810 212.368 213.394 1.00 9.51  ? 2970 GLU A O     1 
ATOM   12043 C  CB    . GLU A 1 2970 ? 209.095 212.820 211.907 1.00 8.53  ? 2970 GLU A CB    1 
ATOM   12044 C  CG    . GLU A 1 2970 ? 208.373 213.756 212.853 1.00 14.23 ? 2970 GLU A CG    1 
ATOM   12045 C  CD    . GLU A 1 2970 ? 206.929 213.350 213.095 1.00 24.13 ? 2970 GLU A CD    1 
ATOM   12046 O  OE1   . GLU A 1 2970 ? 206.564 212.197 212.781 1.00 18.74 ? 2970 GLU A OE1   1 
ATOM   12047 O  OE2   . GLU A 1 2970 ? 206.153 214.193 213.594 1.00 26.04 ? 2970 GLU A OE2   1 
ATOM   12048 N  N     . ASP A 1 2971 ? 210.274 211.726 214.908 1.00 10.01 ? 2971 ASP A N     1 
ATOM   12049 C  CA    . ASP A 1 2971 ? 211.237 211.769 216.004 1.00 8.49  ? 2971 ASP A CA    1 
ATOM   12050 C  C     . ASP A 1 2971 ? 212.218 210.608 215.914 1.00 4.90  ? 2971 ASP A C     1 
ATOM   12051 O  O     . ASP A 1 2971 ? 213.416 210.773 216.172 1.00 5.63  ? 2971 ASP A O     1 
ATOM   12052 C  CB    . ASP A 1 2971 ? 210.516 211.754 217.352 1.00 7.13  ? 2971 ASP A CB    1 
ATOM   12053 C  CG    . ASP A 1 2971 ? 209.565 212.916 217.515 1.00 14.11 ? 2971 ASP A CG    1 
ATOM   12054 O  OD1   . ASP A 1 2971 ? 208.636 213.047 216.692 1.00 20.29 ? 2971 ASP A OD1   1 
ATOM   12055 O  OD2   . ASP A 1 2971 ? 209.750 213.701 218.468 1.00 19.08 ? 2971 ASP A OD2   1 
ATOM   12056 N  N     . PHE A 1 2972 ? 211.722 209.421 215.561 1.00 3.81  ? 2972 PHE A N     1 
ATOM   12057 C  CA    . PHE A 1 2972 ? 212.601 208.271 215.386 1.00 2.66  ? 2972 PHE A CA    1 
ATOM   12058 C  C     . PHE A 1 2972 ? 213.515 208.457 214.182 1.00 2.95  ? 2972 PHE A C     1 
ATOM   12059 O  O     . PHE A 1 2972 ? 214.681 208.049 214.214 1.00 1.97  ? 2972 PHE A O     1 
ATOM   12060 C  CB    . PHE A 1 2972 ? 211.768 206.997 215.249 1.00 3.15  ? 2972 PHE A CB    1 
ATOM   12061 C  CG    . PHE A 1 2972 ? 212.580 205.735 215.257 1.00 3.16  ? 2972 PHE A CG    1 
ATOM   12062 C  CD1   . PHE A 1 2972 ? 213.294 205.362 216.382 1.00 2.89  ? 2972 PHE A CD1   1 
ATOM   12063 C  CD2   . PHE A 1 2972 ? 212.621 204.913 214.144 1.00 2.47  ? 2972 PHE A CD2   1 
ATOM   12064 C  CE1   . PHE A 1 2972 ? 214.040 204.200 216.393 1.00 2.33  ? 2972 PHE A CE1   1 
ATOM   12065 C  CE2   . PHE A 1 2972 ? 213.364 203.753 214.151 1.00 1.98  ? 2972 PHE A CE2   1 
ATOM   12066 C  CZ    . PHE A 1 2972 ? 214.074 203.396 215.277 1.00 1.83  ? 2972 PHE A CZ    1 
ATOM   12067 N  N     . ASP A 1 2973 ? 213.001 209.068 213.110 1.00 4.80  ? 2973 ASP A N     1 
ATOM   12068 C  CA    . ASP A 1 2973 ? 213.824 209.318 211.932 1.00 3.06  ? 2973 ASP A CA    1 
ATOM   12069 C  C     . ASP A 1 2973 ? 214.947 210.300 212.236 1.00 2.19  ? 2973 ASP A C     1 
ATOM   12070 O  O     . ASP A 1 2973 ? 216.087 210.105 211.798 1.00 1.86  ? 2973 ASP A O     1 
ATOM   12071 C  CB    . ASP A 1 2973 ? 212.954 209.833 210.786 1.00 4.72  ? 2973 ASP A CB    1 
ATOM   12072 C  CG    . ASP A 1 2973 ? 212.269 208.717 210.027 1.00 11.09 ? 2973 ASP A CG    1 
ATOM   12073 O  OD1   . ASP A 1 2973 ? 212.452 207.542 210.404 1.00 16.70 ? 2973 ASP A OD1   1 
ATOM   12074 O  OD2   . ASP A 1 2973 ? 211.549 209.012 209.052 1.00 12.80 ? 2973 ASP A OD2   1 
ATOM   12075 N  N     . GLU A 1 2974 ? 214.645 211.367 212.979 1.00 2.57  ? 2974 GLU A N     1 
ATOM   12076 C  CA    . GLU A 1 2974 ? 215.689 212.305 213.375 1.00 4.55  ? 2974 GLU A CA    1 
ATOM   12077 C  C     . GLU A 1 2974 ? 216.697 211.645 214.305 1.00 5.37  ? 2974 GLU A C     1 
ATOM   12078 O  O     . GLU A 1 2974 ? 217.902 211.906 214.212 1.00 3.23  ? 2974 GLU A O     1 
ATOM   12079 C  CB    . GLU A 1 2974 ? 215.067 213.540 214.027 1.00 4.00  ? 2974 GLU A CB    1 
ATOM   12080 C  CG    . GLU A 1 2974 ? 216.077 214.600 214.439 1.00 10.34 ? 2974 GLU A CG    1 
ATOM   12081 C  CD    . GLU A 1 2974 ? 216.804 215.221 213.258 1.00 20.29 ? 2974 GLU A CD    1 
ATOM   12082 O  OE1   . GLU A 1 2974 ? 216.247 215.229 212.140 1.00 18.86 ? 2974 GLU A OE1   1 
ATOM   12083 O  OE2   . GLU A 1 2974 ? 217.943 215.696 213.449 1.00 22.19 ? 2974 GLU A OE2   1 
ATOM   12084 N  N     . ASP A 1 2975 ? 216.223 210.785 215.210 1.00 3.29  ? 2975 ASP A N     1 
ATOM   12085 C  CA    . ASP A 1 2975 ? 217.136 210.035 216.064 1.00 2.52  ? 2975 ASP A CA    1 
ATOM   12086 C  C     . ASP A 1 2975 ? 218.001 209.086 215.244 1.00 1.89  ? 2975 ASP A C     1 
ATOM   12087 O  O     . ASP A 1 2975 ? 219.191 208.918 215.527 1.00 2.80  ? 2975 ASP A O     1 
ATOM   12088 C  CB    . ASP A 1 2975 ? 216.351 209.270 217.129 1.00 2.75  ? 2975 ASP A CB    1 
ATOM   12089 C  CG    . ASP A 1 2975 ? 216.048 210.117 218.346 1.00 8.35  ? 2975 ASP A CG    1 
ATOM   12090 O  OD1   . ASP A 1 2975 ? 216.662 211.193 218.491 1.00 15.00 ? 2975 ASP A OD1   1 
ATOM   12091 O  OD2   . ASP A 1 2975 ? 215.190 209.713 219.158 1.00 8.17  ? 2975 ASP A OD2   1 
ATOM   12092 N  N     . LEU A 1 2976 ? 217.418 208.458 214.219 1.00 1.69  ? 2976 LEU A N     1 
ATOM   12093 C  CA    . LEU A 1 2976 ? 218.201 207.604 213.331 1.00 1.05  ? 2976 LEU A CA    1 
ATOM   12094 C  C     . LEU A 1 2976 ? 219.271 208.402 212.600 1.00 1.17  ? 2976 LEU A C     1 
ATOM   12095 O  O     . LEU A 1 2976 ? 220.400 207.930 212.431 1.00 1.52  ? 2976 LEU A O     1 
ATOM   12096 C  CB    . LEU A 1 2976 ? 217.288 206.901 212.328 1.00 1.22  ? 2976 LEU A CB    1 
ATOM   12097 C  CG    . LEU A 1 2976 ? 216.523 205.670 212.807 1.00 1.10  ? 2976 LEU A CG    1 
ATOM   12098 C  CD1   . LEU A 1 2976 ? 215.679 205.114 211.673 1.00 2.23  ? 2976 LEU A CD1   1 
ATOM   12099 C  CD2   . LEU A 1 2976 ? 217.475 204.617 213.343 1.00 1.12  ? 2976 LEU A CD2   1 
ATOM   12100 N  N     . ARG A 1 2977 ? 218.932 209.613 212.153 1.00 1.69  ? 2977 ARG A N     1 
ATOM   12101 C  CA    . ARG A 1 2977 ? 219.911 210.451 211.469 1.00 0.85  ? 2977 ARG A CA    1 
ATOM   12102 C  C     . ARG A 1 2977 ? 221.069 210.806 212.389 1.00 1.03  ? 2977 ARG A C     1 
ATOM   12103 O  O     . ARG A 1 2977 ? 222.225 210.842 211.954 1.00 2.03  ? 2977 ARG A O     1 
ATOM   12104 C  CB    . ARG A 1 2977 ? 219.243 211.720 210.939 1.00 1.62  ? 2977 ARG A CB    1 
ATOM   12105 C  CG    . ARG A 1 2977 ? 218.404 211.515 209.696 1.00 1.15  ? 2977 ARG A CG    1 
ATOM   12106 C  CD    . ARG A 1 2977 ? 217.619 212.768 209.344 1.00 2.50  ? 2977 ARG A CD    1 
ATOM   12107 N  NE    . ARG A 1 2977 ? 216.370 212.443 208.671 1.00 4.86  ? 2977 ARG A NE    1 
ATOM   12108 C  CZ    . ARG A 1 2977 ? 215.166 212.720 209.149 1.00 2.25  ? 2977 ARG A CZ    1 
ATOM   12109 N  NH1   . ARG A 1 2977 ? 215.008 213.367 210.291 1.00 1.33  ? 2977 ARG A NH1   1 
ATOM   12110 N  NH2   . ARG A 1 2977 ? 214.093 212.339 208.462 1.00 3.86  ? 2977 ARG A NH2   1 
ATOM   12111 N  N     . THR A 1 2978 ? 220.779 211.074 213.662 1.00 1.23  ? 2978 THR A N     1 
ATOM   12112 C  CA    . THR A 1 2978 ? 221.833 211.425 214.607 1.00 1.54  ? 2978 THR A CA    1 
ATOM   12113 C  C     . THR A 1 2978 ? 222.820 210.278 214.792 1.00 1.39  ? 2978 THR A C     1 
ATOM   12114 O  O     . THR A 1 2978 ? 224.037 210.490 214.784 1.00 1.51  ? 2978 THR A O     1 
ATOM   12115 C  CB    . THR A 1 2978 ? 221.218 211.831 215.947 1.00 1.99  ? 2978 THR A CB    1 
ATOM   12116 O  OG1   . THR A 1 2978 ? 220.485 213.051 215.786 1.00 6.14  ? 2978 THR A OG1   1 
ATOM   12117 C  CG2   . THR A 1 2978 ? 222.296 212.032 217.000 1.00 1.72  ? 2978 THR A CG2   1 
ATOM   12118 N  N     . VAL A 1 2979 ? 222.314 209.053 214.945 1.00 1.00  ? 2979 VAL A N     1 
ATOM   12119 C  CA    . VAL A 1 2979 ? 223.193 207.906 215.153 1.00 0.92  ? 2979 VAL A CA    1 
ATOM   12120 C  C     . VAL A 1 2979 ? 223.988 207.600 213.891 1.00 1.18  ? 2979 VAL A C     1 
ATOM   12121 O  O     . VAL A 1 2979 ? 225.175 207.263 213.955 1.00 2.28  ? 2979 VAL A O     1 
ATOM   12122 C  CB    . VAL A 1 2979 ? 222.380 206.683 215.616 1.00 1.34  ? 2979 VAL A CB    1 
ATOM   12123 C  CG1   . VAL A 1 2979 ? 223.305 205.579 216.093 1.00 1.51  ? 2979 VAL A CG1   1 
ATOM   12124 C  CG2   . VAL A 1 2979 ? 221.431 207.077 216.715 1.00 2.40  ? 2979 VAL A CG2   1 
ATOM   12125 N  N     . LEU A 1 2980 ? 223.347 207.702 212.725 1.00 1.41  ? 2980 LEU A N     1 
ATOM   12126 C  CA    . LEU A 1 2980 ? 224.036 207.393 211.477 1.00 0.77  ? 2980 LEU A CA    1 
ATOM   12127 C  C     . LEU A 1 2980 ? 225.129 208.410 211.175 1.00 0.71  ? 2980 LEU A C     1 
ATOM   12128 O  O     . LEU A 1 2980 ? 226.200 208.043 210.682 1.00 1.55  ? 2980 LEU A O     1 
ATOM   12129 C  CB    . LEU A 1 2980 ? 223.030 207.312 210.330 1.00 1.29  ? 2980 LEU A CB    1 
ATOM   12130 C  CG    . LEU A 1 2980 ? 222.093 206.103 210.374 1.00 0.48  ? 2980 LEU A CG    1 
ATOM   12131 C  CD1   . LEU A 1 2980 ? 221.236 206.040 209.127 1.00 2.31  ? 2980 LEU A CD1   1 
ATOM   12132 C  CD2   . LEU A 1 2980 ? 222.875 204.818 210.551 1.00 0.36  ? 2980 LEU A CD2   1 
ATOM   12133 N  N     . ARG A 1 2981 ? 224.881 209.691 211.456 1.00 1.55  ? 2981 ARG A N     1 
ATOM   12134 C  CA    . ARG A 1 2981 ? 225.915 210.701 211.250 1.00 1.46  ? 2981 ARG A CA    1 
ATOM   12135 C  C     . ARG A 1 2981 ? 227.127 210.435 212.132 1.00 1.56  ? 2981 ARG A C     1 
ATOM   12136 O  O     . ARG A 1 2981 ? 228.271 210.559 211.683 1.00 2.09  ? 2981 ARG A O     1 
ATOM   12137 C  CB    . ARG A 1 2981 ? 225.364 212.100 211.526 1.00 2.02  ? 2981 ARG A CB    1 
ATOM   12138 C  CG    . ARG A 1 2981 ? 224.362 212.611 210.517 1.00 2.35  ? 2981 ARG A CG    1 
ATOM   12139 C  CD    . ARG A 1 2981 ? 223.691 213.877 211.033 1.00 2.83  ? 2981 ARG A CD    1 
ATOM   12140 N  NE    . ARG A 1 2981 ? 222.664 214.395 210.136 1.00 3.16  ? 2981 ARG A NE    1 
ATOM   12141 C  CZ    . ARG A 1 2981 ? 222.897 214.920 208.941 1.00 5.86  ? 2981 ARG A CZ    1 
ATOM   12142 N  NH1   . ARG A 1 2981 ? 224.122 215.015 208.451 1.00 6.48  ? 2981 ARG A NH1   1 
ATOM   12143 N  NH2   . ARG A 1 2981 ? 221.873 215.367 208.219 1.00 4.80  ? 2981 ARG A NH2   1 
ATOM   12144 N  N     . ARG A 1 2982 ? 226.896 210.070 213.393 1.00 1.16  ? 2982 ARG A N     1 
ATOM   12145 C  CA    . ARG A 1 2982 ? 228.009 209.834 214.305 1.00 1.33  ? 2982 ARG A CA    1 
ATOM   12146 C  C     . ARG A 1 2982 ? 228.816 208.607 213.897 1.00 1.66  ? 2982 ARG A C     1 
ATOM   12147 O  O     . ARG A 1 2982 ? 230.052 208.636 213.921 1.00 4.54  ? 2982 ARG A O     1 
ATOM   12148 C  CB    . ARG A 1 2982 ? 227.491 209.694 215.734 1.00 1.76  ? 2982 ARG A CB    1 
ATOM   12149 C  CG    . ARG A 1 2982 ? 226.915 210.972 216.313 1.00 1.43  ? 2982 ARG A CG    1 
ATOM   12150 C  CD    . ARG A 1 2982 ? 226.197 210.707 217.620 1.00 1.65  ? 2982 ARG A CD    1 
ATOM   12151 N  NE    . ARG A 1 2982 ? 227.078 210.099 218.608 1.00 3.40  ? 2982 ARG A NE    1 
ATOM   12152 C  CZ    . ARG A 1 2982 ? 226.687 209.674 219.801 1.00 3.23  ? 2982 ARG A CZ    1 
ATOM   12153 N  NH1   . ARG A 1 2982 ? 225.427 209.767 220.189 1.00 2.15  ? 2982 ARG A NH1   1 
ATOM   12154 N  NH2   . ARG A 1 2982 ? 227.582 209.140 220.625 1.00 3.15  ? 2982 ARG A NH2   1 
ATOM   12155 N  N     . SER A 1 2983 ? 228.144 207.525 213.512 1.00 1.19  ? 2983 SER A N     1 
ATOM   12156 C  CA    . SER A 1 2983 ? 228.838 206.298 213.145 1.00 1.04  ? 2983 SER A CA    1 
ATOM   12157 C  C     . SER A 1 2983 ? 229.260 206.262 211.683 1.00 1.85  ? 2983 SER A C     1 
ATOM   12158 O  O     . SER A 1 2983 ? 230.196 205.530 211.343 1.00 1.63  ? 2983 SER A O     1 
ATOM   12159 C  CB    . SER A 1 2983 ? 227.962 205.079 213.453 1.00 0.77  ? 2983 SER A CB    1 
ATOM   12160 O  OG    . SER A 1 2983 ? 226.974 204.887 212.460 1.00 2.42  ? 2983 SER A OG    1 
ATOM   12161 N  N     . GLY A 1 2984 ? 228.605 207.028 210.816 1.00 1.24  ? 2984 GLY A N     1 
ATOM   12162 C  CA    . GLY A 1 2984 ? 228.946 207.019 209.410 1.00 0.78  ? 2984 GLY A CA    1 
ATOM   12163 C  C     . GLY A 1 2984 ? 229.913 208.109 208.998 1.00 2.04  ? 2984 GLY A C     1 
ATOM   12164 O  O     . GLY A 1 2984 ? 230.693 207.928 208.060 1.00 2.82  ? 2984 GLY A O     1 
ATOM   12165 N  N     . CYS A 1 2985 ? 229.880 209.246 209.689 1.00 2.01  ? 2985 CYS A N     1 
ATOM   12166 C  CA    . CYS A 1 2985 ? 230.722 210.387 209.349 1.00 3.51  ? 2985 CYS A CA    1 
ATOM   12167 C  C     . CYS A 1 2985 ? 231.845 210.632 210.341 1.00 3.62  ? 2985 CYS A C     1 
ATOM   12168 O  O     . CYS A 1 2985 ? 232.953 210.982 209.933 1.00 5.24  ? 2985 CYS A O     1 
ATOM   12169 C  CB    . CYS A 1 2985 ? 229.872 211.657 209.232 1.00 2.14  ? 2985 CYS A CB    1 
ATOM   12170 S  SG    . CYS A 1 2985 ? 228.504 211.542 208.064 1.00 12.57 ? 2985 CYS A SG    1 
ATOM   12171 N  N     . LYS A 1 2986 ? 231.591 210.458 211.636 1.00 2.93  ? 2986 LYS A N     1 
ATOM   12172 C  CA    . LYS A 1 2986 ? 232.574 210.734 212.674 1.00 2.53  ? 2986 LYS A CA    1 
ATOM   12173 C  C     . LYS A 1 2986 ? 233.351 209.497 213.105 1.00 2.60  ? 2986 LYS A C     1 
ATOM   12174 O  O     . LYS A 1 2986 ? 234.178 209.590 214.018 1.00 7.21  ? 2986 LYS A O     1 
ATOM   12175 C  CB    . LYS A 1 2986 ? 231.893 211.372 213.885 1.00 2.16  ? 2986 LYS A CB    1 
ATOM   12176 C  CG    . LYS A 1 2986 ? 231.235 212.705 213.589 1.00 4.39  ? 2986 LYS A CG    1 
ATOM   12177 C  CD    . LYS A 1 2986 ? 232.288 213.753 213.264 1.00 9.22  ? 2986 LYS A CD    1 
ATOM   12178 C  CE    . LYS A 1 2986 ? 231.672 215.119 213.040 1.00 10.89 ? 2986 LYS A CE    1 
ATOM   12179 N  NZ    . LYS A 1 2986 ? 232.713 216.121 212.682 1.00 15.28 ? 2986 LYS A NZ    1 
ATOM   12180 N  N     . ASN A 1 2987 ? 233.105 208.347 212.474 1.00 2.29  ? 2987 ASN A N     1 
ATOM   12181 C  CA    . ASN A 1 2987 ? 233.825 207.107 212.767 1.00 1.55  ? 2987 ASN A CA    1 
ATOM   12182 C  C     . ASN A 1 2987 ? 233.693 206.709 214.237 1.00 1.87  ? 2987 ASN A C     1 
ATOM   12183 O  O     . ASN A 1 2987 ? 234.636 206.208 214.852 1.00 1.95  ? 2987 ASN A O     1 
ATOM   12184 C  CB    . ASN A 1 2987 ? 235.297 207.224 212.364 1.00 1.58  ? 2987 ASN A CB    1 
ATOM   12185 C  CG    . ASN A 1 2987 ? 235.948 205.880 212.142 1.00 2.85  ? 2987 ASN A CG    1 
ATOM   12186 O  OD1   . ASN A 1 2987 ? 235.433 205.041 211.405 1.00 5.37  ? 2987 ASN A OD1   1 
ATOM   12187 N  ND2   . ASN A 1 2987 ? 237.092 205.667 212.777 1.00 1.57  ? 2987 ASN A ND2   1 
ATOM   12188 N  N     . GLU A 1 2988 ? 232.510 206.920 214.802 1.00 1.46  ? 2988 GLU A N     1 
ATOM   12189 C  CA    . GLU A 1 2988 ? 232.256 206.653 216.212 1.00 1.57  ? 2988 GLU A CA    1 
ATOM   12190 C  C     . GLU A 1 2988 ? 231.565 205.304 216.359 1.00 2.26  ? 2988 GLU A C     1 
ATOM   12191 O  O     . GLU A 1 2988 ? 230.480 205.095 215.806 1.00 2.94  ? 2988 GLU A O     1 
ATOM   12192 C  CB    . GLU A 1 2988 ? 231.407 207.763 216.827 1.00 2.11  ? 2988 GLU A CB    1 
ATOM   12193 C  CG    . GLU A 1 2988 ? 231.061 207.536 218.285 1.00 3.39  ? 2988 GLU A CG    1 
ATOM   12194 C  CD    . GLU A 1 2988 ? 230.154 208.611 218.843 1.00 7.99  ? 2988 GLU A CD    1 
ATOM   12195 O  OE1   . GLU A 1 2988 ? 229.764 209.520 218.081 1.00 10.74 ? 2988 GLU A OE1   1 
ATOM   12196 O  OE2   . GLU A 1 2988 ? 229.830 208.547 220.045 1.00 10.20 ? 2988 GLU A OE2   1 
ATOM   12197 N  N     . LYS A 1 2989 ? 232.189 204.396 217.106 1.00 1.95  ? 2989 LYS A N     1 
ATOM   12198 C  CA    . LYS A 1 2989 ? 231.580 203.105 217.396 1.00 1.05  ? 2989 LYS A CA    1 
ATOM   12199 C  C     . LYS A 1 2989 ? 230.435 203.296 218.384 1.00 0.72  ? 2989 LYS A C     1 
ATOM   12200 O  O     . LYS A 1 2989 ? 230.633 203.829 219.480 1.00 1.04  ? 2989 LYS A O     1 
ATOM   12201 C  CB    . LYS A 1 2989 ? 232.624 202.141 217.953 1.00 2.46  ? 2989 LYS A CB    1 
ATOM   12202 C  CG    . LYS A 1 2989 ? 233.696 201.750 216.948 1.00 3.18  ? 2989 LYS A CG    1 
ATOM   12203 C  CD    . LYS A 1 2989 ? 234.614 200.668 217.489 1.00 3.90  ? 2989 LYS A CD    1 
ATOM   12204 C  CE    . LYS A 1 2989 ? 235.568 201.212 218.533 1.00 12.56 ? 2989 LYS A CE    1 
ATOM   12205 N  NZ    . LYS A 1 2989 ? 236.540 200.179 218.982 1.00 24.52 ? 2989 LYS A NZ    1 
ATOM   12206 N  N     . ILE A 1 2990 ? 229.237 202.865 217.997 1.00 1.75  ? 2990 ILE A N     1 
ATOM   12207 C  CA    . ILE A 1 2990 ? 228.019 203.149 218.744 1.00 0.49  ? 2990 ILE A CA    1 
ATOM   12208 C  C     . ILE A 1 2990 ? 227.257 201.852 218.973 1.00 0.47  ? 2990 ILE A C     1 
ATOM   12209 O  O     . ILE A 1 2990 ? 227.050 201.072 218.036 1.00 0.41  ? 2990 ILE A O     1 
ATOM   12210 C  CB    . ILE A 1 2990 ? 227.131 204.172 218.009 1.00 0.62  ? 2990 ILE A CB    1 
ATOM   12211 C  CG1   . ILE A 1 2990 ? 227.783 205.555 218.035 1.00 1.35  ? 2990 ILE A CG1   1 
ATOM   12212 C  CG2   . ILE A 1 2990 ? 225.738 204.220 218.622 1.00 0.57  ? 2990 ILE A CG2   1 
ATOM   12213 C  CD1   . ILE A 1 2990 ? 226.931 206.639 217.441 1.00 1.18  ? 2990 ILE A CD1   1 
ATOM   12214 N  N     . ALA A 1 2991 ? 226.843 201.624 220.216 1.00 0.66  ? 2991 ALA A N     1 
ATOM   12215 C  CA    . ALA A 1 2991 ? 225.918 200.547 220.560 1.00 0.46  ? 2991 ALA A CA    1 
ATOM   12216 C  C     . ALA A 1 2991 ? 224.525 201.160 220.659 1.00 0.71  ? 2991 ALA A C     1 
ATOM   12217 O  O     . ALA A 1 2991 ? 224.185 201.802 221.655 1.00 0.75  ? 2991 ALA A O     1 
ATOM   12218 C  CB    . ALA A 1 2991 ? 226.325 199.860 221.858 1.00 0.26  ? 2991 ALA A CB    1 
ATOM   12219 N  N     . PHE A 1 2992 ? 223.725 200.968 219.616 1.00 0.47  ? 2992 PHE A N     1 
ATOM   12220 C  CA    . PHE A 1 2992 ? 222.365 201.496 219.559 1.00 0.56  ? 2992 PHE A CA    1 
ATOM   12221 C  C     . PHE A 1 2992 ? 221.451 200.488 220.245 1.00 0.98  ? 2992 PHE A C     1 
ATOM   12222 O  O     . PHE A 1 2992 ? 220.983 199.531 219.626 1.00 2.31  ? 2992 PHE A O     1 
ATOM   12223 C  CB    . PHE A 1 2992 ? 221.960 201.761 218.111 1.00 0.87  ? 2992 PHE A CB    1 
ATOM   12224 C  CG    . PHE A 1 2992 ? 220.567 202.301 217.952 1.00 1.14  ? 2992 PHE A CG    1 
ATOM   12225 C  CD1   . PHE A 1 2992 ? 219.963 203.022 218.966 1.00 1.79  ? 2992 PHE A CD1   1 
ATOM   12226 C  CD2   . PHE A 1 2992 ? 219.865 202.091 216.778 1.00 2.15  ? 2992 PHE A CD2   1 
ATOM   12227 C  CE1   . PHE A 1 2992 ? 218.685 203.510 218.818 1.00 6.02  ? 2992 PHE A CE1   1 
ATOM   12228 C  CE2   . PHE A 1 2992 ? 218.586 202.582 216.621 1.00 2.83  ? 2992 PHE A CE2   1 
ATOM   12229 C  CZ    . PHE A 1 2992 ? 217.994 203.293 217.641 1.00 5.61  ? 2992 PHE A CZ    1 
ATOM   12230 N  N     . ILE A 1 2993 ? 221.195 200.708 221.529 1.00 1.21  ? 2993 ILE A N     1 
ATOM   12231 C  CA    . ILE A 1 2993 ? 220.409 199.787 222.341 1.00 0.79  ? 2993 ILE A CA    1 
ATOM   12232 C  C     . ILE A 1 2993 ? 218.962 200.257 222.338 1.00 1.08  ? 2993 ILE A C     1 
ATOM   12233 O  O     . ILE A 1 2993 ? 218.661 201.375 222.770 1.00 2.78  ? 2993 ILE A O     1 
ATOM   12234 C  CB    . ILE A 1 2993 ? 220.960 199.698 223.771 1.00 0.63  ? 2993 ILE A CB    1 
ATOM   12235 C  CG1   . ILE A 1 2993 ? 222.460 199.402 223.737 1.00 0.20  ? 2993 ILE A CG1   1 
ATOM   12236 C  CG2   . ILE A 1 2993 ? 220.208 198.638 224.566 1.00 0.46  ? 2993 ILE A CG2   1 
ATOM   12237 C  CD1   . ILE A 1 2993 ? 223.101 199.319 225.099 1.00 0.23  ? 2993 ILE A CD1   1 
ATOM   12238 N  N     . MET A 1 2994 ? 218.066 199.406 221.852 1.00 1.62  ? 2994 MET A N     1 
ATOM   12239 C  CA    . MET A 1 2994 ? 216.661 199.749 221.710 1.00 3.06  ? 2994 MET A CA    1 
ATOM   12240 C  C     . MET A 1 2994 ? 215.797 198.565 222.118 1.00 1.95  ? 2994 MET A C     1 
ATOM   12241 O  O     . MET A 1 2994 ? 216.026 197.435 221.680 1.00 3.00  ? 2994 MET A O     1 
ATOM   12242 C  CB    . MET A 1 2994 ? 216.361 200.192 220.270 1.00 5.53  ? 2994 MET A CB    1 
ATOM   12243 C  CG    . MET A 1 2994 ? 214.932 200.625 220.017 1.00 15.46 ? 2994 MET A CG    1 
ATOM   12244 S  SD    . MET A 1 2994 ? 214.677 201.165 218.314 1.00 38.27 ? 2994 MET A SD    1 
ATOM   12245 C  CE    . MET A 1 2994 ? 214.759 199.621 217.424 1.00 18.23 ? 2994 MET A CE    1 
ATOM   12246 N  N     . ASP A 1 2995 ? 214.814 198.832 222.969 1.00 3.10  ? 2995 ASP A N     1 
ATOM   12247 C  CA    . ASP A 1 2995 ? 213.920 197.812 223.492 1.00 7.54  ? 2995 ASP A CA    1 
ATOM   12248 C  C     . ASP A 1 2995 ? 212.670 197.687 222.628 1.00 4.79  ? 2995 ASP A C     1 
ATOM   12249 O  O     . ASP A 1 2995 ? 212.372 198.546 221.794 1.00 5.59  ? 2995 ASP A O     1 
ATOM   12250 C  CB    . ASP A 1 2995 ? 213.526 198.130 224.936 1.00 4.47  ? 2995 ASP A CB    1 
ATOM   12251 C  CG    . ASP A 1 2995 ? 213.101 196.899 225.711 1.00 6.70  ? 2995 ASP A CG    1 
ATOM   12252 O  OD1   . ASP A 1 2995 ? 213.983 196.181 226.222 1.00 10.19 ? 2995 ASP A OD1   1 
ATOM   12253 O  OD2   . ASP A 1 2995 ? 211.882 196.646 225.806 1.00 14.33 ? 2995 ASP A OD2   1 
ATOM   12254 N  N     . GLU A 1 2996 ? 211.937 196.592 222.842 1.00 9.20  ? 2996 GLU A N     1 
ATOM   12255 C  CA    . GLU A 1 2996 ? 210.658 196.410 222.162 1.00 10.14 ? 2996 GLU A CA    1 
ATOM   12256 C  C     . GLU A 1 2996 ? 209.662 197.491 222.563 1.00 6.65  ? 2996 GLU A C     1 
ATOM   12257 O  O     . GLU A 1 2996 ? 208.822 197.902 221.756 1.00 5.40  ? 2996 GLU A O     1 
ATOM   12258 C  CB    . GLU A 1 2996 ? 210.094 195.017 222.457 1.00 8.82  ? 2996 GLU A CB    1 
ATOM   12259 C  CG    . GLU A 1 2996 ? 209.728 194.786 223.916 1.00 9.39  ? 2996 GLU A CG    1 
ATOM   12260 C  CD    . GLU A 1 2996 ? 209.226 193.381 224.196 1.00 14.11 ? 2996 GLU A CD    1 
ATOM   12261 O  OE1   . GLU A 1 2996 ? 209.173 192.560 223.257 1.00 14.69 ? 2996 GLU A OE1   1 
ATOM   12262 O  OE2   . GLU A 1 2996 ? 208.894 193.094 225.361 1.00 9.34  ? 2996 GLU A OE2   1 
ATOM   12263 N  N     . SER A 1 2997 ? 209.742 197.964 223.809 1.00 7.48  ? 2997 SER A N     1 
ATOM   12264 C  CA    . SER A 1 2997 ? 208.847 199.024 224.260 1.00 9.61  ? 2997 SER A CA    1 
ATOM   12265 C  C     . SER A 1 2997 ? 209.117 200.329 223.523 1.00 8.91  ? 2997 SER A C     1 
ATOM   12266 O  O     . SER A 1 2997 ? 208.223 201.173 223.391 1.00 13.56 ? 2997 SER A O     1 
ATOM   12267 C  CB    . SER A 1 2997 ? 208.982 199.215 225.770 1.00 10.12 ? 2997 SER A CB    1 
ATOM   12268 O  OG    . SER A 1 2997 ? 210.342 199.329 226.145 1.00 12.39 ? 2997 SER A OG    1 
ATOM   12269 N  N     . ASN A 1 2998 ? 210.346 200.518 223.039 1.00 10.43 ? 2998 ASN A N     1 
ATOM   12270 C  CA    . ASN A 1 2998 ? 210.664 201.699 222.245 1.00 10.80 ? 2998 ASN A CA    1 
ATOM   12271 C  C     . ASN A 1 2998 ? 209.921 201.715 220.916 1.00 10.04 ? 2998 ASN A C     1 
ATOM   12272 O  O     . ASN A 1 2998 ? 209.788 202.780 220.306 1.00 15.54 ? 2998 ASN A O     1 
ATOM   12273 C  CB    . ASN A 1 2998 ? 212.170 201.777 221.990 1.00 7.15  ? 2998 ASN A CB    1 
ATOM   12274 C  CG    . ASN A 1 2998 ? 212.958 202.104 223.236 1.00 8.54  ? 2998 ASN A CG    1 
ATOM   12275 O  OD1   . ASN A 1 2998 ? 212.392 202.304 224.309 1.00 13.14 ? 2998 ASN A OD1   1 
ATOM   12276 N  ND2   . ASN A 1 2998 ? 214.275 202.155 223.103 1.00 10.16 ? 2998 ASN A ND2   1 
ATOM   12277 N  N     . VAL A 1 2999 ? 209.436 200.564 220.458 1.00 7.34  ? 2999 VAL A N     1 
ATOM   12278 C  CA    . VAL A 1 2999 ? 208.714 200.481 219.196 1.00 8.87  ? 2999 VAL A CA    1 
ATOM   12279 C  C     . VAL A 1 2999 ? 207.286 200.959 219.425 1.00 12.87 ? 2999 VAL A C     1 
ATOM   12280 O  O     . VAL A 1 2999 ? 206.404 200.174 219.792 1.00 13.95 ? 2999 VAL A O     1 
ATOM   12281 C  CB    . VAL A 1 2999 ? 208.743 199.049 218.629 1.00 8.10  ? 2999 VAL A CB    1 
ATOM   12282 C  CG1   . VAL A 1 2999 ? 207.914 198.954 217.356 1.00 9.88  ? 2999 VAL A CG1   1 
ATOM   12283 C  CG2   . VAL A 1 2999 ? 210.176 198.604 218.382 1.00 4.93  ? 2999 VAL A CG2   1 
ATOM   12284 N  N     . LEU A 1 3000 ? 207.054 202.256 219.224 1.00 14.90 ? 3000 LEU A N     1 
ATOM   12285 C  CA    . LEU A 1 3000 ? 205.723 202.819 219.402 1.00 13.87 ? 3000 LEU A CA    1 
ATOM   12286 C  C     . LEU A 1 3000 ? 204.873 202.707 218.147 1.00 15.62 ? 3000 LEU A C     1 
ATOM   12287 O  O     . LEU A 1 3000 ? 203.672 202.993 218.198 1.00 18.59 ? 3000 LEU A O     1 
ATOM   12288 C  CB    . LEU A 1 3000 ? 205.823 204.283 219.831 1.00 12.73 ? 3000 LEU A CB    1 
ATOM   12289 C  CG    . LEU A 1 3000 ? 206.808 204.587 220.959 1.00 12.94 ? 3000 LEU A CG    1 
ATOM   12290 C  CD1   . LEU A 1 3000 ? 206.710 206.041 221.382 1.00 10.96 ? 3000 LEU A CD1   1 
ATOM   12291 C  CD2   . LEU A 1 3000 ? 206.552 203.671 222.146 1.00 15.79 ? 3000 LEU A CD2   1 
ATOM   12292 N  N     . ASP A 1 3001 ? 205.466 202.293 217.031 1.00 11.81 ? 3001 ASP A N     1 
ATOM   12293 C  CA    . ASP A 1 3001 ? 204.758 202.161 215.770 1.00 12.60 ? 3001 ASP A CA    1 
ATOM   12294 C  C     . ASP A 1 3001 ? 205.484 201.136 214.911 1.00 15.10 ? 3001 ASP A C     1 
ATOM   12295 O  O     . ASP A 1 3001 ? 206.700 200.963 215.021 1.00 21.20 ? 3001 ASP A O     1 
ATOM   12296 C  CB    . ASP A 1 3001 ? 204.657 203.517 215.048 1.00 15.64 ? 3001 ASP A CB    1 
ATOM   12297 C  CG    . ASP A 1 3001 ? 204.264 203.383 213.590 1.00 21.96 ? 3001 ASP A CG    1 
ATOM   12298 O  OD1   . ASP A 1 3001 ? 203.441 202.500 213.266 1.00 25.55 ? 3001 ASP A OD1   1 
ATOM   12299 O  OD2   . ASP A 1 3001 ? 204.780 204.166 212.765 1.00 24.87 ? 3001 ASP A OD2   1 
ATOM   12300 N  N     . SER A 1 3002 ? 204.720 200.456 214.053 1.00 18.10 ? 3002 SER A N     1 
ATOM   12301 C  CA    . SER A 1 3002 ? 205.306 199.466 213.157 1.00 16.16 ? 3002 SER A CA    1 
ATOM   12302 C  C     . SER A 1 3002 ? 206.299 200.083 212.183 1.00 17.13 ? 3002 SER A C     1 
ATOM   12303 O  O     . SER A 1 3002 ? 207.179 199.376 211.681 1.00 20.17 ? 3002 SER A O     1 
ATOM   12304 C  CB    . SER A 1 3002 ? 204.205 198.741 212.383 1.00 19.14 ? 3002 SER A CB    1 
ATOM   12305 O  OG    . SER A 1 3002 ? 203.517 199.634 211.526 1.00 29.47 ? 3002 SER A OG    1 
ATOM   12306 N  N     . GLY A 1 3003 ? 206.178 201.382 211.901 1.00 11.81 ? 3003 GLY A N     1 
ATOM   12307 C  CA    . GLY A 1 3003 ? 207.116 202.034 211.007 1.00 7.77  ? 3003 GLY A CA    1 
ATOM   12308 C  C     . GLY A 1 3003 ? 208.514 202.152 211.569 1.00 10.48 ? 3003 GLY A C     1 
ATOM   12309 O  O     . GLY A 1 3003 ? 209.463 202.353 210.804 1.00 11.12 ? 3003 GLY A O     1 
ATOM   12310 N  N     . PHE A 1 3004 ? 208.662 202.037 212.891 1.00 10.84 ? 3004 PHE A N     1 
ATOM   12311 C  CA    . PHE A 1 3004 ? 209.990 202.063 213.493 1.00 7.47  ? 3004 PHE A CA    1 
ATOM   12312 C  C     . PHE A 1 3004 ? 210.836 200.900 212.994 1.00 4.35  ? 3004 PHE A C     1 
ATOM   12313 O  O     . PHE A 1 3004 ? 212.003 201.079 212.627 1.00 4.45  ? 3004 PHE A O     1 
ATOM   12314 C  CB    . PHE A 1 3004 ? 209.883 202.009 215.019 1.00 7.34  ? 3004 PHE A CB    1 
ATOM   12315 C  CG    . PHE A 1 3004 ? 209.472 203.307 215.662 1.00 6.24  ? 3004 PHE A CG    1 
ATOM   12316 C  CD1   . PHE A 1 3004 ? 208.603 204.178 215.028 1.00 6.20  ? 3004 PHE A CD1   1 
ATOM   12317 C  CD2   . PHE A 1 3004 ? 209.941 203.640 216.919 1.00 7.09  ? 3004 PHE A CD2   1 
ATOM   12318 C  CE1   . PHE A 1 3004 ? 208.221 205.358 215.628 1.00 5.07  ? 3004 PHE A CE1   1 
ATOM   12319 C  CE2   . PHE A 1 3004 ? 209.563 204.820 217.525 1.00 7.75  ? 3004 PHE A CE2   1 
ATOM   12320 C  CZ    . PHE A 1 3004 ? 208.701 205.680 216.877 1.00 6.76  ? 3004 PHE A CZ    1 
ATOM   12321 N  N     . LEU A 1 3005 ? 210.257 199.700 212.962 1.00 6.70  ? 3005 LEU A N     1 
ATOM   12322 C  CA    . LEU A 1 3005 ? 210.999 198.501 212.599 1.00 5.94  ? 3005 LEU A CA    1 
ATOM   12323 C  C     . LEU A 1 3005 ? 211.225 198.367 211.102 1.00 5.24  ? 3005 LEU A C     1 
ATOM   12324 O  O     . LEU A 1 3005 ? 212.174 197.688 210.694 1.00 8.10  ? 3005 LEU A O     1 
ATOM   12325 C  CB    . LEU A 1 3005 ? 210.277 197.262 213.121 1.00 5.88  ? 3005 LEU A CB    1 
ATOM   12326 C  CG    . LEU A 1 3005 ? 210.301 197.142 214.641 1.00 12.60 ? 3005 LEU A CG    1 
ATOM   12327 C  CD1   . LEU A 1 3005 ? 209.656 195.850 215.058 1.00 12.15 ? 3005 LEU A CD1   1 
ATOM   12328 C  CD2   . LEU A 1 3005 ? 211.728 197.227 215.161 1.00 5.80  ? 3005 LEU A CD2   1 
ATOM   12329 N  N     . GLU A 1 3006 ? 210.378 198.982 210.277 1.00 4.73  ? 3006 GLU A N     1 
ATOM   12330 C  CA    . GLU A 1 3006 ? 210.634 198.989 208.842 1.00 6.72  ? 3006 GLU A CA    1 
ATOM   12331 C  C     . GLU A 1 3006 ? 211.920 199.744 208.531 1.00 5.91  ? 3006 GLU A C     1 
ATOM   12332 O  O     . GLU A 1 3006 ? 212.646 199.391 207.595 1.00 8.03  ? 3006 GLU A O     1 
ATOM   12333 C  CB    . GLU A 1 3006 ? 209.436 199.593 208.107 1.00 8.24  ? 3006 GLU A CB    1 
ATOM   12334 C  CG    . GLU A 1 3006 ? 209.455 199.457 206.591 1.00 6.07  ? 3006 GLU A CG    1 
ATOM   12335 C  CD    . GLU A 1 3006 ? 210.268 200.540 205.907 1.00 24.78 ? 3006 GLU A CD    1 
ATOM   12336 O  OE1   . GLU A 1 3006 ? 210.364 201.654 206.462 1.00 18.48 ? 3006 GLU A OE1   1 
ATOM   12337 O  OE2   . GLU A 1 3006 ? 210.804 200.277 204.811 1.00 26.61 ? 3006 GLU A OE2   1 
ATOM   12338 N  N     . ARG A 1 3007 ? 212.225 200.775 209.321 1.00 4.00  ? 3007 ARG A N     1 
ATOM   12339 C  CA    . ARG A 1 3007 ? 213.500 201.468 209.184 1.00 3.46  ? 3007 ARG A CA    1 
ATOM   12340 C  C     . ARG A 1 3007 ? 214.651 200.617 209.706 1.00 3.59  ? 3007 ARG A C     1 
ATOM   12341 O  O     . ARG A 1 3007 ? 215.713 200.546 209.077 1.00 5.27  ? 3007 ARG A O     1 
ATOM   12342 C  CB    . ARG A 1 3007 ? 213.452 202.806 209.921 1.00 2.81  ? 3007 ARG A CB    1 
ATOM   12343 C  CG    . ARG A 1 3007 ? 212.391 203.770 209.428 1.00 1.85  ? 3007 ARG A CG    1 
ATOM   12344 C  CD    . ARG A 1 3007 ? 212.854 204.503 208.185 1.00 7.31  ? 3007 ARG A CD    1 
ATOM   12345 N  NE    . ARG A 1 3007 ? 212.177 205.783 208.028 1.00 14.00 ? 3007 ARG A NE    1 
ATOM   12346 C  CZ    . ARG A 1 3007 ? 212.351 206.604 207.001 1.00 11.31 ? 3007 ARG A CZ    1 
ATOM   12347 N  NH1   . ARG A 1 3007 ? 213.167 206.303 206.007 1.00 7.42  ? 3007 ARG A NH1   1 
ATOM   12348 N  NH2   . ARG A 1 3007 ? 211.687 207.755 206.972 1.00 16.18 ? 3007 ARG A NH2   1 
ATOM   12349 N  N     . MET A 1 3008 ? 214.461 199.967 210.858 1.00 1.87  ? 3008 MET A N     1 
ATOM   12350 C  CA    . MET A 1 3008 ? 215.519 199.136 211.423 1.00 2.38  ? 3008 MET A CA    1 
ATOM   12351 C  C     . MET A 1 3008 ? 215.769 197.891 210.588 1.00 2.33  ? 3008 MET A C     1 
ATOM   12352 O  O     . MET A 1 3008 ? 216.910 197.424 210.505 1.00 4.47  ? 3008 MET A O     1 
ATOM   12353 C  CB    . MET A 1 3008 ? 215.182 198.750 212.863 1.00 2.68  ? 3008 MET A CB    1 
ATOM   12354 C  CG    . MET A 1 3008 ? 214.829 199.925 213.748 1.00 5.01  ? 3008 MET A CG    1 
ATOM   12355 S  SD    . MET A 1 3008 ? 216.291 200.877 214.202 1.00 22.10 ? 3008 MET A SD    1 
ATOM   12356 C  CE    . MET A 1 3008 ? 217.428 199.566 214.644 1.00 6.55  ? 3008 MET A CE    1 
ATOM   12357 N  N     . ASN A 1 3009 ? 214.726 197.343 209.962 1.00 2.86  ? 3009 ASN A N     1 
ATOM   12358 C  CA    . ASN A 1 3009 ? 214.907 196.172 209.113 1.00 2.15  ? 3009 ASN A CA    1 
ATOM   12359 C  C     . ASN A 1 3009 ? 215.859 196.473 207.962 1.00 1.92  ? 3009 ASN A C     1 
ATOM   12360 O  O     . ASN A 1 3009 ? 216.682 195.630 207.589 1.00 1.97  ? 3009 ASN A O     1 
ATOM   12361 C  CB    . ASN A 1 3009 ? 213.555 195.696 208.583 1.00 2.13  ? 3009 ASN A CB    1 
ATOM   12362 C  CG    . ASN A 1 3009 ? 213.622 194.315 207.975 1.00 3.11  ? 3009 ASN A CG    1 
ATOM   12363 O  OD1   . ASN A 1 3009 ? 213.855 193.329 208.672 1.00 4.27  ? 3009 ASN A OD1   1 
ATOM   12364 N  ND2   . ASN A 1 3009 ? 213.420 194.235 206.667 1.00 1.15  ? 3009 ASN A ND2   1 
ATOM   12365 N  N     . THR A 1 3010 ? 215.758 197.670 207.386 1.00 2.77  ? 3010 THR A N     1 
ATOM   12366 C  CA    . THR A 1 3010 ? 216.697 198.072 206.344 1.00 3.22  ? 3010 THR A CA    1 
ATOM   12367 C  C     . THR A 1 3010 ? 218.074 198.363 206.928 1.00 2.34  ? 3010 THR A C     1 
ATOM   12368 O  O     . THR A 1 3010 ? 219.095 197.984 206.343 1.00 1.68  ? 3010 THR A O     1 
ATOM   12369 C  CB    . THR A 1 3010 ? 216.161 199.294 205.600 1.00 3.99  ? 3010 THR A CB    1 
ATOM   12370 O  OG1   . THR A 1 3010 ? 214.764 199.119 205.340 1.00 11.29 ? 3010 THR A OG1   1 
ATOM   12371 C  CG2   . THR A 1 3010 ? 216.895 199.482 204.286 1.00 2.67  ? 3010 THR A CG2   1 
ATOM   12372 N  N     . LEU A 1 3011 ? 218.117 199.032 208.081 1.00 2.78  ? 3011 LEU A N     1 
ATOM   12373 C  CA    . LEU A 1 3011 ? 219.391 199.415 208.683 1.00 1.54  ? 3011 LEU A CA    1 
ATOM   12374 C  C     . LEU A 1 3011 ? 220.202 198.195 209.103 1.00 1.90  ? 3011 LEU A C     1 
ATOM   12375 O  O     . LEU A 1 3011 ? 221.424 198.164 208.921 1.00 2.03  ? 3011 LEU A O     1 
ATOM   12376 C  CB    . LEU A 1 3011 ? 219.144 200.335 209.877 1.00 1.57  ? 3011 LEU A CB    1 
ATOM   12377 C  CG    . LEU A 1 3011 ? 220.379 200.820 210.640 1.00 1.25  ? 3011 LEU A CG    1 
ATOM   12378 C  CD1   . LEU A 1 3011 ? 221.370 201.480 209.694 1.00 0.98  ? 3011 LEU A CD1   1 
ATOM   12379 C  CD2   . LEU A 1 3011 ? 219.975 201.772 211.749 1.00 0.88  ? 3011 LEU A CD2   1 
ATOM   12380 N  N     . LEU A 1 3012 ? 219.541 197.184 209.672 1.00 1.33  ? 3012 LEU A N     1 
ATOM   12381 C  CA    . LEU A 1 3012 ? 220.253 195.998 210.137 1.00 0.91  ? 3012 LEU A CA    1 
ATOM   12382 C  C     . LEU A 1 3012 ? 220.883 195.237 208.979 1.00 1.37  ? 3012 LEU A C     1 
ATOM   12383 O  O     . LEU A 1 3012 ? 221.983 194.691 209.114 1.00 1.39  ? 3012 LEU A O     1 
ATOM   12384 C  CB    . LEU A 1 3012 ? 219.305 195.088 210.914 1.00 2.15  ? 3012 LEU A CB    1 
ATOM   12385 C  CG    . LEU A 1 3012 ? 218.800 195.572 212.273 1.00 0.94  ? 3012 LEU A CG    1 
ATOM   12386 C  CD1   . LEU A 1 3012 ? 217.606 194.742 212.708 1.00 2.24  ? 3012 LEU A CD1   1 
ATOM   12387 C  CD2   . LEU A 1 3012 ? 219.903 195.521 213.309 1.00 0.25  ? 3012 LEU A CD2   1 
ATOM   12388 N  N     . ALA A 1 3013 ? 220.201 195.182 207.839 1.00 3.23  ? 3013 ALA A N     1 
ATOM   12389 C  CA    . ALA A 1 3013 ? 220.661 194.374 206.717 1.00 2.44  ? 3013 ALA A CA    1 
ATOM   12390 C  C     . ALA A 1 3013 ? 221.641 195.114 205.812 1.00 2.85  ? 3013 ALA A C     1 
ATOM   12391 O  O     . ALA A 1 3013 ? 222.655 194.539 205.406 1.00 6.24  ? 3013 ALA A O     1 
ATOM   12392 C  CB    . ALA A 1 3013 ? 219.463 193.891 205.900 1.00 2.27  ? 3013 ALA A CB    1 
ATOM   12393 N  N     . ASN A 1 3014 ? 221.365 196.376 205.486 1.00 3.71  ? 3014 ASN A N     1 
ATOM   12394 C  CA    . ASN A 1 3014 ? 222.152 197.102 204.502 1.00 5.15  ? 3014 ASN A CA    1 
ATOM   12395 C  C     . ASN A 1 3014 ? 223.014 198.208 205.091 1.00 4.98  ? 3014 ASN A C     1 
ATOM   12396 O  O     . ASN A 1 3014 ? 223.842 198.769 204.366 1.00 6.75  ? 3014 ASN A O     1 
ATOM   12397 C  CB    . ASN A 1 3014 ? 221.235 197.704 203.427 1.00 2.85  ? 3014 ASN A CB    1 
ATOM   12398 C  CG    . ASN A 1 3014 ? 220.329 196.671 202.792 1.00 7.45  ? 3014 ASN A CG    1 
ATOM   12399 O  OD1   . ASN A 1 3014 ? 220.797 195.714 202.177 1.00 8.24  ? 3014 ASN A OD1   1 
ATOM   12400 N  ND2   . ASN A 1 3014 ? 219.021 196.856 202.942 1.00 4.76  ? 3014 ASN A ND2   1 
ATOM   12401 N  N     . GLY A 1 3015 ? 222.848 198.540 206.368 1.00 4.10  ? 3015 GLY A N     1 
ATOM   12402 C  CA    . GLY A 1 3015 ? 223.590 199.647 206.934 1.00 2.08  ? 3015 GLY A CA    1 
ATOM   12403 C  C     . GLY A 1 3015 ? 223.195 200.998 206.391 1.00 2.55  ? 3015 GLY A C     1 
ATOM   12404 O  O     . GLY A 1 3015 ? 223.963 201.954 206.509 1.00 4.85  ? 3015 GLY A O     1 
ATOM   12405 N  N     . GLU A 1 3016 ? 222.013 201.102 205.792 1.00 2.91  ? 3016 GLU A N     1 
ATOM   12406 C  CA    . GLU A 1 3016 ? 221.567 202.335 205.164 1.00 2.78  ? 3016 GLU A CA    1 
ATOM   12407 C  C     . GLU A 1 3016 ? 220.052 202.307 205.066 1.00 3.31  ? 3016 GLU A C     1 
ATOM   12408 O  O     . GLU A 1 3016 ? 219.442 201.237 205.016 1.00 5.45  ? 3016 GLU A O     1 
ATOM   12409 C  CB    . GLU A 1 3016 ? 222.192 202.508 203.774 1.00 5.24  ? 3016 GLU A CB    1 
ATOM   12410 C  CG    . GLU A 1 3016 ? 221.742 201.459 202.775 1.00 8.44  ? 3016 GLU A CG    1 
ATOM   12411 C  CD    . GLU A 1 3016 ? 222.417 201.598 201.428 1.00 15.96 ? 3016 GLU A CD    1 
ATOM   12412 O  OE1   . GLU A 1 3016 ? 223.261 202.505 201.271 1.00 29.21 ? 3016 GLU A OE1   1 
ATOM   12413 O  OE2   . GLU A 1 3016 ? 222.106 200.797 200.524 1.00 19.54 ? 3016 GLU A OE2   1 
ATOM   12414 N  N     . VAL A 1 3017 ? 219.453 203.491 205.056 1.00 3.11  ? 3017 VAL A N     1 
ATOM   12415 C  CA    . VAL A 1 3017 ? 218.021 203.663 204.864 1.00 3.09  ? 3017 VAL A CA    1 
ATOM   12416 C  C     . VAL A 1 3017 ? 217.836 204.559 203.646 1.00 6.82  ? 3017 VAL A C     1 
ATOM   12417 O  O     . VAL A 1 3017 ? 218.198 205.738 203.689 1.00 12.45 ? 3017 VAL A O     1 
ATOM   12418 C  CB    . VAL A 1 3017 ? 217.333 204.268 206.100 1.00 4.87  ? 3017 VAL A CB    1 
ATOM   12419 C  CG1   . VAL A 1 3017 ? 215.829 204.311 205.900 1.00 8.51  ? 3017 VAL A CG1   1 
ATOM   12420 C  CG2   . VAL A 1 3017 ? 217.692 203.476 207.347 1.00 1.22  ? 3017 VAL A CG2   1 
ATOM   12421 N  N     . PRO A 1 3018 ? 217.287 204.047 202.537 1.00 9.88  ? 3018 PRO A N     1 
ATOM   12422 C  CA    . PRO A 1 3018 ? 217.298 204.826 201.284 1.00 8.56  ? 3018 PRO A CA    1 
ATOM   12423 C  C     . PRO A 1 3018 ? 216.638 206.192 201.381 1.00 6.45  ? 3018 PRO A C     1 
ATOM   12424 O  O     . PRO A 1 3018 ? 217.131 207.149 200.775 1.00 8.96  ? 3018 PRO A O     1 
ATOM   12425 C  CB    . PRO A 1 3018 ? 216.558 203.910 200.293 1.00 8.29  ? 3018 PRO A CB    1 
ATOM   12426 C  CG    . PRO A 1 3018 ? 215.925 202.825 201.125 1.00 9.59  ? 3018 PRO A CG    1 
ATOM   12427 C  CD    . PRO A 1 3018 ? 216.767 202.685 202.344 1.00 8.40  ? 3018 PRO A CD    1 
ATOM   12428 N  N     . GLY A 1 3019 ? 215.539 206.318 202.123 1.00 3.39  ? 3019 GLY A N     1 
ATOM   12429 C  CA    . GLY A 1 3019 ? 214.830 207.578 202.216 1.00 6.63  ? 3019 GLY A CA    1 
ATOM   12430 C  C     . GLY A 1 3019 ? 215.017 208.372 203.488 1.00 8.29  ? 3019 GLY A C     1 
ATOM   12431 O  O     . GLY A 1 3019 ? 214.283 209.346 203.702 1.00 11.85 ? 3019 GLY A O     1 
ATOM   12432 N  N     . LEU A 1 3020 ? 215.969 208.005 204.348 1.00 3.44  ? 3020 LEU A N     1 
ATOM   12433 C  CA    . LEU A 1 3020 ? 216.105 208.683 205.633 1.00 3.15  ? 3020 LEU A CA    1 
ATOM   12434 C  C     . LEU A 1 3020 ? 216.661 210.093 205.461 1.00 2.70  ? 3020 LEU A C     1 
ATOM   12435 O  O     . LEU A 1 3020 ? 216.176 211.042 206.086 1.00 3.29  ? 3020 LEU A O     1 
ATOM   12436 C  CB    . LEU A 1 3020 ? 216.993 207.862 206.566 1.00 4.66  ? 3020 LEU A CB    1 
ATOM   12437 C  CG    . LEU A 1 3020 ? 217.020 208.317 208.025 1.00 1.94  ? 3020 LEU A CG    1 
ATOM   12438 C  CD1   . LEU A 1 3020 ? 215.639 208.222 208.648 1.00 2.39  ? 3020 LEU A CD1   1 
ATOM   12439 C  CD2   . LEU A 1 3020 ? 218.016 207.502 208.810 1.00 1.15  ? 3020 LEU A CD2   1 
ATOM   12440 N  N     . PHE A 1 3021 ? 217.677 210.250 204.619 1.00 4.14  ? 3021 PHE A N     1 
ATOM   12441 C  CA    . PHE A 1 3021 ? 218.295 211.545 204.360 1.00 2.37  ? 3021 PHE A CA    1 
ATOM   12442 C  C     . PHE A 1 3021 ? 217.714 212.110 203.069 1.00 3.63  ? 3021 PHE A C     1 
ATOM   12443 O  O     . PHE A 1 3021 ? 217.964 211.577 201.983 1.00 4.33  ? 3021 PHE A O     1 
ATOM   12444 C  CB    . PHE A 1 3021 ? 219.813 211.413 204.267 1.00 1.12  ? 3021 PHE A CB    1 
ATOM   12445 C  CG    . PHE A 1 3021 ? 220.472 211.039 205.563 1.00 1.56  ? 3021 PHE A CG    1 
ATOM   12446 C  CD1   . PHE A 1 3021 ? 220.879 212.017 206.454 1.00 1.24  ? 3021 PHE A CD1   1 
ATOM   12447 C  CD2   . PHE A 1 3021 ? 220.694 209.710 205.885 1.00 1.01  ? 3021 PHE A CD2   1 
ATOM   12448 C  CE1   . PHE A 1 3021 ? 221.490 211.677 207.645 1.00 0.81  ? 3021 PHE A CE1   1 
ATOM   12449 C  CE2   . PHE A 1 3021 ? 221.304 209.364 207.073 1.00 1.04  ? 3021 PHE A CE2   1 
ATOM   12450 C  CZ    . PHE A 1 3021 ? 221.702 210.348 207.954 1.00 0.90  ? 3021 PHE A CZ    1 
ATOM   12451 N  N     . GLU A 1 3022 ? 216.942 213.188 203.185 1.00 4.21  ? 3022 GLU A N     1 
ATOM   12452 C  CA    . GLU A 1 3022 ? 216.312 213.811 202.031 1.00 5.48  ? 3022 GLU A CA    1 
ATOM   12453 C  C     . GLU A 1 3022 ? 216.402 215.324 202.145 1.00 5.43  ? 3022 GLU A C     1 
ATOM   12454 O  O     . GLU A 1 3022 ? 216.426 215.871 203.251 1.00 7.94  ? 3022 GLU A O     1 
ATOM   12455 C  CB    . GLU A 1 3022 ? 214.843 213.390 201.893 1.00 4.39  ? 3022 GLU A CB    1 
ATOM   12456 C  CG    . GLU A 1 3022 ? 214.643 212.028 201.260 1.00 7.22  ? 3022 GLU A CG    1 
ATOM   12457 C  CD    . GLU A 1 3022 ? 213.183 211.639 201.169 1.00 19.34 ? 3022 GLU A CD    1 
ATOM   12458 O  OE1   . GLU A 1 3022 ? 212.876 210.438 201.315 1.00 19.78 ? 3022 GLU A OE1   1 
ATOM   12459 O  OE2   . GLU A 1 3022 ? 212.339 212.533 200.950 1.00 21.30 ? 3022 GLU A OE2   1 
ATOM   12460 N  N     . GLY A 1 3023 ? 216.444 215.990 200.997 1.00 4.63  ? 3023 GLY A N     1 
ATOM   12461 C  CA    . GLY A 1 3023 ? 216.454 217.445 200.991 1.00 2.80  ? 3023 GLY A CA    1 
ATOM   12462 C  C     . GLY A 1 3023 ? 217.726 217.999 201.597 1.00 3.61  ? 3023 GLY A C     1 
ATOM   12463 O  O     . GLY A 1 3023 ? 218.840 217.615 201.224 1.00 6.17  ? 3023 GLY A O     1 
ATOM   12464 N  N     . ASP A 1 3024 ? 217.562 218.927 202.543 1.00 8.16  ? 3024 ASP A N     1 
ATOM   12465 C  CA    . ASP A 1 3024 ? 218.714 219.549 203.186 1.00 4.39  ? 3024 ASP A CA    1 
ATOM   12466 C  C     . ASP A 1 3024 ? 219.487 218.556 204.043 1.00 3.64  ? 3024 ASP A C     1 
ATOM   12467 O  O     . ASP A 1 3024 ? 220.699 218.715 204.227 1.00 5.05  ? 3024 ASP A O     1 
ATOM   12468 C  CB    . ASP A 1 3024 ? 218.264 220.739 204.030 1.00 6.04  ? 3024 ASP A CB    1 
ATOM   12469 C  CG    . ASP A 1 3024 ? 217.867 221.934 203.187 1.00 11.17 ? 3024 ASP A CG    1 
ATOM   12470 O  OD1   . ASP A 1 3024 ? 218.244 221.975 201.998 1.00 20.87 ? 3024 ASP A OD1   1 
ATOM   12471 O  OD2   . ASP A 1 3024 ? 217.175 222.830 203.710 1.00 15.40 ? 3024 ASP A OD2   1 
ATOM   12472 N  N     . GLU A 1 3025 ? 218.809 217.537 204.574 1.00 3.67  ? 3025 GLU A N     1 
ATOM   12473 C  CA    . GLU A 1 3025 ? 219.498 216.526 205.369 1.00 3.97  ? 3025 GLU A CA    1 
ATOM   12474 C  C     . GLU A 1 3025 ? 220.521 215.770 204.531 1.00 4.84  ? 3025 GLU A C     1 
ATOM   12475 O  O     . GLU A 1 3025 ? 221.626 215.479 205.003 1.00 7.58  ? 3025 GLU A O     1 
ATOM   12476 C  CB    . GLU A 1 3025 ? 218.485 215.559 205.982 1.00 3.60  ? 3025 GLU A CB    1 
ATOM   12477 C  CG    . GLU A 1 3025 ? 217.559 216.189 207.012 1.00 4.93  ? 3025 GLU A CG    1 
ATOM   12478 C  CD    . GLU A 1 3025 ? 218.288 216.633 208.264 1.00 15.70 ? 3025 GLU A CD    1 
ATOM   12479 O  OE1   . GLU A 1 3025 ? 219.290 215.989 208.634 1.00 16.10 ? 3025 GLU A OE1   1 
ATOM   12480 O  OE2   . GLU A 1 3025 ? 217.856 217.629 208.880 1.00 22.29 ? 3025 GLU A OE2   1 
ATOM   12481 N  N     . TYR A 1 3026 ? 220.170 215.438 203.286 1.00 2.96  ? 3026 TYR A N     1 
ATOM   12482 C  CA    . TYR A 1 3026 ? 221.124 214.768 202.410 1.00 2.85  ? 3026 TYR A CA    1 
ATOM   12483 C  C     . TYR A 1 3026 ? 222.287 215.683 202.054 1.00 2.96  ? 3026 TYR A C     1 
ATOM   12484 O  O     . TYR A 1 3026 ? 223.438 215.238 201.993 1.00 3.07  ? 3026 TYR A O     1 
ATOM   12485 C  CB    . TYR A 1 3026 ? 220.428 214.267 201.145 1.00 2.99  ? 3026 TYR A CB    1 
ATOM   12486 C  CG    . TYR A 1 3026 ? 221.278 213.318 200.333 1.00 2.66  ? 3026 TYR A CG    1 
ATOM   12487 C  CD1   . TYR A 1 3026 ? 221.355 211.971 200.662 1.00 1.69  ? 3026 TYR A CD1   1 
ATOM   12488 C  CD2   . TYR A 1 3026 ? 222.009 213.768 199.242 1.00 1.36  ? 3026 TYR A CD2   1 
ATOM   12489 C  CE1   . TYR A 1 3026 ? 222.131 211.100 199.927 1.00 3.09  ? 3026 TYR A CE1   1 
ATOM   12490 C  CE2   . TYR A 1 3026 ? 222.788 212.905 198.500 1.00 1.57  ? 3026 TYR A CE2   1 
ATOM   12491 C  CZ    . TYR A 1 3026 ? 222.846 211.571 198.847 1.00 4.42  ? 3026 TYR A CZ    1 
ATOM   12492 O  OH    . TYR A 1 3026 ? 223.619 210.705 198.111 1.00 5.81  ? 3026 TYR A OH    1 
ATOM   12493 N  N     . ALA A 1 3027 ? 222.004 216.963 201.800 1.00 3.29  ? 3027 ALA A N     1 
ATOM   12494 C  CA    . ALA A 1 3027 ? 223.066 217.905 201.466 1.00 3.70  ? 3027 ALA A CA    1 
ATOM   12495 C  C     . ALA A 1 3027 ? 224.037 218.076 202.628 1.00 2.75  ? 3027 ALA A C     1 
ATOM   12496 O  O     . ALA A 1 3027 ? 225.256 218.123 202.427 1.00 2.16  ? 3027 ALA A O     1 
ATOM   12497 C  CB    . ALA A 1 3027 ? 222.467 219.250 201.059 1.00 2.40  ? 3027 ALA A CB    1 
ATOM   12498 N  N     . THR A 1 3028 ? 223.513 218.182 203.851 1.00 3.25  ? 3028 THR A N     1 
ATOM   12499 C  CA    . THR A 1 3028 ? 224.378 218.263 205.023 1.00 4.12  ? 3028 THR A CA    1 
ATOM   12500 C  C     . THR A 1 3028 ? 225.164 216.972 205.213 1.00 5.04  ? 3028 THR A C     1 
ATOM   12501 O  O     . THR A 1 3028 ? 226.347 217.003 205.575 1.00 4.77  ? 3028 THR A O     1 
ATOM   12502 C  CB    . THR A 1 3028 ? 223.545 218.583 206.266 1.00 5.72  ? 3028 THR A CB    1 
ATOM   12503 O  OG1   . THR A 1 3028 ? 222.880 219.837 206.085 1.00 9.59  ? 3028 THR A OG1   1 
ATOM   12504 C  CG2   . THR A 1 3028 ? 224.424 218.664 207.499 1.00 6.72  ? 3028 THR A CG2   1 
ATOM   12505 N  N     . LEU A 1 3029 ? 224.526 215.827 204.962 1.00 2.70  ? 3029 LEU A N     1 
ATOM   12506 C  CA    . LEU A 1 3029 ? 225.216 214.547 205.075 1.00 2.32  ? 3029 LEU A CA    1 
ATOM   12507 C  C     . LEU A 1 3029 ? 226.385 214.459 204.103 1.00 2.93  ? 3029 LEU A C     1 
ATOM   12508 O  O     . LEU A 1 3029 ? 227.461 213.966 204.461 1.00 6.79  ? 3029 LEU A O     1 
ATOM   12509 C  CB    . LEU A 1 3029 ? 224.236 213.399 204.836 1.00 3.57  ? 3029 LEU A CB    1 
ATOM   12510 C  CG    . LEU A 1 3029 ? 224.824 211.987 204.877 1.00 1.93  ? 3029 LEU A CG    1 
ATOM   12511 C  CD1   . LEU A 1 3029 ? 225.331 211.663 206.267 1.00 1.43  ? 3029 LEU A CD1   1 
ATOM   12512 C  CD2   . LEU A 1 3029 ? 223.803 210.958 204.422 1.00 1.12  ? 3029 LEU A CD2   1 
ATOM   12513 N  N     . MET A 1 3030 ? 226.196 214.934 202.871 1.00 3.38  ? 3030 MET A N     1 
ATOM   12514 C  CA    . MET A 1 3030 ? 227.274 214.897 201.890 1.00 2.92  ? 3030 MET A CA    1 
ATOM   12515 C  C     . MET A 1 3030 ? 228.448 215.770 202.310 1.00 3.62  ? 3030 MET A C     1 
ATOM   12516 O  O     . MET A 1 3030 ? 229.606 215.396 202.096 1.00 7.34  ? 3030 MET A O     1 
ATOM   12517 C  CB    . MET A 1 3030 ? 226.755 215.324 200.518 1.00 2.81  ? 3030 MET A CB    1 
ATOM   12518 C  CG    . MET A 1 3030 ? 225.773 214.354 199.859 1.00 3.98  ? 3030 MET A CG    1 
ATOM   12519 S  SD    . MET A 1 3030 ? 226.449 212.757 199.341 1.00 15.31 ? 3030 MET A SD    1 
ATOM   12520 C  CE    . MET A 1 3030 ? 226.347 211.763 200.829 1.00 2.16  ? 3030 MET A CE    1 
ATOM   12521 N  N     . THR A 1 3031 ? 228.173 216.935 202.897 1.00 2.94  ? 3031 THR A N     1 
ATOM   12522 C  CA    . THR A 1 3031 ? 229.246 217.781 203.409 1.00 3.51  ? 3031 THR A CA    1 
ATOM   12523 C  C     . THR A 1 3031 ? 230.013 217.081 204.524 1.00 6.20  ? 3031 THR A C     1 
ATOM   12524 O  O     . THR A 1 3031 ? 231.246 217.137 204.569 1.00 7.51  ? 3031 THR A O     1 
ATOM   12525 C  CB    . THR A 1 3031 ? 228.674 219.108 203.907 1.00 5.53  ? 3031 THR A CB    1 
ATOM   12526 O  OG1   . THR A 1 3031 ? 227.950 219.745 202.848 1.00 5.82  ? 3031 THR A OG1   1 
ATOM   12527 C  CG2   . THR A 1 3031 ? 229.787 220.028 204.382 1.00 4.00  ? 3031 THR A CG2   1 
ATOM   12528 N  N     . GLN A 1 3032 ? 229.297 216.416 205.430 1.00 5.03  ? 3032 GLN A N     1 
ATOM   12529 C  CA    . GLN A 1 3032 ? 229.952 215.745 206.548 1.00 3.62  ? 3032 GLN A CA    1 
ATOM   12530 C  C     . GLN A 1 3032 ? 230.707 214.505 206.085 1.00 5.48  ? 3032 GLN A C     1 
ATOM   12531 O  O     . GLN A 1 3032 ? 231.781 214.194 206.612 1.00 6.07  ? 3032 GLN A O     1 
ATOM   12532 C  CB    . GLN A 1 3032 ? 228.913 215.391 207.610 1.00 5.29  ? 3032 GLN A CB    1 
ATOM   12533 C  CG    . GLN A 1 3032 ? 228.301 216.612 208.268 1.00 4.70  ? 3032 GLN A CG    1 
ATOM   12534 C  CD    . GLN A 1 3032 ? 227.248 216.264 209.299 1.00 7.48  ? 3032 GLN A CD    1 
ATOM   12535 O  OE1   . GLN A 1 3032 ? 226.909 215.098 209.491 1.00 11.01 ? 3032 GLN A OE1   1 
ATOM   12536 N  NE2   . GLN A 1 3032 ? 226.722 217.281 209.966 1.00 12.81 ? 3032 GLN A NE2   1 
ATOM   12537 N  N     . CYS A 1 3033 ? 230.160 213.782 205.105 1.00 6.16  ? 3033 CYS A N     1 
ATOM   12538 C  CA    . CYS A 1 3033 ? 230.854 212.612 204.575 1.00 4.22  ? 3033 CYS A CA    1 
ATOM   12539 C  C     . CYS A 1 3033 ? 232.145 213.006 203.873 1.00 5.17  ? 3033 CYS A C     1 
ATOM   12540 O  O     . CYS A 1 3033 ? 233.160 212.310 203.987 1.00 6.13  ? 3033 CYS A O     1 
ATOM   12541 C  CB    . CYS A 1 3033 ? 229.937 211.841 203.625 1.00 4.37  ? 3033 CYS A CB    1 
ATOM   12542 S  SG    . CYS A 1 3033 ? 228.552 211.023 204.433 1.00 17.02 ? 3033 CYS A SG    1 
ATOM   12543 N  N     . LYS A 1 3034 ? 232.124 214.114 203.127 1.00 5.74  ? 3034 LYS A N     1 
ATOM   12544 C  CA    . LYS A 1 3034 ? 233.342 214.591 202.482 1.00 5.93  ? 3034 LYS A CA    1 
ATOM   12545 C  C     . LYS A 1 3034 ? 234.391 214.977 203.516 1.00 7.33  ? 3034 LYS A C     1 
ATOM   12546 O  O     . LYS A 1 3034 ? 235.578 214.668 203.354 1.00 7.27  ? 3034 LYS A O     1 
ATOM   12547 C  CB    . LYS A 1 3034 ? 233.023 215.770 201.565 1.00 9.36  ? 3034 LYS A CB    1 
ATOM   12548 C  CG    . LYS A 1 3034 ? 234.220 216.297 200.800 1.00 8.39  ? 3034 LYS A CG    1 
ATOM   12549 C  CD    . LYS A 1 3034 ? 233.817 217.391 199.832 1.00 9.94  ? 3034 LYS A CD    1 
ATOM   12550 C  CE    . LYS A 1 3034 ? 235.035 218.019 199.176 1.00 19.05 ? 3034 LYS A CE    1 
ATOM   12551 N  NZ    . LYS A 1 3034 ? 235.745 217.049 198.297 1.00 21.67 ? 3034 LYS A NZ    1 
ATOM   12552 N  N     . GLU A 1 3035 ? 233.973 215.653 204.588 1.00 6.24  ? 3035 GLU A N     1 
ATOM   12553 C  CA    . GLU A 1 3035 ? 234.888 215.952 205.685 1.00 6.59  ? 3035 GLU A CA    1 
ATOM   12554 C  C     . GLU A 1 3035 ? 235.359 214.680 206.379 1.00 8.72  ? 3035 GLU A C     1 
ATOM   12555 O  O     . GLU A 1 3035 ? 236.541 214.553 206.719 1.00 11.20 ? 3035 GLU A O     1 
ATOM   12556 C  CB    . GLU A 1 3035 ? 234.215 216.889 206.689 1.00 5.76  ? 3035 GLU A CB    1 
ATOM   12557 C  CG    . GLU A 1 3035 ? 235.117 217.321 207.832 1.00 10.25 ? 3035 GLU A CG    1 
ATOM   12558 C  CD    . GLU A 1 3035 ? 234.440 218.289 208.781 1.00 24.45 ? 3035 GLU A CD    1 
ATOM   12559 O  OE1   . GLU A 1 3035 ? 233.254 218.609 208.559 1.00 28.48 ? 3035 GLU A OE1   1 
ATOM   12560 O  OE2   . GLU A 1 3035 ? 235.094 218.729 209.748 1.00 27.51 ? 3035 GLU A OE2   1 
ATOM   12561 N  N     . GLY A 1 3036 ? 234.448 213.733 206.606 1.00 7.47  ? 3036 GLY A N     1 
ATOM   12562 C  CA    . GLY A 1 3036 ? 234.822 212.511 207.297 1.00 5.94  ? 3036 GLY A CA    1 
ATOM   12563 C  C     . GLY A 1 3036 ? 235.778 211.646 206.499 1.00 7.19  ? 3036 GLY A C     1 
ATOM   12564 O  O     . GLY A 1 3036 ? 236.727 211.083 207.050 1.00 13.83 ? 3036 GLY A O     1 
ATOM   12565 N  N     . ALA A 1 3037 ? 235.538 211.521 205.193 1.00 5.92  ? 3037 ALA A N     1 
ATOM   12566 C  CA    . ALA A 1 3037 ? 236.419 210.714 204.357 1.00 5.74  ? 3037 ALA A CA    1 
ATOM   12567 C  C     . ALA A 1 3037 ? 237.790 211.359 204.197 1.00 13.48 ? 3037 ALA A C     1 
ATOM   12568 O  O     . ALA A 1 3037 ? 238.789 210.650 204.034 1.00 17.40 ? 3037 ALA A O     1 
ATOM   12569 C  CB    . ALA A 1 3037 ? 235.775 210.476 202.992 1.00 5.90  ? 3037 ALA A CB    1 
ATOM   12570 N  N     . GLN A 1 3038 ? 237.857 212.692 204.234 1.00 14.70 ? 3038 GLN A N     1 
ATOM   12571 C  CA    . GLN A 1 3038 ? 239.144 213.376 204.147 1.00 16.40 ? 3038 GLN A CA    1 
ATOM   12572 C  C     . GLN A 1 3038 ? 240.035 213.034 205.336 1.00 17.77 ? 3038 GLN A C     1 
ATOM   12573 O  O     . GLN A 1 3038 ? 241.241 212.818 205.173 1.00 18.09 ? 3038 GLN A O     1 
ATOM   12574 C  CB    . GLN A 1 3038 ? 238.930 214.886 204.054 1.00 15.46 ? 3038 GLN A CB    1 
ATOM   12575 C  CG    . GLN A 1 3038 ? 240.207 215.687 203.890 1.00 22.91 ? 3038 GLN A CG    1 
ATOM   12576 C  CD    . GLN A 1 3038 ? 240.947 215.352 202.613 1.00 28.61 ? 3038 GLN A CD    1 
ATOM   12577 O  OE1   . GLN A 1 3038 ? 241.966 214.663 202.636 1.00 27.50 ? 3038 GLN A OE1   1 
ATOM   12578 N  NE2   . GLN A 1 3038 ? 240.435 215.839 201.489 1.00 26.02 ? 3038 GLN A NE2   1 
ATOM   12579 N  N     . LYS A 1 3039 ? 239.456 212.974 206.537 1.00 15.60 ? 3039 LYS A N     1 
ATOM   12580 C  CA    . LYS A 1 3039 ? 240.223 212.613 207.722 1.00 14.70 ? 3039 LYS A CA    1 
ATOM   12581 C  C     . LYS A 1 3039 ? 240.750 211.186 207.656 1.00 21.81 ? 3039 LYS A C     1 
ATOM   12582 O  O     . LYS A 1 3039 ? 241.678 210.845 208.399 1.00 24.63 ? 3039 LYS A O     1 
ATOM   12583 C  CB    . LYS A 1 3039 ? 239.363 212.796 208.973 1.00 10.35 ? 3039 LYS A CB    1 
ATOM   12584 C  CG    . LYS A 1 3039 ? 239.215 214.244 209.410 1.00 17.12 ? 3039 LYS A CG    1 
ATOM   12585 C  CD    . LYS A 1 3039 ? 238.057 214.431 210.381 1.00 17.28 ? 3039 LYS A CD    1 
ATOM   12586 C  CE    . LYS A 1 3039 ? 238.005 213.326 211.426 1.00 18.39 ? 3039 LYS A CE    1 
ATOM   12587 N  NZ    . LYS A 1 3039 ? 239.236 213.281 212.262 1.00 20.14 ? 3039 LYS A NZ    1 
ATOM   12588 N  N     . GLU A 1 3040 ? 240.177 210.350 206.795 1.00 21.53 ? 3040 GLU A N     1 
ATOM   12589 C  CA    . GLU A 1 3040 ? 240.622 208.978 206.602 1.00 18.29 ? 3040 GLU A CA    1 
ATOM   12590 C  C     . GLU A 1 3040 ? 241.628 208.847 205.465 1.00 22.70 ? 3040 GLU A C     1 
ATOM   12591 O  O     . GLU A 1 3040 ? 242.167 207.756 205.250 1.00 28.77 ? 3040 GLU A O     1 
ATOM   12592 C  CB    . GLU A 1 3040 ? 239.408 208.077 206.345 1.00 17.58 ? 3040 GLU A CB    1 
ATOM   12593 C  CG    . GLU A 1 3040 ? 239.638 206.594 206.581 1.00 20.10 ? 3040 GLU A CG    1 
ATOM   12594 C  CD    . GLU A 1 3040 ? 238.337 205.821 206.701 1.00 21.45 ? 3040 GLU A CD    1 
ATOM   12595 O  OE1   . GLU A 1 3040 ? 238.016 205.042 205.778 1.00 12.20 ? 3040 GLU A OE1   1 
ATOM   12596 O  OE2   . GLU A 1 3040 ? 237.634 205.999 207.717 1.00 18.60 ? 3040 GLU A OE2   1 
ATOM   12597 N  N     . GLY A 1 3041 ? 241.900 209.930 204.741 1.00 19.72 ? 3041 GLY A N     1 
ATOM   12598 C  CA    . GLY A 1 3041 ? 242.848 209.900 203.648 1.00 18.53 ? 3041 GLY A CA    1 
ATOM   12599 C  C     . GLY A 1 3041 ? 242.305 209.408 202.326 1.00 21.98 ? 3041 GLY A C     1 
ATOM   12600 O  O     . GLY A 1 3041 ? 243.093 209.151 201.410 1.00 29.32 ? 3041 GLY A O     1 
ATOM   12601 N  N     . LEU A 1 3042 ? 240.990 209.267 202.192 1.00 21.94 ? 3042 LEU A N     1 
ATOM   12602 C  CA    . LEU A 1 3042 ? 240.392 208.795 200.952 1.00 23.17 ? 3042 LEU A CA    1 
ATOM   12603 C  C     . LEU A 1 3042 ? 240.067 209.966 200.038 1.00 27.34 ? 3042 LEU A C     1 
ATOM   12604 O  O     . LEU A 1 3042 ? 239.664 211.038 200.498 1.00 27.83 ? 3042 LEU A O     1 
ATOM   12605 C  CB    . LEU A 1 3042 ? 239.127 207.983 201.231 1.00 14.56 ? 3042 LEU A CB    1 
ATOM   12606 C  CG    . LEU A 1 3042 ? 239.243 206.896 202.298 1.00 17.17 ? 3042 LEU A CG    1 
ATOM   12607 C  CD1   . LEU A 1 3042 ? 237.973 206.065 202.343 1.00 23.93 ? 3042 LEU A CD1   1 
ATOM   12608 C  CD2   . LEU A 1 3042 ? 240.451 206.014 202.038 1.00 17.91 ? 3042 LEU A CD2   1 
ATOM   12609 N  N     . MET A 1 3043 ? 240.248 209.754 198.735 1.00 24.05 ? 3043 MET A N     1 
ATOM   12610 C  CA    . MET A 1 3043 ? 239.967 210.776 197.728 1.00 23.20 ? 3043 MET A CA    1 
ATOM   12611 C  C     . MET A 1 3043 ? 238.567 210.530 197.181 1.00 24.34 ? 3043 MET A C     1 
ATOM   12612 O  O     . MET A 1 3043 ? 238.369 209.765 196.238 1.00 28.59 ? 3043 MET A O     1 
ATOM   12613 C  CB    . MET A 1 3043 ? 241.019 210.745 196.628 1.00 25.87 ? 3043 MET A CB    1 
ATOM   12614 C  CG    . MET A 1 3043 ? 242.410 211.148 197.092 1.00 28.08 ? 3043 MET A CG    1 
ATOM   12615 S  SD    . MET A 1 3043 ? 243.616 211.163 195.753 1.00 57.69 ? 3043 MET A SD    1 
ATOM   12616 C  CE    . MET A 1 3043 ? 243.864 209.408 195.503 1.00 32.14 ? 3043 MET A CE    1 
ATOM   12617 N  N     . LEU A 1 3044 ? 237.579 211.189 197.783 1.00 18.45 ? 3044 LEU A N     1 
ATOM   12618 C  CA    . LEU A 1 3044 ? 236.183 211.030 197.395 1.00 14.78 ? 3044 LEU A CA    1 
ATOM   12619 C  C     . LEU A 1 3044 ? 235.545 212.399 197.209 1.00 15.77 ? 3044 LEU A C     1 
ATOM   12620 O  O     . LEU A 1 3044 ? 235.653 213.262 198.085 1.00 13.46 ? 3044 LEU A O     1 
ATOM   12621 C  CB    . LEU A 1 3044 ? 235.405 210.228 198.440 1.00 12.26 ? 3044 LEU A CB    1 
ATOM   12622 C  CG    . LEU A 1 3044 ? 235.834 208.778 198.658 1.00 13.32 ? 3044 LEU A CG    1 
ATOM   12623 C  CD1   . LEU A 1 3044 ? 235.016 208.146 199.769 1.00 11.04 ? 3044 LEU A CD1   1 
ATOM   12624 C  CD2   . LEU A 1 3044 ? 235.708 207.977 197.374 1.00 10.54 ? 3044 LEU A CD2   1 
ATOM   12625 N  N     . ASP A 1 3045 ? 234.885 212.592 196.069 1.00 19.20 ? 3045 ASP A N     1 
ATOM   12626 C  CA    . ASP A 1 3045 ? 234.186 213.841 195.797 1.00 20.49 ? 3045 ASP A CA    1 
ATOM   12627 C  C     . ASP A 1 3045 ? 232.774 213.576 195.290 1.00 17.37 ? 3045 ASP A C     1 
ATOM   12628 O  O     . ASP A 1 3045 ? 231.872 214.397 195.489 1.00 23.35 ? 3045 ASP A O     1 
ATOM   12629 C  CB    . ASP A 1 3045 ? 234.966 214.679 194.782 1.00 25.38 ? 3045 ASP A CB    1 
ATOM   12630 C  CG    . ASP A 1 3045 ? 234.308 216.014 194.502 1.00 33.09 ? 3045 ASP A CG    1 
ATOM   12631 O  OD1   . ASP A 1 3045 ? 234.168 216.818 195.447 1.00 23.80 ? 3045 ASP A OD1   1 
ATOM   12632 O  OD2   . ASP A 1 3045 ? 233.926 216.256 193.338 1.00 36.01 ? 3045 ASP A OD2   1 
ATOM   12633 N  N     . SER A 1 3046 ? 232.574 212.433 194.639 1.00 14.58 ? 3046 SER A N     1 
ATOM   12634 C  CA    . SER A 1 3046 ? 231.260 212.082 194.120 1.00 7.63  ? 3046 SER A CA    1 
ATOM   12635 C  C     . SER A 1 3046 ? 230.294 211.783 195.258 1.00 10.95 ? 3046 SER A C     1 
ATOM   12636 O  O     . SER A 1 3046 ? 230.660 211.164 196.258 1.00 13.78 ? 3046 SER A O     1 
ATOM   12637 C  CB    . SER A 1 3046 ? 231.367 210.875 193.189 1.00 8.85  ? 3046 SER A CB    1 
ATOM   12638 O  OG    . SER A 1 3046 ? 230.092 210.327 192.910 1.00 13.00 ? 3046 SER A OG    1 
ATOM   12639 N  N     . HIS A 1 3047 ? 229.046 212.232 195.100 1.00 11.77 ? 3047 HIS A N     1 
ATOM   12640 C  CA    . HIS A 1 3047 ? 228.032 211.965 196.115 1.00 7.48  ? 3047 HIS A CA    1 
ATOM   12641 C  C     . HIS A 1 3047 ? 227.770 210.471 196.255 1.00 8.45  ? 3047 HIS A C     1 
ATOM   12642 O  O     . HIS A 1 3047 ? 227.608 209.964 197.370 1.00 13.17 ? 3047 HIS A O     1 
ATOM   12643 C  CB    . HIS A 1 3047 ? 226.739 212.706 195.781 1.00 4.57  ? 3047 HIS A CB    1 
ATOM   12644 C  CG    . HIS A 1 3047 ? 226.744 214.144 196.193 1.00 10.36 ? 3047 HIS A CG    1 
ATOM   12645 N  ND1   . HIS A 1 3047 ? 225.611 214.928 196.166 1.00 10.48 ? 3047 HIS A ND1   1 
ATOM   12646 C  CD2   . HIS A 1 3047 ? 227.743 214.942 196.638 1.00 10.91 ? 3047 HIS A CD2   1 
ATOM   12647 C  CE1   . HIS A 1 3047 ? 225.912 216.146 196.579 1.00 9.99  ? 3047 HIS A CE1   1 
ATOM   12648 N  NE2   . HIS A 1 3047 ? 227.200 216.181 196.872 1.00 10.21 ? 3047 HIS A NE2   1 
ATOM   12649 N  N     . GLU A 1 3048 ? 227.713 209.753 195.131 1.00 10.08 ? 3048 GLU A N     1 
ATOM   12650 C  CA    . GLU A 1 3048 ? 227.526 208.307 195.185 1.00 5.58  ? 3048 GLU A CA    1 
ATOM   12651 C  C     . GLU A 1 3048 ? 228.695 207.630 195.887 1.00 6.52  ? 3048 GLU A C     1 
ATOM   12652 O  O     . GLU A 1 3048 ? 228.498 206.724 196.705 1.00 7.01  ? 3048 GLU A O     1 
ATOM   12653 C  CB    . GLU A 1 3048 ? 227.348 207.745 193.773 1.00 6.41  ? 3048 GLU A CB    1 
ATOM   12654 C  CG    . GLU A 1 3048 ? 225.999 208.030 193.120 1.00 14.98 ? 3048 GLU A CG    1 
ATOM   12655 C  CD    . GLU A 1 3048 ? 225.717 209.511 192.930 1.00 19.88 ? 3048 GLU A CD    1 
ATOM   12656 O  OE1   . GLU A 1 3048 ? 226.369 210.142 192.073 1.00 19.68 ? 3048 GLU A OE1   1 
ATOM   12657 O  OE2   . GLU A 1 3048 ? 224.832 210.040 193.637 1.00 15.38 ? 3048 GLU A OE2   1 
ATOM   12658 N  N     . GLU A 1 3049 ? 229.921 208.058 195.579 1.00 7.57  ? 3049 GLU A N     1 
ATOM   12659 C  CA    . GLU A 1 3049 ? 231.090 207.509 196.256 1.00 5.57  ? 3049 GLU A CA    1 
ATOM   12660 C  C     . GLU A 1 3049 ? 231.080 207.848 197.740 1.00 6.09  ? 3049 GLU A C     1 
ATOM   12661 O  O     . GLU A 1 3049 ? 231.463 207.021 198.576 1.00 7.23  ? 3049 GLU A O     1 
ATOM   12662 C  CB    . GLU A 1 3049 ? 232.367 208.025 195.598 1.00 7.38  ? 3049 GLU A CB    1 
ATOM   12663 C  CG    . GLU A 1 3049 ? 232.860 207.171 194.451 1.00 10.88 ? 3049 GLU A CG    1 
ATOM   12664 C  CD    . GLU A 1 3049 ? 233.867 207.896 193.584 1.00 21.87 ? 3049 GLU A CD    1 
ATOM   12665 O  OE1   . GLU A 1 3049 ? 233.668 207.945 192.352 1.00 22.15 ? 3049 GLU A OE1   1 
ATOM   12666 O  OE2   . GLU A 1 3049 ? 234.858 208.417 194.138 1.00 23.07 ? 3049 GLU A OE2   1 
ATOM   12667 N  N     . LEU A 1 3050 ? 230.655 209.065 198.085 1.00 7.10  ? 3050 LEU A N     1 
ATOM   12668 C  CA    . LEU A 1 3050 ? 230.561 209.448 199.489 1.00 4.02  ? 3050 LEU A CA    1 
ATOM   12669 C  C     . LEU A 1 3050 ? 229.524 208.612 200.225 1.00 2.64  ? 3050 LEU A C     1 
ATOM   12670 O  O     . LEU A 1 3050 ? 229.742 208.209 201.372 1.00 3.51  ? 3050 LEU A O     1 
ATOM   12671 C  CB    . LEU A 1 3050 ? 230.231 210.936 199.607 1.00 6.02  ? 3050 LEU A CB    1 
ATOM   12672 C  CG    . LEU A 1 3050 ? 231.366 211.918 199.318 1.00 9.19  ? 3050 LEU A CG    1 
ATOM   12673 C  CD1   . LEU A 1 3050 ? 230.859 213.346 199.392 1.00 8.33  ? 3050 LEU A CD1   1 
ATOM   12674 C  CD2   . LEU A 1 3050 ? 232.521 211.705 200.278 1.00 7.14  ? 3050 LEU A CD2   1 
ATOM   12675 N  N     . TYR A 1 3051 ? 228.386 208.342 199.581 1.00 2.77  ? 3051 TYR A N     1 
ATOM   12676 C  CA    . TYR A 1 3051 ? 227.326 207.587 200.241 1.00 1.46  ? 3051 TYR A CA    1 
ATOM   12677 C  C     . TYR A 1 3051 ? 227.731 206.133 200.461 1.00 2.46  ? 3051 TYR A C     1 
ATOM   12678 O  O     . TYR A 1 3051 ? 227.370 205.535 201.481 1.00 2.71  ? 3051 TYR A O     1 
ATOM   12679 C  CB    . TYR A 1 3051 ? 226.034 207.676 199.429 1.00 1.34  ? 3051 TYR A CB    1 
ATOM   12680 C  CG    . TYR A 1 3051 ? 224.810 207.237 200.199 1.00 3.02  ? 3051 TYR A CG    1 
ATOM   12681 C  CD1   . TYR A 1 3051 ? 224.158 208.110 201.058 1.00 3.33  ? 3051 TYR A CD1   1 
ATOM   12682 C  CD2   . TYR A 1 3051 ? 224.310 205.948 200.071 1.00 4.53  ? 3051 TYR A CD2   1 
ATOM   12683 C  CE1   . TYR A 1 3051 ? 223.043 207.712 201.770 1.00 3.53  ? 3051 TYR A CE1   1 
ATOM   12684 C  CE2   . TYR A 1 3051 ? 223.196 205.543 200.776 1.00 3.98  ? 3051 TYR A CE2   1 
ATOM   12685 C  CZ    . TYR A 1 3051 ? 222.567 206.427 201.623 1.00 5.03  ? 3051 TYR A CZ    1 
ATOM   12686 O  OH    . TYR A 1 3051 ? 221.455 206.025 202.325 1.00 11.76 ? 3051 TYR A OH    1 
ATOM   12687 N  N     . LYS A 1 3052 ? 228.467 205.544 199.516 1.00 2.85  ? 3052 LYS A N     1 
ATOM   12688 C  CA    . LYS A 1 3052 ? 228.958 204.181 199.710 1.00 1.60  ? 3052 LYS A CA    1 
ATOM   12689 C  C     . LYS A 1 3052 ? 229.940 204.106 200.873 1.00 1.85  ? 3052 LYS A C     1 
ATOM   12690 O  O     . LYS A 1 3052 ? 229.895 203.162 201.671 1.00 2.35  ? 3052 LYS A O     1 
ATOM   12691 C  CB    . LYS A 1 3052 ? 229.609 203.659 198.430 1.00 3.43  ? 3052 LYS A CB    1 
ATOM   12692 C  CG    . LYS A 1 3052 ? 228.655 203.471 197.268 1.00 3.81  ? 3052 LYS A CG    1 
ATOM   12693 C  CD    . LYS A 1 3052 ? 229.379 202.937 196.044 1.00 6.27  ? 3052 LYS A CD    1 
ATOM   12694 C  CE    . LYS A 1 3052 ? 228.414 202.659 194.903 1.00 15.88 ? 3052 LYS A CE    1 
ATOM   12695 N  NZ    . LYS A 1 3052 ? 227.798 203.904 194.369 1.00 19.39 ? 3052 LYS A NZ    1 
ATOM   12696 N  N     . TRP A 1 3053 ? 230.841 205.084 200.979 1.00 1.97  ? 3053 TRP A N     1 
ATOM   12697 C  CA    . TRP A 1 3053 ? 231.764 205.117 202.109 1.00 0.93  ? 3053 TRP A CA    1 
ATOM   12698 C  C     . TRP A 1 3053 ? 231.013 205.314 203.418 1.00 1.28  ? 3053 TRP A C     1 
ATOM   12699 O  O     . TRP A 1 3053 ? 231.358 204.709 204.439 1.00 1.13  ? 3053 TRP A O     1 
ATOM   12700 C  CB    . TRP A 1 3053 ? 232.798 206.224 201.908 1.00 0.94  ? 3053 TRP A CB    1 
ATOM   12701 C  CG    . TRP A 1 3053 ? 233.624 206.504 203.124 1.00 1.43  ? 3053 TRP A CG    1 
ATOM   12702 C  CD1   . TRP A 1 3053 ? 234.767 205.868 203.498 1.00 1.27  ? 3053 TRP A CD1   1 
ATOM   12703 C  CD2   . TRP A 1 3053 ? 233.367 207.491 204.130 1.00 1.37  ? 3053 TRP A CD2   1 
ATOM   12704 N  NE1   . TRP A 1 3053 ? 235.242 206.397 204.670 1.00 2.93  ? 3053 TRP A NE1   1 
ATOM   12705 C  CE2   . TRP A 1 3053 ? 234.400 207.396 205.081 1.00 1.74  ? 3053 TRP A CE2   1 
ATOM   12706 C  CE3   . TRP A 1 3053 ? 232.363 208.445 204.318 1.00 1.34  ? 3053 TRP A CE3   1 
ATOM   12707 C  CZ2   . TRP A 1 3053 ? 234.459 208.217 206.202 1.00 1.70  ? 3053 TRP A CZ2   1 
ATOM   12708 C  CZ3   . TRP A 1 3053 ? 232.424 209.258 205.431 1.00 2.37  ? 3053 TRP A CZ3   1 
ATOM   12709 C  CH2   . TRP A 1 3053 ? 233.464 209.139 206.359 1.00 2.62  ? 3053 TRP A CH2   1 
ATOM   12710 N  N     . PHE A 1 3054 ? 229.983 206.160 203.401 1.00 0.90  ? 3054 PHE A N     1 
ATOM   12711 C  CA    . PHE A 1 3054 ? 229.156 206.372 204.585 1.00 0.88  ? 3054 PHE A CA    1 
ATOM   12712 C  C     . PHE A 1 3054 ? 228.443 205.090 204.999 1.00 0.79  ? 3054 PHE A C     1 
ATOM   12713 O  O     . PHE A 1 3054 ? 228.335 204.789 206.194 1.00 0.85  ? 3054 PHE A O     1 
ATOM   12714 C  CB    . PHE A 1 3054 ? 228.162 207.501 204.305 1.00 0.57  ? 3054 PHE A CB    1 
ATOM   12715 C  CG    . PHE A 1 3054 ? 227.069 207.633 205.322 1.00 0.38  ? 3054 PHE A CG    1 
ATOM   12716 C  CD1   . PHE A 1 3054 ? 227.297 208.278 206.524 1.00 0.75  ? 3054 PHE A CD1   1 
ATOM   12717 C  CD2   . PHE A 1 3054 ? 225.796 207.162 205.051 1.00 0.65  ? 3054 PHE A CD2   1 
ATOM   12718 C  CE1   . PHE A 1 3054 ? 226.287 208.416 207.452 1.00 0.40  ? 3054 PHE A CE1   1 
ATOM   12719 C  CE2   . PHE A 1 3054 ? 224.780 207.301 205.976 1.00 0.54  ? 3054 PHE A CE2   1 
ATOM   12720 C  CZ    . PHE A 1 3054 ? 225.027 207.929 207.178 1.00 0.39  ? 3054 PHE A CZ    1 
ATOM   12721 N  N     . THR A 1 3055 ? 227.949 204.323 204.028 1.00 0.69  ? 3055 THR A N     1 
ATOM   12722 C  CA    . THR A 1 3055 ? 227.334 203.036 204.336 1.00 0.96  ? 3055 THR A CA    1 
ATOM   12723 C  C     . THR A 1 3055 ? 228.352 202.065 204.921 1.00 0.79  ? 3055 THR A C     1 
ATOM   12724 O  O     . THR A 1 3055 ? 228.052 201.336 205.874 1.00 0.80  ? 3055 THR A O     1 
ATOM   12725 C  CB    . THR A 1 3055 ? 226.694 202.448 203.078 1.00 1.78  ? 3055 THR A CB    1 
ATOM   12726 O  OG1   . THR A 1 3055 ? 225.737 203.375 202.552 1.00 4.51  ? 3055 THR A OG1   1 
ATOM   12727 C  CG2   . THR A 1 3055 ? 225.999 201.135 203.392 1.00 1.59  ? 3055 THR A CG2   1 
ATOM   12728 N  N     . SER A 1 3056 ? 229.564 202.043 204.365 1.00 0.78  ? 3056 SER A N     1 
ATOM   12729 C  CA    . SER A 1 3056 ? 230.590 201.131 204.858 1.00 0.90  ? 3056 SER A CA    1 
ATOM   12730 C  C     . SER A 1 3056 ? 231.007 201.483 206.281 1.00 0.69  ? 3056 SER A C     1 
ATOM   12731 O  O     . SER A 1 3056 ? 231.372 200.600 207.065 1.00 0.62  ? 3056 SER A O     1 
ATOM   12732 C  CB    . SER A 1 3056 ? 231.795 201.142 203.916 1.00 0.93  ? 3056 SER A CB    1 
ATOM   12733 O  OG    . SER A 1 3056 ? 232.424 202.410 203.897 1.00 1.62  ? 3056 SER A OG    1 
ATOM   12734 N  N     . GLN A 1 3057 ? 230.972 202.771 206.628 1.00 0.75  ? 3057 GLN A N     1 
ATOM   12735 C  CA    . GLN A 1 3057 ? 231.283 203.176 207.996 1.00 0.68  ? 3057 GLN A CA    1 
ATOM   12736 C  C     . GLN A 1 3057 ? 230.185 202.754 208.963 1.00 0.62  ? 3057 GLN A C     1 
ATOM   12737 O  O     . GLN A 1 3057 ? 230.475 202.290 210.071 1.00 1.32  ? 3057 GLN A O     1 
ATOM   12738 C  CB    . GLN A 1 3057 ? 231.505 204.687 208.057 1.00 1.18  ? 3057 GLN A CB    1 
ATOM   12739 C  CG    . GLN A 1 3057 ? 232.728 205.166 207.294 1.00 0.82  ? 3057 GLN A CG    1 
ATOM   12740 C  CD    . GLN A 1 3057 ? 234.022 204.890 208.031 1.00 2.03  ? 3057 GLN A CD    1 
ATOM   12741 O  OE1   . GLN A 1 3057 ? 234.881 204.160 207.545 1.00 3.27  ? 3057 GLN A OE1   1 
ATOM   12742 N  NE2   . GLN A 1 3057 ? 234.171 205.484 209.206 1.00 3.18  ? 3057 GLN A NE2   1 
ATOM   12743 N  N     . VAL A 1 3058 ? 228.922 202.907 208.562 1.00 0.43  ? 3058 VAL A N     1 
ATOM   12744 C  CA    . VAL A 1 3058 ? 227.811 202.474 209.406 1.00 0.39  ? 3058 VAL A CA    1 
ATOM   12745 C  C     . VAL A 1 3058 ? 227.864 200.968 209.618 1.00 0.65  ? 3058 VAL A C     1 
ATOM   12746 O  O     . VAL A 1 3058 ? 227.567 200.465 210.709 1.00 0.81  ? 3058 VAL A O     1 
ATOM   12747 C  CB    . VAL A 1 3058 ? 226.469 202.916 208.790 1.00 0.41  ? 3058 VAL A CB    1 
ATOM   12748 C  CG1   . VAL A 1 3058 ? 225.300 202.253 209.507 1.00 0.31  ? 3058 VAL A CG1   1 
ATOM   12749 C  CG2   . VAL A 1 3058 ? 226.336 204.427 208.832 1.00 0.53  ? 3058 VAL A CG2   1 
ATOM   12750 N  N     . ILE A 1 3059 ? 228.261 200.227 208.581 1.00 0.59  ? 3059 ILE A N     1 
ATOM   12751 C  CA    . ILE A 1 3059 ? 228.342 198.773 208.679 1.00 0.77  ? 3059 ILE A CA    1 
ATOM   12752 C  C     . ILE A 1 3059 ? 229.354 198.359 209.739 1.00 0.84  ? 3059 ILE A C     1 
ATOM   12753 O  O     . ILE A 1 3059 ? 229.100 197.449 210.537 1.00 1.12  ? 3059 ILE A O     1 
ATOM   12754 C  CB    . ILE A 1 3059 ? 228.674 198.172 207.299 1.00 1.05  ? 3059 ILE A CB    1 
ATOM   12755 C  CG1   . ILE A 1 3059 ? 227.416 198.127 206.428 1.00 0.93  ? 3059 ILE A CG1   1 
ATOM   12756 C  CG2   . ILE A 1 3059 ? 229.308 196.797 207.433 1.00 1.45  ? 3059 ILE A CG2   1 
ATOM   12757 C  CD1   . ILE A 1 3059 ? 227.624 197.476 205.088 1.00 1.11  ? 3059 ILE A CD1   1 
ATOM   12758 N  N     . ARG A 1 3060 ? 230.505 199.025 209.780 1.00 0.86  ? 3060 ARG A N     1 
ATOM   12759 C  CA    . ARG A 1 3060 ? 231.567 198.634 210.696 1.00 1.23  ? 3060 ARG A CA    1 
ATOM   12760 C  C     . ARG A 1 3060 ? 231.443 199.253 212.084 1.00 1.00  ? 3060 ARG A C     1 
ATOM   12761 O  O     . ARG A 1 3060 ? 232.000 198.699 213.038 1.00 1.74  ? 3060 ARG A O     1 
ATOM   12762 C  CB    . ARG A 1 3060 ? 232.932 198.990 210.100 1.00 0.83  ? 3060 ARG A CB    1 
ATOM   12763 C  CG    . ARG A 1 3060 ? 233.159 200.474 209.903 1.00 2.13  ? 3060 ARG A CG    1 
ATOM   12764 C  CD    . ARG A 1 3060 ? 234.479 200.744 209.198 1.00 4.91  ? 3060 ARG A CD    1 
ATOM   12765 N  NE    . ARG A 1 3060 ? 235.618 200.260 209.966 1.00 3.97  ? 3060 ARG A NE    1 
ATOM   12766 C  CZ    . ARG A 1 3060 ? 236.267 200.979 210.872 1.00 4.70  ? 3060 ARG A CZ    1 
ATOM   12767 N  NH1   . ARG A 1 3060 ? 235.917 202.224 211.146 1.00 3.42  ? 3060 ARG A NH1   1 
ATOM   12768 N  NH2   . ARG A 1 3060 ? 237.293 200.434 211.520 1.00 8.50  ? 3060 ARG A NH2   1 
ATOM   12769 N  N     . ASN A 1 3061 ? 230.725 200.365 212.233 1.00 0.66  ? 3061 ASN A N     1 
ATOM   12770 C  CA    . ASN A 1 3061 ? 230.689 201.079 213.503 1.00 0.61  ? 3061 ASN A CA    1 
ATOM   12771 C  C     . ASN A 1 3061 ? 229.374 200.965 214.256 1.00 0.60  ? 3061 ASN A C     1 
ATOM   12772 O  O     . ASN A 1 3061 ? 229.389 200.949 215.488 1.00 1.08  ? 3061 ASN A O     1 
ATOM   12773 C  CB    . ASN A 1 3061 ? 230.999 202.566 213.293 1.00 0.93  ? 3061 ASN A CB    1 
ATOM   12774 C  CG    . ASN A 1 3061 ? 232.446 202.812 212.930 1.00 1.36  ? 3061 ASN A CG    1 
ATOM   12775 O  OD1   . ASN A 1 3061 ? 233.350 202.212 213.505 1.00 5.55  ? 3061 ASN A OD1   1 
ATOM   12776 N  ND2   . ASN A 1 3061 ? 232.674 203.714 211.987 1.00 1.18  ? 3061 ASN A ND2   1 
ATOM   12777 N  N     . LEU A 1 3062 ? 228.243 200.890 213.564 1.00 0.35  ? 3062 LEU A N     1 
ATOM   12778 C  CA    . LEU A 1 3062 ? 226.951 200.893 214.237 1.00 0.19  ? 3062 LEU A CA    1 
ATOM   12779 C  C     . LEU A 1 3062 ? 226.595 199.481 214.686 1.00 0.09  ? 3062 LEU A C     1 
ATOM   12780 O  O     . LEU A 1 3062 ? 226.551 198.553 213.874 1.00 0.43  ? 3062 LEU A O     1 
ATOM   12781 C  CB    . LEU A 1 3062 ? 225.870 201.458 213.320 1.00 0.22  ? 3062 LEU A CB    1 
ATOM   12782 C  CG    . LEU A 1 3062 ? 224.458 201.481 213.905 1.00 0.16  ? 3062 LEU A CG    1 
ATOM   12783 C  CD1   . LEU A 1 3062 ? 224.441 202.201 215.245 1.00 0.20  ? 3062 LEU A CD1   1 
ATOM   12784 C  CD2   . LEU A 1 3062 ? 223.488 202.125 212.938 1.00 0.23  ? 3062 LEU A CD2   1 
ATOM   12785 N  N     . HIS A 1 3063 ? 226.350 199.322 215.983 1.00 0.20  ? 3063 HIS A N     1 
ATOM   12786 C  CA    . HIS A 1 3063 ? 225.910 198.064 216.565 1.00 0.12  ? 3063 HIS A CA    1 
ATOM   12787 C  C     . HIS A 1 3063 ? 224.534 198.274 217.175 1.00 0.09  ? 3063 HIS A C     1 
ATOM   12788 O  O     . HIS A 1 3063 ? 224.342 199.195 217.975 1.00 0.35  ? 3063 HIS A O     1 
ATOM   12789 C  CB    . HIS A 1 3063 ? 226.891 197.571 217.632 1.00 0.10  ? 3063 HIS A CB    1 
ATOM   12790 C  CG    . HIS A 1 3063 ? 228.243 197.219 217.096 1.00 0.10  ? 3063 HIS A CG    1 
ATOM   12791 N  ND1   . HIS A 1 3063 ? 228.585 195.939 216.723 1.00 0.20  ? 3063 HIS A ND1   1 
ATOM   12792 C  CD2   . HIS A 1 3063 ? 229.339 197.982 216.874 1.00 0.17  ? 3063 HIS A CD2   1 
ATOM   12793 C  CE1   . HIS A 1 3063 ? 229.834 195.927 216.292 1.00 0.47  ? 3063 HIS A CE1   1 
ATOM   12794 N  NE2   . HIS A 1 3063 ? 230.313 197.155 216.373 1.00 0.22  ? 3063 HIS A NE2   1 
ATOM   12795 N  N     . VAL A 1 3064 ? 223.583 197.430 216.798 1.00 0.11  ? 3064 VAL A N     1 
ATOM   12796 C  CA    . VAL A 1 3064 ? 222.215 197.526 217.287 1.00 0.19  ? 3064 VAL A CA    1 
ATOM   12797 C  C     . VAL A 1 3064 ? 221.979 196.372 218.247 1.00 0.08  ? 3064 VAL A C     1 
ATOM   12798 O  O     . VAL A 1 3064 ? 222.212 195.208 217.902 1.00 0.07  ? 3064 VAL A O     1 
ATOM   12799 C  CB    . VAL A 1 3064 ? 221.197 197.512 216.138 1.00 0.27  ? 3064 VAL A CB    1 
ATOM   12800 C  CG1   . VAL A 1 3064 ? 219.788 197.317 216.679 1.00 0.05  ? 3064 VAL A CG1   1 
ATOM   12801 C  CG2   . VAL A 1 3064 ? 221.294 198.797 215.336 1.00 0.30  ? 3064 VAL A CG2   1 
ATOM   12802 N  N     . VAL A 1 3065 ? 221.535 196.696 219.455 1.00 0.14  ? 3065 VAL A N     1 
ATOM   12803 C  CA    . VAL A 1 3065 ? 221.143 195.704 220.446 1.00 0.11  ? 3065 VAL A CA    1 
ATOM   12804 C  C     . VAL A 1 3065 ? 219.637 195.808 220.627 1.00 0.08  ? 3065 VAL A C     1 
ATOM   12805 O  O     . VAL A 1 3065 ? 219.127 196.848 221.060 1.00 0.24  ? 3065 VAL A O     1 
ATOM   12806 C  CB    . VAL A 1 3065 ? 221.880 195.903 221.778 1.00 0.10  ? 3065 VAL A CB    1 
ATOM   12807 C  CG1   . VAL A 1 3065 ? 221.467 194.834 222.775 1.00 0.06  ? 3065 VAL A CG1   1 
ATOM   12808 C  CG2   . VAL A 1 3065 ? 223.383 195.888 221.560 1.00 0.05  ? 3065 VAL A CG2   1 
ATOM   12809 N  N     . PHE A 1 3066 ? 218.930 194.738 220.291 1.00 0.04  ? 3066 PHE A N     1 
ATOM   12810 C  CA    . PHE A 1 3066 ? 217.484 194.659 220.449 1.00 0.19  ? 3066 PHE A CA    1 
ATOM   12811 C  C     . PHE A 1 3066 ? 217.165 193.790 221.655 1.00 0.25  ? 3066 PHE A C     1 
ATOM   12812 O  O     . PHE A 1 3066 ? 217.605 192.639 221.728 1.00 0.19  ? 3066 PHE A O     1 
ATOM   12813 C  CB    . PHE A 1 3066 ? 216.822 194.100 219.190 1.00 0.79  ? 3066 PHE A CB    1 
ATOM   12814 C  CG    . PHE A 1 3066 ? 215.445 194.636 218.944 1.00 2.95  ? 3066 PHE A CG    1 
ATOM   12815 C  CD1   . PHE A 1 3066 ? 215.257 195.894 218.403 1.00 3.74  ? 3066 PHE A CD1   1 
ATOM   12816 C  CD2   . PHE A 1 3066 ? 214.332 193.880 219.273 1.00 4.28  ? 3066 PHE A CD2   1 
ATOM   12817 C  CE1   . PHE A 1 3066 ? 213.984 196.382 218.185 1.00 12.11 ? 3066 PHE A CE1   1 
ATOM   12818 C  CE2   . PHE A 1 3066 ? 213.058 194.364 219.058 1.00 8.72  ? 3066 PHE A CE2   1 
ATOM   12819 C  CZ    . PHE A 1 3066 ? 212.883 195.617 218.513 1.00 7.94  ? 3066 PHE A CZ    1 
ATOM   12820 N  N     . THR A 1 3067 ? 216.400 194.340 222.592 1.00 1.10  ? 3067 THR A N     1 
ATOM   12821 C  CA    . THR A 1 3067 ? 215.967 193.623 223.781 1.00 2.12  ? 3067 THR A CA    1 
ATOM   12822 C  C     . THR A 1 3067 ? 214.453 193.470 223.749 1.00 1.85  ? 3067 THR A C     1 
ATOM   12823 O  O     . THR A 1 3067 ? 213.734 194.436 223.482 1.00 4.16  ? 3067 THR A O     1 
ATOM   12824 C  CB    . THR A 1 3067 ? 216.404 194.346 225.057 1.00 1.60  ? 3067 THR A CB    1 
ATOM   12825 O  OG1   . THR A 1 3067 ? 215.943 195.701 225.025 1.00 5.25  ? 3067 THR A OG1   1 
ATOM   12826 C  CG2   . THR A 1 3067 ? 217.916 194.334 225.182 1.00 0.48  ? 3067 THR A CG2   1 
ATOM   12827 N  N     . MET A 1 3068 ? 213.976 192.254 224.006 1.00 2.67  ? 3068 MET A N     1 
ATOM   12828 C  CA    . MET A 1 3068 ? 212.549 191.975 224.000 1.00 4.60  ? 3068 MET A CA    1 
ATOM   12829 C  C     . MET A 1 3068 ? 212.250 190.837 224.965 1.00 2.59  ? 3068 MET A C     1 
ATOM   12830 O  O     . MET A 1 3068 ? 213.096 189.975 225.211 1.00 1.52  ? 3068 MET A O     1 
ATOM   12831 C  CB    . MET A 1 3068 ? 212.056 191.627 222.591 1.00 3.87  ? 3068 MET A CB    1 
ATOM   12832 C  CG    . MET A 1 3068 ? 212.780 190.465 221.942 1.00 3.94  ? 3068 MET A CG    1 
ATOM   12833 S  SD    . MET A 1 3068 ? 212.242 190.185 220.246 1.00 18.13 ? 3068 MET A SD    1 
ATOM   12834 C  CE    . MET A 1 3068 ? 210.467 190.265 220.439 1.00 17.25 ? 3068 MET A CE    1 
ATOM   12835 N  N     . ASN A 1 3069 ? 211.032 190.846 225.509 1.00 7.36  ? 3069 ASN A N     1 
ATOM   12836 C  CA    . ASN A 1 3069 ? 210.600 189.772 226.389 1.00 6.11  ? 3069 ASN A CA    1 
ATOM   12837 C  C     . ASN A 1 3069 ? 210.212 188.532 225.585 1.00 6.69  ? 3069 ASN A C     1 
ATOM   12838 O  O     . ASN A 1 3069 ? 209.789 188.637 224.433 1.00 7.42  ? 3069 ASN A O     1 
ATOM   12839 C  CB    . ASN A 1 3069 ? 209.416 190.213 227.243 1.00 5.86  ? 3069 ASN A CB    1 
ATOM   12840 C  CG    . ASN A 1 3069 ? 209.764 191.339 228.186 1.00 7.55  ? 3069 ASN A CG    1 
ATOM   12841 O  OD1   . ASN A 1 3069 ? 210.569 191.176 229.100 1.00 10.11 ? 3069 ASN A OD1   1 
ATOM   12842 N  ND2   . ASN A 1 3069 ? 209.163 192.494 227.964 1.00 14.76 ? 3069 ASN A ND2   1 
ATOM   12843 N  N     . PRO A 1 3070 ? 210.357 187.345 226.175 1.00 6.56  ? 3070 PRO A N     1 
ATOM   12844 C  CA    . PRO A 1 3070 ? 209.896 186.123 225.502 1.00 7.33  ? 3070 PRO A CA    1 
ATOM   12845 C  C     . PRO A 1 3070 ? 208.378 186.085 225.425 1.00 10.95 ? 3070 PRO A C     1 
ATOM   12846 O  O     . PRO A 1 3070 ? 207.687 186.020 226.443 1.00 16.42 ? 3070 PRO A O     1 
ATOM   12847 C  CB    . PRO A 1 3070 ? 210.445 184.999 226.391 1.00 5.41  ? 3070 PRO A CB    1 
ATOM   12848 C  CG    . PRO A 1 3070 ? 211.508 185.637 227.226 1.00 4.19  ? 3070 PRO A CG    1 
ATOM   12849 C  CD    . PRO A 1 3070 ? 211.066 187.047 227.428 1.00 3.49  ? 3070 PRO A CD    1 
ATOM   12850 N  N     . SER A 1 3071 ? 207.861 186.139 224.201 1.00 13.46 ? 3071 SER A N     1 
ATOM   12851 C  CA    . SER A 1 3071 ? 206.432 185.986 223.942 1.00 14.71 ? 3071 SER A CA    1 
ATOM   12852 C  C     . SER A 1 3071 ? 206.291 185.084 222.727 1.00 18.30 ? 3071 SER A C     1 
ATOM   12853 O  O     . SER A 1 3071 ? 206.750 185.440 221.639 1.00 18.02 ? 3071 SER A O     1 
ATOM   12854 C  CB    . SER A 1 3071 ? 205.757 187.337 223.709 1.00 15.19 ? 3071 SER A CB    1 
ATOM   12855 O  OG    . SER A 1 3071 ? 205.977 188.211 224.802 1.00 18.34 ? 3071 SER A OG    1 
ATOM   12856 N  N     . SER A 1 3072 ? 205.666 183.919 222.913 1.00 24.41 ? 3072 SER A N     1 
ATOM   12857 C  CA    . SER A 1 3072 ? 205.567 182.948 221.827 1.00 20.54 ? 3072 SER A CA    1 
ATOM   12858 C  C     . SER A 1 3072 ? 204.854 183.540 220.618 1.00 19.07 ? 3072 SER A C     1 
ATOM   12859 O  O     . SER A 1 3072 ? 205.341 183.444 219.487 1.00 20.99 ? 3072 SER A O     1 
ATOM   12860 C  CB    . SER A 1 3072 ? 204.849 181.690 222.317 1.00 17.92 ? 3072 SER A CB    1 
ATOM   12861 O  OG    . SER A 1 3072 ? 205.566 181.075 223.372 1.00 22.83 ? 3072 SER A OG    1 
ATOM   12862 N  N     . GLU A 1 3073 ? 203.698 184.166 220.840 1.00 20.80 ? 3073 GLU A N     1 
ATOM   12863 C  CA    . GLU A 1 3073 ? 203.003 184.834 219.745 1.00 22.85 ? 3073 GLU A CA    1 
ATOM   12864 C  C     . GLU A 1 3073 ? 203.800 186.032 219.244 1.00 18.75 ? 3073 GLU A C     1 
ATOM   12865 O  O     . GLU A 1 3073 ? 203.922 186.248 218.032 1.00 24.19 ? 3073 GLU A O     1 
ATOM   12866 C  CB    . GLU A 1 3073 ? 201.606 185.263 220.192 1.00 22.77 ? 3073 GLU A CB    1 
ATOM   12867 C  CG    . GLU A 1 3073 ? 200.836 186.044 219.140 1.00 25.47 ? 3073 GLU A CG    1 
ATOM   12868 C  CD    . GLU A 1 3073 ? 199.462 186.472 219.618 1.00 35.47 ? 3073 GLU A CD    1 
ATOM   12869 O  OE1   . GLU A 1 3073 ? 199.383 187.210 220.623 1.00 33.57 ? 3073 GLU A OE1   1 
ATOM   12870 O  OE2   . GLU A 1 3073 ? 198.461 186.070 218.989 1.00 37.00 ? 3073 GLU A OE2   1 
ATOM   12871 N  N     . GLY A 1 3074 ? 204.355 186.821 220.166 1.00 17.76 ? 3074 GLY A N     1 
ATOM   12872 C  CA    . GLY A 1 3074 ? 205.100 188.002 219.761 1.00 16.30 ? 3074 GLY A CA    1 
ATOM   12873 C  C     . GLY A 1 3074 ? 206.359 187.663 218.984 1.00 17.67 ? 3074 GLY A C     1 
ATOM   12874 O  O     . GLY A 1 3074 ? 206.696 188.330 218.003 1.00 15.23 ? 3074 GLY A O     1 
ATOM   12875 N  N     . LEU A 1 3075 ? 207.074 186.624 219.421 1.00 14.03 ? 3075 LEU A N     1 
ATOM   12876 C  CA    . LEU A 1 3075 ? 208.317 186.251 218.754 1.00 12.97 ? 3075 LEU A CA    1 
ATOM   12877 C  C     . LEU A 1 3075 ? 208.054 185.752 217.338 1.00 17.15 ? 3075 LEU A C     1 
ATOM   12878 O  O     . LEU A 1 3075 ? 208.767 186.120 216.397 1.00 12.77 ? 3075 LEU A O     1 
ATOM   12879 C  CB    . LEU A 1 3075 ? 209.051 185.192 219.575 1.00 15.91 ? 3075 LEU A CB    1 
ATOM   12880 C  CG    . LEU A 1 3075 ? 210.469 184.855 219.125 1.00 15.41 ? 3075 LEU A CG    1 
ATOM   12881 C  CD1   . LEU A 1 3075 ? 211.377 186.049 219.355 1.00 12.36 ? 3075 LEU A CD1   1 
ATOM   12882 C  CD2   . LEU A 1 3075 ? 210.989 183.627 219.847 1.00 12.30 ? 3075 LEU A CD2   1 
ATOM   12883 N  N     . LYS A 1 3076 ? 207.032 184.908 217.166 1.00 17.71 ? 3076 LYS A N     1 
ATOM   12884 C  CA    . LYS A 1 3076 ? 206.683 184.435 215.828 1.00 12.70 ? 3076 LYS A CA    1 
ATOM   12885 C  C     . LYS A 1 3076 ? 206.233 185.582 214.934 1.00 14.33 ? 3076 LYS A C     1 
ATOM   12886 O  O     . LYS A 1 3076 ? 206.616 185.651 213.761 1.00 22.65 ? 3076 LYS A O     1 
ATOM   12887 C  CB    . LYS A 1 3076 ? 205.593 183.364 215.905 1.00 13.57 ? 3076 LYS A CB    1 
ATOM   12888 C  CG    . LYS A 1 3076 ? 205.993 182.110 216.653 1.00 12.15 ? 3076 LYS A CG    1 
ATOM   12889 C  CD    . LYS A 1 3076 ? 204.906 181.054 216.577 1.00 14.01 ? 3076 LYS A CD    1 
ATOM   12890 C  CE    . LYS A 1 3076 ? 205.352 179.755 217.223 1.00 12.56 ? 3076 LYS A CE    1 
ATOM   12891 N  NZ    . LYS A 1 3076 ? 204.299 178.706 217.137 1.00 22.79 ? 3076 LYS A NZ    1 
ATOM   12892 N  N     . ASP A 1 3077 ? 205.415 186.490 215.470 1.00 14.33 ? 3077 ASP A N     1 
ATOM   12893 C  CA    . ASP A 1 3077 ? 204.984 187.642 214.687 1.00 16.16 ? 3077 ASP A CA    1 
ATOM   12894 C  C     . ASP A 1 3077 ? 206.150 188.579 214.398 1.00 13.49 ? 3077 ASP A C     1 
ATOM   12895 O  O     . ASP A 1 3077 ? 206.140 189.301 213.395 1.00 20.06 ? 3077 ASP A O     1 
ATOM   12896 C  CB    . ASP A 1 3077 ? 203.870 188.388 215.419 1.00 19.93 ? 3077 ASP A CB    1 
ATOM   12897 C  CG    . ASP A 1 3077 ? 202.578 187.598 215.473 1.00 27.53 ? 3077 ASP A CG    1 
ATOM   12898 O  OD1   . ASP A 1 3077 ? 202.331 186.795 214.551 1.00 28.62 ? 3077 ASP A OD1   1 
ATOM   12899 O  OD2   . ASP A 1 3077 ? 201.810 187.782 216.440 1.00 29.94 ? 3077 ASP A OD2   1 
ATOM   12900 N  N     . ARG A 1 3078 ? 207.163 188.577 215.266 1.00 15.83 ? 3078 ARG A N     1 
ATOM   12901 C  CA    . ARG A 1 3078 ? 208.256 189.532 215.127 1.00 14.75 ? 3078 ARG A CA    1 
ATOM   12902 C  C     . ARG A 1 3078 ? 209.081 189.237 213.881 1.00 12.27 ? 3078 ARG A C     1 
ATOM   12903 O  O     . ARG A 1 3078 ? 209.678 190.147 213.297 1.00 11.24 ? 3078 ARG A O     1 
ATOM   12904 C  CB    . ARG A 1 3078 ? 209.146 189.486 216.371 1.00 13.69 ? 3078 ARG A CB    1 
ATOM   12905 C  CG    . ARG A 1 3078 ? 210.316 190.438 216.330 1.00 17.44 ? 3078 ARG A CG    1 
ATOM   12906 C  CD    . ARG A 1 3078 ? 209.767 191.850 216.356 1.00 13.60 ? 3078 ARG A CD    1 
ATOM   12907 N  NE    . ARG A 1 3078 ? 209.107 192.087 217.635 1.00 21.12 ? 3078 ARG A NE    1 
ATOM   12908 C  CZ    . ARG A 1 3078 ? 208.321 193.117 217.910 1.00 23.55 ? 3078 ARG A CZ    1 
ATOM   12909 N  NH1   . ARG A 1 3078 ? 208.010 194.015 216.993 1.00 21.31 ? 3078 ARG A NH1   1 
ATOM   12910 N  NH2   . ARG A 1 3078 ? 207.818 193.239 219.136 1.00 24.75 ? 3078 ARG A NH2   1 
ATOM   12911 N  N     . ALA A 1 3079 ? 209.116 187.970 213.460 1.00 8.68  ? 3079 ALA A N     1 
ATOM   12912 C  CA    . ALA A 1 3079 ? 209.934 187.575 212.318 1.00 9.16  ? 3079 ALA A CA    1 
ATOM   12913 C  C     . ALA A 1 3079 ? 209.449 188.229 211.029 1.00 13.20 ? 3079 ALA A C     1 
ATOM   12914 O  O     . ALA A 1 3079 ? 210.256 188.658 210.199 1.00 11.04 ? 3079 ALA A O     1 
ATOM   12915 C  CB    . ALA A 1 3079 ? 209.936 186.052 212.184 1.00 6.27  ? 3079 ALA A CB    1 
ATOM   12916 N  N     . ALA A 1 3080 ? 208.131 188.299 210.833 1.00 10.44 ? 3080 ALA A N     1 
ATOM   12917 C  CA    . ALA A 1 3080 ? 207.610 188.910 209.616 1.00 7.25  ? 3080 ALA A CA    1 
ATOM   12918 C  C     . ALA A 1 3080 ? 207.843 190.416 209.607 1.00 5.58  ? 3080 ALA A C     1 
ATOM   12919 O  O     . ALA A 1 3080 ? 208.205 190.987 208.571 1.00 3.40  ? 3080 ALA A O     1 
ATOM   12920 C  CB    . ALA A 1 3080 ? 206.123 188.593 209.462 1.00 6.25  ? 3080 ALA A CB    1 
ATOM   12921 N  N     . THR A 1 3081 ? 207.633 191.076 210.748 1.00 8.47  ? 3081 THR A N     1 
ATOM   12922 C  CA    . THR A 1 3081 ? 207.798 192.525 210.813 1.00 7.87  ? 3081 THR A CA    1 
ATOM   12923 C  C     . THR A 1 3081 ? 209.251 192.933 210.593 1.00 9.24  ? 3081 THR A C     1 
ATOM   12924 O  O     . THR A 1 3081 ? 209.525 193.918 209.897 1.00 12.92 ? 3081 THR A O     1 
ATOM   12925 C  CB    . THR A 1 3081 ? 207.289 193.047 212.158 1.00 11.81 ? 3081 THR A CB    1 
ATOM   12926 O  OG1   . THR A 1 3081 ? 205.900 192.724 212.299 1.00 11.60 ? 3081 THR A OG1   1 
ATOM   12927 C  CG2   . THR A 1 3081 ? 207.461 194.553 212.254 1.00 9.76  ? 3081 THR A CG2   1 
ATOM   12928 N  N     . SER A 1 3082 ? 210.194 192.205 211.188 1.00 7.94  ? 3082 SER A N     1 
ATOM   12929 C  CA    . SER A 1 3082 ? 211.621 192.480 211.033 1.00 5.98  ? 3082 SER A CA    1 
ATOM   12930 C  C     . SER A 1 3082 ? 212.360 191.169 210.806 1.00 5.12  ? 3082 SER A C     1 
ATOM   12931 O  O     . SER A 1 3082 ? 212.947 190.604 211.738 1.00 8.14  ? 3082 SER A O     1 
ATOM   12932 C  CB    . SER A 1 3082 ? 212.174 193.227 212.247 1.00 7.42  ? 3082 SER A CB    1 
ATOM   12933 O  OG    . SER A 1 3082 ? 213.563 193.465 212.108 1.00 8.23  ? 3082 SER A OG    1 
ATOM   12934 N  N     . PRO A 1 3083 ? 212.348 190.651 209.574 1.00 6.49  ? 3083 PRO A N     1 
ATOM   12935 C  CA    . PRO A 1 3083 ? 213.122 189.430 209.293 1.00 5.67  ? 3083 PRO A CA    1 
ATOM   12936 C  C     . PRO A 1 3083 ? 214.613 189.596 209.513 1.00 2.22  ? 3083 PRO A C     1 
ATOM   12937 O  O     . PRO A 1 3083 ? 215.309 188.601 209.750 1.00 2.11  ? 3083 PRO A O     1 
ATOM   12938 C  CB    . PRO A 1 3083 ? 212.793 189.137 207.821 1.00 3.39  ? 3083 PRO A CB    1 
ATOM   12939 C  CG    . PRO A 1 3083 ? 212.249 190.417 207.281 1.00 2.29  ? 3083 PRO A CG    1 
ATOM   12940 C  CD    . PRO A 1 3083 ? 211.548 191.073 208.415 1.00 2.89  ? 3083 PRO A CD    1 
ATOM   12941 N  N     . ALA A 1 3084 ? 215.128 190.825 209.439 1.00 3.06  ? 3084 ALA A N     1 
ATOM   12942 C  CA    . ALA A 1 3084 ? 216.534 191.068 209.732 1.00 2.95  ? 3084 ALA A CA    1 
ATOM   12943 C  C     . ALA A 1 3084 ? 216.879 190.788 211.189 1.00 3.35  ? 3084 ALA A C     1 
ATOM   12944 O  O     . ALA A 1 3084 ? 218.037 190.483 211.489 1.00 3.45  ? 3084 ALA A O     1 
ATOM   12945 C  CB    . ALA A 1 3084 ? 216.905 192.506 209.373 1.00 2.70  ? 3084 ALA A CB    1 
ATOM   12946 N  N     . LEU A 1 3085 ? 215.903 190.880 212.097 1.00 2.71  ? 3085 LEU A N     1 
ATOM   12947 C  CA    . LEU A 1 3085 ? 216.167 190.584 213.501 1.00 3.26  ? 3085 LEU A CA    1 
ATOM   12948 C  C     . LEU A 1 3085 ? 216.592 189.136 213.706 1.00 4.47  ? 3085 LEU A C     1 
ATOM   12949 O  O     . LEU A 1 3085 ? 217.288 188.828 214.679 1.00 6.58  ? 3085 LEU A O     1 
ATOM   12950 C  CB    . LEU A 1 3085 ? 214.929 190.883 214.348 1.00 4.33  ? 3085 LEU A CB    1 
ATOM   12951 C  CG    . LEU A 1 3085 ? 214.735 192.296 214.898 1.00 3.68  ? 3085 LEU A CG    1 
ATOM   12952 C  CD1   . LEU A 1 3085 ? 213.646 192.295 215.953 1.00 8.32  ? 3085 LEU A CD1   1 
ATOM   12953 C  CD2   . LEU A 1 3085 ? 216.026 192.843 215.469 1.00 3.69  ? 3085 LEU A CD2   1 
ATOM   12954 N  N     . PHE A 1 3086 ? 216.194 188.240 212.807 1.00 3.00  ? 3086 PHE A N     1 
ATOM   12955 C  CA    . PHE A 1 3086 ? 216.432 186.817 212.983 1.00 1.89  ? 3086 PHE A CA    1 
ATOM   12956 C  C     . PHE A 1 3086 ? 217.435 186.238 211.995 1.00 2.91  ? 3086 PHE A C     1 
ATOM   12957 O  O     . PHE A 1 3086 ? 217.804 185.068 212.132 1.00 5.36  ? 3086 PHE A O     1 
ATOM   12958 C  CB    . PHE A 1 3086 ? 215.106 186.056 212.902 1.00 3.00  ? 3086 PHE A CB    1 
ATOM   12959 C  CG    . PHE A 1 3086 ? 214.161 186.389 214.019 1.00 5.98  ? 3086 PHE A CG    1 
ATOM   12960 C  CD1   . PHE A 1 3086 ? 213.300 187.467 213.917 1.00 4.69  ? 3086 PHE A CD1   1 
ATOM   12961 C  CD2   . PHE A 1 3086 ? 214.151 185.637 215.180 1.00 6.35  ? 3086 PHE A CD2   1 
ATOM   12962 C  CE1   . PHE A 1 3086 ? 212.441 187.781 214.945 1.00 6.62  ? 3086 PHE A CE1   1 
ATOM   12963 C  CE2   . PHE A 1 3086 ? 213.291 185.948 216.211 1.00 7.84  ? 3086 PHE A CE2   1 
ATOM   12964 C  CZ    . PHE A 1 3086 ? 212.436 187.020 216.092 1.00 8.60  ? 3086 PHE A CZ    1 
ATOM   12965 N  N     . ASN A 1 3087 ? 217.891 187.014 211.011 1.00 3.96  ? 3087 ASN A N     1 
ATOM   12966 C  CA    . ASN A 1 3087 ? 218.953 186.563 210.125 1.00 3.65  ? 3087 ASN A CA    1 
ATOM   12967 C  C     . ASN A 1 3087 ? 220.139 187.514 210.035 1.00 4.47  ? 3087 ASN A C     1 
ATOM   12968 O  O     . ASN A 1 3087 ? 221.174 187.121 209.488 1.00 6.96  ? 3087 ASN A O     1 
ATOM   12969 C  CB    . ASN A 1 3087 ? 218.404 186.287 208.712 1.00 4.22  ? 3087 ASN A CB    1 
ATOM   12970 C  CG    . ASN A 1 3087 ? 217.809 187.517 208.051 1.00 7.73  ? 3087 ASN A CG    1 
ATOM   12971 O  OD1   . ASN A 1 3087 ? 218.467 188.543 207.903 1.00 12.46 ? 3087 ASN A OD1   1 
ATOM   12972 N  ND2   . ASN A 1 3087 ? 216.556 187.408 207.631 1.00 9.95  ? 3087 ASN A ND2   1 
ATOM   12973 N  N     . ARG A 1 3088 ? 220.026 188.739 210.553 1.00 3.98  ? 3088 ARG A N     1 
ATOM   12974 C  CA    . ARG A 1 3088 ? 221.155 189.654 210.636 1.00 4.45  ? 3088 ARG A CA    1 
ATOM   12975 C  C     . ARG A 1 3088 ? 221.621 189.919 212.060 1.00 4.74  ? 3088 ARG A C     1 
ATOM   12976 O  O     . ARG A 1 3088 ? 222.692 190.510 212.238 1.00 3.53  ? 3088 ARG A O     1 
ATOM   12977 C  CB    . ARG A 1 3088 ? 220.823 191.001 209.971 1.00 5.98  ? 3088 ARG A CB    1 
ATOM   12978 C  CG    . ARG A 1 3088 ? 220.353 190.912 208.530 1.00 3.85  ? 3088 ARG A CG    1 
ATOM   12979 C  CD    . ARG A 1 3088 ? 221.344 190.169 207.654 1.00 6.05  ? 3088 ARG A CD    1 
ATOM   12980 N  NE    . ARG A 1 3088 ? 221.591 190.873 206.400 1.00 12.61 ? 3088 ARG A NE    1 
ATOM   12981 C  CZ    . ARG A 1 3088 ? 220.887 190.693 205.290 1.00 12.50 ? 3088 ARG A CZ    1 
ATOM   12982 N  NH1   . ARG A 1 3088 ? 219.886 189.831 205.236 1.00 9.93  ? 3088 ARG A NH1   1 
ATOM   12983 N  NH2   . ARG A 1 3088 ? 221.197 191.400 204.205 1.00 9.28  ? 3088 ARG A NH2   1 
ATOM   12984 N  N     . CYS A 1 3089 ? 220.863 189.509 213.071 1.00 6.54  ? 3089 CYS A N     1 
ATOM   12985 C  CA    . CYS A 1 3089 ? 221.233 189.705 214.465 1.00 2.10  ? 3089 CYS A CA    1 
ATOM   12986 C  C     . CYS A 1 3089 ? 221.513 188.359 215.116 1.00 1.63  ? 3089 CYS A C     1 
ATOM   12987 O  O     . CYS A 1 3089 ? 220.820 187.374 214.852 1.00 2.61  ? 3089 CYS A O     1 
ATOM   12988 C  CB    . CYS A 1 3089 ? 220.128 190.431 215.237 1.00 0.43  ? 3089 CYS A CB    1 
ATOM   12989 S  SG    . CYS A 1 3089 ? 219.498 191.923 214.446 1.00 7.73  ? 3089 CYS A SG    1 
ATOM   12990 N  N     . VAL A 1 3090 ? 222.533 188.324 215.966 1.00 1.38  ? 3090 VAL A N     1 
ATOM   12991 C  CA    . VAL A 1 3090 ? 222.836 187.130 216.747 1.00 1.58  ? 3090 VAL A CA    1 
ATOM   12992 C  C     . VAL A 1 3090 ? 221.872 187.076 217.923 1.00 0.67  ? 3090 VAL A C     1 
ATOM   12993 O  O     . VAL A 1 3090 ? 221.763 188.033 218.695 1.00 0.90  ? 3090 VAL A O     1 
ATOM   12994 C  CB    . VAL A 1 3090 ? 224.296 187.132 217.222 1.00 1.18  ? 3090 VAL A CB    1 
ATOM   12995 C  CG1   . VAL A 1 3090 ? 224.522 186.041 218.251 1.00 0.67  ? 3090 VAL A CG1   1 
ATOM   12996 C  CG2   . VAL A 1 3090 ? 225.231 186.965 216.041 1.00 0.76  ? 3090 VAL A CG2   1 
ATOM   12997 N  N     . LEU A 1 3091 ? 221.161 185.962 218.056 1.00 0.82  ? 3091 LEU A N     1 
ATOM   12998 C  CA    . LEU A 1 3091 ? 220.139 185.826 219.081 1.00 0.41  ? 3091 LEU A CA    1 
ATOM   12999 C  C     . LEU A 1 3091 ? 220.725 185.114 220.293 1.00 0.50  ? 3091 LEU A C     1 
ATOM   13000 O  O     . LEU A 1 3091 ? 221.322 184.042 220.166 1.00 0.38  ? 3091 LEU A O     1 
ATOM   13001 C  CB    . LEU A 1 3091 ? 218.928 185.067 218.530 1.00 0.50  ? 3091 LEU A CB    1 
ATOM   13002 C  CG    . LEU A 1 3091 ? 217.608 185.039 219.315 1.00 0.63  ? 3091 LEU A CG    1 
ATOM   13003 C  CD1   . LEU A 1 3091 ? 216.480 184.628 218.389 1.00 0.54  ? 3091 LEU A CD1   1 
ATOM   13004 C  CD2   . LEU A 1 3091 ? 217.644 184.115 220.528 1.00 0.32  ? 3091 LEU A CD2   1 
ATOM   13005 N  N     . ASN A 1 3092 ? 220.560 185.724 221.461 1.00 0.58  ? 3092 ASN A N     1 
ATOM   13006 C  CA    . ASN A 1 3092 ? 220.974 185.141 222.732 1.00 0.50  ? 3092 ASN A CA    1 
ATOM   13007 C  C     . ASN A 1 3092 ? 219.755 185.086 223.640 1.00 0.34  ? 3092 ASN A C     1 
ATOM   13008 O  O     . ASN A 1 3092 ? 219.225 186.128 224.040 1.00 0.23  ? 3092 ASN A O     1 
ATOM   13009 C  CB    . ASN A 1 3092 ? 222.104 185.948 223.369 1.00 0.72  ? 3092 ASN A CB    1 
ATOM   13010 C  CG    . ASN A 1 3092 ? 223.365 185.941 222.534 1.00 1.91  ? 3092 ASN A CG    1 
ATOM   13011 O  OD1   . ASN A 1 3092 ? 223.789 186.973 222.022 1.00 13.57 ? 3092 ASN A OD1   1 
ATOM   13012 N  ND2   . ASN A 1 3092 ? 223.977 184.775 222.399 1.00 4.52  ? 3092 ASN A ND2   1 
ATOM   13013 N  N     . TRP A 1 3093 ? 219.306 183.874 223.954 1.00 0.27  ? 3093 TRP A N     1 
ATOM   13014 C  CA    . TRP A 1 3093 ? 218.148 183.678 224.823 1.00 0.45  ? 3093 TRP A CA    1 
ATOM   13015 C  C     . TRP A 1 3093 ? 218.610 183.747 226.270 1.00 0.41  ? 3093 TRP A C     1 
ATOM   13016 O  O     . TRP A 1 3093 ? 218.977 182.742 226.880 1.00 2.46  ? 3093 TRP A O     1 
ATOM   13017 C  CB    . TRP A 1 3093 ? 217.464 182.351 224.527 1.00 0.79  ? 3093 TRP A CB    1 
ATOM   13018 C  CG    . TRP A 1 3093 ? 216.045 182.310 224.989 1.00 1.02  ? 3093 TRP A CG    1 
ATOM   13019 C  CD1   . TRP A 1 3093 ? 215.600 181.989 226.237 1.00 0.62  ? 3093 TRP A CD1   1 
ATOM   13020 C  CD2   . TRP A 1 3093 ? 214.879 182.591 224.208 1.00 1.17  ? 3093 TRP A CD2   1 
ATOM   13021 N  NE1   . TRP A 1 3093 ? 214.233 182.060 226.285 1.00 1.16  ? 3093 TRP A NE1   1 
ATOM   13022 C  CE2   . TRP A 1 3093 ? 213.763 182.427 225.051 1.00 1.43  ? 3093 TRP A CE2   1 
ATOM   13023 C  CE3   . TRP A 1 3093 ? 214.670 182.969 222.879 1.00 1.04  ? 3093 TRP A CE3   1 
ATOM   13024 C  CZ2   . TRP A 1 3093 ? 212.460 182.626 224.609 1.00 1.36  ? 3093 TRP A CZ2   1 
ATOM   13025 C  CZ3   . TRP A 1 3093 ? 213.376 183.167 222.443 1.00 2.18  ? 3093 TRP A CZ3   1 
ATOM   13026 C  CH2   . TRP A 1 3093 ? 212.287 182.995 223.304 1.00 1.89  ? 3093 TRP A CH2   1 
ATOM   13027 N  N     . PHE A 1 3094 ? 218.599 184.955 226.828 1.00 0.37  ? 3094 PHE A N     1 
ATOM   13028 C  CA    . PHE A 1 3094 ? 218.891 185.100 228.248 1.00 0.44  ? 3094 PHE A CA    1 
ATOM   13029 C  C     . PHE A 1 3094 ? 217.748 184.577 229.107 1.00 0.84  ? 3094 PHE A C     1 
ATOM   13030 O  O     . PHE A 1 3094 ? 217.993 184.004 230.174 1.00 2.38  ? 3094 PHE A O     1 
ATOM   13031 C  CB    . PHE A 1 3094 ? 219.194 186.562 228.581 1.00 0.46  ? 3094 PHE A CB    1 
ATOM   13032 C  CG    . PHE A 1 3094 ? 220.496 187.061 228.010 1.00 1.70  ? 3094 PHE A CG    1 
ATOM   13033 C  CD1   . PHE A 1 3094 ? 221.365 186.197 227.357 1.00 1.44  ? 3094 PHE A CD1   1 
ATOM   13034 C  CD2   . PHE A 1 3094 ? 220.856 188.392 228.135 1.00 1.15  ? 3094 PHE A CD2   1 
ATOM   13035 C  CE1   . PHE A 1 3094 ? 222.561 186.654 226.834 1.00 1.02  ? 3094 PHE A CE1   1 
ATOM   13036 C  CE2   . PHE A 1 3094 ? 222.050 188.854 227.619 1.00 1.35  ? 3094 PHE A CE2   1 
ATOM   13037 C  CZ    . PHE A 1 3094 ? 222.903 187.985 226.967 1.00 2.28  ? 3094 PHE A CZ    1 
ATOM   13038 N  N     . GLY A 1 3095 ? 216.508 184.750 228.654 1.00 0.57  ? 3095 GLY A N     1 
ATOM   13039 C  CA    . GLY A 1 3095 ? 215.360 184.222 229.369 1.00 0.68  ? 3095 GLY A CA    1 
ATOM   13040 C  C     . GLY A 1 3095 ? 215.224 184.822 230.752 1.00 1.72  ? 3095 GLY A C     1 
ATOM   13041 O  O     . GLY A 1 3095 ? 215.491 186.008 230.978 1.00 4.03  ? 3095 GLY A O     1 
ATOM   13042 N  N     . ASP A 1 3096 ? 214.796 183.992 231.692 1.00 2.08  ? 3096 ASP A N     1 
ATOM   13043 C  CA    . ASP A 1 3096 ? 214.690 184.360 233.094 1.00 2.05  ? 3096 ASP A CA    1 
ATOM   13044 C  C     . ASP A 1 3096 ? 215.886 183.807 233.858 1.00 1.64  ? 3096 ASP A C     1 
ATOM   13045 O  O     . ASP A 1 3096 ? 216.587 182.907 233.391 1.00 2.68  ? 3096 ASP A O     1 
ATOM   13046 C  CB    . ASP A 1 3096 ? 213.383 183.832 233.691 1.00 2.70  ? 3096 ASP A CB    1 
ATOM   13047 C  CG    . ASP A 1 3096 ? 212.981 184.555 234.961 1.00 6.78  ? 3096 ASP A CG    1 
ATOM   13048 O  OD1   . ASP A 1 3096 ? 213.835 185.239 235.562 1.00 4.09  ? 3096 ASP A OD1   1 
ATOM   13049 O  OD2   . ASP A 1 3096 ? 211.807 184.437 235.362 1.00 10.58 ? 3096 ASP A OD2   1 
ATOM   13050 N  N     . TRP A 1 3097 ? 216.125 184.371 235.041 1.00 1.52  ? 3097 TRP A N     1 
ATOM   13051 C  CA    . TRP A 1 3097 ? 217.180 183.857 235.903 1.00 1.08  ? 3097 TRP A CA    1 
ATOM   13052 C  C     . TRP A 1 3097 ? 216.846 182.438 236.345 1.00 2.29  ? 3097 TRP A C     1 
ATOM   13053 O  O     . TRP A 1 3097 ? 215.720 182.151 236.760 1.00 4.99  ? 3097 TRP A O     1 
ATOM   13054 C  CB    . TRP A 1 3097 ? 217.367 184.759 237.123 1.00 0.74  ? 3097 TRP A CB    1 
ATOM   13055 C  CG    . TRP A 1 3097 ? 218.053 186.055 236.827 1.00 0.53  ? 3097 TRP A CG    1 
ATOM   13056 C  CD1   . TRP A 1 3097 ? 218.368 186.553 235.599 1.00 0.56  ? 3097 TRP A CD1   1 
ATOM   13057 C  CD2   . TRP A 1 3097 ? 218.515 187.019 237.780 1.00 0.58  ? 3097 TRP A CD2   1 
ATOM   13058 N  NE1   . TRP A 1 3097 ? 218.992 187.768 235.726 1.00 0.47  ? 3097 TRP A NE1   1 
ATOM   13059 C  CE2   . TRP A 1 3097 ? 219.095 188.078 237.055 1.00 0.55  ? 3097 TRP A CE2   1 
ATOM   13060 C  CE3   . TRP A 1 3097 ? 218.490 187.092 239.176 1.00 0.48  ? 3097 TRP A CE3   1 
ATOM   13061 C  CZ2   . TRP A 1 3097 ? 219.649 189.194 237.678 1.00 0.87  ? 3097 TRP A CZ2   1 
ATOM   13062 C  CZ3   . TRP A 1 3097 ? 219.040 188.201 239.792 1.00 1.13  ? 3097 TRP A CZ3   1 
ATOM   13063 C  CH2   . TRP A 1 3097 ? 219.613 189.237 239.044 1.00 0.55  ? 3097 TRP A CH2   1 
ATOM   13064 N  N     . SER A 1 3098 ? 217.829 181.552 236.254 1.00 2.09  ? 3098 SER A N     1 
ATOM   13065 C  CA    . SER A 1 3098 ? 217.620 180.163 236.620 1.00 2.47  ? 3098 SER A CA    1 
ATOM   13066 C  C     . SER A 1 3098 ? 217.669 179.992 238.137 1.00 2.63  ? 3098 SER A C     1 
ATOM   13067 O  O     . SER A 1 3098 ? 217.936 180.932 238.891 1.00 2.25  ? 3098 SER A O     1 
ATOM   13068 C  CB    . SER A 1 3098 ? 218.663 179.274 235.947 1.00 2.07  ? 3098 SER A CB    1 
ATOM   13069 O  OG    . SER A 1 3098 ? 219.969 179.608 236.380 1.00 4.16  ? 3098 SER A OG    1 
ATOM   13070 N  N     . THR A 1 3099 ? 217.401 178.764 238.580 1.00 3.04  ? 3099 THR A N     1 
ATOM   13071 C  CA    . THR A 1 3099 ? 217.531 178.447 239.999 1.00 1.63  ? 3099 THR A CA    1 
ATOM   13072 C  C     . THR A 1 3099 ? 218.976 178.601 240.456 1.00 3.04  ? 3099 THR A C     1 
ATOM   13073 O  O     . THR A 1 3099 ? 219.239 179.063 241.572 1.00 4.40  ? 3099 THR A O     1 
ATOM   13074 C  CB    . THR A 1 3099 ? 217.025 177.029 240.266 1.00 2.06  ? 3099 THR A CB    1 
ATOM   13075 O  OG1   . THR A 1 3099 ? 215.632 176.952 239.940 1.00 4.70  ? 3099 THR A OG1   1 
ATOM   13076 C  CG2   . THR A 1 3099 ? 217.212 176.652 241.725 1.00 4.15  ? 3099 THR A CG2   1 
ATOM   13077 N  N     . GLU A 1 3100 ? 219.927 178.224 239.599 1.00 3.75  ? 3100 GLU A N     1 
ATOM   13078 C  CA    . GLU A 1 3100 ? 221.337 178.424 239.914 1.00 5.20  ? 3100 GLU A CA    1 
ATOM   13079 C  C     . GLU A 1 3100 ? 221.665 179.903 240.053 1.00 4.92  ? 3100 GLU A C     1 
ATOM   13080 O  O     . GLU A 1 3100 ? 222.400 180.301 240.964 1.00 5.31  ? 3100 GLU A O     1 
ATOM   13081 C  CB    . GLU A 1 3100 ? 222.207 177.786 238.832 1.00 9.13  ? 3100 GLU A CB    1 
ATOM   13082 C  CG    . GLU A 1 3100 ? 223.695 177.864 239.096 1.00 12.46 ? 3100 GLU A CG    1 
ATOM   13083 C  CD    . GLU A 1 3100 ? 224.502 177.177 238.016 1.00 26.10 ? 3100 GLU A CD    1 
ATOM   13084 O  OE1   . GLU A 1 3100 ? 223.890 176.663 237.056 1.00 26.93 ? 3100 GLU A OE1   1 
ATOM   13085 O  OE2   . GLU A 1 3100 ? 225.746 177.149 238.122 1.00 25.85 ? 3100 GLU A OE2   1 
ATOM   13086 N  N     . ALA A 1 3101 ? 221.136 180.733 239.149 1.00 3.12  ? 3101 ALA A N     1 
ATOM   13087 C  CA    . ALA A 1 3101 ? 221.384 182.168 239.228 1.00 3.44  ? 3101 ALA A CA    1 
ATOM   13088 C  C     . ALA A 1 3101 ? 220.787 182.761 240.496 1.00 3.41  ? 3101 ALA A C     1 
ATOM   13089 O  O     . ALA A 1 3101 ? 221.431 183.571 241.171 1.00 2.50  ? 3101 ALA A O     1 
ATOM   13090 C  CB    . ALA A 1 3101 ? 220.822 182.866 237.991 1.00 2.27  ? 3101 ALA A CB    1 
ATOM   13091 N  N     . LEU A 1 3102 ? 219.561 182.358 240.842 1.00 2.50  ? 3102 LEU A N     1 
ATOM   13092 C  CA    . LEU A 1 3102 ? 218.919 182.862 242.052 1.00 0.70  ? 3102 LEU A CA    1 
ATOM   13093 C  C     . LEU A 1 3102 ? 219.723 182.499 243.294 1.00 1.82  ? 3102 LEU A C     1 
ATOM   13094 O  O     . LEU A 1 3102 ? 219.904 183.325 244.195 1.00 2.80  ? 3102 LEU A O     1 
ATOM   13095 C  CB    . LEU A 1 3102 ? 217.495 182.315 242.155 1.00 0.73  ? 3102 LEU A CB    1 
ATOM   13096 C  CG    . LEU A 1 3102 ? 216.455 182.829 241.160 1.00 0.83  ? 3102 LEU A CG    1 
ATOM   13097 C  CD1   . LEU A 1 3102 ? 215.163 182.047 241.293 1.00 0.59  ? 3102 LEU A CD1   1 
ATOM   13098 C  CD2   . LEU A 1 3102 ? 216.201 184.311 241.368 1.00 0.13  ? 3102 LEU A CD2   1 
ATOM   13099 N  N     . TYR A 1 3103 ? 220.215 181.260 243.358 1.00 1.48  ? 3103 TYR A N     1 
ATOM   13100 C  CA    . TYR A 1 3103 ? 220.992 180.827 244.512 1.00 1.46  ? 3103 TYR A CA    1 
ATOM   13101 C  C     . TYR A 1 3103 ? 222.299 181.601 244.624 1.00 1.85  ? 3103 TYR A C     1 
ATOM   13102 O  O     . TYR A 1 3103 ? 222.701 182.008 245.720 1.00 2.49  ? 3103 TYR A O     1 
ATOM   13103 C  CB    . TYR A 1 3103 ? 221.260 179.323 244.430 1.00 2.27  ? 3103 TYR A CB    1 
ATOM   13104 C  CG    . TYR A 1 3103 ? 221.956 178.768 245.650 1.00 2.66  ? 3103 TYR A CG    1 
ATOM   13105 C  CD1   . TYR A 1 3103 ? 221.230 178.311 246.740 1.00 3.16  ? 3103 TYR A CD1   1 
ATOM   13106 C  CD2   . TYR A 1 3103 ? 223.340 178.698 245.708 1.00 2.41  ? 3103 TYR A CD2   1 
ATOM   13107 C  CE1   . TYR A 1 3103 ? 221.865 177.807 247.855 1.00 5.30  ? 3103 TYR A CE1   1 
ATOM   13108 C  CE2   . TYR A 1 3103 ? 223.982 178.196 246.818 1.00 3.82  ? 3103 TYR A CE2   1 
ATOM   13109 C  CZ    . TYR A 1 3103 ? 223.241 177.750 247.888 1.00 7.88  ? 3103 TYR A CZ    1 
ATOM   13110 O  OH    . TYR A 1 3103 ? 223.881 177.248 248.995 1.00 16.23 ? 3103 TYR A OH    1 
ATOM   13111 N  N     . GLN A 1 3104 ? 222.985 181.804 243.499 1.00 3.86  ? 3104 GLN A N     1 
ATOM   13112 C  CA    . GLN A 1 3104 ? 224.257 182.517 243.531 1.00 2.61  ? 3104 GLN A CA    1 
ATOM   13113 C  C     . GLN A 1 3104 ? 224.055 183.978 243.909 1.00 1.55  ? 3104 GLN A C     1 
ATOM   13114 O  O     . GLN A 1 3104 ? 224.844 184.546 244.672 1.00 2.66  ? 3104 GLN A O     1 
ATOM   13115 C  CB    . GLN A 1 3104 ? 224.963 182.386 242.181 1.00 2.82  ? 3104 GLN A CB    1 
ATOM   13116 C  CG    . GLN A 1 3104 ? 225.410 180.968 241.873 1.00 3.42  ? 3104 GLN A CG    1 
ATOM   13117 C  CD    . GLN A 1 3104 ? 226.090 180.839 240.526 1.00 10.19 ? 3104 GLN A CD    1 
ATOM   13118 O  OE1   . GLN A 1 3104 ? 226.184 181.804 239.769 1.00 11.50 ? 3104 GLN A OE1   1 
ATOM   13119 N  NE2   . GLN A 1 3104 ? 226.566 179.640 240.217 1.00 6.58  ? 3104 GLN A NE2   1 
ATOM   13120 N  N     . VAL A 1 3105 ? 222.997 184.601 243.389 1.00 1.28  ? 3105 VAL A N     1 
ATOM   13121 C  CA    . VAL A 1 3105 ? 222.682 185.974 243.778 1.00 1.37  ? 3105 VAL A CA    1 
ATOM   13122 C  C     . VAL A 1 3105 ? 222.359 186.037 245.264 1.00 2.05  ? 3105 VAL A C     1 
ATOM   13123 O  O     . VAL A 1 3105 ? 222.843 186.914 245.987 1.00 6.58  ? 3105 VAL A O     1 
ATOM   13124 C  CB    . VAL A 1 3105 ? 221.525 186.525 242.926 1.00 1.47  ? 3105 VAL A CB    1 
ATOM   13125 C  CG1   . VAL A 1 3105 ? 221.054 187.860 243.474 1.00 1.13  ? 3105 VAL A CG1   1 
ATOM   13126 C  CG2   . VAL A 1 3105 ? 221.955 186.673 241.489 1.00 1.29  ? 3105 VAL A CG2   1 
ATOM   13127 N  N     . GLY A 1 3106 ? 221.543 185.098 245.741 1.00 1.64  ? 3106 GLY A N     1 
ATOM   13128 C  CA    . GLY A 1 3106 ? 221.185 185.090 247.149 1.00 2.08  ? 3106 GLY A CA    1 
ATOM   13129 C  C     . GLY A 1 3106 ? 222.377 184.857 248.057 1.00 1.98  ? 3106 GLY A C     1 
ATOM   13130 O  O     . GLY A 1 3106 ? 222.555 185.555 249.057 1.00 5.64  ? 3106 GLY A O     1 
ATOM   13131 N  N     . LYS A 1 3107 ? 223.210 183.870 247.723 1.00 1.64  ? 3107 LYS A N     1 
ATOM   13132 C  CA    . LYS A 1 3107 ? 224.367 183.577 248.561 1.00 3.09  ? 3107 LYS A CA    1 
ATOM   13133 C  C     . LYS A 1 3107 ? 225.368 184.723 248.540 1.00 5.26  ? 3107 LYS A C     1 
ATOM   13134 O  O     . LYS A 1 3107 ? 225.946 185.075 249.575 1.00 11.53 ? 3107 LYS A O     1 
ATOM   13135 C  CB    . LYS A 1 3107 ? 225.030 182.271 248.118 1.00 3.23  ? 3107 LYS A CB    1 
ATOM   13136 C  CG    . LYS A 1 3107 ? 226.223 181.867 248.971 1.00 8.74  ? 3107 LYS A CG    1 
ATOM   13137 C  CD    . LYS A 1 3107 ? 226.769 180.500 248.578 1.00 14.98 ? 3107 LYS A CD    1 
ATOM   13138 C  CE    . LYS A 1 3107 ? 227.514 180.556 247.253 1.00 17.04 ? 3107 LYS A CE    1 
ATOM   13139 N  NZ    . LYS A 1 3107 ? 228.152 179.256 246.914 1.00 23.24 ? 3107 LYS A NZ    1 
ATOM   13140 N  N     . GLU A 1 3108 ? 225.588 185.320 247.367 1.00 7.40  ? 3108 GLU A N     1 
ATOM   13141 C  CA    . GLU A 1 3108 ? 226.523 186.433 247.270 1.00 10.33 ? 3108 GLU A CA    1 
ATOM   13142 C  C     . GLU A 1 3108 ? 225.999 187.665 248.000 1.00 8.53  ? 3108 GLU A C     1 
ATOM   13143 O  O     . GLU A 1 3108 ? 226.762 188.363 248.675 1.00 12.19 ? 3108 GLU A O     1 
ATOM   13144 C  CB    . GLU A 1 3108 ? 226.800 186.754 245.800 1.00 10.86 ? 3108 GLU A CB    1 
ATOM   13145 C  CG    . GLU A 1 3108 ? 227.770 187.904 245.574 1.00 14.71 ? 3108 GLU A CG    1 
ATOM   13146 C  CD    . GLU A 1 3108 ? 229.194 187.580 245.993 1.00 23.13 ? 3108 GLU A CD    1 
ATOM   13147 O  OE1   . GLU A 1 3108 ? 229.456 186.438 246.429 1.00 22.23 ? 3108 GLU A OE1   1 
ATOM   13148 O  OE2   . GLU A 1 3108 ? 230.055 188.478 245.892 1.00 25.35 ? 3108 GLU A OE2   1 
ATOM   13149 N  N     . PHE A 1 3109 ? 224.699 187.942 247.879 1.00 6.20  ? 3109 PHE A N     1 
ATOM   13150 C  CA    . PHE A 1 3109 ? 224.143 189.159 248.460 1.00 6.04  ? 3109 PHE A CA    1 
ATOM   13151 C  C     . PHE A 1 3109 ? 223.995 189.048 249.974 1.00 5.79  ? 3109 PHE A C     1 
ATOM   13152 O  O     . PHE A 1 3109 ? 223.997 190.070 250.669 1.00 9.91  ? 3109 PHE A O     1 
ATOM   13153 C  CB    . PHE A 1 3109 ? 222.799 189.477 247.802 1.00 4.43  ? 3109 PHE A CB    1 
ATOM   13154 C  CG    . PHE A 1 3109 ? 222.262 190.841 248.131 1.00 5.25  ? 3109 PHE A CG    1 
ATOM   13155 C  CD1   . PHE A 1 3109 ? 221.465 191.043 249.244 1.00 3.33  ? 3109 PHE A CD1   1 
ATOM   13156 C  CD2   . PHE A 1 3109 ? 222.555 191.925 247.317 1.00 2.86  ? 3109 PHE A CD2   1 
ATOM   13157 C  CE1   . PHE A 1 3109 ? 220.973 192.296 249.543 1.00 1.29  ? 3109 PHE A CE1   1 
ATOM   13158 C  CE2   . PHE A 1 3109 ? 222.066 193.182 247.612 1.00 1.63  ? 3109 PHE A CE2   1 
ATOM   13159 C  CZ    . PHE A 1 3109 ? 221.272 193.367 248.726 1.00 3.41  ? 3109 PHE A CZ    1 
ATOM   13160 N  N     . THR A 1 3110 ? 223.873 187.832 250.503 1.00 6.94  ? 3110 THR A N     1 
ATOM   13161 C  CA    . THR A 1 3110 ? 223.708 187.617 251.934 1.00 7.77  ? 3110 THR A CA    1 
ATOM   13162 C  C     . THR A 1 3110 ? 225.021 187.305 252.643 1.00 9.36  ? 3110 THR A C     1 
ATOM   13163 O  O     . THR A 1 3110 ? 224.999 186.776 253.758 1.00 11.55 ? 3110 THR A O     1 
ATOM   13164 C  CB    . THR A 1 3110 ? 222.703 186.492 252.193 1.00 6.05  ? 3110 THR A CB    1 
ATOM   13165 O  OG1   . THR A 1 3110 ? 223.140 185.294 251.538 1.00 9.26  ? 3110 THR A OG1   1 
ATOM   13166 C  CG2   . THR A 1 3110 ? 221.331 186.876 251.664 1.00 3.79  ? 3110 THR A CG2   1 
ATOM   13167 N  N     . SER A 1 3111 ? 226.162 187.601 252.019 1.00 12.13 ? 3111 SER A N     1 
ATOM   13168 C  CA    . SER A 1 3111 ? 227.443 187.378 252.681 1.00 9.04  ? 3111 SER A CA    1 
ATOM   13169 C  C     . SER A 1 3111 ? 227.594 188.279 253.901 1.00 10.50 ? 3111 SER A C     1 
ATOM   13170 O  O     . SER A 1 3111 ? 228.098 187.852 254.946 1.00 12.30 ? 3111 SER A O     1 
ATOM   13171 C  CB    . SER A 1 3111 ? 228.587 187.600 251.693 1.00 14.08 ? 3111 SER A CB    1 
ATOM   13172 O  OG    . SER A 1 3111 ? 228.453 186.755 250.564 1.00 21.74 ? 3111 SER A OG    1 
ATOM   13173 N  N     . LYS A 1 3112 ? 227.162 189.538 253.782 1.00 12.82 ? 3112 LYS A N     1 
ATOM   13174 C  CA    . LYS A 1 3112 ? 227.193 190.453 254.920 1.00 10.95 ? 3112 LYS A CA    1 
ATOM   13175 C  C     . LYS A 1 3112 ? 226.286 189.977 256.046 1.00 10.93 ? 3112 LYS A C     1 
ATOM   13176 O  O     . LYS A 1 3112 ? 226.518 190.307 257.213 1.00 10.79 ? 3112 LYS A O     1 
ATOM   13177 C  CB    . LYS A 1 3112 ? 226.779 191.853 254.470 1.00 18.44 ? 3112 LYS A CB    1 
ATOM   13178 C  CG    . LYS A 1 3112 ? 225.470 191.873 253.696 1.00 17.53 ? 3112 LYS A CG    1 
ATOM   13179 C  CD    . LYS A 1 3112 ? 225.170 193.244 253.110 1.00 23.25 ? 3112 LYS A CD    1 
ATOM   13180 C  CE    . LYS A 1 3112 ? 223.907 193.207 252.260 1.00 20.63 ? 3112 LYS A CE    1 
ATOM   13181 N  NZ    . LYS A 1 3112 ? 223.598 194.524 251.644 1.00 16.50 ? 3112 LYS A NZ    1 
ATOM   13182 N  N     . MET A 1 3113 ? 225.249 189.219 255.707 1.00 16.55 ? 3113 MET A N     1 
ATOM   13183 C  CA    . MET A 1 3113 ? 224.305 188.708 256.689 1.00 10.00 ? 3113 MET A CA    1 
ATOM   13184 C  C     . MET A 1 3113 ? 225.004 187.759 257.657 1.00 12.93 ? 3113 MET A C     1 
ATOM   13185 O  O     . MET A 1 3113 ? 225.917 187.018 257.285 1.00 15.33 ? 3113 MET A O     1 
ATOM   13186 C  CB    . MET A 1 3113 ? 223.175 187.980 255.963 1.00 10.42 ? 3113 MET A CB    1 
ATOM   13187 C  CG    . MET A 1 3113 ? 222.169 188.888 255.277 1.00 8.02  ? 3113 MET A CG    1 
ATOM   13188 S  SD    . MET A 1 3113 ? 220.649 188.011 254.879 1.00 26.88 ? 3113 MET A SD    1 
ATOM   13189 C  CE    . MET A 1 3113 ? 219.497 188.759 255.998 1.00 2.51  ? 3113 MET A CE    1 
ATOM   13190 N  N     . ASP A 1 3114 ? 224.569 187.790 258.917 1.00 16.03 ? 3114 ASP A N     1 
ATOM   13191 C  CA    . ASP A 1 3114 ? 225.086 186.883 259.939 1.00 13.07 ? 3114 ASP A CA    1 
ATOM   13192 C  C     . ASP A 1 3114 ? 224.101 185.727 260.084 1.00 14.48 ? 3114 ASP A C     1 
ATOM   13193 O  O     . ASP A 1 3114 ? 223.300 185.661 261.017 1.00 21.37 ? 3114 ASP A O     1 
ATOM   13194 C  CB    . ASP A 1 3114 ? 225.311 187.618 261.257 1.00 16.90 ? 3114 ASP A CB    1 
ATOM   13195 C  CG    . ASP A 1 3114 ? 225.797 186.699 262.359 1.00 27.93 ? 3114 ASP A CG    1 
ATOM   13196 O  OD1   . ASP A 1 3114 ? 226.794 185.980 262.138 1.00 34.89 ? 3114 ASP A OD1   1 
ATOM   13197 O  OD2   . ASP A 1 3114 ? 225.184 186.695 263.448 1.00 35.12 ? 3114 ASP A OD2   1 
ATOM   13198 N  N     . LEU A 1 3115 ? 224.169 184.798 259.130 1.00 16.47 ? 3115 LEU A N     1 
ATOM   13199 C  CA    . LEU A 1 3115 ? 223.256 183.668 259.061 1.00 10.54 ? 3115 LEU A CA    1 
ATOM   13200 C  C     . LEU A 1 3115 ? 223.883 182.376 259.566 1.00 13.60 ? 3115 LEU A C     1 
ATOM   13201 O  O     . LEU A 1 3115 ? 223.430 181.287 259.196 1.00 19.51 ? 3115 LEU A O     1 
ATOM   13202 C  CB    . LEU A 1 3115 ? 222.759 183.482 257.627 1.00 9.19  ? 3115 LEU A CB    1 
ATOM   13203 C  CG    . LEU A 1 3115 ? 222.082 184.699 256.999 1.00 12.35 ? 3115 LEU A CG    1 
ATOM   13204 C  CD1   . LEU A 1 3115 ? 221.644 184.395 255.575 1.00 8.49  ? 3115 LEU A CD1   1 
ATOM   13205 C  CD2   . LEU A 1 3115 ? 220.904 185.155 257.845 1.00 10.25 ? 3115 LEU A CD2   1 
ATOM   13206 N  N     . GLU A 1 3116 ? 224.908 182.469 260.404 1.00 16.88 ? 3116 GLU A N     1 
ATOM   13207 C  CA    . GLU A 1 3116 ? 225.616 181.293 260.891 1.00 17.74 ? 3116 GLU A CA    1 
ATOM   13208 C  C     . GLU A 1 3116 ? 224.937 180.774 262.153 1.00 19.30 ? 3116 GLU A C     1 
ATOM   13209 O  O     . GLU A 1 3116 ? 224.885 181.471 263.171 1.00 25.53 ? 3116 GLU A O     1 
ATOM   13210 C  CB    . GLU A 1 3116 ? 227.084 181.621 261.161 1.00 16.44 ? 3116 GLU A CB    1 
ATOM   13211 C  CG    . GLU A 1 3116 ? 227.908 181.933 259.911 1.00 22.28 ? 3116 GLU A CG    1 
ATOM   13212 C  CD    . GLU A 1 3116 ? 228.054 180.756 258.952 1.00 27.94 ? 3116 GLU A CD    1 
ATOM   13213 O  OE1   . GLU A 1 3116 ? 228.691 180.938 257.894 1.00 26.68 ? 3116 GLU A OE1   1 
ATOM   13214 O  OE2   . GLU A 1 3116 ? 227.566 179.647 259.256 1.00 26.06 ? 3116 GLU A OE2   1 
ATOM   13215 N  N     . LYS A 1 3117 ? 224.406 179.555 262.077 1.00 20.71 ? 3117 LYS A N     1 
ATOM   13216 C  CA    . LYS A 1 3117 ? 223.799 178.876 263.221 1.00 19.46 ? 3117 LYS A CA    1 
ATOM   13217 C  C     . LYS A 1 3117 ? 224.450 177.506 263.335 1.00 21.75 ? 3117 LYS A C     1 
ATOM   13218 O  O     . LYS A 1 3117 ? 223.996 176.536 262.712 1.00 20.14 ? 3117 LYS A O     1 
ATOM   13219 C  CB    . LYS A 1 3117 ? 222.281 178.768 263.071 1.00 17.46 ? 3117 LYS A CB    1 
ATOM   13220 C  CG    . LYS A 1 3117 ? 221.589 178.190 264.294 1.00 18.18 ? 3117 LYS A CG    1 
ATOM   13221 C  CD    . LYS A 1 3117 ? 220.089 178.444 264.282 1.00 15.71 ? 3117 LYS A CD    1 
ATOM   13222 C  CE    . LYS A 1 3117 ? 219.410 177.725 263.135 1.00 18.64 ? 3117 LYS A CE    1 
ATOM   13223 N  NZ    . LYS A 1 3117 ? 217.941 177.955 263.120 1.00 20.88 ? 3117 LYS A NZ    1 
ATOM   13224 N  N     . PRO A 1 3118 ? 225.529 177.390 264.115 1.00 22.86 ? 3118 PRO A N     1 
ATOM   13225 C  CA    . PRO A 1 3118 ? 226.217 176.093 264.226 1.00 21.71 ? 3118 PRO A CA    1 
ATOM   13226 C  C     . PRO A 1 3118 ? 225.346 174.985 264.791 1.00 24.46 ? 3118 PRO A C     1 
ATOM   13227 O  O     . PRO A 1 3118 ? 225.607 173.807 264.521 1.00 26.25 ? 3118 PRO A O     1 
ATOM   13228 C  CB    . PRO A 1 3118 ? 227.401 176.407 265.153 1.00 18.17 ? 3118 PRO A CB    1 
ATOM   13229 C  CG    . PRO A 1 3118 ? 226.978 177.629 265.905 1.00 20.35 ? 3118 PRO A CG    1 
ATOM   13230 C  CD    . PRO A 1 3118 ? 226.176 178.429 264.929 1.00 21.76 ? 3118 PRO A CD    1 
ATOM   13231 N  N     . ASN A 1 3119 ? 224.319 175.326 265.565 1.00 22.53 ? 3119 ASN A N     1 
ATOM   13232 C  CA    . ASN A 1 3119 ? 223.438 174.335 266.168 1.00 17.70 ? 3119 ASN A CA    1 
ATOM   13233 C  C     . ASN A 1 3119 ? 222.294 173.915 265.254 1.00 23.34 ? 3119 ASN A C     1 
ATOM   13234 O  O     . ASN A 1 3119 ? 221.435 173.141 265.689 1.00 28.02 ? 3119 ASN A O     1 
ATOM   13235 C  CB    . ASN A 1 3119 ? 222.875 174.871 267.487 1.00 20.75 ? 3119 ASN A CB    1 
ATOM   13236 C  CG    . ASN A 1 3119 ? 222.096 176.160 267.310 1.00 24.98 ? 3119 ASN A CG    1 
ATOM   13237 O  OD1   . ASN A 1 3119 ? 221.009 176.171 266.733 1.00 24.39 ? 3119 ASN A OD1   1 
ATOM   13238 N  ND2   . ASN A 1 3119 ? 222.652 177.257 267.810 1.00 27.87 ? 3119 ASN A ND2   1 
ATOM   13239 N  N     . TYR A 1 3120 ? 222.253 174.410 264.019 1.00 23.23 ? 3120 TYR A N     1 
ATOM   13240 C  CA    . TYR A 1 3120 ? 221.185 174.053 263.094 1.00 16.54 ? 3120 TYR A CA    1 
ATOM   13241 C  C     . TYR A 1 3120 ? 221.202 172.557 262.802 1.00 16.24 ? 3120 TYR A C     1 
ATOM   13242 O  O     . TYR A 1 3120 ? 222.262 171.955 262.619 1.00 19.84 ? 3120 TYR A O     1 
ATOM   13243 C  CB    . TYR A 1 3120 ? 221.335 174.856 261.800 1.00 16.95 ? 3120 TYR A CB    1 
ATOM   13244 C  CG    . TYR A 1 3120 ? 220.462 174.400 260.651 1.00 13.70 ? 3120 TYR A CG    1 
ATOM   13245 C  CD1   . TYR A 1 3120 ? 219.122 174.749 260.594 1.00 11.16 ? 3120 TYR A CD1   1 
ATOM   13246 C  CD2   . TYR A 1 3120 ? 220.985 173.643 259.612 1.00 12.07 ? 3120 TYR A CD2   1 
ATOM   13247 C  CE1   . TYR A 1 3120 ? 218.322 174.347 259.544 1.00 12.19 ? 3120 TYR A CE1   1 
ATOM   13248 C  CE2   . TYR A 1 3120 ? 220.193 173.233 258.558 1.00 10.68 ? 3120 TYR A CE2   1 
ATOM   13249 C  CZ    . TYR A 1 3120 ? 218.862 173.588 258.528 1.00 13.96 ? 3120 TYR A CZ    1 
ATOM   13250 O  OH    . TYR A 1 3120 ? 218.067 173.185 257.481 1.00 14.77 ? 3120 TYR A OH    1 
ATOM   13251 N  N     . ILE A 1 3121 ? 220.015 171.954 262.769 1.00 14.53 ? 3121 ILE A N     1 
ATOM   13252 C  CA    . ILE A 1 3121 ? 219.858 170.534 262.470 1.00 15.15 ? 3121 ILE A CA    1 
ATOM   13253 C  C     . ILE A 1 3121 ? 219.291 170.397 261.066 1.00 14.57 ? 3121 ILE A C     1 
ATOM   13254 O  O     . ILE A 1 3121 ? 218.258 170.997 260.744 1.00 18.57 ? 3121 ILE A O     1 
ATOM   13255 C  CB    . ILE A 1 3121 ? 218.944 169.828 263.489 1.00 18.07 ? 3121 ILE A CB    1 
ATOM   13256 C  CG1   . ILE A 1 3121 ? 219.528 169.869 264.903 1.00 17.67 ? 3121 ILE A CG1   1 
ATOM   13257 C  CG2   . ILE A 1 3121 ? 218.693 168.388 263.071 1.00 17.61 ? 3121 ILE A CG2   1 
ATOM   13258 C  CD1   . ILE A 1 3121 ? 219.126 171.088 265.701 1.00 16.02 ? 3121 ILE A CD1   1 
ATOM   13259 N  N     . VAL A 1 3122 ? 219.959 169.607 260.232 1.00 15.33 ? 3122 VAL A N     1 
ATOM   13260 C  CA    . VAL A 1 3122 ? 219.472 169.338 258.882 1.00 12.86 ? 3122 VAL A CA    1 
ATOM   13261 C  C     . VAL A 1 3122 ? 218.314 168.355 258.969 1.00 17.35 ? 3122 VAL A C     1 
ATOM   13262 O  O     . VAL A 1 3122 ? 218.475 167.257 259.523 1.00 24.16 ? 3122 VAL A O     1 
ATOM   13263 C  CB    . VAL A 1 3122 ? 220.589 168.800 257.978 1.00 15.55 ? 3122 VAL A CB    1 
ATOM   13264 C  CG1   . VAL A 1 3122 ? 220.032 168.437 256.613 1.00 18.60 ? 3122 VAL A CG1   1 
ATOM   13265 C  CG2   . VAL A 1 3122 ? 221.699 169.821 257.849 1.00 11.59 ? 3122 VAL A CG2   1 
ATOM   13266 N  N     . PRO A 1 3123 ? 217.140 168.698 258.445 1.00 15.22 ? 3123 PRO A N     1 
ATOM   13267 C  CA    . PRO A 1 3123 ? 216.015 167.760 258.484 1.00 16.28 ? 3123 PRO A CA    1 
ATOM   13268 C  C     . PRO A 1 3123 ? 216.265 166.553 257.593 1.00 22.45 ? 3123 PRO A C     1 
ATOM   13269 O  O     . PRO A 1 3123 ? 217.040 166.608 256.636 1.00 28.63 ? 3123 PRO A O     1 
ATOM   13270 C  CB    . PRO A 1 3123 ? 214.840 168.596 257.966 1.00 19.11 ? 3123 PRO A CB    1 
ATOM   13271 C  CG    . PRO A 1 3123 ? 215.481 169.644 257.122 1.00 15.17 ? 3123 PRO A CG    1 
ATOM   13272 C  CD    . PRO A 1 3123 ? 216.777 169.970 257.802 1.00 16.16 ? 3123 PRO A CD    1 
ATOM   13273 N  N     . ASP A 1 3124 ? 215.597 165.448 257.928 1.00 24.03 ? 3124 ASP A N     1 
ATOM   13274 C  CA    . ASP A 1 3124 ? 215.691 164.245 257.108 1.00 26.05 ? 3124 ASP A CA    1 
ATOM   13275 C  C     . ASP A 1 3124 ? 215.177 164.506 255.699 1.00 30.85 ? 3124 ASP A C     1 
ATOM   13276 O  O     . ASP A 1 3124 ? 215.794 164.099 254.709 1.00 34.66 ? 3124 ASP A O     1 
ATOM   13277 C  CB    . ASP A 1 3124 ? 214.920 163.101 257.767 1.00 24.93 ? 3124 ASP A CB    1 
ATOM   13278 C  CG    . ASP A 1 3124 ? 215.412 162.798 259.167 1.00 33.43 ? 3124 ASP A CG    1 
ATOM   13279 O  OD1   . ASP A 1 3124 ? 216.603 162.451 259.318 1.00 32.17 ? 3124 ASP A OD1   1 
ATOM   13280 O  OD2   . ASP A 1 3124 ? 214.609 162.906 260.119 1.00 34.30 ? 3124 ASP A OD2   1 
ATOM   13281 N  N     . TYR A 1 3125 ? 214.038 165.187 255.589 1.00 28.01 ? 3125 TYR A N     1 
ATOM   13282 C  CA    . TYR A 1 3125 ? 213.498 165.600 254.296 1.00 27.39 ? 3125 TYR A CA    1 
ATOM   13283 C  C     . TYR A 1 3125 ? 213.754 167.094 254.146 1.00 31.86 ? 3125 TYR A C     1 
ATOM   13284 O  O     . TYR A 1 3125 ? 213.054 167.920 254.737 1.00 27.84 ? 3125 TYR A O     1 
ATOM   13285 C  CB    . TYR A 1 3125 ? 212.015 165.259 254.188 1.00 27.23 ? 3125 TYR A CB    1 
ATOM   13286 C  CG    . TYR A 1 3125 ? 211.320 165.869 252.988 1.00 31.00 ? 3125 TYR A CG    1 
ATOM   13287 C  CD1   . TYR A 1 3125 ? 211.320 165.222 251.759 1.00 27.78 ? 3125 TYR A CD1   1 
ATOM   13288 C  CD2   . TYR A 1 3125 ? 210.641 167.079 253.089 1.00 37.24 ? 3125 TYR A CD2   1 
ATOM   13289 C  CE1   . TYR A 1 3125 ? 210.683 165.771 250.661 1.00 30.49 ? 3125 TYR A CE1   1 
ATOM   13290 C  CE2   . TYR A 1 3125 ? 210.003 167.636 251.997 1.00 30.85 ? 3125 TYR A CE2   1 
ATOM   13291 C  CZ    . TYR A 1 3125 ? 210.026 166.976 250.786 1.00 35.26 ? 3125 TYR A CZ    1 
ATOM   13292 O  OH    . TYR A 1 3125 ? 209.389 167.524 249.697 1.00 39.89 ? 3125 TYR A OH    1 
ATOM   13293 N  N     . MET A 1 3126 ? 214.770 167.439 253.369 1.00 35.18 ? 3126 MET A N     1 
ATOM   13294 C  CA    . MET A 1 3126 ? 215.151 168.825 253.116 1.00 22.21 ? 3126 MET A CA    1 
ATOM   13295 C  C     . MET A 1 3126 ? 214.422 169.338 251.881 1.00 22.09 ? 3126 MET A C     1 
ATOM   13296 O  O     . MET A 1 3126 ? 214.552 168.743 250.804 1.00 19.50 ? 3126 MET A O     1 
ATOM   13297 C  CB    . MET A 1 3126 ? 216.656 168.935 252.914 1.00 19.20 ? 3126 MET A CB    1 
ATOM   13298 C  CG    . MET A 1 3126 ? 217.193 170.354 252.797 1.00 19.54 ? 3126 MET A CG    1 
ATOM   13299 S  SD    . MET A 1 3126 ? 217.032 171.333 254.300 1.00 42.38 ? 3126 MET A SD    1 
ATOM   13300 C  CE    . MET A 1 3126 ? 217.057 172.987 253.620 1.00 11.72 ? 3126 MET A CE    1 
ATOM   13301 N  N     . PRO A 1 3127 ? 213.649 170.420 251.990 1.00 22.31 ? 3127 PRO A N     1 
ATOM   13302 C  CA    . PRO A 1 3127 ? 212.915 170.948 250.827 1.00 14.59 ? 3127 PRO A CA    1 
ATOM   13303 C  C     . PRO A 1 3127 ? 213.841 171.635 249.827 1.00 19.05 ? 3127 PRO A C     1 
ATOM   13304 O  O     . PRO A 1 3127 ? 213.845 172.859 249.673 1.00 18.54 ? 3127 PRO A O     1 
ATOM   13305 C  CB    . PRO A 1 3127 ? 211.921 171.915 251.483 1.00 13.73 ? 3127 PRO A CB    1 
ATOM   13306 C  CG    . PRO A 1 3127 ? 212.632 172.402 252.694 1.00 13.63 ? 3127 PRO A CG    1 
ATOM   13307 C  CD    . PRO A 1 3127 ? 213.453 171.246 253.195 1.00 14.96 ? 3127 PRO A CD    1 
ATOM   13308 N  N     . VAL A 1 3128 ? 214.638 170.827 249.129 1.00 18.68 ? 3128 VAL A N     1 
ATOM   13309 C  CA    . VAL A 1 3128 ? 215.687 171.354 248.266 1.00 18.76 ? 3128 VAL A CA    1 
ATOM   13310 C  C     . VAL A 1 3128 ? 215.082 171.849 246.959 1.00 19.53 ? 3128 VAL A C     1 
ATOM   13311 O  O     . VAL A 1 3128 ? 214.320 171.134 246.294 1.00 17.89 ? 3128 VAL A O     1 
ATOM   13312 C  CB    . VAL A 1 3128 ? 216.753 170.279 248.009 1.00 21.65 ? 3128 VAL A CB    1 
ATOM   13313 C  CG1   . VAL A 1 3128 ? 217.792 170.787 247.034 1.00 16.14 ? 3128 VAL A CG1   1 
ATOM   13314 C  CG2   . VAL A 1 3128 ? 217.402 169.852 249.314 1.00 23.30 ? 3128 VAL A CG2   1 
ATOM   13315 N  N     . VAL A 1 3129 ? 215.422 173.080 246.583 1.00 16.84 ? 3129 VAL A N     1 
ATOM   13316 C  CA    . VAL A 1 3129 ? 215.014 173.629 245.297 1.00 9.45  ? 3129 VAL A CA    1 
ATOM   13317 C  C     . VAL A 1 3129 ? 216.190 173.871 244.361 1.00 10.52 ? 3129 VAL A C     1 
ATOM   13318 O  O     . VAL A 1 3129 ? 215.976 173.986 243.143 1.00 10.75 ? 3129 VAL A O     1 
ATOM   13319 C  CB    . VAL A 1 3129 ? 214.203 174.930 245.478 1.00 13.45 ? 3129 VAL A CB    1 
ATOM   13320 C  CG1   . VAL A 1 3129 ? 212.933 174.656 246.265 1.00 10.12 ? 3129 VAL A CG1   1 
ATOM   13321 C  CG2   . VAL A 1 3129 ? 215.040 175.995 246.156 1.00 6.56  ? 3129 VAL A CG2   1 
ATOM   13322 N  N     . TYR A 1 3130 ? 217.414 173.949 244.873 1.00 14.27 ? 3130 TYR A N     1 
ATOM   13323 C  CA    . TYR A 1 3130 ? 218.619 174.084 244.062 1.00 7.86  ? 3130 TYR A CA    1 
ATOM   13324 C  C     . TYR A 1 3130 ? 219.268 172.711 243.943 1.00 15.58 ? 3130 TYR A C     1 
ATOM   13325 O  O     . TYR A 1 3130 ? 219.691 172.129 244.947 1.00 17.60 ? 3130 TYR A O     1 
ATOM   13326 C  CB    . TYR A 1 3130 ? 219.570 175.099 244.692 1.00 7.83  ? 3130 TYR A CB    1 
ATOM   13327 C  CG    . TYR A 1 3130 ? 220.879 175.284 243.960 1.00 8.02  ? 3130 TYR A CG    1 
ATOM   13328 C  CD1   . TYR A 1 3130 ? 220.934 175.302 242.573 1.00 6.55  ? 3130 TYR A CD1   1 
ATOM   13329 C  CD2   . TYR A 1 3130 ? 222.063 175.440 244.665 1.00 5.96  ? 3130 TYR A CD2   1 
ATOM   13330 C  CE1   . TYR A 1 3130 ? 222.136 175.470 241.911 1.00 8.43  ? 3130 TYR A CE1   1 
ATOM   13331 C  CE2   . TYR A 1 3130 ? 223.264 175.609 244.014 1.00 9.53  ? 3130 TYR A CE2   1 
ATOM   13332 C  CZ    . TYR A 1 3130 ? 223.298 175.622 242.639 1.00 11.58 ? 3130 TYR A CZ    1 
ATOM   13333 O  OH    . TYR A 1 3130 ? 224.502 175.791 241.996 1.00 17.42 ? 3130 TYR A OH    1 
ATOM   13334 N  N     . ASP A 1 3131 ? 219.360 172.201 242.710 1.00 18.82 ? 3131 ASP A N     1 
ATOM   13335 C  CA    . ASP A 1 3131 ? 219.818 170.831 242.501 1.00 17.14 ? 3131 ASP A CA    1 
ATOM   13336 C  C     . ASP A 1 3131 ? 221.231 170.607 243.026 1.00 17.84 ? 3131 ASP A C     1 
ATOM   13337 O  O     . ASP A 1 3131 ? 221.549 169.507 243.493 1.00 25.06 ? 3131 ASP A O     1 
ATOM   13338 C  CB    . ASP A 1 3131 ? 219.747 170.472 241.018 1.00 17.34 ? 3131 ASP A CB    1 
ATOM   13339 C  CG    . ASP A 1 3131 ? 218.324 170.358 240.510 1.00 29.35 ? 3131 ASP A CG    1 
ATOM   13340 O  OD1   . ASP A 1 3131 ? 217.431 170.005 241.308 1.00 29.04 ? 3131 ASP A OD1   1 
ATOM   13341 O  OD2   . ASP A 1 3131 ? 218.098 170.617 239.309 1.00 30.56 ? 3131 ASP A OD2   1 
ATOM   13342 N  N     . LYS A 1 3132 ? 222.088 171.623 242.970 1.00 11.57 ? 3132 LYS A N     1 
ATOM   13343 C  CA    . LYS A 1 3132 ? 223.462 171.488 243.433 1.00 15.48 ? 3132 LYS A CA    1 
ATOM   13344 C  C     . LYS A 1 3132 ? 223.671 172.040 244.837 1.00 15.22 ? 3132 LYS A C     1 
ATOM   13345 O  O     . LYS A 1 3132 ? 224.805 172.374 245.196 1.00 17.53 ? 3132 LYS A O     1 
ATOM   13346 C  CB    . LYS A 1 3132 ? 224.426 172.162 242.457 1.00 14.46 ? 3132 LYS A CB    1 
ATOM   13347 C  CG    . LYS A 1 3132 ? 224.504 171.483 241.103 1.00 16.00 ? 3132 LYS A CG    1 
ATOM   13348 C  CD    . LYS A 1 3132 ? 225.598 172.096 240.245 1.00 19.22 ? 3132 LYS A CD    1 
ATOM   13349 C  CE    . LYS A 1 3132 ? 225.205 173.465 239.720 1.00 23.98 ? 3132 LYS A CE    1 
ATOM   13350 N  NZ    . LYS A 1 3132 ? 226.236 174.008 238.793 1.00 28.86 ? 3132 LYS A NZ    1 
ATOM   13351 N  N     . LEU A 1 3133 ? 222.615 172.153 245.631 1.00 16.63 ? 3133 LEU A N     1 
ATOM   13352 C  CA    . LEU A 1 3133 ? 222.763 172.494 247.038 1.00 13.94 ? 3133 LEU A CA    1 
ATOM   13353 C  C     . LEU A 1 3133 ? 223.513 171.371 247.747 1.00 15.53 ? 3133 LEU A C     1 
ATOM   13354 O  O     . LEU A 1 3133 ? 223.148 170.197 247.583 1.00 24.70 ? 3133 LEU A O     1 
ATOM   13355 C  CB    . LEU A 1 3133 ? 221.397 172.720 247.681 1.00 12.74 ? 3133 LEU A CB    1 
ATOM   13356 C  CG    . LEU A 1 3133 ? 221.368 173.160 249.148 1.00 14.68 ? 3133 LEU A CG    1 
ATOM   13357 C  CD1   . LEU A 1 3133 ? 221.995 174.534 249.310 1.00 8.00  ? 3133 LEU A CD1   1 
ATOM   13358 C  CD2   . LEU A 1 3133 ? 219.949 173.151 249.685 1.00 14.93 ? 3133 LEU A CD2   1 
ATOM   13359 N  N     . PRO A 1 3134 ? 224.561 171.673 248.521 1.00 14.50 ? 3134 PRO A N     1 
ATOM   13360 C  CA    . PRO A 1 3134 ? 225.367 170.607 249.134 1.00 17.62 ? 3134 PRO A CA    1 
ATOM   13361 C  C     . PRO A 1 3134 ? 224.573 169.654 250.014 1.00 24.94 ? 3134 PRO A C     1 
ATOM   13362 O  O     . PRO A 1 3134 ? 223.638 170.063 250.709 1.00 28.76 ? 3134 PRO A O     1 
ATOM   13363 C  CB    . PRO A 1 3134 ? 226.396 171.400 249.944 1.00 16.35 ? 3134 PRO A CB    1 
ATOM   13364 C  CG    . PRO A 1 3134 ? 226.633 172.596 249.084 1.00 11.93 ? 3134 PRO A CG    1 
ATOM   13365 C  CD    . PRO A 1 3134 ? 225.244 172.977 248.604 1.00 12.32 ? 3134 PRO A CD    1 
ATOM   13366 N  N     . GLN A 1 3135 ? 224.948 168.371 249.976 1.00 24.15 ? 3135 GLN A N     1 
ATOM   13367 C  CA    . GLN A 1 3135 ? 224.162 167.329 250.635 1.00 20.90 ? 3135 GLN A CA    1 
ATOM   13368 C  C     . GLN A 1 3135 ? 223.998 167.553 252.134 1.00 24.98 ? 3135 GLN A C     1 
ATOM   13369 O  O     . GLN A 1 3135 ? 222.891 167.314 252.647 1.00 34.41 ? 3135 GLN A O     1 
ATOM   13370 C  CB    . GLN A 1 3135 ? 224.775 165.955 250.339 1.00 28.82 ? 3135 GLN A CB    1 
ATOM   13371 C  CG    . GLN A 1 3135 ? 224.816 165.583 248.864 1.00 30.92 ? 3135 GLN A CG    1 
ATOM   13372 C  CD    . GLN A 1 3135 ? 223.443 165.583 248.225 1.00 36.49 ? 3135 GLN A CD    1 
ATOM   13373 O  OE1   . GLN A 1 3135 ? 222.533 164.890 248.680 1.00 31.66 ? 3135 GLN A OE1   1 
ATOM   13374 N  NE2   . GLN A 1 3135 ? 223.287 166.359 247.157 1.00 36.83 ? 3135 GLN A NE2   1 
ATOM   13375 N  N     . PRO A 1 3136 ? 225.030 167.910 252.899 1.00 23.02 ? 3136 PRO A N     1 
ATOM   13376 C  CA    . PRO A 1 3136 ? 224.804 168.423 254.256 1.00 17.82 ? 3136 PRO A CA    1 
ATOM   13377 C  C     . PRO A 1 3136 ? 224.703 169.938 254.260 1.00 23.86 ? 3136 PRO A C     1 
ATOM   13378 O  O     . PRO A 1 3136 ? 225.695 170.624 254.551 1.00 26.08 ? 3136 PRO A O     1 
ATOM   13379 C  CB    . PRO A 1 3136 ? 226.042 167.940 255.022 1.00 17.89 ? 3136 PRO A CB    1 
ATOM   13380 C  CG    . PRO A 1 3136 ? 227.119 167.849 253.982 1.00 22.41 ? 3136 PRO A CG    1 
ATOM   13381 C  CD    . PRO A 1 3136 ? 226.473 167.793 252.612 1.00 22.13 ? 3136 PRO A CD    1 
ATOM   13382 N  N     . PRO A 1 3137 ? 223.543 170.507 253.928 1.00 20.54 ? 3137 PRO A N     1 
ATOM   13383 C  CA    . PRO A 1 3137 ? 223.457 171.968 253.831 1.00 18.78 ? 3137 PRO A CA    1 
ATOM   13384 C  C     . PRO A 1 3137 ? 223.691 172.622 255.184 1.00 16.63 ? 3137 PRO A C     1 
ATOM   13385 O  O     . PRO A 1 3137 ? 223.333 172.077 256.229 1.00 21.88 ? 3137 PRO A O     1 
ATOM   13386 C  CB    . PRO A 1 3137 ? 222.028 172.205 253.334 1.00 17.21 ? 3137 PRO A CB    1 
ATOM   13387 C  CG    . PRO A 1 3137 ? 221.266 171.063 253.886 1.00 20.42 ? 3137 PRO A CG    1 
ATOM   13388 C  CD    . PRO A 1 3137 ? 222.207 169.886 253.911 1.00 20.73 ? 3137 PRO A CD    1 
ATOM   13389 N  N     . SER A 1 3138 ? 224.309 173.798 255.156 1.00 16.22 ? 3138 SER A N     1 
ATOM   13390 C  CA    . SER A 1 3138 ? 224.463 174.599 256.357 1.00 12.00 ? 3138 SER A CA    1 
ATOM   13391 C  C     . SER A 1 3138 ? 223.229 175.479 256.541 1.00 11.70 ? 3138 SER A C     1 
ATOM   13392 O  O     . SER A 1 3138 ? 222.330 175.515 255.698 1.00 12.77 ? 3138 SER A O     1 
ATOM   13393 C  CB    . SER A 1 3138 ? 225.740 175.433 256.286 1.00 13.81 ? 3138 SER A CB    1 
ATOM   13394 O  OG    . SER A 1 3138 ? 225.633 176.442 255.299 1.00 16.35 ? 3138 SER A OG    1 
ATOM   13395 N  N     . HIS A 1 3139 ? 223.180 176.196 257.666 1.00 15.81 ? 3139 HIS A N     1 
ATOM   13396 C  CA    . HIS A 1 3139 ? 222.038 177.066 257.929 1.00 8.51  ? 3139 HIS A CA    1 
ATOM   13397 C  C     . HIS A 1 3139 ? 221.947 178.185 256.898 1.00 8.22  ? 3139 HIS A C     1 
ATOM   13398 O  O     . HIS A 1 3139 ? 220.852 178.523 256.435 1.00 9.81  ? 3139 HIS A O     1 
ATOM   13399 C  CB    . HIS A 1 3139 ? 222.125 177.640 259.342 1.00 10.10 ? 3139 HIS A CB    1 
ATOM   13400 C  CG    . HIS A 1 3139 ? 221.032 178.610 259.665 1.00 14.43 ? 3139 HIS A CG    1 
ATOM   13401 N  ND1   . HIS A 1 3139 ? 221.259 179.956 259.847 1.00 10.29 ? 3139 HIS A ND1   1 
ATOM   13402 C  CD2   . HIS A 1 3139 ? 219.699 178.428 259.819 1.00 7.89  ? 3139 HIS A CD2   1 
ATOM   13403 C  CE1   . HIS A 1 3139 ? 220.115 180.561 260.112 1.00 10.97 ? 3139 HIS A CE1   1 
ATOM   13404 N  NE2   . HIS A 1 3139 ? 219.153 179.657 260.100 1.00 10.84 ? 3139 HIS A NE2   1 
ATOM   13405 N  N     . ARG A 1 3140 ? 223.088 178.774 256.533 1.00 10.43 ? 3140 ARG A N     1 
ATOM   13406 C  CA    . ARG A 1 3140 ? 223.097 179.783 255.478 1.00 6.38  ? 3140 ARG A CA    1 
ATOM   13407 C  C     . ARG A 1 3140 ? 222.669 179.187 254.144 1.00 5.06  ? 3140 ARG A C     1 
ATOM   13408 O  O     . ARG A 1 3140 ? 221.924 179.815 253.384 1.00 6.83  ? 3140 ARG A O     1 
ATOM   13409 C  CB    . ARG A 1 3140 ? 224.487 180.409 255.371 1.00 7.13  ? 3140 ARG A CB    1 
ATOM   13410 C  CG    . ARG A 1 3140 ? 224.576 181.577 254.410 1.00 6.84  ? 3140 ARG A CG    1 
ATOM   13411 C  CD    . ARG A 1 3140 ? 226.018 182.001 254.210 1.00 3.91  ? 3140 ARG A CD    1 
ATOM   13412 N  NE    . ARG A 1 3140 ? 226.560 182.667 255.389 1.00 7.09  ? 3140 ARG A NE    1 
ATOM   13413 C  CZ    . ARG A 1 3140 ? 226.284 183.916 255.738 1.00 10.20 ? 3140 ARG A CZ    1 
ATOM   13414 N  NH1   . ARG A 1 3140 ? 225.486 184.679 255.009 1.00 9.52  ? 3140 ARG A NH1   1 
ATOM   13415 N  NH2   . ARG A 1 3140 ? 226.822 184.412 256.848 1.00 12.95 ? 3140 ARG A NH2   1 
ATOM   13416 N  N     . GLU A 1 3141 ? 223.134 177.974 253.846 1.00 10.99 ? 3141 GLU A N     1 
ATOM   13417 C  CA    . GLU A 1 3141 ? 222.728 177.297 252.619 1.00 9.43  ? 3141 GLU A CA    1 
ATOM   13418 C  C     . GLU A 1 3141 ? 221.229 177.035 252.604 1.00 7.17  ? 3141 GLU A C     1 
ATOM   13419 O  O     . GLU A 1 3141 ? 220.582 177.144 251.557 1.00 6.59  ? 3141 GLU A O     1 
ATOM   13420 C  CB    . GLU A 1 3141 ? 223.509 175.993 252.478 1.00 8.42  ? 3141 GLU A CB    1 
ATOM   13421 C  CG    . GLU A 1 3141 ? 224.937 176.182 252.014 1.00 11.07 ? 3141 GLU A CG    1 
ATOM   13422 C  CD    . GLU A 1 3141 ? 225.807 174.985 252.333 1.00 24.11 ? 3141 GLU A CD    1 
ATOM   13423 O  OE1   . GLU A 1 3141 ? 225.699 173.970 251.625 1.00 22.37 ? 3141 GLU A OE1   1 
ATOM   13424 O  OE2   . GLU A 1 3141 ? 226.613 175.065 253.282 1.00 25.16 ? 3141 GLU A OE2   1 
ATOM   13425 N  N     . ALA A 1 3142 ? 220.661 176.676 253.757 1.00 7.60  ? 3142 ALA A N     1 
ATOM   13426 C  CA    . ALA A 1 3142 ? 219.219 176.479 253.845 1.00 6.16  ? 3142 ALA A CA    1 
ATOM   13427 C  C     . ALA A 1 3142 ? 218.468 177.794 253.670 1.00 5.58  ? 3142 ALA A C     1 
ATOM   13428 O  O     . ALA A 1 3142 ? 217.409 177.826 253.032 1.00 7.38  ? 3142 ALA A O     1 
ATOM   13429 C  CB    . ALA A 1 3142 ? 218.860 175.825 255.178 1.00 5.29  ? 3142 ALA A CB    1 
ATOM   13430 N  N     . ILE A 1 3143 ? 218.996 178.885 254.231 1.00 3.28  ? 3143 ILE A N     1 
ATOM   13431 C  CA    . ILE A 1 3143 ? 218.327 180.181 254.127 1.00 2.69  ? 3143 ILE A CA    1 
ATOM   13432 C  C     . ILE A 1 3143 ? 218.258 180.633 252.675 1.00 4.17  ? 3143 ILE A C     1 
ATOM   13433 O  O     . ILE A 1 3143 ? 217.197 181.031 252.179 1.00 6.59  ? 3143 ILE A O     1 
ATOM   13434 C  CB    . ILE A 1 3143 ? 219.039 181.226 255.005 1.00 3.18  ? 3143 ILE A CB    1 
ATOM   13435 C  CG1   . ILE A 1 3143 ? 218.731 180.992 256.484 1.00 2.97  ? 3143 ILE A CG1   1 
ATOM   13436 C  CG2   . ILE A 1 3143 ? 218.628 182.633 254.595 1.00 3.18  ? 3143 ILE A CG2   1 
ATOM   13437 C  CD1   . ILE A 1 3143 ? 217.347 181.427 256.891 1.00 2.15  ? 3143 ILE A CD1   1 
ATOM   13438 N  N     . VAL A 1 3144 ? 219.389 180.578 251.970 1.00 5.58  ? 3144 VAL A N     1 
ATOM   13439 C  CA    . VAL A 1 3144 ? 219.411 180.983 250.569 1.00 2.55  ? 3144 VAL A CA    1 
ATOM   13440 C  C     . VAL A 1 3144 ? 218.542 180.052 249.737 1.00 2.32  ? 3144 VAL A C     1 
ATOM   13441 O  O     . VAL A 1 3144 ? 217.848 180.489 248.811 1.00 3.32  ? 3144 VAL A O     1 
ATOM   13442 C  CB    . VAL A 1 3144 ? 220.860 181.033 250.049 1.00 3.30  ? 3144 VAL A CB    1 
ATOM   13443 C  CG1   . VAL A 1 3144 ? 220.886 181.379 248.572 1.00 1.67  ? 3144 VAL A CG1   1 
ATOM   13444 C  CG2   . VAL A 1 3144 ? 221.672 182.041 250.846 1.00 2.52  ? 3144 VAL A CG2   1 
ATOM   13445 N  N     . ASN A 1 3145 ? 218.550 178.758 250.065 1.00 3.49  ? 3145 ASN A N     1 
ATOM   13446 C  CA    . ASN A 1 3145 ? 217.665 177.815 249.391 1.00 3.08  ? 3145 ASN A CA    1 
ATOM   13447 C  C     . ASN A 1 3145 ? 216.205 178.192 249.601 1.00 2.42  ? 3145 ASN A C     1 
ATOM   13448 O  O     . ASN A 1 3145 ? 215.391 178.101 248.675 1.00 2.60  ? 3145 ASN A O     1 
ATOM   13449 C  CB    . ASN A 1 3145 ? 217.934 176.398 249.898 1.00 3.09  ? 3145 ASN A CB    1 
ATOM   13450 C  CG    . ASN A 1 3145 ? 217.270 175.337 249.050 1.00 7.59  ? 3145 ASN A CG    1 
ATOM   13451 O  OD1   . ASN A 1 3145 ? 217.587 175.180 247.873 1.00 14.25 ? 3145 ASN A OD1   1 
ATOM   13452 N  ND2   . ASN A 1 3145 ? 216.340 174.602 249.644 1.00 9.44  ? 3145 ASN A ND2   1 
ATOM   13453 N  N     . SER A 1 3146 ? 215.854 178.618 250.817 1.00 2.60  ? 3146 SER A N     1 
ATOM   13454 C  CA    . SER A 1 3146 ? 214.494 179.076 251.082 1.00 1.88  ? 3146 SER A CA    1 
ATOM   13455 C  C     . SER A 1 3146 ? 214.188 180.365 250.330 1.00 1.27  ? 3146 SER A C     1 
ATOM   13456 O  O     . SER A 1 3146 ? 213.057 180.570 249.876 1.00 0.60  ? 3146 SER A O     1 
ATOM   13457 C  CB    . SER A 1 3146 ? 214.290 179.269 252.584 1.00 3.24  ? 3146 SER A CB    1 
ATOM   13458 O  OG    . SER A 1 3146 ? 214.528 178.064 253.288 1.00 7.96  ? 3146 SER A OG    1 
ATOM   13459 N  N     . CYS A 1 3147 ? 215.180 181.249 250.197 1.00 2.91  ? 3147 CYS A N     1 
ATOM   13460 C  CA    . CYS A 1 3147 ? 214.984 182.472 249.427 1.00 0.74  ? 3147 CYS A CA    1 
ATOM   13461 C  C     . CYS A 1 3147 ? 214.693 182.160 247.966 1.00 0.51  ? 3147 CYS A C     1 
ATOM   13462 O  O     . CYS A 1 3147 ? 213.865 182.825 247.334 1.00 0.45  ? 3147 CYS A O     1 
ATOM   13463 C  CB    . CYS A 1 3147 ? 216.210 183.377 249.550 1.00 0.71  ? 3147 CYS A CB    1 
ATOM   13464 S  SG    . CYS A 1 3147 ? 216.473 184.089 251.188 1.00 4.88  ? 3147 CYS A SG    1 
ATOM   13465 N  N     . VAL A 1 3148 ? 215.372 181.156 247.408 1.00 0.53  ? 3148 VAL A N     1 
ATOM   13466 C  CA    . VAL A 1 3148 ? 215.087 180.739 246.039 1.00 0.44  ? 3148 VAL A CA    1 
ATOM   13467 C  C     . VAL A 1 3148 ? 213.676 180.178 245.941 1.00 0.35  ? 3148 VAL A C     1 
ATOM   13468 O  O     . VAL A 1 3148 ? 212.948 180.455 244.980 1.00 0.37  ? 3148 VAL A O     1 
ATOM   13469 C  CB    . VAL A 1 3148 ? 216.138 179.719 245.556 1.00 0.67  ? 3148 VAL A CB    1 
ATOM   13470 C  CG1   . VAL A 1 3148 ? 215.804 179.231 244.157 1.00 0.96  ? 3148 VAL A CG1   1 
ATOM   13471 C  CG2   . VAL A 1 3148 ? 217.522 180.331 245.590 1.00 0.46  ? 3148 VAL A CG2   1 
ATOM   13472 N  N     . PHE A 1 3149 ? 213.262 179.392 246.938 1.00 0.45  ? 3149 PHE A N     1 
ATOM   13473 C  CA    . PHE A 1 3149 ? 211.937 178.784 246.911 1.00 0.34  ? 3149 PHE A CA    1 
ATOM   13474 C  C     . PHE A 1 3149 ? 210.839 179.840 246.897 1.00 0.43  ? 3149 PHE A C     1 
ATOM   13475 O  O     . PHE A 1 3149 ? 209.830 179.686 246.200 1.00 0.49  ? 3149 PHE A O     1 
ATOM   13476 C  CB    . PHE A 1 3149 ? 211.757 177.852 248.110 1.00 0.57  ? 3149 PHE A CB    1 
ATOM   13477 C  CG    . PHE A 1 3149 ? 210.345 177.371 248.293 1.00 0.80  ? 3149 PHE A CG    1 
ATOM   13478 C  CD1   . PHE A 1 3149 ? 209.875 176.284 247.578 1.00 0.49  ? 3149 PHE A CD1   1 
ATOM   13479 C  CD2   . PHE A 1 3149 ? 209.485 178.009 249.173 1.00 0.77  ? 3149 PHE A CD2   1 
ATOM   13480 C  CE1   . PHE A 1 3149 ? 208.579 175.840 247.738 1.00 0.71  ? 3149 PHE A CE1   1 
ATOM   13481 C  CE2   . PHE A 1 3149 ? 208.186 177.570 249.332 1.00 0.55  ? 3149 PHE A CE2   1 
ATOM   13482 C  CZ    . PHE A 1 3149 ? 207.733 176.484 248.616 1.00 0.72  ? 3149 PHE A CZ    1 
ATOM   13483 N  N     . VAL A 1 3150 ? 211.012 180.913 247.672 1.00 0.38  ? 3150 VAL A N     1 
ATOM   13484 C  CA    . VAL A 1 3150 ? 209.976 181.939 247.772 1.00 0.27  ? 3150 VAL A CA    1 
ATOM   13485 C  C     . VAL A 1 3150 ? 209.736 182.591 246.418 1.00 0.45  ? 3150 VAL A C     1 
ATOM   13486 O  O     . VAL A 1 3150 ? 208.588 182.814 246.014 1.00 1.31  ? 3150 VAL A O     1 
ATOM   13487 C  CB    . VAL A 1 3150 ? 210.356 182.977 248.844 1.00 0.24  ? 3150 VAL A CB    1 
ATOM   13488 C  CG1   . VAL A 1 3150 ? 209.426 184.169 248.782 1.00 0.14  ? 3150 VAL A CG1   1 
ATOM   13489 C  CG2   . VAL A 1 3150 ? 210.326 182.349 250.227 1.00 0.19  ? 3150 VAL A CG2   1 
ATOM   13490 N  N     . HIS A 1 3151 ? 210.814 182.901 245.693 1.00 0.51  ? 3151 HIS A N     1 
ATOM   13491 C  CA    . HIS A 1 3151 ? 210.674 183.513 244.376 1.00 0.19  ? 3151 HIS A CA    1 
ATOM   13492 C  C     . HIS A 1 3151 ? 209.937 182.596 243.410 1.00 0.72  ? 3151 HIS A C     1 
ATOM   13493 O  O     . HIS A 1 3151 ? 209.072 183.047 242.652 1.00 0.87  ? 3151 HIS A O     1 
ATOM   13494 C  CB    . HIS A 1 3151 ? 212.053 183.876 243.823 1.00 0.21  ? 3151 HIS A CB    1 
ATOM   13495 C  CG    . HIS A 1 3151 ? 212.006 184.573 242.500 1.00 0.09  ? 3151 HIS A CG    1 
ATOM   13496 N  ND1   . HIS A 1 3151 ? 211.715 185.913 242.373 1.00 0.06  ? 3151 HIS A ND1   1 
ATOM   13497 C  CD2   . HIS A 1 3151 ? 212.215 184.114 241.245 1.00 0.08  ? 3151 HIS A CD2   1 
ATOM   13498 C  CE1   . HIS A 1 3151 ? 211.744 186.250 241.098 1.00 0.10  ? 3151 HIS A CE1   1 
ATOM   13499 N  NE2   . HIS A 1 3151 ? 212.045 185.175 240.391 1.00 0.24  ? 3151 HIS A NE2   1 
ATOM   13500 N  N     . GLN A 1 3152 ? 210.263 181.303 243.425 1.00 0.80  ? 3152 GLN A N     1 
ATOM   13501 C  CA    . GLN A 1 3152 ? 209.607 180.355 242.534 1.00 1.08  ? 3152 GLN A CA    1 
ATOM   13502 C  C     . GLN A 1 3152 ? 208.144 180.138 242.894 1.00 1.54  ? 3152 GLN A C     1 
ATOM   13503 O  O     . GLN A 1 3152 ? 207.365 179.712 242.035 1.00 2.85  ? 3152 GLN A O     1 
ATOM   13504 C  CB    . GLN A 1 3152 ? 210.359 179.024 242.549 1.00 1.38  ? 3152 GLN A CB    1 
ATOM   13505 C  CG    . GLN A 1 3152 ? 211.857 179.175 242.368 1.00 3.76  ? 3152 GLN A CG    1 
ATOM   13506 C  CD    . GLN A 1 3152 ? 212.498 177.970 241.716 1.00 5.55  ? 3152 GLN A CD    1 
ATOM   13507 O  OE1   . GLN A 1 3152 ? 213.273 178.101 240.769 1.00 7.24  ? 3152 GLN A OE1   1 
ATOM   13508 N  NE2   . GLN A 1 3152 ? 212.186 176.786 242.225 1.00 6.54  ? 3152 GLN A NE2   1 
ATOM   13509 N  N     . THR A 1 3153 ? 207.757 180.418 244.139 1.00 1.16  ? 3153 THR A N     1 
ATOM   13510 C  CA    . THR A 1 3153 ? 206.359 180.286 244.531 1.00 1.34  ? 3153 THR A CA    1 
ATOM   13511 C  C     . THR A 1 3153 ? 205.480 181.313 243.824 1.00 1.56  ? 3153 THR A C     1 
ATOM   13512 O  O     . THR A 1 3153 ? 204.332 181.011 243.478 1.00 2.67  ? 3153 THR A O     1 
ATOM   13513 C  CB    . THR A 1 3153 ? 206.236 180.413 246.053 1.00 1.01  ? 3153 THR A CB    1 
ATOM   13514 O  OG1   . THR A 1 3153 ? 206.817 179.261 246.674 1.00 1.35  ? 3153 THR A OG1   1 
ATOM   13515 C  CG2   . THR A 1 3153 ? 204.786 180.512 246.478 1.00 4.69  ? 3153 THR A CG2   1 
ATOM   13516 N  N     . LEU A 1 3154 ? 206.004 182.517 243.581 1.00 1.05  ? 3154 LEU A N     1 
ATOM   13517 C  CA    . LEU A 1 3154 ? 205.223 183.535 242.887 1.00 1.37  ? 3154 LEU A CA    1 
ATOM   13518 C  C     . LEU A 1 3154 ? 204.906 183.127 241.456 1.00 2.31  ? 3154 LEU A C     1 
ATOM   13519 O  O     . LEU A 1 3154 ? 203.842 183.478 240.934 1.00 4.71  ? 3154 LEU A O     1 
ATOM   13520 C  CB    . LEU A 1 3154 ? 205.952 184.879 242.910 1.00 0.88  ? 3154 LEU A CB    1 
ATOM   13521 C  CG    . LEU A 1 3154 ? 205.769 185.746 244.158 1.00 0.32  ? 3154 LEU A CG    1 
ATOM   13522 C  CD1   . LEU A 1 3154 ? 204.311 186.157 244.310 1.00 0.51  ? 3154 LEU A CD1   1 
ATOM   13523 C  CD2   . LEU A 1 3154 ? 206.276 185.078 245.423 1.00 0.19  ? 3154 LEU A CD2   1 
ATOM   13524 N  N     . HIS A 1 3155 ? 205.815 182.401 240.801 1.00 2.10  ? 3155 HIS A N     1 
ATOM   13525 C  CA    . HIS A 1 3155 ? 205.508 181.867 239.479 1.00 2.51  ? 3155 HIS A CA    1 
ATOM   13526 C  C     . HIS A 1 3155 ? 204.371 180.858 239.546 1.00 3.85  ? 3155 HIS A C     1 
ATOM   13527 O  O     . HIS A 1 3155 ? 203.471 180.866 238.700 1.00 9.38  ? 3155 HIS A O     1 
ATOM   13528 C  CB    . HIS A 1 3155 ? 206.756 181.238 238.863 1.00 2.34  ? 3155 HIS A CB    1 
ATOM   13529 C  CG    . HIS A 1 3155 ? 207.785 182.236 238.438 1.00 2.41  ? 3155 HIS A CG    1 
ATOM   13530 N  ND1   . HIS A 1 3155 ? 209.036 182.305 239.010 1.00 3.06  ? 3155 HIS A ND1   1 
ATOM   13531 C  CD2   . HIS A 1 3155 ? 207.747 183.209 237.498 1.00 2.78  ? 3155 HIS A CD2   1 
ATOM   13532 C  CE1   . HIS A 1 3155 ? 209.726 183.275 238.440 1.00 4.16  ? 3155 HIS A CE1   1 
ATOM   13533 N  NE2   . HIS A 1 3155 ? 208.967 183.840 237.519 1.00 5.66  ? 3155 HIS A NE2   1 
ATOM   13534 N  N     . GLN A 1 3156 ? 204.395 179.980 240.551 1.00 4.89  ? 3156 GLN A N     1 
ATOM   13535 C  CA    . GLN A 1 3156 ? 203.269 179.078 240.771 1.00 6.76  ? 3156 GLN A CA    1 
ATOM   13536 C  C     . GLN A 1 3156 ? 202.009 179.858 241.115 1.00 7.89  ? 3156 GLN A C     1 
ATOM   13537 O  O     . GLN A 1 3156 ? 200.914 179.523 240.649 1.00 12.57 ? 3156 GLN A O     1 
ATOM   13538 C  CB    . GLN A 1 3156 ? 203.602 178.080 241.882 1.00 6.61  ? 3156 GLN A CB    1 
ATOM   13539 C  CG    . GLN A 1 3156 ? 204.930 177.320 241.747 1.00 6.76  ? 3156 GLN A CG    1 
ATOM   13540 C  CD    . GLN A 1 3156 ? 205.057 176.450 240.493 1.00 20.87 ? 3156 GLN A CD    1 
ATOM   13541 O  OE1   . GLN A 1 3156 ? 204.531 176.762 239.425 1.00 15.97 ? 3156 GLN A OE1   1 
ATOM   13542 N  NE2   . GLN A 1 3156 ? 205.772 175.341 240.636 1.00 23.60 ? 3156 GLN A NE2   1 
ATOM   13543 N  N     . ALA A 1 3157 ? 202.148 180.904 241.932 1.00 8.49  ? 3157 ALA A N     1 
ATOM   13544 C  CA    . ALA A 1 3157 ? 200.996 181.708 242.323 1.00 7.96  ? 3157 ALA A CA    1 
ATOM   13545 C  C     . ALA A 1 3157 ? 200.375 182.413 241.126 1.00 8.77  ? 3157 ALA A C     1 
ATOM   13546 O  O     . ALA A 1 3157 ? 199.147 182.457 240.994 1.00 9.76  ? 3157 ALA A O     1 
ATOM   13547 C  CB    . ALA A 1 3157 ? 201.408 182.721 243.393 1.00 3.53  ? 3157 ALA A CB    1 
ATOM   13548 N  N     . ASN A 1 3158 ? 201.202 182.976 240.241 1.00 8.74  ? 3158 ASN A N     1 
ATOM   13549 C  CA    . ASN A 1 3158 ? 200.665 183.618 239.046 1.00 6.76  ? 3158 ASN A CA    1 
ATOM   13550 C  C     . ASN A 1 3158 ? 199.954 182.612 238.152 1.00 10.20 ? 3158 ASN A C     1 
ATOM   13551 O  O     . ASN A 1 3158 ? 198.914 182.923 237.562 1.00 13.59 ? 3158 ASN A O     1 
ATOM   13552 C  CB    . ASN A 1 3158 ? 201.776 184.326 238.272 1.00 5.30  ? 3158 ASN A CB    1 
ATOM   13553 C  CG    . ASN A 1 3158 ? 202.057 185.719 238.797 1.00 4.90  ? 3158 ASN A CG    1 
ATOM   13554 O  OD1   . ASN A 1 3158 ? 201.512 186.132 239.817 1.00 5.80  ? 3158 ASN A OD1   1 
ATOM   13555 N  ND2   . ASN A 1 3158 ? 202.900 186.458 238.086 1.00 4.01  ? 3158 ASN A ND2   1 
ATOM   13556 N  N     . ALA A 1 3159 ? 200.503 181.399 238.042 1.00 14.92 ? 3159 ALA A N     1 
ATOM   13557 C  CA    . ALA A 1 3159 ? 199.893 180.378 237.198 1.00 10.26 ? 3159 ALA A CA    1 
ATOM   13558 C  C     . ALA A 1 3159 ? 198.500 180.007 237.692 1.00 11.93 ? 3159 ALA A C     1 
ATOM   13559 O  O     . ALA A 1 3159 ? 197.583 179.805 236.889 1.00 20.24 ? 3159 ALA A O     1 
ATOM   13560 C  CB    . ALA A 1 3159 ? 200.792 179.144 237.141 1.00 9.65  ? 3159 ALA A CB    1 
ATOM   13561 N  N     . ARG A 1 3160 ? 198.323 179.906 239.012 1.00 13.16 ? 3160 ARG A N     1 
ATOM   13562 C  CA    . ARG A 1 3160 ? 197.015 179.556 239.559 1.00 13.82 ? 3160 ARG A CA    1 
ATOM   13563 C  C     . ARG A 1 3160 ? 195.978 180.633 239.266 1.00 18.41 ? 3160 ARG A C     1 
ATOM   13564 O  O     . ARG A 1 3160 ? 194.840 180.322 238.897 1.00 29.79 ? 3160 ARG A O     1 
ATOM   13565 C  CB    . ARG A 1 3160 ? 197.123 179.304 241.062 1.00 16.52 ? 3160 ARG A CB    1 
ATOM   13566 C  CG    . ARG A 1 3160 ? 197.582 177.897 241.411 1.00 22.74 ? 3160 ARG A CG    1 
ATOM   13567 C  CD    . ARG A 1 3160 ? 197.540 177.637 242.909 1.00 26.00 ? 3160 ARG A CD    1 
ATOM   13568 N  NE    . ARG A 1 3160 ? 196.292 178.073 243.522 1.00 22.17 ? 3160 ARG A NE    1 
ATOM   13569 C  CZ    . ARG A 1 3160 ? 196.214 178.918 244.540 1.00 29.63 ? 3160 ARG A CZ    1 
ATOM   13570 N  NH1   . ARG A 1 3160 ? 197.297 179.447 245.084 1.00 28.48 ? 3160 ARG A NH1   1 
ATOM   13571 N  NH2   . ARG A 1 3160 ? 195.018 179.236 245.031 1.00 29.11 ? 3160 ARG A NH2   1 
ATOM   13572 N  N     . LEU A 1 3161 ? 196.340 181.907 239.429 1.00 11.73 ? 3161 LEU A N     1 
ATOM   13573 C  CA    . LEU A 1 3161 ? 195.390 182.971 239.117 1.00 13.32 ? 3161 LEU A CA    1 
ATOM   13574 C  C     . LEU A 1 3161 ? 195.161 183.091 237.616 1.00 16.01 ? 3161 LEU A C     1 
ATOM   13575 O  O     . LEU A 1 3161 ? 194.043 183.381 237.176 1.00 18.29 ? 3161 LEU A O     1 
ATOM   13576 C  CB    . LEU A 1 3161 ? 195.858 184.304 239.700 1.00 9.56  ? 3161 LEU A CB    1 
ATOM   13577 C  CG    . LEU A 1 3161 ? 195.611 184.560 241.190 1.00 12.87 ? 3161 LEU A CG    1 
ATOM   13578 C  CD1   . LEU A 1 3161 ? 196.505 183.719 242.083 1.00 14.14 ? 3161 LEU A CD1   1 
ATOM   13579 C  CD2   . LEU A 1 3161 ? 195.774 186.040 241.504 1.00 10.13 ? 3161 LEU A CD2   1 
ATOM   13580 N  N     . ALA A 1 3162 ? 196.207 182.877 236.813 1.00 14.73 ? 3162 ALA A N     1 
ATOM   13581 C  CA    . ALA A 1 3162 ? 196.042 182.931 235.366 1.00 14.62 ? 3162 ALA A CA    1 
ATOM   13582 C  C     . ALA A 1 3162 ? 195.115 181.826 234.874 1.00 23.17 ? 3162 ALA A C     1 
ATOM   13583 O  O     . ALA A 1 3162 ? 194.260 182.064 234.012 1.00 26.41 ? 3162 ALA A O     1 
ATOM   13584 C  CB    . ALA A 1 3162 ? 197.403 182.840 234.677 1.00 13.75 ? 3162 ALA A CB    1 
ATOM   13585 N  N     . LYS A 1 3163 ? 195.259 180.615 235.417 1.00 22.29 ? 3163 LYS A N     1 
ATOM   13586 C  CA    . LYS A 1 3163 ? 194.405 179.506 235.008 1.00 20.36 ? 3163 LYS A CA    1 
ATOM   13587 C  C     . LYS A 1 3163 ? 192.952 179.706 235.424 1.00 20.32 ? 3163 LYS A C     1 
ATOM   13588 O  O     . LYS A 1 3163 ? 192.063 179.093 234.826 1.00 33.45 ? 3163 LYS A O     1 
ATOM   13589 C  CB    . LYS A 1 3163 ? 194.942 178.190 235.576 1.00 22.27 ? 3163 LYS A CB    1 
ATOM   13590 C  CG    . LYS A 1 3163 ? 194.456 177.864 236.978 1.00 23.28 ? 3163 LYS A CG    1 
ATOM   13591 C  CD    . LYS A 1 3163 ? 195.224 176.697 237.575 1.00 24.66 ? 3163 LYS A CD    1 
ATOM   13592 C  CE    . LYS A 1 3163 ? 194.819 176.454 239.020 1.00 26.49 ? 3163 LYS A CE    1 
ATOM   13593 N  NZ    . LYS A 1 3163 ? 193.351 176.237 239.157 1.00 27.22 ? 3163 LYS A NZ    1 
ATOM   13594 N  N     . ARG A 1 3164 ? 192.692 180.546 236.425 1.00 17.17 ? 3164 ARG A N     1 
ATOM   13595 C  CA    . ARG A 1 3164 ? 191.336 180.888 236.832 1.00 19.08 ? 3164 ARG A CA    1 
ATOM   13596 C  C     . ARG A 1 3164 ? 190.837 182.171 236.184 1.00 19.53 ? 3164 ARG A C     1 
ATOM   13597 O  O     . ARG A 1 3164 ? 189.767 182.663 236.551 1.00 17.95 ? 3164 ARG A O     1 
ATOM   13598 C  CB    . ARG A 1 3164 ? 191.251 181.018 238.356 1.00 16.31 ? 3164 ARG A CB    1 
ATOM   13599 C  CG    . ARG A 1 3164 ? 191.735 179.805 239.126 1.00 24.93 ? 3164 ARG A CG    1 
ATOM   13600 C  CD    . ARG A 1 3164 ? 191.310 179.887 240.585 1.00 28.02 ? 3164 ARG A CD    1 
ATOM   13601 N  NE    . ARG A 1 3164 ? 192.330 180.506 241.423 1.00 34.36 ? 3164 ARG A NE    1 
ATOM   13602 C  CZ    . ARG A 1 3164 ? 193.484 179.941 241.751 1.00 32.44 ? 3164 ARG A CZ    1 
ATOM   13603 N  NH1   . ARG A 1 3164 ? 193.795 178.718 241.353 1.00 28.65 ? 3164 ARG A NH1   1 
ATOM   13604 N  NH2   . ARG A 1 3164 ? 194.348 180.619 242.501 1.00 28.55 ? 3164 ARG A NH2   1 
ATOM   13605 N  N     . GLY A 1 3165 ? 191.590 182.730 235.240 1.00 22.72 ? 3165 GLY A N     1 
ATOM   13606 C  CA    . GLY A 1 3165 ? 191.207 183.975 234.611 1.00 18.89 ? 3165 GLY A CA    1 
ATOM   13607 C  C     . GLY A 1 3165 ? 191.540 185.218 235.400 1.00 21.51 ? 3165 GLY A C     1 
ATOM   13608 O  O     . GLY A 1 3165 ? 191.170 186.319 234.977 1.00 20.86 ? 3165 GLY A O     1 
ATOM   13609 N  N     . GLY A 1 3166 ? 192.223 185.082 236.534 1.00 23.67 ? 3166 GLY A N     1 
ATOM   13610 C  CA    . GLY A 1 3166 ? 192.598 186.241 237.312 1.00 16.23 ? 3166 GLY A CA    1 
ATOM   13611 C  C     . GLY A 1 3166 ? 193.716 187.031 236.657 1.00 16.63 ? 3166 GLY A C     1 
ATOM   13612 O  O     . GLY A 1 3166 ? 194.457 186.534 235.811 1.00 12.52 ? 3166 GLY A O     1 
ATOM   13613 N  N     . ARG A 1 3167 ? 193.829 188.289 237.066 1.00 17.29 ? 3167 ARG A N     1 
ATOM   13614 C  CA    . ARG A 1 3167 ? 194.841 189.183 236.522 1.00 14.43 ? 3167 ARG A CA    1 
ATOM   13615 C  C     . ARG A 1 3167 ? 196.140 188.996 237.293 1.00 12.62 ? 3167 ARG A C     1 
ATOM   13616 O  O     . ARG A 1 3167 ? 196.149 189.035 238.527 1.00 12.34 ? 3167 ARG A O     1 
ATOM   13617 C  CB    . ARG A 1 3167 ? 194.369 190.634 236.609 1.00 17.76 ? 3167 ARG A CB    1 
ATOM   13618 C  CG    . ARG A 1 3167 ? 193.378 191.043 235.529 1.00 22.17 ? 3167 ARG A CG    1 
ATOM   13619 C  CD    . ARG A 1 3167 ? 191.992 190.458 235.796 1.00 27.57 ? 3167 ARG A CD    1 
ATOM   13620 N  NE    . ARG A 1 3167 ? 191.009 190.880 234.807 1.00 30.45 ? 3167 ARG A NE    1 
ATOM   13621 C  CZ    . ARG A 1 3167 ? 190.287 191.987 234.900 1.00 26.46 ? 3167 ARG A CZ    1 
ATOM   13622 N  NH1   . ARG A 1 3167 ? 190.392 192.791 235.945 1.00 23.22 ? 3167 ARG A NH1   1 
ATOM   13623 N  NH2   . ARG A 1 3167 ? 189.433 192.289 233.927 1.00 24.11 ? 3167 ARG A NH2   1 
ATOM   13624 N  N     . THR A 1 3168 ? 197.235 188.783 236.569 1.00 7.96  ? 3168 THR A N     1 
ATOM   13625 C  CA    . THR A 1 3168 ? 198.534 188.551 237.181 1.00 8.86  ? 3168 THR A CA    1 
ATOM   13626 C  C     . THR A 1 3168 ? 199.543 189.553 236.643 1.00 7.26  ? 3168 THR A C     1 
ATOM   13627 O  O     . THR A 1 3168 ? 199.416 190.046 235.520 1.00 8.22  ? 3168 THR A O     1 
ATOM   13628 C  CB    . THR A 1 3168 ? 199.048 187.121 236.925 1.00 6.86  ? 3168 THR A CB    1 
ATOM   13629 O  OG1   . THR A 1 3168 ? 199.274 186.932 235.522 1.00 10.53 ? 3168 THR A OG1   1 
ATOM   13630 C  CG2   . THR A 1 3168 ? 198.041 186.099 237.411 1.00 10.96 ? 3168 THR A CG2   1 
ATOM   13631 N  N     . MET A 1 3169 ? 200.547 189.851 237.462 1.00 6.64  ? 3169 MET A N     1 
ATOM   13632 C  CA    . MET A 1 3169 ? 201.624 190.749 237.085 1.00 4.45  ? 3169 MET A CA    1 
ATOM   13633 C  C     . MET A 1 3169 ? 202.930 189.973 237.011 1.00 3.81  ? 3169 MET A C     1 
ATOM   13634 O  O     . MET A 1 3169 ? 203.144 189.013 237.757 1.00 4.17  ? 3169 MET A O     1 
ATOM   13635 C  CB    . MET A 1 3169 ? 201.745 191.912 238.073 1.00 3.89  ? 3169 MET A CB    1 
ATOM   13636 C  CG    . MET A 1 3169 ? 200.509 192.789 238.085 1.00 4.90  ? 3169 MET A CG    1 
ATOM   13637 S  SD    . MET A 1 3169 ? 200.339 193.785 236.596 1.00 22.67 ? 3169 MET A SD    1 
ATOM   13638 C  CE    . MET A 1 3169 ? 198.863 194.711 236.992 1.00 12.39 ? 3169 MET A CE    1 
ATOM   13639 N  N     . ALA A 1 3170 ? 203.796 190.393 236.092 1.00 3.39  ? 3170 ALA A N     1 
ATOM   13640 C  CA    . ALA A 1 3170 ? 205.011 189.642 235.803 1.00 2.43  ? 3170 ALA A CA    1 
ATOM   13641 C  C     . ALA A 1 3170 ? 205.923 189.575 237.020 1.00 1.35  ? 3170 ALA A C     1 
ATOM   13642 O  O     . ALA A 1 3170 ? 206.100 190.558 237.744 1.00 1.97  ? 3170 ALA A O     1 
ATOM   13643 C  CB    . ALA A 1 3170 ? 205.753 190.280 234.628 1.00 2.36  ? 3170 ALA A CB    1 
ATOM   13644 N  N     . ILE A 1 3171 ? 206.502 188.402 237.242 1.00 0.93  ? 3171 ILE A N     1 
ATOM   13645 C  CA    . ILE A 1 3171 ? 207.503 188.196 238.279 1.00 0.72  ? 3171 ILE A CA    1 
ATOM   13646 C  C     . ILE A 1 3171 ? 208.870 188.248 237.614 1.00 1.09  ? 3171 ILE A C     1 
ATOM   13647 O  O     . ILE A 1 3171 ? 209.150 187.478 236.687 1.00 2.75  ? 3171 ILE A O     1 
ATOM   13648 C  CB    . ILE A 1 3171 ? 207.289 186.866 239.016 1.00 2.12  ? 3171 ILE A CB    1 
ATOM   13649 C  CG1   . ILE A 1 3171 ? 205.891 186.824 239.638 1.00 1.57  ? 3171 ILE A CG1   1 
ATOM   13650 C  CG2   . ILE A 1 3171 ? 208.354 186.671 240.082 1.00 0.77  ? 3171 ILE A CG2   1 
ATOM   13651 C  CD1   . ILE A 1 3171 ? 205.596 187.988 240.554 1.00 0.84  ? 3171 ILE A CD1   1 
ATOM   13652 N  N     . THR A 1 3172 ? 209.715 189.154 238.080 1.00 0.71  ? 3172 THR A N     1 
ATOM   13653 C  CA    . THR A 1 3172 ? 210.985 189.473 237.454 1.00 0.78  ? 3172 THR A CA    1 
ATOM   13654 C  C     . THR A 1 3172 ? 212.125 189.297 238.448 1.00 0.18  ? 3172 THR A C     1 
ATOM   13655 O  O     . THR A 1 3172 ? 211.896 189.234 239.661 1.00 0.15  ? 3172 THR A O     1 
ATOM   13656 C  CB    . THR A 1 3172 ? 210.980 190.915 236.919 1.00 0.53  ? 3172 THR A CB    1 
ATOM   13657 O  OG1   . THR A 1 3172 ? 211.070 191.838 238.010 1.00 0.88  ? 3172 THR A OG1   1 
ATOM   13658 C  CG2   . THR A 1 3172 ? 209.710 191.190 236.132 1.00 1.21  ? 3172 THR A CG2   1 
ATOM   13659 N  N     . PRO A 1 3173 ? 213.367 189.190 237.968 1.00 0.39  ? 3173 PRO A N     1 
ATOM   13660 C  CA    . PRO A 1 3173 ? 214.506 189.150 238.898 1.00 0.27  ? 3173 PRO A CA    1 
ATOM   13661 C  C     . PRO A 1 3173 ? 214.605 190.373 239.791 1.00 0.07  ? 3173 PRO A C     1 
ATOM   13662 O  O     . PRO A 1 3173 ? 215.198 190.284 240.872 1.00 0.05  ? 3173 PRO A O     1 
ATOM   13663 C  CB    . PRO A 1 3173 ? 215.716 189.039 237.961 1.00 0.19  ? 3173 PRO A CB    1 
ATOM   13664 C  CG    . PRO A 1 3173 ? 215.174 188.380 236.749 1.00 0.12  ? 3173 PRO A CG    1 
ATOM   13665 C  CD    . PRO A 1 3173 ? 213.789 188.928 236.581 1.00 0.17  ? 3173 PRO A CD    1 
ATOM   13666 N  N     . ARG A 1 3174 ? 214.050 191.512 239.377 1.00 0.12  ? 3174 ARG A N     1 
ATOM   13667 C  CA    . ARG A 1 3174 ? 214.051 192.685 240.242 1.00 0.20  ? 3174 ARG A CA    1 
ATOM   13668 C  C     . ARG A 1 3174 ? 213.191 192.473 241.481 1.00 0.11  ? 3174 ARG A C     1 
ATOM   13669 O  O     . ARG A 1 3174 ? 213.437 193.099 242.517 1.00 0.09  ? 3174 ARG A O     1 
ATOM   13670 C  CB    . ARG A 1 3174 ? 213.589 193.912 239.461 1.00 0.34  ? 3174 ARG A CB    1 
ATOM   13671 C  CG    . ARG A 1 3174 ? 214.582 194.349 238.404 1.00 0.60  ? 3174 ARG A CG    1 
ATOM   13672 C  CD    . ARG A 1 3174 ? 214.351 195.777 237.969 1.00 0.71  ? 3174 ARG A CD    1 
ATOM   13673 N  NE    . ARG A 1 3174 ? 214.634 196.728 239.034 1.00 0.84  ? 3174 ARG A NE    1 
ATOM   13674 C  CZ    . ARG A 1 3174 ? 214.422 198.033 238.943 1.00 2.53  ? 3174 ARG A CZ    1 
ATOM   13675 N  NH1   . ARG A 1 3174 ? 213.931 198.577 237.843 1.00 1.64  ? 3174 ARG A NH1   1 
ATOM   13676 N  NH2   . ARG A 1 3174 ? 214.711 198.812 239.982 1.00 3.35  ? 3174 ARG A NH2   1 
ATOM   13677 N  N     . HIS A 1 3175 ? 212.182 191.605 241.397 1.00 0.13  ? 3175 HIS A N     1 
ATOM   13678 C  CA    . HIS A 1 3175 ? 211.464 191.192 242.598 1.00 0.06  ? 3175 HIS A CA    1 
ATOM   13679 C  C     . HIS A 1 3175 ? 212.383 190.441 243.553 1.00 0.06  ? 3175 HIS A C     1 
ATOM   13680 O  O     . HIS A 1 3175 ? 212.334 190.653 244.769 1.00 0.10  ? 3175 HIS A O     1 
ATOM   13681 C  CB    . HIS A 1 3175 ? 210.267 190.321 242.224 1.00 0.17  ? 3175 HIS A CB    1 
ATOM   13682 C  CG    . HIS A 1 3175 ? 209.191 191.047 241.482 1.00 0.22  ? 3175 HIS A CG    1 
ATOM   13683 N  ND1   . HIS A 1 3175 ? 209.295 191.369 240.146 1.00 0.34  ? 3175 HIS A ND1   1 
ATOM   13684 C  CD2   . HIS A 1 3175 ? 207.977 191.495 241.883 1.00 0.23  ? 3175 HIS A CD2   1 
ATOM   13685 C  CE1   . HIS A 1 3175 ? 208.198 191.993 239.759 1.00 0.76  ? 3175 HIS A CE1   1 
ATOM   13686 N  NE2   . HIS A 1 3175 ? 207.383 192.083 240.794 1.00 0.64  ? 3175 HIS A NE2   1 
ATOM   13687 N  N     . TYR A 1 3176 ? 213.219 189.547 243.019 1.00 0.05  ? 3176 TYR A N     1 
ATOM   13688 C  CA    . TYR A 1 3176 ? 214.161 188.809 243.853 1.00 0.04  ? 3176 TYR A CA    1 
ATOM   13689 C  C     . TYR A 1 3176 ? 215.197 189.738 244.472 1.00 0.05  ? 3176 TYR A C     1 
ATOM   13690 O  O     . TYR A 1 3176 ? 215.526 189.612 245.656 1.00 0.04  ? 3176 TYR A O     1 
ATOM   13691 C  CB    . TYR A 1 3176 ? 214.839 187.714 243.025 1.00 0.06  ? 3176 TYR A CB    1 
ATOM   13692 C  CG    . TYR A 1 3176 ? 215.701 186.768 243.826 1.00 0.05  ? 3176 TYR A CG    1 
ATOM   13693 C  CD1   . TYR A 1 3176 ? 215.132 185.754 244.580 1.00 0.08  ? 3176 TYR A CD1   1 
ATOM   13694 C  CD2   . TYR A 1 3176 ? 217.086 186.877 243.815 1.00 0.07  ? 3176 TYR A CD2   1 
ATOM   13695 C  CE1   . TYR A 1 3176 ? 215.911 184.883 245.308 1.00 0.14  ? 3176 TYR A CE1   1 
ATOM   13696 C  CE2   . TYR A 1 3176 ? 217.874 186.008 244.542 1.00 0.09  ? 3176 TYR A CE2   1 
ATOM   13697 C  CZ    . TYR A 1 3176 ? 217.280 185.013 245.287 1.00 0.13  ? 3176 TYR A CZ    1 
ATOM   13698 O  OH    . TYR A 1 3176 ? 218.051 184.142 246.015 1.00 0.51  ? 3176 TYR A OH    1 
ATOM   13699 N  N     . LEU A 1 3177 ? 215.728 190.674 243.682 1.00 0.12  ? 3177 LEU A N     1 
ATOM   13700 C  CA    . LEU A 1 3177 ? 216.657 191.658 244.226 1.00 0.09  ? 3177 LEU A CA    1 
ATOM   13701 C  C     . LEU A 1 3177 ? 215.973 192.529 245.267 1.00 0.09  ? 3177 LEU A C     1 
ATOM   13702 O  O     . LEU A 1 3177 ? 216.575 192.883 246.287 1.00 0.13  ? 3177 LEU A O     1 
ATOM   13703 C  CB    . LEU A 1 3177 ? 217.237 192.507 243.097 1.00 0.08  ? 3177 LEU A CB    1 
ATOM   13704 C  CG    . LEU A 1 3177 ? 218.204 191.761 242.180 1.00 0.16  ? 3177 LEU A CG    1 
ATOM   13705 C  CD1   . LEU A 1 3177 ? 218.295 192.441 240.827 1.00 0.29  ? 3177 LEU A CD1   1 
ATOM   13706 C  CD2   . LEU A 1 3177 ? 219.575 191.651 242.826 1.00 0.10  ? 3177 LEU A CD2   1 
ATOM   13707 N  N     . ASP A 1 3178 ? 214.711 192.883 245.026 1.00 0.07  ? 3178 ASP A N     1 
ATOM   13708 C  CA    . ASP A 1 3178 ? 213.918 193.561 246.042 1.00 0.08  ? 3178 ASP A CA    1 
ATOM   13709 C  C     . ASP A 1 3178 ? 213.796 192.709 247.298 1.00 0.12  ? 3178 ASP A C     1 
ATOM   13710 O  O     . ASP A 1 3178 ? 213.910 193.218 248.417 1.00 0.22  ? 3178 ASP A O     1 
ATOM   13711 C  CB    . ASP A 1 3178 ? 212.537 193.890 245.477 1.00 0.23  ? 3178 ASP A CB    1 
ATOM   13712 C  CG    . ASP A 1 3178 ? 212.008 195.211 245.963 1.00 3.95  ? 3178 ASP A CG    1 
ATOM   13713 O  OD1   . ASP A 1 3178 ? 212.440 195.657 247.044 1.00 9.80  ? 3178 ASP A OD1   1 
ATOM   13714 O  OD2   . ASP A 1 3178 ? 211.163 195.809 245.265 1.00 11.55 ? 3178 ASP A OD2   1 
ATOM   13715 N  N     . PHE A 1 3179 ? 213.578 191.405 247.125 1.00 0.09  ? 3179 PHE A N     1 
ATOM   13716 C  CA    . PHE A 1 3179 ? 213.394 190.505 248.259 1.00 0.03  ? 3179 PHE A CA    1 
ATOM   13717 C  C     . PHE A 1 3179 ? 214.648 190.439 249.126 1.00 0.05  ? 3179 PHE A C     1 
ATOM   13718 O  O     . PHE A 1 3179 ? 214.587 190.660 250.339 1.00 0.12  ? 3179 PHE A O     1 
ATOM   13719 C  CB    . PHE A 1 3179 ? 213.003 189.117 247.738 1.00 0.04  ? 3179 PHE A CB    1 
ATOM   13720 C  CG    . PHE A 1 3179 ? 213.017 188.029 248.780 1.00 0.04  ? 3179 PHE A CG    1 
ATOM   13721 C  CD1   . PHE A 1 3179 ? 212.579 188.262 250.070 1.00 0.03  ? 3179 PHE A CD1   1 
ATOM   13722 C  CD2   . PHE A 1 3179 ? 213.460 186.762 248.454 1.00 0.11  ? 3179 PHE A CD2   1 
ATOM   13723 C  CE1   . PHE A 1 3179 ? 212.595 187.257 251.011 1.00 0.13  ? 3179 PHE A CE1   1 
ATOM   13724 C  CE2   . PHE A 1 3179 ? 213.472 185.754 249.394 1.00 0.21  ? 3179 PHE A CE2   1 
ATOM   13725 C  CZ    . PHE A 1 3179 ? 213.039 186.002 250.674 1.00 0.12  ? 3179 PHE A CZ    1 
ATOM   13726 N  N     . ILE A 1 3180 ? 215.801 190.149 248.519 1.00 0.07  ? 3180 ILE A N     1 
ATOM   13727 C  CA    . ILE A 1 3180 ? 217.012 189.975 249.314 1.00 0.13  ? 3180 ILE A CA    1 
ATOM   13728 C  C     . ILE A 1 3180 ? 217.478 191.301 249.895 1.00 0.12  ? 3180 ILE A C     1 
ATOM   13729 O  O     . ILE A 1 3180 ? 218.079 191.335 250.975 1.00 0.16  ? 3180 ILE A O     1 
ATOM   13730 C  CB    . ILE A 1 3180 ? 218.117 189.300 248.480 1.00 0.27  ? 3180 ILE A CB    1 
ATOM   13731 C  CG1   . ILE A 1 3180 ? 218.426 190.122 247.229 1.00 0.28  ? 3180 ILE A CG1   1 
ATOM   13732 C  CG2   . ILE A 1 3180 ? 217.713 187.879 248.118 1.00 0.06  ? 3180 ILE A CG2   1 
ATOM   13733 C  CD1   . ILE A 1 3180 ? 219.398 189.465 246.293 1.00 0.55  ? 3180 ILE A CD1   1 
ATOM   13734 N  N     . ASN A 1 3181 ? 217.218 192.408 249.200 1.00 0.24  ? 3181 ASN A N     1 
ATOM   13735 C  CA    . ASN A 1 3181 ? 217.543 193.721 249.744 1.00 0.61  ? 3181 ASN A CA    1 
ATOM   13736 C  C     . ASN A 1 3181 ? 216.764 193.977 251.030 1.00 0.42  ? 3181 ASN A C     1 
ATOM   13737 O  O     . ASN A 1 3181 ? 217.337 194.381 252.047 1.00 0.89  ? 3181 ASN A O     1 
ATOM   13738 C  CB    . ASN A 1 3181 ? 217.248 194.804 248.703 1.00 1.50  ? 3181 ASN A CB    1 
ATOM   13739 C  CG    . ASN A 1 3181 ? 217.750 196.173 249.115 1.00 6.20  ? 3181 ASN A CG    1 
ATOM   13740 O  OD1   . ASN A 1 3181 ? 218.306 196.349 250.197 1.00 13.03 ? 3181 ASN A OD1   1 
ATOM   13741 N  ND2   . ASN A 1 3181 ? 217.539 197.159 248.251 1.00 11.22 ? 3181 ASN A ND2   1 
ATOM   13742 N  N     . HIS A 1 3182 ? 215.455 193.720 251.005 1.00 0.20  ? 3182 HIS A N     1 
ATOM   13743 C  CA    . HIS A 1 3182 ? 214.644 193.874 252.207 1.00 0.26  ? 3182 HIS A CA    1 
ATOM   13744 C  C     . HIS A 1 3182 ? 215.085 192.906 253.296 1.00 0.51  ? 3182 HIS A C     1 
ATOM   13745 O  O     . HIS A 1 3182 ? 215.045 193.241 254.485 1.00 2.11  ? 3182 HIS A O     1 
ATOM   13746 C  CB    . HIS A 1 3182 ? 213.166 193.667 251.873 1.00 0.24  ? 3182 HIS A CB    1 
ATOM   13747 C  CG    . HIS A 1 3182 ? 212.519 194.852 251.229 1.00 0.47  ? 3182 HIS A CG    1 
ATOM   13748 N  ND1   . HIS A 1 3182 ? 211.587 194.733 250.223 1.00 0.28  ? 3182 HIS A ND1   1 
ATOM   13749 C  CD2   . HIS A 1 3182 ? 212.654 196.179 251.463 1.00 0.73  ? 3182 HIS A CD2   1 
ATOM   13750 C  CE1   . HIS A 1 3182 ? 211.188 195.935 249.851 1.00 0.43  ? 3182 HIS A CE1   1 
ATOM   13751 N  NE2   . HIS A 1 3182 ? 211.818 196.830 250.589 1.00 0.69  ? 3182 HIS A NE2   1 
ATOM   13752 N  N     . TYR A 1 3183 ? 215.504 191.701 252.911 1.00 0.18  ? 3183 TYR A N     1 
ATOM   13753 C  CA    . TYR A 1 3183 ? 215.941 190.717 253.896 1.00 0.42  ? 3183 TYR A CA    1 
ATOM   13754 C  C     . TYR A 1 3183 ? 217.177 191.203 254.643 1.00 0.88  ? 3183 TYR A C     1 
ATOM   13755 O  O     . TYR A 1 3183 ? 217.263 191.079 255.869 1.00 1.89  ? 3183 TYR A O     1 
ATOM   13756 C  CB    . TYR A 1 3183 ? 216.201 189.377 253.209 1.00 0.67  ? 3183 TYR A CB    1 
ATOM   13757 C  CG    . TYR A 1 3183 ? 216.488 188.224 254.148 1.00 0.81  ? 3183 TYR A CG    1 
ATOM   13758 C  CD1   . TYR A 1 3183 ? 216.003 188.219 255.446 1.00 0.96  ? 3183 TYR A CD1   1 
ATOM   13759 C  CD2   . TYR A 1 3183 ? 217.231 187.134 253.722 1.00 1.08  ? 3183 TYR A CD2   1 
ATOM   13760 C  CE1   . TYR A 1 3183 ? 216.264 187.164 256.300 1.00 0.92  ? 3183 TYR A CE1   1 
ATOM   13761 C  CE2   . TYR A 1 3183 ? 217.493 186.076 254.563 1.00 2.33  ? 3183 TYR A CE2   1 
ATOM   13762 C  CZ    . TYR A 1 3183 ? 217.007 186.096 255.851 1.00 1.59  ? 3183 TYR A CZ    1 
ATOM   13763 O  OH    . TYR A 1 3183 ? 217.269 185.041 256.691 1.00 1.92  ? 3183 TYR A OH    1 
ATOM   13764 N  N     . ALA A 1 3184 ? 218.142 191.773 253.920 1.00 1.26  ? 3184 ALA A N     1 
ATOM   13765 C  CA    . ALA A 1 3184 ? 219.344 192.290 254.565 1.00 1.49  ? 3184 ALA A CA    1 
ATOM   13766 C  C     . ALA A 1 3184 ? 219.021 193.469 255.478 1.00 2.00  ? 3184 ALA A C     1 
ATOM   13767 O  O     . ALA A 1 3184 ? 219.539 193.564 256.596 1.00 3.30  ? 3184 ALA A O     1 
ATOM   13768 C  CB    . ALA A 1 3184 ? 220.372 192.693 253.507 1.00 1.85  ? 3184 ALA A CB    1 
ATOM   13769 N  N     . ASN A 1 3185 ? 218.162 194.380 255.014 1.00 1.92  ? 3185 ASN A N     1 
ATOM   13770 C  CA    . ASN A 1 3185 ? 217.841 195.570 255.795 1.00 1.74  ? 3185 ASN A CA    1 
ATOM   13771 C  C     . ASN A 1 3185 ? 217.067 195.214 257.059 1.00 4.64  ? 3185 ASN A C     1 
ATOM   13772 O  O     . ASN A 1 3185 ? 217.401 195.675 258.156 1.00 7.65  ? 3185 ASN A O     1 
ATOM   13773 C  CB    . ASN A 1 3185 ? 217.048 196.559 254.942 1.00 1.88  ? 3185 ASN A CB    1 
ATOM   13774 C  CG    . ASN A 1 3185 ? 217.787 196.966 253.686 1.00 3.20  ? 3185 ASN A CG    1 
ATOM   13775 O  OD1   . ASN A 1 3185 ? 218.941 196.595 253.483 1.00 5.44  ? 3185 ASN A OD1   1 
ATOM   13776 N  ND2   . ASN A 1 3185 ? 217.120 197.731 252.833 1.00 5.55  ? 3185 ASN A ND2   1 
ATOM   13777 N  N     . LEU A 1 3186 ? 216.020 194.397 256.921 1.00 4.45  ? 3186 LEU A N     1 
ATOM   13778 C  CA    . LEU A 1 3186 ? 215.212 194.022 258.076 1.00 3.00  ? 3186 LEU A CA    1 
ATOM   13779 C  C     . LEU A 1 3186 ? 216.025 193.227 259.089 1.00 4.55  ? 3186 LEU A C     1 
ATOM   13780 O  O     . LEU A 1 3186 ? 215.887 193.428 260.301 1.00 9.63  ? 3186 LEU A O     1 
ATOM   13781 C  CB    . LEU A 1 3186 ? 213.990 193.226 257.622 1.00 1.84  ? 3186 LEU A CB    1 
ATOM   13782 C  CG    . LEU A 1 3186 ? 212.922 194.034 256.885 1.00 2.75  ? 3186 LEU A CG    1 
ATOM   13783 C  CD1   . LEU A 1 3186 ? 211.796 193.139 256.403 1.00 1.97  ? 3186 LEU A CD1   1 
ATOM   13784 C  CD2   . LEU A 1 3186 ? 212.387 195.139 257.784 1.00 5.58  ? 3186 LEU A CD2   1 
ATOM   13785 N  N     . PHE A 1 3187 ? 216.874 192.317 258.610 1.00 4.20  ? 3187 PHE A N     1 
ATOM   13786 C  CA    . PHE A 1 3187 ? 217.704 191.516 259.504 1.00 3.66  ? 3187 PHE A CA    1 
ATOM   13787 C  C     . PHE A 1 3187 ? 218.635 192.396 260.325 1.00 5.08  ? 3187 PHE A C     1 
ATOM   13788 O  O     . PHE A 1 3187 ? 218.765 192.218 261.540 1.00 6.03  ? 3187 PHE A O     1 
ATOM   13789 C  CB    . PHE A 1 3187 ? 218.499 190.507 258.683 1.00 3.87  ? 3187 PHE A CB    1 
ATOM   13790 C  CG    . PHE A 1 3187 ? 219.228 189.479 259.496 1.00 4.96  ? 3187 PHE A CG    1 
ATOM   13791 C  CD1   . PHE A 1 3187 ? 218.561 188.382 260.011 1.00 5.75  ? 3187 PHE A CD1   1 
ATOM   13792 C  CD2   . PHE A 1 3187 ? 220.592 189.588 259.709 1.00 6.52  ? 3187 PHE A CD2   1 
ATOM   13793 C  CE1   . PHE A 1 3187 ? 219.233 187.427 260.747 1.00 11.37 ? 3187 PHE A CE1   1 
ATOM   13794 C  CE2   . PHE A 1 3187 ? 221.270 188.636 260.441 1.00 9.18  ? 3187 PHE A CE2   1 
ATOM   13795 C  CZ    . PHE A 1 3187 ? 220.591 187.554 260.960 1.00 8.95  ? 3187 PHE A CZ    1 
ATOM   13796 N  N     . HIS A 1 3188 ? 219.298 193.352 259.673 1.00 7.67  ? 3188 HIS A N     1 
ATOM   13797 C  CA    . HIS A 1 3188 ? 220.147 194.282 260.404 1.00 7.41  ? 3188 HIS A CA    1 
ATOM   13798 C  C     . HIS A 1 3188 ? 219.325 195.159 261.338 1.00 9.63  ? 3188 HIS A C     1 
ATOM   13799 O  O     . HIS A 1 3188 ? 219.722 195.400 262.482 1.00 11.78 ? 3188 HIS A O     1 
ATOM   13800 C  CB    . HIS A 1 3188 ? 220.950 195.139 259.428 1.00 5.43  ? 3188 HIS A CB    1 
ATOM   13801 C  CG    . HIS A 1 3188 ? 221.622 196.312 260.069 1.00 14.51 ? 3188 HIS A CG    1 
ATOM   13802 N  ND1   . HIS A 1 3188 ? 222.681 196.180 260.939 1.00 19.40 ? 3188 HIS A ND1   1 
ATOM   13803 C  CD2   . HIS A 1 3188 ? 221.376 197.640 259.973 1.00 14.72 ? 3188 HIS A CD2   1 
ATOM   13804 C  CE1   . HIS A 1 3188 ? 223.063 197.375 261.350 1.00 20.17 ? 3188 HIS A CE1   1 
ATOM   13805 N  NE2   . HIS A 1 3188 ? 222.288 198.279 260.778 1.00 20.89 ? 3188 HIS A NE2   1 
ATOM   13806 N  N     . GLU A 1 3189 ? 218.171 195.639 260.865 1.00 6.63  ? 3189 GLU A N     1 
ATOM   13807 C  CA    . GLU A 1 3189 ? 217.320 196.497 261.682 1.00 7.17  ? 3189 GLU A CA    1 
ATOM   13808 C  C     . GLU A 1 3189 ? 216.800 195.756 262.908 1.00 11.20 ? 3189 GLU A C     1 
ATOM   13809 O  O     . GLU A 1 3189 ? 216.813 196.289 264.023 1.00 13.74 ? 3189 GLU A O     1 
ATOM   13810 C  CB    . GLU A 1 3189 ? 216.162 197.025 260.836 1.00 9.05  ? 3189 GLU A CB    1 
ATOM   13811 C  CG    . GLU A 1 3189 ? 215.257 198.018 261.538 1.00 13.29 ? 3189 GLU A CG    1 
ATOM   13812 C  CD    . GLU A 1 3189 ? 213.910 198.152 260.854 1.00 16.31 ? 3189 GLU A CD    1 
ATOM   13813 O  OE1   . GLU A 1 3189 ? 213.886 198.367 259.624 1.00 17.40 ? 3189 GLU A OE1   1 
ATOM   13814 O  OE2   . GLU A 1 3189 ? 212.876 198.044 261.545 1.00 15.73 ? 3189 GLU A OE2   1 
ATOM   13815 N  N     . LYS A 1 3190 ? 216.340 194.517 262.722 1.00 9.38  ? 3190 LYS A N     1 
ATOM   13816 C  CA    . LYS A 1 3190 ? 215.782 193.763 263.841 1.00 6.61  ? 3190 LYS A CA    1 
ATOM   13817 C  C     . LYS A 1 3190 ? 216.870 193.316 264.806 1.00 6.84  ? 3190 LYS A C     1 
ATOM   13818 O  O     . LYS A 1 3190 ? 216.664 193.317 266.025 1.00 13.55 ? 3190 LYS A O     1 
ATOM   13819 C  CB    . LYS A 1 3190 ? 214.993 192.564 263.325 1.00 6.40  ? 3190 LYS A CB    1 
ATOM   13820 C  CG    . LYS A 1 3190 ? 213.667 192.937 262.711 1.00 5.63  ? 3190 LYS A CG    1 
ATOM   13821 C  CD    . LYS A 1 3190 ? 212.772 193.626 263.720 1.00 4.72  ? 3190 LYS A CD    1 
ATOM   13822 C  CE    . LYS A 1 3190 ? 211.416 193.925 263.122 1.00 6.68  ? 3190 LYS A CE    1 
ATOM   13823 N  NZ    . LYS A 1 3190 ? 210.394 194.211 264.163 1.00 7.09  ? 3190 LYS A NZ    1 
ATOM   13824 N  N     . ARG A 1 3191 ? 218.028 192.913 264.280 1.00 13.28 ? 3191 ARG A N     1 
ATOM   13825 C  CA    . ARG A 1 3191 ? 219.143 192.540 265.143 1.00 10.43 ? 3191 ARG A CA    1 
ATOM   13826 C  C     . ARG A 1 3191 ? 219.633 193.737 265.948 1.00 9.03  ? 3191 ARG A C     1 
ATOM   13827 O  O     . ARG A 1 3191 ? 219.900 193.618 267.150 1.00 11.23 ? 3191 ARG A O     1 
ATOM   13828 C  CB    . ARG A 1 3191 ? 220.275 191.957 264.298 1.00 10.22 ? 3191 ARG A CB    1 
ATOM   13829 C  CG    . ARG A 1 3191 ? 221.467 191.436 265.076 1.00 16.41 ? 3191 ARG A CG    1 
ATOM   13830 C  CD    . ARG A 1 3191 ? 222.475 190.808 264.125 1.00 23.53 ? 3191 ARG A CD    1 
ATOM   13831 N  NE    . ARG A 1 3191 ? 223.683 190.355 264.802 1.00 34.59 ? 3191 ARG A NE    1 
ATOM   13832 C  CZ    . ARG A 1 3191 ? 223.821 189.160 265.361 1.00 35.19 ? 3191 ARG A CZ    1 
ATOM   13833 N  NH1   . ARG A 1 3191 ? 222.859 188.255 265.301 1.00 27.88 ? 3191 ARG A NH1   1 
ATOM   13834 N  NH2   . ARG A 1 3191 ? 224.959 188.863 265.983 1.00 31.76 ? 3191 ARG A NH2   1 
ATOM   13835 N  N     . SER A 1 3192 ? 219.747 194.899 265.302 1.00 9.39  ? 3192 SER A N     1 
ATOM   13836 C  CA    . SER A 1 3192 ? 220.206 196.101 265.994 1.00 12.50 ? 3192 SER A CA    1 
ATOM   13837 C  C     . SER A 1 3192 ? 219.214 196.542 267.064 1.00 14.80 ? 3192 SER A C     1 
ATOM   13838 O  O     . SER A 1 3192 ? 219.617 196.925 268.168 1.00 15.23 ? 3192 SER A O     1 
ATOM   13839 C  CB    . SER A 1 3192 ? 220.445 197.223 264.985 1.00 11.85 ? 3192 SER A CB    1 
ATOM   13840 O  OG    . SER A 1 3192 ? 220.860 198.414 265.627 1.00 20.87 ? 3192 SER A OG    1 
ATOM   13841 N  N     . GLU A 1 3193 ? 217.915 196.504 266.754 1.00 13.67 ? 3193 GLU A N     1 
ATOM   13842 C  CA    . GLU A 1 3193 ? 216.909 196.894 267.738 1.00 10.33 ? 3193 GLU A CA    1 
ATOM   13843 C  C     . GLU A 1 3193 ? 216.926 195.966 268.945 1.00 13.06 ? 3193 GLU A C     1 
ATOM   13844 O  O     . GLU A 1 3193 ? 216.846 196.423 270.090 1.00 17.88 ? 3193 GLU A O     1 
ATOM   13845 C  CB    . GLU A 1 3193 ? 215.519 196.909 267.100 1.00 8.93  ? 3193 GLU A CB    1 
ATOM   13846 C  CG    . GLU A 1 3193 ? 215.269 198.078 266.168 1.00 15.33 ? 3193 GLU A CG    1 
ATOM   13847 C  CD    . GLU A 1 3193 ? 213.828 198.156 265.702 1.00 29.34 ? 3193 GLU A CD    1 
ATOM   13848 O  OE1   . GLU A 1 3193 ? 213.523 197.619 264.616 1.00 23.88 ? 3193 GLU A OE1   1 
ATOM   13849 O  OE2   . GLU A 1 3193 ? 213.000 198.754 266.421 1.00 34.90 ? 3193 GLU A OE2   1 
ATOM   13850 N  N     . LEU A 1 3194 ? 217.031 194.658 268.706 1.00 12.42 ? 3194 LEU A N     1 
ATOM   13851 C  CA    . LEU A 1 3194 ? 217.001 193.698 269.804 1.00 11.17 ? 3194 LEU A CA    1 
ATOM   13852 C  C     . LEU A 1 3194 ? 218.229 193.834 270.694 1.00 17.03 ? 3194 LEU A C     1 
ATOM   13853 O  O     . LEU A 1 3194 ? 218.118 193.827 271.926 1.00 26.33 ? 3194 LEU A O     1 
ATOM   13854 C  CB    . LEU A 1 3194 ? 216.892 192.279 269.252 1.00 12.21 ? 3194 LEU A CB    1 
ATOM   13855 C  CG    . LEU A 1 3194 ? 216.478 191.201 270.250 1.00 17.77 ? 3194 LEU A CG    1 
ATOM   13856 C  CD1   . LEU A 1 3194 ? 215.150 191.548 270.904 1.00 21.07 ? 3194 LEU A CD1   1 
ATOM   13857 C  CD2   . LEU A 1 3194 ? 216.397 189.867 269.554 1.00 20.73 ? 3194 LEU A CD2   1 
ATOM   13858 N  N     . GLU A 1 3195 ? 219.411 193.952 270.088 1.00 18.65 ? 3195 GLU A N     1 
ATOM   13859 C  CA    . GLU A 1 3195 ? 220.628 194.110 270.879 1.00 16.52 ? 3195 GLU A CA    1 
ATOM   13860 C  C     . GLU A 1 3195 ? 220.617 195.427 271.641 1.00 13.99 ? 3195 GLU A C     1 
ATOM   13861 O  O     . GLU A 1 3195 ? 221.063 195.491 272.792 1.00 16.86 ? 3195 GLU A O     1 
ATOM   13862 C  CB    . GLU A 1 3195 ? 221.859 194.018 269.977 1.00 17.25 ? 3195 GLU A CB    1 
ATOM   13863 C  CG    . GLU A 1 3195 ? 222.076 192.642 269.371 1.00 19.17 ? 3195 GLU A CG    1 
ATOM   13864 C  CD    . GLU A 1 3195 ? 223.291 192.588 268.469 1.00 31.87 ? 3195 GLU A CD    1 
ATOM   13865 O  OE1   . GLU A 1 3195 ? 223.894 193.651 268.217 1.00 31.26 ? 3195 GLU A OE1   1 
ATOM   13866 O  OE2   . GLU A 1 3195 ? 223.642 191.482 268.011 1.00 35.95 ? 3195 GLU A OE2   1 
ATOM   13867 N  N     . GLU A 1 3196 ? 220.119 196.492 271.010 1.00 19.47 ? 3196 GLU A N     1 
ATOM   13868 C  CA    . GLU A 1 3196 ? 220.014 197.776 271.694 1.00 20.05 ? 3196 GLU A CA    1 
ATOM   13869 C  C     . GLU A 1 3196 ? 219.035 197.689 272.858 1.00 18.86 ? 3196 GLU A C     1 
ATOM   13870 O  O     . GLU A 1 3196 ? 219.287 198.241 273.935 1.00 21.00 ? 3196 GLU A O     1 
ATOM   13871 C  CB    . GLU A 1 3196 ? 219.579 198.858 270.704 1.00 16.62 ? 3196 GLU A CB    1 
ATOM   13872 C  CG    . GLU A 1 3196 ? 219.481 200.260 271.279 1.00 18.97 ? 3196 GLU A CG    1 
ATOM   13873 C  CD    . GLU A 1 3196 ? 220.831 200.804 271.717 1.00 34.47 ? 3196 GLU A CD    1 
ATOM   13874 O  OE1   . GLU A 1 3196 ? 221.861 200.361 271.166 1.00 38.53 ? 3196 GLU A OE1   1 
ATOM   13875 O  OE2   . GLU A 1 3196 ? 220.866 201.685 272.599 1.00 34.36 ? 3196 GLU A OE2   1 
ATOM   13876 N  N     . GLN A 1 3197 ? 217.910 196.998 272.656 1.00 17.86 ? 3197 GLN A N     1 
ATOM   13877 C  CA    . GLN A 1 3197 ? 216.953 196.793 273.739 1.00 18.47 ? 3197 GLN A CA    1 
ATOM   13878 C  C     . GLN A 1 3197 ? 217.562 195.974 274.869 1.00 18.95 ? 3197 GLN A C     1 
ATOM   13879 O  O     . GLN A 1 3197 ? 217.383 196.300 276.049 1.00 22.21 ? 3197 GLN A O     1 
ATOM   13880 C  CB    . GLN A 1 3197 ? 215.695 196.109 273.208 1.00 18.90 ? 3197 GLN A CB    1 
ATOM   13881 C  CG    . GLN A 1 3197 ? 214.606 195.933 274.253 1.00 22.53 ? 3197 GLN A CG    1 
ATOM   13882 C  CD    . GLN A 1 3197 ? 213.349 195.306 273.689 1.00 25.43 ? 3197 GLN A CD    1 
ATOM   13883 O  OE1   . GLN A 1 3197 ? 213.288 194.961 272.509 1.00 30.11 ? 3197 GLN A OE1   1 
ATOM   13884 N  NE2   . GLN A 1 3197 ? 212.337 195.147 274.534 1.00 25.35 ? 3197 GLN A NE2   1 
ATOM   13885 N  N     . GLN A 1 3198 ? 218.283 194.905 274.528 1.00 16.16 ? 3198 GLN A N     1 
ATOM   13886 C  CA    . GLN A 1 3198 ? 218.918 194.084 275.553 1.00 16.43 ? 3198 GLN A CA    1 
ATOM   13887 C  C     . GLN A 1 3198 ? 219.976 194.865 276.320 1.00 20.28 ? 3198 GLN A C     1 
ATOM   13888 O  O     . GLN A 1 3198 ? 220.247 194.559 277.487 1.00 23.73 ? 3198 GLN A O     1 
ATOM   13889 C  CB    . GLN A 1 3198 ? 219.529 192.836 274.918 1.00 20.56 ? 3198 GLN A CB    1 
ATOM   13890 C  CG    . GLN A 1 3198 ? 219.793 191.701 275.893 1.00 20.93 ? 3198 GLN A CG    1 
ATOM   13891 C  CD    . GLN A 1 3198 ? 218.617 191.435 276.813 1.00 25.26 ? 3198 GLN A CD    1 
ATOM   13892 O  OE1   . GLN A 1 3198 ? 217.503 191.176 276.360 1.00 28.37 ? 3198 GLN A OE1   1 
ATOM   13893 N  NE2   . GLN A 1 3198 ? 218.861 191.498 278.116 1.00 27.08 ? 3198 GLN A NE2   1 
ATOM   13894 N  N     . MET A 1 3199 ? 220.582 195.870 275.687 1.00 19.78 ? 3199 MET A N     1 
ATOM   13895 C  CA    . MET A 1 3199 ? 221.560 196.702 276.378 1.00 19.97 ? 3199 MET A CA    1 
ATOM   13896 C  C     . MET A 1 3199 ? 220.891 197.532 277.468 1.00 23.90 ? 3199 MET A C     1 
ATOM   13897 O  O     . MET A 1 3199 ? 221.395 197.620 278.593 1.00 31.68 ? 3199 MET A O     1 
ATOM   13898 C  CB    . MET A 1 3199 ? 222.292 197.588 275.364 1.00 21.15 ? 3199 MET A CB    1 
ATOM   13899 C  CG    . MET A 1 3199 ? 223.403 198.490 275.917 1.00 29.19 ? 3199 MET A CG    1 
ATOM   13900 S  SD    . MET A 1 3199 ? 222.893 199.913 276.908 1.00 50.51 ? 3199 MET A SD    1 
ATOM   13901 C  CE    . MET A 1 3199 ? 222.297 201.022 275.634 1.00 27.12 ? 3199 MET A CE    1 
ATOM   13902 N  N     . HIS A 1 3200 ? 219.750 198.151 277.150 1.00 24.53 ? 3200 HIS A N     1 
ATOM   13903 C  CA    . HIS A 1 3200 ? 219.045 198.954 278.142 1.00 24.37 ? 3200 HIS A CA    1 
ATOM   13904 C  C     . HIS A 1 3200 ? 218.533 198.093 279.291 1.00 23.84 ? 3200 HIS A C     1 
ATOM   13905 O  O     . HIS A 1 3200 ? 218.625 198.488 280.460 1.00 27.26 ? 3200 HIS A O     1 
ATOM   13906 C  CB    . HIS A 1 3200 ? 217.884 199.705 277.491 1.00 21.44 ? 3200 HIS A CB    1 
ATOM   13907 C  CG    . HIS A 1 3200 ? 218.313 200.804 276.569 1.00 21.99 ? 3200 HIS A CG    1 
ATOM   13908 N  ND1   . HIS A 1 3200 ? 218.398 200.639 275.205 1.00 28.25 ? 3200 HIS A ND1   1 
ATOM   13909 C  CD2   . HIS A 1 3200 ? 218.690 202.080 276.818 1.00 25.88 ? 3200 HIS A CD2   1 
ATOM   13910 C  CE1   . HIS A 1 3200 ? 218.799 201.769 274.651 1.00 30.19 ? 3200 HIS A CE1   1 
ATOM   13911 N  NE2   . HIS A 1 3200 ? 218.987 202.659 275.609 1.00 26.52 ? 3200 HIS A NE2   1 
ATOM   13912 N  N     . LEU A 1 3201 ? 217.989 196.914 278.979 1.00 15.35 ? 3201 LEU A N     1 
ATOM   13913 C  CA    . LEU A 1 3201 ? 217.448 196.050 280.021 1.00 17.65 ? 3201 LEU A CA    1 
ATOM   13914 C  C     . LEU A 1 3201 ? 218.533 195.617 280.997 1.00 22.59 ? 3201 LEU A C     1 
ATOM   13915 O  O     . LEU A 1 3201 ? 218.307 195.578 282.211 1.00 23.00 ? 3201 LEU A O     1 
ATOM   13916 C  CB    . LEU A 1 3201 ? 216.772 194.829 279.397 1.00 18.86 ? 3201 LEU A CB    1 
ATOM   13917 C  CG    . LEU A 1 3201 ? 215.498 195.070 278.583 1.00 23.30 ? 3201 LEU A CG    1 
ATOM   13918 C  CD1   . LEU A 1 3201 ? 214.840 193.748 278.227 1.00 28.55 ? 3201 LEU A CD1   1 
ATOM   13919 C  CD2   . LEU A 1 3201 ? 214.528 195.967 279.333 1.00 16.24 ? 3201 LEU A CD2   1 
ATOM   13920 N  N     . ASN A 1 3202 ? 219.718 195.281 280.485 1.00 25.64 ? 3202 ASN A N     1 
ATOM   13921 C  CA    . ASN A 1 3202 ? 220.816 194.884 281.360 1.00 21.52 ? 3202 ASN A CA    1 
ATOM   13922 C  C     . ASN A 1 3202 ? 221.273 196.042 282.237 1.00 24.39 ? 3202 ASN A C     1 
ATOM   13923 O  O     . ASN A 1 3202 ? 221.565 195.851 283.423 1.00 25.73 ? 3202 ASN A O     1 
ATOM   13924 C  CB    . ASN A 1 3202 ? 221.973 194.341 280.528 1.00 26.54 ? 3202 ASN A CB    1 
ATOM   13925 C  CG    . ASN A 1 3202 ? 221.751 192.908 280.098 1.00 32.26 ? 3202 ASN A CG    1 
ATOM   13926 O  OD1   . ASN A 1 3202 ? 220.732 192.303 280.434 1.00 24.44 ? 3202 ASN A OD1   1 
ATOM   13927 N  ND2   . ASN A 1 3202 ? 222.700 192.357 279.353 1.00 35.43 ? 3202 ASN A ND2   1 
ATOM   13928 N  N     . VAL A 1 3203 ? 221.352 197.248 281.672 1.00 25.68 ? 3203 VAL A N     1 
ATOM   13929 C  CA    . VAL A 1 3203 ? 221.696 198.416 282.475 1.00 23.21 ? 3203 VAL A CA    1 
ATOM   13930 C  C     . VAL A 1 3203 ? 220.588 198.721 283.474 1.00 27.69 ? 3203 VAL A C     1 
ATOM   13931 O  O     . VAL A 1 3203 ? 220.853 198.994 284.651 1.00 26.84 ? 3203 VAL A O     1 
ATOM   13932 C  CB    . VAL A 1 3203 ? 221.992 199.623 281.567 1.00 17.60 ? 3203 VAL A CB    1 
ATOM   13933 C  CG1   . VAL A 1 3203 ? 222.076 200.898 282.391 1.00 20.96 ? 3203 VAL A CG1   1 
ATOM   13934 C  CG2   . VAL A 1 3203 ? 223.279 199.397 280.795 1.00 23.46 ? 3203 VAL A CG2   1 
ATOM   13935 N  N     . GLY A 1 3204 ? 219.332 198.677 283.027 1.00 25.44 ? 3204 GLY A N     1 
ATOM   13936 C  CA    . GLY A 1 3204 ? 218.229 198.953 283.932 1.00 23.18 ? 3204 GLY A CA    1 
ATOM   13937 C  C     . GLY A 1 3204 ? 218.146 197.957 285.072 1.00 25.55 ? 3204 GLY A C     1 
ATOM   13938 O  O     . GLY A 1 3204 ? 217.876 198.328 286.216 1.00 32.38 ? 3204 GLY A O     1 
ATOM   13939 N  N     . LEU A 1 3205 ? 218.372 196.676 284.774 1.00 22.09 ? 3205 LEU A N     1 
ATOM   13940 C  CA    . LEU A 1 3205 ? 218.356 195.661 285.819 1.00 22.42 ? 3205 LEU A CA    1 
ATOM   13941 C  C     . LEU A 1 3205 ? 219.494 195.862 286.811 1.00 25.80 ? 3205 LEU A C     1 
ATOM   13942 O  O     . LEU A 1 3205 ? 219.303 195.697 288.022 1.00 29.68 ? 3205 LEU A O     1 
ATOM   13943 C  CB    . LEU A 1 3205 ? 218.424 194.266 285.198 1.00 23.26 ? 3205 LEU A CB    1 
ATOM   13944 C  CG    . LEU A 1 3205 ? 217.114 193.750 284.602 1.00 22.66 ? 3205 LEU A CG    1 
ATOM   13945 C  CD1   . LEU A 1 3205 ? 217.265 192.316 284.137 1.00 27.69 ? 3205 LEU A CD1   1 
ATOM   13946 C  CD2   . LEU A 1 3205 ? 215.995 193.872 285.620 1.00 24.30 ? 3205 LEU A CD2   1 
ATOM   13947 N  N     . ARG A 1 3206 ? 220.687 196.215 286.321 1.00 22.18 ? 3206 ARG A N     1 
ATOM   13948 C  CA    . ARG A 1 3206 ? 221.834 196.331 287.215 1.00 23.94 ? 3206 ARG A CA    1 
ATOM   13949 C  C     . ARG A 1 3206 ? 221.720 197.549 288.122 1.00 25.74 ? 3206 ARG A C     1 
ATOM   13950 O  O     . ARG A 1 3206 ? 222.218 197.523 289.253 1.00 31.86 ? 3206 ARG A O     1 
ATOM   13951 C  CB    . ARG A 1 3206 ? 223.140 196.369 286.412 1.00 24.45 ? 3206 ARG A CB    1 
ATOM   13952 C  CG    . ARG A 1 3206 ? 223.468 197.704 285.768 1.00 27.58 ? 3206 ARG A CG    1 
ATOM   13953 C  CD    . ARG A 1 3206 ? 224.798 197.665 285.028 1.00 28.23 ? 3206 ARG A CD    1 
ATOM   13954 N  NE    . ARG A 1 3206 ? 224.738 196.851 283.820 1.00 32.45 ? 3206 ARG A NE    1 
ATOM   13955 C  CZ    . ARG A 1 3206 ? 225.344 195.680 283.671 1.00 33.60 ? 3206 ARG A CZ    1 
ATOM   13956 N  NH1   . ARG A 1 3206 ? 226.065 195.147 284.643 1.00 31.48 ? 3206 ARG A NH1   1 
ATOM   13957 N  NH2   . ARG A 1 3206 ? 225.224 195.030 282.517 1.00 30.85 ? 3206 ARG A NH2   1 
ATOM   13958 N  N     . LYS A 1 3207 ? 221.078 198.623 287.652 1.00 25.75 ? 3207 LYS A N     1 
ATOM   13959 C  CA    . LYS A 1 3207 ? 220.851 199.777 288.516 1.00 27.52 ? 3207 LYS A CA    1 
ATOM   13960 C  C     . LYS A 1 3207 ? 219.889 199.438 289.647 1.00 26.86 ? 3207 LYS A C     1 
ATOM   13961 O  O     . LYS A 1 3207 ? 220.083 199.880 290.786 1.00 27.53 ? 3207 LYS A O     1 
ATOM   13962 C  CB    . LYS A 1 3207 ? 220.331 200.960 287.698 1.00 22.22 ? 3207 LYS A CB    1 
ATOM   13963 C  CG    . LYS A 1 3207 ? 221.277 201.427 286.607 1.00 20.48 ? 3207 LYS A CG    1 
ATOM   13964 C  CD    . LYS A 1 3207 ? 222.554 201.997 287.200 1.00 27.62 ? 3207 LYS A CD    1 
ATOM   13965 C  CE    . LYS A 1 3207 ? 223.435 202.620 286.129 1.00 32.70 ? 3207 LYS A CE    1 
ATOM   13966 N  NZ    . LYS A 1 3207 ? 224.008 201.595 285.215 1.00 33.20 ? 3207 LYS A NZ    1 
ATOM   13967 N  N     . ILE A 1 3208 ? 218.844 198.663 289.353 1.00 24.99 ? 3208 ILE A N     1 
ATOM   13968 C  CA    . ILE A 1 3208 ? 217.917 198.242 290.397 1.00 24.93 ? 3208 ILE A CA    1 
ATOM   13969 C  C     . ILE A 1 3208 ? 218.622 197.345 291.408 1.00 26.58 ? 3208 ILE A C     1 
ATOM   13970 O  O     . ILE A 1 3208 ? 218.452 197.505 292.622 1.00 33.07 ? 3208 ILE A O     1 
ATOM   13971 C  CB    . ILE A 1 3208 ? 216.695 197.542 289.778 1.00 26.35 ? 3208 ILE A CB    1 
ATOM   13972 C  CG1   . ILE A 1 3208 ? 215.933 198.504 288.865 1.00 26.74 ? 3208 ILE A CG1   1 
ATOM   13973 C  CG2   . ILE A 1 3208 ? 215.779 197.011 290.864 1.00 25.21 ? 3208 ILE A CG2   1 
ATOM   13974 C  CD1   . ILE A 1 3208 ? 214.729 197.878 288.207 1.00 22.11 ? 3208 ILE A CD1   1 
ATOM   13975 N  N     . LYS A 1 3209 ? 219.424 196.393 290.926 1.00 25.25 ? 3209 LYS A N     1 
ATOM   13976 C  CA    . LYS A 1 3209 ? 220.147 195.506 291.832 1.00 26.05 ? 3209 LYS A CA    1 
ATOM   13977 C  C     . LYS A 1 3209 ? 221.123 196.285 292.704 1.00 30.20 ? 3209 LYS A C     1 
ATOM   13978 O  O     . LYS A 1 3209 ? 221.254 196.009 293.902 1.00 31.43 ? 3209 LYS A O     1 
ATOM   13979 C  CB    . LYS A 1 3209 ? 220.882 194.427 291.040 1.00 28.52 ? 3209 LYS A CB    1 
ATOM   13980 C  CG    . LYS A 1 3209 ? 221.561 193.380 291.906 1.00 26.05 ? 3209 LYS A CG    1 
ATOM   13981 C  CD    . LYS A 1 3209 ? 221.739 192.072 291.157 1.00 22.40 ? 3209 LYS A CD    1 
ATOM   13982 C  CE    . LYS A 1 3209 ? 220.421 191.594 290.574 1.00 26.52 ? 3209 LYS A CE    1 
ATOM   13983 N  NZ    . LYS A 1 3209 ? 219.438 191.260 291.641 1.00 24.91 ? 3209 LYS A NZ    1 
ATOM   13984 N  N     . GLU A 1 3210 ? 221.820 197.262 292.120 1.00 27.75 ? 3210 GLU A N     1 
ATOM   13985 C  CA    . GLU A 1 3210 ? 222.698 198.116 292.913 1.00 30.59 ? 3210 GLU A CA    1 
ATOM   13986 C  C     . GLU A 1 3210 ? 221.903 198.905 293.945 1.00 32.14 ? 3210 GLU A C     1 
ATOM   13987 O  O     . GLU A 1 3210 ? 222.355 199.087 295.082 1.00 33.57 ? 3210 GLU A O     1 
ATOM   13988 C  CB    . GLU A 1 3210 ? 223.480 199.059 291.999 1.00 24.95 ? 3210 GLU A CB    1 
ATOM   13989 C  CG    . GLU A 1 3210 ? 224.634 198.398 291.266 1.00 32.07 ? 3210 GLU A CG    1 
ATOM   13990 C  CD    . GLU A 1 3210 ? 225.229 199.289 290.194 1.00 38.54 ? 3210 GLU A CD    1 
ATOM   13991 O  OE1   . GLU A 1 3210 ? 224.724 200.416 290.007 1.00 37.14 ? 3210 GLU A OE1   1 
ATOM   13992 O  OE2   . GLU A 1 3210 ? 226.202 198.863 289.538 1.00 34.60 ? 3210 GLU A OE2   1 
ATOM   13993 N  N     . THR A 1 3211 ? 220.712 199.375 293.568 1.00 27.72 ? 3211 THR A N     1 
ATOM   13994 C  CA    . THR A 1 3211 ? 219.876 200.136 294.491 1.00 28.19 ? 3211 THR A CA    1 
ATOM   13995 C  C     . THR A 1 3211 ? 219.487 199.300 295.705 1.00 29.78 ? 3211 THR A C     1 
ATOM   13996 O  O     . THR A 1 3211 ? 219.487 199.797 296.837 1.00 31.89 ? 3211 THR A O     1 
ATOM   13997 C  CB    . THR A 1 3211 ? 218.633 200.644 293.761 1.00 30.59 ? 3211 THR A CB    1 
ATOM   13998 O  OG1   . THR A 1 3211 ? 219.009 201.655 292.816 1.00 33.18 ? 3211 THR A OG1   1 
ATOM   13999 C  CG2   . THR A 1 3211 ? 217.625 201.224 294.742 1.00 25.24 ? 3211 THR A CG2   1 
ATOM   14000 N  N     . VAL A 1 3212 ? 219.158 198.024 295.489 1.00 29.24 ? 3212 VAL A N     1 
ATOM   14001 C  CA    . VAL A 1 3212 ? 218.830 197.139 296.604 1.00 27.50 ? 3212 VAL A CA    1 
ATOM   14002 C  C     . VAL A 1 3212 ? 220.026 196.999 297.539 1.00 33.69 ? 3212 VAL A C     1 
ATOM   14003 O  O     . VAL A 1 3212 ? 219.871 196.909 298.763 1.00 35.42 ? 3212 VAL A O     1 
ATOM   14004 C  CB    . VAL A 1 3212 ? 218.356 195.772 296.077 1.00 25.95 ? 3212 VAL A CB    1 
ATOM   14005 C  CG1   . VAL A 1 3212 ? 218.029 194.835 297.231 1.00 30.02 ? 3212 VAL A CG1   1 
ATOM   14006 C  CG2   . VAL A 1 3212 ? 217.154 195.944 295.170 1.00 28.08 ? 3212 VAL A CG2   1 
ATOM   14007 N  N     . ASP A 1 3213 ? 221.236 196.966 296.976 1.00 31.63 ? 3213 ASP A N     1 
ATOM   14008 C  CA    . ASP A 1 3213 ? 222.438 196.924 297.803 1.00 29.89 ? 3213 ASP A CA    1 
ATOM   14009 C  C     . ASP A 1 3213 ? 222.628 198.223 298.575 1.00 32.26 ? 3213 ASP A C     1 
ATOM   14010 O  O     . ASP A 1 3213 ? 223.045 198.202 299.740 1.00 37.37 ? 3213 ASP A O     1 
ATOM   14011 C  CB    . ASP A 1 3213 ? 223.662 196.633 296.936 1.00 32.50 ? 3213 ASP A CB    1 
ATOM   14012 C  CG    . ASP A 1 3213 ? 223.524 195.351 296.140 1.00 34.19 ? 3213 ASP A CG    1 
ATOM   14013 O  OD1   . ASP A 1 3213 ? 223.065 194.342 296.714 1.00 37.07 ? 3213 ASP A OD1   1 
ATOM   14014 O  OD2   . ASP A 1 3213 ? 223.874 195.353 294.942 1.00 34.32 ? 3213 ASP A OD2   1 
ATOM   14015 N  N     . GLN A 1 3214 ? 222.339 199.366 297.944 1.00 33.33 ? 3214 GLN A N     1 
ATOM   14016 C  CA    . GLN A 1 3214 ? 222.578 200.654 298.588 1.00 30.93 ? 3214 GLN A CA    1 
ATOM   14017 C  C     . GLN A 1 3214 ? 221.729 200.823 299.843 1.00 37.72 ? 3214 GLN A C     1 
ATOM   14018 O  O     . GLN A 1 3214 ? 222.215 201.318 300.866 1.00 37.87 ? 3214 GLN A O     1 
ATOM   14019 C  CB    . GLN A 1 3214 ? 222.307 201.797 297.607 1.00 25.93 ? 3214 GLN A CB    1 
ATOM   14020 C  CG    . GLN A 1 3214 ? 223.215 201.826 296.386 1.00 33.32 ? 3214 GLN A CG    1 
ATOM   14021 C  CD    . GLN A 1 3214 ? 224.588 201.241 296.654 1.00 38.37 ? 3214 GLN A CD    1 
ATOM   14022 O  OE1   . GLN A 1 3214 ? 225.375 201.797 297.420 1.00 36.01 ? 3214 GLN A OE1   1 
ATOM   14023 N  NE2   . GLN A 1 3214 ? 224.883 200.112 296.020 1.00 34.09 ? 3214 GLN A NE2   1 
ATOM   14024 N  N     . VAL A 1 3215 ? 220.455 200.433 299.782 1.00 32.35 ? 3215 VAL A N     1 
ATOM   14025 C  CA    . VAL A 1 3215 ? 219.596 200.583 300.950 1.00 30.46 ? 3215 VAL A CA    1 
ATOM   14026 C  C     . VAL A 1 3215 ? 220.018 199.625 302.058 1.00 35.95 ? 3215 VAL A C     1 
ATOM   14027 O  O     . VAL A 1 3215 ? 219.846 199.927 303.245 1.00 32.66 ? 3215 VAL A O     1 
ATOM   14028 C  CB    . VAL A 1 3215 ? 218.115 200.395 300.567 1.00 32.97 ? 3215 VAL A CB    1 
ATOM   14029 C  CG1   . VAL A 1 3215 ? 217.722 201.395 299.493 1.00 32.50 ? 3215 VAL A CG1   1 
ATOM   14030 C  CG2   . VAL A 1 3215 ? 217.852 198.975 300.096 1.00 26.82 ? 3215 VAL A CG2   1 
ATOM   14031 N  N     . GLU A 1 3216 ? 220.566 198.462 301.699 1.00 32.85 ? 3216 GLU A N     1 
ATOM   14032 C  CA    . GLU A 1 3216 ? 221.019 197.511 302.708 1.00 35.41 ? 3216 GLU A CA    1 
ATOM   14033 C  C     . GLU A 1 3216 ? 222.141 198.105 303.550 1.00 35.93 ? 3216 GLU A C     1 
ATOM   14034 O  O     . GLU A 1 3216 ? 222.134 197.995 304.782 1.00 35.35 ? 3216 GLU A O     1 
ATOM   14035 C  CB    . GLU A 1 3216 ? 221.469 196.213 302.036 1.00 33.78 ? 3216 GLU A CB    1 
ATOM   14036 C  CG    . GLU A 1 3216 ? 221.607 195.030 302.983 1.00 32.57 ? 3216 GLU A CG    1 
ATOM   14037 C  CD    . GLU A 1 3216 ? 222.971 194.963 303.643 1.00 36.57 ? 3216 GLU A CD    1 
ATOM   14038 O  OE1   . GLU A 1 3216 ? 223.984 194.925 302.915 1.00 39.57 ? 3216 GLU A OE1   1 
ATOM   14039 O  OE2   . GLU A 1 3216 ? 223.027 194.950 304.891 1.00 36.63 ? 3216 GLU A OE2   1 
ATOM   14040 N  N     . GLU A 1 3217 ? 223.118 198.746 302.902 1.00 32.78 ? 3217 GLU A N     1 
ATOM   14041 C  CA    . GLU A 1 3217 ? 224.181 199.399 303.658 1.00 34.79 ? 3217 GLU A CA    1 
ATOM   14042 C  C     . GLU A 1 3217 ? 223.697 200.698 304.285 1.00 37.87 ? 3217 GLU A C     1 
ATOM   14043 O  O     . GLU A 1 3217 ? 224.215 201.110 305.329 1.00 39.40 ? 3217 GLU A O     1 
ATOM   14044 C  CB    . GLU A 1 3217 ? 225.397 199.651 302.764 1.00 34.17 ? 3217 GLU A CB    1 
ATOM   14045 C  CG    . GLU A 1 3217 ? 225.223 200.764 301.745 1.00 33.67 ? 3217 GLU A CG    1 
ATOM   14046 C  CD    . GLU A 1 3217 ? 226.454 200.963 300.884 1.00 38.73 ? 3217 GLU A CD    1 
ATOM   14047 O  OE1   . GLU A 1 3217 ? 227.404 200.163 301.009 1.00 40.88 ? 3217 GLU A OE1   1 
ATOM   14048 O  OE2   . GLU A 1 3217 ? 226.473 201.922 300.084 1.00 38.24 ? 3217 GLU A OE2   1 
ATOM   14049 N  N     . LEU A 1 3218 ? 222.714 201.355 303.667 1.00 34.30 ? 3218 LEU A N     1 
ATOM   14050 C  CA    . LEU A 1 3218 ? 222.161 202.570 304.251 1.00 33.27 ? 3218 LEU A CA    1 
ATOM   14051 C  C     . LEU A 1 3218 ? 221.368 202.253 305.512 1.00 36.27 ? 3218 LEU A C     1 
ATOM   14052 O  O     . LEU A 1 3218 ? 221.412 203.013 306.488 1.00 39.60 ? 3218 LEU A O     1 
ATOM   14053 C  CB    . LEU A 1 3218 ? 221.297 203.301 303.223 1.00 29.93 ? 3218 LEU A CB    1 
ATOM   14054 C  CG    . LEU A 1 3218 ? 220.704 204.645 303.638 1.00 32.36 ? 3218 LEU A CG    1 
ATOM   14055 C  CD1   . LEU A 1 3218 ? 221.811 205.640 303.936 1.00 28.59 ? 3218 LEU A CD1   1 
ATOM   14056 C  CD2   . LEU A 1 3218 ? 219.796 205.179 302.540 1.00 32.12 ? 3218 LEU A CD2   1 
ATOM   14057 N  N     . ARG A 1 3219 ? 220.638 201.135 305.514 1.00 34.89 ? 3219 ARG A N     1 
ATOM   14058 C  CA    . ARG A 1 3219 ? 220.029 200.657 306.751 1.00 34.81 ? 3219 ARG A CA    1 
ATOM   14059 C  C     . ARG A 1 3219 ? 221.096 200.303 307.778 1.00 37.68 ? 3219 ARG A C     1 
ATOM   14060 O  O     . ARG A 1 3219 ? 220.936 200.575 308.974 1.00 35.17 ? 3219 ARG A O     1 
ATOM   14061 C  CB    . ARG A 1 3219 ? 219.135 199.449 306.473 1.00 29.77 ? 3219 ARG A CB    1 
ATOM   14062 C  CG    . ARG A 1 3219 ? 217.844 199.773 305.737 1.00 33.07 ? 3219 ARG A CG    1 
ATOM   14063 C  CD    . ARG A 1 3219 ? 216.911 198.570 305.719 1.00 31.62 ? 3219 ARG A CD    1 
ATOM   14064 N  NE    . ARG A 1 3219 ? 217.507 197.426 305.038 1.00 36.45 ? 3219 ARG A NE    1 
ATOM   14065 C  CZ    . ARG A 1 3219 ? 216.987 196.833 303.972 1.00 39.36 ? 3219 ARG A CZ    1 
ATOM   14066 N  NH1   . ARG A 1 3219 ? 215.850 197.247 303.436 1.00 37.42 ? 3219 ARG A NH1   1 
ATOM   14067 N  NH2   . ARG A 1 3219 ? 217.624 195.799 303.429 1.00 36.38 ? 3219 ARG A NH2   1 
ATOM   14068 N  N     . ARG A 1 3220 ? 222.191 199.683 307.330 1.00 33.83 ? 3220 ARG A N     1 
ATOM   14069 C  CA    . ARG A 1 3220 ? 223.324 199.448 308.217 1.00 34.65 ? 3220 ARG A CA    1 
ATOM   14070 C  C     . ARG A 1 3220 ? 223.914 200.766 308.701 1.00 37.44 ? 3220 ARG A C     1 
ATOM   14071 O  O     . ARG A 1 3220 ? 224.268 200.903 309.878 1.00 39.88 ? 3220 ARG A O     1 
ATOM   14072 C  CB    . ARG A 1 3220 ? 224.383 198.607 307.503 1.00 38.82 ? 3220 ARG A CB    1 
ATOM   14073 C  CG    . ARG A 1 3220 ? 225.769 198.681 308.123 1.00 37.74 ? 3220 ARG A CG    1 
ATOM   14074 C  CD    . ARG A 1 3220 ? 226.859 198.472 307.081 1.00 35.03 ? 3220 ARG A CD    1 
ATOM   14075 N  NE    . ARG A 1 3220 ? 226.801 199.460 306.010 1.00 40.50 ? 3220 ARG A NE    1 
ATOM   14076 C  CZ    . ARG A 1 3220 ? 227.206 200.718 306.125 1.00 44.05 ? 3220 ARG A CZ    1 
ATOM   14077 N  NH1   . ARG A 1 3220 ? 227.717 201.180 307.255 1.00 40.96 ? 3220 ARG A NH1   1 
ATOM   14078 N  NH2   . ARG A 1 3220 ? 227.100 201.532 305.078 1.00 39.43 ? 3220 ARG A NH2   1 
ATOM   14079 N  N     . ASP A 1 3221 ? 224.024 201.748 307.805 1.00 38.23 ? 3221 ASP A N     1 
ATOM   14080 C  CA    . ASP A 1 3221 ? 224.450 203.082 308.216 1.00 38.86 ? 3221 ASP A CA    1 
ATOM   14081 C  C     . ASP A 1 3221 ? 223.435 203.709 309.163 1.00 34.83 ? 3221 ASP A C     1 
ATOM   14082 O  O     . ASP A 1 3221 ? 223.809 204.385 310.128 1.00 33.38 ? 3221 ASP A O     1 
ATOM   14083 C  CB    . ASP A 1 3221 ? 224.664 203.967 306.988 1.00 34.98 ? 3221 ASP A CB    1 
ATOM   14084 C  CG    . ASP A 1 3221 ? 225.194 205.342 307.345 1.00 39.15 ? 3221 ASP A CG    1 
ATOM   14085 O  OD1   . ASP A 1 3221 ? 224.387 206.211 307.738 1.00 39.19 ? 3221 ASP A OD1   1 
ATOM   14086 O  OD2   . ASP A 1 3221 ? 226.419 205.555 307.232 1.00 39.69 ? 3221 ASP A OD2   1 
ATOM   14087 N  N     . LEU A 1 3222 ? 222.143 203.494 308.901 1.00 34.15 ? 3222 LEU A N     1 
ATOM   14088 C  CA    . LEU A 1 3222 ? 221.107 204.013 309.791 1.00 37.88 ? 3222 LEU A CA    1 
ATOM   14089 C  C     . LEU A 1 3222 ? 221.249 203.439 311.194 1.00 38.86 ? 3222 LEU A C     1 
ATOM   14090 O  O     . LEU A 1 3222 ? 221.091 204.159 312.188 1.00 38.94 ? 3222 LEU A O     1 
ATOM   14091 C  CB    . LEU A 1 3222 ? 219.722 203.704 309.223 1.00 37.64 ? 3222 LEU A CB    1 
ATOM   14092 C  CG    . LEU A 1 3222 ? 218.530 204.098 310.098 1.00 37.32 ? 3222 LEU A CG    1 
ATOM   14093 C  CD1   . LEU A 1 3222 ? 218.284 205.596 310.036 1.00 34.77 ? 3222 LEU A CD1   1 
ATOM   14094 C  CD2   . LEU A 1 3222 ? 217.284 203.329 309.684 1.00 30.28 ? 3222 LEU A CD2   1 
ATOM   14095 N  N     . ARG A 1 3223 ? 221.537 202.139 311.298 1.00 36.00 ? 3223 ARG A N     1 
ATOM   14096 C  CA    . ARG A 1 3223 ? 221.793 201.546 312.605 1.00 36.01 ? 3223 ARG A CA    1 
ATOM   14097 C  C     . ARG A 1 3223 ? 223.063 202.114 313.226 1.00 36.31 ? 3223 ARG A C     1 
ATOM   14098 O  O     . ARG A 1 3223 ? 223.116 202.359 314.438 1.00 36.81 ? 3223 ARG A O     1 
ATOM   14099 C  CB    . ARG A 1 3223 ? 221.884 200.024 312.484 1.00 36.56 ? 3223 ARG A CB    1 
ATOM   14100 C  CG    . ARG A 1 3223 ? 222.212 199.312 313.788 1.00 34.92 ? 3223 ARG A CG    1 
ATOM   14101 C  CD    . ARG A 1 3223 ? 222.796 197.930 313.537 1.00 39.32 ? 3223 ARG A CD    1 
ATOM   14102 N  NE    . ARG A 1 3223 ? 223.755 197.927 312.439 1.00 39.92 ? 3223 ARG A NE    1 
ATOM   14103 C  CZ    . ARG A 1 3223 ? 225.006 198.358 312.534 1.00 42.35 ? 3223 ARG A CZ    1 
ATOM   14104 N  NH1   . ARG A 1 3223 ? 225.489 198.833 313.670 1.00 37.90 ? 3223 ARG A NH1   1 
ATOM   14105 N  NH2   . ARG A 1 3223 ? 225.792 198.309 311.462 1.00 42.60 ? 3223 ARG A NH2   1 
ATOM   14106 N  N     . ILE A 1 3224 ? 224.099 202.328 312.413 1.00 36.74 ? 3224 ILE A N     1 
ATOM   14107 C  CA    . ILE A 1 3224 ? 225.350 202.884 312.921 1.00 35.60 ? 3224 ILE A CA    1 
ATOM   14108 C  C     . ILE A 1 3224 ? 225.134 204.298 313.446 1.00 37.10 ? 3224 ILE A C     1 
ATOM   14109 O  O     . ILE A 1 3224 ? 225.628 204.660 314.521 1.00 36.97 ? 3224 ILE A O     1 
ATOM   14110 C  CB    . ILE A 1 3224 ? 226.437 202.841 311.830 1.00 37.02 ? 3224 ILE A CB    1 
ATOM   14111 C  CG1   . ILE A 1 3224 ? 227.064 201.447 311.758 1.00 38.08 ? 3224 ILE A CG1   1 
ATOM   14112 C  CG2   . ILE A 1 3224 ? 227.509 203.892 312.087 1.00 33.84 ? 3224 ILE A CG2   1 
ATOM   14113 C  CD1   . ILE A 1 3224 ? 228.144 201.316 310.708 1.00 33.24 ? 3224 ILE A CD1   1 
ATOM   14114 N  N     . LYS A 1 3225 ? 224.388 205.120 312.699 1.00 34.70 ? 3225 LYS A N     1 
ATOM   14115 C  CA    . LYS A 1 3225 ? 224.099 206.475 313.159 1.00 35.38 ? 3225 LYS A CA    1 
ATOM   14116 C  C     . LYS A 1 3225 ? 223.281 206.466 314.442 1.00 38.82 ? 3225 LYS A C     1 
ATOM   14117 O  O     . LYS A 1 3225 ? 223.455 207.345 315.295 1.00 39.53 ? 3225 LYS A O     1 
ATOM   14118 C  CB    . LYS A 1 3225 ? 223.369 207.259 312.067 1.00 36.84 ? 3225 LYS A CB    1 
ATOM   14119 C  CG    . LYS A 1 3225 ? 224.170 207.443 310.788 1.00 36.15 ? 3225 LYS A CG    1 
ATOM   14120 C  CD    . LYS A 1 3225 ? 225.468 208.194 311.041 1.00 35.25 ? 3225 LYS A CD    1 
ATOM   14121 C  CE    . LYS A 1 3225 ? 225.202 209.612 311.514 1.00 34.22 ? 3225 LYS A CE    1 
ATOM   14122 N  NZ    . LYS A 1 3225 ? 224.098 210.256 310.752 1.00 37.89 ? 3225 LYS A NZ    1 
ATOM   14123 N  N     . SER A 1 3226 ? 222.381 205.492 314.595 1.00 37.36 ? 3226 SER A N     1 
ATOM   14124 C  CA    . SER A 1 3226 ? 221.643 205.360 315.847 1.00 35.69 ? 3226 SER A CA    1 
ATOM   14125 C  C     . SER A 1 3226 ? 222.582 205.051 317.005 1.00 38.85 ? 3226 SER A C     1 
ATOM   14126 O  O     . SER A 1 3226 ? 222.417 205.587 318.108 1.00 41.03 ? 3226 SER A O     1 
ATOM   14127 C  CB    . SER A 1 3226 ? 220.575 204.274 315.714 1.00 36.28 ? 3226 SER A CB    1 
ATOM   14128 O  OG    . SER A 1 3226 ? 221.163 202.987 315.639 1.00 39.51 ? 3226 SER A OG    1 
ATOM   14129 N  N     . GLN A 1 3227 ? 223.571 204.185 316.774 1.00 39.53 ? 3227 GLN A N     1 
ATOM   14130 C  CA    . GLN A 1 3227 ? 224.553 203.881 317.811 1.00 38.91 ? 3227 GLN A CA    1 
ATOM   14131 C  C     . GLN A 1 3227 ? 225.366 205.115 318.176 1.00 38.33 ? 3227 GLN A C     1 
ATOM   14132 O  O     . GLN A 1 3227 ? 225.695 205.327 319.349 1.00 39.38 ? 3227 GLN A O     1 
ATOM   14133 C  CB    . GLN A 1 3227 ? 225.469 202.748 317.350 1.00 35.93 ? 3227 GLN A CB    1 
ATOM   14134 C  CG    . GLN A 1 3227 ? 226.143 201.991 318.483 1.00 35.94 ? 3227 GLN A CG    1 
ATOM   14135 C  CD    . GLN A 1 3227 ? 227.487 202.581 318.860 1.00 38.30 ? 3227 GLN A CD    1 
ATOM   14136 O  OE1   . GLN A 1 3227 ? 228.024 203.435 318.155 1.00 39.53 ? 3227 GLN A OE1   1 
ATOM   14137 N  NE2   . GLN A 1 3227 ? 228.040 202.124 319.978 1.00 37.05 ? 3227 GLN A NE2   1 
ATOM   14138 N  N     . GLU A 1 3228 ? 225.708 205.938 317.181 1.00 36.51 ? 3228 GLU A N     1 
ATOM   14139 C  CA    . GLU A 1 3228 ? 226.433 207.174 317.456 1.00 35.92 ? 3228 GLU A CA    1 
ATOM   14140 C  C     . GLU A 1 3228 ? 225.608 208.114 318.325 1.00 37.83 ? 3228 GLU A C     1 
ATOM   14141 O  O     . GLU A 1 3228 ? 226.142 208.759 319.236 1.00 35.03 ? 3228 GLU A O     1 
ATOM   14142 C  CB    . GLU A 1 3228 ? 226.822 207.855 316.144 1.00 33.64 ? 3228 GLU A CB    1 
ATOM   14143 C  CG    . GLU A 1 3228 ? 227.674 209.101 316.315 1.00 36.29 ? 3228 GLU A CG    1 
ATOM   14144 C  CD    . GLU A 1 3228 ? 228.111 209.692 314.989 1.00 38.95 ? 3228 GLU A CD    1 
ATOM   14145 O  OE1   . GLU A 1 3228 ? 227.737 209.137 313.936 1.00 38.12 ? 3228 GLU A OE1   1 
ATOM   14146 O  OE2   . GLU A 1 3228 ? 228.830 210.714 315.001 1.00 39.54 ? 3228 GLU A OE2   1 
ATOM   14147 N  N     . LEU A 1 3229 ? 224.303 208.207 318.057 1.00 39.21 ? 3229 LEU A N     1 
ATOM   14148 C  CA    . LEU A 1 3229 ? 223.436 209.044 318.880 1.00 35.83 ? 3229 LEU A CA    1 
ATOM   14149 C  C     . LEU A 1 3229 ? 223.382 208.544 320.317 1.00 38.90 ? 3229 LEU A C     1 
ATOM   14150 O  O     . LEU A 1 3229 ? 223.402 209.343 321.261 1.00 38.07 ? 3229 LEU A O     1 
ATOM   14151 C  CB    . LEU A 1 3229 ? 222.032 209.096 318.279 1.00 35.68 ? 3229 LEU A CB    1 
ATOM   14152 C  CG    . LEU A 1 3229 ? 221.875 209.986 317.047 1.00 38.17 ? 3229 LEU A CG    1 
ATOM   14153 C  CD1   . LEU A 1 3229 ? 220.460 209.905 316.500 1.00 35.60 ? 3229 LEU A CD1   1 
ATOM   14154 C  CD2   . LEU A 1 3229 ? 222.237 211.415 317.400 1.00 33.67 ? 3229 LEU A CD2   1 
ATOM   14155 N  N     . GLU A 1 3230 ? 223.304 207.224 320.504 1.00 38.22 ? 3230 GLU A N     1 
ATOM   14156 C  CA    . GLU A 1 3230 ? 223.270 206.670 321.853 1.00 36.44 ? 3230 GLU A CA    1 
ATOM   14157 C  C     . GLU A 1 3230 ? 224.558 206.975 322.609 1.00 38.56 ? 3230 GLU A C     1 
ATOM   14158 O  O     . GLU A 1 3230 ? 224.524 207.306 323.799 1.00 38.72 ? 3230 GLU A O     1 
ATOM   14159 C  CB    . GLU A 1 3230 ? 223.027 205.162 321.795 1.00 34.97 ? 3230 GLU A CB    1 
ATOM   14160 C  CG    . GLU A 1 3230 ? 221.682 204.770 321.206 1.00 36.87 ? 3230 GLU A CG    1 
ATOM   14161 C  CD    . GLU A 1 3230 ? 221.695 203.384 320.593 1.00 43.93 ? 3230 GLU A CD    1 
ATOM   14162 O  OE1   . GLU A 1 3230 ? 222.753 202.721 320.641 1.00 42.69 ? 3230 GLU A OE1   1 
ATOM   14163 O  OE2   . GLU A 1 3230 ? 220.648 202.956 320.063 1.00 45.62 ? 3230 GLU A OE2   1 
ATOM   14164 N  N     . VAL A 1 3231 ? 225.703 206.865 321.935 1.00 35.72 ? 3231 VAL A N     1 
ATOM   14165 C  CA    . VAL A 1 3231 ? 226.982 207.139 322.586 1.00 33.47 ? 3231 VAL A CA    1 
ATOM   14166 C  C     . VAL A 1 3231 ? 227.111 208.624 322.905 1.00 38.89 ? 3231 VAL A C     1 
ATOM   14167 O  O     . VAL A 1 3231 ? 227.492 209.006 324.018 1.00 38.94 ? 3231 VAL A O     1 
ATOM   14168 C  CB    . VAL A 1 3231 ? 228.145 206.644 321.708 1.00 36.42 ? 3231 VAL A CB    1 
ATOM   14169 C  CG1   . VAL A 1 3231 ? 229.451 207.302 322.128 1.00 30.61 ? 3231 VAL A CG1   1 
ATOM   14170 C  CG2   . VAL A 1 3231 ? 228.256 205.128 321.779 1.00 33.48 ? 3231 VAL A CG2   1 
ATOM   14171 N  N     . LYS A 1 3232 ? 226.794 209.485 321.933 1.00 36.97 ? 3232 LYS A N     1 
ATOM   14172 C  CA    . LYS A 1 3232 ? 226.923 210.924 322.145 1.00 35.26 ? 3232 LYS A CA    1 
ATOM   14173 C  C     . LYS A 1 3232 ? 225.959 211.421 323.217 1.00 37.70 ? 3232 LYS A C     1 
ATOM   14174 O  O     . LYS A 1 3232 ? 226.334 212.241 324.062 1.00 39.07 ? 3232 LYS A O     1 
ATOM   14175 C  CB    . LYS A 1 3232 ? 226.697 211.672 320.832 1.00 36.72 ? 3232 LYS A CB    1 
ATOM   14176 C  CG    . LYS A 1 3232 ? 227.806 211.486 319.808 1.00 37.19 ? 3232 LYS A CG    1 
ATOM   14177 C  CD    . LYS A 1 3232 ? 229.180 211.599 320.450 1.00 31.53 ? 3232 LYS A CD    1 
ATOM   14178 C  CE    . LYS A 1 3232 ? 230.247 210.943 319.587 1.00 36.71 ? 3232 LYS A CE    1 
ATOM   14179 N  NZ    . LYS A 1 3232 ? 231.558 210.866 320.289 1.00 30.94 ? 3232 LYS A NZ    1 
ATOM   14180 N  N     . ASN A 1 3233 ? 224.711 210.945 323.192 1.00 34.86 ? 3233 ASN A N     1 
ATOM   14181 C  CA    . ASN A 1 3233 ? 223.739 211.376 324.192 1.00 35.56 ? 3233 ASN A CA    1 
ATOM   14182 C  C     . ASN A 1 3233 ? 224.140 210.917 325.589 1.00 38.93 ? 3233 ASN A C     1 
ATOM   14183 O  O     . ASN A 1 3233 ? 224.029 211.681 326.555 1.00 36.89 ? 3233 ASN A O     1 
ATOM   14184 C  CB    . ASN A 1 3233 ? 222.348 210.855 323.833 1.00 34.17 ? 3233 ASN A CB    1 
ATOM   14185 C  CG    . ASN A 1 3233 ? 221.237 211.692 324.436 1.00 37.48 ? 3233 ASN A CG    1 
ATOM   14186 O  OD1   . ASN A 1 3233 ? 221.293 212.069 325.607 1.00 40.13 ? 3233 ASN A OD1   1 
ATOM   14187 N  ND2   . ASN A 1 3233 ? 220.219 211.989 323.636 1.00 35.94 ? 3233 ASN A ND2   1 
ATOM   14188 N  N     . ALA A 1 3234 ? 224.603 209.670 325.716 1.00 38.96 ? 3234 ALA A N     1 
ATOM   14189 C  CA    . ALA A 1 3234 ? 225.030 209.172 327.019 1.00 37.22 ? 3234 ALA A CA    1 
ATOM   14190 C  C     . ALA A 1 3234 ? 226.246 209.932 327.531 1.00 38.81 ? 3234 ALA A C     1 
ATOM   14191 O  O     . ALA A 1 3234 ? 226.320 210.275 328.717 1.00 38.28 ? 3234 ALA A O     1 
ATOM   14192 C  CB    . ALA A 1 3234 ? 225.327 207.674 326.939 1.00 32.01 ? 3234 ALA A CB    1 
ATOM   14193 N  N     . ALA A 1 3235 ? 227.214 210.202 326.651 1.00 37.10 ? 3235 ALA A N     1 
ATOM   14194 C  CA    . ALA A 1 3235 ? 228.401 210.946 327.062 1.00 35.49 ? 3235 ALA A CA    1 
ATOM   14195 C  C     . ALA A 1 3235 ? 228.044 212.368 327.476 1.00 39.47 ? 3235 ALA A C     1 
ATOM   14196 O  O     . ALA A 1 3235 ? 228.576 212.887 328.465 1.00 39.03 ? 3235 ALA A O     1 
ATOM   14197 C  CB    . ALA A 1 3235 ? 229.432 210.957 325.934 1.00 31.49 ? 3235 ALA A CB    1 
ATOM   14198 N  N     . ALA A 1 3236 ? 227.150 213.016 326.728 1.00 38.46 ? 3236 ALA A N     1 
ATOM   14199 C  CA    . ALA A 1 3236 ? 226.731 214.368 327.080 1.00 34.63 ? 3236 ALA A CA    1 
ATOM   14200 C  C     . ALA A 1 3236 ? 225.980 214.389 328.406 1.00 38.19 ? 3236 ALA A C     1 
ATOM   14201 O  O     . ALA A 1 3236 ? 226.180 215.293 329.226 1.00 36.47 ? 3236 ALA A O     1 
ATOM   14202 C  CB    . ALA A 1 3236 ? 225.869 214.959 325.964 1.00 32.78 ? 3236 ALA A CB    1 
ATOM   14203 N  N     . ASN A 1 3237 ? 225.104 213.405 328.631 1.00 35.38 ? 3237 ASN A N     1 
ATOM   14204 C  CA    . ASN A 1 3237 ? 224.360 213.350 329.886 1.00 34.16 ? 3237 ASN A CA    1 
ATOM   14205 C  C     . ASN A 1 3237 ? 225.289 213.121 331.072 1.00 37.49 ? 3237 ASN A C     1 
ATOM   14206 O  O     . ASN A 1 3237 ? 225.133 213.753 332.123 1.00 39.46 ? 3237 ASN A O     1 
ATOM   14207 C  CB    . ASN A 1 3237 ? 223.296 212.255 329.818 1.00 35.34 ? 3237 ASN A CB    1 
ATOM   14208 C  CG    . ASN A 1 3237 ? 222.147 212.617 328.896 1.00 39.86 ? 3237 ASN A CG    1 
ATOM   14209 O  OD1   . ASN A 1 3237 ? 222.086 213.726 328.367 1.00 37.63 ? 3237 ASN A OD1   1 
ATOM   14210 N  ND2   . ASN A 1 3237 ? 221.228 211.678 328.700 1.00 34.19 ? 3237 ASN A ND2   1 
ATOM   14211 N  N     . ASP A 1 3238 ? 226.260 212.215 330.924 1.00 36.20 ? 3238 ASP A N     1 
ATOM   14212 C  CA    . ASP A 1 3238 ? 227.202 211.956 332.009 1.00 36.40 ? 3238 ASP A CA    1 
ATOM   14213 C  C     . ASP A 1 3238 ? 228.058 213.182 332.301 1.00 37.06 ? 3238 ASP A C     1 
ATOM   14214 O  O     . ASP A 1 3238 ? 228.315 213.505 333.466 1.00 37.04 ? 3238 ASP A O     1 
ATOM   14215 C  CB    . ASP A 1 3238 ? 228.083 210.754 331.664 1.00 35.55 ? 3238 ASP A CB    1 
ATOM   14216 C  CG    . ASP A 1 3238 ? 227.290 209.470 331.534 1.00 40.65 ? 3238 ASP A CG    1 
ATOM   14217 O  OD1   . ASP A 1 3238 ? 226.060 209.503 331.748 1.00 40.52 ? 3238 ASP A OD1   1 
ATOM   14218 O  OD2   . ASP A 1 3238 ? 227.897 208.425 331.217 1.00 36.82 ? 3238 ASP A OD2   1 
ATOM   14219 N  N     . LYS A 1 3239 ? 228.512 213.875 331.254 1.00 34.61 ? 3239 LYS A N     1 
ATOM   14220 C  CA    . LYS A 1 3239 ? 229.305 215.083 331.456 1.00 36.31 ? 3239 LYS A CA    1 
ATOM   14221 C  C     . LYS A 1 3239 ? 228.478 216.187 332.102 1.00 38.56 ? 3239 LYS A C     1 
ATOM   14222 O  O     . LYS A 1 3239 ? 228.980 216.923 332.960 1.00 40.17 ? 3239 LYS A O     1 
ATOM   14223 C  CB    . LYS A 1 3239 ? 229.887 215.555 330.123 1.00 36.88 ? 3239 LYS A CB    1 
ATOM   14224 C  CG    . LYS A 1 3239 ? 231.096 214.759 329.661 1.00 36.45 ? 3239 LYS A CG    1 
ATOM   14225 C  CD    . LYS A 1 3239 ? 231.524 215.162 328.259 1.00 35.89 ? 3239 LYS A CD    1 
ATOM   14226 C  CE    . LYS A 1 3239 ? 232.536 214.183 327.688 1.00 34.80 ? 3239 LYS A CE    1 
ATOM   14227 N  NZ    . LYS A 1 3239 ? 232.835 214.462 326.257 1.00 31.91 ? 3239 LYS A NZ    1 
ATOM   14228 N  N     . LEU A 1 3240 ? 227.212 216.322 331.701 1.00 38.25 ? 3240 LEU A N     1 
ATOM   14229 C  CA    . LEU A 1 3240 ? 226.347 217.330 332.305 1.00 35.58 ? 3240 LEU A CA    1 
ATOM   14230 C  C     . LEU A 1 3240 ? 226.065 217.024 333.770 1.00 39.22 ? 3240 LEU A C     1 
ATOM   14231 O  O     . LEU A 1 3240 ? 225.989 217.945 334.590 1.00 39.92 ? 3240 LEU A O     1 
ATOM   14232 C  CB    . LEU A 1 3240 ? 225.039 217.438 331.522 1.00 36.86 ? 3240 LEU A CB    1 
ATOM   14233 C  CG    . LEU A 1 3240 ? 224.975 218.547 330.471 1.00 39.77 ? 3240 LEU A CG    1 
ATOM   14234 C  CD1   . LEU A 1 3240 ? 223.590 218.619 329.847 1.00 32.39 ? 3240 LEU A CD1   1 
ATOM   14235 C  CD2   . LEU A 1 3240 ? 225.364 219.886 331.080 1.00 33.59 ? 3240 LEU A CD2   1 
ATOM   14236 N  N     . LYS A 1 3241 ? 225.907 215.745 334.118 1.00 36.74 ? 3241 LYS A N     1 
ATOM   14237 C  CA    . LYS A 1 3241 ? 225.650 215.358 335.500 1.00 34.93 ? 3241 LYS A CA    1 
ATOM   14238 C  C     . LYS A 1 3241 ? 226.846 215.592 336.414 1.00 35.77 ? 3241 LYS A C     1 
ATOM   14239 O  O     . LYS A 1 3241 ? 226.679 215.563 337.638 1.00 36.38 ? 3241 LYS A O     1 
ATOM   14240 C  CB    . LYS A 1 3241 ? 225.236 213.886 335.563 1.00 33.29 ? 3241 LYS A CB    1 
ATOM   14241 C  CG    . LYS A 1 3241 ? 223.813 213.619 335.101 1.00 32.27 ? 3241 LYS A CG    1 
ATOM   14242 C  CD    . LYS A 1 3241 ? 223.622 212.161 334.720 1.00 35.55 ? 3241 LYS A CD    1 
ATOM   14243 C  CE    . LYS A 1 3241 ? 222.350 211.963 333.910 1.00 32.84 ? 3241 LYS A CE    1 
ATOM   14244 N  NZ    . LYS A 1 3241 ? 222.266 210.590 333.338 1.00 34.41 ? 3241 LYS A NZ    1 
ATOM   14245 N  N     . LYS A 1 3242 ? 228.033 215.816 335.859 1.00 35.94 ? 3242 LYS A N     1 
ATOM   14246 C  CA    . LYS A 1 3242 ? 229.224 216.061 336.665 1.00 37.54 ? 3242 LYS A CA    1 
ATOM   14247 C  C     . LYS A 1 3242 ? 229.120 217.387 337.410 1.00 31.83 ? 3242 LYS A C     1 
ATOM   14248 O  O     . LYS A 1 3242 ? 228.372 218.282 337.012 0.00 28.42 ? 3242 LYS A O     1 
ATOM   14249 C  CB    . LYS A 1 3242 ? 230.477 216.049 335.788 1.00 36.48 ? 3242 LYS A CB    1 
ATOM   14250 C  CG    . LYS A 1 3242 ? 230.853 214.676 335.255 1.00 36.32 ? 3242 LYS A CG    1 
ATOM   14251 C  CD    . LYS A 1 3242 ? 232.002 214.765 334.265 1.00 37.12 ? 3242 LYS A CD    1 
ATOM   14252 C  CE    . LYS A 1 3242 ? 232.333 213.403 333.678 1.00 34.67 ? 3242 LYS A CE    1 
ATOM   14253 N  NZ    . LYS A 1 3242 ? 233.281 213.508 332.534 1.00 34.18 ? 3242 LYS A NZ    1 
ATOM   14254 N  N     . GLU A 1 3449 ? 229.379 224.813 329.028 1.00 35.51 ? 3449 GLU A N     1 
ATOM   14255 C  CA    . GLU A 1 3449 ? 229.385 225.525 327.755 1.00 38.41 ? 3449 GLU A CA    1 
ATOM   14256 C  C     . GLU A 1 3449 ? 229.756 224.590 326.608 1.00 41.25 ? 3449 GLU A C     1 
ATOM   14257 O  O     . GLU A 1 3449 ? 229.098 224.578 325.568 1.00 41.70 ? 3449 GLU A O     1 
ATOM   14258 C  CB    . GLU A 1 3449 ? 230.352 226.708 327.807 1.00 36.95 ? 3449 GLU A CB    1 
ATOM   14259 C  CG    . GLU A 1 3449 ? 230.057 227.695 328.924 1.00 35.67 ? 3449 GLU A CG    1 
ATOM   14260 C  CD    . GLU A 1 3449 ? 231.039 228.849 328.958 1.00 42.81 ? 3449 GLU A CD    1 
ATOM   14261 O  OE1   . GLU A 1 3449 ? 231.975 228.858 328.132 1.00 43.39 ? 3449 GLU A OE1   1 
ATOM   14262 O  OE2   . GLU A 1 3449 ? 230.874 229.747 329.810 1.00 39.68 ? 3449 GLU A OE2   1 
ATOM   14263 N  N     . GLU A 1 3450 ? 230.821 223.809 326.805 1.00 40.55 ? 3450 GLU A N     1 
ATOM   14264 C  CA    . GLU A 1 3450 ? 231.222 222.841 325.790 1.00 39.22 ? 3450 GLU A CA    1 
ATOM   14265 C  C     . GLU A 1 3450 ? 230.191 221.731 325.637 1.00 37.47 ? 3450 GLU A C     1 
ATOM   14266 O  O     . GLU A 1 3450 ? 230.001 221.211 324.531 1.00 40.12 ? 3450 GLU A O     1 
ATOM   14267 C  CB    . GLU A 1 3450 ? 232.591 222.254 326.133 1.00 37.29 ? 3450 GLU A CB    1 
ATOM   14268 C  CG    . GLU A 1 3450 ? 233.190 221.388 325.036 1.00 34.96 ? 3450 GLU A CG    1 
ATOM   14269 C  CD    . GLU A 1 3450 ? 234.677 221.159 325.219 1.00 40.69 ? 3450 GLU A CD    1 
ATOM   14270 O  OE1   . GLU A 1 3450 ? 235.202 221.493 326.301 1.00 40.03 ? 3450 GLU A OE1   1 
ATOM   14271 O  OE2   . GLU A 1 3450 ? 235.320 220.645 324.279 1.00 38.89 ? 3450 GLU A OE2   1 
ATOM   14272 N  N     . TYR A 1 3451 ? 229.519 221.355 326.728 1.00 36.10 ? 3451 TYR A N     1 
ATOM   14273 C  CA    . TYR A 1 3451 ? 228.477 220.337 326.646 1.00 36.43 ? 3451 TYR A CA    1 
ATOM   14274 C  C     . TYR A 1 3451 ? 227.304 220.802 325.794 1.00 37.71 ? 3451 TYR A C     1 
ATOM   14275 O  O     . TYR A 1 3451 ? 226.616 219.975 325.185 1.00 35.77 ? 3451 TYR A O     1 
ATOM   14276 C  CB    . TYR A 1 3451 ? 228.002 219.957 328.049 1.00 37.82 ? 3451 TYR A CB    1 
ATOM   14277 C  CG    . TYR A 1 3451 ? 229.125 219.738 329.039 1.00 39.02 ? 3451 TYR A CG    1 
ATOM   14278 C  CD1   . TYR A 1 3451 ? 230.237 218.974 328.702 1.00 38.15 ? 3451 TYR A CD1   1 
ATOM   14279 C  CD2   . TYR A 1 3451 ? 229.077 220.298 330.308 1.00 37.99 ? 3451 TYR A CD2   1 
ATOM   14280 C  CE1   . TYR A 1 3451 ? 231.265 218.774 329.602 1.00 38.49 ? 3451 TYR A CE1   1 
ATOM   14281 C  CE2   . TYR A 1 3451 ? 230.100 220.103 331.215 1.00 38.48 ? 3451 TYR A CE2   1 
ATOM   14282 C  CZ    . TYR A 1 3451 ? 231.192 219.340 330.857 1.00 42.95 ? 3451 TYR A CZ    1 
ATOM   14283 O  OH    . TYR A 1 3451 ? 232.213 219.143 331.758 1.00 45.01 ? 3451 TYR A OH    1 
ATOM   14284 N  N     . ALA A 1 3452 ? 227.058 222.114 325.743 1.00 40.27 ? 3452 ALA A N     1 
ATOM   14285 C  CA    . ALA A 1 3452 ? 226.021 222.638 324.861 1.00 38.88 ? 3452 ALA A CA    1 
ATOM   14286 C  C     . ALA A 1 3452 ? 226.373 222.392 323.399 1.00 39.33 ? 3452 ALA A C     1 
ATOM   14287 O  O     . ALA A 1 3452 ? 225.491 222.119 322.577 1.00 38.27 ? 3452 ALA A O     1 
ATOM   14288 C  CB    . ALA A 1 3452 ? 225.812 224.129 325.120 1.00 33.51 ? 3452 ALA A CB    1 
ATOM   14289 N  N     . VAL A 1 3453 ? 227.657 222.497 323.054 1.00 35.52 ? 3453 VAL A N     1 
ATOM   14290 C  CA    . VAL A 1 3453 ? 228.090 222.157 321.704 1.00 34.84 ? 3453 VAL A CA    1 
ATOM   14291 C  C     . VAL A 1 3453 ? 227.940 220.660 321.458 1.00 36.93 ? 3453 VAL A C     1 
ATOM   14292 O  O     . VAL A 1 3453 ? 227.560 220.232 320.361 1.00 35.86 ? 3453 VAL A O     1 
ATOM   14293 C  CB    . VAL A 1 3453 ? 229.538 222.629 321.472 1.00 34.12 ? 3453 VAL A CB    1 
ATOM   14294 C  CG1   . VAL A 1 3453 ? 229.974 222.338 320.043 1.00 32.51 ? 3453 VAL A CG1   1 
ATOM   14295 C  CG2   . VAL A 1 3453 ? 229.667 224.112 321.785 1.00 30.75 ? 3453 VAL A CG2   1 
ATOM   14296 N  N     . LEU A 1 3454 ? 228.234 219.843 322.473 1.00 35.34 ? 3454 LEU A N     1 
ATOM   14297 C  CA    . LEU A 1 3454 ? 228.134 218.395 322.315 1.00 36.04 ? 3454 LEU A CA    1 
ATOM   14298 C  C     . LEU A 1 3454 ? 226.697 217.959 322.061 1.00 37.88 ? 3454 LEU A C     1 
ATOM   14299 O  O     . LEU A 1 3454 ? 226.443 217.115 321.193 1.00 37.52 ? 3454 LEU A O     1 
ATOM   14300 C  CB    . LEU A 1 3454 ? 228.697 217.694 323.551 1.00 37.98 ? 3454 LEU A CB    1 
ATOM   14301 C  CG    . LEU A 1 3454 ? 229.045 216.213 323.390 1.00 38.92 ? 3454 LEU A CG    1 
ATOM   14302 C  CD1   . LEU A 1 3454 ? 230.159 216.030 322.370 1.00 32.67 ? 3454 LEU A CD1   1 
ATOM   14303 C  CD2   . LEU A 1 3454 ? 229.431 215.602 324.728 1.00 33.91 ? 3454 LEU A CD2   1 
ATOM   14304 N  N     . ILE A 1 3455 ? 225.740 218.516 322.809 1.00 35.87 ? 3455 ILE A N     1 
ATOM   14305 C  CA    . ILE A 1 3455 ? 224.343 218.166 322.577 1.00 37.04 ? 3455 ILE A CA    1 
ATOM   14306 C  C     . ILE A 1 3455 ? 223.857 218.749 321.256 1.00 36.73 ? 3455 ILE A C     1 
ATOM   14307 O  O     . ILE A 1 3455 ? 222.990 218.166 320.593 1.00 35.72 ? 3455 ILE A O     1 
ATOM   14308 C  CB    . ILE A 1 3455 ? 223.460 218.612 323.760 1.00 36.36 ? 3455 ILE A CB    1 
ATOM   14309 C  CG1   . ILE A 1 3455 ? 223.449 220.135 323.896 1.00 36.94 ? 3455 ILE A CG1   1 
ATOM   14310 C  CG2   . ILE A 1 3455 ? 223.935 217.966 325.051 1.00 28.33 ? 3455 ILE A CG2   1 
ATOM   14311 C  CD1   . ILE A 1 3455 ? 222.419 220.652 324.877 1.00 31.58 ? 3455 ILE A CD1   1 
ATOM   14312 N  N     . SER A 1 3456 ? 224.395 219.905 320.853 1.00 34.64 ? 3456 SER A N     1 
ATOM   14313 C  CA    . SER A 1 3456 ? 224.079 220.444 319.535 1.00 36.57 ? 3456 SER A CA    1 
ATOM   14314 C  C     . SER A 1 3456 ? 224.601 219.531 318.434 1.00 37.44 ? 3456 SER A C     1 
ATOM   14315 O  O     . SER A 1 3456 ? 223.939 219.339 317.408 1.00 36.99 ? 3456 SER A O     1 
ATOM   14316 C  CB    . SER A 1 3456 ? 224.658 221.851 319.389 1.00 32.94 ? 3456 SER A CB    1 
ATOM   14317 O  OG    . SER A 1 3456 ? 226.043 221.802 319.086 1.00 36.85 ? 3456 SER A OG    1 
ATOM   14318 N  N     . GLU A 1 3457 ? 225.794 218.964 318.629 1.00 34.30 ? 3457 GLU A N     1 
ATOM   14319 C  CA    . GLU A 1 3457 ? 226.322 218.000 317.670 1.00 35.11 ? 3457 GLU A CA    1 
ATOM   14320 C  C     . GLU A 1 3457 ? 225.441 216.759 317.600 1.00 37.23 ? 3457 GLU A C     1 
ATOM   14321 O  O     . GLU A 1 3457 ? 225.190 216.227 316.513 1.00 38.82 ? 3457 GLU A O     1 
ATOM   14322 C  CB    . GLU A 1 3457 ? 227.757 217.626 318.041 1.00 30.82 ? 3457 GLU A CB    1 
ATOM   14323 C  CG    . GLU A 1 3457 ? 228.503 216.846 316.968 1.00 31.64 ? 3457 GLU A CG    1 
ATOM   14324 C  CD    . GLU A 1 3457 ? 228.328 215.347 317.109 1.00 41.80 ? 3457 GLU A CD    1 
ATOM   14325 O  OE1   . GLU A 1 3457 ? 228.087 214.878 318.242 1.00 43.62 ? 3457 GLU A OE1   1 
ATOM   14326 O  OE2   . GLU A 1 3457 ? 228.434 214.636 316.088 1.00 41.20 ? 3457 GLU A OE2   1 
ATOM   14327 N  N     . ALA A 1 3458 ? 224.966 216.282 318.753 1.00 35.05 ? 3458 ALA A N     1 
ATOM   14328 C  CA    . ALA A 1 3458 ? 224.053 215.144 318.763 1.00 36.19 ? 3458 ALA A CA    1 
ATOM   14329 C  C     . ALA A 1 3458 ? 222.744 215.484 318.061 1.00 37.76 ? 3458 ALA A C     1 
ATOM   14330 O  O     . ALA A 1 3458 ? 222.196 214.657 317.320 1.00 38.95 ? 3458 ALA A O     1 
ATOM   14331 C  CB    . ALA A 1 3458 ? 223.792 214.692 320.200 1.00 31.95 ? 3458 ALA A CB    1 
ATOM   14332 N  N     . GLN A 1 3459 ? 222.225 216.694 318.285 1.00 37.77 ? 3459 GLN A N     1 
ATOM   14333 C  CA    . GLN A 1 3459 ? 220.998 217.109 317.612 1.00 37.96 ? 3459 GLN A CA    1 
ATOM   14334 C  C     . GLN A 1 3459 ? 221.200 217.195 316.104 1.00 38.14 ? 3459 GLN A C     1 
ATOM   14335 O  O     . GLN A 1 3459 ? 220.304 216.845 315.328 1.00 37.20 ? 3459 GLN A O     1 
ATOM   14336 C  CB    . GLN A 1 3459 ? 220.518 218.447 318.172 1.00 32.77 ? 3459 GLN A CB    1 
ATOM   14337 C  CG    . GLN A 1 3459 ? 219.175 218.903 317.623 1.00 34.91 ? 3459 GLN A CG    1 
ATOM   14338 C  CD    . GLN A 1 3459 ? 218.654 220.146 318.314 1.00 40.82 ? 3459 GLN A CD    1 
ATOM   14339 O  OE1   . GLN A 1 3459 ? 218.386 220.137 319.516 1.00 37.46 ? 3459 GLN A OE1   1 
ATOM   14340 N  NE2   . GLN A 1 3459 ? 218.506 221.226 317.555 1.00 34.15 ? 3459 GLN A NE2   1 
ATOM   14341 N  N     . ALA A 1 3460 ? 222.371 217.671 315.672 1.00 36.07 ? 3460 ALA A N     1 
ATOM   14342 C  CA    . ALA A 1 3460 ? 222.666 217.723 314.243 1.00 35.03 ? 3460 ALA A CA    1 
ATOM   14343 C  C     . ALA A 1 3460 ? 222.688 216.325 313.635 1.00 37.93 ? 3460 ALA A C     1 
ATOM   14344 O  O     . ALA A 1 3460 ? 222.198 216.118 312.519 1.00 38.85 ? 3460 ALA A O     1 
ATOM   14345 C  CB    . ALA A 1 3460 ? 223.998 218.434 314.007 1.00 27.91 ? 3460 ALA A CB    1 
ATOM   14346 N  N     . ILE A 1 3461 ? 223.258 215.356 314.354 1.00 35.07 ? 3461 ILE A N     1 
ATOM   14347 C  CA    . ILE A 1 3461 ? 223.253 213.976 313.880 1.00 34.96 ? 3461 ILE A CA    1 
ATOM   14348 C  C     . ILE A 1 3461 ? 221.831 213.430 313.831 1.00 35.17 ? 3461 ILE A C     1 
ATOM   14349 O  O     . ILE A 1 3461 ? 221.495 212.633 312.945 1.00 36.26 ? 3461 ILE A O     1 
ATOM   14350 C  CB    . ILE A 1 3461 ? 224.169 213.107 314.760 1.00 33.09 ? 3461 ILE A CB    1 
ATOM   14351 C  CG1   . ILE A 1 3461 ? 225.606 213.631 314.712 1.00 35.00 ? 3461 ILE A CG1   1 
ATOM   14352 C  CG2   . ILE A 1 3461 ? 224.134 211.656 314.311 1.00 34.30 ? 3461 ILE A CG2   1 
ATOM   14353 C  CD1   . ILE A 1 3461 ? 226.129 213.857 313.310 1.00 34.60 ? 3461 ILE A CD1   1 
ATOM   14354 N  N     . LYS A 1 3462 ? 220.974 213.845 314.769 1.00 33.51 ? 3462 LYS A N     1 
ATOM   14355 C  CA    . LYS A 1 3462 ? 219.576 213.419 314.738 1.00 34.82 ? 3462 LYS A CA    1 
ATOM   14356 C  C     . LYS A 1 3462 ? 218.905 213.842 313.438 1.00 32.99 ? 3462 LYS A C     1 
ATOM   14357 O  O     . LYS A 1 3462 ? 218.124 213.079 312.857 1.00 32.52 ? 3462 LYS A O     1 
ATOM   14358 C  CB    . LYS A 1 3462 ? 218.823 213.991 315.940 1.00 32.51 ? 3462 LYS A CB    1 
ATOM   14359 C  CG    . LYS A 1 3462 ? 219.184 213.353 317.270 1.00 34.64 ? 3462 LYS A CG    1 
ATOM   14360 C  CD    . LYS A 1 3462 ? 218.102 213.593 318.311 1.00 32.67 ? 3462 LYS A CD    1 
ATOM   14361 C  CE    . LYS A 1 3462 ? 216.838 212.814 317.986 1.00 31.00 ? 3462 LYS A CE    1 
ATOM   14362 N  NZ    . LYS A 1 3462 ? 217.104 211.355 317.860 1.00 30.22 ? 3462 LYS A NZ    1 
ATOM   14363 N  N     . ALA A 1 3463 ? 219.191 215.059 312.970 1.00 34.07 ? 3463 ALA A N     1 
ATOM   14364 C  CA    . ALA A 1 3463 ? 218.689 215.485 311.669 1.00 36.75 ? 3463 ALA A CA    1 
ATOM   14365 C  C     . ALA A 1 3463 ? 219.259 214.622 310.552 1.00 36.87 ? 3463 ALA A C     1 
ATOM   14366 O  O     . ALA A 1 3463 ? 218.554 214.287 309.592 1.00 38.31 ? 3463 ALA A O     1 
ATOM   14367 C  CB    . ALA A 1 3463 ? 219.019 216.959 311.434 1.00 28.57 ? 3463 ALA A CB    1 
ATOM   14368 N  N     . ASP A 1 3464 ? 220.540 214.255 310.656 1.00 32.95 ? 3464 ASP A N     1 
ATOM   14369 C  CA    . ASP A 1 3464 ? 221.142 213.373 309.662 1.00 33.86 ? 3464 ASP A CA    1 
ATOM   14370 C  C     . ASP A 1 3464 ? 220.467 212.007 309.657 1.00 36.45 ? 3464 ASP A C     1 
ATOM   14371 O  O     . ASP A 1 3464 ? 220.208 211.438 308.590 1.00 35.01 ? 3464 ASP A O     1 
ATOM   14372 C  CB    . ASP A 1 3464 ? 222.640 213.231 309.926 1.00 34.00 ? 3464 ASP A CB    1 
ATOM   14373 C  CG    . ASP A 1 3464 ? 223.394 212.684 308.730 1.00 38.62 ? 3464 ASP A CG    1 
ATOM   14374 O  OD1   . ASP A 1 3464 ? 222.801 212.611 307.633 1.00 40.12 ? 3464 ASP A OD1   1 
ATOM   14375 O  OD2   . ASP A 1 3464 ? 224.580 212.328 308.887 1.00 39.00 ? 3464 ASP A OD2   1 
ATOM   14376 N  N     . LEU A 1 3465 ? 220.179 211.461 310.842 1.00 34.46 ? 3465 LEU A N     1 
ATOM   14377 C  CA    . LEU A 1 3465 ? 219.478 210.184 310.918 1.00 31.51 ? 3465 LEU A CA    1 
ATOM   14378 C  C     . LEU A 1 3465 ? 218.069 210.299 310.350 1.00 36.17 ? 3465 LEU A C     1 
ATOM   14379 O  O     . LEU A 1 3465 ? 217.580 209.376 309.690 1.00 36.25 ? 3465 LEU A O     1 
ATOM   14380 C  CB    . LEU A 1 3465 ? 219.444 209.689 312.364 1.00 30.51 ? 3465 LEU A CB    1 
ATOM   14381 C  CG    . LEU A 1 3465 ? 218.885 208.288 312.622 1.00 33.76 ? 3465 LEU A CG    1 
ATOM   14382 C  CD1   . LEU A 1 3465 ? 219.692 207.592 313.703 1.00 33.90 ? 3465 LEU A CD1   1 
ATOM   14383 C  CD2   . LEU A 1 3465 ? 217.418 208.347 313.019 1.00 28.51 ? 3465 LEU A CD2   1 
ATOM   14384 N  N     . ALA A 1 3466 ? 217.397 211.424 310.607 1.00 35.53 ? 3466 ALA A N     1 
ATOM   14385 C  CA    . ALA A 1 3466 ? 216.074 211.644 310.030 1.00 34.57 ? 3466 ALA A CA    1 
ATOM   14386 C  C     . ALA A 1 3466 ? 216.142 211.693 308.509 1.00 35.98 ? 3466 ALA A C     1 
ATOM   14387 O  O     . ALA A 1 3466 ? 215.268 211.150 307.823 1.00 35.66 ? 3466 ALA A O     1 
ATOM   14388 C  CB    . ALA A 1 3466 ? 215.465 212.930 310.585 1.00 27.69 ? 3466 ALA A CB    1 
ATOM   14389 N  N     . ALA A 1 3467 ? 217.171 212.346 307.964 1.00 31.10 ? 3467 ALA A N     1 
ATOM   14390 C  CA    . ALA A 1 3467 ? 217.352 212.362 306.517 1.00 31.38 ? 3467 ALA A CA    1 
ATOM   14391 C  C     . ALA A 1 3467 ? 217.660 210.968 305.985 1.00 33.71 ? 3467 ALA A C     1 
ATOM   14392 O  O     . ALA A 1 3467 ? 217.225 210.606 304.885 1.00 34.50 ? 3467 ALA A O     1 
ATOM   14393 C  CB    . ALA A 1 3467 ? 218.461 213.340 306.136 1.00 28.44 ? 3467 ALA A CB    1 
ATOM   14394 N  N     . VAL A 1 3468 ? 218.420 210.177 306.745 1.00 31.64 ? 3468 VAL A N     1 
ATOM   14395 C  CA    . VAL A 1 3468 ? 218.765 208.828 306.308 1.00 29.36 ? 3468 VAL A CA    1 
ATOM   14396 C  C     . VAL A 1 3468 ? 217.535 207.926 306.324 1.00 30.04 ? 3468 VAL A C     1 
ATOM   14397 O  O     . VAL A 1 3468 ? 217.271 207.196 305.363 1.00 32.08 ? 3468 VAL A O     1 
ATOM   14398 C  CB    . VAL A 1 3468 ? 219.899 208.257 307.178 1.00 33.83 ? 3468 VAL A CB    1 
ATOM   14399 C  CG1   . VAL A 1 3468 ? 219.980 206.746 307.028 1.00 33.70 ? 3468 VAL A CG1   1 
ATOM   14400 C  CG2   . VAL A 1 3468 ? 221.226 208.899 306.804 1.00 32.66 ? 3468 VAL A CG2   1 
ATOM   14401 N  N     . GLU A 1 3469 ? 216.763 207.965 307.415 1.00 32.54 ? 3469 GLU A N     1 
ATOM   14402 C  CA    . GLU A 1 3469 ? 215.616 207.067 307.533 1.00 32.21 ? 3469 GLU A CA    1 
ATOM   14403 C  C     . GLU A 1 3469 ? 214.537 207.409 306.513 1.00 35.23 ? 3469 GLU A C     1 
ATOM   14404 O  O     . GLU A 1 3469 ? 213.878 206.511 305.975 1.00 38.26 ? 3469 GLU A O     1 
ATOM   14405 C  CB    . GLU A 1 3469 ? 215.053 207.099 308.955 1.00 30.24 ? 3469 GLU A CB    1 
ATOM   14406 C  CG    . GLU A 1 3469 ? 214.483 208.437 309.394 1.00 34.59 ? 3469 GLU A CG    1 
ATOM   14407 C  CD    . GLU A 1 3469 ? 213.928 208.396 310.804 1.00 37.95 ? 3469 GLU A CD    1 
ATOM   14408 O  OE1   . GLU A 1 3469 ? 212.949 207.658 311.037 1.00 35.43 ? 3469 GLU A OE1   1 
ATOM   14409 O  OE2   . GLU A 1 3469 ? 214.471 209.104 311.679 1.00 41.41 ? 3469 GLU A OE2   1 
ATOM   14410 N  N     . ALA A 1 3470 ? 214.341 208.700 306.232 1.00 33.04 ? 3470 ALA A N     1 
ATOM   14411 C  CA    . ALA A 1 3470 ? 213.402 209.092 305.187 1.00 34.07 ? 3470 ALA A CA    1 
ATOM   14412 C  C     . ALA A 1 3470 ? 213.871 208.605 303.824 1.00 35.82 ? 3470 ALA A C     1 
ATOM   14413 O  O     . ALA A 1 3470 ? 213.060 208.183 302.991 1.00 35.91 ? 3470 ALA A O     1 
ATOM   14414 C  CB    . ALA A 1 3470 ? 213.219 210.609 305.186 1.00 30.80 ? 3470 ALA A CB    1 
ATOM   14415 N  N     . LYS A 1 3471 ? 215.182 208.658 303.579 1.00 30.83 ? 3471 LYS A N     1 
ATOM   14416 C  CA    . LYS A 1 3471 ? 215.725 208.173 302.316 1.00 28.10 ? 3471 LYS A CA    1 
ATOM   14417 C  C     . LYS A 1 3471 ? 215.562 206.663 302.189 1.00 29.94 ? 3471 LYS A C     1 
ATOM   14418 O  O     . LYS A 1 3471 ? 215.360 206.146 301.084 1.00 30.76 ? 3471 LYS A O     1 
ATOM   14419 C  CB    . LYS A 1 3471 ? 217.195 208.574 302.199 1.00 28.88 ? 3471 LYS A CB    1 
ATOM   14420 C  CG    . LYS A 1 3471 ? 217.853 208.201 300.883 1.00 29.59 ? 3471 LYS A CG    1 
ATOM   14421 C  CD    . LYS A 1 3471 ? 219.338 208.519 300.913 1.00 29.89 ? 3471 LYS A CD    1 
ATOM   14422 C  CE    . LYS A 1 3471 ? 219.768 209.271 299.666 1.00 32.07 ? 3471 LYS A CE    1 
ATOM   14423 N  NZ    . LYS A 1 3471 ? 221.249 209.308 299.523 1.00 33.47 ? 3471 LYS A NZ    1 
ATOM   14424 N  N     . VAL A 1 3472 ? 215.651 205.942 303.308 1.00 33.43 ? 3472 VAL A N     1 
ATOM   14425 C  CA    . VAL A 1 3472 ? 215.456 204.494 303.279 1.00 31.08 ? 3472 VAL A CA    1 
ATOM   14426 C  C     . VAL A 1 3472 ? 214.021 204.161 302.891 1.00 32.88 ? 3472 VAL A C     1 
ATOM   14427 O  O     . VAL A 1 3472 ? 213.772 203.300 302.038 1.00 34.73 ? 3472 VAL A O     1 
ATOM   14428 C  CB    . VAL A 1 3472 ? 215.830 203.874 304.638 1.00 31.29 ? 3472 VAL A CB    1 
ATOM   14429 C  CG1   . VAL A 1 3472 ? 215.203 202.496 304.792 1.00 28.59 ? 3472 VAL A CG1   1 
ATOM   14430 C  CG2   . VAL A 1 3472 ? 217.334 203.794 304.790 1.00 31.88 ? 3472 VAL A CG2   1 
ATOM   14431 N  N     . ASN A 1 3473 ? 213.055 204.842 303.513 1.00 33.02 ? 3473 ASN A N     1 
ATOM   14432 C  CA    . ASN A 1 3473 ? 211.652 204.556 303.235 1.00 30.91 ? 3473 ASN A CA    1 
ATOM   14433 C  C     . ASN A 1 3473 ? 211.278 204.931 301.807 1.00 32.25 ? 3473 ASN A C     1 
ATOM   14434 O  O     . ASN A 1 3473 ? 210.555 204.187 301.133 1.00 34.98 ? 3473 ASN A O     1 
ATOM   14435 C  CB    . ASN A 1 3473 ? 210.760 205.292 304.234 1.00 28.38 ? 3473 ASN A CB    1 
ATOM   14436 C  CG    . ASN A 1 3473 ? 211.048 204.903 305.669 1.00 34.77 ? 3473 ASN A CG    1 
ATOM   14437 O  OD1   . ASN A 1 3473 ? 211.894 204.050 305.934 1.00 35.30 ? 3473 ASN A OD1   1 
ATOM   14438 N  ND2   . ASN A 1 3473 ? 210.344 205.528 306.605 1.00 33.37 ? 3473 ASN A ND2   1 
ATOM   14439 N  N     . ARG A 1 3474 ? 211.754 206.083 301.329 1.00 28.87 ? 3474 ARG A N     1 
ATOM   14440 C  CA    . ARG A 1 3474 ? 211.423 206.506 299.973 1.00 29.61 ? 3474 ARG A CA    1 
ATOM   14441 C  C     . ARG A 1 3474 ? 212.053 205.588 298.934 1.00 31.20 ? 3474 ARG A C     1 
ATOM   14442 O  O     . ARG A 1 3474 ? 211.415 205.245 297.933 1.00 31.62 ? 3474 ARG A O     1 
ATOM   14443 C  CB    . ARG A 1 3474 ? 211.861 207.954 299.751 1.00 29.01 ? 3474 ARG A CB    1 
ATOM   14444 C  CG    . ARG A 1 3474 ? 211.477 208.507 298.390 1.00 27.19 ? 3474 ARG A CG    1 
ATOM   14445 C  CD    . ARG A 1 3474 ? 211.902 209.954 298.229 1.00 28.20 ? 3474 ARG A CD    1 
ATOM   14446 N  NE    . ARG A 1 3474 ? 213.351 210.110 298.256 1.00 34.35 ? 3474 ARG A NE    1 
ATOM   14447 C  CZ    . ARG A 1 3474 ? 213.974 211.279 298.322 1.00 37.36 ? 3474 ARG A CZ    1 
ATOM   14448 N  NH1   . ARG A 1 3474 ? 213.304 212.418 298.365 1.00 35.49 ? 3474 ARG A NH1   1 
ATOM   14449 N  NH2   . ARG A 1 3474 ? 215.304 211.305 298.342 1.00 37.57 ? 3474 ARG A NH2   1 
ATOM   14450 N  N     . SER A 1 3475 ? 213.304 205.179 299.155 1.00 30.53 ? 3475 SER A N     1 
ATOM   14451 C  CA    . SER A 1 3475 ? 213.962 204.285 298.207 1.00 30.76 ? 3475 SER A CA    1 
ATOM   14452 C  C     . SER A 1 3475 ? 213.365 202.885 298.264 1.00 29.04 ? 3475 SER A C     1 
ATOM   14453 O  O     . SER A 1 3475 ? 213.287 202.197 297.240 1.00 33.31 ? 3475 SER A O     1 
ATOM   14454 C  CB    . SER A 1 3475 ? 215.465 204.243 298.480 1.00 32.55 ? 3475 SER A CB    1 
ATOM   14455 O  OG    . SER A 1 3475 ? 216.117 203.363 297.583 1.00 37.43 ? 3475 SER A OG    1 
ATOM   14456 N  N     . THR A 1 3476 ? 212.954 202.441 299.454 1.00 28.62 ? 3476 THR A N     1 
ATOM   14457 C  CA    . THR A 1 3476 ? 212.276 201.154 299.565 1.00 28.99 ? 3476 THR A CA    1 
ATOM   14458 C  C     . THR A 1 3476 ? 210.931 201.182 298.851 1.00 28.57 ? 3476 THR A C     1 
ATOM   14459 O  O     . THR A 1 3476 ? 210.560 200.217 298.173 1.00 34.35 ? 3476 THR A O     1 
ATOM   14460 C  CB    . THR A 1 3476 ? 212.098 200.778 301.036 1.00 28.01 ? 3476 THR A CB    1 
ATOM   14461 O  OG1   . THR A 1 3476 ? 213.374 200.792 301.690 1.00 32.04 ? 3476 THR A OG1   1 
ATOM   14462 C  CG2   . THR A 1 3476 ? 211.486 199.394 301.167 1.00 24.11 ? 3476 THR A CG2   1 
ATOM   14463 N  N     . ALA A 1 3477 ? 210.187 202.281 298.994 1.00 29.02 ? 3477 ALA A N     1 
ATOM   14464 C  CA    . ALA A 1 3477 ? 208.934 202.430 298.260 1.00 33.53 ? 3477 ALA A CA    1 
ATOM   14465 C  C     . ALA A 1 3477 ? 209.183 202.503 296.760 1.00 30.75 ? 3477 ALA A C     1 
ATOM   14466 O  O     . ALA A 1 3477 ? 208.409 201.956 295.965 1.00 28.94 ? 3477 ALA A O     1 
ATOM   14467 C  CB    . ALA A 1 3477 ? 208.184 203.671 298.744 1.00 29.54 ? 3477 ALA A CB    1 
ATOM   14468 N  N     . LEU A 1 3478 ? 210.258 203.185 296.353 1.00 29.50 ? 3478 LEU A N     1 
ATOM   14469 C  CA    . LEU A 1 3478 ? 210.641 203.192 294.946 1.00 26.09 ? 3478 LEU A CA    1 
ATOM   14470 C  C     . LEU A 1 3478 ? 210.964 201.787 294.460 1.00 28.22 ? 3478 LEU A C     1 
ATOM   14471 O  O     . LEU A 1 3478 ? 210.548 201.388 293.368 1.00 29.71 ? 3478 LEU A O     1 
ATOM   14472 C  CB    . LEU A 1 3478 ? 211.838 204.119 294.733 1.00 23.67 ? 3478 LEU A CB    1 
ATOM   14473 C  CG    . LEU A 1 3478 ? 212.406 204.191 293.314 1.00 31.25 ? 3478 LEU A CG    1 
ATOM   14474 C  CD1   . LEU A 1 3478 ? 211.451 204.919 292.386 1.00 26.62 ? 3478 LEU A CD1   1 
ATOM   14475 C  CD2   . LEU A 1 3478 ? 213.771 204.855 293.312 1.00 27.80 ? 3478 LEU A CD2   1 
ATOM   14476 N  N     . LEU A 1 3479 ? 211.702 201.019 295.265 1.00 24.19 ? 3479 LEU A N     1 
ATOM   14477 C  CA    . LEU A 1 3479 ? 212.023 199.646 294.893 1.00 24.98 ? 3479 LEU A CA    1 
ATOM   14478 C  C     . LEU A 1 3479 ? 210.767 198.792 294.796 1.00 27.51 ? 3479 LEU A C     1 
ATOM   14479 O  O     . LEU A 1 3479 ? 210.631 197.976 293.877 1.00 31.82 ? 3479 LEU A O     1 
ATOM   14480 C  CB    . LEU A 1 3479 ? 213.006 199.050 295.899 1.00 27.69 ? 3479 LEU A CB    1 
ATOM   14481 C  CG    . LEU A 1 3479 ? 214.480 199.339 295.623 1.00 26.15 ? 3479 LEU A CG    1 
ATOM   14482 C  CD1   . LEU A 1 3479 ? 215.358 198.767 296.720 1.00 26.01 ? 3479 LEU A CD1   1 
ATOM   14483 C  CD2   . LEU A 1 3479 ? 214.874 198.780 294.268 1.00 28.14 ? 3479 LEU A CD2   1 
ATOM   14484 N  N     . LYS A 1 3480 ? 209.840 198.958 295.741 1.00 28.86 ? 3480 LYS A N     1 
ATOM   14485 C  CA    . LYS A 1 3480 ? 208.573 198.241 295.662 1.00 28.65 ? 3480 LYS A CA    1 
ATOM   14486 C  C     . LYS A 1 3480 ? 207.769 198.689 294.448 1.00 28.42 ? 3480 LYS A C     1 
ATOM   14487 O  O     . LYS A 1 3480 ? 207.124 197.871 293.783 1.00 28.57 ? 3480 LYS A O     1 
ATOM   14488 C  CB    . LYS A 1 3480 ? 207.775 198.442 296.952 1.00 27.94 ? 3480 LYS A CB    1 
ATOM   14489 C  CG    . LYS A 1 3480 ? 206.493 197.625 297.041 1.00 28.66 ? 3480 LYS A CG    1 
ATOM   14490 C  CD    . LYS A 1 3480 ? 205.265 198.453 296.687 1.00 32.26 ? 3480 LYS A CD    1 
ATOM   14491 C  CE    . LYS A 1 3480 ? 204.981 199.502 297.750 1.00 33.17 ? 3480 LYS A CE    1 
ATOM   14492 N  NZ    . LYS A 1 3480 ? 203.779 200.316 297.420 1.00 33.36 ? 3480 LYS A NZ    1 
ATOM   14493 N  N     . SER A 1 3481 ? 207.795 199.990 294.145 1.00 28.06 ? 3481 SER A N     1 
ATOM   14494 C  CA    . SER A 1 3481 ? 207.114 200.489 292.954 1.00 25.71 ? 3481 SER A CA    1 
ATOM   14495 C  C     . SER A 1 3481 ? 207.803 200.024 291.678 1.00 28.74 ? 3481 SER A C     1 
ATOM   14496 O  O     . SER A 1 3481 ? 207.154 199.909 290.632 1.00 28.66 ? 3481 SER A O     1 
ATOM   14497 C  CB    . SER A 1 3481 ? 207.042 202.015 292.996 1.00 26.97 ? 3481 SER A CB    1 
ATOM   14498 O  OG    . SER A 1 3481 ? 206.347 202.525 291.873 1.00 37.75 ? 3481 SER A OG    1 
ATOM   14499 N  N     . LEU A 1 3482 ? 209.106 199.760 291.739 1.00 29.42 ? 3482 LEU A N     1 
ATOM   14500 C  CA    . LEU A 1 3482 ? 209.863 199.262 290.599 1.00 27.33 ? 3482 LEU A CA    1 
ATOM   14501 C  C     . LEU A 1 3482 ? 209.946 197.743 290.568 1.00 30.64 ? 3482 LEU A C     1 
ATOM   14502 O  O     . LEU A 1 3482 ? 210.677 197.193 289.738 1.00 37.28 ? 3482 LEU A O     1 
ATOM   14503 C  CB    . LEU A 1 3482 ? 211.274 199.859 290.599 1.00 23.09 ? 3482 LEU A CB    1 
ATOM   14504 C  CG    . LEU A 1 3482 ? 211.391 201.347 290.264 1.00 24.50 ? 3482 LEU A CG    1 
ATOM   14505 C  CD1   . LEU A 1 3482 ? 212.846 201.746 290.087 1.00 22.60 ? 3482 LEU A CD1   1 
ATOM   14506 C  CD2   . LEU A 1 3482 ? 210.592 201.676 289.016 1.00 25.53 ? 3482 LEU A CD2   1 
ATOM   14507 N  N     . SER A 1 3483 ? 209.230 197.057 291.463 1.00 30.49 ? 3483 SER A N     1 
ATOM   14508 C  CA    . SER A 1 3483 ? 209.248 195.598 291.463 1.00 27.93 ? 3483 SER A CA    1 
ATOM   14509 C  C     . SER A 1 3483 ? 208.660 195.036 290.174 1.00 28.27 ? 3483 SER A C     1 
ATOM   14510 O  O     . SER A 1 3483 ? 209.208 194.090 289.596 1.00 33.80 ? 3483 SER A O     1 
ATOM   14511 C  CB    . SER A 1 3483 ? 208.487 195.066 292.677 1.00 32.76 ? 3483 SER A CB    1 
ATOM   14512 O  OG    . SER A 1 3483 ? 208.416 193.650 292.660 1.00 40.17 ? 3483 SER A OG    1 
ATOM   14513 N  N     . ALA A 1 3484 ? 207.544 195.605 289.710 1.00 30.75 ? 3484 ALA A N     1 
ATOM   14514 C  CA    . ALA A 1 3484 ? 206.924 195.118 288.483 1.00 25.80 ? 3484 ALA A CA    1 
ATOM   14515 C  C     . ALA A 1 3484 ? 207.822 195.349 287.276 1.00 29.95 ? 3484 ALA A C     1 
ATOM   14516 O  O     . ALA A 1 3484 ? 207.979 194.463 286.428 1.00 28.35 ? 3484 ALA A O     1 
ATOM   14517 C  CB    . ALA A 1 3484 ? 205.566 195.789 288.280 1.00 22.60 ? 3484 ALA A CB    1 
ATOM   14518 N  N     . GLU A 1 3485 ? 208.423 196.537 287.180 1.00 32.35 ? 3485 GLU A N     1 
ATOM   14519 C  CA    . GLU A 1 3485 ? 209.320 196.823 286.066 1.00 28.68 ? 3485 GLU A CA    1 
ATOM   14520 C  C     . GLU A 1 3485 ? 210.556 195.934 286.113 1.00 28.89 ? 3485 GLU A C     1 
ATOM   14521 O  O     . GLU A 1 3485 ? 211.034 195.472 285.071 1.00 28.27 ? 3485 GLU A O     1 
ATOM   14522 C  CB    . GLU A 1 3485 ? 209.711 198.300 286.075 1.00 27.57 ? 3485 GLU A CB    1 
ATOM   14523 C  CG    . GLU A 1 3485 ? 208.620 199.226 285.562 1.00 30.69 ? 3485 GLU A CG    1 
ATOM   14524 C  CD    . GLU A 1 3485 ? 207.545 199.500 286.600 1.00 36.35 ? 3485 GLU A CD    1 
ATOM   14525 O  OE1   . GLU A 1 3485 ? 207.701 199.054 287.758 1.00 36.88 ? 3485 GLU A OE1   1 
ATOM   14526 O  OE2   . GLU A 1 3485 ? 206.539 200.155 286.258 1.00 35.18 ? 3485 GLU A OE2   1 
ATOM   14527 N  N     . ARG A 1 3486 ? 211.085 195.680 287.313 1.00 27.05 ? 3486 ARG A N     1 
ATOM   14528 C  CA    . ARG A 1 3486 ? 212.226 194.778 287.435 1.00 29.73 ? 3486 ARG A CA    1 
ATOM   14529 C  C     . ARG A 1 3486 ? 211.858 193.365 286.996 1.00 31.16 ? 3486 ARG A C     1 
ATOM   14530 O  O     . ARG A 1 3486 ? 212.650 192.688 286.332 1.00 32.01 ? 3486 ARG A O     1 
ATOM   14531 C  CB    . ARG A 1 3486 ? 212.747 194.781 288.872 1.00 24.75 ? 3486 ARG A CB    1 
ATOM   14532 C  CG    . ARG A 1 3486 ? 214.036 194.000 289.068 1.00 24.37 ? 3486 ARG A CG    1 
ATOM   14533 C  CD    . ARG A 1 3486 ? 214.299 193.708 290.539 1.00 27.64 ? 3486 ARG A CD    1 
ATOM   14534 N  NE    . ARG A 1 3486 ? 213.108 193.244 291.242 1.00 35.17 ? 3486 ARG A NE    1 
ATOM   14535 C  CZ    . ARG A 1 3486 ? 212.510 192.080 291.026 1.00 31.82 ? 3486 ARG A CZ    1 
ATOM   14536 N  NH1   . ARG A 1 3486 ? 212.980 191.212 290.145 1.00 24.63 ? 3486 ARG A NH1   1 
ATOM   14537 N  NH2   . ARG A 1 3486 ? 211.415 191.775 291.717 1.00 35.25 ? 3486 ARG A NH2   1 
ATOM   14538 N  N     . GLU A 1 3487 ? 210.657 192.905 287.359 1.00 29.51 ? 3487 GLU A N     1 
ATOM   14539 C  CA    . GLU A 1 3487 ? 210.212 191.579 286.941 1.00 28.56 ? 3487 GLU A CA    1 
ATOM   14540 C  C     . GLU A 1 3487 ? 210.019 191.500 285.432 1.00 28.16 ? 3487 GLU A C     1 
ATOM   14541 O  O     . GLU A 1 3487 ? 210.409 190.512 284.803 1.00 29.76 ? 3487 GLU A O     1 
ATOM   14542 C  CB    . GLU A 1 3487 ? 208.915 191.210 287.664 1.00 28.33 ? 3487 GLU A CB    1 
ATOM   14543 C  CG    . GLU A 1 3487 ? 209.081 190.892 289.142 1.00 29.77 ? 3487 GLU A CG    1 
ATOM   14544 C  CD    . GLU A 1 3487 ? 209.692 189.523 289.389 1.00 37.18 ? 3487 GLU A CD    1 
ATOM   14545 O  OE1   . GLU A 1 3487 ? 210.864 189.309 289.014 1.00 35.45 ? 3487 GLU A OE1   1 
ATOM   14546 O  OE2   . GLU A 1 3487 ? 208.995 188.658 289.958 1.00 34.55 ? 3487 GLU A OE2   1 
ATOM   14547 N  N     . ARG A 1 3488 ? 209.408 192.528 284.836 1.00 26.63 ? 3488 ARG A N     1 
ATOM   14548 C  CA    . ARG A 1 3488 ? 209.147 192.508 283.399 1.00 21.04 ? 3488 ARG A CA    1 
ATOM   14549 C  C     . ARG A 1 3488 ? 210.441 192.521 282.596 1.00 26.56 ? 3488 ARG A C     1 
ATOM   14550 O  O     . ARG A 1 3488 ? 210.574 191.789 281.608 1.00 32.49 ? 3488 ARG A O     1 
ATOM   14551 C  CB    . ARG A 1 3488 ? 208.262 193.692 283.014 1.00 22.94 ? 3488 ARG A CB    1 
ATOM   14552 C  CG    . ARG A 1 3488 ? 207.909 193.753 281.539 1.00 23.86 ? 3488 ARG A CG    1 
ATOM   14553 C  CD    . ARG A 1 3488 ? 207.621 195.179 281.098 1.00 24.65 ? 3488 ARG A CD    1 
ATOM   14554 N  NE    . ARG A 1 3488 ? 206.802 195.900 282.065 1.00 30.03 ? 3488 ARG A NE    1 
ATOM   14555 C  CZ    . ARG A 1 3488 ? 207.220 196.938 282.777 1.00 30.94 ? 3488 ARG A CZ    1 
ATOM   14556 N  NH1   . ARG A 1 3488 ? 208.453 197.405 282.659 1.00 30.97 ? 3488 ARG A NH1   1 
ATOM   14557 N  NH2   . ARG A 1 3488 ? 206.382 197.519 283.629 1.00 34.12 ? 3488 ARG A NH2   1 
ATOM   14558 N  N     . TRP A 1 3489 ? 211.407 193.346 283.005 1.00 24.23 ? 3489 TRP A N     1 
ATOM   14559 C  CA    . TRP A 1 3489 ? 212.674 193.411 282.287 1.00 24.49 ? 3489 TRP A CA    1 
ATOM   14560 C  C     . TRP A 1 3489 ? 213.458 192.111 282.407 1.00 31.24 ? 3489 TRP A C     1 
ATOM   14561 O  O     . TRP A 1 3489 ? 214.184 191.740 281.478 1.00 34.34 ? 3489 TRP A O     1 
ATOM   14562 C  CB    . TRP A 1 3489 ? 213.504 194.585 282.800 1.00 24.23 ? 3489 TRP A CB    1 
ATOM   14563 C  CG    . TRP A 1 3489 ? 212.834 195.911 282.618 1.00 23.77 ? 3489 TRP A CG    1 
ATOM   14564 C  CD1   . TRP A 1 3489 ? 211.848 196.216 281.726 1.00 22.72 ? 3489 TRP A CD1   1 
ATOM   14565 C  CD2   . TRP A 1 3489 ? 213.102 197.113 283.346 1.00 24.72 ? 3489 TRP A CD2   1 
ATOM   14566 N  NE1   . TRP A 1 3489 ? 211.485 197.534 281.854 1.00 25.11 ? 3489 TRP A NE1   1 
ATOM   14567 C  CE2   . TRP A 1 3489 ? 212.241 198.107 282.843 1.00 25.46 ? 3489 TRP A CE2   1 
ATOM   14568 C  CE3   . TRP A 1 3489 ? 213.986 197.445 284.377 1.00 22.02 ? 3489 TRP A CE3   1 
ATOM   14569 C  CZ2   . TRP A 1 3489 ? 212.237 199.409 283.335 1.00 22.95 ? 3489 TRP A CZ2   1 
ATOM   14570 C  CZ3   . TRP A 1 3489 ? 213.983 198.736 284.861 1.00 25.96 ? 3489 TRP A CZ3   1 
ATOM   14571 C  CH2   . TRP A 1 3489 ? 213.116 199.704 284.341 1.00 31.56 ? 3489 TRP A CH2   1 
ATOM   14572 N  N     . GLU A 1 3490 ? 213.333 191.414 283.538 1.00 27.80 ? 3490 GLU A N     1 
ATOM   14573 C  CA    . GLU A 1 3490 ? 214.017 190.134 283.697 1.00 28.05 ? 3490 GLU A CA    1 
ATOM   14574 C  C     . GLU A 1 3490 ? 213.450 189.081 282.753 1.00 29.33 ? 3490 GLU A C     1 
ATOM   14575 O  O     . GLU A 1 3490 ? 214.205 188.282 282.184 1.00 30.74 ? 3490 GLU A O     1 
ATOM   14576 C  CB    . GLU A 1 3490 ? 213.920 189.664 285.148 1.00 23.57 ? 3490 GLU A CB    1 
ATOM   14577 C  CG    . GLU A 1 3490 ? 214.862 190.387 286.091 1.00 28.75 ? 3490 GLU A CG    1 
ATOM   14578 C  CD    . GLU A 1 3490 ? 214.484 190.202 287.547 1.00 37.07 ? 3490 GLU A CD    1 
ATOM   14579 O  OE1   . GLU A 1 3490 ? 213.473 189.520 287.818 1.00 37.36 ? 3490 GLU A OE1   1 
ATOM   14580 O  OE2   . GLU A 1 3490 ? 215.192 190.744 288.421 1.00 32.44 ? 3490 GLU A OE2   1 
ATOM   14581 N  N     . LYS A 1 3491 ? 212.126 189.057 282.583 1.00 27.27 ? 3491 LYS A N     1 
ATOM   14582 C  CA    . LYS A 1 3491 ? 211.504 188.069 281.705 1.00 27.73 ? 3491 LYS A CA    1 
ATOM   14583 C  C     . LYS A 1 3491 ? 211.955 188.248 280.261 1.00 27.59 ? 3491 LYS A C     1 
ATOM   14584 O  O     . LYS A 1 3491 ? 212.293 187.275 279.580 1.00 32.90 ? 3491 LYS A O     1 
ATOM   14585 C  CB    . LYS A 1 3491 ? 209.981 188.162 281.807 1.00 30.51 ? 3491 LYS A CB    1 
ATOM   14586 C  CG    . LYS A 1 3491 ? 209.420 187.930 283.202 1.00 29.85 ? 3491 LYS A CG    1 
ATOM   14587 C  CD    . LYS A 1 3491 ? 209.931 186.629 283.798 1.00 30.69 ? 3491 LYS A CD    1 
ATOM   14588 C  CE    . LYS A 1 3491 ? 209.443 186.450 285.228 1.00 30.56 ? 3491 LYS A CE    1 
ATOM   14589 N  NZ    . LYS A 1 3491 ? 209.872 187.571 286.110 1.00 31.24 ? 3491 LYS A NZ    1 
ATOM   14590 N  N     . THR A 1 3492 ? 211.971 189.493 279.776 1.00 29.66 ? 3492 THR A N     1 
ATOM   14591 C  CA    . THR A 1 3492 ? 212.384 189.745 278.398 1.00 28.07 ? 3492 THR A CA    1 
ATOM   14592 C  C     . THR A 1 3492 ? 213.855 189.410 278.192 1.00 28.98 ? 3492 THR A C     1 
ATOM   14593 O  O     . THR A 1 3492 ? 214.237 188.889 277.137 1.00 32.25 ? 3492 THR A O     1 
ATOM   14594 C  CB    . THR A 1 3492 ? 212.102 191.200 278.022 1.00 26.20 ? 3492 THR A CB    1 
ATOM   14595 O  OG1   . THR A 1 3492 ? 210.705 191.471 278.178 1.00 32.22 ? 3492 THR A OG1   1 
ATOM   14596 C  CG2   . THR A 1 3492 ? 212.496 191.465 276.578 1.00 22.73 ? 3492 THR A CG2   1 
ATOM   14597 N  N     . SER A 1 3493 ? 214.696 189.698 279.189 1.00 28.13 ? 3493 SER A N     1 
ATOM   14598 C  CA    . SER A 1 3493 ? 216.118 189.390 279.074 1.00 28.03 ? 3493 SER A CA    1 
ATOM   14599 C  C     . SER A 1 3493 ? 216.345 187.896 278.885 1.00 34.05 ? 3493 SER A C     1 
ATOM   14600 O  O     . SER A 1 3493 ? 217.246 187.486 278.145 1.00 36.26 ? 3493 SER A O     1 
ATOM   14601 C  CB    . SER A 1 3493 ? 216.865 189.894 280.306 1.00 25.99 ? 3493 SER A CB    1 
ATOM   14602 O  OG    . SER A 1 3493 ? 218.231 189.525 280.260 1.00 29.50 ? 3493 SER A OG    1 
ATOM   14603 N  N     . GLU A 1 3494 ? 215.543 187.064 279.555 1.00 28.79 ? 3494 GLU A N     1 
ATOM   14604 C  CA    . GLU A 1 3494 ? 215.638 185.624 279.346 1.00 30.53 ? 3494 GLU A CA    1 
ATOM   14605 C  C     . GLU A 1 3494 ? 215.239 185.245 277.925 1.00 33.58 ? 3494 GLU A C     1 
ATOM   14606 O  O     . GLU A 1 3494 ? 215.891 184.406 277.294 1.00 34.47 ? 3494 GLU A O     1 
ATOM   14607 C  CB    . GLU A 1 3494 ? 214.770 184.887 280.365 1.00 29.47 ? 3494 GLU A CB    1 
ATOM   14608 C  CG    . GLU A 1 3494 ? 214.644 183.382 280.132 1.00 31.72 ? 3494 GLU A CG    1 
ATOM   14609 C  CD    . GLU A 1 3494 ? 215.944 182.629 280.357 1.00 38.78 ? 3494 GLU A CD    1 
ATOM   14610 O  OE1   . GLU A 1 3494 ? 216.887 182.789 279.553 1.00 40.53 ? 3494 GLU A OE1   1 
ATOM   14611 O  OE2   . GLU A 1 3494 ? 216.024 181.871 281.346 1.00 38.89 ? 3494 GLU A OE2   1 
ATOM   14612 N  N     . THR A 1 3495 ? 214.180 185.858 277.403 1.00 29.65 ? 3495 THR A N     1 
ATOM   14613 C  CA    . THR A 1 3495 ? 213.707 185.587 276.046 1.00 30.46 ? 3495 THR A CA    1 
ATOM   14614 C  C     . THR A 1 3495 ? 214.580 186.216 274.971 1.00 27.70 ? 3495 THR A C     1 
ATOM   14615 O  O     . THR A 1 3495 ? 214.187 186.186 273.799 1.00 28.72 ? 3495 THR A O     1 
ATOM   14616 C  CB    . THR A 1 3495 ? 212.266 186.073 275.880 1.00 29.03 ? 3495 THR A CB    1 
ATOM   14617 O  OG1   . THR A 1 3495 ? 212.246 187.505 275.830 1.00 26.50 ? 3495 THR A OG1   1 
ATOM   14618 C  CG2   . THR A 1 3495 ? 211.407 185.593 277.037 1.00 23.62 ? 3495 THR A CG2   1 
ATOM   14619 N  N     . PHE A 1 3496 ? 215.731 186.787 275.334 1.00 26.75 ? 3496 PHE A N     1 
ATOM   14620 C  CA    . PHE A 1 3496 ? 216.617 187.374 274.335 1.00 21.44 ? 3496 PHE A CA    1 
ATOM   14621 C  C     . PHE A 1 3496 ? 217.123 186.324 273.357 1.00 24.49 ? 3496 PHE A C     1 
ATOM   14622 O  O     . PHE A 1 3496 ? 217.174 186.567 272.145 1.00 29.80 ? 3496 PHE A O     1 
ATOM   14623 C  CB    . PHE A 1 3496 ? 217.792 188.067 275.021 1.00 21.65 ? 3496 PHE A CB    1 
ATOM   14624 C  CG    . PHE A 1 3496 ? 218.775 188.673 274.066 1.00 22.53 ? 3496 PHE A CG    1 
ATOM   14625 C  CD1   . PHE A 1 3496 ? 218.348 189.520 273.056 1.00 25.19 ? 3496 PHE A CD1   1 
ATOM   14626 C  CD2   . PHE A 1 3496 ? 220.124 188.379 274.162 1.00 23.14 ? 3496 PHE A CD2   1 
ATOM   14627 C  CE1   . PHE A 1 3496 ? 219.252 190.072 272.172 1.00 26.34 ? 3496 PHE A CE1   1 
ATOM   14628 C  CE2   . PHE A 1 3496 ? 221.028 188.928 273.280 1.00 21.22 ? 3496 PHE A CE2   1 
ATOM   14629 C  CZ    . PHE A 1 3496 ? 220.593 189.775 272.285 1.00 21.00 ? 3496 PHE A CZ    1 
ATOM   14630 N  N     . LYS A 1 3497 ? 217.510 185.150 273.863 1.00 24.90 ? 3497 LYS A N     1 
ATOM   14631 C  CA    . LYS A 1 3497 ? 218.072 184.117 272.997 1.00 25.50 ? 3497 LYS A CA    1 
ATOM   14632 C  C     . LYS A 1 3497 ? 217.045 183.610 271.993 1.00 21.05 ? 3497 LYS A C     1 
ATOM   14633 O  O     . LYS A 1 3497 ? 217.374 183.392 270.821 1.00 22.07 ? 3497 LYS A O     1 
ATOM   14634 C  CB    . LYS A 1 3497 ? 218.614 182.964 273.839 1.00 26.09 ? 3497 LYS A CB    1 
ATOM   14635 C  CG    . LYS A 1 3497 ? 219.587 183.393 274.924 1.00 31.26 ? 3497 LYS A CG    1 
ATOM   14636 C  CD    . LYS A 1 3497 ? 220.222 182.190 275.601 1.00 32.18 ? 3497 LYS A CD    1 
ATOM   14637 C  CE    . LYS A 1 3497 ? 220.946 181.313 274.594 1.00 35.32 ? 3497 LYS A CE    1 
ATOM   14638 N  NZ    . LYS A 1 3497 ? 221.959 182.081 273.819 1.00 35.53 ? 3497 LYS A NZ    1 
ATOM   14639 N  N     . ASN A 1 3498 ? 215.800 183.414 272.434 1.00 20.68 ? 3498 ASN A N     1 
ATOM   14640 C  CA    . ASN A 1 3498 ? 214.768 182.904 271.535 1.00 20.09 ? 3498 ASN A CA    1 
ATOM   14641 C  C     . ASN A 1 3498 ? 214.522 183.865 270.379 1.00 23.07 ? 3498 ASN A C     1 
ATOM   14642 O  O     . ASN A 1 3498 ? 214.409 183.442 269.223 1.00 19.93 ? 3498 ASN A O     1 
ATOM   14643 C  CB    . ASN A 1 3498 ? 213.478 182.654 272.316 1.00 20.30 ? 3498 ASN A CB    1 
ATOM   14644 C  CG    . ASN A 1 3498 ? 212.426 181.919 271.503 1.00 26.38 ? 3498 ASN A CG    1 
ATOM   14645 O  OD1   . ASN A 1 3498 ? 212.631 181.601 270.333 1.00 36.95 ? 3498 ASN A OD1   1 
ATOM   14646 N  ND2   . ASN A 1 3498 ? 211.287 181.647 272.127 1.00 27.08 ? 3498 ASN A ND2   1 
ATOM   14647 N  N     . GLN A 1 3499 ? 214.441 185.166 270.671 1.00 20.11 ? 3499 GLN A N     1 
ATOM   14648 C  CA    . GLN A 1 3499 ? 214.217 186.143 269.611 1.00 18.43 ? 3499 GLN A CA    1 
ATOM   14649 C  C     . GLN A 1 3499 ? 215.399 186.201 268.649 1.00 20.49 ? 3499 GLN A C     1 
ATOM   14650 O  O     . GLN A 1 3499 ? 215.211 186.313 267.432 1.00 23.21 ? 3499 GLN A O     1 
ATOM   14651 C  CB    . GLN A 1 3499 ? 213.935 187.517 270.213 1.00 18.55 ? 3499 GLN A CB    1 
ATOM   14652 C  CG    . GLN A 1 3499 ? 212.775 187.541 271.185 1.00 23.34 ? 3499 GLN A CG    1 
ATOM   14653 C  CD    . GLN A 1 3499 ? 212.494 188.930 271.717 1.00 24.81 ? 3499 GLN A CD    1 
ATOM   14654 O  OE1   . GLN A 1 3499 ? 212.649 189.193 272.909 1.00 29.63 ? 3499 GLN A OE1   1 
ATOM   14655 N  NE2   . GLN A 1 3499 ? 212.078 189.828 270.832 1.00 28.66 ? 3499 GLN A NE2   1 
ATOM   14656 N  N     . MET A 1 3500 ? 216.626 186.123 269.174 1.00 17.12 ? 3500 MET A N     1 
ATOM   14657 C  CA    . MET A 1 3500 ? 217.799 186.047 268.307 1.00 16.29 ? 3500 MET A CA    1 
ATOM   14658 C  C     . MET A 1 3500 ? 217.756 184.822 267.403 1.00 16.97 ? 3500 MET A C     1 
ATOM   14659 O  O     . MET A 1 3500 ? 218.305 184.851 266.297 1.00 21.36 ? 3500 MET A O     1 
ATOM   14660 C  CB    . MET A 1 3500 ? 219.080 186.030 269.143 1.00 18.27 ? 3500 MET A CB    1 
ATOM   14661 C  CG    . MET A 1 3500 ? 219.366 187.304 269.919 1.00 22.65 ? 3500 MET A CG    1 
ATOM   14662 S  SD    . MET A 1 3500 ? 219.576 188.734 268.846 1.00 31.34 ? 3500 MET A SD    1 
ATOM   14663 C  CE    . MET A 1 3500 ? 221.130 188.332 268.055 1.00 26.36 ? 3500 MET A CE    1 
ATOM   14664 N  N     . SER A 1 3501 ? 217.113 183.745 267.848 1.00 14.85 ? 3501 SER A N     1 
ATOM   14665 C  CA    . SER A 1 3501 ? 217.065 182.502 267.094 1.00 12.80 ? 3501 SER A CA    1 
ATOM   14666 C  C     . SER A 1 3501 ? 215.984 182.481 266.021 1.00 11.71 ? 3501 SER A C     1 
ATOM   14667 O  O     . SER A 1 3501 ? 215.965 181.549 265.209 1.00 23.94 ? 3501 SER A O     1 
ATOM   14668 C  CB    . SER A 1 3501 ? 216.856 181.317 268.043 1.00 17.13 ? 3501 SER A CB    1 
ATOM   14669 O  OG    . SER A 1 3501 ? 215.538 181.300 268.561 1.00 26.70 ? 3501 SER A OG    1 
ATOM   14670 N  N     . THR A 1 3502 ? 215.090 183.467 265.987 1.00 9.75  ? 3502 THR A N     1 
ATOM   14671 C  CA    . THR A 1 3502 ? 214.021 183.497 264.999 1.00 10.23 ? 3502 THR A CA    1 
ATOM   14672 C  C     . THR A 1 3502 ? 214.081 184.705 264.075 1.00 9.97  ? 3502 THR A C     1 
ATOM   14673 O  O     . THR A 1 3502 ? 213.260 184.798 263.158 1.00 11.49 ? 3502 THR A O     1 
ATOM   14674 C  CB    . THR A 1 3502 ? 212.646 183.463 265.684 1.00 11.86 ? 3502 THR A CB    1 
ATOM   14675 O  OG1   . THR A 1 3502 ? 212.593 184.455 266.715 1.00 12.07 ? 3502 THR A OG1   1 
ATOM   14676 C  CG2   . THR A 1 3502 ? 212.375 182.089 266.283 1.00 11.29 ? 3502 THR A CG2   1 
ATOM   14677 N  N     . ILE A 1 3503 ? 215.021 185.631 264.286 1.00 7.97  ? 3503 ILE A N     1 
ATOM   14678 C  CA    . ILE A 1 3503 ? 215.111 186.808 263.426 1.00 8.20  ? 3503 ILE A CA    1 
ATOM   14679 C  C     . ILE A 1 3503 ? 215.423 186.399 261.993 1.00 5.74  ? 3503 ILE A C     1 
ATOM   14680 O  O     . ILE A 1 3503 ? 214.877 186.964 261.038 1.00 8.52  ? 3503 ILE A O     1 
ATOM   14681 C  CB    . ILE A 1 3503 ? 216.153 187.799 263.981 1.00 11.20 ? 3503 ILE A CB    1 
ATOM   14682 C  CG1   . ILE A 1 3503 ? 215.582 188.563 265.174 1.00 9.74  ? 3503 ILE A CG1   1 
ATOM   14683 C  CG2   . ILE A 1 3503 ? 216.594 188.782 262.907 1.00 7.57  ? 3503 ILE A CG2   1 
ATOM   14684 C  CD1   . ILE A 1 3503 ? 216.564 189.519 265.810 1.00 16.09 ? 3503 ILE A CD1   1 
ATOM   14685 N  N     . ALA A 1 3504 ? 216.290 185.397 261.821 1.00 4.84  ? 3504 ALA A N     1 
ATOM   14686 C  CA    . ALA A 1 3504 ? 216.644 184.942 260.481 1.00 4.75  ? 3504 ALA A CA    1 
ATOM   14687 C  C     . ALA A 1 3504 ? 215.417 184.467 259.714 1.00 3.18  ? 3504 ALA A C     1 
ATOM   14688 O  O     . ALA A 1 3504 ? 215.265 184.766 258.525 1.00 2.73  ? 3504 ALA A O     1 
ATOM   14689 C  CB    . ALA A 1 3504 ? 217.690 183.833 260.565 1.00 3.31  ? 3504 ALA A CB    1 
ATOM   14690 N  N     . GLY A 1 3505 ? 214.531 183.726 260.376 1.00 4.17  ? 3505 GLY A N     1 
ATOM   14691 C  CA    . GLY A 1 3505 ? 213.302 183.280 259.751 1.00 3.66  ? 3505 GLY A CA    1 
ATOM   14692 C  C     . GLY A 1 3505 ? 212.216 184.335 259.694 1.00 2.55  ? 3505 GLY A C     1 
ATOM   14693 O  O     . GLY A 1 3505 ? 211.491 184.431 258.699 1.00 2.02  ? 3505 GLY A O     1 
ATOM   14694 N  N     . ASP A 1 3506 ? 212.086 185.129 260.760 1.00 2.36  ? 3506 ASP A N     1 
ATOM   14695 C  CA    . ASP A 1 3506 ? 211.044 186.153 260.798 1.00 2.70  ? 3506 ASP A CA    1 
ATOM   14696 C  C     . ASP A 1 3506 ? 211.272 187.220 259.737 1.00 1.95  ? 3506 ASP A C     1 
ATOM   14697 O  O     . ASP A 1 3506 ? 210.330 187.639 259.055 1.00 0.80  ? 3506 ASP A O     1 
ATOM   14698 C  CB    . ASP A 1 3506 ? 210.980 186.788 262.186 1.00 4.46  ? 3506 ASP A CB    1 
ATOM   14699 C  CG    . ASP A 1 3506 ? 210.235 185.929 263.186 1.00 11.51 ? 3506 ASP A CG    1 
ATOM   14700 O  OD1   . ASP A 1 3506 ? 209.521 185.000 262.760 1.00 13.23 ? 3506 ASP A OD1   1 
ATOM   14701 O  OD2   . ASP A 1 3506 ? 210.371 186.179 264.403 1.00 15.22 ? 3506 ASP A OD2   1 
ATOM   14702 N  N     . CYS A 1 3507 ? 212.518 187.673 259.583 1.00 3.24  ? 3507 CYS A N     1 
ATOM   14703 C  CA    . CYS A 1 3507 ? 212.814 188.696 258.589 1.00 1.52  ? 3507 CYS A CA    1 
ATOM   14704 C  C     . CYS A 1 3507 ? 212.682 188.158 257.170 1.00 1.85  ? 3507 CYS A C     1 
ATOM   14705 O  O     . CYS A 1 3507 ? 212.292 188.900 256.264 1.00 1.56  ? 3507 CYS A O     1 
ATOM   14706 C  CB    . CYS A 1 3507 ? 214.214 189.264 258.823 1.00 2.29  ? 3507 CYS A CB    1 
ATOM   14707 S  SG    . CYS A 1 3507 ? 214.362 190.250 260.325 1.00 6.53  ? 3507 CYS A SG    1 
ATOM   14708 N  N     . LEU A 1 3508 ? 212.998 186.878 256.961 1.00 1.10  ? 3508 LEU A N     1 
ATOM   14709 C  CA    . LEU A 1 3508 ? 212.835 186.275 255.643 1.00 0.59  ? 3508 LEU A CA    1 
ATOM   14710 C  C     . LEU A 1 3508 ? 211.376 186.303 255.204 1.00 0.54  ? 3508 LEU A C     1 
ATOM   14711 O  O     . LEU A 1 3508 ? 211.065 186.661 254.062 1.00 0.52  ? 3508 LEU A O     1 
ATOM   14712 C  CB    . LEU A 1 3508 ? 213.369 184.842 255.663 1.00 1.21  ? 3508 LEU A CB    1 
ATOM   14713 C  CG    . LEU A 1 3508 ? 213.776 184.167 254.352 1.00 0.78  ? 3508 LEU A CG    1 
ATOM   14714 C  CD1   . LEU A 1 3508 ? 214.759 183.052 254.646 1.00 1.11  ? 3508 LEU A CD1   1 
ATOM   14715 C  CD2   . LEU A 1 3508 ? 212.571 183.622 253.600 1.00 0.50  ? 3508 LEU A CD2   1 
ATOM   14716 N  N     . LEU A 1 3509 ? 210.465 185.927 256.103 1.00 0.54  ? 3509 LEU A N     1 
ATOM   14717 C  CA    . LEU A 1 3509 ? 209.041 185.972 255.783 1.00 0.34  ? 3509 LEU A CA    1 
ATOM   14718 C  C     . LEU A 1 3509 ? 208.563 187.405 255.590 1.00 0.34  ? 3509 LEU A C     1 
ATOM   14719 O  O     . LEU A 1 3509 ? 207.798 187.692 254.662 1.00 0.12  ? 3509 LEU A O     1 
ATOM   14720 C  CB    . LEU A 1 3509 ? 208.237 185.289 256.887 1.00 0.57  ? 3509 LEU A CB    1 
ATOM   14721 C  CG    . LEU A 1 3509 ? 208.464 183.794 257.097 1.00 1.28  ? 3509 LEU A CG    1 
ATOM   14722 C  CD1   . LEU A 1 3509 ? 207.735 183.319 258.344 1.00 1.03  ? 3509 LEU A CD1   1 
ATOM   14723 C  CD2   . LEU A 1 3509 ? 208.017 183.011 255.880 1.00 0.67  ? 3509 LEU A CD2   1 
ATOM   14724 N  N     . SER A 1 3510 ? 209.002 188.314 256.461 1.00 0.86  ? 3510 SER A N     1 
ATOM   14725 C  CA    . SER A 1 3510 ? 208.584 189.708 256.363 1.00 0.32  ? 3510 SER A CA    1 
ATOM   14726 C  C     . SER A 1 3510 ? 209.097 190.354 255.083 1.00 0.28  ? 3510 SER A C     1 
ATOM   14727 O  O     . SER A 1 3510 ? 208.358 191.079 254.409 1.00 0.25  ? 3510 SER A O     1 
ATOM   14728 C  CB    . SER A 1 3510 ? 209.069 190.480 257.588 1.00 0.57  ? 3510 SER A CB    1 
ATOM   14729 O  OG    . SER A 1 3510 ? 208.626 189.863 258.781 1.00 2.09  ? 3510 SER A OG    1 
ATOM   14730 N  N     . ALA A 1 3511 ? 210.358 190.098 254.735 1.00 0.67  ? 3511 ALA A N     1 
ATOM   14731 C  CA    . ALA A 1 3511 ? 210.925 190.675 253.520 1.00 0.21  ? 3511 ALA A CA    1 
ATOM   14732 C  C     . ALA A 1 3511 ? 210.213 190.160 252.279 1.00 0.15  ? 3511 ALA A C     1 
ATOM   14733 O  O     . ALA A 1 3511 ? 209.960 190.921 251.339 1.00 0.61  ? 3511 ALA A O     1 
ATOM   14734 C  CB    . ALA A 1 3511 ? 212.419 190.374 253.446 1.00 0.22  ? 3511 ALA A CB    1 
ATOM   14735 N  N     . ALA A 1 3512 ? 209.885 188.866 252.255 1.00 0.17  ? 3512 ALA A N     1 
ATOM   14736 C  CA    . ALA A 1 3512 ? 209.178 188.300 251.112 1.00 0.05  ? 3512 ALA A CA    1 
ATOM   14737 C  C     . ALA A 1 3512 ? 207.803 188.929 250.952 1.00 0.08  ? 3512 ALA A C     1 
ATOM   14738 O  O     . ALA A 1 3512 ? 207.349 189.170 249.827 1.00 0.10  ? 3512 ALA A O     1 
ATOM   14739 C  CB    . ALA A 1 3512 ? 209.065 186.785 251.263 1.00 0.06  ? 3512 ALA A CB    1 
ATOM   14740 N  N     . PHE A 1 3513 ? 207.121 189.199 252.066 1.00 0.10  ? 3513 PHE A N     1 
ATOM   14741 C  CA    . PHE A 1 3513 ? 205.803 189.816 252.000 1.00 0.12  ? 3513 PHE A CA    1 
ATOM   14742 C  C     . PHE A 1 3513 ? 205.874 191.221 251.413 1.00 0.11  ? 3513 PHE A C     1 
ATOM   14743 O  O     . PHE A 1 3513 ? 205.008 191.613 250.624 1.00 0.14  ? 3513 PHE A O     1 
ATOM   14744 C  CB    . PHE A 1 3513 ? 205.169 189.833 253.391 1.00 0.10  ? 3513 PHE A CB    1 
ATOM   14745 C  CG    . PHE A 1 3513 ? 203.688 190.048 253.377 1.00 0.19  ? 3513 PHE A CG    1 
ATOM   14746 C  CD1   . PHE A 1 3513 ? 202.823 188.973 253.288 1.00 0.37  ? 3513 PHE A CD1   1 
ATOM   14747 C  CD2   . PHE A 1 3513 ? 203.159 191.322 253.458 1.00 0.27  ? 3513 PHE A CD2   1 
ATOM   14748 C  CE1   . PHE A 1 3513 ? 201.459 189.167 253.270 1.00 0.48  ? 3513 PHE A CE1   1 
ATOM   14749 C  CE2   . PHE A 1 3513 ? 201.796 191.518 253.442 1.00 0.46  ? 3513 PHE A CE2   1 
ATOM   14750 C  CZ    . PHE A 1 3513 ? 200.947 190.439 253.350 1.00 0.59  ? 3513 PHE A CZ    1 
ATOM   14751 N  N     . ILE A 1 3514 ? 206.896 191.993 251.786 1.00 0.13  ? 3514 ILE A N     1 
ATOM   14752 C  CA    . ILE A 1 3514 ? 207.039 193.347 251.260 1.00 0.25  ? 3514 ILE A CA    1 
ATOM   14753 C  C     . ILE A 1 3514 ? 207.350 193.329 249.768 1.00 0.22  ? 3514 ILE A C     1 
ATOM   14754 O  O     . ILE A 1 3514 ? 206.885 194.196 249.019 1.00 0.46  ? 3514 ILE A O     1 
ATOM   14755 C  CB    . ILE A 1 3514 ? 208.117 194.113 252.050 1.00 0.52  ? 3514 ILE A CB    1 
ATOM   14756 C  CG1   . ILE A 1 3514 ? 207.772 194.129 253.538 1.00 0.45  ? 3514 ILE A CG1   1 
ATOM   14757 C  CG2   . ILE A 1 3514 ? 208.257 195.532 251.530 1.00 0.72  ? 3514 ILE A CG2   1 
ATOM   14758 C  CD1   . ILE A 1 3514 ? 206.434 194.751 253.834 1.00 0.89  ? 3514 ILE A CD1   1 
ATOM   14759 N  N     . ALA A 1 3515 ? 208.124 192.351 249.306 1.00 0.12  ? 3515 ALA A N     1 
ATOM   14760 C  CA    . ALA A 1 3515 ? 208.580 192.331 247.923 1.00 0.14  ? 3515 ALA A CA    1 
ATOM   14761 C  C     . ALA A 1 3515 ? 207.584 191.714 246.951 1.00 0.08  ? 3515 ALA A C     1 
ATOM   14762 O  O     . ALA A 1 3515 ? 207.614 192.051 245.764 1.00 0.07  ? 3515 ALA A O     1 
ATOM   14763 C  CB    . ALA A 1 3515 ? 209.910 191.582 247.818 1.00 0.14  ? 3515 ALA A CB    1 
ATOM   14764 N  N     . TYR A 1 3516 ? 206.709 190.835 247.409 1.00 0.15  ? 3516 TYR A N     1 
ATOM   14765 C  CA    . TYR A 1 3516 ? 205.880 190.090 246.466 1.00 0.11  ? 3516 TYR A CA    1 
ATOM   14766 C  C     . TYR A 1 3516 ? 204.385 190.252 246.686 1.00 0.09  ? 3516 TYR A C     1 
ATOM   14767 O  O     . TYR A 1 3516 ? 203.629 190.238 245.714 1.00 0.73  ? 3516 TYR A O     1 
ATOM   14768 C  CB    . TYR A 1 3516 ? 206.224 188.598 246.521 1.00 0.06  ? 3516 TYR A CB    1 
ATOM   14769 C  CG    . TYR A 1 3516 ? 207.628 188.245 246.106 1.00 0.03  ? 3516 TYR A CG    1 
ATOM   14770 C  CD1   . TYR A 1 3516 ? 208.004 188.276 244.773 1.00 0.05  ? 3516 TYR A CD1   1 
ATOM   14771 C  CD2   . TYR A 1 3516 ? 208.570 187.849 247.042 1.00 0.03  ? 3516 TYR A CD2   1 
ATOM   14772 C  CE1   . TYR A 1 3516 ? 209.280 187.933 244.387 1.00 0.04  ? 3516 TYR A CE1   1 
ATOM   14773 C  CE2   . TYR A 1 3516 ? 209.850 187.508 246.662 1.00 0.03  ? 3516 TYR A CE2   1 
ATOM   14774 C  CZ    . TYR A 1 3516 ? 210.199 187.554 245.334 1.00 0.03  ? 3516 TYR A CZ    1 
ATOM   14775 O  OH    . TYR A 1 3516 ? 211.470 187.220 244.947 1.00 0.04  ? 3516 TYR A OH    1 
ATOM   14776 N  N     . ALA A 1 3517 ? 203.938 190.401 247.930 1.00 0.11  ? 3517 ALA A N     1 
ATOM   14777 C  CA    . ALA A 1 3517 ? 202.526 190.247 248.254 1.00 0.25  ? 3517 ALA A CA    1 
ATOM   14778 C  C     . ALA A 1 3517 ? 201.674 191.460 247.907 1.00 0.15  ? 3517 ALA A C     1 
ATOM   14779 O  O     . ALA A 1 3517 ? 200.449 191.380 248.024 1.00 0.89  ? 3517 ALA A O     1 
ATOM   14780 C  CB    . ALA A 1 3517 ? 202.367 189.928 249.743 1.00 0.21  ? 3517 ALA A CB    1 
ATOM   14781 N  N     . GLY A 1 3518 ? 202.281 192.564 247.475 1.00 0.21  ? 3518 GLY A N     1 
ATOM   14782 C  CA    . GLY A 1 3518 ? 201.547 193.817 247.388 1.00 0.18  ? 3518 GLY A CA    1 
ATOM   14783 C  C     . GLY A 1 3518 ? 200.398 193.787 246.398 1.00 0.23  ? 3518 GLY A C     1 
ATOM   14784 O  O     . GLY A 1 3518 ? 199.327 194.335 246.664 1.00 0.29  ? 3518 GLY A O     1 
ATOM   14785 N  N     . TYR A 1 3519 ? 200.602 193.151 245.244 1.00 0.44  ? 3519 TYR A N     1 
ATOM   14786 C  CA    . TYR A 1 3519 ? 199.575 193.175 244.209 1.00 0.30  ? 3519 TYR A CA    1 
ATOM   14787 C  C     . TYR A 1 3519 ? 198.379 192.298 244.557 1.00 0.40  ? 3519 TYR A C     1 
ATOM   14788 O  O     . TYR A 1 3519 ? 197.271 192.546 244.072 1.00 1.11  ? 3519 TYR A O     1 
ATOM   14789 C  CB    . TYR A 1 3519 ? 200.163 192.747 242.865 1.00 0.63  ? 3519 TYR A CB    1 
ATOM   14790 C  CG    . TYR A 1 3519 ? 199.156 192.818 241.747 1.00 1.45  ? 3519 TYR A CG    1 
ATOM   14791 C  CD1   . TYR A 1 3519 ? 198.732 194.042 241.255 1.00 1.19  ? 3519 TYR A CD1   1 
ATOM   14792 C  CD2   . TYR A 1 3519 ? 198.610 191.665 241.201 1.00 1.96  ? 3519 TYR A CD2   1 
ATOM   14793 C  CE1   . TYR A 1 3519 ? 197.802 194.119 240.246 1.00 4.22  ? 3519 TYR A CE1   1 
ATOM   14794 C  CE2   . TYR A 1 3519 ? 197.680 191.732 240.187 1.00 2.82  ? 3519 TYR A CE2   1 
ATOM   14795 C  CZ    . TYR A 1 3519 ? 197.279 192.963 239.713 1.00 4.38  ? 3519 TYR A CZ    1 
ATOM   14796 O  OH    . TYR A 1 3519 ? 196.352 193.043 238.702 1.00 9.23  ? 3519 TYR A OH    1 
ATOM   14797 N  N     . PHE A 1 3520 ? 198.571 191.283 245.392 1.00 0.46  ? 3520 PHE A N     1 
ATOM   14798 C  CA    . PHE A 1 3520 ? 197.534 190.290 245.607 1.00 1.24  ? 3520 PHE A CA    1 
ATOM   14799 C  C     . PHE A 1 3520 ? 196.541 190.737 246.680 1.00 1.72  ? 3520 PHE A C     1 
ATOM   14800 O  O     . PHE A 1 3520 ? 196.796 191.655 247.462 1.00 1.33  ? 3520 PHE A O     1 
ATOM   14801 C  CB    . PHE A 1 3520 ? 198.164 188.952 245.985 1.00 1.12  ? 3520 PHE A CB    1 
ATOM   14802 C  CG    . PHE A 1 3520 ? 199.183 188.473 244.997 1.00 1.16  ? 3520 PHE A CG    1 
ATOM   14803 C  CD1   . PHE A 1 3520 ? 198.789 187.883 243.808 1.00 1.18  ? 3520 PHE A CD1   1 
ATOM   14804 C  CD2   . PHE A 1 3520 ? 200.536 188.631 245.245 1.00 0.57  ? 3520 PHE A CD2   1 
ATOM   14805 C  CE1   . PHE A 1 3520 ? 199.724 187.450 242.894 1.00 2.68  ? 3520 PHE A CE1   1 
ATOM   14806 C  CE2   . PHE A 1 3520 ? 201.473 188.203 244.333 1.00 1.56  ? 3520 PHE A CE2   1 
ATOM   14807 C  CZ    . PHE A 1 3520 ? 201.068 187.609 243.157 1.00 3.40  ? 3520 PHE A CZ    1 
ATOM   14808 N  N     . ASP A 1 3521 ? 195.388 190.072 246.697 1.00 2.65  ? 3521 ASP A N     1 
ATOM   14809 C  CA    . ASP A 1 3521 ? 194.346 190.364 247.670 1.00 1.85  ? 3521 ASP A CA    1 
ATOM   14810 C  C     . ASP A 1 3521 ? 194.610 189.604 248.969 1.00 1.44  ? 3521 ASP A C     1 
ATOM   14811 O  O     . ASP A 1 3521 ? 195.615 188.904 249.116 1.00 2.01  ? 3521 ASP A O     1 
ATOM   14812 C  CB    . ASP A 1 3521 ? 192.969 190.045 247.087 1.00 1.96  ? 3521 ASP A CB    1 
ATOM   14813 C  CG    . ASP A 1 3521 ? 192.824 188.591 246.660 1.00 7.00  ? 3521 ASP A CG    1 
ATOM   14814 O  OD1   . ASP A 1 3521 ? 193.756 187.792 246.877 1.00 10.23 ? 3521 ASP A OD1   1 
ATOM   14815 O  OD2   . ASP A 1 3521 ? 191.764 188.246 246.099 1.00 8.66  ? 3521 ASP A OD2   1 
ATOM   14816 N  N     . GLN A 1 3522 ? 193.684 189.734 249.922 1.00 2.02  ? 3522 GLN A N     1 
ATOM   14817 C  CA    . GLN A 1 3522 ? 193.907 189.197 251.261 1.00 1.95  ? 3522 GLN A CA    1 
ATOM   14818 C  C     . GLN A 1 3522 ? 194.098 187.684 251.242 1.00 3.15  ? 3522 GLN A C     1 
ATOM   14819 O  O     . GLN A 1 3522 ? 195.002 187.159 251.903 1.00 2.40  ? 3522 GLN A O     1 
ATOM   14820 C  CB    . GLN A 1 3522 ? 192.745 189.573 252.180 1.00 1.75  ? 3522 GLN A CB    1 
ATOM   14821 C  CG    . GLN A 1 3522 ? 192.728 188.800 253.490 1.00 3.08  ? 3522 GLN A CG    1 
ATOM   14822 C  CD    . GLN A 1 3522 ? 191.826 189.424 254.532 1.00 6.32  ? 3522 GLN A CD    1 
ATOM   14823 O  OE1   . GLN A 1 3522 ? 190.875 190.129 254.203 1.00 10.65 ? 3522 GLN A OE1   1 
ATOM   14824 N  NE2   . GLN A 1 3522 ? 192.121 189.167 255.799 1.00 11.54 ? 3522 GLN A NE2   1 
ATOM   14825 N  N     . GLN A 1 3523 ? 193.259 186.966 250.493 1.00 3.87  ? 3523 GLN A N     1 
ATOM   14826 C  CA    . GLN A 1 3523 ? 193.350 185.509 250.467 1.00 4.00  ? 3523 GLN A CA    1 
ATOM   14827 C  C     . GLN A 1 3523 ? 194.666 185.044 249.856 1.00 5.54  ? 3523 GLN A C     1 
ATOM   14828 O  O     . GLN A 1 3523 ? 195.303 184.116 250.369 1.00 6.71  ? 3523 GLN A O     1 
ATOM   14829 C  CB    . GLN A 1 3523 ? 192.167 184.922 249.700 1.00 6.14  ? 3523 GLN A CB    1 
ATOM   14830 C  CG    . GLN A 1 3523 ? 192.131 183.399 249.655 1.00 7.12  ? 3523 GLN A CG    1 
ATOM   14831 C  CD    . GLN A 1 3523 ? 191.953 182.771 251.027 1.00 18.38 ? 3523 GLN A CD    1 
ATOM   14832 O  OE1   . GLN A 1 3523 ? 192.919 182.571 251.763 1.00 20.83 ? 3523 GLN A OE1   1 
ATOM   14833 N  NE2   . GLN A 1 3523 ? 190.711 182.455 251.374 1.00 13.06 ? 3523 GLN A NE2   1 
ATOM   14834 N  N     . MET A 1 3524 ? 195.090 185.674 248.761 1.00 3.40  ? 3524 MET A N     1 
ATOM   14835 C  CA    . MET A 1 3524 ? 196.310 185.242 248.089 1.00 2.60  ? 3524 MET A CA    1 
ATOM   14836 C  C     . MET A 1 3524 ? 197.548 185.619 248.894 1.00 3.85  ? 3524 MET A C     1 
ATOM   14837 O  O     . MET A 1 3524 ? 198.541 184.882 248.897 1.00 5.02  ? 3524 MET A O     1 
ATOM   14838 C  CB    . MET A 1 3524 ? 196.373 185.835 246.684 1.00 3.49  ? 3524 MET A CB    1 
ATOM   14839 C  CG    . MET A 1 3524 ? 197.492 185.269 245.837 1.00 5.94  ? 3524 MET A CG    1 
ATOM   14840 S  SD    . MET A 1 3524 ? 197.260 183.506 245.548 1.00 27.38 ? 3524 MET A SD    1 
ATOM   14841 C  CE    . MET A 1 3524 ? 198.889 182.885 245.944 1.00 9.90  ? 3524 MET A CE    1 
ATOM   14842 N  N     . ARG A 1 3525 ? 197.511 186.764 249.580 1.00 2.31  ? 3525 ARG A N     1 
ATOM   14843 C  CA    . ARG A 1 3525 ? 198.618 187.140 250.456 1.00 1.79  ? 3525 ARG A CA    1 
ATOM   14844 C  C     . ARG A 1 3525 ? 198.800 186.117 251.568 1.00 3.02  ? 3525 ARG A C     1 
ATOM   14845 O  O     . ARG A 1 3525 ? 199.928 185.732 251.897 1.00 6.40  ? 3525 ARG A O     1 
ATOM   14846 C  CB    . ARG A 1 3525 ? 198.376 188.530 251.046 1.00 1.57  ? 3525 ARG A CB    1 
ATOM   14847 C  CG    . ARG A 1 3525 ? 198.493 189.675 250.058 1.00 0.93  ? 3525 ARG A CG    1 
ATOM   14848 C  CD    . ARG A 1 3525 ? 198.407 191.012 250.769 1.00 0.46  ? 3525 ARG A CD    1 
ATOM   14849 N  NE    . ARG A 1 3525 ? 198.521 192.139 249.851 1.00 0.38  ? 3525 ARG A NE    1 
ATOM   14850 C  CZ    . ARG A 1 3525 ? 198.519 193.410 250.226 1.00 0.32  ? 3525 ARG A CZ    1 
ATOM   14851 N  NH1   . ARG A 1 3525 ? 198.431 193.753 251.500 1.00 0.34  ? 3525 ARG A NH1   1 
ATOM   14852 N  NH2   . ARG A 1 3525 ? 198.610 194.360 249.303 1.00 0.25  ? 3525 ARG A NH2   1 
ATOM   14853 N  N     . GLN A 1 3526 ? 197.693 185.668 252.163 1.00 3.59  ? 3526 GLN A N     1 
ATOM   14854 C  CA    . GLN A 1 3526 ? 197.770 184.680 253.233 1.00 2.95  ? 3526 GLN A CA    1 
ATOM   14855 C  C     . GLN A 1 3526 ? 198.271 183.339 252.709 1.00 3.46  ? 3526 GLN A C     1 
ATOM   14856 O  O     . GLN A 1 3526 ? 199.037 182.646 253.389 1.00 2.84  ? 3526 GLN A O     1 
ATOM   14857 C  CB    . GLN A 1 3526 ? 196.402 184.529 253.898 1.00 3.87  ? 3526 GLN A CB    1 
ATOM   14858 C  CG    . GLN A 1 3526 ? 196.389 183.641 255.128 1.00 2.16  ? 3526 GLN A CG    1 
ATOM   14859 C  CD    . GLN A 1 3526 ? 197.478 184.001 256.115 1.00 3.08  ? 3526 GLN A CD    1 
ATOM   14860 O  OE1   . GLN A 1 3526 ? 197.569 185.139 256.568 1.00 8.04  ? 3526 GLN A OE1   1 
ATOM   14861 N  NE2   . GLN A 1 3526 ? 198.305 183.026 256.465 1.00 5.69  ? 3526 GLN A NE2   1 
ATOM   14862 N  N     . ASN A 1 3527 ? 197.846 182.957 251.501 1.00 2.95  ? 3527 ASN A N     1 
ATOM   14863 C  CA    . ASN A 1 3527 ? 198.312 181.707 250.909 1.00 1.71  ? 3527 ASN A CA    1 
ATOM   14864 C  C     . ASN A 1 3527 ? 199.816 181.730 250.673 1.00 2.24  ? 3527 ASN A C     1 
ATOM   14865 O  O     . ASN A 1 3527 ? 200.503 180.732 250.913 1.00 2.65  ? 3527 ASN A O     1 
ATOM   14866 C  CB    . ASN A 1 3527 ? 197.572 181.432 249.599 1.00 3.82  ? 3527 ASN A CB    1 
ATOM   14867 C  CG    . ASN A 1 3527 ? 196.095 181.162 249.806 1.00 9.33  ? 3527 ASN A CG    1 
ATOM   14868 O  OD1   . ASN A 1 3527 ? 195.673 180.739 250.883 1.00 14.91 ? 3527 ASN A OD1   1 
ATOM   14869 N  ND2   . ASN A 1 3527 ? 195.300 181.395 248.770 1.00 10.18 ? 3527 ASN A ND2   1 
ATOM   14870 N  N     . LEU A 1 3528 ? 200.344 182.855 250.184 1.00 1.78  ? 3528 LEU A N     1 
ATOM   14871 C  CA    . LEU A 1 3528 ? 201.783 182.965 249.967 1.00 0.90  ? 3528 LEU A CA    1 
ATOM   14872 C  C     . LEU A 1 3528 ? 202.550 182.866 251.278 1.00 0.54  ? 3528 LEU A C     1 
ATOM   14873 O  O     . LEU A 1 3528 ? 203.582 182.190 251.352 1.00 0.65  ? 3528 LEU A O     1 
ATOM   14874 C  CB    . LEU A 1 3528 ? 202.111 184.276 249.254 1.00 0.63  ? 3528 LEU A CB    1 
ATOM   14875 C  CG    . LEU A 1 3528 ? 201.752 184.359 247.771 1.00 0.76  ? 3528 LEU A CG    1 
ATOM   14876 C  CD1   . LEU A 1 3528 ? 201.815 185.793 247.287 1.00 0.96  ? 3528 LEU A CD1   1 
ATOM   14877 C  CD2   . LEU A 1 3528 ? 202.676 183.476 246.952 1.00 0.86  ? 3528 LEU A CD2   1 
ATOM   14878 N  N     . PHE A 1 3529 ? 202.062 183.537 252.321 1.00 1.28  ? 3529 PHE A N     1 
ATOM   14879 C  CA    . PHE A 1 3529 ? 202.755 183.519 253.605 1.00 1.13  ? 3529 PHE A CA    1 
ATOM   14880 C  C     . PHE A 1 3529 ? 202.718 182.132 254.236 1.00 1.82  ? 3529 PHE A C     1 
ATOM   14881 O  O     . PHE A 1 3529 ? 203.705 181.691 254.833 1.00 2.09  ? 3529 PHE A O     1 
ATOM   14882 C  CB    . PHE A 1 3529 ? 202.142 184.563 254.538 1.00 0.93  ? 3529 PHE A CB    1 
ATOM   14883 C  CG    . PHE A 1 3529 ? 203.059 185.008 255.639 1.00 1.76  ? 3529 PHE A CG    1 
ATOM   14884 C  CD1   . PHE A 1 3529 ? 203.095 184.334 256.846 1.00 0.84  ? 3529 PHE A CD1   1 
ATOM   14885 C  CD2   . PHE A 1 3529 ? 203.888 186.105 255.464 1.00 0.58  ? 3529 PHE A CD2   1 
ATOM   14886 C  CE1   . PHE A 1 3529 ? 203.939 184.744 257.856 1.00 0.38  ? 3529 PHE A CE1   1 
ATOM   14887 C  CE2   . PHE A 1 3529 ? 204.733 186.518 256.470 1.00 0.35  ? 3529 PHE A CE2   1 
ATOM   14888 C  CZ    . PHE A 1 3529 ? 204.759 185.837 257.667 1.00 0.46  ? 3529 PHE A CZ    1 
ATOM   14889 N  N     . THR A 1 3530 ? 201.587 181.433 254.116 1.00 2.13  ? 3530 THR A N     1 
ATOM   14890 C  CA    . THR A 1 3530 ? 201.497 180.073 254.642 1.00 2.59  ? 3530 THR A CA    1 
ATOM   14891 C  C     . THR A 1 3530 ? 202.418 179.125 253.882 1.00 2.03  ? 3530 THR A C     1 
ATOM   14892 O  O     . THR A 1 3530 ? 203.050 178.249 254.484 1.00 3.98  ? 3530 THR A O     1 
ATOM   14893 C  CB    . THR A 1 3530 ? 200.047 179.587 254.590 1.00 2.19  ? 3530 THR A CB    1 
ATOM   14894 O  OG1   . THR A 1 3530 ? 199.252 180.365 255.492 1.00 2.19  ? 3530 THR A OG1   1 
ATOM   14895 C  CG2   . THR A 1 3530 ? 199.950 178.121 254.987 1.00 2.73  ? 3530 THR A CG2   1 
ATOM   14896 N  N     . THR A 1 3531 ? 202.510 179.287 252.560 1.00 1.63  ? 3531 THR A N     1 
ATOM   14897 C  CA    . THR A 1 3531 ? 203.412 178.454 251.770 1.00 0.89  ? 3531 THR A CA    1 
ATOM   14898 C  C     . THR A 1 3531 ? 204.868 178.685 252.159 1.00 1.67  ? 3531 THR A C     1 
ATOM   14899 O  O     . THR A 1 3531 ? 205.638 177.727 252.295 1.00 2.72  ? 3531 THR A O     1 
ATOM   14900 C  CB    . THR A 1 3531 ? 203.206 178.727 250.280 1.00 1.70  ? 3531 THR A CB    1 
ATOM   14901 O  OG1   . THR A 1 3531 ? 201.821 178.575 249.952 1.00 3.12  ? 3531 THR A OG1   1 
ATOM   14902 C  CG2   . THR A 1 3531 ? 204.029 177.764 249.439 1.00 1.46  ? 3531 THR A CG2   1 
ATOM   14903 N  N     . TRP A 1 3532 ? 205.266 179.948 252.335 1.00 2.03  ? 3532 TRP A N     1 
ATOM   14904 C  CA    . TRP A 1 3532 ? 206.626 180.237 252.780 1.00 1.13  ? 3532 TRP A CA    1 
ATOM   14905 C  C     . TRP A 1 3532 ? 206.860 179.730 254.195 1.00 1.33  ? 3532 TRP A C     1 
ATOM   14906 O  O     . TRP A 1 3532 ? 207.912 179.151 254.488 1.00 2.95  ? 3532 TRP A O     1 
ATOM   14907 C  CB    . TRP A 1 3532 ? 206.903 181.739 252.713 1.00 0.35  ? 3532 TRP A CB    1 
ATOM   14908 C  CG    . TRP A 1 3532 ? 206.628 182.370 251.396 1.00 0.19  ? 3532 TRP A CG    1 
ATOM   14909 C  CD1   . TRP A 1 3532 ? 206.725 181.787 250.168 1.00 0.24  ? 3532 TRP A CD1   1 
ATOM   14910 C  CD2   . TRP A 1 3532 ? 206.208 183.717 251.169 1.00 0.20  ? 3532 TRP A CD2   1 
ATOM   14911 N  NE1   . TRP A 1 3532 ? 206.389 182.687 249.192 1.00 0.16  ? 3532 TRP A NE1   1 
ATOM   14912 C  CE2   . TRP A 1 3532 ? 206.066 183.881 249.779 1.00 0.11  ? 3532 TRP A CE2   1 
ATOM   14913 C  CE3   . TRP A 1 3532 ? 205.934 184.801 252.007 1.00 0.15  ? 3532 TRP A CE3   1 
ATOM   14914 C  CZ2   . TRP A 1 3532 ? 205.669 185.083 249.209 1.00 0.14  ? 3532 TRP A CZ2   1 
ATOM   14915 C  CZ3   . TRP A 1 3532 ? 205.539 185.992 251.440 1.00 0.08  ? 3532 TRP A CZ3   1 
ATOM   14916 C  CH2   . TRP A 1 3532 ? 205.411 186.126 250.054 1.00 0.11  ? 3532 TRP A CH2   1 
ATOM   14917 N  N     . SER A 1 3533 ? 205.888 179.946 255.086 1.00 1.98  ? 3533 SER A N     1 
ATOM   14918 C  CA    . SER A 1 3533 ? 206.031 179.499 256.468 1.00 2.31  ? 3533 SER A CA    1 
ATOM   14919 C  C     . SER A 1 3533 ? 206.141 177.984 256.545 1.00 3.53  ? 3533 SER A C     1 
ATOM   14920 O  O     . SER A 1 3533 ? 206.939 177.451 257.326 1.00 3.08  ? 3533 SER A O     1 
ATOM   14921 C  CB    . SER A 1 3533 ? 204.851 179.996 257.302 1.00 1.92  ? 3533 SER A CB    1 
ATOM   14922 O  OG    . SER A 1 3533 ? 204.821 181.412 257.345 1.00 3.30  ? 3533 SER A OG    1 
ATOM   14923 N  N     . HIS A 1 3534 ? 205.348 177.272 255.742 1.00 2.73  ? 3534 HIS A N     1 
ATOM   14924 C  CA    . HIS A 1 3534 ? 205.450 175.818 255.701 1.00 4.26  ? 3534 HIS A CA    1 
ATOM   14925 C  C     . HIS A 1 3534 ? 206.831 175.374 255.241 1.00 4.20  ? 3534 HIS A C     1 
ATOM   14926 O  O     . HIS A 1 3534 ? 207.419 174.454 255.819 1.00 4.84  ? 3534 HIS A O     1 
ATOM   14927 C  CB    . HIS A 1 3534 ? 204.375 175.238 254.783 1.00 4.33  ? 3534 HIS A CB    1 
ATOM   14928 C  CG    . HIS A 1 3534 ? 203.019 175.163 255.408 1.00 10.93 ? 3534 HIS A CG    1 
ATOM   14929 N  ND1   . HIS A 1 3534 ? 202.816 175.284 256.766 1.00 10.53 ? 3534 HIS A ND1   1 
ATOM   14930 C  CD2   . HIS A 1 3534 ? 201.795 174.972 254.861 1.00 9.94  ? 3534 HIS A CD2   1 
ATOM   14931 C  CE1   . HIS A 1 3534 ? 201.525 175.175 257.027 1.00 12.56 ? 3534 HIS A CE1   1 
ATOM   14932 N  NE2   . HIS A 1 3534 ? 200.884 174.984 255.888 1.00 11.20 ? 3534 HIS A NE2   1 
ATOM   14933 N  N     . HIS A 1 3535 ? 207.370 176.029 254.210 1.00 3.86  ? 3535 HIS A N     1 
ATOM   14934 C  CA    . HIS A 1 3535 ? 208.675 175.645 253.685 1.00 2.26  ? 3535 HIS A CA    1 
ATOM   14935 C  C     . HIS A 1 3535 ? 209.774 175.846 254.720 1.00 3.44  ? 3535 HIS A C     1 
ATOM   14936 O  O     . HIS A 1 3535 ? 210.692 175.025 254.827 1.00 9.11  ? 3535 HIS A O     1 
ATOM   14937 C  CB    . HIS A 1 3535 ? 208.983 176.439 252.420 1.00 1.13  ? 3535 HIS A CB    1 
ATOM   14938 C  CG    . HIS A 1 3535 ? 210.247 176.022 251.738 1.00 2.04  ? 3535 HIS A CG    1 
ATOM   14939 N  ND1   . HIS A 1 3535 ? 211.470 176.588 252.028 1.00 2.83  ? 3535 HIS A ND1   1 
ATOM   14940 C  CD2   . HIS A 1 3535 ? 210.480 175.092 250.782 1.00 1.88  ? 3535 HIS A CD2   1 
ATOM   14941 C  CE1   . HIS A 1 3535 ? 212.401 176.025 251.281 1.00 3.50  ? 3535 HIS A CE1   1 
ATOM   14942 N  NE2   . HIS A 1 3535 ? 211.826 175.114 250.517 1.00 3.71  ? 3535 HIS A NE2   1 
ATOM   14943 N  N     . LEU A 1 3536 ? 209.705 176.940 255.479 1.00 2.52  ? 3536 LEU A N     1 
ATOM   14944 C  CA    . LEU A 1 3536 ? 210.692 177.171 256.527 1.00 3.59  ? 3536 LEU A CA    1 
ATOM   14945 C  C     . LEU A 1 3536 ? 210.631 176.077 257.585 1.00 5.53  ? 3536 LEU A C     1 
ATOM   14946 O  O     . LEU A 1 3536 ? 211.665 175.675 258.132 1.00 8.45  ? 3536 LEU A O     1 
ATOM   14947 C  CB    . LEU A 1 3536 ? 210.475 178.545 257.159 1.00 5.53  ? 3536 LEU A CB    1 
ATOM   14948 C  CG    . LEU A 1 3536 ? 210.757 179.771 256.286 1.00 3.38  ? 3536 LEU A CG    1 
ATOM   14949 C  CD1   . LEU A 1 3536 ? 210.878 181.015 257.144 1.00 4.29  ? 3536 LEU A CD1   1 
ATOM   14950 C  CD2   . LEU A 1 3536 ? 212.008 179.572 255.449 1.00 3.74  ? 3536 LEU A CD2   1 
ATOM   14951 N  N     . GLN A 1 3537 ? 209.427 175.589 257.892 1.00 6.62  ? 3537 GLN A N     1 
ATOM   14952 C  CA    . GLN A 1 3537 ? 209.287 174.502 258.856 1.00 6.65  ? 3537 GLN A CA    1 
ATOM   14953 C  C     . GLN A 1 3537 ? 209.962 173.228 258.364 1.00 7.92  ? 3537 GLN A C     1 
ATOM   14954 O  O     . GLN A 1 3537 ? 210.660 172.553 259.128 1.00 10.58 ? 3537 GLN A O     1 
ATOM   14955 C  CB    . GLN A 1 3537 ? 207.808 174.251 259.153 1.00 8.35  ? 3537 GLN A CB    1 
ATOM   14956 C  CG    . GLN A 1 3537 ? 207.122 175.388 259.887 1.00 10.68 ? 3537 GLN A CG    1 
ATOM   14957 C  CD    . GLN A 1 3537 ? 205.651 175.121 260.146 1.00 20.10 ? 3537 GLN A CD    1 
ATOM   14958 O  OE1   . GLN A 1 3537 ? 205.108 174.105 259.716 1.00 18.54 ? 3537 GLN A OE1   1 
ATOM   14959 N  NE2   . GLN A 1 3537 ? 205.001 176.035 260.859 1.00 19.79 ? 3537 GLN A NE2   1 
ATOM   14960 N  N     . GLN A 1 3538 ? 209.772 172.882 257.088 1.00 5.14  ? 3538 GLN A N     1 
ATOM   14961 C  CA    . GLN A 1 3538 ? 210.428 171.696 256.548 1.00 5.70  ? 3538 GLN A CA    1 
ATOM   14962 C  C     . GLN A 1 3538 ? 211.934 171.865 256.438 1.00 10.73 ? 3538 GLN A C     1 
ATOM   14963 O  O     . GLN A 1 3538 ? 212.649 170.863 256.345 1.00 21.73 ? 3538 GLN A O     1 
ATOM   14964 C  CB    . GLN A 1 3538 ? 209.851 171.331 255.178 1.00 10.15 ? 3538 GLN A CB    1 
ATOM   14965 C  CG    . GLN A 1 3538 ? 208.381 171.640 255.008 1.00 5.22  ? 3538 GLN A CG    1 
ATOM   14966 C  CD    . GLN A 1 3538 ? 207.779 170.952 253.801 1.00 21.45 ? 3538 GLN A CD    1 
ATOM   14967 O  OE1   . GLN A 1 3538 ? 208.494 170.418 252.954 1.00 26.19 ? 3538 GLN A OE1   1 
ATOM   14968 N  NE2   . GLN A 1 3538 ? 206.453 170.960 253.716 1.00 23.05 ? 3538 GLN A NE2   1 
ATOM   14969 N  N     . ALA A 1 3539 ? 212.432 173.100 256.442 1.00 9.73  ? 3539 ALA A N     1 
ATOM   14970 C  CA    . ALA A 1 3539 ? 213.859 173.371 256.374 1.00 8.29  ? 3539 ALA A CA    1 
ATOM   14971 C  C     . ALA A 1 3539 ? 214.479 173.608 257.745 1.00 9.44  ? 3539 ALA A C     1 
ATOM   14972 O  O     . ALA A 1 3539 ? 215.669 173.931 257.825 1.00 19.13 ? 3539 ALA A O     1 
ATOM   14973 C  CB    . ALA A 1 3539 ? 214.125 174.571 255.467 1.00 5.39  ? 3539 ALA A CB    1 
ATOM   14974 N  N     . ASN A 1 3540 ? 213.700 173.460 258.818 1.00 6.53  ? 3540 ASN A N     1 
ATOM   14975 C  CA    . ASN A 1 3540 ? 214.157 173.703 260.189 1.00 8.42  ? 3540 ASN A CA    1 
ATOM   14976 C  C     . ASN A 1 3540 ? 214.646 175.135 260.384 1.00 8.75  ? 3540 ASN A C     1 
ATOM   14977 O  O     . ASN A 1 3540 ? 215.559 175.388 261.174 1.00 15.63 ? 3540 ASN A O     1 
ATOM   14978 C  CB    . ASN A 1 3540 ? 215.249 172.712 260.604 1.00 10.62 ? 3540 ASN A CB    1 
ATOM   14979 C  CG    . ASN A 1 3540 ? 214.701 171.334 260.907 1.00 14.34 ? 3540 ASN A CG    1 
ATOM   14980 O  OD1   . ASN A 1 3540 ? 213.625 170.964 260.442 1.00 15.66 ? 3540 ASN A OD1   1 
ATOM   14981 N  ND2   . ASN A 1 3540 ? 215.447 170.563 261.689 1.00 17.14 ? 3540 ASN A ND2   1 
ATOM   14982 N  N     . ILE A 1 3541 ? 214.045 176.085 259.674 1.00 8.56  ? 3541 ILE A N     1 
ATOM   14983 C  CA    . ILE A 1 3541 ? 214.340 177.500 259.861 1.00 7.92  ? 3541 ILE A CA    1 
ATOM   14984 C  C     . ILE A 1 3541 ? 213.398 178.037 260.930 1.00 8.90  ? 3541 ILE A C     1 
ATOM   14985 O  O     . ILE A 1 3541 ? 212.173 177.938 260.797 1.00 12.01 ? 3541 ILE A O     1 
ATOM   14986 C  CB    . ILE A 1 3541 ? 214.193 178.285 258.548 1.00 6.41  ? 3541 ILE A CB    1 
ATOM   14987 C  CG1   . ILE A 1 3541 ? 214.995 177.615 257.430 1.00 7.78  ? 3541 ILE A CG1   1 
ATOM   14988 C  CG2   . ILE A 1 3541 ? 214.623 179.732 258.745 1.00 4.81  ? 3541 ILE A CG2   1 
ATOM   14989 C  CD1   . ILE A 1 3541 ? 216.480 177.876 257.493 1.00 7.61  ? 3541 ILE A CD1   1 
ATOM   14990 N  N     . GLN A 1 3542 ? 213.964 178.608 261.986 1.00 9.88  ? 3542 GLN A N     1 
ATOM   14991 C  CA    . GLN A 1 3542 ? 213.174 179.023 263.136 1.00 10.19 ? 3542 GLN A CA    1 
ATOM   14992 C  C     . GLN A 1 3542 ? 212.499 180.363 262.871 1.00 8.50  ? 3542 GLN A C     1 
ATOM   14993 O  O     . GLN A 1 3542 ? 213.144 181.321 262.435 1.00 10.32 ? 3542 GLN A O     1 
ATOM   14994 C  CB    . GLN A 1 3542 ? 214.058 179.114 264.378 1.00 10.83 ? 3542 GLN A CB    1 
ATOM   14995 C  CG    . GLN A 1 3542 ? 214.627 177.781 264.821 1.00 13.19 ? 3542 GLN A CG    1 
ATOM   14996 C  CD    . GLN A 1 3542 ? 213.550 176.796 265.218 1.00 24.83 ? 3542 GLN A CD    1 
ATOM   14997 O  OE1   . GLN A 1 3542 ? 213.302 175.816 264.518 1.00 31.49 ? 3542 GLN A OE1   1 
ATOM   14998 N  NE2   . GLN A 1 3542 ? 212.899 177.053 266.347 1.00 22.40 ? 3542 GLN A NE2   1 
ATOM   14999 N  N     . PHE A 1 3543 ? 211.196 180.422 263.137 1.00 7.59  ? 3543 PHE A N     1 
ATOM   15000 C  CA    . PHE A 1 3543 ? 210.433 181.657 263.040 1.00 6.38  ? 3543 PHE A CA    1 
ATOM   15001 C  C     . PHE A 1 3543 ? 209.250 181.567 263.993 1.00 10.25 ? 3543 PHE A C     1 
ATOM   15002 O  O     . PHE A 1 3543 ? 208.689 180.489 264.204 1.00 12.79 ? 3543 PHE A O     1 
ATOM   15003 C  CB    . PHE A 1 3543 ? 209.945 181.919 261.610 1.00 4.66  ? 3543 PHE A CB    1 
ATOM   15004 C  CG    . PHE A 1 3543 ? 208.951 180.908 261.113 1.00 6.23  ? 3543 PHE A CG    1 
ATOM   15005 C  CD1   . PHE A 1 3543 ? 209.375 179.707 260.570 1.00 6.62  ? 3543 PHE A CD1   1 
ATOM   15006 C  CD2   . PHE A 1 3543 ? 207.594 181.163 261.180 1.00 5.92  ? 3543 PHE A CD2   1 
ATOM   15007 C  CE1   . PHE A 1 3543 ? 208.464 178.779 260.114 1.00 6.60  ? 3543 PHE A CE1   1 
ATOM   15008 C  CE2   . PHE A 1 3543 ? 206.679 180.239 260.721 1.00 6.25  ? 3543 PHE A CE2   1 
ATOM   15009 C  CZ    . PHE A 1 3543 ? 207.113 179.046 260.189 1.00 4.96  ? 3543 PHE A CZ    1 
ATOM   15010 N  N     . ARG A 1 3544 ? 208.878 182.706 264.564 1.00 10.63 ? 3544 ARG A N     1 
ATOM   15011 C  CA    . ARG A 1 3544 ? 207.737 182.757 265.467 1.00 11.14 ? 3544 ARG A CA    1 
ATOM   15012 C  C     . ARG A 1 3544 ? 206.433 182.801 264.681 1.00 12.44 ? 3544 ARG A C     1 
ATOM   15013 O  O     . ARG A 1 3544 ? 206.363 183.380 263.593 1.00 15.76 ? 3544 ARG A O     1 
ATOM   15014 C  CB    . ARG A 1 3544 ? 207.845 183.965 266.395 1.00 10.85 ? 3544 ARG A CB    1 
ATOM   15015 C  CG    . ARG A 1 3544 ? 209.070 183.918 267.293 1.00 13.05 ? 3544 ARG A CG    1 
ATOM   15016 C  CD    . ARG A 1 3544 ? 209.414 185.279 267.862 1.00 15.30 ? 3544 ARG A CD    1 
ATOM   15017 N  NE    . ARG A 1 3544 ? 209.118 186.359 266.931 1.00 17.04 ? 3544 ARG A NE    1 
ATOM   15018 C  CZ    . ARG A 1 3544 ? 209.337 187.641 267.185 1.00 18.71 ? 3544 ARG A CZ    1 
ATOM   15019 N  NH1   . ARG A 1 3544 ? 209.874 188.038 268.327 1.00 19.07 ? 3544 ARG A NH1   1 
ATOM   15020 N  NH2   . ARG A 1 3544 ? 209.007 188.547 266.270 1.00 16.05 ? 3544 ARG A NH2   1 
ATOM   15021 N  N     . THR A 1 3545 ? 205.396 182.168 265.236 1.00 18.20 ? 3545 THR A N     1 
ATOM   15022 C  CA    . THR A 1 3545 ? 204.092 182.077 264.587 1.00 18.51 ? 3545 THR A CA    1 
ATOM   15023 C  C     . THR A 1 3545 ? 203.008 182.816 265.363 1.00 21.39 ? 3545 THR A C     1 
ATOM   15024 O  O     . THR A 1 3545 ? 201.819 182.612 265.104 1.00 21.52 ? 3545 THR A O     1 
ATOM   15025 C  CB    . THR A 1 3545 ? 203.688 180.613 264.393 1.00 21.65 ? 3545 THR A CB    1 
ATOM   15026 O  OG1   . THR A 1 3545 ? 203.587 179.971 265.671 1.00 28.13 ? 3545 THR A OG1   1 
ATOM   15027 C  CG2   . THR A 1 3545 ? 204.716 179.884 263.553 1.00 14.83 ? 3545 THR A CG2   1 
ATOM   15028 N  N     . ASP A 1 3546 ? 203.390 183.674 266.307 1.00 22.68 ? 3546 ASP A N     1 
ATOM   15029 C  CA    . ASP A 1 3546 ? 202.433 184.389 267.145 1.00 24.85 ? 3546 ASP A CA    1 
ATOM   15030 C  C     . ASP A 1 3546 ? 202.250 185.824 266.667 1.00 28.31 ? 3546 ASP A C     1 
ATOM   15031 O  O     . ASP A 1 3546 ? 201.115 186.269 266.471 1.00 26.10 ? 3546 ASP A O     1 
ATOM   15032 C  CB    . ASP A 1 3546 ? 202.882 184.349 268.608 1.00 19.70 ? 3546 ASP A CB    1 
ATOM   15033 C  CG    . ASP A 1 3546 ? 204.342 184.713 268.775 1.00 27.83 ? 3546 ASP A CG    1 
ATOM   15034 O  OD1   . ASP A 1 3546 ? 205.000 184.999 267.754 1.00 30.61 ? 3546 ASP A OD1   1 
ATOM   15035 O  OD2   . ASP A 1 3546 ? 204.832 184.715 269.924 1.00 31.88 ? 3546 ASP A OD2   1 
ATOM   15036 N  N     . ILE A 1 3547 ? 203.341 186.568 266.475 1.00 23.04 ? 3547 ILE A N     1 
ATOM   15037 C  CA    . ILE A 1 3547 ? 203.229 187.974 266.115 1.00 21.38 ? 3547 ILE A CA    1 
ATOM   15038 C  C     . ILE A 1 3547 ? 202.747 188.108 264.678 1.00 23.16 ? 3547 ILE A C     1 
ATOM   15039 O  O     . ILE A 1 3547 ? 203.202 187.396 263.775 1.00 21.01 ? 3547 ILE A O     1 
ATOM   15040 C  CB    . ILE A 1 3547 ? 204.576 188.686 266.340 1.00 26.73 ? 3547 ILE A CB    1 
ATOM   15041 C  CG1   . ILE A 1 3547 ? 204.458 190.180 266.025 1.00 18.53 ? 3547 ILE A CG1   1 
ATOM   15042 C  CG2   . ILE A 1 3547 ? 205.688 188.028 265.528 1.00 19.57 ? 3547 ILE A CG2   1 
ATOM   15043 C  CD1   . ILE A 1 3547 ? 205.679 190.977 266.405 1.00 12.99 ? 3547 ILE A CD1   1 
ATOM   15044 N  N     . ALA A 1 3548 ? 201.797 189.012 264.470 1.00 20.50 ? 3548 ALA A N     1 
ATOM   15045 C  CA    . ALA A 1 3548 ? 201.292 189.299 263.139 1.00 13.80 ? 3548 ALA A CA    1 
ATOM   15046 C  C     . ALA A 1 3548 ? 202.333 190.065 262.329 1.00 12.65 ? 3548 ALA A C     1 
ATOM   15047 O  O     . ALA A 1 3548 ? 203.225 190.720 262.876 1.00 11.91 ? 3548 ALA A O     1 
ATOM   15048 C  CB    . ALA A 1 3548 ? 199.992 190.096 263.218 1.00 15.99 ? 3548 ALA A CB    1 
ATOM   15049 N  N     . ARG A 1 3549 ? 202.210 189.976 261.004 1.00 9.77  ? 3549 ARG A N     1 
ATOM   15050 C  CA    . ARG A 1 3549 ? 203.187 190.617 260.132 1.00 6.62  ? 3549 ARG A CA    1 
ATOM   15051 C  C     . ARG A 1 3549 ? 203.106 192.137 260.234 1.00 6.03  ? 3549 ARG A C     1 
ATOM   15052 O  O     . ARG A 1 3549 ? 204.125 192.828 260.122 1.00 12.27 ? 3549 ARG A O     1 
ATOM   15053 C  CB    . ARG A 1 3549 ? 202.992 190.157 258.686 1.00 6.60  ? 3549 ARG A CB    1 
ATOM   15054 C  CG    . ARG A 1 3549 ? 201.547 190.069 258.238 1.00 11.22 ? 3549 ARG A CG    1 
ATOM   15055 C  CD    . ARG A 1 3549 ? 201.362 189.034 257.140 1.00 2.62  ? 3549 ARG A CD    1 
ATOM   15056 N  NE    . ARG A 1 3549 ? 199.957 188.895 256.780 1.00 3.05  ? 3549 ARG A NE    1 
ATOM   15057 C  CZ    . ARG A 1 3549 ? 199.483 188.008 255.917 1.00 3.56  ? 3549 ARG A CZ    1 
ATOM   15058 N  NH1   . ARG A 1 3549 ? 200.269 187.112 255.346 1.00 13.03 ? 3549 ARG A NH1   1 
ATOM   15059 N  NH2   . ARG A 1 3549 ? 198.187 188.014 255.626 1.00 2.93  ? 3549 ARG A NH2   1 
ATOM   15060 N  N     . THR A 1 3550 ? 201.904 192.678 260.443 1.00 7.01  ? 3550 THR A N     1 
ATOM   15061 C  CA    . THR A 1 3550 ? 201.763 194.122 260.607 1.00 7.28  ? 3550 THR A CA    1 
ATOM   15062 C  C     . THR A 1 3550 ? 202.447 194.616 261.874 1.00 9.38  ? 3550 THR A C     1 
ATOM   15063 O  O     . THR A 1 3550 ? 203.046 195.697 261.873 1.00 7.93  ? 3550 THR A O     1 
ATOM   15064 C  CB    . THR A 1 3550 ? 200.286 194.520 260.619 1.00 6.34  ? 3550 THR A CB    1 
ATOM   15065 O  OG1   . THR A 1 3550 ? 199.597 193.796 261.646 1.00 16.31 ? 3550 THR A OG1   1 
ATOM   15066 C  CG2   . THR A 1 3550 ? 199.645 194.231 259.278 1.00 4.15  ? 3550 THR A CG2   1 
ATOM   15067 N  N     . GLU A 1 3551 ? 202.360 193.852 262.961 1.00 12.71 ? 3551 GLU A N     1 
ATOM   15068 C  CA    . GLU A 1 3551 ? 202.992 194.261 264.211 1.00 9.96  ? 3551 GLU A CA    1 
ATOM   15069 C  C     . GLU A 1 3551 ? 204.508 194.151 264.154 1.00 8.50  ? 3551 GLU A C     1 
ATOM   15070 O  O     . GLU A 1 3551 ? 205.207 194.935 264.805 1.00 10.91 ? 3551 GLU A O     1 
ATOM   15071 C  CB    . GLU A 1 3551 ? 202.452 193.425 265.370 1.00 11.15 ? 3551 GLU A CB    1 
ATOM   15072 C  CG    . GLU A 1 3551 ? 200.941 193.353 265.423 1.00 12.21 ? 3551 GLU A CG    1 
ATOM   15073 C  CD    . GLU A 1 3551 ? 200.306 194.714 265.611 1.00 21.62 ? 3551 GLU A CD    1 
ATOM   15074 O  OE1   . GLU A 1 3551 ? 200.288 195.209 266.757 1.00 19.38 ? 3551 GLU A OE1   1 
ATOM   15075 O  OE2   . GLU A 1 3551 ? 199.826 195.290 264.610 1.00 26.57 ? 3551 GLU A OE2   1 
ATOM   15076 N  N     . TYR A 1 3552 ? 205.034 193.192 263.396 1.00 8.49  ? 3552 TYR A N     1 
ATOM   15077 C  CA    . TYR A 1 3552 ? 206.472 192.984 263.316 1.00 6.92  ? 3552 TYR A CA    1 
ATOM   15078 C  C     . TYR A 1 3552 ? 207.163 193.951 262.361 1.00 5.14  ? 3552 TYR A C     1 
ATOM   15079 O  O     . TYR A 1 3552 ? 208.377 194.143 262.474 1.00 5.97  ? 3552 TYR A O     1 
ATOM   15080 C  CB    . TYR A 1 3552 ? 206.761 191.536 262.900 1.00 6.53  ? 3552 TYR A CB    1 
ATOM   15081 C  CG    . TYR A 1 3552 ? 208.223 191.156 262.870 1.00 7.11  ? 3552 TYR A CG    1 
ATOM   15082 C  CD1   . TYR A 1 3552 ? 208.883 190.783 264.032 1.00 5.80  ? 3552 TYR A CD1   1 
ATOM   15083 C  CD2   . TYR A 1 3552 ? 208.936 191.133 261.678 1.00 5.28  ? 3552 TYR A CD2   1 
ATOM   15084 C  CE1   . TYR A 1 3552 ? 210.211 190.425 264.015 1.00 6.56  ? 3552 TYR A CE1   1 
ATOM   15085 C  CE2   . TYR A 1 3552 ? 210.267 190.771 261.651 1.00 5.43  ? 3552 TYR A CE2   1 
ATOM   15086 C  CZ    . TYR A 1 3552 ? 210.900 190.417 262.824 1.00 8.84  ? 3552 TYR A CZ    1 
ATOM   15087 O  OH    . TYR A 1 3552 ? 212.225 190.056 262.812 1.00 6.54  ? 3552 TYR A OH    1 
ATOM   15088 N  N     . LEU A 1 3553 ? 206.425 194.574 261.447 1.00 5.84  ? 3553 LEU A N     1 
ATOM   15089 C  CA    . LEU A 1 3553 ? 207.006 195.478 260.464 1.00 4.80  ? 3553 LEU A CA    1 
ATOM   15090 C  C     . LEU A 1 3553 ? 206.636 196.935 260.688 1.00 4.07  ? 3553 LEU A C     1 
ATOM   15091 O  O     . LEU A 1 3553 ? 206.989 197.783 259.864 1.00 4.04  ? 3553 LEU A O     1 
ATOM   15092 C  CB    . LEU A 1 3553 ? 206.598 195.053 259.050 1.00 3.01  ? 3553 LEU A CB    1 
ATOM   15093 C  CG    . LEU A 1 3553 ? 207.219 193.745 258.573 1.00 4.39  ? 3553 LEU A CG    1 
ATOM   15094 C  CD1   . LEU A 1 3553 ? 206.674 193.352 257.212 1.00 2.44  ? 3553 LEU A CD1   1 
ATOM   15095 C  CD2   . LEU A 1 3553 ? 208.730 193.897 258.527 1.00 3.38  ? 3553 LEU A CD2   1 
ATOM   15096 N  N     . SER A 1 3554 ? 205.938 197.252 261.773 1.00 6.22  ? 3554 SER A N     1 
ATOM   15097 C  CA    . SER A 1 3554 ? 205.605 198.631 262.093 1.00 6.31  ? 3554 SER A CA    1 
ATOM   15098 C  C     . SER A 1 3554 ? 205.396 198.742 263.593 1.00 5.53  ? 3554 SER A C     1 
ATOM   15099 O  O     . SER A 1 3554 ? 205.025 197.770 264.255 1.00 9.24  ? 3554 SER A O     1 
ATOM   15100 C  CB    . SER A 1 3554 ? 204.359 199.105 261.336 1.00 3.54  ? 3554 SER A CB    1 
ATOM   15101 O  OG    . SER A 1 3554 ? 203.183 198.549 261.890 1.00 7.62  ? 3554 SER A OG    1 
ATOM   15102 N  N     . ASN A 1 3555 ? 205.649 199.931 264.125 1.00 7.33  ? 3555 ASN A N     1 
ATOM   15103 C  CA    . ASN A 1 3555 ? 205.441 200.206 265.538 1.00 7.11  ? 3555 ASN A CA    1 
ATOM   15104 C  C     . ASN A 1 3555 ? 204.071 200.840 265.757 1.00 6.73  ? 3555 ASN A C     1 
ATOM   15105 O  O     . ASN A 1 3555 ? 203.409 201.295 264.823 1.00 9.07  ? 3555 ASN A O     1 
ATOM   15106 C  CB    . ASN A 1 3555 ? 206.552 201.108 266.084 1.00 6.29  ? 3555 ASN A CB    1 
ATOM   15107 C  CG    . ASN A 1 3555 ? 206.779 202.340 265.234 1.00 9.46  ? 3555 ASN A CG    1 
ATOM   15108 O  OD1   . ASN A 1 3555 ? 205.975 203.269 265.244 1.00 13.45 ? 3555 ASN A OD1   1 
ATOM   15109 N  ND2   . ASN A 1 3555 ? 207.882 202.357 264.497 1.00 11.32 ? 3555 ASN A ND2   1 
ATOM   15110 N  N     . ALA A 1 3556 ? 203.646 200.854 267.022 1.00 7.96  ? 3556 ALA A N     1 
ATOM   15111 C  CA    . ALA A 1 3556 ? 202.360 201.452 267.363 1.00 7.39  ? 3556 ALA A CA    1 
ATOM   15112 C  C     . ALA A 1 3556 ? 202.353 202.955 267.113 1.00 8.32  ? 3556 ALA A C     1 
ATOM   15113 O  O     . ALA A 1 3556 ? 201.309 203.518 266.766 1.00 13.72 ? 3556 ALA A O     1 
ATOM   15114 C  CB    . ALA A 1 3556 ? 202.013 201.154 268.820 1.00 8.77  ? 3556 ALA A CB    1 
ATOM   15115 N  N     . ASP A 1 3557 ? 203.499 203.617 267.288 1.00 7.69  ? 3557 ASP A N     1 
ATOM   15116 C  CA    . ASP A 1 3557 ? 203.571 205.051 267.032 1.00 8.14  ? 3557 ASP A CA    1 
ATOM   15117 C  C     . ASP A 1 3557 ? 203.301 205.366 265.567 1.00 11.75 ? 3557 ASP A C     1 
ATOM   15118 O  O     . ASP A 1 3557 ? 202.588 206.325 265.250 1.00 10.99 ? 3557 ASP A O     1 
ATOM   15119 C  CB    . ASP A 1 3557 ? 204.939 205.588 267.451 1.00 8.71  ? 3557 ASP A CB    1 
ATOM   15120 C  CG    . ASP A 1 3557 ? 205.115 205.617 268.954 1.00 18.04 ? 3557 ASP A CG    1 
ATOM   15121 O  OD1   . ASP A 1 3557 ? 204.115 205.828 269.666 1.00 20.73 ? 3557 ASP A OD1   1 
ATOM   15122 O  OD2   . ASP A 1 3557 ? 206.257 205.426 269.424 1.00 24.65 ? 3557 ASP A OD2   1 
ATOM   15123 N  N     . GLU A 1 3558 ? 203.868 204.572 264.658 1.00 6.61  ? 3558 GLU A N     1 
ATOM   15124 C  CA    . GLU A 1 3558 ? 203.654 204.813 263.235 1.00 8.27  ? 3558 GLU A CA    1 
ATOM   15125 C  C     . GLU A 1 3558 ? 202.218 204.508 262.832 1.00 7.00  ? 3558 GLU A C     1 
ATOM   15126 O  O     . GLU A 1 3558 ? 201.639 205.213 261.997 1.00 5.82  ? 3558 GLU A O     1 
ATOM   15127 C  CB    . GLU A 1 3558 ? 204.634 203.982 262.411 1.00 9.08  ? 3558 GLU A CB    1 
ATOM   15128 C  CG    . GLU A 1 3558 ? 204.742 204.426 260.973 1.00 12.59 ? 3558 GLU A CG    1 
ATOM   15129 C  CD    . GLU A 1 3558 ? 205.919 203.799 260.256 1.00 23.28 ? 3558 GLU A CD    1 
ATOM   15130 O  OE1   . GLU A 1 3558 ? 206.408 202.745 260.718 1.00 19.86 ? 3558 GLU A OE1   1 
ATOM   15131 O  OE2   . GLU A 1 3558 ? 206.352 204.363 259.230 1.00 23.18 ? 3558 GLU A OE2   1 
ATOM   15132 N  N     . ARG A 1 3559 ? 201.628 203.460 263.408 1.00 7.36  ? 3559 ARG A N     1 
ATOM   15133 C  CA    . ARG A 1 3559 ? 200.238 203.137 263.107 1.00 5.65  ? 3559 ARG A CA    1 
ATOM   15134 C  C     . ARG A 1 3559 ? 199.295 204.224 263.605 1.00 6.32  ? 3559 ARG A C     1 
ATOM   15135 O  O     . ARG A 1 3559 ? 198.275 204.502 262.965 1.00 6.20  ? 3559 ARG A O     1 
ATOM   15136 C  CB    . ARG A 1 3559 ? 199.874 201.783 263.713 1.00 4.93  ? 3559 ARG A CB    1 
ATOM   15137 C  CG    . ARG A 1 3559 ? 200.564 200.612 263.039 1.00 4.91  ? 3559 ARG A CG    1 
ATOM   15138 C  CD    . ARG A 1 3559 ? 200.089 199.278 263.586 1.00 5.87  ? 3559 ARG A CD    1 
ATOM   15139 N  NE    . ARG A 1 3559 ? 200.336 199.150 265.016 1.00 8.35  ? 3559 ARG A NE    1 
ATOM   15140 C  CZ    . ARG A 1 3559 ? 201.217 198.316 265.553 1.00 9.09  ? 3559 ARG A CZ    1 
ATOM   15141 N  NH1   . ARG A 1 3559 ? 201.979 197.539 264.802 1.00 8.20  ? 3559 ARG A NH1   1 
ATOM   15142 N  NH2   . ARG A 1 3559 ? 201.339 198.266 266.875 1.00 10.16 ? 3559 ARG A NH2   1 
ATOM   15143 N  N     . LEU A 1 3560 ? 199.620 204.847 264.741 1.00 8.84  ? 3560 LEU A N     1 
ATOM   15144 C  CA    . LEU A 1 3560 ? 198.813 205.954 265.242 1.00 7.34  ? 3560 LEU A CA    1 
ATOM   15145 C  C     . LEU A 1 3560 ? 198.820 207.126 264.271 1.00 6.84  ? 3560 LEU A C     1 
ATOM   15146 O  O     . LEU A 1 3560 ? 197.779 207.744 264.023 1.00 10.63 ? 3560 LEU A O     1 
ATOM   15147 C  CB    . LEU A 1 3560 ? 199.324 206.389 266.615 1.00 11.81 ? 3560 LEU A CB    1 
ATOM   15148 C  CG    . LEU A 1 3560 ? 198.401 207.256 267.472 1.00 11.48 ? 3560 LEU A CG    1 
ATOM   15149 C  CD1   . LEU A 1 3560 ? 197.156 206.486 267.861 1.00 6.76  ? 3560 LEU A CD1   1 
ATOM   15150 C  CD2   . LEU A 1 3560 ? 199.135 207.752 268.704 1.00 16.65 ? 3560 LEU A CD2   1 
ATOM   15151 N  N     . ARG A 1 3561 ? 199.990 207.453 263.714 1.00 7.20  ? 3561 ARG A N     1 
ATOM   15152 C  CA    . ARG A 1 3561 ? 200.063 208.533 262.735 1.00 6.08  ? 3561 ARG A CA    1 
ATOM   15153 C  C     . ARG A 1 3561 ? 199.367 208.147 261.436 1.00 7.98  ? 3561 ARG A C     1 
ATOM   15154 O  O     . ARG A 1 3561 ? 198.735 208.991 260.791 1.00 10.14 ? 3561 ARG A O     1 
ATOM   15155 C  CB    . ARG A 1 3561 ? 201.522 208.910 262.475 1.00 8.03  ? 3561 ARG A CB    1 
ATOM   15156 C  CG    . ARG A 1 3561 ? 201.710 209.917 261.353 1.00 11.42 ? 3561 ARG A CG    1 
ATOM   15157 C  CD    . ARG A 1 3561 ? 203.172 210.281 261.164 1.00 15.34 ? 3561 ARG A CD    1 
ATOM   15158 N  NE    . ARG A 1 3561 ? 203.812 209.435 260.164 1.00 21.94 ? 3561 ARG A NE    1 
ATOM   15159 C  CZ    . ARG A 1 3561 ? 204.446 208.305 260.437 1.00 18.48 ? 3561 ARG A CZ    1 
ATOM   15160 N  NH1   . ARG A 1 3561 ? 204.570 207.864 261.677 1.00 18.53 ? 3561 ARG A NH1   1 
ATOM   15161 N  NH2   . ARG A 1 3561 ? 204.972 207.599 259.439 1.00 16.97 ? 3561 ARG A NH2   1 
ATOM   15162 N  N     . TRP A 1 3562 ? 199.466 206.875 261.040 1.00 7.73  ? 3562 TRP A N     1 
ATOM   15163 C  CA    . TRP A 1 3562 ? 198.802 206.423 259.822 1.00 5.92  ? 3562 TRP A CA    1 
ATOM   15164 C  C     . TRP A 1 3562 ? 197.295 206.617 259.915 1.00 6.99  ? 3562 TRP A C     1 
ATOM   15165 O  O     . TRP A 1 3562 ? 196.651 207.008 258.936 1.00 10.89 ? 3562 TRP A O     1 
ATOM   15166 C  CB    . TRP A 1 3562 ? 199.139 204.957 259.549 1.00 4.82  ? 3562 TRP A CB    1 
ATOM   15167 C  CG    . TRP A 1 3562 ? 200.527 204.738 259.042 1.00 3.37  ? 3562 TRP A CG    1 
ATOM   15168 C  CD1   . TRP A 1 3562 ? 201.373 205.680 258.536 1.00 3.72  ? 3562 TRP A CD1   1 
ATOM   15169 C  CD2   . TRP A 1 3562 ? 201.234 203.495 258.990 1.00 4.19  ? 3562 TRP A CD2   1 
ATOM   15170 N  NE1   . TRP A 1 3562 ? 202.563 205.101 258.174 1.00 4.59  ? 3562 TRP A NE1   1 
ATOM   15171 C  CE2   . TRP A 1 3562 ? 202.503 203.760 258.441 1.00 4.22  ? 3562 TRP A CE2   1 
ATOM   15172 C  CE3   . TRP A 1 3562 ? 200.918 202.183 259.356 1.00 3.11  ? 3562 TRP A CE3   1 
ATOM   15173 C  CZ2   . TRP A 1 3562 ? 203.454 202.761 258.246 1.00 2.30  ? 3562 TRP A CZ2   1 
ATOM   15174 C  CZ3   . TRP A 1 3562 ? 201.864 201.196 259.165 1.00 1.76  ? 3562 TRP A CZ3   1 
ATOM   15175 C  CH2   . TRP A 1 3562 ? 203.118 201.489 258.617 1.00 2.15  ? 3562 TRP A CH2   1 
ATOM   15176 N  N     . GLN A 1 3563 ? 196.718 206.353 261.088 1.00 8.43  ? 3563 GLN A N     1 
ATOM   15177 C  CA    . GLN A 1 3563 ? 195.295 206.604 261.285 1.00 6.83  ? 3563 GLN A CA    1 
ATOM   15178 C  C     . GLN A 1 3563 ? 194.971 208.085 261.132 1.00 6.47  ? 3563 GLN A C     1 
ATOM   15179 O  O     . GLN A 1 3563 ? 193.955 208.446 260.527 1.00 5.75  ? 3563 GLN A O     1 
ATOM   15180 C  CB    . GLN A 1 3563 ? 194.860 206.101 262.660 1.00 6.14  ? 3563 GLN A CB    1 
ATOM   15181 C  CG    . GLN A 1 3563 ? 194.235 204.722 262.644 1.00 12.68 ? 3563 GLN A CG    1 
ATOM   15182 C  CD    . GLN A 1 3563 ? 194.066 204.146 264.034 1.00 23.09 ? 3563 GLN A CD    1 
ATOM   15183 O  OE1   . GLN A 1 3563 ? 193.868 204.880 265.003 1.00 26.17 ? 3563 GLN A OE1   1 
ATOM   15184 N  NE2   . GLN A 1 3563 ? 194.146 202.824 264.140 1.00 25.82 ? 3563 GLN A NE2   1 
ATOM   15185 N  N     . ALA A 1 3564 ? 195.826 208.957 261.672 1.00 8.83  ? 3564 ALA A N     1 
ATOM   15186 C  CA    . ALA A 1 3564 ? 195.611 210.392 261.531 1.00 5.97  ? 3564 ALA A CA    1 
ATOM   15187 C  C     . ALA A 1 3564 ? 195.680 210.830 260.073 1.00 10.06 ? 3564 ALA A C     1 
ATOM   15188 O  O     . ALA A 1 3564 ? 195.061 211.830 259.694 1.00 13.24 ? 3564 ALA A O     1 
ATOM   15189 C  CB    . ALA A 1 3564 ? 196.632 211.160 262.367 1.00 4.41  ? 3564 ALA A CB    1 
ATOM   15190 N  N     . SER A 1 3565 ? 196.421 210.098 259.244 1.00 8.79  ? 3565 SER A N     1 
ATOM   15191 C  CA    . SER A 1 3565 ? 196.500 210.361 257.816 1.00 5.06  ? 3565 SER A CA    1 
ATOM   15192 C  C     . SER A 1 3565 ? 195.365 209.715 257.034 1.00 6.25  ? 3565 SER A C     1 
ATOM   15193 O  O     . SER A 1 3565 ? 195.475 209.581 255.809 1.00 9.36  ? 3565 SER A O     1 
ATOM   15194 C  CB    . SER A 1 3565 ? 197.849 209.892 257.267 1.00 8.86  ? 3565 SER A CB    1 
ATOM   15195 O  OG    . SER A 1 3565 ? 198.912 210.649 257.813 1.00 9.84  ? 3565 SER A OG    1 
ATOM   15196 N  N     . SER A 1 3566 ? 194.295 209.313 257.723 1.00 8.76  ? 3566 SER A N     1 
ATOM   15197 C  CA    . SER A 1 3566 ? 193.093 208.733 257.122 1.00 4.98  ? 3566 SER A CA    1 
ATOM   15198 C  C     . SER A 1 3566 ? 193.355 207.376 256.473 1.00 6.96  ? 3566 SER A C     1 
ATOM   15199 O  O     . SER A 1 3566 ? 192.692 207.012 255.502 1.00 12.94 ? 3566 SER A O     1 
ATOM   15200 C  CB    . SER A 1 3566 ? 192.450 209.688 256.109 1.00 7.34  ? 3566 SER A CB    1 
ATOM   15201 O  OG    . SER A 1 3566 ? 193.256 209.840 254.953 1.00 14.32 ? 3566 SER A OG    1 
ATOM   15202 N  N     . LEU A 1 3567 ? 194.311 206.617 256.995 1.00 5.84  ? 3567 LEU A N     1 
ATOM   15203 C  CA    . LEU A 1 3567 ? 194.481 205.242 256.540 1.00 5.35  ? 3567 LEU A CA    1 
ATOM   15204 C  C     . LEU A 1 3567 ? 193.423 204.353 257.187 1.00 8.28  ? 3567 LEU A C     1 
ATOM   15205 O  O     . LEU A 1 3567 ? 193.272 204.376 258.412 1.00 8.53  ? 3567 LEU A O     1 
ATOM   15206 C  CB    . LEU A 1 3567 ? 195.872 204.718 256.873 1.00 5.45  ? 3567 LEU A CB    1 
ATOM   15207 C  CG    . LEU A 1 3567 ? 196.178 203.312 256.349 1.00 3.99  ? 3567 LEU A CG    1 
ATOM   15208 C  CD1   . LEU A 1 3567 ? 196.540 203.352 254.872 1.00 3.37  ? 3567 LEU A CD1   1 
ATOM   15209 C  CD2   . LEU A 1 3567 ? 197.278 202.651 257.161 1.00 2.03  ? 3567 LEU A CD2   1 
ATOM   15210 N  N     . PRO A 1 3568 ? 192.677 203.572 256.406 1.00 5.04  ? 3568 PRO A N     1 
ATOM   15211 C  CA    . PRO A 1 3568 ? 191.631 202.726 256.990 1.00 4.15  ? 3568 PRO A CA    1 
ATOM   15212 C  C     . PRO A 1 3568 ? 192.194 201.746 258.009 1.00 7.98  ? 3568 PRO A C     1 
ATOM   15213 O  O     . PRO A 1 3568 ? 193.294 201.214 257.849 1.00 8.30  ? 3568 PRO A O     1 
ATOM   15214 C  CB    . PRO A 1 3568 ? 191.051 201.998 255.774 1.00 4.56  ? 3568 PRO A CB    1 
ATOM   15215 C  CG    . PRO A 1 3568 ? 191.351 202.893 254.626 1.00 4.72  ? 3568 PRO A CG    1 
ATOM   15216 C  CD    . PRO A 1 3568 ? 192.676 203.516 254.935 1.00 6.30  ? 3568 PRO A CD    1 
ATOM   15217 N  N     . ALA A 1 3569 ? 191.419 201.513 259.070 1.00 6.34  ? 3569 ALA A N     1 
ATOM   15218 C  CA    . ALA A 1 3569 ? 191.811 200.596 260.141 1.00 6.81  ? 3569 ALA A CA    1 
ATOM   15219 C  C     . ALA A 1 3569 ? 191.568 199.169 259.663 1.00 16.22 ? 3569 ALA A C     1 
ATOM   15220 O  O     . ALA A 1 3569 ? 190.578 198.517 260.002 1.00 23.37 ? 3569 ALA A O     1 
ATOM   15221 C  CB    . ALA A 1 3569 ? 191.049 200.904 261.423 1.00 9.26  ? 3569 ALA A CB    1 
ATOM   15222 N  N     . ASP A 1 3570 ? 192.504 198.682 258.851 1.00 10.40 ? 3570 ASP A N     1 
ATOM   15223 C  CA    . ASP A 1 3570 ? 192.398 197.374 258.226 1.00 6.54  ? 3570 ASP A CA    1 
ATOM   15224 C  C     . ASP A 1 3570 ? 193.794 196.780 258.115 1.00 5.75  ? 3570 ASP A C     1 
ATOM   15225 O  O     . ASP A 1 3570 ? 194.762 197.502 257.867 1.00 7.94  ? 3570 ASP A O     1 
ATOM   15226 C  CB    . ASP A 1 3570 ? 191.740 197.484 256.846 1.00 5.77  ? 3570 ASP A CB    1 
ATOM   15227 C  CG    . ASP A 1 3570 ? 191.652 196.156 256.133 1.00 8.40  ? 3570 ASP A CG    1 
ATOM   15228 O  OD1   . ASP A 1 3570 ? 191.222 195.169 256.764 1.00 14.26 ? 3570 ASP A OD1   1 
ATOM   15229 O  OD2   . ASP A 1 3570 ? 192.011 196.102 254.941 1.00 8.12  ? 3570 ASP A OD2   1 
ATOM   15230 N  N     . ASP A 1 3571 ? 193.892 195.462 258.305 1.00 3.97  ? 3571 ASP A N     1 
ATOM   15231 C  CA    . ASP A 1 3571 ? 195.197 194.808 258.283 1.00 5.34  ? 3571 ASP A CA    1 
ATOM   15232 C  C     . ASP A 1 3571 ? 195.851 194.909 256.911 1.00 3.73  ? 3571 ASP A C     1 
ATOM   15233 O  O     . ASP A 1 3571 ? 197.050 195.187 256.808 1.00 2.13  ? 3571 ASP A O     1 
ATOM   15234 C  CB    . ASP A 1 3571 ? 195.063 193.348 258.709 1.00 7.53  ? 3571 ASP A CB    1 
ATOM   15235 C  CG    . ASP A 1 3571 ? 195.147 193.173 260.209 1.00 14.52 ? 3571 ASP A CG    1 
ATOM   15236 O  OD1   . ASP A 1 3571 ? 195.293 194.189 260.919 1.00 10.68 ? 3571 ASP A OD1   1 
ATOM   15237 O  OD2   . ASP A 1 3571 ? 195.074 192.018 260.681 1.00 22.06 ? 3571 ASP A OD2   1 
ATOM   15238 N  N     . LEU A 1 3572 ? 195.081 194.686 255.844 1.00 3.63  ? 3572 LEU A N     1 
ATOM   15239 C  CA    . LEU A 1 3572 ? 195.637 194.810 254.501 1.00 2.53  ? 3572 LEU A CA    1 
ATOM   15240 C  C     . LEU A 1 3572 ? 196.050 196.249 254.208 1.00 1.91  ? 3572 LEU A C     1 
ATOM   15241 O  O     . LEU A 1 3572 ? 197.072 196.488 253.556 1.00 1.12  ? 3572 LEU A O     1 
ATOM   15242 C  CB    . LEU A 1 3572 ? 194.635 194.290 253.467 1.00 1.02  ? 3572 LEU A CB    1 
ATOM   15243 C  CG    . LEU A 1 3572 ? 195.081 194.158 252.006 1.00 1.27  ? 3572 LEU A CG    1 
ATOM   15244 C  CD1   . LEU A 1 3572 ? 194.308 193.054 251.321 1.00 1.25  ? 3572 LEU A CD1   1 
ATOM   15245 C  CD2   . LEU A 1 3572 ? 194.878 195.463 251.245 1.00 0.77  ? 3572 LEU A CD2   1 
ATOM   15246 N  N     . CYS A 1 3573 ? 195.266 197.220 254.679 1.00 1.82  ? 3573 CYS A N     1 
ATOM   15247 C  CA    . CYS A 1 3573 ? 195.658 198.618 254.531 1.00 1.94  ? 3573 CYS A CA    1 
ATOM   15248 C  C     . CYS A 1 3573 ? 196.923 198.924 255.325 1.00 1.20  ? 3573 CYS A C     1 
ATOM   15249 O  O     . CYS A 1 3573 ? 197.780 199.687 254.866 1.00 0.78  ? 3573 CYS A O     1 
ATOM   15250 C  CB    . CYS A 1 3573 ? 194.511 199.532 254.957 1.00 2.78  ? 3573 CYS A CB    1 
ATOM   15251 S  SG    . CYS A 1 3573 ? 193.142 199.585 253.779 1.00 14.26 ? 3573 CYS A SG    1 
ATOM   15252 N  N     . THR A 1 3574 ? 197.053 198.345 256.521 1.00 1.99  ? 3574 THR A N     1 
ATOM   15253 C  CA    . THR A 1 3574 ? 198.279 198.509 257.296 1.00 0.96  ? 3574 THR A CA    1 
ATOM   15254 C  C     . THR A 1 3574 ? 199.465 197.853 256.595 1.00 0.62  ? 3574 THR A C     1 
ATOM   15255 O  O     . THR A 1 3574 ? 200.575 198.396 256.601 1.00 1.00  ? 3574 THR A O     1 
ATOM   15256 C  CB    . THR A 1 3574 ? 198.092 197.932 258.699 1.00 0.77  ? 3574 THR A CB    1 
ATOM   15257 O  OG1   . THR A 1 3574 ? 196.963 198.555 259.321 1.00 7.14  ? 3574 THR A OG1   1 
ATOM   15258 C  CG2   . THR A 1 3574 ? 199.324 198.184 259.550 1.00 0.53  ? 3574 THR A CG2   1 
ATOM   15259 N  N     . GLU A 1 3575 ? 199.248 196.686 255.986 1.00 0.59  ? 3575 GLU A N     1 
ATOM   15260 C  CA    . GLU A 1 3575 ? 200.299 196.049 255.200 1.00 0.74  ? 3575 GLU A CA    1 
ATOM   15261 C  C     . GLU A 1 3575 ? 200.731 196.934 254.039 1.00 0.53  ? 3575 GLU A C     1 
ATOM   15262 O  O     . GLU A 1 3575 ? 201.923 197.022 253.722 1.00 0.54  ? 3575 GLU A O     1 
ATOM   15263 C  CB    . GLU A 1 3575 ? 199.823 194.692 254.683 1.00 0.77  ? 3575 GLU A CB    1 
ATOM   15264 C  CG    . GLU A 1 3575 ? 199.683 193.623 255.747 1.00 1.09  ? 3575 GLU A CG    1 
ATOM   15265 C  CD    . GLU A 1 3575 ? 198.958 192.386 255.247 1.00 3.16  ? 3575 GLU A CD    1 
ATOM   15266 O  OE1   . GLU A 1 3575 ? 198.484 192.392 254.093 1.00 3.90  ? 3575 GLU A OE1   1 
ATOM   15267 O  OE2   . GLU A 1 3575 ? 198.871 191.402 256.009 1.00 9.29  ? 3575 GLU A OE2   1 
ATOM   15268 N  N     . ASN A 1 3576 ? 199.771 197.588 253.384 1.00 0.43  ? 3576 ASN A N     1 
ATOM   15269 C  CA    . ASN A 1 3576 ? 200.094 198.494 252.289 1.00 0.33  ? 3576 ASN A CA    1 
ATOM   15270 C  C     . ASN A 1 3576 ? 200.914 199.683 252.772 1.00 0.36  ? 3576 ASN A C     1 
ATOM   15271 O  O     . ASN A 1 3576 ? 201.853 200.114 252.095 1.00 0.39  ? 3576 ASN A O     1 
ATOM   15272 C  CB    . ASN A 1 3576 ? 198.809 198.962 251.609 1.00 0.42  ? 3576 ASN A CB    1 
ATOM   15273 C  CG    . ASN A 1 3576 ? 198.130 197.857 250.832 1.00 0.26  ? 3576 ASN A CG    1 
ATOM   15274 O  OD1   . ASN A 1 3576 ? 198.595 196.723 250.820 1.00 0.67  ? 3576 ASN A OD1   1 
ATOM   15275 N  ND2   . ASN A 1 3576 ? 197.030 198.185 250.171 1.00 0.21  ? 3576 ASN A ND2   1 
ATOM   15276 N  N     . ALA A 1 3577 ? 200.572 200.227 253.943 1.00 0.37  ? 3577 ALA A N     1 
ATOM   15277 C  CA    . ALA A 1 3577 ? 201.328 201.346 254.493 1.00 0.29  ? 3577 ALA A CA    1 
ATOM   15278 C  C     . ALA A 1 3577 ? 202.777 200.958 254.761 1.00 0.46  ? 3577 ALA A C     1 
ATOM   15279 O  O     . ALA A 1 3577 ? 203.695 201.745 254.505 1.00 0.59  ? 3577 ALA A O     1 
ATOM   15280 C  CB    . ALA A 1 3577 ? 200.661 201.848 255.772 1.00 0.57  ? 3577 ALA A CB    1 
ATOM   15281 N  N     . ILE A 1 3578 ? 202.999 199.748 255.280 1.00 0.45  ? 3578 ILE A N     1 
ATOM   15282 C  CA    . ILE A 1 3578 ? 204.359 199.261 255.495 1.00 0.49  ? 3578 ILE A CA    1 
ATOM   15283 C  C     . ILE A 1 3578 ? 205.109 199.177 254.172 1.00 0.43  ? 3578 ILE A C     1 
ATOM   15284 O  O     . ILE A 1 3578 ? 206.288 199.543 254.084 1.00 0.50  ? 3578 ILE A O     1 
ATOM   15285 C  CB    . ILE A 1 3578 ? 204.325 197.902 256.218 1.00 0.79  ? 3578 ILE A CB    1 
ATOM   15286 C  CG1   . ILE A 1 3578 ? 203.634 198.041 257.574 1.00 0.56  ? 3578 ILE A CG1   1 
ATOM   15287 C  CG2   . ILE A 1 3578 ? 205.729 197.343 256.368 1.00 0.72  ? 3578 ILE A CG2   1 
ATOM   15288 C  CD1   . ILE A 1 3578 ? 203.453 196.739 258.306 1.00 1.22  ? 3578 ILE A CD1   1 
ATOM   15289 N  N     . MET A 1 3579 ? 204.439 198.693 253.126 1.00 0.31  ? 3579 MET A N     1 
ATOM   15290 C  CA    . MET A 1 3579 ? 205.045 198.652 251.801 1.00 0.24  ? 3579 MET A CA    1 
ATOM   15291 C  C     . MET A 1 3579 ? 205.363 200.048 251.285 1.00 0.24  ? 3579 MET A C     1 
ATOM   15292 O  O     . MET A 1 3579 ? 206.406 200.253 250.654 1.00 0.39  ? 3579 MET A O     1 
ATOM   15293 C  CB    . MET A 1 3579 ? 204.115 197.925 250.835 1.00 0.28  ? 3579 MET A CB    1 
ATOM   15294 C  CG    . MET A 1 3579 ? 203.926 196.465 251.163 1.00 0.25  ? 3579 MET A CG    1 
ATOM   15295 S  SD    . MET A 1 3579 ? 202.699 195.676 250.115 1.00 4.08  ? 3579 MET A SD    1 
ATOM   15296 C  CE    . MET A 1 3579 ? 202.560 194.077 250.907 1.00 0.36  ? 3579 MET A CE    1 
ATOM   15297 N  N     . LEU A 1 3580 ? 204.488 201.016 251.545 1.00 0.32  ? 3580 LEU A N     1 
ATOM   15298 C  CA    . LEU A 1 3580 ? 204.699 202.398 251.137 1.00 0.21  ? 3580 LEU A CA    1 
ATOM   15299 C  C     . LEU A 1 3580 ? 205.796 203.089 251.931 1.00 0.26  ? 3580 LEU A C     1 
ATOM   15300 O  O     . LEU A 1 3580 ? 206.176 204.212 251.583 1.00 1.01  ? 3580 LEU A O     1 
ATOM   15301 C  CB    . LEU A 1 3580 ? 203.394 203.187 251.260 1.00 0.31  ? 3580 LEU A CB    1 
ATOM   15302 C  CG    . LEU A 1 3580 ? 202.268 202.764 250.314 1.00 0.26  ? 3580 LEU A CG    1 
ATOM   15303 C  CD1   . LEU A 1 3580 ? 200.967 203.460 250.671 1.00 0.39  ? 3580 LEU A CD1   1 
ATOM   15304 C  CD2   . LEU A 1 3580 ? 202.651 203.046 248.874 1.00 0.20  ? 3580 LEU A CD2   1 
ATOM   15305 N  N     . LYS A 1 3581 ? 206.304 202.459 252.983 1.00 0.41  ? 3581 LYS A N     1 
ATOM   15306 C  CA    . LYS A 1 3581 ? 207.392 203.004 253.783 1.00 0.55  ? 3581 LYS A CA    1 
ATOM   15307 C  C     . LYS A 1 3581 ? 208.712 202.278 253.574 1.00 1.38  ? 3581 LYS A C     1 
ATOM   15308 O  O     . LYS A 1 3581 ? 209.762 202.922 253.543 1.00 5.00  ? 3581 LYS A O     1 
ATOM   15309 C  CB    . LYS A 1 3581 ? 207.010 202.962 255.271 1.00 0.85  ? 3581 LYS A CB    1 
ATOM   15310 C  CG    . LYS A 1 3581 ? 208.126 203.348 256.220 1.00 6.85  ? 3581 LYS A CG    1 
ATOM   15311 C  CD    . LYS A 1 3581 ? 208.121 202.469 257.458 1.00 13.46 ? 3581 LYS A CD    1 
ATOM   15312 C  CE    . LYS A 1 3581 ? 209.157 202.935 258.468 1.00 15.79 ? 3581 LYS A CE    1 
ATOM   15313 N  NZ    . LYS A 1 3581 ? 209.245 202.026 259.643 1.00 10.24 ? 3581 LYS A NZ    1 
ATOM   15314 N  N     . ARG A 1 3582 ? 208.686 200.955 253.410 1.00 1.84  ? 3582 ARG A N     1 
ATOM   15315 C  CA    . ARG A 1 3582 ? 209.897 200.149 253.293 1.00 2.32  ? 3582 ARG A CA    1 
ATOM   15316 C  C     . ARG A 1 3582 ? 210.212 199.756 251.854 1.00 1.10  ? 3582 ARG A C     1 
ATOM   15317 O  O     . ARG A 1 3582 ? 211.008 198.840 251.631 1.00 2.91  ? 3582 ARG A O     1 
ATOM   15318 C  CB    . ARG A 1 3582 ? 209.791 198.890 254.154 1.00 1.28  ? 3582 ARG A CB    1 
ATOM   15319 C  CG    . ARG A 1 3582 ? 209.597 199.130 255.633 1.00 1.41  ? 3582 ARG A CG    1 
ATOM   15320 C  CD    . ARG A 1 3582 ? 209.389 197.807 256.353 1.00 2.05  ? 3582 ARG A CD    1 
ATOM   15321 N  NE    . ARG A 1 3582 ? 209.285 197.949 257.801 1.00 7.44  ? 3582 ARG A NE    1 
ATOM   15322 C  CZ    . ARG A 1 3582 ? 210.261 198.373 258.593 1.00 5.77  ? 3582 ARG A CZ    1 
ATOM   15323 N  NH1   . ARG A 1 3582 ? 211.458 198.677 258.120 1.00 6.10  ? 3582 ARG A NH1   1 
ATOM   15324 N  NH2   . ARG A 1 3582 ? 210.032 198.485 259.898 1.00 4.92  ? 3582 ARG A NH2   1 
ATOM   15325 N  N     . PHE A 1 3583 ? 209.603 200.418 250.876 1.00 0.50  ? 3583 PHE A N     1 
ATOM   15326 C  CA    . PHE A 1 3583 ? 209.799 200.037 249.484 1.00 0.82  ? 3583 PHE A CA    1 
ATOM   15327 C  C     . PHE A 1 3583 ? 211.238 200.281 249.047 1.00 0.71  ? 3583 PHE A C     1 
ATOM   15328 O  O     . PHE A 1 3583 ? 211.898 201.214 249.512 1.00 1.00  ? 3583 PHE A O     1 
ATOM   15329 C  CB    . PHE A 1 3583 ? 208.848 200.819 248.577 1.00 0.31  ? 3583 PHE A CB    1 
ATOM   15330 C  CG    . PHE A 1 3583 ? 209.085 202.300 248.590 1.00 0.47  ? 3583 PHE A CG    1 
ATOM   15331 C  CD1   . PHE A 1 3583 ? 209.964 202.887 247.693 1.00 0.44  ? 3583 PHE A CD1   1 
ATOM   15332 C  CD2   . PHE A 1 3583 ? 208.437 203.109 249.508 1.00 0.41  ? 3583 PHE A CD2   1 
ATOM   15333 C  CE1   . PHE A 1 3583 ? 210.190 204.242 247.712 1.00 0.26  ? 3583 PHE A CE1   1 
ATOM   15334 C  CE2   . PHE A 1 3583 ? 208.655 204.466 249.527 1.00 0.41  ? 3583 PHE A CE2   1 
ATOM   15335 C  CZ    . PHE A 1 3583 ? 209.533 205.033 248.630 1.00 0.41  ? 3583 PHE A CZ    1 
ATOM   15336 N  N     . ASN A 1 3584 ? 211.723 199.429 248.148 1.00 1.16  ? 3584 ASN A N     1 
ATOM   15337 C  CA    . ASN A 1 3584 ? 212.969 199.685 247.436 1.00 2.34  ? 3584 ASN A CA    1 
ATOM   15338 C  C     . ASN A 1 3584 ? 212.687 200.238 246.044 1.00 1.67  ? 3584 ASN A C     1 
ATOM   15339 O  O     . ASN A 1 3584 ? 213.126 201.341 245.707 1.00 12.04 ? 3584 ASN A O     1 
ATOM   15340 C  CB    . ASN A 1 3584 ? 213.814 198.408 247.353 1.00 2.18  ? 3584 ASN A CB    1 
ATOM   15341 C  CG    . ASN A 1 3584 ? 214.276 197.929 248.710 1.00 4.13  ? 3584 ASN A CG    1 
ATOM   15342 O  OD1   . ASN A 1 3584 ? 214.573 198.729 249.597 1.00 11.52 ? 3584 ASN A OD1   1 
ATOM   15343 N  ND2   . ASN A 1 3584 ? 214.345 196.616 248.882 1.00 1.60  ? 3584 ASN A ND2   1 
ATOM   15344 N  N     . ARG A 1 3585 ? 211.950 199.490 245.233 1.00 0.67  ? 3585 ARG A N     1 
ATOM   15345 C  CA    . ARG A 1 3585 ? 211.403 200.035 244.003 1.00 0.56  ? 3585 ARG A CA    1 
ATOM   15346 C  C     . ARG A 1 3585 ? 210.250 200.973 244.333 1.00 0.33  ? 3585 ARG A C     1 
ATOM   15347 O  O     . ARG A 1 3585 ? 209.549 200.798 245.332 1.00 1.09  ? 3585 ARG A O     1 
ATOM   15348 C  CB    . ARG A 1 3585 ? 210.929 198.918 243.074 1.00 0.76  ? 3585 ARG A CB    1 
ATOM   15349 C  CG    . ARG A 1 3585 ? 212.049 198.085 242.476 1.00 0.92  ? 3585 ARG A CG    1 
ATOM   15350 C  CD    . ARG A 1 3585 ? 211.487 196.949 241.643 1.00 1.15  ? 3585 ARG A CD    1 
ATOM   15351 N  NE    . ARG A 1 3585 ? 210.691 196.031 242.445 1.00 0.36  ? 3585 ARG A NE    1 
ATOM   15352 C  CZ    . ARG A 1 3585 ? 210.035 194.986 241.961 1.00 0.22  ? 3585 ARG A CZ    1 
ATOM   15353 N  NH1   . ARG A 1 3585 ? 210.030 194.713 240.668 1.00 0.49  ? 3585 ARG A NH1   1 
ATOM   15354 N  NH2   . ARG A 1 3585 ? 209.359 194.201 242.794 1.00 0.36  ? 3585 ARG A NH2   1 
ATOM   15355 N  N     . TYR A 1 3586 ? 210.065 201.979 243.488 1.00 0.22  ? 3586 TYR A N     1 
ATOM   15356 C  CA    . TYR A 1 3586 ? 209.058 202.989 243.768 1.00 0.20  ? 3586 TYR A CA    1 
ATOM   15357 C  C     . TYR A 1 3586 ? 207.662 202.379 243.690 1.00 0.15  ? 3586 TYR A C     1 
ATOM   15358 O  O     . TYR A 1 3586 ? 207.396 201.538 242.825 1.00 0.16  ? 3586 TYR A O     1 
ATOM   15359 C  CB    . TYR A 1 3586 ? 209.187 204.162 242.796 1.00 0.14  ? 3586 TYR A CB    1 
ATOM   15360 C  CG    . TYR A 1 3586 ? 210.419 205.003 243.035 1.00 0.16  ? 3586 TYR A CG    1 
ATOM   15361 C  CD1   . TYR A 1 3586 ? 210.554 205.753 244.194 1.00 0.15  ? 3586 TYR A CD1   1 
ATOM   15362 C  CD2   . TYR A 1 3586 ? 211.447 205.050 242.100 1.00 0.34  ? 3586 TYR A CD2   1 
ATOM   15363 C  CE1   . TYR A 1 3586 ? 211.676 206.524 244.417 1.00 0.21  ? 3586 TYR A CE1   1 
ATOM   15364 C  CE2   . TYR A 1 3586 ? 212.571 205.819 242.315 1.00 0.28  ? 3586 TYR A CE2   1 
ATOM   15365 C  CZ    . TYR A 1 3586 ? 212.679 206.555 243.476 1.00 0.26  ? 3586 TYR A CZ    1 
ATOM   15366 O  OH    . TYR A 1 3586 ? 213.798 207.323 243.697 1.00 0.33  ? 3586 TYR A OH    1 
ATOM   15367 N  N     . PRO A 1 3587 ? 206.752 202.772 244.578 1.00 0.26  ? 3587 PRO A N     1 
ATOM   15368 C  CA    . PRO A 1 3587 ? 205.447 202.107 244.646 1.00 0.15  ? 3587 PRO A CA    1 
ATOM   15369 C  C     . PRO A 1 3587 ? 204.503 202.539 243.536 1.00 0.11  ? 3587 PRO A C     1 
ATOM   15370 O  O     . PRO A 1 3587 ? 204.391 203.721 243.204 1.00 0.10  ? 3587 PRO A O     1 
ATOM   15371 C  CB    . PRO A 1 3587 ? 204.905 202.539 246.017 1.00 0.12  ? 3587 PRO A CB    1 
ATOM   15372 C  CG    . PRO A 1 3587 ? 206.085 203.115 246.747 1.00 0.18  ? 3587 PRO A CG    1 
ATOM   15373 C  CD    . PRO A 1 3587 ? 206.933 203.718 245.686 1.00 0.09  ? 3587 PRO A CD    1 
ATOM   15374 N  N     . LEU A 1 3588 ? 203.820 201.556 242.960 1.00 0.17  ? 3588 LEU A N     1 
ATOM   15375 C  CA    . LEU A 1 3588 ? 202.664 201.791 242.107 1.00 0.16  ? 3588 LEU A CA    1 
ATOM   15376 C  C     . LEU A 1 3588 ? 201.420 201.450 242.916 1.00 0.11  ? 3588 LEU A C     1 
ATOM   15377 O  O     . LEU A 1 3588 ? 201.254 200.308 243.355 1.00 0.09  ? 3588 LEU A O     1 
ATOM   15378 C  CB    . LEU A 1 3588 ? 202.738 200.954 240.829 1.00 0.17  ? 3588 LEU A CB    1 
ATOM   15379 C  CG    . LEU A 1 3588 ? 201.900 201.400 239.625 1.00 0.21  ? 3588 LEU A CG    1 
ATOM   15380 C  CD1   . LEU A 1 3588 ? 202.451 200.793 238.347 1.00 0.26  ? 3588 LEU A CD1   1 
ATOM   15381 C  CD2   . LEU A 1 3588 ? 200.425 201.041 239.787 1.00 0.12  ? 3588 LEU A CD2   1 
ATOM   15382 N  N     . ILE A 1 3589 ? 200.551 202.436 243.112 1.00 0.21  ? 3589 ILE A N     1 
ATOM   15383 C  CA    . ILE A 1 3589 ? 199.397 202.306 243.993 1.00 0.30  ? 3589 ILE A CA    1 
ATOM   15384 C  C     . ILE A 1 3589 ? 198.154 202.045 243.157 1.00 0.27  ? 3589 ILE A C     1 
ATOM   15385 O  O     . ILE A 1 3589 ? 197.872 202.776 242.201 1.00 0.40  ? 3589 ILE A O     1 
ATOM   15386 C  CB    . ILE A 1 3589 ? 199.220 203.561 244.864 1.00 0.30  ? 3589 ILE A CB    1 
ATOM   15387 C  CG1   . ILE A 1 3589 ? 200.438 203.760 245.765 1.00 0.23  ? 3589 ILE A CG1   1 
ATOM   15388 C  CG2   . ILE A 1 3589 ? 197.947 203.465 245.683 1.00 0.37  ? 3589 ILE A CG2   1 
ATOM   15389 C  CD1   . ILE A 1 3589 ? 200.505 205.126 246.402 1.00 2.94  ? 3589 ILE A CD1   1 
ATOM   15390 N  N     . ILE A 1 3590 ? 197.416 201.002 243.514 1.00 0.38  ? 3590 ILE A N     1 
ATOM   15391 C  CA    . ILE A 1 3590 ? 196.131 200.688 242.903 1.00 0.77  ? 3590 ILE A CA    1 
ATOM   15392 C  C     . ILE A 1 3590 ? 195.071 200.890 243.978 1.00 1.48  ? 3590 ILE A C     1 
ATOM   15393 O  O     . ILE A 1 3590 ? 194.936 200.073 244.894 1.00 1.67  ? 3590 ILE A O     1 
ATOM   15394 C  CB    . ILE A 1 3590 ? 196.096 199.265 242.336 1.00 0.61  ? 3590 ILE A CB    1 
ATOM   15395 C  CG1   . ILE A 1 3590 ? 197.205 199.077 241.300 1.00 0.43  ? 3590 ILE A CG1   1 
ATOM   15396 C  CG2   . ILE A 1 3590 ? 194.734 198.968 241.734 1.00 1.80  ? 3590 ILE A CG2   1 
ATOM   15397 C  CD1   . ILE A 1 3590 ? 197.328 197.670 240.787 1.00 0.41  ? 3590 ILE A CD1   1 
ATOM   15398 N  N     . ASP A 1 3591 ? 194.317 201.983 243.878 1.00 1.68  ? 3591 ASP A N     1 
ATOM   15399 C  CA    . ASP A 1 3591 ? 193.242 202.274 244.824 1.00 3.20  ? 3591 ASP A CA    1 
ATOM   15400 C  C     . ASP A 1 3591 ? 192.039 202.830 244.079 1.00 3.31  ? 3591 ASP A C     1 
ATOM   15401 O  O     . ASP A 1 3591 ? 191.963 204.033 243.801 1.00 4.03  ? 3591 ASP A O     1 
ATOM   15402 C  CB    . ASP A 1 3591 ? 193.696 203.248 245.909 1.00 3.82  ? 3591 ASP A CB    1 
ATOM   15403 C  CG    . ASP A 1 3591 ? 192.701 203.349 247.047 1.00 8.52  ? 3591 ASP A CG    1 
ATOM   15404 O  OD1   . ASP A 1 3591 ? 191.804 202.483 247.129 1.00 10.22 ? 3591 ASP A OD1   1 
ATOM   15405 O  OD2   . ASP A 1 3591 ? 192.803 204.295 247.852 1.00 12.06 ? 3591 ASP A OD2   1 
ATOM   15406 N  N     . PRO A 1 3592 ? 191.075 201.975 243.735 1.00 3.19  ? 3592 PRO A N     1 
ATOM   15407 C  CA    . PRO A 1 3592 ? 189.846 202.482 243.104 1.00 4.75  ? 3592 PRO A CA    1 
ATOM   15408 C  C     . PRO A 1 3592 ? 189.067 203.449 243.980 1.00 6.01  ? 3592 PRO A C     1 
ATOM   15409 O  O     . PRO A 1 3592 ? 188.457 204.389 243.458 1.00 7.90  ? 3592 PRO A O     1 
ATOM   15410 C  CB    . PRO A 1 3592 ? 189.043 201.204 242.816 1.00 1.94  ? 3592 PRO A CB    1 
ATOM   15411 C  CG    . PRO A 1 3592 ? 189.642 200.153 243.684 1.00 3.70  ? 3592 PRO A CG    1 
ATOM   15412 C  CD    . PRO A 1 3592 ? 191.078 200.511 243.869 1.00 3.69  ? 3592 PRO A CD    1 
ATOM   15413 N  N     . SER A 1 3593 ? 189.073 203.250 245.299 1.00 6.03  ? 3593 SER A N     1 
ATOM   15414 C  CA    . SER A 1 3593 ? 188.292 204.114 246.179 1.00 9.42  ? 3593 SER A CA    1 
ATOM   15415 C  C     . SER A 1 3593 ? 188.952 205.477 246.358 1.00 10.19 ? 3593 SER A C     1 
ATOM   15416 O  O     . SER A 1 3593 ? 188.261 206.500 246.432 1.00 13.39 ? 3593 SER A O     1 
ATOM   15417 C  CB    . SER A 1 3593 ? 188.088 203.433 247.527 1.00 10.86 ? 3593 SER A CB    1 
ATOM   15418 O  OG    . SER A 1 3593 ? 189.260 203.527 248.317 1.00 10.22 ? 3593 SER A OG    1 
ATOM   15419 N  N     . GLY A 1 3594 ? 190.280 205.513 246.448 1.00 11.32 ? 3594 GLY A N     1 
ATOM   15420 C  CA    . GLY A 1 3594 ? 191.011 206.759 246.512 1.00 6.74  ? 3594 GLY A CA    1 
ATOM   15421 C  C     . GLY A 1 3594 ? 191.530 207.169 247.875 1.00 8.89  ? 3594 GLY A C     1 
ATOM   15422 O  O     . GLY A 1 3594 ? 192.089 208.266 247.992 1.00 11.12 ? 3594 GLY A O     1 
ATOM   15423 N  N     . GLN A 1 3595 ? 191.370 206.339 248.912 1.00 12.82 ? 3595 GLN A N     1 
ATOM   15424 C  CA    . GLN A 1 3595 ? 191.935 206.698 250.211 1.00 8.79  ? 3595 GLN A CA    1 
ATOM   15425 C  C     . GLN A 1 3595 ? 193.456 206.636 250.210 1.00 6.60  ? 3595 GLN A C     1 
ATOM   15426 O  O     . GLN A 1 3595 ? 194.101 207.391 250.944 1.00 8.68  ? 3595 GLN A O     1 
ATOM   15427 C  CB    . GLN A 1 3595 ? 191.385 205.806 251.331 1.00 11.35 ? 3595 GLN A CB    1 
ATOM   15428 C  CG    . GLN A 1 3595 ? 189.942 206.078 251.725 1.00 11.12 ? 3595 GLN A CG    1 
ATOM   15429 C  CD    . GLN A 1 3595 ? 188.948 205.674 250.670 1.00 20.16 ? 3595 GLN A CD    1 
ATOM   15430 O  OE1   . GLN A 1 3595 ? 188.858 204.507 250.293 1.00 27.60 ? 3595 GLN A OE1   1 
ATOM   15431 N  NE2   . GLN A 1 3595 ? 188.225 206.653 250.148 1.00 21.28 ? 3595 GLN A NE2   1 
ATOM   15432 N  N     . ALA A 1 3596 ? 194.044 205.739 249.416 1.00 7.64  ? 3596 ALA A N     1 
ATOM   15433 C  CA    . ALA A 1 3596 ? 195.500 205.657 249.354 1.00 4.09  ? 3596 ALA A CA    1 
ATOM   15434 C  C     . ALA A 1 3596 ? 196.101 206.949 248.819 1.00 4.17  ? 3596 ALA A C     1 
ATOM   15435 O  O     . ALA A 1 3596 ? 197.134 207.414 249.316 1.00 5.03  ? 3596 ALA A O     1 
ATOM   15436 C  CB    . ALA A 1 3596 ? 195.926 204.472 248.492 1.00 2.17  ? 3596 ALA A CB    1 
ATOM   15437 N  N     . THR A 1 3597 ? 195.470 207.540 247.803 1.00 5.65  ? 3597 THR A N     1 
ATOM   15438 C  CA    . THR A 1 3597 ? 195.921 208.832 247.299 1.00 6.72  ? 3597 THR A CA    1 
ATOM   15439 C  C     . THR A 1 3597 ? 195.867 209.889 248.392 1.00 7.31  ? 3597 THR A C     1 
ATOM   15440 O  O     . THR A 1 3597 ? 196.811 210.666 248.561 1.00 10.67 ? 3597 THR A O     1 
ATOM   15441 C  CB    . THR A 1 3597 ? 195.069 209.254 246.102 1.00 10.94 ? 3597 THR A CB    1 
ATOM   15442 O  OG1   . THR A 1 3597 ? 195.189 208.279 245.060 1.00 15.51 ? 3597 THR A OG1   1 
ATOM   15443 C  CG2   . THR A 1 3597 ? 195.512 210.609 245.575 1.00 11.43 ? 3597 THR A CG2   1 
ATOM   15444 N  N     . GLU A 1 3598 ? 194.771 209.922 249.152 1.00 8.07  ? 3598 GLU A N     1 
ATOM   15445 C  CA    . GLU A 1 3598 ? 194.673 210.856 250.267 1.00 6.12  ? 3598 GLU A CA    1 
ATOM   15446 C  C     . GLU A 1 3598 ? 195.711 210.551 251.339 1.00 7.43  ? 3598 GLU A C     1 
ATOM   15447 O  O     . GLU A 1 3598 ? 196.367 211.462 251.855 1.00 10.30 ? 3598 GLU A O     1 
ATOM   15448 C  CB    . GLU A 1 3598 ? 193.259 210.822 250.851 1.00 7.69  ? 3598 GLU A CB    1 
ATOM   15449 C  CG    . GLU A 1 3598 ? 192.903 212.000 251.750 1.00 14.84 ? 3598 GLU A CG    1 
ATOM   15450 C  CD    . GLU A 1 3598 ? 193.466 213.326 251.266 1.00 25.95 ? 3598 GLU A CD    1 
ATOM   15451 O  OE1   . GLU A 1 3598 ? 193.386 213.617 250.054 1.00 21.35 ? 3598 GLU A OE1   1 
ATOM   15452 O  OE2   . GLU A 1 3598 ? 193.991 214.084 252.108 1.00 22.59 ? 3598 GLU A OE2   1 
ATOM   15453 N  N     . PHE A 1 3599 ? 195.900 209.268 251.659 1.00 7.27  ? 3599 PHE A N     1 
ATOM   15454 C  CA    . PHE A 1 3599 ? 196.859 208.883 252.692 1.00 4.25  ? 3599 PHE A CA    1 
ATOM   15455 C  C     . PHE A 1 3599 ? 198.273 209.314 252.326 1.00 5.18  ? 3599 PHE A C     1 
ATOM   15456 O  O     . PHE A 1 3599 ? 199.027 209.787 253.185 1.00 5.79  ? 3599 PHE A O     1 
ATOM   15457 C  CB    . PHE A 1 3599 ? 196.794 207.371 252.918 1.00 4.26  ? 3599 PHE A CB    1 
ATOM   15458 C  CG    . PHE A 1 3599 ? 197.941 206.821 253.713 1.00 4.30  ? 3599 PHE A CG    1 
ATOM   15459 C  CD1   . PHE A 1 3599 ? 197.988 206.978 255.087 1.00 4.12  ? 3599 PHE A CD1   1 
ATOM   15460 C  CD2   . PHE A 1 3599 ? 198.971 206.138 253.083 1.00 2.21  ? 3599 PHE A CD2   1 
ATOM   15461 C  CE1   . PHE A 1 3599 ? 199.045 206.468 255.818 1.00 4.70  ? 3599 PHE A CE1   1 
ATOM   15462 C  CE2   . PHE A 1 3599 ? 200.026 205.628 253.808 1.00 1.12  ? 3599 PHE A CE2   1 
ATOM   15463 C  CZ    . PHE A 1 3599 ? 200.064 205.791 255.175 1.00 2.26  ? 3599 PHE A CZ    1 
ATOM   15464 N  N     . ILE A 1 3600 ? 198.653 209.153 251.058 1.00 4.40  ? 3600 ILE A N     1 
ATOM   15465 C  CA    . ILE A 1 3600 ? 199.978 209.573 250.619 1.00 4.31  ? 3600 ILE A CA    1 
ATOM   15466 C  C     . ILE A 1 3600 ? 200.132 211.084 250.748 1.00 6.18  ? 3600 ILE A C     1 
ATOM   15467 O  O     . ILE A 1 3600 ? 201.189 211.581 251.153 1.00 7.71  ? 3600 ILE A O     1 
ATOM   15468 C  CB    . ILE A 1 3600 ? 200.237 209.087 249.180 1.00 5.52  ? 3600 ILE A CB    1 
ATOM   15469 C  CG1   . ILE A 1 3600 ? 200.432 207.571 249.169 1.00 4.45  ? 3600 ILE A CG1   1 
ATOM   15470 C  CG2   . ILE A 1 3600 ? 201.453 209.773 248.586 1.00 2.21  ? 3600 ILE A CG2   1 
ATOM   15471 C  CD1   . ILE A 1 3600 ? 201.559 207.097 250.057 1.00 2.37  ? 3600 ILE A CD1   1 
ATOM   15472 N  N     . MET A 1 3601 ? 199.087 211.840 250.401 1.00 7.60  ? 3601 MET A N     1 
ATOM   15473 C  CA    . MET A 1 3601 ? 199.158 213.292 250.527 1.00 5.84  ? 3601 MET A CA    1 
ATOM   15474 C  C     . MET A 1 3601 ? 199.131 213.742 251.984 1.00 7.28  ? 3601 MET A C     1 
ATOM   15475 O  O     . MET A 1 3601 ? 199.793 214.723 252.339 1.00 14.88 ? 3601 MET A O     1 
ATOM   15476 C  CB    . MET A 1 3601 ? 198.036 213.949 249.727 1.00 5.98  ? 3601 MET A CB    1 
ATOM   15477 C  CG    . MET A 1 3601 ? 197.992 213.503 248.280 1.00 7.84  ? 3601 MET A CG    1 
ATOM   15478 S  SD    . MET A 1 3601 ? 199.360 214.183 247.317 1.00 21.30 ? 3601 MET A SD    1 
ATOM   15479 C  CE    . MET A 1 3601 ? 198.961 215.927 247.337 1.00 7.04  ? 3601 MET A CE    1 
ATOM   15480 N  N     . ASN A 1 3602 ? 198.373 213.053 252.846 1.00 9.78  ? 3602 ASN A N     1 
ATOM   15481 C  CA    . ASN A 1 3602 ? 198.423 213.386 254.267 1.00 6.64  ? 3602 ASN A CA    1 
ATOM   15482 C  C     . ASN A 1 3602 ? 199.807 213.115 254.844 1.00 7.14  ? 3602 ASN A C     1 
ATOM   15483 O  O     . ASN A 1 3602 ? 200.320 213.906 255.642 1.00 9.89  ? 3602 ASN A O     1 
ATOM   15484 C  CB    . ASN A 1 3602 ? 197.371 212.607 255.061 1.00 7.54  ? 3602 ASN A CB    1 
ATOM   15485 C  CG    . ASN A 1 3602 ? 195.948 212.947 254.666 1.00 12.53 ? 3602 ASN A CG    1 
ATOM   15486 O  OD1   . ASN A 1 3602 ? 195.217 212.107 254.142 1.00 19.00 ? 3602 ASN A OD1   1 
ATOM   15487 N  ND2   . ASN A 1 3602 ? 195.543 214.179 254.924 1.00 12.34 ? 3602 ASN A ND2   1 
ATOM   15488 N  N     . GLU A 1 3603 ? 200.428 212.004 254.443 1.00 7.68  ? 3603 GLU A N     1 
ATOM   15489 C  CA    . GLU A 1 3603 ? 201.691 211.597 255.047 1.00 7.25  ? 3603 GLU A CA    1 
ATOM   15490 C  C     . GLU A 1 3603 ? 202.846 212.496 254.623 1.00 7.55  ? 3603 GLU A C     1 
ATOM   15491 O  O     . GLU A 1 3603 ? 203.895 212.497 255.278 1.00 6.66  ? 3603 GLU A O     1 
ATOM   15492 C  CB    . GLU A 1 3603 ? 202.002 210.146 254.679 1.00 5.28  ? 3603 GLU A CB    1 
ATOM   15493 C  CG    . GLU A 1 3603 ? 201.422 209.124 255.634 1.00 3.68  ? 3603 GLU A CG    1 
ATOM   15494 C  CD    . GLU A 1 3603 ? 202.042 209.185 257.013 1.00 12.75 ? 3603 GLU A CD    1 
ATOM   15495 O  OE1   . GLU A 1 3603 ? 203.286 209.164 257.113 1.00 11.51 ? 3603 GLU A OE1   1 
ATOM   15496 O  OE2   . GLU A 1 3603 ? 201.282 209.262 258.001 1.00 15.42 ? 3603 GLU A OE2   1 
ATOM   15497 N  N     . TYR A 1 3604 ? 202.683 213.264 253.545 1.00 9.16  ? 3604 TYR A N     1 
ATOM   15498 C  CA    . TYR A 1 3604 ? 203.795 214.009 252.970 1.00 6.54  ? 3604 TYR A CA    1 
ATOM   15499 C  C     . TYR A 1 3604 ? 203.514 215.503 252.813 1.00 10.80 ? 3604 TYR A C     1 
ATOM   15500 O  O     . TYR A 1 3604 ? 204.153 216.154 251.981 1.00 13.95 ? 3604 TYR A O     1 
ATOM   15501 C  CB    . TYR A 1 3604 ? 204.192 213.403 251.622 1.00 6.79  ? 3604 TYR A CB    1 
ATOM   15502 C  CG    . TYR A 1 3604 ? 204.926 212.083 251.725 1.00 7.51  ? 3604 TYR A CG    1 
ATOM   15503 C  CD1   . TYR A 1 3604 ? 204.232 210.884 251.823 1.00 6.48  ? 3604 TYR A CD1   1 
ATOM   15504 C  CD2   . TYR A 1 3604 ? 206.312 212.036 251.728 1.00 6.05  ? 3604 TYR A CD2   1 
ATOM   15505 C  CE1   . TYR A 1 3604 ? 204.899 209.677 251.917 1.00 4.60  ? 3604 TYR A CE1   1 
ATOM   15506 C  CE2   . TYR A 1 3604 ? 206.987 210.837 251.820 1.00 6.12  ? 3604 TYR A CE2   1 
ATOM   15507 C  CZ    . TYR A 1 3604 ? 206.277 209.660 251.915 1.00 5.23  ? 3604 TYR A CZ    1 
ATOM   15508 O  OH    . TYR A 1 3604 ? 206.951 208.466 252.009 1.00 8.84  ? 3604 TYR A OH    1 
ATOM   15509 N  N     . LYS A 1 3605 ? 202.582 216.071 253.588 1.00 14.46 ? 3605 LYS A N     1 
ATOM   15510 C  CA    . LYS A 1 3605 ? 202.429 217.525 253.559 1.00 11.31 ? 3605 LYS A CA    1 
ATOM   15511 C  C     . LYS A 1 3605 ? 203.672 218.231 254.083 1.00 14.07 ? 3605 LYS A C     1 
ATOM   15512 O  O     . LYS A 1 3605 ? 204.109 219.234 253.506 1.00 22.45 ? 3605 LYS A O     1 
ATOM   15513 C  CB    . LYS A 1 3605 ? 201.207 217.991 254.351 1.00 10.48 ? 3605 LYS A CB    1 
ATOM   15514 C  CG    . LYS A 1 3605 ? 199.854 217.595 253.811 1.00 15.58 ? 3605 LYS A CG    1 
ATOM   15515 C  CD    . LYS A 1 3605 ? 198.767 218.167 254.714 1.00 21.10 ? 3605 LYS A CD    1 
ATOM   15516 C  CE    . LYS A 1 3605 ? 197.376 217.891 254.182 1.00 20.67 ? 3605 LYS A CE    1 
ATOM   15517 N  NZ    . LYS A 1 3605 ? 197.059 216.450 254.211 1.00 17.24 ? 3605 LYS A NZ    1 
ATOM   15518 N  N     . ASP A 1 3606 ? 204.253 217.733 255.179 1.00 10.48 ? 3606 ASP A N     1 
ATOM   15519 C  CA    . ASP A 1 3606 ? 205.406 218.407 255.762 1.00 14.66 ? 3606 ASP A CA    1 
ATOM   15520 C  C     . ASP A 1 3606 ? 206.593 218.439 254.812 1.00 15.64 ? 3606 ASP A C     1 
ATOM   15521 O  O     . ASP A 1 3606 ? 207.459 219.309 254.948 1.00 22.34 ? 3606 ASP A O     1 
ATOM   15522 C  CB    . ASP A 1 3606 ? 205.811 217.740 257.080 1.00 21.52 ? 3606 ASP A CB    1 
ATOM   15523 C  CG    . ASP A 1 3606 ? 206.143 216.267 256.919 1.00 25.50 ? 3606 ASP A CG    1 
ATOM   15524 O  OD1   . ASP A 1 3606 ? 206.021 215.739 255.794 1.00 17.37 ? 3606 ASP A OD1   1 
ATOM   15525 O  OD2   . ASP A 1 3606 ? 206.535 215.637 257.923 1.00 28.83 ? 3606 ASP A OD2   1 
ATOM   15526 N  N     . ARG A 1 3607 ? 206.644 217.519 253.853 1.00 17.84 ? 3607 ARG A N     1 
ATOM   15527 C  CA    . ARG A 1 3607 ? 207.694 217.482 252.848 1.00 9.91  ? 3607 ARG A CA    1 
ATOM   15528 C  C     . ARG A 1 3607 ? 207.248 218.077 251.517 1.00 13.24 ? 3607 ARG A C     1 
ATOM   15529 O  O     . ARG A 1 3607 ? 207.972 217.958 250.525 1.00 17.11 ? 3607 ARG A O     1 
ATOM   15530 C  CB    . ARG A 1 3607 ? 208.181 216.046 252.657 1.00 10.32 ? 3607 ARG A CB    1 
ATOM   15531 C  CG    . ARG A 1 3607 ? 209.164 215.597 253.726 1.00 9.95  ? 3607 ARG A CG    1 
ATOM   15532 C  CD    . ARG A 1 3607 ? 209.407 214.100 253.690 1.00 15.08 ? 3607 ARG A CD    1 
ATOM   15533 N  NE    . ARG A 1 3607 ? 208.360 213.338 254.358 1.00 21.26 ? 3607 ARG A NE    1 
ATOM   15534 C  CZ    . ARG A 1 3607 ? 208.420 212.034 254.594 1.00 20.02 ? 3607 ARG A CZ    1 
ATOM   15535 N  NH1   . ARG A 1 3607 ? 209.474 211.315 254.243 1.00 18.42 ? 3607 ARG A NH1   1 
ATOM   15536 N  NH2   . ARG A 1 3607 ? 207.396 211.435 255.194 1.00 11.78 ? 3607 ARG A NH2   1 
ATOM   15537 N  N     . LYS A 1 3608 ? 206.074 218.712 251.480 1.00 13.34 ? 3608 LYS A N     1 
ATOM   15538 C  CA    . LYS A 1 3608 ? 205.582 219.445 250.313 1.00 10.22 ? 3608 LYS A CA    1 
ATOM   15539 C  C     . LYS A 1 3608 ? 205.466 218.537 249.086 1.00 8.73  ? 3608 LYS A C     1 
ATOM   15540 O  O     . LYS A 1 3608 ? 206.155 218.711 248.080 1.00 18.00 ? 3608 LYS A O     1 
ATOM   15541 C  CB    . LYS A 1 3608 ? 206.465 220.664 250.018 1.00 17.19 ? 3608 LYS A CB    1 
ATOM   15542 C  CG    . LYS A 1 3608 ? 206.460 221.715 251.117 1.00 19.56 ? 3608 LYS A CG    1 
ATOM   15543 C  CD    . LYS A 1 3608 ? 207.299 222.928 250.736 1.00 21.36 ? 3608 LYS A CD    1 
ATOM   15544 C  CE    . LYS A 1 3608 ? 208.784 222.601 250.730 1.00 29.20 ? 3608 LYS A CE    1 
ATOM   15545 N  NZ    . LYS A 1 3608 ? 209.287 222.283 252.094 1.00 29.45 ? 3608 LYS A NZ    1 
ATOM   15546 N  N     . ILE A 1 3609 ? 204.571 217.559 249.188 1.00 8.26  ? 3609 ILE A N     1 
ATOM   15547 C  CA    . ILE A 1 3609 ? 204.303 216.652 248.079 1.00 5.65  ? 3609 ILE A CA    1 
ATOM   15548 C  C     . ILE A 1 3609 ? 203.385 217.337 247.077 1.00 5.85  ? 3609 ILE A C     1 
ATOM   15549 O  O     . ILE A 1 3609 ? 202.479 218.091 247.449 1.00 7.80  ? 3609 ILE A O     1 
ATOM   15550 C  CB    . ILE A 1 3609 ? 203.698 215.331 248.592 1.00 5.33  ? 3609 ILE A CB    1 
ATOM   15551 C  CG1   . ILE A 1 3609 ? 203.491 214.347 247.437 1.00 3.57  ? 3609 ILE A CG1   1 
ATOM   15552 C  CG2   . ILE A 1 3609 ? 202.388 215.581 249.329 1.00 5.13  ? 3609 ILE A CG2   1 
ATOM   15553 C  CD1   . ILE A 1 3609 ? 203.168 212.945 247.879 1.00 4.20  ? 3609 ILE A CD1   1 
ATOM   15554 N  N     . THR A 1 3610 ? 203.625 217.084 245.795 1.00 7.68  ? 3610 THR A N     1 
ATOM   15555 C  CA    . THR A 1 3610 ? 202.843 217.656 244.709 1.00 5.15  ? 3610 THR A CA    1 
ATOM   15556 C  C     . THR A 1 3610 ? 202.103 216.544 243.979 1.00 5.54  ? 3610 THR A C     1 
ATOM   15557 O  O     . THR A 1 3610 ? 202.700 215.521 243.628 1.00 9.14  ? 3610 THR A O     1 
ATOM   15558 C  CB    . THR A 1 3610 ? 203.740 218.421 243.732 1.00 4.31  ? 3610 THR A CB    1 
ATOM   15559 O  OG1   . THR A 1 3610 ? 204.405 219.485 244.423 1.00 7.50  ? 3610 THR A OG1   1 
ATOM   15560 C  CG2   . THR A 1 3610 ? 202.926 218.998 242.588 1.00 7.59  ? 3610 THR A CG2   1 
ATOM   15561 N  N     . ARG A 1 3611 ? 200.805 216.740 243.763 1.00 5.12  ? 3611 ARG A N     1 
ATOM   15562 C  CA    . ARG A 1 3611 ? 200.011 215.823 242.961 1.00 3.91  ? 3611 ARG A CA    1 
ATOM   15563 C  C     . ARG A 1 3611 ? 200.065 216.256 241.503 1.00 5.36  ? 3611 ARG A C     1 
ATOM   15564 O  O     . ARG A 1 3611 ? 199.898 217.441 241.194 1.00 15.64 ? 3611 ARG A O     1 
ATOM   15565 C  CB    . ARG A 1 3611 ? 198.557 215.784 243.436 1.00 4.69  ? 3611 ARG A CB    1 
ATOM   15566 C  CG    . ARG A 1 3611 ? 197.715 214.754 242.699 1.00 7.98  ? 3611 ARG A CG    1 
ATOM   15567 C  CD    . ARG A 1 3611 ? 196.266 214.726 243.159 1.00 14.10 ? 3611 ARG A CD    1 
ATOM   15568 N  NE    . ARG A 1 3611 ? 196.088 214.316 244.546 1.00 20.32 ? 3611 ARG A NE    1 
ATOM   15569 C  CZ    . ARG A 1 3611 ? 195.643 215.115 245.506 1.00 20.45 ? 3611 ARG A CZ    1 
ATOM   15570 N  NH1   . ARG A 1 3611 ? 195.363 216.385 245.272 1.00 23.34 ? 3611 ARG A NH1   1 
ATOM   15571 N  NH2   . ARG A 1 3611 ? 195.470 214.625 246.728 1.00 18.50 ? 3611 ARG A NH2   1 
ATOM   15572 N  N     . THR A 1 3612 ? 200.298 215.301 240.610 1.00 3.27  ? 3612 THR A N     1 
ATOM   15573 C  CA    . THR A 1 3612 ? 200.276 215.556 239.179 1.00 5.51  ? 3612 THR A CA    1 
ATOM   15574 C  C     . THR A 1 3612 ? 199.813 214.288 238.474 1.00 2.89  ? 3612 THR A C     1 
ATOM   15575 O  O     . THR A 1 3612 ? 199.480 213.286 239.111 1.00 3.10  ? 3612 THR A O     1 
ATOM   15576 C  CB    . THR A 1 3612 ? 201.648 216.023 238.669 1.00 7.11  ? 3612 THR A CB    1 
ATOM   15577 O  OG1   . THR A 1 3612 ? 201.544 216.406 237.292 1.00 9.32  ? 3612 THR A OG1   1 
ATOM   15578 C  CG2   . THR A 1 3612 ? 202.679 214.922 238.809 1.00 3.12  ? 3612 THR A CG2   1 
ATOM   15579 N  N     . SER A 1 3613 ? 199.787 214.338 237.148 1.00 3.14  ? 3613 SER A N     1 
ATOM   15580 C  CA    . SER A 1 3613 ? 199.328 213.215 236.347 1.00 3.47  ? 3613 SER A CA    1 
ATOM   15581 C  C     . SER A 1 3613 ? 200.181 213.105 235.094 1.00 4.65  ? 3613 SER A C     1 
ATOM   15582 O  O     . SER A 1 3613 ? 200.759 214.091 234.630 1.00 6.49  ? 3613 SER A O     1 
ATOM   15583 C  CB    . SER A 1 3613 ? 197.850 213.364 235.967 1.00 3.23  ? 3613 SER A CB    1 
ATOM   15584 O  OG    . SER A 1 3613 ? 197.512 212.516 234.886 1.00 6.20  ? 3613 SER A OG    1 
ATOM   15585 N  N     . PHE A 1 3614 ? 200.251 211.890 234.547 1.00 4.31  ? 3614 PHE A N     1 
ATOM   15586 C  CA    . PHE A 1 3614 ? 200.960 211.678 233.292 1.00 3.81  ? 3614 PHE A CA    1 
ATOM   15587 C  C     . PHE A 1 3614 ? 200.316 212.435 232.140 1.00 6.38  ? 3614 PHE A C     1 
ATOM   15588 O  O     . PHE A 1 3614 ? 200.986 212.702 231.136 1.00 11.38 ? 3614 PHE A O     1 
ATOM   15589 C  CB    . PHE A 1 3614 ? 201.015 210.189 232.954 1.00 3.77  ? 3614 PHE A CB    1 
ATOM   15590 C  CG    . PHE A 1 3614 ? 201.981 209.407 233.791 1.00 3.72  ? 3614 PHE A CG    1 
ATOM   15591 C  CD1   . PHE A 1 3614 ? 203.345 209.521 233.584 1.00 3.73  ? 3614 PHE A CD1   1 
ATOM   15592 C  CD2   . PHE A 1 3614 ? 201.526 208.535 234.766 1.00 2.08  ? 3614 PHE A CD2   1 
ATOM   15593 C  CE1   . PHE A 1 3614 ? 204.237 208.798 234.347 1.00 2.67  ? 3614 PHE A CE1   1 
ATOM   15594 C  CE2   . PHE A 1 3614 ? 202.415 207.805 235.532 1.00 1.98  ? 3614 PHE A CE2   1 
ATOM   15595 C  CZ    . PHE A 1 3614 ? 203.773 207.939 235.323 1.00 2.11  ? 3614 PHE A CZ    1 
ATOM   15596 N  N     . LEU A 1 3615 ? 199.035 212.775 232.259 1.00 8.68  ? 3615 LEU A N     1 
ATOM   15597 C  CA    . LEU A 1 3615 ? 198.307 213.472 231.211 1.00 8.26  ? 3615 LEU A CA    1 
ATOM   15598 C  C     . LEU A 1 3615 ? 198.395 214.987 231.327 1.00 9.07  ? 3615 LEU A C     1 
ATOM   15599 O  O     . LEU A 1 3615 ? 198.071 215.684 230.360 1.00 14.47 ? 3615 LEU A O     1 
ATOM   15600 C  CB    . LEU A 1 3615 ? 196.838 213.041 231.234 1.00 6.87  ? 3615 LEU A CB    1 
ATOM   15601 C  CG    . LEU A 1 3615 ? 196.631 211.530 231.122 1.00 9.46  ? 3615 LEU A CG    1 
ATOM   15602 C  CD1   . LEU A 1 3615 ? 195.229 211.143 231.545 1.00 6.64  ? 3615 LEU A CD1   1 
ATOM   15603 C  CD2   . LEU A 1 3615 ? 196.927 211.042 229.714 1.00 8.03  ? 3615 LEU A CD2   1 
ATOM   15604 N  N     . ASP A 1 3616 ? 198.819 215.509 232.473 1.00 7.58  ? 3616 ASP A N     1 
ATOM   15605 C  CA    . ASP A 1 3616 ? 198.936 216.948 232.645 1.00 8.73  ? 3616 ASP A CA    1 
ATOM   15606 C  C     . ASP A 1 3616 ? 200.064 217.502 231.782 1.00 16.33 ? 3616 ASP A C     1 
ATOM   15607 O  O     . ASP A 1 3616 ? 201.041 216.812 231.476 1.00 17.42 ? 3616 ASP A O     1 
ATOM   15608 C  CB    . ASP A 1 3616 ? 199.181 217.293 234.114 1.00 9.89  ? 3616 ASP A CB    1 
ATOM   15609 C  CG    . ASP A 1 3616 ? 197.960 217.062 234.981 1.00 17.71 ? 3616 ASP A CG    1 
ATOM   15610 O  OD1   . ASP A 1 3616 ? 196.988 216.447 234.491 1.00 21.75 ? 3616 ASP A OD1   1 
ATOM   15611 O  OD2   . ASP A 1 3616 ? 197.969 217.493 236.153 1.00 21.50 ? 3616 ASP A OD2   1 
ATOM   15612 N  N     . ASP A 1 3617 ? 199.913 218.763 231.374 1.00 19.37 ? 3617 ASP A N     1 
ATOM   15613 C  CA    . ASP A 1 3617 ? 200.938 219.403 230.559 1.00 16.10 ? 3617 ASP A CA    1 
ATOM   15614 C  C     . ASP A 1 3617 ? 202.177 219.762 231.365 1.00 13.80 ? 3617 ASP A C     1 
ATOM   15615 O  O     . ASP A 1 3617 ? 203.263 219.879 230.790 1.00 15.45 ? 3617 ASP A O     1 
ATOM   15616 C  CB    . ASP A 1 3617 ? 200.375 220.656 229.889 1.00 19.03 ? 3617 ASP A CB    1 
ATOM   15617 C  CG    . ASP A 1 3617 ? 201.325 221.245 228.864 1.00 30.97 ? 3617 ASP A CG    1 
ATOM   15618 O  OD1   . ASP A 1 3617 ? 201.337 220.760 227.713 1.00 35.45 ? 3617 ASP A OD1   1 
ATOM   15619 O  OD2   . ASP A 1 3617 ? 202.063 222.192 229.211 1.00 29.90 ? 3617 ASP A OD2   1 
ATOM   15620 N  N     . ALA A 1 3618 ? 202.043 219.928 232.678 1.00 18.20 ? 3618 ALA A N     1 
ATOM   15621 C  CA    . ALA A 1 3618 ? 203.147 220.333 233.535 1.00 15.18 ? 3618 ALA A CA    1 
ATOM   15622 C  C     . ALA A 1 3618 ? 203.876 219.152 234.156 1.00 15.11 ? 3618 ALA A C     1 
ATOM   15623 O  O     . ALA A 1 3618 ? 204.726 219.355 235.028 1.00 19.03 ? 3618 ALA A O     1 
ATOM   15624 C  CB    . ALA A 1 3618 ? 202.642 221.270 234.632 1.00 11.50 ? 3618 ALA A CB    1 
ATOM   15625 N  N     . PHE A 1 3619 ? 203.567 217.923 233.729 1.00 13.07 ? 3619 PHE A N     1 
ATOM   15626 C  CA    . PHE A 1 3619 ? 204.148 216.749 234.369 1.00 8.08  ? 3619 PHE A CA    1 
ATOM   15627 C  C     . PHE A 1 3619 ? 205.666 216.734 234.243 1.00 8.27  ? 3619 PHE A C     1 
ATOM   15628 O  O     . PHE A 1 3619 ? 206.370 216.424 235.211 1.00 11.84 ? 3619 PHE A O     1 
ATOM   15629 C  CB    . PHE A 1 3619 ? 203.556 215.471 233.776 1.00 8.08  ? 3619 PHE A CB    1 
ATOM   15630 C  CG    . PHE A 1 3619 ? 204.364 214.243 234.072 1.00 7.86  ? 3619 PHE A CG    1 
ATOM   15631 C  CD1   . PHE A 1 3619 ? 204.375 213.699 235.347 1.00 5.54  ? 3619 PHE A CD1   1 
ATOM   15632 C  CD2   . PHE A 1 3619 ? 205.122 213.640 233.085 1.00 5.18  ? 3619 PHE A CD2   1 
ATOM   15633 C  CE1   . PHE A 1 3619 ? 205.124 212.574 235.629 1.00 3.71  ? 3619 PHE A CE1   1 
ATOM   15634 C  CE2   . PHE A 1 3619 ? 205.872 212.514 233.363 1.00 7.24  ? 3619 PHE A CE2   1 
ATOM   15635 C  CZ    . PHE A 1 3619 ? 205.873 211.982 234.636 1.00 7.06  ? 3619 PHE A CZ    1 
ATOM   15636 N  N     . ARG A 1 3620 ? 206.190 217.056 233.058 1.00 7.68  ? 3620 ARG A N     1 
ATOM   15637 C  CA    . ARG A 1 3620 ? 207.638 217.076 232.878 1.00 7.02  ? 3620 ARG A CA    1 
ATOM   15638 C  C     . ARG A 1 3620 ? 208.284 218.144 233.752 1.00 8.06  ? 3620 ARG A C     1 
ATOM   15639 O  O     . ARG A 1 3620 ? 209.330 217.903 234.367 1.00 9.55  ? 3620 ARG A O     1 
ATOM   15640 C  CB    . ARG A 1 3620 ? 207.984 217.304 231.407 1.00 12.58 ? 3620 ARG A CB    1 
ATOM   15641 C  CG    . ARG A 1 3620 ? 207.575 216.167 230.492 1.00 14.27 ? 3620 ARG A CG    1 
ATOM   15642 C  CD    . ARG A 1 3620 ? 207.904 216.487 229.048 1.00 22.69 ? 3620 ARG A CD    1 
ATOM   15643 N  NE    . ARG A 1 3620 ? 209.341 216.602 228.842 1.00 30.30 ? 3620 ARG A NE    1 
ATOM   15644 C  CZ    . ARG A 1 3620 ? 210.138 215.582 228.553 1.00 25.05 ? 3620 ARG A CZ    1 
ATOM   15645 N  NH1   . ARG A 1 3620 ? 209.662 214.360 228.388 1.00 16.10 ? 3620 ARG A NH1   1 
ATOM   15646 N  NH2   . ARG A 1 3620 ? 211.443 215.796 228.418 1.00 21.82 ? 3620 ARG A NH2   1 
ATOM   15647 N  N     . LYS A 1 3621 ? 207.678 219.332 233.817 1.00 9.42  ? 3621 LYS A N     1 
ATOM   15648 C  CA    . LYS A 1 3621 ? 208.186 220.375 234.702 1.00 6.78  ? 3621 LYS A CA    1 
ATOM   15649 C  C     . LYS A 1 3621 ? 208.082 219.962 236.164 1.00 7.98  ? 3621 LYS A C     1 
ATOM   15650 O  O     . LYS A 1 3621 ? 209.016 220.182 236.943 1.00 11.77 ? 3621 LYS A O     1 
ATOM   15651 C  CB    . LYS A 1 3621 ? 207.428 221.680 234.463 1.00 10.94 ? 3621 LYS A CB    1 
ATOM   15652 C  CG    . LYS A 1 3621 ? 207.927 222.843 235.303 1.00 12.90 ? 3621 LYS A CG    1 
ATOM   15653 C  CD    . LYS A 1 3621 ? 207.214 224.137 234.945 1.00 24.77 ? 3621 LYS A CD    1 
ATOM   15654 C  CE    . LYS A 1 3621 ? 207.608 225.261 235.885 1.00 27.02 ? 3621 LYS A CE    1 
ATOM   15655 N  NZ    . LYS A 1 3621 ? 209.043 225.627 235.737 1.00 26.65 ? 3621 LYS A NZ    1 
ATOM   15656 N  N     . ASN A 1 3622 ? 206.950 219.371 236.555 1.00 6.52  ? 3622 ASN A N     1 
ATOM   15657 C  CA    . ASN A 1 3622 ? 206.783 218.929 237.936 1.00 6.96  ? 3622 ASN A CA    1 
ATOM   15658 C  C     . ASN A 1 3622 ? 207.779 217.831 238.286 1.00 4.90  ? 3622 ASN A C     1 
ATOM   15659 O  O     . ASN A 1 3622 ? 208.377 217.847 239.368 1.00 4.63  ? 3622 ASN A O     1 
ATOM   15660 C  CB    . ASN A 1 3622 ? 205.350 218.448 238.157 1.00 8.19  ? 3622 ASN A CB    1 
ATOM   15661 C  CG    . ASN A 1 3622 ? 204.339 219.572 238.061 1.00 12.36 ? 3622 ASN A CG    1 
ATOM   15662 O  OD1   . ASN A 1 3622 ? 204.699 220.747 238.077 1.00 15.64 ? 3622 ASN A OD1   1 
ATOM   15663 N  ND2   . ASN A 1 3622 ? 203.068 219.216 237.941 1.00 11.48 ? 3622 ASN A ND2   1 
ATOM   15664 N  N     . LEU A 1 3623 ? 207.971 216.873 237.378 1.00 4.07  ? 3623 LEU A N     1 
ATOM   15665 C  CA    . LEU A 1 3623 ? 208.942 215.808 237.610 1.00 2.71  ? 3623 LEU A CA    1 
ATOM   15666 C  C     . LEU A 1 3623 ? 210.356 216.361 237.722 1.00 4.78  ? 3623 LEU A C     1 
ATOM   15667 O  O     . LEU A 1 3623 ? 211.126 215.942 238.593 1.00 4.20  ? 3623 LEU A O     1 
ATOM   15668 C  CB    . LEU A 1 3623 ? 208.858 214.780 236.488 1.00 2.66  ? 3623 LEU A CB    1 
ATOM   15669 C  CG    . LEU A 1 3623 ? 209.948 213.709 236.483 1.00 3.49  ? 3623 LEU A CG    1 
ATOM   15670 C  CD1   . LEU A 1 3623 ? 209.885 212.846 237.741 1.00 3.34  ? 3623 LEU A CD1   1 
ATOM   15671 C  CD2   . LEU A 1 3623 ? 209.853 212.877 235.224 1.00 0.63  ? 3623 LEU A CD2   1 
ATOM   15672 N  N     . GLU A 1 3624 ? 210.716 217.301 236.845 1.00 7.05  ? 3624 GLU A N     1 
ATOM   15673 C  CA    . GLU A 1 3624 ? 212.039 217.913 236.914 1.00 6.87  ? 3624 GLU A CA    1 
ATOM   15674 C  C     . GLU A 1 3624 ? 212.230 218.669 238.223 1.00 5.91  ? 3624 GLU A C     1 
ATOM   15675 O  O     . GLU A 1 3624 ? 213.302 218.603 238.835 1.00 8.12  ? 3624 GLU A O     1 
ATOM   15676 C  CB    . GLU A 1 3624 ? 212.242 218.845 235.720 1.00 9.27  ? 3624 GLU A CB    1 
ATOM   15677 C  CG    . GLU A 1 3624 ? 213.599 219.519 235.678 1.00 14.99 ? 3624 GLU A CG    1 
ATOM   15678 C  CD    . GLU A 1 3624 ? 213.668 220.617 234.636 1.00 23.86 ? 3624 GLU A CD    1 
ATOM   15679 O  OE1   . GLU A 1 3624 ? 213.833 220.294 233.441 1.00 25.18 ? 3624 GLU A OE1   1 
ATOM   15680 O  OE2   . GLU A 1 3624 ? 213.554 221.802 235.012 1.00 18.92 ? 3624 GLU A OE2   1 
ATOM   15681 N  N     . SER A 1 3625 ? 211.202 219.396 238.662 1.00 7.18  ? 3625 SER A N     1 
ATOM   15682 C  CA    . SER A 1 3625 ? 211.296 220.143 239.912 1.00 5.72  ? 3625 SER A CA    1 
ATOM   15683 C  C     . SER A 1 3625 ? 211.429 219.212 241.111 1.00 6.05  ? 3625 SER A C     1 
ATOM   15684 O  O     . SER A 1 3625 ? 212.232 219.466 242.015 1.00 6.84  ? 3625 SER A O     1 
ATOM   15685 C  CB    . SER A 1 3625 ? 210.077 221.050 240.066 1.00 6.08  ? 3625 SER A CB    1 
ATOM   15686 O  OG    . SER A 1 3625 ? 210.121 221.763 241.286 1.00 14.65 ? 3625 SER A OG    1 
ATOM   15687 N  N     . ALA A 1 3626 ? 210.646 218.130 241.138 1.00 4.92  ? 3626 ALA A N     1 
ATOM   15688 C  CA    . ALA A 1 3626 ? 210.719 217.194 242.254 1.00 2.82  ? 3626 ALA A CA    1 
ATOM   15689 C  C     . ALA A 1 3626 ? 212.080 216.513 242.319 1.00 4.25  ? 3626 ALA A C     1 
ATOM   15690 O  O     . ALA A 1 3626 ? 212.639 216.328 243.406 1.00 3.55  ? 3626 ALA A O     1 
ATOM   15691 C  CB    . ALA A 1 3626 ? 209.601 216.158 242.142 1.00 1.82  ? 3626 ALA A CB    1 
ATOM   15692 N  N     . LEU A 1 3627 ? 212.626 216.126 241.164 1.00 3.24  ? 3627 LEU A N     1 
ATOM   15693 C  CA    . LEU A 1 3627 ? 213.949 215.511 241.137 1.00 1.91  ? 3627 LEU A CA    1 
ATOM   15694 C  C     . LEU A 1 3627 ? 215.026 216.495 241.581 1.00 5.45  ? 3627 LEU A C     1 
ATOM   15695 O  O     . LEU A 1 3627 ? 215.953 216.123 242.307 1.00 4.35  ? 3627 LEU A O     1 
ATOM   15696 C  CB    . LEU A 1 3627 ? 214.254 214.987 239.735 1.00 2.40  ? 3627 LEU A CB    1 
ATOM   15697 C  CG    . LEU A 1 3627 ? 213.455 213.787 239.226 1.00 1.79  ? 3627 LEU A CG    1 
ATOM   15698 C  CD1   . LEU A 1 3627 ? 213.485 213.753 237.705 1.00 2.81  ? 3627 LEU A CD1   1 
ATOM   15699 C  CD2   . LEU A 1 3627 ? 213.986 212.492 239.802 1.00 0.36  ? 3627 LEU A CD2   1 
ATOM   15700 N  N     . ARG A 1 3628 ? 214.916 217.755 241.154 1.00 4.92  ? 3628 ARG A N     1 
ATOM   15701 C  CA    . ARG A 1 3628 ? 215.956 218.735 241.447 1.00 4.58  ? 3628 ARG A CA    1 
ATOM   15702 C  C     . ARG A 1 3628 ? 215.945 219.141 242.915 1.00 4.36  ? 3628 ARG A C     1 
ATOM   15703 O  O     . ARG A 1 3628 ? 216.999 219.221 243.556 1.00 10.19 ? 3628 ARG A O     1 
ATOM   15704 C  CB    . ARG A 1 3628 ? 215.786 219.957 240.542 1.00 7.00  ? 3628 ARG A CB    1 
ATOM   15705 C  CG    . ARG A 1 3628 ? 216.758 221.087 240.826 1.00 6.56  ? 3628 ARG A CG    1 
ATOM   15706 C  CD    . ARG A 1 3628 ? 216.599 222.224 239.832 1.00 7.93  ? 3628 ARG A CD    1 
ATOM   15707 N  NE    . ARG A 1 3628 ? 217.178 221.884 238.538 1.00 15.20 ? 3628 ARG A NE    1 
ATOM   15708 C  CZ    . ARG A 1 3628 ? 216.476 221.674 237.434 1.00 9.34  ? 3628 ARG A CZ    1 
ATOM   15709 N  NH1   . ARG A 1 3628 ? 215.161 221.810 237.416 1.00 10.62 ? 3628 ARG A NH1   1 
ATOM   15710 N  NH2   . ARG A 1 3628 ? 217.108 221.320 236.319 1.00 10.21 ? 3628 ARG A NH2   1 
ATOM   15711 N  N     . PHE A 1 3629 ? 214.765 219.400 243.470 1.00 4.86  ? 3629 PHE A N     1 
ATOM   15712 C  CA    . PHE A 1 3629 ? 214.646 219.865 244.845 1.00 4.81  ? 3629 PHE A CA    1 
ATOM   15713 C  C     . PHE A 1 3629 ? 214.442 218.737 245.846 1.00 6.26  ? 3629 PHE A C     1 
ATOM   15714 O  O     . PHE A 1 3629 ? 214.432 218.997 247.053 1.00 10.45 ? 3629 PHE A O     1 
ATOM   15715 C  CB    . PHE A 1 3629 ? 213.499 220.872 244.959 1.00 5.62  ? 3629 PHE A CB    1 
ATOM   15716 C  CG    . PHE A 1 3629 ? 213.623 222.030 244.018 1.00 8.04  ? 3629 PHE A CG    1 
ATOM   15717 C  CD1   . PHE A 1 3629 ? 214.821 222.717 243.903 1.00 9.53  ? 3629 PHE A CD1   1 
ATOM   15718 C  CD2   . PHE A 1 3629 ? 212.552 222.424 243.237 1.00 5.85  ? 3629 PHE A CD2   1 
ATOM   15719 C  CE1   . PHE A 1 3629 ? 214.944 223.780 243.030 1.00 10.82 ? 3629 PHE A CE1   1 
ATOM   15720 C  CE2   . PHE A 1 3629 ? 212.671 223.488 242.364 1.00 12.50 ? 3629 PHE A CE2   1 
ATOM   15721 C  CZ    . PHE A 1 3629 ? 213.869 224.166 242.261 1.00 8.70  ? 3629 PHE A CZ    1 
ATOM   15722 N  N     . GLY A 1 3630 ? 214.293 217.501 245.384 1.00 5.80  ? 3630 GLY A N     1 
ATOM   15723 C  CA    . GLY A 1 3630 ? 214.064 216.382 246.280 1.00 5.29  ? 3630 GLY A CA    1 
ATOM   15724 C  C     . GLY A 1 3630 ? 212.735 216.411 247.000 1.00 6.50  ? 3630 GLY A C     1 
ATOM   15725 O  O     . GLY A 1 3630 ? 212.678 216.112 248.199 1.00 8.41  ? 3630 GLY A O     1 
ATOM   15726 N  N     . ASN A 1 3631 ? 211.676 216.762 246.309 1.00 4.32  ? 3631 ASN A N     1 
ATOM   15727 C  CA    . ASN A 1 3631 ? 210.370 216.746 246.937 1.00 4.82  ? 3631 ASN A CA    1 
ATOM   15728 C  C     . ASN A 1 3631 ? 209.590 215.504 246.523 1.00 4.45  ? 3631 ASN A C     1 
ATOM   15729 O  O     . ASN A 1 3631 ? 209.755 215.004 245.407 1.00 3.21  ? 3631 ASN A O     1 
ATOM   15730 C  CB    . ASN A 1 3631 ? 209.569 217.995 246.560 1.00 7.21  ? 3631 ASN A CB    1 
ATOM   15731 C  CG    . ASN A 1 3631 ? 210.322 219.278 246.844 1.00 8.46  ? 3631 ASN A CG    1 
ATOM   15732 O  OD1   . ASN A 1 3631 ? 210.471 220.129 245.969 1.00 9.83  ? 3631 ASN A OD1   1 
ATOM   15733 N  ND2   . ASN A 1 3631 ? 210.803 219.425 248.072 1.00 9.10  ? 3631 ASN A ND2   1 
ATOM   15734 N  N     . PRO A 1 3632 ? 208.750 214.975 247.410 1.00 6.10  ? 3632 PRO A N     1 
ATOM   15735 C  CA    . PRO A 1 3632 ? 207.887 213.854 247.024 1.00 2.57  ? 3632 PRO A CA    1 
ATOM   15736 C  C     . PRO A 1 3632 ? 206.917 214.257 245.925 1.00 2.11  ? 3632 PRO A C     1 
ATOM   15737 O  O     . PRO A 1 3632 ? 206.387 215.370 245.913 1.00 6.47  ? 3632 PRO A O     1 
ATOM   15738 C  CB    . PRO A 1 3632 ? 207.157 213.501 248.325 1.00 3.12  ? 3632 PRO A CB    1 
ATOM   15739 C  CG    . PRO A 1 3632 ? 207.292 214.705 249.187 1.00 3.81  ? 3632 PRO A CG    1 
ATOM   15740 C  CD    . PRO A 1 3632 ? 208.595 215.331 248.827 1.00 5.45  ? 3632 PRO A CD    1 
ATOM   15741 N  N     . LEU A 1 3633 ? 206.686 213.334 244.995 1.00 1.12  ? 3633 LEU A N     1 
ATOM   15742 C  CA    . LEU A 1 3633 ? 205.791 213.561 243.871 1.00 1.14  ? 3633 LEU A CA    1 
ATOM   15743 C  C     . LEU A 1 3633 ? 204.821 212.396 243.763 1.00 0.97  ? 3633 LEU A C     1 
ATOM   15744 O  O     . LEU A 1 3633 ? 205.237 211.234 243.794 1.00 1.24  ? 3633 LEU A O     1 
ATOM   15745 C  CB    . LEU A 1 3633 ? 206.574 213.727 242.565 1.00 1.55  ? 3633 LEU A CB    1 
ATOM   15746 C  CG    . LEU A 1 3633 ? 205.777 214.134 241.323 1.00 1.37  ? 3633 LEU A CG    1 
ATOM   15747 C  CD1   . LEU A 1 3633 ? 205.186 215.522 241.487 1.00 2.39  ? 3633 LEU A CD1   1 
ATOM   15748 C  CD2   . LEU A 1 3633 ? 206.649 214.065 240.085 1.00 1.24  ? 3633 LEU A CD2   1 
ATOM   15749 N  N     . LEU A 1 3634 ? 203.536 212.707 243.642 1.00 1.16  ? 3634 LEU A N     1 
ATOM   15750 C  CA    . LEU A 1 3634 ? 202.497 211.711 243.412 1.00 0.93  ? 3634 LEU A CA    1 
ATOM   15751 C  C     . LEU A 1 3634 ? 201.953 211.907 242.003 1.00 1.53  ? 3634 LEU A C     1 
ATOM   15752 O  O     . LEU A 1 3634 ? 201.422 212.975 241.683 1.00 3.05  ? 3634 LEU A O     1 
ATOM   15753 C  CB    . LEU A 1 3634 ? 201.378 211.831 244.445 1.00 1.41  ? 3634 LEU A CB    1 
ATOM   15754 C  CG    . LEU A 1 3634 ? 200.127 210.995 244.169 1.00 2.16  ? 3634 LEU A CG    1 
ATOM   15755 C  CD1   . LEU A 1 3634 ? 200.457 209.510 244.133 1.00 0.70  ? 3634 LEU A CD1   1 
ATOM   15756 C  CD2   . LEU A 1 3634 ? 199.051 211.285 245.195 1.00 4.36  ? 3634 LEU A CD2   1 
ATOM   15757 N  N     . VAL A 1 3635 ? 202.084 210.881 241.170 1.00 0.77  ? 3635 VAL A N     1 
ATOM   15758 C  CA    . VAL A 1 3635 ? 201.686 210.959 239.770 1.00 1.37  ? 3635 VAL A CA    1 
ATOM   15759 C  C     . VAL A 1 3635 ? 200.541 209.978 239.558 1.00 1.07  ? 3635 VAL A C     1 
ATOM   15760 O  O     . VAL A 1 3635 ? 200.689 208.776 239.811 1.00 1.17  ? 3635 VAL A O     1 
ATOM   15761 C  CB    . VAL A 1 3635 ? 202.861 210.651 238.830 1.00 2.11  ? 3635 VAL A CB    1 
ATOM   15762 C  CG1   . VAL A 1 3635 ? 202.402 210.682 237.388 1.00 1.57  ? 3635 VAL A CG1   1 
ATOM   15763 C  CG2   . VAL A 1 3635 ? 204.012 211.609 239.069 1.00 1.49  ? 3635 VAL A CG2   1 
ATOM   15764 N  N     . GLN A 1 3636 ? 199.408 210.484 239.091 1.00 1.52  ? 3636 GLN A N     1 
ATOM   15765 C  CA    . GLN A 1 3636 ? 198.220 209.675 238.872 1.00 2.01  ? 3636 GLN A CA    1 
ATOM   15766 C  C     . GLN A 1 3636 ? 198.116 209.252 237.412 1.00 2.53  ? 3636 GLN A C     1 
ATOM   15767 O  O     . GLN A 1 3636 ? 198.892 209.680 236.553 1.00 5.37  ? 3636 GLN A O     1 
ATOM   15768 C  CB    . GLN A 1 3636 ? 196.962 210.438 239.299 1.00 3.76  ? 3636 GLN A CB    1 
ATOM   15769 C  CG    . GLN A 1 3636 ? 196.973 210.883 240.751 1.00 6.47  ? 3636 GLN A CG    1 
ATOM   15770 C  CD    . GLN A 1 3636 ? 195.687 211.571 241.162 1.00 13.12 ? 3636 GLN A CD    1 
ATOM   15771 O  OE1   . GLN A 1 3636 ? 195.013 211.142 242.097 1.00 16.82 ? 3636 GLN A OE1   1 
ATOM   15772 N  NE2   . GLN A 1 3636 ? 195.337 212.641 240.460 1.00 15.98 ? 3636 GLN A NE2   1 
ATOM   15773 N  N     . ASP A 1 3637 ? 197.136 208.386 237.145 1.00 3.11  ? 3637 ASP A N     1 
ATOM   15774 C  CA    . ASP A 1 3637 ? 196.846 207.886 235.800 1.00 5.61  ? 3637 ASP A CA    1 
ATOM   15775 C  C     . ASP A 1 3637 ? 198.050 207.150 235.211 1.00 5.52  ? 3637 ASP A C     1 
ATOM   15776 O  O     . ASP A 1 3637 ? 198.497 207.427 234.097 1.00 9.80  ? 3637 ASP A O     1 
ATOM   15777 C  CB    . ASP A 1 3637 ? 196.385 209.021 234.880 1.00 5.78  ? 3637 ASP A CB    1 
ATOM   15778 C  CG    . ASP A 1 3637 ? 195.272 209.853 235.494 1.00 8.82  ? 3637 ASP A CG    1 
ATOM   15779 O  OD1   . ASP A 1 3637 ? 194.200 209.291 235.796 1.00 12.68 ? 3637 ASP A OD1   1 
ATOM   15780 O  OD2   . ASP A 1 3637 ? 195.469 211.070 235.681 1.00 11.12 ? 3637 ASP A OD2   1 
ATOM   15781 N  N     . VAL A 1 3638 ? 198.568 206.185 235.974 1.00 4.02  ? 3638 VAL A N     1 
ATOM   15782 C  CA    . VAL A 1 3638 ? 199.730 205.418 235.541 1.00 3.11  ? 3638 VAL A CA    1 
ATOM   15783 C  C     . VAL A 1 3638 ? 199.406 204.468 234.397 1.00 2.74  ? 3638 VAL A C     1 
ATOM   15784 O  O     . VAL A 1 3638 ? 200.321 203.893 233.800 1.00 4.92  ? 3638 VAL A O     1 
ATOM   15785 C  CB    . VAL A 1 3638 ? 200.334 204.667 236.749 1.00 1.79  ? 3638 VAL A CB    1 
ATOM   15786 C  CG1   . VAL A 1 3638 ? 199.468 203.485 237.143 1.00 2.15  ? 3638 VAL A CG1   1 
ATOM   15787 C  CG2   . VAL A 1 3638 ? 201.775 204.242 236.472 1.00 1.61  ? 3638 VAL A CG2   1 
ATOM   15788 N  N     . GLU A 1 3639 ? 198.123 204.298 234.067 1.00 3.62  ? 3639 GLU A N     1 
ATOM   15789 C  CA    . GLU A 1 3639 ? 197.755 203.578 232.853 1.00 6.21  ? 3639 GLU A CA    1 
ATOM   15790 C  C     . GLU A 1 3639 ? 198.257 204.287 231.603 1.00 5.77  ? 3639 GLU A C     1 
ATOM   15791 O  O     . GLU A 1 3639 ? 198.404 203.650 230.554 1.00 8.89  ? 3639 GLU A O     1 
ATOM   15792 C  CB    . GLU A 1 3639 ? 196.236 203.406 232.780 1.00 3.50  ? 3639 GLU A CB    1 
ATOM   15793 C  CG    . GLU A 1 3639 ? 195.440 204.687 233.004 1.00 6.24  ? 3639 GLU A CG    1 
ATOM   15794 C  CD    . GLU A 1 3639 ? 195.174 204.984 234.472 1.00 11.10 ? 3639 GLU A CD    1 
ATOM   15795 O  OE1   . GLU A 1 3639 ? 196.016 204.632 235.322 1.00 6.55  ? 3639 GLU A OE1   1 
ATOM   15796 O  OE2   . GLU A 1 3639 ? 194.118 205.575 234.773 1.00 17.44 ? 3639 GLU A OE2   1 
ATOM   15797 N  N     . SER A 1 3640 ? 198.518 205.589 231.694 1.00 3.31  ? 3640 SER A N     1 
ATOM   15798 C  CA    . SER A 1 3640 ? 199.123 206.378 230.625 1.00 4.92  ? 3640 SER A CA    1 
ATOM   15799 C  C     . SER A 1 3640 ? 200.593 206.651 230.907 1.00 5.38  ? 3640 SER A C     1 
ATOM   15800 O  O     . SER A 1 3640 ? 201.085 207.757 230.674 1.00 6.10  ? 3640 SER A O     1 
ATOM   15801 C  CB    . SER A 1 3640 ? 198.360 207.684 230.432 1.00 5.50  ? 3640 SER A CB    1 
ATOM   15802 O  OG    . SER A 1 3640 ? 197.022 207.435 230.040 1.00 12.01 ? 3640 SER A OG    1 
ATOM   15803 N  N     . TYR A 1 3641 ? 201.300 205.647 231.426 1.00 4.37  ? 3641 TYR A N     1 
ATOM   15804 C  CA    . TYR A 1 3641 ? 202.667 205.822 231.906 1.00 2.29  ? 3641 TYR A CA    1 
ATOM   15805 C  C     . TYR A 1 3641 ? 203.570 206.417 230.832 1.00 5.43  ? 3641 TYR A C     1 
ATOM   15806 O  O     . TYR A 1 3641 ? 203.585 205.961 229.685 1.00 8.00  ? 3641 TYR A O     1 
ATOM   15807 C  CB    . TYR A 1 3641 ? 203.222 204.478 232.375 1.00 2.27  ? 3641 TYR A CB    1 
ATOM   15808 C  CG    . TYR A 1 3641 ? 204.705 204.484 232.661 1.00 1.92  ? 3641 TYR A CG    1 
ATOM   15809 C  CD1   . TYR A 1 3641 ? 205.202 205.011 233.844 1.00 1.25  ? 3641 TYR A CD1   1 
ATOM   15810 C  CD2   . TYR A 1 3641 ? 205.609 203.958 231.747 1.00 0.80  ? 3641 TYR A CD2   1 
ATOM   15811 C  CE1   . TYR A 1 3641 ? 206.554 205.018 234.108 1.00 1.50  ? 3641 TYR A CE1   1 
ATOM   15812 C  CE2   . TYR A 1 3641 ? 206.960 203.961 232.003 1.00 1.37  ? 3641 TYR A CE2   1 
ATOM   15813 C  CZ    . TYR A 1 3641 ? 207.429 204.491 233.183 1.00 1.55  ? 3641 TYR A CZ    1 
ATOM   15814 O  OH    . TYR A 1 3641 ? 208.777 204.495 233.442 1.00 1.69  ? 3641 TYR A OH    1 
ATOM   15815 N  N     . ASP A 1 3642 ? 204.331 207.436 231.219 1.00 4.89  ? 3642 ASP A N     1 
ATOM   15816 C  CA    . ASP A 1 3642 ? 205.266 208.092 230.318 1.00 3.24  ? 3642 ASP A CA    1 
ATOM   15817 C  C     . ASP A 1 3642 ? 206.635 207.443 230.460 1.00 2.84  ? 3642 ASP A C     1 
ATOM   15818 O  O     . ASP A 1 3642 ? 207.198 207.452 231.563 1.00 1.48  ? 3642 ASP A O     1 
ATOM   15819 C  CB    . ASP A 1 3642 ? 205.349 209.578 230.634 1.00 6.12  ? 3642 ASP A CB    1 
ATOM   15820 C  CG    . ASP A 1 3642 ? 205.929 210.392 229.495 1.00 8.14  ? 3642 ASP A CG    1 
ATOM   15821 O  OD1   . ASP A 1 3642 ? 206.326 209.805 228.471 1.00 9.76  ? 3642 ASP A OD1   1 
ATOM   15822 O  OD2   . ASP A 1 3642 ? 205.977 211.632 229.623 1.00 12.16 ? 3642 ASP A OD2   1 
ATOM   15823 N  N     . PRO A 1 3643 ? 207.206 206.874 229.392 1.00 4.52  ? 3643 PRO A N     1 
ATOM   15824 C  CA    . PRO A 1 3643 ? 208.489 206.167 229.523 1.00 2.38  ? 3643 PRO A CA    1 
ATOM   15825 C  C     . PRO A 1 3643 ? 209.658 207.076 229.873 1.00 3.32  ? 3643 PRO A C     1 
ATOM   15826 O  O     . PRO A 1 3643 ? 210.798 206.614 229.967 1.00 6.83  ? 3643 PRO A O     1 
ATOM   15827 C  CB    . PRO A 1 3643 ? 208.678 205.530 228.139 1.00 3.56  ? 3643 PRO A CB    1 
ATOM   15828 C  CG    . PRO A 1 3643 ? 207.314 205.490 227.547 1.00 4.21  ? 3643 PRO A CG    1 
ATOM   15829 C  CD    . PRO A 1 3643 ? 206.627 206.711 228.050 1.00 2.73  ? 3643 PRO A CD    1 
ATOM   15830 N  N     . VAL A 1 3644 ? 209.389 208.369 230.063 1.00 4.27  ? 3644 VAL A N     1 
ATOM   15831 C  CA    . VAL A 1 3644 ? 210.426 209.298 230.490 1.00 3.02  ? 3644 VAL A CA    1 
ATOM   15832 C  C     . VAL A 1 3644 ? 210.907 208.984 231.902 1.00 4.40  ? 3644 VAL A C     1 
ATOM   15833 O  O     . VAL A 1 3644 ? 212.012 209.383 232.281 1.00 11.75 ? 3644 VAL A O     1 
ATOM   15834 C  CB    . VAL A 1 3644 ? 209.908 210.750 230.373 1.00 5.20  ? 3644 VAL A CB    1 
ATOM   15835 C  CG1   . VAL A 1 3644 ? 208.896 211.059 231.471 1.00 6.44  ? 3644 VAL A CG1   1 
ATOM   15836 C  CG2   . VAL A 1 3644 ? 211.059 211.741 230.386 1.00 6.46  ? 3644 VAL A CG2   1 
ATOM   15837 N  N     . LEU A 1 3645 ? 210.107 208.261 232.690 1.00 2.45  ? 3645 LEU A N     1 
ATOM   15838 C  CA    . LEU A 1 3645 ? 210.505 207.848 234.031 1.00 3.23  ? 3645 LEU A CA    1 
ATOM   15839 C  C     . LEU A 1 3645 ? 211.370 206.599 234.064 1.00 1.90  ? 3645 LEU A C     1 
ATOM   15840 O  O     . LEU A 1 3645 ? 211.782 206.196 235.156 1.00 3.07  ? 3645 LEU A O     1 
ATOM   15841 C  CB    . LEU A 1 3645 ? 209.283 207.594 234.918 1.00 4.10  ? 3645 LEU A CB    1 
ATOM   15842 C  CG    . LEU A 1 3645 ? 208.407 208.757 235.353 1.00 1.69  ? 3645 LEU A CG    1 
ATOM   15843 C  CD1   . LEU A 1 3645 ? 207.197 208.233 236.092 1.00 1.95  ? 3645 LEU A CD1   1 
ATOM   15844 C  CD2   . LEU A 1 3645 ? 209.234 209.614 236.272 1.00 0.79  ? 3645 LEU A CD2   1 
ATOM   15845 N  N     . ASN A 1 3646 ? 211.638 205.972 232.920 1.00 2.79  ? 3646 ASN A N     1 
ATOM   15846 C  CA    . ASN A 1 3646 ? 212.407 204.730 232.928 1.00 2.01  ? 3646 ASN A CA    1 
ATOM   15847 C  C     . ASN A 1 3646 ? 213.754 204.872 233.626 1.00 1.97  ? 3646 ASN A C     1 
ATOM   15848 O  O     . ASN A 1 3646 ? 214.071 204.021 234.476 1.00 2.50  ? 3646 ASN A O     1 
ATOM   15849 C  CB    . ASN A 1 3646 ? 212.564 204.211 231.494 1.00 1.30  ? 3646 ASN A CB    1 
ATOM   15850 C  CG    . ASN A 1 3646 ? 211.323 203.511 230.989 1.00 1.12  ? 3646 ASN A CG    1 
ATOM   15851 O  OD1   . ASN A 1 3646 ? 210.346 203.359 231.716 1.00 2.33  ? 3646 ASN A OD1   1 
ATOM   15852 N  ND2   . ASN A 1 3646 ? 211.356 203.077 229.737 1.00 2.58  ? 3646 ASN A ND2   1 
ATOM   15853 N  N     . PRO A 1 3647 ? 214.582 205.884 233.343 1.00 2.48  ? 3647 PRO A N     1 
ATOM   15854 C  CA    . PRO A 1 3647 ? 215.813 206.044 234.135 1.00 2.50  ? 3647 PRO A CA    1 
ATOM   15855 C  C     . PRO A 1 3647 ? 215.563 206.347 235.603 1.00 2.35  ? 3647 PRO A C     1 
ATOM   15856 O  O     . PRO A 1 3647 ? 216.366 205.945 236.452 1.00 2.30  ? 3647 PRO A O     1 
ATOM   15857 C  CB    . PRO A 1 3647 ? 216.533 207.201 233.429 1.00 2.42  ? 3647 PRO A CB    1 
ATOM   15858 C  CG    . PRO A 1 3647 ? 215.444 207.954 232.760 1.00 3.75  ? 3647 PRO A CG    1 
ATOM   15859 C  CD    . PRO A 1 3647 ? 214.493 206.910 232.288 1.00 2.52  ? 3647 PRO A CD    1 
ATOM   15860 N  N     . VAL A 1 3648 ? 214.480 207.055 235.930 1.00 2.90  ? 3648 VAL A N     1 
ATOM   15861 C  CA    . VAL A 1 3648 ? 214.201 207.385 237.325 1.00 1.98  ? 3648 VAL A CA    1 
ATOM   15862 C  C     . VAL A 1 3648 ? 213.829 206.130 238.107 1.00 1.54  ? 3648 VAL A C     1 
ATOM   15863 O  O     . VAL A 1 3648 ? 214.323 205.902 239.216 1.00 2.46  ? 3648 VAL A O     1 
ATOM   15864 C  CB    . VAL A 1 3648 ? 213.097 208.453 237.417 1.00 2.75  ? 3648 VAL A CB    1 
ATOM   15865 C  CG1   . VAL A 1 3648 ? 212.718 208.702 238.869 1.00 0.56  ? 3648 VAL A CG1   1 
ATOM   15866 C  CG2   . VAL A 1 3648 ? 213.550 209.745 236.756 1.00 1.35  ? 3648 VAL A CG2   1 
ATOM   15867 N  N     . LEU A 1 3649 ? 212.955 205.297 237.537 1.00 1.32  ? 3649 LEU A N     1 
ATOM   15868 C  CA    . LEU A 1 3649 ? 212.524 204.091 238.231 1.00 1.11  ? 3649 LEU A CA    1 
ATOM   15869 C  C     . LEU A 1 3649 ? 213.650 203.073 238.350 1.00 1.95  ? 3649 LEU A C     1 
ATOM   15870 O  O     . LEU A 1 3649 ? 213.734 202.363 239.357 1.00 4.82  ? 3649 LEU A O     1 
ATOM   15871 C  CB    . LEU A 1 3649 ? 211.319 203.474 237.520 1.00 1.24  ? 3649 LEU A CB    1 
ATOM   15872 C  CG    . LEU A 1 3649 ? 210.074 204.357 237.416 1.00 1.66  ? 3649 LEU A CG    1 
ATOM   15873 C  CD1   . LEU A 1 3649 ? 208.899 203.573 236.858 1.00 0.67  ? 3649 LEU A CD1   1 
ATOM   15874 C  CD2   . LEU A 1 3649 ? 209.725 204.970 238.764 1.00 1.28  ? 3649 LEU A CD2   1 
ATOM   15875 N  N     . ASN A 1 3650 ? 214.521 202.989 237.347 1.00 1.61  ? 3650 ASN A N     1 
ATOM   15876 C  CA    . ASN A 1 3650 ? 215.675 202.102 237.406 1.00 1.24  ? 3650 ASN A CA    1 
ATOM   15877 C  C     . ASN A 1 3650 ? 216.836 202.685 238.196 1.00 2.22  ? 3650 ASN A C     1 
ATOM   15878 O  O     . ASN A 1 3650 ? 217.835 201.985 238.392 1.00 8.54  ? 3650 ASN A O     1 
ATOM   15879 C  CB    . ASN A 1 3650 ? 216.152 201.747 235.996 1.00 1.86  ? 3650 ASN A CB    1 
ATOM   15880 C  CG    . ASN A 1 3650 ? 215.183 200.856 235.259 1.00 2.65  ? 3650 ASN A CG    1 
ATOM   15881 O  OD1   . ASN A 1 3650 ? 214.227 200.347 235.839 1.00 8.20  ? 3650 ASN A OD1   1 
ATOM   15882 N  ND2   . ASN A 1 3650 ? 215.430 200.652 233.974 1.00 3.65  ? 3650 ASN A ND2   1 
ATOM   15883 N  N     . ARG A 1 3651 ? 216.732 203.938 238.644 1.00 1.82  ? 3651 ARG A N     1 
ATOM   15884 C  CA    . ARG A 1 3651 ? 217.774 204.580 239.446 1.00 2.22  ? 3651 ARG A CA    1 
ATOM   15885 C  C     . ARG A 1 3651 ? 219.106 204.612 238.699 1.00 4.26  ? 3651 ARG A C     1 
ATOM   15886 O  O     . ARG A 1 3651 ? 220.167 204.335 239.261 1.00 5.05  ? 3651 ARG A O     1 
ATOM   15887 C  CB    . ARG A 1 3651 ? 217.914 203.890 240.804 1.00 4.20  ? 3651 ARG A CB    1 
ATOM   15888 C  CG    . ARG A 1 3651 ? 216.710 204.086 241.711 1.00 3.96  ? 3651 ARG A CG    1 
ATOM   15889 C  CD    . ARG A 1 3651 ? 216.844 203.315 243.009 1.00 5.55  ? 3651 ARG A CD    1 
ATOM   15890 N  NE    . ARG A 1 3651 ? 215.548 203.115 243.645 1.00 10.65 ? 3651 ARG A NE    1 
ATOM   15891 C  CZ    . ARG A 1 3651 ? 214.997 203.956 244.510 1.00 3.47  ? 3651 ARG A CZ    1 
ATOM   15892 N  NH1   . ARG A 1 3651 ? 215.615 205.062 244.888 1.00 3.59  ? 3651 ARG A NH1   1 
ATOM   15893 N  NH2   . ARG A 1 3651 ? 213.793 203.682 245.004 1.00 0.49  ? 3651 ARG A NH2   1 
ATOM   15894 N  N     . GLU A 1 3652 ? 219.043 204.950 237.411 1.00 3.95  ? 3652 GLU A N     1 
ATOM   15895 C  CA    . GLU A 1 3652 ? 220.227 205.034 236.553 1.00 3.01  ? 3652 GLU A CA    1 
ATOM   15896 C  C     . GLU A 1 3652 ? 220.890 206.393 236.757 1.00 5.16  ? 3652 GLU A C     1 
ATOM   15897 O  O     . GLU A 1 3652 ? 220.720 207.332 235.977 1.00 12.10 ? 3652 GLU A O     1 
ATOM   15898 C  CB    . GLU A 1 3652 ? 219.851 204.822 235.092 1.00 5.12  ? 3652 GLU A CB    1 
ATOM   15899 C  CG    . GLU A 1 3652 ? 218.938 203.644 234.823 1.00 2.96  ? 3652 GLU A CG    1 
ATOM   15900 C  CD    . GLU A 1 3652 ? 218.344 203.685 233.428 1.00 6.94  ? 3652 GLU A CD    1 
ATOM   15901 O  OE1   . GLU A 1 3652 ? 218.907 204.388 232.562 1.00 7.32  ? 3652 GLU A OE1   1 
ATOM   15902 O  OE2   . GLU A 1 3652 ? 217.312 203.023 233.194 1.00 6.34  ? 3652 GLU A OE2   1 
ATOM   15903 N  N     . VAL A 1 3653 ? 221.667 206.493 237.824 1.00 6.69  ? 3653 VAL A N     1 
ATOM   15904 C  CA    . VAL A 1 3653 ? 222.316 207.746 238.188 1.00 8.89  ? 3653 VAL A CA    1 
ATOM   15905 C  C     . VAL A 1 3653 ? 223.793 207.675 237.829 1.00 9.20  ? 3653 VAL A C     1 
ATOM   15906 O  O     . VAL A 1 3653 ? 224.426 206.615 237.890 1.00 10.84 ? 3653 VAL A O     1 
ATOM   15907 C  CB    . VAL A 1 3653 ? 222.118 208.073 239.682 1.00 8.85  ? 3653 VAL A CB    1 
ATOM   15908 C  CG1   . VAL A 1 3653 ? 220.644 208.246 239.981 1.00 10.30 ? 3653 VAL A CG1   1 
ATOM   15909 C  CG2   . VAL A 1 3653 ? 222.707 206.978 240.552 1.00 7.37  ? 3653 VAL A CG2   1 
ATOM   15910 N  N     . ARG A 1 3654 ? 224.342 208.821 237.435 1.00 10.15 ? 3654 ARG A N     1 
ATOM   15911 C  CA    . ARG A 1 3654 ? 225.746 208.945 237.060 1.00 10.13 ? 3654 ARG A CA    1 
ATOM   15912 C  C     . ARG A 1 3654 ? 226.403 209.903 238.045 1.00 13.24 ? 3654 ARG A C     1 
ATOM   15913 O  O     . ARG A 1 3654 ? 226.075 211.093 238.074 1.00 17.21 ? 3654 ARG A O     1 
ATOM   15914 C  CB    . ARG A 1 3654 ? 225.876 209.416 235.608 1.00 13.68 ? 3654 ARG A CB    1 
ATOM   15915 C  CG    . ARG A 1 3654 ? 227.293 209.458 235.039 1.00 18.06 ? 3654 ARG A CG    1 
ATOM   15916 C  CD    . ARG A 1 3654 ? 228.004 210.771 235.327 1.00 24.65 ? 3654 ARG A CD    1 
ATOM   15917 N  NE    . ARG A 1 3654 ? 227.257 211.918 234.825 1.00 29.87 ? 3654 ARG A NE    1 
ATOM   15918 C  CZ    . ARG A 1 3654 ? 227.291 212.339 233.567 1.00 30.49 ? 3654 ARG A CZ    1 
ATOM   15919 N  NH1   . ARG A 1 3654 ? 228.038 211.737 232.656 1.00 30.25 ? 3654 ARG A NH1   1 
ATOM   15920 N  NH2   . ARG A 1 3654 ? 226.561 213.393 233.216 1.00 24.19 ? 3654 ARG A NH2   1 
ATOM   15921 N  N     . ARG A 1 3655 ? 227.322 209.380 238.856 1.00 13.46 ? 3655 ARG A N     1 
ATOM   15922 C  CA    . ARG A 1 3655 ? 228.004 210.167 239.882 1.00 14.56 ? 3655 ARG A CA    1 
ATOM   15923 C  C     . ARG A 1 3655 ? 229.415 210.486 239.409 1.00 21.35 ? 3655 ARG A C     1 
ATOM   15924 O  O     . ARG A 1 3655 ? 230.332 209.674 239.548 1.00 27.20 ? 3655 ARG A O     1 
ATOM   15925 C  CB    . ARG A 1 3655 ? 228.003 209.430 241.219 1.00 10.95 ? 3655 ARG A CB    1 
ATOM   15926 C  CG    . ARG A 1 3655 ? 226.638 209.406 241.888 1.00 14.37 ? 3655 ARG A CG    1 
ATOM   15927 C  CD    . ARG A 1 3655 ? 226.562 208.445 243.064 1.00 14.99 ? 3655 ARG A CD    1 
ATOM   15928 N  NE    . ARG A 1 3655 ? 225.269 208.543 243.731 1.00 16.53 ? 3655 ARG A NE    1 
ATOM   15929 C  CZ    . ARG A 1 3655 ? 224.379 207.564 243.808 1.00 18.91 ? 3655 ARG A CZ    1 
ATOM   15930 N  NH1   . ARG A 1 3655 ? 224.602 206.381 243.260 1.00 24.71 ? 3655 ARG A NH1   1 
ATOM   15931 N  NH2   . ARG A 1 3655 ? 223.232 207.777 244.448 1.00 17.86 ? 3655 ARG A NH2   1 
ATOM   15932 N  N     . THR A 1 3656 ? 229.586 211.680 238.845 1.00 24.61 ? 3656 THR A N     1 
ATOM   15933 C  CA    . THR A 1 3656 ? 230.881 212.163 238.393 1.00 25.71 ? 3656 THR A CA    1 
ATOM   15934 C  C     . THR A 1 3656 ? 231.019 213.633 238.760 1.00 24.61 ? 3656 THR A C     1 
ATOM   15935 O  O     . THR A 1 3656 ? 230.064 214.408 238.652 1.00 22.38 ? 3656 THR A O     1 
ATOM   15936 C  CB    . THR A 1 3656 ? 231.060 211.972 236.878 1.00 28.57 ? 3656 THR A CB    1 
ATOM   15937 O  OG1   . THR A 1 3656 ? 230.903 210.588 236.549 1.00 31.20 ? 3656 THR A OG1   1 
ATOM   15938 C  CG2   . THR A 1 3656 ? 232.439 212.437 236.429 1.00 25.00 ? 3656 THR A CG2   1 
ATOM   15939 N  N     . GLY A 1 3657 ? 232.217 214.008 239.197 1.00 28.27 ? 3657 GLY A N     1 
ATOM   15940 C  CA    . GLY A 1 3657 ? 232.493 215.394 239.540 1.00 20.72 ? 3657 GLY A CA    1 
ATOM   15941 C  C     . GLY A 1 3657 ? 231.744 215.890 240.755 1.00 16.08 ? 3657 GLY A C     1 
ATOM   15942 O  O     . GLY A 1 3657 ? 231.308 217.048 240.781 1.00 23.89 ? 3657 GLY A O     1 
ATOM   15943 N  N     . GLY A 1 3658 ? 231.584 215.040 241.766 1.00 18.62 ? 3658 GLY A N     1 
ATOM   15944 C  CA    . GLY A 1 3658 ? 230.873 215.433 242.971 1.00 15.15 ? 3658 GLY A CA    1 
ATOM   15945 C  C     . GLY A 1 3658 ? 229.407 215.724 242.750 1.00 16.99 ? 3658 GLY A C     1 
ATOM   15946 O  O     . GLY A 1 3658 ? 228.770 216.353 243.601 1.00 21.69 ? 3658 GLY A O     1 
ATOM   15947 N  N     . ARG A 1 3659 ? 228.851 215.275 241.631 1.00 12.91 ? 3659 ARG A N     1 
ATOM   15948 C  CA    . ARG A 1 3659 ? 227.469 215.554 241.270 1.00 12.13 ? 3659 ARG A CA    1 
ATOM   15949 C  C     . ARG A 1 3659 ? 226.750 214.248 240.974 1.00 14.46 ? 3659 ARG A C     1 
ATOM   15950 O  O     . ARG A 1 3659 ? 227.304 213.367 240.310 1.00 16.99 ? 3659 ARG A O     1 
ATOM   15951 C  CB    . ARG A 1 3659 ? 227.394 216.480 240.054 1.00 14.65 ? 3659 ARG A CB    1 
ATOM   15952 C  CG    . ARG A 1 3659 ? 227.691 217.933 240.332 1.00 14.37 ? 3659 ARG A CG    1 
ATOM   15953 C  CD    . ARG A 1 3659 ? 227.849 218.697 239.030 1.00 14.98 ? 3659 ARG A CD    1 
ATOM   15954 N  NE    . ARG A 1 3659 ? 226.571 218.911 238.364 1.00 11.58 ? 3659 ARG A NE    1 
ATOM   15955 C  CZ    . ARG A 1 3659 ? 226.381 218.810 237.056 1.00 13.61 ? 3659 ARG A CZ    1 
ATOM   15956 N  NH1   . ARG A 1 3659 ? 227.371 218.496 236.236 1.00 13.94 ? 3659 ARG A NH1   1 
ATOM   15957 N  NH2   . ARG A 1 3659 ? 225.169 219.033 236.558 1.00 11.60 ? 3659 ARG A NH2   1 
ATOM   15958 N  N     . VAL A 1 3660 ? 225.520 214.129 241.459 1.00 14.95 ? 3660 VAL A N     1 
ATOM   15959 C  CA    . VAL A 1 3660 ? 224.675 212.973 241.180 1.00 11.27 ? 3660 VAL A CA    1 
ATOM   15960 C  C     . VAL A 1 3660 ? 223.676 213.373 240.103 1.00 8.34  ? 3660 VAL A C     1 
ATOM   15961 O  O     . VAL A 1 3660 ? 222.790 214.200 240.346 1.00 13.78 ? 3660 VAL A O     1 
ATOM   15962 C  CB    . VAL A 1 3660 ? 223.961 212.488 242.449 1.00 8.24  ? 3660 VAL A CB    1 
ATOM   15963 C  CG1   . VAL A 1 3660 ? 223.158 211.233 242.162 1.00 7.05  ? 3660 VAL A CG1   1 
ATOM   15964 C  CG2   . VAL A 1 3660 ? 224.968 212.249 243.562 1.00 9.42  ? 3660 VAL A CG2   1 
ATOM   15965 N  N     . LEU A 1 3661 ? 223.809 212.785 238.919 1.00 5.59  ? 3661 LEU A N     1 
ATOM   15966 C  CA    . LEU A 1 3661 ? 223.041 213.192 237.751 1.00 8.21  ? 3661 LEU A CA    1 
ATOM   15967 C  C     . LEU A 1 3661 ? 222.082 212.092 237.323 1.00 9.17  ? 3661 LEU A C     1 
ATOM   15968 O  O     . LEU A 1 3661 ? 222.433 210.909 237.328 1.00 12.89 ? 3661 LEU A O     1 
ATOM   15969 C  CB    . LEU A 1 3661 ? 223.955 213.551 236.575 1.00 13.12 ? 3661 LEU A CB    1 
ATOM   15970 C  CG    . LEU A 1 3661 ? 224.467 214.990 236.457 1.00 10.81 ? 3661 LEU A CG    1 
ATOM   15971 C  CD1   . LEU A 1 3661 ? 223.346 215.940 236.088 1.00 14.15 ? 3661 LEU A CD1   1 
ATOM   15972 C  CD2   . LEU A 1 3661 ? 225.135 215.441 237.725 1.00 9.36  ? 3661 LEU A CD2   1 
ATOM   15973 N  N     . ILE A 1 3662 ? 220.871 212.494 236.952 1.00 11.97 ? 3662 ILE A N     1 
ATOM   15974 C  CA    . ILE A 1 3662 ? 219.873 211.604 236.372 1.00 6.86  ? 3662 ILE A CA    1 
ATOM   15975 C  C     . ILE A 1 3662 ? 219.507 212.159 235.002 1.00 6.58  ? 3662 ILE A C     1 
ATOM   15976 O  O     . ILE A 1 3662 ? 219.236 213.356 234.863 1.00 11.44 ? 3662 ILE A O     1 
ATOM   15977 C  CB    . ILE A 1 3662 ? 218.635 211.466 237.282 1.00 7.47  ? 3662 ILE A CB    1 
ATOM   15978 C  CG1   . ILE A 1 3662 ? 217.586 210.552 236.646 1.00 7.09  ? 3662 ILE A CG1   1 
ATOM   15979 C  CG2   . ILE A 1 3662 ? 218.047 212.829 237.638 1.00 6.66  ? 3662 ILE A CG2   1 
ATOM   15980 C  CD1   . ILE A 1 3662 ? 217.966 209.092 236.666 1.00 7.55  ? 3662 ILE A CD1   1 
ATOM   15981 N  N     . THR A 1 3663 ? 219.533 211.299 233.988 1.00 9.07  ? 3663 THR A N     1 
ATOM   15982 C  CA    . THR A 1 3663 ? 219.308 211.729 232.610 1.00 12.13 ? 3663 THR A CA    1 
ATOM   15983 C  C     . THR A 1 3663 ? 217.818 211.620 232.311 1.00 12.04 ? 3663 THR A C     1 
ATOM   15984 O  O     . THR A 1 3663 ? 217.296 210.527 232.082 1.00 14.16 ? 3663 THR A O     1 
ATOM   15985 C  CB    . THR A 1 3663 ? 220.138 210.899 231.639 1.00 14.88 ? 3663 THR A CB    1 
ATOM   15986 O  OG1   . THR A 1 3663 ? 221.525 211.016 231.977 1.00 17.82 ? 3663 THR A OG1   1 
ATOM   15987 C  CG2   . THR A 1 3663 ? 219.932 211.390 230.214 1.00 15.35 ? 3663 THR A CG2   1 
ATOM   15988 N  N     . LEU A 1 3664 ? 217.131 212.759 232.313 1.00 9.34  ? 3664 LEU A N     1 
ATOM   15989 C  CA    . LEU A 1 3664 ? 215.700 212.824 232.032 1.00 9.08  ? 3664 LEU A CA    1 
ATOM   15990 C  C     . LEU A 1 3664 ? 215.533 213.336 230.607 1.00 12.01 ? 3664 LEU A C     1 
ATOM   15991 O  O     . LEU A 1 3664 ? 215.683 214.531 230.343 1.00 13.09 ? 3664 LEU A O     1 
ATOM   15992 C  CB    . LEU A 1 3664 ? 214.987 213.721 233.037 1.00 6.33  ? 3664 LEU A CB    1 
ATOM   15993 C  CG    . LEU A 1 3664 ? 213.466 213.723 232.915 1.00 5.33  ? 3664 LEU A CG    1 
ATOM   15994 C  CD1   . LEU A 1 3664 ? 212.923 212.393 233.393 1.00 4.86  ? 3664 LEU A CD1   1 
ATOM   15995 C  CD2   . LEU A 1 3664 ? 212.848 214.875 233.689 1.00 6.50  ? 3664 LEU A CD2   1 
ATOM   15996 N  N     . GLY A 1 3665 ? 215.205 212.431 229.691 1.00 12.69 ? 3665 GLY A N     1 
ATOM   15997 C  CA    . GLY A 1 3665 ? 215.210 212.767 228.283 1.00 11.19 ? 3665 GLY A CA    1 
ATOM   15998 C  C     . GLY A 1 3665 ? 216.610 213.076 227.797 1.00 14.91 ? 3665 GLY A C     1 
ATOM   15999 O  O     . GLY A 1 3665 ? 217.525 212.266 227.968 1.00 25.52 ? 3665 GLY A O     1 
ATOM   16000 N  N     . ASP A 1 3666 ? 216.793 214.245 227.190 1.00 18.53 ? 3666 ASP A N     1 
ATOM   16001 C  CA    . ASP A 1 3666 ? 218.098 214.689 226.724 1.00 18.71 ? 3666 ASP A CA    1 
ATOM   16002 C  C     . ASP A 1 3666 ? 218.753 215.695 227.663 1.00 20.95 ? 3666 ASP A C     1 
ATOM   16003 O  O     . ASP A 1 3666 ? 219.821 216.221 227.336 1.00 25.04 ? 3666 ASP A O     1 
ATOM   16004 C  CB    . ASP A 1 3666 ? 217.977 215.294 225.324 1.00 25.81 ? 3666 ASP A CB    1 
ATOM   16005 C  CG    . ASP A 1 3666 ? 217.106 216.532 225.303 1.00 32.05 ? 3666 ASP A CG    1 
ATOM   16006 O  OD1   . ASP A 1 3666 ? 215.944 216.446 225.752 1.00 28.14 ? 3666 ASP A OD1   1 
ATOM   16007 O  OD2   . ASP A 1 3666 ? 217.583 217.590 224.840 1.00 31.84 ? 3666 ASP A OD2   1 
ATOM   16008 N  N     . GLN A 1 3667 ? 218.146 215.972 228.811 1.00 16.28 ? 3667 GLN A N     1 
ATOM   16009 C  CA    . GLN A 1 3667 ? 218.658 216.940 229.769 1.00 15.92 ? 3667 GLN A CA    1 
ATOM   16010 C  C     . GLN A 1 3667 ? 219.088 216.221 231.039 1.00 17.54 ? 3667 GLN A C     1 
ATOM   16011 O  O     . GLN A 1 3667 ? 218.332 215.409 231.581 1.00 24.38 ? 3667 GLN A O     1 
ATOM   16012 C  CB    . GLN A 1 3667 ? 217.600 217.998 230.092 1.00 21.25 ? 3667 GLN A CB    1 
ATOM   16013 C  CG    . GLN A 1 3667 ? 218.079 219.102 231.020 1.00 24.39 ? 3667 GLN A CG    1 
ATOM   16014 C  CD    . GLN A 1 3667 ? 217.017 220.156 231.266 1.00 32.28 ? 3667 GLN A CD    1 
ATOM   16015 O  OE1   . GLN A 1 3667 ? 215.895 220.050 230.772 1.00 35.44 ? 3667 GLN A OE1   1 
ATOM   16016 N  NE2   . GLN A 1 3667 ? 217.366 221.181 232.035 1.00 36.59 ? 3667 GLN A NE2   1 
ATOM   16017 N  N     . ASP A 1 3668 ? 220.299 216.514 231.505 1.00 11.33 ? 3668 ASP A N     1 
ATOM   16018 C  CA    . ASP A 1 3668 ? 220.790 215.953 232.753 1.00 11.70 ? 3668 ASP A CA    1 
ATOM   16019 C  C     . ASP A 1 3668 ? 220.372 216.823 233.936 1.00 10.67 ? 3668 ASP A C     1 
ATOM   16020 O  O     . ASP A 1 3668 ? 220.418 218.054 233.871 1.00 16.48 ? 3668 ASP A O     1 
ATOM   16021 C  CB    . ASP A 1 3668 ? 222.312 215.763 232.707 1.00 18.96 ? 3668 ASP A CB    1 
ATOM   16022 C  CG    . ASP A 1 3668 ? 223.081 217.063 232.483 1.00 30.90 ? 3668 ASP A CG    1 
ATOM   16023 O  OD1   . ASP A 1 3668 ? 222.464 218.130 232.290 1.00 40.72 ? 3668 ASP A OD1   1 
ATOM   16024 O  OD2   . ASP A 1 3668 ? 224.328 217.013 232.502 1.00 28.09 ? 3668 ASP A OD2   1 
ATOM   16025 N  N     . ILE A 1 3669 ? 219.932 216.171 235.007 1.00 8.40  ? 3669 ILE A N     1 
ATOM   16026 C  CA    . ILE A 1 3669 ? 219.392 216.849 236.179 1.00 4.83  ? 3669 ILE A CA    1 
ATOM   16027 C  C     . ILE A 1 3669 ? 220.113 216.337 237.415 1.00 7.11  ? 3669 ILE A C     1 
ATOM   16028 O  O     . ILE A 1 3669 ? 220.344 215.132 237.554 1.00 9.90  ? 3669 ILE A O     1 
ATOM   16029 C  CB    . ILE A 1 3669 ? 217.868 216.633 236.314 1.00 7.07  ? 3669 ILE A CB    1 
ATOM   16030 C  CG1   . ILE A 1 3669 ? 217.158 216.985 235.008 1.00 8.59  ? 3669 ILE A CG1   1 
ATOM   16031 C  CG2   . ILE A 1 3669 ? 217.304 217.452 237.464 1.00 6.03  ? 3669 ILE A CG2   1 
ATOM   16032 C  CD1   . ILE A 1 3669 ? 215.687 216.702 235.029 1.00 7.93  ? 3669 ILE A CD1   1 
ATOM   16033 N  N     . ASP A 1 3670 ? 220.474 217.254 238.307 1.00 6.80  ? 3670 ASP A N     1 
ATOM   16034 C  CA    . ASP A 1 3670 ? 221.032 216.866 239.595 1.00 8.67  ? 3670 ASP A CA    1 
ATOM   16035 C  C     . ASP A 1 3670 ? 219.938 216.241 240.452 1.00 8.79  ? 3670 ASP A C     1 
ATOM   16036 O  O     . ASP A 1 3670 ? 218.889 216.852 240.676 1.00 10.06 ? 3670 ASP A O     1 
ATOM   16037 C  CB    . ASP A 1 3670 ? 221.641 218.079 240.292 1.00 10.60 ? 3670 ASP A CB    1 
ATOM   16038 C  CG    . ASP A 1 3670 ? 222.740 218.726 239.476 1.00 19.61 ? 3670 ASP A CG    1 
ATOM   16039 O  OD1   . ASP A 1 3670 ? 223.734 218.038 239.167 1.00 18.01 ? 3670 ASP A OD1   1 
ATOM   16040 O  OD2   . ASP A 1 3670 ? 222.610 219.922 239.142 1.00 29.54 ? 3670 ASP A OD2   1 
ATOM   16041 N  N     . LEU A 1 3671 ? 220.181 215.024 240.930 1.00 11.46 ? 3671 LEU A N     1 
ATOM   16042 C  CA    . LEU A 1 3671 ? 219.190 214.275 241.692 1.00 5.58  ? 3671 LEU A CA    1 
ATOM   16043 C  C     . LEU A 1 3671 ? 219.397 214.510 243.182 1.00 6.21  ? 3671 LEU A C     1 
ATOM   16044 O  O     . LEU A 1 3671 ? 220.450 214.170 243.730 1.00 7.62  ? 3671 LEU A O     1 
ATOM   16045 C  CB    . LEU A 1 3671 ? 219.278 212.784 241.372 1.00 6.97  ? 3671 LEU A CB    1 
ATOM   16046 C  CG    . LEU A 1 3671 ? 218.332 211.900 242.187 1.00 5.69  ? 3671 LEU A CG    1 
ATOM   16047 C  CD1   . LEU A 1 3671 ? 216.888 212.251 241.894 1.00 4.34  ? 3671 LEU A CD1   1 
ATOM   16048 C  CD2   . LEU A 1 3671 ? 218.595 210.433 241.926 1.00 6.90  ? 3671 LEU A CD2   1 
ATOM   16049 N  N     . SER A 1 3672 ? 218.398 215.093 243.831 1.00 6.61  ? 3672 SER A N     1 
ATOM   16050 C  CA    . SER A 1 3672 ? 218.451 215.247 245.277 1.00 5.21  ? 3672 SER A CA    1 
ATOM   16051 C  C     . SER A 1 3672 ? 218.095 213.925 245.957 1.00 6.95  ? 3672 SER A C     1 
ATOM   16052 O  O     . SER A 1 3672 ? 217.210 213.205 245.489 1.00 9.07  ? 3672 SER A O     1 
ATOM   16053 C  CB    . SER A 1 3672 ? 217.502 216.346 245.733 1.00 6.67  ? 3672 SER A CB    1 
ATOM   16054 O  OG    . SER A 1 3672 ? 217.287 216.292 247.132 1.00 12.48 ? 3672 SER A OG    1 
ATOM   16055 N  N     . PRO A 1 3673 ? 218.774 213.578 247.054 1.00 7.26  ? 3673 PRO A N     1 
ATOM   16056 C  CA    . PRO A 1 3673 ? 218.517 212.283 247.704 1.00 4.50  ? 3673 PRO A CA    1 
ATOM   16057 C  C     . PRO A 1 3673 ? 217.163 212.183 248.385 1.00 6.46  ? 3673 PRO A C     1 
ATOM   16058 O  O     . PRO A 1 3673 ? 216.743 211.066 248.715 1.00 12.29 ? 3673 PRO A O     1 
ATOM   16059 C  CB    . PRO A 1 3673 ? 219.659 212.175 248.720 1.00 7.37  ? 3673 PRO A CB    1 
ATOM   16060 C  CG    . PRO A 1 3673 ? 220.011 213.585 249.022 1.00 8.59  ? 3673 PRO A CG    1 
ATOM   16061 C  CD    . PRO A 1 3673 ? 219.843 214.330 247.731 1.00 6.20  ? 3673 PRO A CD    1 
ATOM   16062 N  N     . SER A 1 3674 ? 216.469 213.292 248.612 1.00 8.98  ? 3674 SER A N     1 
ATOM   16063 C  CA    . SER A 1 3674 ? 215.168 213.262 249.263 1.00 5.28  ? 3674 SER A CA    1 
ATOM   16064 C  C     . SER A 1 3674 ? 214.021 213.039 248.287 1.00 7.85  ? 3674 SER A C     1 
ATOM   16065 O  O     . SER A 1 3674 ? 212.864 213.002 248.716 1.00 9.02  ? 3674 SER A O     1 
ATOM   16066 C  CB    . SER A 1 3674 ? 214.937 214.559 250.043 1.00 6.26  ? 3674 SER A CB    1 
ATOM   16067 O  OG    . SER A 1 3674 ? 215.269 215.692 249.263 1.00 15.66 ? 3674 SER A OG    1 
ATOM   16068 N  N     . PHE A 1 3675 ? 214.309 212.888 246.998 1.00 6.64  ? 3675 PHE A N     1 
ATOM   16069 C  CA    . PHE A 1 3675 ? 213.256 212.683 246.016 1.00 1.56  ? 3675 PHE A CA    1 
ATOM   16070 C  C     . PHE A 1 3675 ? 212.599 211.320 246.199 1.00 0.74  ? 3675 PHE A C     1 
ATOM   16071 O  O     . PHE A 1 3675 ? 213.264 210.321 246.482 1.00 2.17  ? 3675 PHE A O     1 
ATOM   16072 C  CB    . PHE A 1 3675 ? 213.809 212.807 244.595 1.00 1.92  ? 3675 PHE A CB    1 
ATOM   16073 C  CG    . PHE A 1 3675 ? 212.914 212.211 243.543 1.00 0.56  ? 3675 PHE A CG    1 
ATOM   16074 C  CD1   . PHE A 1 3675 ? 211.877 212.949 243.003 1.00 0.44  ? 3675 PHE A CD1   1 
ATOM   16075 C  CD2   . PHE A 1 3675 ? 213.106 210.913 243.098 1.00 0.21  ? 3675 PHE A CD2   1 
ATOM   16076 C  CE1   . PHE A 1 3675 ? 211.052 212.408 242.046 1.00 0.30  ? 3675 PHE A CE1   1 
ATOM   16077 C  CE2   . PHE A 1 3675 ? 212.279 210.366 242.141 1.00 0.23  ? 3675 PHE A CE2   1 
ATOM   16078 C  CZ    . PHE A 1 3675 ? 211.254 211.115 241.613 1.00 0.15  ? 3675 PHE A CZ    1 
ATOM   16079 N  N     . VAL A 1 3676 ? 211.284 211.289 246.024 1.00 0.46  ? 3676 VAL A N     1 
ATOM   16080 C  CA    . VAL A 1 3676 ? 210.517 210.049 246.007 1.00 0.31  ? 3676 VAL A CA    1 
ATOM   16081 C  C     . VAL A 1 3676 ? 209.314 210.261 245.102 1.00 0.34  ? 3676 VAL A C     1 
ATOM   16082 O  O     . VAL A 1 3676 ? 208.781 211.369 245.009 1.00 0.57  ? 3676 VAL A O     1 
ATOM   16083 C  CB    . VAL A 1 3676 ? 210.113 209.610 247.434 1.00 0.40  ? 3676 VAL A CB    1 
ATOM   16084 C  CG1   . VAL A 1 3676 ? 209.180 210.616 248.069 1.00 0.66  ? 3676 VAL A CG1   1 
ATOM   16085 C  CG2   . VAL A 1 3676 ? 209.466 208.244 247.408 1.00 0.25  ? 3676 VAL A CG2   1 
ATOM   16086 N  N     . ILE A 1 3677 ? 208.909 209.204 244.405 1.00 0.28  ? 3677 ILE A N     1 
ATOM   16087 C  CA    . ILE A 1 3677 ? 207.807 209.264 243.456 1.00 0.18  ? 3677 ILE A CA    1 
ATOM   16088 C  C     . ILE A 1 3677 ? 206.838 208.128 243.753 1.00 0.20  ? 3677 ILE A C     1 
ATOM   16089 O  O     . ILE A 1 3677 ? 207.258 206.991 243.992 1.00 0.25  ? 3677 ILE A O     1 
ATOM   16090 C  CB    . ILE A 1 3677 ? 208.309 209.202 241.998 1.00 0.23  ? 3677 ILE A CB    1 
ATOM   16091 C  CG1   . ILE A 1 3677 ? 207.137 209.226 241.016 1.00 0.11  ? 3677 ILE A CG1   1 
ATOM   16092 C  CG2   . ILE A 1 3677 ? 209.210 207.992 241.775 1.00 0.10  ? 3677 ILE A CG2   1 
ATOM   16093 C  CD1   . ILE A 1 3677 ? 207.532 209.635 239.618 1.00 0.13  ? 3677 ILE A CD1   1 
ATOM   16094 N  N     . PHE A 1 3678 ? 205.546 208.442 243.759 1.00 0.26  ? 3678 PHE A N     1 
ATOM   16095 C  CA    . PHE A 1 3678 ? 204.486 207.454 243.898 1.00 0.13  ? 3678 PHE A CA    1 
ATOM   16096 C  C     . PHE A 1 3678 ? 203.620 207.488 242.648 1.00 0.25  ? 3678 PHE A C     1 
ATOM   16097 O  O     . PHE A 1 3678 ? 203.179 208.559 242.226 1.00 1.39  ? 3678 PHE A O     1 
ATOM   16098 C  CB    . PHE A 1 3678 ? 203.625 207.720 245.138 1.00 0.22  ? 3678 PHE A CB    1 
ATOM   16099 C  CG    . PHE A 1 3678 ? 204.386 207.673 246.430 1.00 0.16  ? 3678 PHE A CG    1 
ATOM   16100 C  CD1   . PHE A 1 3678 ? 204.982 208.813 246.941 1.00 0.12  ? 3678 PHE A CD1   1 
ATOM   16101 C  CD2   . PHE A 1 3678 ? 204.498 206.490 247.139 1.00 0.11  ? 3678 PHE A CD2   1 
ATOM   16102 C  CE1   . PHE A 1 3678 ? 205.680 208.773 248.129 1.00 0.27  ? 3678 PHE A CE1   1 
ATOM   16103 C  CE2   . PHE A 1 3678 ? 205.194 206.444 248.330 1.00 0.19  ? 3678 PHE A CE2   1 
ATOM   16104 C  CZ    . PHE A 1 3678 ? 205.785 207.587 248.826 1.00 0.21  ? 3678 PHE A CZ    1 
ATOM   16105 N  N     . LEU A 1 3679 ? 203.385 206.321 242.062 1.00 0.26  ? 3679 LEU A N     1 
ATOM   16106 C  CA    . LEU A 1 3679 ? 202.494 206.179 240.922 1.00 0.31  ? 3679 LEU A CA    1 
ATOM   16107 C  C     . LEU A 1 3679 ? 201.171 205.589 241.390 1.00 0.62  ? 3679 LEU A C     1 
ATOM   16108 O  O     . LEU A 1 3679 ? 201.150 204.687 242.231 1.00 2.23  ? 3679 LEU A O     1 
ATOM   16109 C  CB    . LEU A 1 3679 ? 203.116 205.292 239.841 1.00 0.20  ? 3679 LEU A CB    1 
ATOM   16110 C  CG    . LEU A 1 3679 ? 204.571 205.584 239.462 1.00 0.35  ? 3679 LEU A CG    1 
ATOM   16111 C  CD1   . LEU A 1 3679 ? 205.017 204.689 238.318 1.00 0.39  ? 3679 LEU A CD1   1 
ATOM   16112 C  CD2   . LEU A 1 3679 ? 204.766 207.052 239.107 1.00 0.21  ? 3679 LEU A CD2   1 
ATOM   16113 N  N     . SER A 1 3680 ? 200.070 206.104 240.853 1.00 0.90  ? 3680 SER A N     1 
ATOM   16114 C  CA    . SER A 1 3680 ? 198.751 205.679 241.293 1.00 0.85  ? 3680 SER A CA    1 
ATOM   16115 C  C     . SER A 1 3680 ? 197.825 205.493 240.102 1.00 1.40  ? 3680 SER A C     1 
ATOM   16116 O  O     . SER A 1 3680 ? 197.952 206.168 239.078 1.00 1.72  ? 3680 SER A O     1 
ATOM   16117 C  CB    . SER A 1 3680 ? 198.138 206.681 242.279 1.00 1.32  ? 3680 SER A CB    1 
ATOM   16118 O  OG    . SER A 1 3680 ? 198.191 207.999 241.768 1.00 3.68  ? 3680 SER A OG    1 
ATOM   16119 N  N     . THR A 1 3681 ? 196.892 204.559 240.255 1.00 1.70  ? 3681 THR A N     1 
ATOM   16120 C  CA    . THR A 1 3681 ? 195.801 204.361 239.315 1.00 1.65  ? 3681 THR A CA    1 
ATOM   16121 C  C     . THR A 1 3681 ? 194.537 204.045 240.098 1.00 1.21  ? 3681 THR A C     1 
ATOM   16122 O  O     . THR A 1 3681 ? 194.594 203.503 241.204 1.00 1.96  ? 3681 THR A O     1 
ATOM   16123 C  CB    . THR A 1 3681 ? 196.088 203.232 238.311 1.00 3.44  ? 3681 THR A CB    1 
ATOM   16124 O  OG1   . THR A 1 3681 ? 194.960 203.060 237.446 1.00 4.00  ? 3681 THR A OG1   1 
ATOM   16125 C  CG2   . THR A 1 3681 ? 196.369 201.923 239.032 1.00 1.58  ? 3681 THR A CG2   1 
ATOM   16126 N  N     . ARG A 1 3682 ? 193.394 204.399 239.520 1.00 3.78  ? 3682 ARG A N     1 
ATOM   16127 C  CA    . ARG A 1 3682 ? 192.102 204.072 240.101 1.00 3.90  ? 3682 ARG A CA    1 
ATOM   16128 C  C     . ARG A 1 3682 ? 191.444 202.873 239.434 1.00 3.89  ? 3682 ARG A C     1 
ATOM   16129 O  O     . ARG A 1 3682 ? 190.329 202.505 239.812 1.00 9.16  ? 3682 ARG A O     1 
ATOM   16130 C  CB    . ARG A 1 3682 ? 191.170 205.285 240.028 1.00 1.97  ? 3682 ARG A CB    1 
ATOM   16131 C  CG    . ARG A 1 3682 ? 191.562 206.421 240.954 1.00 2.19  ? 3682 ARG A CG    1 
ATOM   16132 C  CD    . ARG A 1 3682 ? 190.548 207.548 240.902 1.00 2.16  ? 3682 ARG A CD    1 
ATOM   16133 N  NE    . ARG A 1 3682 ? 190.552 208.219 239.607 1.00 4.32  ? 3682 ARG A NE    1 
ATOM   16134 C  CZ    . ARG A 1 3682 ? 189.593 208.099 238.700 1.00 6.17  ? 3682 ARG A CZ    1 
ATOM   16135 N  NH1   . ARG A 1 3682 ? 188.536 207.333 238.909 1.00 5.54  ? 3682 ARG A NH1   1 
ATOM   16136 N  NH2   . ARG A 1 3682 ? 189.702 208.759 237.552 1.00 8.52  ? 3682 ARG A NH2   1 
ATOM   16137 N  N     . ASP A 1 3683 ? 192.107 202.254 238.459 1.00 3.43  ? 3683 ASP A N     1 
ATOM   16138 C  CA    . ASP A 1 3683 ? 191.529 201.137 237.731 1.00 4.42  ? 3683 ASP A CA    1 
ATOM   16139 C  C     . ASP A 1 3683 ? 192.149 199.844 238.236 1.00 6.56  ? 3683 ASP A C     1 
ATOM   16140 O  O     . ASP A 1 3683 ? 193.329 199.588 237.959 1.00 8.49  ? 3683 ASP A O     1 
ATOM   16141 C  CB    . ASP A 1 3683 ? 191.775 201.299 236.231 1.00 4.56  ? 3683 ASP A CB    1 
ATOM   16142 C  CG    . ASP A 1 3683 ? 190.959 200.335 235.390 1.00 9.98  ? 3683 ASP A CG    1 
ATOM   16143 O  OD1   . ASP A 1 3683 ? 190.618 199.235 235.870 1.00 17.15 ? 3683 ASP A OD1   1 
ATOM   16144 O  OD2   . ASP A 1 3683 ? 190.654 200.684 234.231 1.00 12.26 ? 3683 ASP A OD2   1 
ATOM   16145 N  N     . PRO A 1 3684 ? 191.416 199.009 238.977 1.00 6.94  ? 3684 PRO A N     1 
ATOM   16146 C  CA    . PRO A 1 3684 ? 191.979 197.720 239.406 1.00 7.80  ? 3684 PRO A CA    1 
ATOM   16147 C  C     . PRO A 1 3684 ? 192.169 196.729 238.272 1.00 10.73 ? 3684 PRO A C     1 
ATOM   16148 O  O     . PRO A 1 3684 ? 192.909 195.753 238.447 1.00 15.82 ? 3684 PRO A O     1 
ATOM   16149 C  CB    . PRO A 1 3684 ? 190.949 197.212 240.420 1.00 11.13 ? 3684 PRO A CB    1 
ATOM   16150 C  CG    . PRO A 1 3684 ? 189.673 197.841 239.986 1.00 11.12 ? 3684 PRO A CG    1 
ATOM   16151 C  CD    . PRO A 1 3684 ? 190.042 199.201 239.468 1.00 6.59  ? 3684 PRO A CD    1 
ATOM   16152 N  N     . THR A 1 3685 ? 191.533 196.947 237.124 1.00 9.43  ? 3685 THR A N     1 
ATOM   16153 C  CA    . THR A 1 3685 ? 191.574 196.019 236.005 1.00 7.17  ? 3685 THR A CA    1 
ATOM   16154 C  C     . THR A 1 3685 ? 192.627 196.378 234.968 1.00 9.11  ? 3685 THR A C     1 
ATOM   16155 O  O     . THR A 1 3685 ? 192.712 195.705 233.935 1.00 19.79 ? 3685 THR A O     1 
ATOM   16156 C  CB    . THR A 1 3685 ? 190.197 195.951 235.329 1.00 10.39 ? 3685 THR A CB    1 
ATOM   16157 O  OG1   . THR A 1 3685 ? 190.046 197.061 234.437 1.00 14.50 ? 3685 THR A OG1   1 
ATOM   16158 C  CG2   . THR A 1 3685 ? 189.096 195.991 236.370 1.00 13.17 ? 3685 THR A CG2   1 
ATOM   16159 N  N     . VAL A 1 3686 ? 193.428 197.414 235.208 1.00 8.36  ? 3686 VAL A N     1 
ATOM   16160 C  CA    . VAL A 1 3686 ? 194.430 197.827 234.234 1.00 6.67  ? 3686 VAL A CA    1 
ATOM   16161 C  C     . VAL A 1 3686 ? 195.551 196.796 234.184 1.00 7.71  ? 3686 VAL A C     1 
ATOM   16162 O  O     . VAL A 1 3686 ? 195.929 196.209 235.206 1.00 8.79  ? 3686 VAL A O     1 
ATOM   16163 C  CB    . VAL A 1 3686 ? 194.957 199.232 234.570 1.00 8.64  ? 3686 VAL A CB    1 
ATOM   16164 C  CG1   . VAL A 1 3686 ? 195.696 199.231 235.893 1.00 6.63  ? 3686 VAL A CG1   1 
ATOM   16165 C  CG2   . VAL A 1 3686 ? 195.854 199.747 233.454 1.00 9.51  ? 3686 VAL A CG2   1 
ATOM   16166 N  N     . GLU A 1 3687 ? 196.066 196.550 232.983 1.00 10.49 ? 3687 GLU A N     1 
ATOM   16167 C  CA    . GLU A 1 3687 ? 197.146 195.594 232.784 1.00 6.93  ? 3687 GLU A CA    1 
ATOM   16168 C  C     . GLU A 1 3687 ? 198.453 196.347 232.576 1.00 4.73  ? 3687 GLU A C     1 
ATOM   16169 O  O     . GLU A 1 3687 ? 198.524 197.260 231.748 1.00 11.46 ? 3687 GLU A O     1 
ATOM   16170 C  CB    . GLU A 1 3687 ? 196.861 194.693 231.582 1.00 9.19  ? 3687 GLU A CB    1 
ATOM   16171 C  CG    . GLU A 1 3687 ? 195.435 194.183 231.510 1.00 16.00 ? 3687 GLU A CG    1 
ATOM   16172 C  CD    . GLU A 1 3687 ? 195.279 192.786 232.075 1.00 21.51 ? 3687 GLU A CD    1 
ATOM   16173 O  OE1   . GLU A 1 3687 ? 196.233 192.287 232.707 1.00 24.15 ? 3687 GLU A OE1   1 
ATOM   16174 O  OE2   . GLU A 1 3687 ? 194.202 192.186 231.887 1.00 27.88 ? 3687 GLU A OE2   1 
ATOM   16175 N  N     . PHE A 1 3688 ? 199.475 195.972 233.331 1.00 4.23  ? 3688 PHE A N     1 
ATOM   16176 C  CA    . PHE A 1 3688 ? 200.668 196.715 232.970 1.00 4.45  ? 3688 PHE A CA    1 
ATOM   16177 C  C     . PHE A 1 3688 ? 201.636 195.837 232.192 1.00 7.81  ? 3688 PHE A C     1 
ATOM   16178 O  O     . PHE A 1 3688 ? 201.677 194.619 232.402 1.00 8.67  ? 3688 PHE A O     1 
ATOM   16179 C  CB    . PHE A 1 3688 ? 201.369 197.271 234.212 1.00 4.01  ? 3688 PHE A CB    1 
ATOM   16180 C  CG    . PHE A 1 3688 ? 200.527 198.222 235.006 1.00 4.84  ? 3688 PHE A CG    1 
ATOM   16181 C  CD1   . PHE A 1 3688 ? 200.419 199.548 234.628 1.00 3.79  ? 3688 PHE A CD1   1 
ATOM   16182 C  CD2   . PHE A 1 3688 ? 199.858 197.800 236.138 1.00 3.32  ? 3688 PHE A CD2   1 
ATOM   16183 C  CE1   . PHE A 1 3688 ? 199.651 200.426 235.355 1.00 3.43  ? 3688 PHE A CE1   1 
ATOM   16184 C  CE2   . PHE A 1 3688 ? 199.089 198.674 236.872 1.00 2.26  ? 3688 PHE A CE2   1 
ATOM   16185 C  CZ    . PHE A 1 3688 ? 198.988 199.990 236.481 1.00 3.15  ? 3688 PHE A CZ    1 
ATOM   16186 N  N     . PRO A 1 3689 ? 202.409 196.431 231.281 1.00 6.84  ? 3689 PRO A N     1 
ATOM   16187 C  CA    . PRO A 1 3689 ? 203.402 195.649 230.551 1.00 6.14  ? 3689 PRO A CA    1 
ATOM   16188 C  C     . PRO A 1 3689 ? 204.492 195.156 231.483 1.00 4.26  ? 3689 PRO A C     1 
ATOM   16189 O  O     . PRO A 1 3689 ? 204.753 195.764 232.535 1.00 6.26  ? 3689 PRO A O     1 
ATOM   16190 C  CB    . PRO A 1 3689 ? 203.948 196.652 229.519 1.00 5.73  ? 3689 PRO A CB    1 
ATOM   16191 C  CG    . PRO A 1 3689 ? 203.734 197.975 230.159 1.00 5.56  ? 3689 PRO A CG    1 
ATOM   16192 C  CD    . PRO A 1 3689 ? 202.417 197.846 230.871 1.00 5.77  ? 3689 PRO A CD    1 
ATOM   16193 N  N     . PRO A 1 3690 ? 205.146 194.040 231.150 1.00 7.53  ? 3690 PRO A N     1 
ATOM   16194 C  CA    . PRO A 1 3690 ? 206.147 193.469 232.067 1.00 5.38  ? 3690 PRO A CA    1 
ATOM   16195 C  C     . PRO A 1 3690 ? 207.294 194.408 232.398 1.00 3.90  ? 3690 PRO A C     1 
ATOM   16196 O  O     . PRO A 1 3690 ? 207.867 194.304 233.490 1.00 3.32  ? 3690 PRO A O     1 
ATOM   16197 C  CB    . PRO A 1 3690 ? 206.637 192.226 231.312 1.00 5.15  ? 3690 PRO A CB    1 
ATOM   16198 C  CG    . PRO A 1 3690 ? 205.495 191.864 230.424 1.00 6.85  ? 3690 PRO A CG    1 
ATOM   16199 C  CD    . PRO A 1 3690 ? 204.918 193.175 229.980 1.00 6.71  ? 3690 PRO A CD    1 
ATOM   16200 N  N     . ASP A 1 3691 ? 207.658 195.312 231.486 1.00 4.14  ? 3691 ASP A N     1 
ATOM   16201 C  CA    . ASP A 1 3691 ? 208.752 196.239 231.761 1.00 5.85  ? 3691 ASP A CA    1 
ATOM   16202 C  C     . ASP A 1 3691 ? 208.404 197.189 232.903 1.00 5.19  ? 3691 ASP A C     1 
ATOM   16203 O  O     . ASP A 1 3691 ? 209.248 197.484 233.757 1.00 5.77  ? 3691 ASP A O     1 
ATOM   16204 C  CB    . ASP A 1 3691 ? 209.125 197.004 230.485 1.00 7.52  ? 3691 ASP A CB    1 
ATOM   16205 C  CG    . ASP A 1 3691 ? 207.994 197.866 229.956 1.00 16.88 ? 3691 ASP A CG    1 
ATOM   16206 O  OD1   . ASP A 1 3691 ? 206.891 197.855 230.542 1.00 17.34 ? 3691 ASP A OD1   1 
ATOM   16207 O  OD2   . ASP A 1 3691 ? 208.209 198.560 228.941 1.00 24.80 ? 3691 ASP A OD2   1 
ATOM   16208 N  N     . LEU A 1 3692 ? 207.162 197.679 232.937 1.00 5.18  ? 3692 LEU A N     1 
ATOM   16209 C  CA    . LEU A 1 3692 ? 206.738 198.535 234.041 1.00 2.20  ? 3692 LEU A CA    1 
ATOM   16210 C  C     . LEU A 1 3692 ? 206.620 197.747 235.340 1.00 1.86  ? 3692 LEU A C     1 
ATOM   16211 O  O     . LEU A 1 3692 ? 206.944 198.263 236.416 1.00 2.11  ? 3692 LEU A O     1 
ATOM   16212 C  CB    . LEU A 1 3692 ? 205.413 199.218 233.706 1.00 4.36  ? 3692 LEU A CB    1 
ATOM   16213 C  CG    . LEU A 1 3692 ? 204.960 200.329 234.661 1.00 3.42  ? 3692 LEU A CG    1 
ATOM   16214 C  CD1   . LEU A 1 3692 ? 206.021 201.410 234.802 1.00 0.68  ? 3692 LEU A CD1   1 
ATOM   16215 C  CD2   . LEU A 1 3692 ? 203.643 200.930 234.209 1.00 2.24  ? 3692 LEU A CD2   1 
ATOM   16216 N  N     . CYS A 1 3693 ? 206.156 196.496 235.259 1.00 3.29  ? 3693 CYS A N     1 
ATOM   16217 C  CA    . CYS A 1 3693 ? 205.998 195.683 236.458 1.00 2.12  ? 3693 CYS A CA    1 
ATOM   16218 C  C     . CYS A 1 3693 ? 207.329 195.430 237.149 1.00 2.02  ? 3693 CYS A C     1 
ATOM   16219 O  O     . CYS A 1 3693 ? 207.372 195.267 238.372 1.00 3.12  ? 3693 CYS A O     1 
ATOM   16220 C  CB    . CYS A 1 3693 ? 205.322 194.356 236.106 1.00 1.69  ? 3693 CYS A CB    1 
ATOM   16221 S  SG    . CYS A 1 3693 ? 203.659 194.518 235.431 1.00 6.74  ? 3693 CYS A SG    1 
ATOM   16222 N  N     . SER A 1 3694 ? 208.423 195.388 236.385 1.00 1.73  ? 3694 SER A N     1 
ATOM   16223 C  CA    . SER A 1 3694 ? 209.738 195.170 236.970 1.00 1.04  ? 3694 SER A CA    1 
ATOM   16224 C  C     . SER A 1 3694 ? 210.300 196.418 237.638 1.00 0.97  ? 3694 SER A C     1 
ATOM   16225 O  O     . SER A 1 3694 ? 211.225 196.307 238.447 1.00 1.14  ? 3694 SER A O     1 
ATOM   16226 C  CB    . SER A 1 3694 ? 210.710 194.674 235.896 1.00 1.33  ? 3694 SER A CB    1 
ATOM   16227 O  OG    . SER A 1 3694 ? 210.847 195.621 234.853 1.00 4.22  ? 3694 SER A OG    1 
ATOM   16228 N  N     . ARG A 1 3695 ? 209.769 197.597 237.327 1.00 1.30  ? 3695 ARG A N     1 
ATOM   16229 C  CA    . ARG A 1 3695 ? 210.319 198.851 237.824 1.00 0.99  ? 3695 ARG A CA    1 
ATOM   16230 C  C     . ARG A 1 3695 ? 209.582 199.402 239.035 1.00 0.80  ? 3695 ARG A C     1 
ATOM   16231 O  O     . ARG A 1 3695 ? 210.036 200.391 239.618 1.00 0.54  ? 3695 ARG A O     1 
ATOM   16232 C  CB    . ARG A 1 3695 ? 210.317 199.899 236.710 1.00 1.22  ? 3695 ARG A CB    1 
ATOM   16233 C  CG    . ARG A 1 3695 ? 211.164 199.531 235.516 1.00 1.41  ? 3695 ARG A CG    1 
ATOM   16234 C  CD    . ARG A 1 3695 ? 211.063 200.577 234.425 1.00 1.22  ? 3695 ARG A CD    1 
ATOM   16235 N  NE    . ARG A 1 3695 ? 211.057 199.975 233.098 1.00 2.53  ? 3695 ARG A NE    1 
ATOM   16236 C  CZ    . ARG A 1 3695 ? 211.969 200.210 232.167 1.00 2.65  ? 3695 ARG A CZ    1 
ATOM   16237 N  NH1   . ARG A 1 3695 ? 212.990 201.022 232.389 1.00 2.34  ? 3695 ARG A NH1   1 
ATOM   16238 N  NH2   . ARG A 1 3695 ? 211.860 199.611 230.986 1.00 2.69  ? 3695 ARG A NH2   1 
ATOM   16239 N  N     . VAL A 1 3696 ? 208.466 198.793 239.440 1.00 1.00  ? 3696 VAL A N     1 
ATOM   16240 C  CA    . VAL A 1 3696 ? 207.617 199.356 240.478 1.00 0.81  ? 3696 VAL A CA    1 
ATOM   16241 C  C     . VAL A 1 3696 ? 207.352 198.314 241.553 1.00 0.32  ? 3696 VAL A C     1 
ATOM   16242 O  O     . VAL A 1 3696 ? 207.579 197.116 241.368 1.00 5.18  ? 3696 VAL A O     1 
ATOM   16243 C  CB    . VAL A 1 3696 ? 206.277 199.887 239.919 1.00 0.63  ? 3696 VAL A CB    1 
ATOM   16244 C  CG1   . VAL A 1 3696 ? 206.517 200.989 238.900 1.00 0.27  ? 3696 VAL A CG1   1 
ATOM   16245 C  CG2   . VAL A 1 3696 ? 205.463 198.751 239.321 1.00 0.41  ? 3696 VAL A CG2   1 
ATOM   16246 N  N     . THR A 1 3697 ? 206.874 198.795 242.694 1.00 0.25  ? 3697 THR A N     1 
ATOM   16247 C  CA    . THR A 1 3697 ? 206.379 197.958 243.781 1.00 0.24  ? 3697 THR A CA    1 
ATOM   16248 C  C     . THR A 1 3697 ? 204.861 198.083 243.791 1.00 0.11  ? 3697 THR A C     1 
ATOM   16249 O  O     . THR A 1 3697 ? 204.325 199.160 244.065 1.00 0.14  ? 3697 THR A O     1 
ATOM   16250 C  CB    . THR A 1 3697 ? 206.973 198.385 245.123 1.00 0.42  ? 3697 THR A CB    1 
ATOM   16251 O  OG1   . THR A 1 3697 ? 208.391 198.191 245.108 1.00 1.23  ? 3697 THR A OG1   1 
ATOM   16252 C  CG2   . THR A 1 3697 ? 206.364 197.579 246.261 1.00 1.11  ? 3697 THR A CG2   1 
ATOM   16253 N  N     . PHE A 1 3698 ? 204.168 196.993 243.481 1.00 0.13  ? 3698 PHE A N     1 
ATOM   16254 C  CA    . PHE A 1 3698 ? 202.713 197.039 243.442 1.00 0.16  ? 3698 PHE A CA    1 
ATOM   16255 C  C     . PHE A 1 3698 ? 202.150 197.058 244.856 1.00 0.13  ? 3698 PHE A C     1 
ATOM   16256 O  O     . PHE A 1 3698 ? 202.510 196.227 245.693 1.00 0.55  ? 3698 PHE A O     1 
ATOM   16257 C  CB    . PHE A 1 3698 ? 202.160 195.851 242.659 1.00 0.12  ? 3698 PHE A CB    1 
ATOM   16258 C  CG    . PHE A 1 3698 ? 202.227 196.029 241.173 1.00 0.22  ? 3698 PHE A CG    1 
ATOM   16259 C  CD1   . PHE A 1 3698 ? 201.395 196.929 240.534 1.00 0.16  ? 3698 PHE A CD1   1 
ATOM   16260 C  CD2   . PHE A 1 3698 ? 203.127 195.301 240.416 1.00 0.54  ? 3698 PHE A CD2   1 
ATOM   16261 C  CE1   . PHE A 1 3698 ? 201.457 197.099 239.167 1.00 0.21  ? 3698 PHE A CE1   1 
ATOM   16262 C  CE2   . PHE A 1 3698 ? 203.194 195.468 239.048 1.00 0.82  ? 3698 PHE A CE2   1 
ATOM   16263 C  CZ    . PHE A 1 3698 ? 202.358 196.368 238.425 1.00 0.53  ? 3698 PHE A CZ    1 
ATOM   16264 N  N     . VAL A 1 3699 ? 201.276 198.023 245.123 1.00 0.10  ? 3699 VAL A N     1 
ATOM   16265 C  CA    . VAL A 1 3699 ? 200.607 198.169 246.412 1.00 0.17  ? 3699 VAL A CA    1 
ATOM   16266 C  C     . VAL A 1 3699 ? 199.120 198.286 246.102 1.00 0.14  ? 3699 VAL A C     1 
ATOM   16267 O  O     . VAL A 1 3699 ? 198.637 199.364 245.743 1.00 0.19  ? 3699 VAL A O     1 
ATOM   16268 C  CB    . VAL A 1 3699 ? 201.110 199.384 247.201 1.00 0.18  ? 3699 VAL A CB    1 
ATOM   16269 C  CG1   . VAL A 1 3699 ? 200.382 199.490 248.520 1.00 0.13  ? 3699 VAL A CG1   1 
ATOM   16270 C  CG2   . VAL A 1 3699 ? 202.610 199.296 247.425 1.00 0.14  ? 3699 VAL A CG2   1 
ATOM   16271 N  N     . ASN A 1 3700 ? 198.393 197.182 246.235 1.00 0.20  ? 3700 ASN A N     1 
ATOM   16272 C  CA    . ASN A 1 3700 ? 197.006 197.096 245.796 1.00 0.65  ? 3700 ASN A CA    1 
ATOM   16273 C  C     . ASN A 1 3700 ? 196.078 197.286 246.989 1.00 0.44  ? 3700 ASN A C     1 
ATOM   16274 O  O     . ASN A 1 3700 ? 196.166 196.550 247.975 1.00 0.31  ? 3700 ASN A O     1 
ATOM   16275 C  CB    . ASN A 1 3700 ? 196.744 195.756 245.109 1.00 0.75  ? 3700 ASN A CB    1 
ATOM   16276 C  CG    . ASN A 1 3700 ? 195.497 195.771 244.254 1.00 0.62  ? 3700 ASN A CG    1 
ATOM   16277 O  OD1   . ASN A 1 3700 ? 194.716 196.719 244.288 1.00 1.01  ? 3700 ASN A OD1   1 
ATOM   16278 N  ND2   . ASN A 1 3700 ? 195.308 194.719 243.471 1.00 0.94  ? 3700 ASN A ND2   1 
ATOM   16279 N  N     . PHE A 1 3701 ? 195.190 198.272 246.891 1.00 1.02  ? 3701 PHE A N     1 
ATOM   16280 C  CA    . PHE A 1 3701 ? 194.216 198.568 247.939 1.00 0.91  ? 3701 PHE A CA    1 
ATOM   16281 C  C     . PHE A 1 3701 ? 192.893 197.935 247.526 1.00 1.76  ? 3701 PHE A C     1 
ATOM   16282 O  O     . PHE A 1 3701 ? 192.070 198.550 246.847 1.00 5.53  ? 3701 PHE A O     1 
ATOM   16283 C  CB    . PHE A 1 3701 ? 194.084 200.070 248.153 1.00 0.87  ? 3701 PHE A CB    1 
ATOM   16284 C  CG    . PHE A 1 3701 ? 195.205 200.671 248.948 1.00 0.78  ? 3701 PHE A CG    1 
ATOM   16285 C  CD1   . PHE A 1 3701 ? 196.442 200.902 248.365 1.00 0.33  ? 3701 PHE A CD1   1 
ATOM   16286 C  CD2   . PHE A 1 3701 ? 195.025 201.007 250.278 1.00 0.46  ? 3701 PHE A CD2   1 
ATOM   16287 C  CE1   . PHE A 1 3701 ? 197.473 201.454 249.093 1.00 0.23  ? 3701 PHE A CE1   1 
ATOM   16288 C  CE2   . PHE A 1 3701 ? 196.055 201.562 251.012 1.00 0.26  ? 3701 PHE A CE2   1 
ATOM   16289 C  CZ    . PHE A 1 3701 ? 197.278 201.788 250.419 1.00 0.25  ? 3701 PHE A CZ    1 
ATOM   16290 N  N     . THR A 1 3702 ? 192.692 196.688 247.938 1.00 2.64  ? 3702 THR A N     1 
ATOM   16291 C  CA    . THR A 1 3702 ? 191.464 195.963 247.658 1.00 1.87  ? 3702 THR A CA    1 
ATOM   16292 C  C     . THR A 1 3702 ? 190.589 195.930 248.901 1.00 3.06  ? 3702 THR A C     1 
ATOM   16293 O  O     . THR A 1 3702 ? 191.092 195.835 250.025 1.00 4.80  ? 3702 THR A O     1 
ATOM   16294 C  CB    . THR A 1 3702 ? 191.754 194.536 247.187 1.00 3.67  ? 3702 THR A CB    1 
ATOM   16295 O  OG1   . THR A 1 3702 ? 192.205 193.745 248.293 1.00 2.60  ? 3702 THR A OG1   1 
ATOM   16296 C  CG2   . THR A 1 3702 ? 192.811 194.537 246.097 1.00 2.15  ? 3702 THR A CG2   1 
ATOM   16297 N  N     . VAL A 1 3703 ? 189.277 196.015 248.694 1.00 3.45  ? 3703 VAL A N     1 
ATOM   16298 C  CA    . VAL A 1 3703 ? 188.340 195.970 249.806 1.00 2.05  ? 3703 VAL A CA    1 
ATOM   16299 C  C     . VAL A 1 3703 ? 188.272 194.550 250.350 1.00 1.10  ? 3703 VAL A C     1 
ATOM   16300 O  O     . VAL A 1 3703 ? 188.043 193.590 249.603 1.00 1.58  ? 3703 VAL A O     1 
ATOM   16301 C  CB    . VAL A 1 3703 ? 186.955 196.466 249.363 1.00 1.64  ? 3703 VAL A CB    1 
ATOM   16302 C  CG1   . VAL A 1 3703 ? 185.931 196.256 250.467 1.00 1.68  ? 3703 VAL A CG1   1 
ATOM   16303 C  CG2   . VAL A 1 3703 ? 187.023 197.925 248.961 1.00 1.33  ? 3703 VAL A CG2   1 
ATOM   16304 N  N     . THR A 1 3704 ? 188.479 194.410 251.652 1.00 2.23  ? 3704 THR A N     1 
ATOM   16305 C  CA    . THR A 1 3704 ? 188.349 193.132 252.332 1.00 2.53  ? 3704 THR A CA    1 
ATOM   16306 C  C     . THR A 1 3704 ? 186.990 193.044 253.014 1.00 2.34  ? 3704 THR A C     1 
ATOM   16307 O  O     . THR A 1 3704 ? 186.355 194.055 253.321 1.00 3.22  ? 3704 THR A O     1 
ATOM   16308 C  CB    . THR A 1 3704 ? 189.469 192.936 253.359 1.00 4.95  ? 3704 THR A CB    1 
ATOM   16309 O  OG1   . THR A 1 3704 ? 189.212 193.742 254.515 1.00 5.10  ? 3704 THR A OG1   1 
ATOM   16310 C  CG2   . THR A 1 3704 ? 190.809 193.327 252.763 1.00 2.40  ? 3704 THR A CG2   1 
ATOM   16311 N  N     . ARG A 1 3705 ? 186.545 191.806 253.242 1.00 2.59  ? 3705 ARG A N     1 
ATOM   16312 C  CA    . ARG A 1 3705 ? 185.239 191.594 253.856 1.00 2.90  ? 3705 ARG A CA    1 
ATOM   16313 C  C     . ARG A 1 3705 ? 185.188 192.166 255.265 1.00 3.73  ? 3705 ARG A C     1 
ATOM   16314 O  O     . ARG A 1 3705 ? 184.181 192.766 255.662 1.00 5.71  ? 3705 ARG A O     1 
ATOM   16315 C  CB    . ARG A 1 3705 ? 184.899 190.104 253.867 1.00 3.62  ? 3705 ARG A CB    1 
ATOM   16316 C  CG    . ARG A 1 3705 ? 184.520 189.558 252.508 1.00 4.74  ? 3705 ARG A CG    1 
ATOM   16317 C  CD    . ARG A 1 3705 ? 184.370 188.050 252.529 1.00 6.93  ? 3705 ARG A CD    1 
ATOM   16318 N  NE    . ARG A 1 3705 ? 183.819 187.540 251.278 1.00 6.26  ? 3705 ARG A NE    1 
ATOM   16319 C  CZ    . ARG A 1 3705 ? 182.551 187.668 250.907 1.00 7.96  ? 3705 ARG A CZ    1 
ATOM   16320 N  NH1   . ARG A 1 3705 ? 181.662 188.270 251.679 1.00 4.14  ? 3705 ARG A NH1   1 
ATOM   16321 N  NH2   . ARG A 1 3705 ? 182.166 187.172 249.735 1.00 5.76  ? 3705 ARG A NH2   1 
ATOM   16322 N  N     . SER A 1 3706 ? 186.261 191.989 256.039 1.00 3.20  ? 3706 SER A N     1 
ATOM   16323 C  CA    . SER A 1 3706 ? 186.290 192.517 257.398 1.00 2.25  ? 3706 SER A CA    1 
ATOM   16324 C  C     . SER A 1 3706 ? 186.261 194.041 257.409 1.00 3.44  ? 3706 SER A C     1 
ATOM   16325 O  O     . SER A 1 3706 ? 185.557 194.646 258.227 1.00 4.50  ? 3706 SER A O     1 
ATOM   16326 C  CB    . SER A 1 3706 ? 187.524 191.999 258.135 1.00 4.37  ? 3706 SER A CB    1 
ATOM   16327 O  OG    . SER A 1 3706 ? 188.713 192.466 257.527 1.00 9.37  ? 3706 SER A OG    1 
ATOM   16328 N  N     . SER A 1 3707 ? 187.026 194.679 256.521 1.00 2.96  ? 3707 SER A N     1 
ATOM   16329 C  CA    . SER A 1 3707 ? 187.069 196.138 256.501 1.00 2.58  ? 3707 SER A CA    1 
ATOM   16330 C  C     . SER A 1 3707 ? 185.722 196.727 256.107 1.00 3.31  ? 3707 SER A C     1 
ATOM   16331 O  O     . SER A 1 3707 ? 185.281 197.726 256.686 1.00 5.91  ? 3707 SER A O     1 
ATOM   16332 C  CB    . SER A 1 3707 ? 188.168 196.623 255.556 1.00 3.56  ? 3707 SER A CB    1 
ATOM   16333 O  OG    . SER A 1 3707 ? 187.941 196.183 254.230 1.00 9.39  ? 3707 SER A OG    1 
ATOM   16334 N  N     . LEU A 1 3708 ? 185.056 196.126 255.120 1.00 4.16  ? 3708 LEU A N     1 
ATOM   16335 C  CA    . LEU A 1 3708 ? 183.735 196.604 254.725 1.00 1.85  ? 3708 LEU A CA    1 
ATOM   16336 C  C     . LEU A 1 3708 ? 182.712 196.374 255.830 1.00 1.88  ? 3708 LEU A C     1 
ATOM   16337 O  O     . LEU A 1 3708 ? 181.820 197.205 256.038 1.00 2.04  ? 3708 LEU A O     1 
ATOM   16338 C  CB    . LEU A 1 3708 ? 183.300 195.925 253.430 1.00 2.52  ? 3708 LEU A CB    1 
ATOM   16339 C  CG    . LEU A 1 3708 ? 182.006 196.446 252.808 1.00 1.75  ? 3708 LEU A CG    1 
ATOM   16340 C  CD1   . LEU A 1 3708 ? 182.030 197.960 252.693 1.00 2.41  ? 3708 LEU A CD1   1 
ATOM   16341 C  CD2   . LEU A 1 3708 ? 181.797 195.813 251.456 1.00 0.99  ? 3708 LEU A CD2   1 
ATOM   16342 N  N     . GLN A 1 3709 ? 182.820 195.253 256.547 1.00 2.17  ? 3709 GLN A N     1 
ATOM   16343 C  CA    . GLN A 1 3709 ? 181.931 195.014 257.680 1.00 2.21  ? 3709 GLN A CA    1 
ATOM   16344 C  C     . GLN A 1 3709 ? 182.107 196.081 258.751 1.00 2.75  ? 3709 GLN A C     1 
ATOM   16345 O  O     . GLN A 1 3709 ? 181.123 196.576 259.311 1.00 7.47  ? 3709 GLN A O     1 
ATOM   16346 C  CB    . GLN A 1 3709 ? 182.177 193.624 258.265 1.00 2.22  ? 3709 GLN A CB    1 
ATOM   16347 C  CG    . GLN A 1 3709 ? 181.437 192.509 257.559 1.00 2.40  ? 3709 GLN A CG    1 
ATOM   16348 C  CD    . GLN A 1 3709 ? 182.142 191.172 257.676 1.00 11.14 ? 3709 GLN A CD    1 
ATOM   16349 O  OE1   . GLN A 1 3709 ? 183.040 190.999 258.501 1.00 13.87 ? 3709 GLN A OE1   1 
ATOM   16350 N  NE2   . GLN A 1 3709 ? 181.734 190.215 256.850 1.00 9.68  ? 3709 GLN A NE2   1 
ATOM   16351 N  N     . SER A 1 3710 ? 183.357 196.447 259.054 1.00 2.88  ? 3710 SER A N     1 
ATOM   16352 C  CA    . SER A 1 3710 ? 183.601 197.515 260.018 1.00 3.07  ? 3710 SER A CA    1 
ATOM   16353 C  C     . SER A 1 3710 ? 183.045 198.842 259.522 1.00 3.78  ? 3710 SER A C     1 
ATOM   16354 O  O     . SER A 1 3710 ? 182.463 199.609 260.297 1.00 6.15  ? 3710 SER A O     1 
ATOM   16355 C  CB    . SER A 1 3710 ? 185.098 197.639 260.303 1.00 4.86  ? 3710 SER A CB    1 
ATOM   16356 O  OG    . SER A 1 3710 ? 185.606 196.472 260.920 1.00 12.56 ? 3710 SER A OG    1 
ATOM   16357 N  N     . GLN A 1 3711 ? 183.223 199.133 258.231 1.00 2.05  ? 3711 GLN A N     1 
ATOM   16358 C  CA    . GLN A 1 3711 ? 182.713 200.381 257.673 1.00 2.65  ? 3711 GLN A CA    1 
ATOM   16359 C  C     . GLN A 1 3711 ? 181.197 200.456 257.774 1.00 2.56  ? 3711 GLN A C     1 
ATOM   16360 O  O     . GLN A 1 3711 ? 180.642 201.496 258.143 1.00 4.07  ? 3711 GLN A O     1 
ATOM   16361 C  CB    . GLN A 1 3711 ? 183.149 200.523 256.215 1.00 3.51  ? 3711 GLN A CB    1 
ATOM   16362 C  CG    . GLN A 1 3711 ? 184.604 200.883 256.020 1.00 4.84  ? 3711 GLN A CG    1 
ATOM   16363 C  CD    . GLN A 1 3711 ? 185.001 200.893 254.558 1.00 10.11 ? 3711 GLN A CD    1 
ATOM   16364 O  OE1   . GLN A 1 3711 ? 185.979 200.259 254.163 1.00 12.56 ? 3711 GLN A OE1   1 
ATOM   16365 N  NE2   . GLN A 1 3711 ? 184.235 201.609 253.743 1.00 10.04 ? 3711 GLN A NE2   1 
ATOM   16366 N  N     . CYS A 1 3712 ? 180.509 199.363 257.445 1.00 3.19  ? 3712 CYS A N     1 
ATOM   16367 C  CA    . CYS A 1 3712 ? 179.053 199.367 257.467 1.00 2.49  ? 3712 CYS A CA    1 
ATOM   16368 C  C     . CYS A 1 3712 ? 178.502 199.291 258.883 1.00 2.63  ? 3712 CYS A C     1 
ATOM   16369 O  O     . CYS A 1 3712 ? 177.450 199.874 259.161 1.00 5.65  ? 3712 CYS A O     1 
ATOM   16370 C  CB    . CYS A 1 3712 ? 178.518 198.218 256.616 1.00 1.96  ? 3712 CYS A CB    1 
ATOM   16371 S  SG    . CYS A 1 3712 ? 179.029 198.309 254.886 1.00 2.49  ? 3712 CYS A SG    1 
ATOM   16372 N  N     . LEU A 1 3713 ? 179.190 198.585 259.784 1.00 2.18  ? 3713 LEU A N     1 
ATOM   16373 C  CA    . LEU A 1 3713 ? 178.777 198.587 261.183 1.00 3.10  ? 3713 LEU A CA    1 
ATOM   16374 C  C     . LEU A 1 3713 ? 178.895 199.980 261.785 1.00 3.26  ? 3713 LEU A C     1 
ATOM   16375 O  O     . LEU A 1 3713 ? 178.020 200.417 262.541 1.00 4.68  ? 3713 LEU A O     1 
ATOM   16376 C  CB    . LEU A 1 3713 ? 179.610 197.586 261.982 1.00 4.27  ? 3713 LEU A CB    1 
ATOM   16377 C  CG    . LEU A 1 3713 ? 179.387 197.598 263.495 1.00 3.12  ? 3713 LEU A CG    1 
ATOM   16378 C  CD1   . LEU A 1 3713 ? 178.006 197.066 263.830 1.00 3.80  ? 3713 LEU A CD1   1 
ATOM   16379 C  CD2   . LEU A 1 3713 ? 180.459 196.799 264.211 1.00 7.11  ? 3713 LEU A CD2   1 
ATOM   16380 N  N     . ASN A 1 3714 ? 179.974 200.696 261.459 1.00 3.29  ? 3714 ASN A N     1 
ATOM   16381 C  CA    . ASN A 1 3714 ? 180.140 202.051 261.971 1.00 5.69  ? 3714 ASN A CA    1 
ATOM   16382 C  C     . ASN A 1 3714 ? 179.098 202.996 261.390 1.00 5.50  ? 3714 ASN A C     1 
ATOM   16383 O  O     . ASN A 1 3714 ? 178.576 203.863 262.099 1.00 7.35  ? 3714 ASN A O     1 
ATOM   16384 C  CB    . ASN A 1 3714 ? 181.550 202.559 261.668 1.00 6.78  ? 3714 ASN A CB    1 
ATOM   16385 C  CG    . ASN A 1 3714 ? 182.607 201.898 262.529 1.00 10.38 ? 3714 ASN A CG    1 
ATOM   16386 O  OD1   . ASN A 1 3714 ? 182.294 201.158 263.462 1.00 10.34 ? 3714 ASN A OD1   1 
ATOM   16387 N  ND2   . ASN A 1 3714 ? 183.870 202.164 262.221 1.00 15.05 ? 3714 ASN A ND2   1 
ATOM   16388 N  N     . GLU A 1 3715 ? 178.787 202.850 260.100 1.00 5.45  ? 3715 GLU A N     1 
ATOM   16389 C  CA    . GLU A 1 3715 ? 177.859 203.776 259.459 1.00 6.76  ? 3715 GLU A CA    1 
ATOM   16390 C  C     . GLU A 1 3715 ? 176.445 203.631 260.014 1.00 6.55  ? 3715 GLU A C     1 
ATOM   16391 O  O     . GLU A 1 3715 ? 175.763 204.635 260.246 1.00 9.06  ? 3715 GLU A O     1 
ATOM   16392 C  CB    . GLU A 1 3715 ? 177.873 203.575 257.943 1.00 6.71  ? 3715 GLU A CB    1 
ATOM   16393 C  CG    . GLU A 1 3715 ? 176.965 204.532 257.193 1.00 12.65 ? 3715 GLU A CG    1 
ATOM   16394 C  CD    . GLU A 1 3715 ? 177.407 205.983 257.312 1.00 26.30 ? 3715 GLU A CD    1 
ATOM   16395 O  OE1   . GLU A 1 3715 ? 178.613 206.228 257.530 1.00 31.23 ? 3715 GLU A OE1   1 
ATOM   16396 O  OE2   . GLU A 1 3715 ? 176.545 206.880 257.196 1.00 29.16 ? 3715 GLU A OE2   1 
ATOM   16397 N  N     . VAL A 1 3716 ? 175.983 202.398 260.227 1.00 4.29  ? 3716 VAL A N     1 
ATOM   16398 C  CA    . VAL A 1 3716 ? 174.653 202.208 260.799 1.00 6.05  ? 3716 VAL A CA    1 
ATOM   16399 C  C     . VAL A 1 3716 ? 174.622 202.679 262.248 1.00 9.32  ? 3716 VAL A C     1 
ATOM   16400 O  O     . VAL A 1 3716 ? 173.615 203.222 262.717 1.00 10.30 ? 3716 VAL A O     1 
ATOM   16401 C  CB    . VAL A 1 3716 ? 174.196 200.741 260.659 1.00 3.53  ? 3716 VAL A CB    1 
ATOM   16402 C  CG1   . VAL A 1 3716 ? 175.102 199.796 261.426 1.00 3.88  ? 3716 VAL A CG1   1 
ATOM   16403 C  CG2   . VAL A 1 3716 ? 172.751 200.590 261.110 1.00 4.49  ? 3716 VAL A CG2   1 
ATOM   16404 N  N     . LEU A 1 3717 ? 175.726 202.490 262.977 1.00 6.09  ? 3717 LEU A N     1 
ATOM   16405 C  CA    . LEU A 1 3717 ? 175.812 203.008 264.337 1.00 5.21  ? 3717 LEU A CA    1 
ATOM   16406 C  C     . LEU A 1 3717 ? 175.701 204.527 264.352 1.00 7.74  ? 3717 LEU A C     1 
ATOM   16407 O  O     . LEU A 1 3717 ? 175.038 205.100 265.222 1.00 9.49  ? 3717 LEU A O     1 
ATOM   16408 C  CB    . LEU A 1 3717 ? 177.119 202.556 264.985 1.00 7.44  ? 3717 LEU A CB    1 
ATOM   16409 C  CG    . LEU A 1 3717 ? 177.115 202.343 266.498 1.00 13.63 ? 3717 LEU A CG    1 
ATOM   16410 C  CD1   . LEU A 1 3717 ? 176.313 201.109 266.872 1.00 7.91  ? 3717 LEU A CD1   1 
ATOM   16411 C  CD2   . LEU A 1 3717 ? 178.538 202.249 267.027 1.00 13.29 ? 3717 LEU A CD2   1 
ATOM   16412 N  N     . LYS A 1 3718 ? 176.346 205.193 263.393 1.00 8.34  ? 3718 LYS A N     1 
ATOM   16413 C  CA    . LYS A 1 3718 ? 176.244 206.643 263.297 1.00 9.12  ? 3718 LYS A CA    1 
ATOM   16414 C  C     . LYS A 1 3718 ? 174.815 207.081 262.996 1.00 12.42 ? 3718 LYS A C     1 
ATOM   16415 O  O     . LYS A 1 3718 ? 174.330 208.071 263.552 1.00 12.04 ? 3718 LYS A O     1 
ATOM   16416 C  CB    . LYS A 1 3718 ? 177.203 207.159 262.225 1.00 8.50  ? 3718 LYS A CB    1 
ATOM   16417 C  CG    . LYS A 1 3718 ? 177.219 208.665 262.072 1.00 12.40 ? 3718 LYS A CG    1 
ATOM   16418 C  CD    . LYS A 1 3718 ? 177.802 209.336 263.304 1.00 19.45 ? 3718 LYS A CD    1 
ATOM   16419 C  CE    . LYS A 1 3718 ? 177.806 210.848 263.156 1.00 24.73 ? 3718 LYS A CE    1 
ATOM   16420 N  NZ    . LYS A 1 3718 ? 178.733 211.290 262.078 1.00 25.35 ? 3718 LYS A NZ    1 
ATOM   16421 N  N     . ALA A 1 3719 ? 174.128 206.359 262.111 1.00 10.46 ? 3719 ALA A N     1 
ATOM   16422 C  CA    . ALA A 1 3719 ? 172.770 206.729 261.735 1.00 7.88  ? 3719 ALA A CA    1 
ATOM   16423 C  C     . ALA A 1 3719 ? 171.759 206.389 262.826 1.00 11.19 ? 3719 ALA A C     1 
ATOM   16424 O  O     . ALA A 1 3719 ? 170.852 207.181 263.099 1.00 14.60 ? 3719 ALA A O     1 
ATOM   16425 C  CB    . ALA A 1 3719 ? 172.383 206.041 260.426 1.00 8.42  ? 3719 ALA A CB    1 
ATOM   16426 N  N     . GLU A 1 3720 ? 171.897 205.226 263.456 1.00 15.44 ? 3720 GLU A N     1 
ATOM   16427 C  CA    . GLU A 1 3720 ? 170.875 204.704 264.356 1.00 10.05 ? 3720 GLU A CA    1 
ATOM   16428 C  C     . GLU A 1 3720 ? 171.121 205.033 265.821 1.00 11.07 ? 3720 GLU A C     1 
ATOM   16429 O  O     . GLU A 1 3720 ? 170.167 205.306 266.553 1.00 18.09 ? 3720 GLU A O     1 
ATOM   16430 C  CB    . GLU A 1 3720 ? 170.756 203.188 264.190 1.00 9.63  ? 3720 GLU A CB    1 
ATOM   16431 C  CG    . GLU A 1 3720 ? 170.069 202.785 262.907 1.00 10.37 ? 3720 GLU A CG    1 
ATOM   16432 C  CD    . GLU A 1 3720 ? 168.621 203.224 262.876 1.00 20.42 ? 3720 GLU A CD    1 
ATOM   16433 O  OE1   . GLU A 1 3720 ? 167.803 202.621 263.602 1.00 22.31 ? 3720 GLU A OE1   1 
ATOM   16434 O  OE2   . GLU A 1 3720 ? 168.304 204.181 262.138 1.00 18.54 ? 3720 GLU A OE2   1 
ATOM   16435 N  N     . ARG A 1 3721 ? 172.373 205.013 266.270 1.00 12.92 ? 3721 ARG A N     1 
ATOM   16436 C  CA    . ARG A 1 3721 ? 172.719 205.275 267.667 1.00 11.33 ? 3721 ARG A CA    1 
ATOM   16437 C  C     . ARG A 1 3721 ? 173.809 206.338 267.715 1.00 15.22 ? 3721 ARG A C     1 
ATOM   16438 O  O     . ARG A 1 3721 ? 174.962 206.049 268.050 1.00 17.07 ? 3721 ARG A O     1 
ATOM   16439 C  CB    . ARG A 1 3721 ? 173.169 203.992 268.369 1.00 12.76 ? 3721 ARG A CB    1 
ATOM   16440 C  CG    . ARG A 1 3721 ? 172.203 202.821 268.230 1.00 8.84  ? 3721 ARG A CG    1 
ATOM   16441 C  CD    . ARG A 1 3721 ? 170.851 203.139 268.843 1.00 11.96 ? 3721 ARG A CD    1 
ATOM   16442 N  NE    . ARG A 1 3721 ? 170.921 203.291 270.292 1.00 20.94 ? 3721 ARG A NE    1 
ATOM   16443 C  CZ    . ARG A 1 3721 ? 171.008 202.284 271.150 1.00 25.79 ? 3721 ARG A CZ    1 
ATOM   16444 N  NH1   . ARG A 1 3721 ? 171.008 201.026 270.742 1.00 18.84 ? 3721 ARG A NH1   1 
ATOM   16445 N  NH2   . ARG A 1 3721 ? 171.086 202.546 272.451 1.00 21.06 ? 3721 ARG A NH2   1 
ATOM   16446 N  N     . PRO A 1 3722 ? 173.472 207.587 267.377 1.00 17.52 ? 3722 PRO A N     1 
ATOM   16447 C  CA    . PRO A 1 3722 ? 174.504 208.636 267.342 1.00 13.88 ? 3722 PRO A CA    1 
ATOM   16448 C  C     . PRO A 1 3722 ? 175.183 208.865 268.681 1.00 15.65 ? 3722 PRO A C     1 
ATOM   16449 O  O     . PRO A 1 3722 ? 176.373 209.204 268.711 1.00 21.93 ? 3722 PRO A O     1 
ATOM   16450 C  CB    . PRO A 1 3722 ? 173.725 209.875 266.877 1.00 12.08 ? 3722 PRO A CB    1 
ATOM   16451 C  CG    . PRO A 1 3722 ? 172.310 209.590 267.247 1.00 13.66 ? 3722 PRO A CG    1 
ATOM   16452 C  CD    . PRO A 1 3722 ? 172.136 208.119 267.057 1.00 13.30 ? 3722 PRO A CD    1 
ATOM   16453 N  N     . ASP A 1 3723 ? 174.462 208.699 269.790 1.00 16.27 ? 3723 ASP A N     1 
ATOM   16454 C  CA    . ASP A 1 3723 ? 175.091 208.792 271.103 1.00 12.76 ? 3723 ASP A CA    1 
ATOM   16455 C  C     . ASP A 1 3723 ? 176.094 207.664 271.317 1.00 17.78 ? 3723 ASP A C     1 
ATOM   16456 O  O     . ASP A 1 3723 ? 177.179 207.886 271.869 1.00 20.71 ? 3723 ASP A O     1 
ATOM   16457 C  CB    . ASP A 1 3723 ? 174.023 208.789 272.196 1.00 17.72 ? 3723 ASP A CB    1 
ATOM   16458 C  CG    . ASP A 1 3723 ? 173.285 207.467 272.289 1.00 24.47 ? 3723 ASP A CG    1 
ATOM   16459 O  OD1   . ASP A 1 3723 ? 172.770 207.000 271.253 1.00 18.26 ? 3723 ASP A OD1   1 
ATOM   16460 O  OD2   . ASP A 1 3723 ? 173.219 206.896 273.399 1.00 28.87 ? 3723 ASP A OD2   1 
ATOM   16461 N  N     . VAL A 1 3724 ? 175.750 206.448 270.891 1.00 17.32 ? 3724 VAL A N     1 
ATOM   16462 C  CA    . VAL A 1 3724 ? 176.659 205.316 271.047 1.00 14.28 ? 3724 VAL A CA    1 
ATOM   16463 C  C     . VAL A 1 3724 ? 177.846 205.446 270.102 1.00 17.96 ? 3724 VAL A C     1 
ATOM   16464 O  O     . VAL A 1 3724 ? 178.988 205.150 270.474 1.00 19.22 ? 3724 VAL A O     1 
ATOM   16465 C  CB    . VAL A 1 3724 ? 175.902 203.993 270.832 1.00 12.96 ? 3724 VAL A CB    1 
ATOM   16466 C  CG1   . VAL A 1 3724 ? 176.848 202.805 270.950 1.00 15.38 ? 3724 VAL A CG1   1 
ATOM   16467 C  CG2   . VAL A 1 3724 ? 174.758 203.867 271.826 1.00 16.27 ? 3724 VAL A CG2   1 
ATOM   16468 N  N     . ASP A 1 3725 ? 177.598 205.880 268.863 1.00 18.20 ? 3725 ASP A N     1 
ATOM   16469 C  CA    . ASP A 1 3725 ? 178.682 206.005 267.894 1.00 15.04 ? 3725 ASP A CA    1 
ATOM   16470 C  C     . ASP A 1 3725 ? 179.687 207.064 268.325 1.00 20.02 ? 3725 ASP A C     1 
ATOM   16471 O  O     . ASP A 1 3725 ? 180.900 206.871 268.187 1.00 27.76 ? 3725 ASP A O     1 
ATOM   16472 C  CB    . ASP A 1 3725 ? 178.119 206.332 266.512 1.00 13.06 ? 3725 ASP A CB    1 
ATOM   16473 C  CG    . ASP A 1 3725 ? 179.107 206.045 265.400 1.00 16.88 ? 3725 ASP A CG    1 
ATOM   16474 O  OD1   . ASP A 1 3725 ? 179.454 204.863 265.202 1.00 16.18 ? 3725 ASP A OD1   1 
ATOM   16475 O  OD2   . ASP A 1 3725 ? 179.547 206.999 264.726 1.00 21.68 ? 3725 ASP A OD2   1 
ATOM   16476 N  N     . GLU A 1 3726 ? 179.200 208.193 268.846 1.00 18.89 ? 3726 GLU A N     1 
ATOM   16477 C  CA    . GLU A 1 3726 ? 180.102 209.229 269.336 1.00 18.40 ? 3726 GLU A CA    1 
ATOM   16478 C  C     . GLU A 1 3726 ? 180.930 208.726 270.511 1.00 21.50 ? 3726 GLU A C     1 
ATOM   16479 O  O     . GLU A 1 3726 ? 182.141 208.965 270.574 1.00 24.14 ? 3726 GLU A O     1 
ATOM   16480 C  CB    . GLU A 1 3726 ? 179.306 210.473 269.726 1.00 17.85 ? 3726 GLU A CB    1 
ATOM   16481 C  CG    . GLU A 1 3726 ? 180.157 211.645 270.176 1.00 23.61 ? 3726 GLU A CG    1 
ATOM   16482 C  CD    . GLU A 1 3726 ? 179.331 212.873 270.504 1.00 31.47 ? 3726 GLU A CD    1 
ATOM   16483 O  OE1   . GLU A 1 3726 ? 178.088 212.802 270.398 1.00 32.63 ? 3726 GLU A OE1   1 
ATOM   16484 O  OE2   . GLU A 1 3726 ? 179.922 213.911 270.866 1.00 35.40 ? 3726 GLU A OE2   1 
ATOM   16485 N  N     . LYS A 1 3727 ? 180.294 208.011 271.443 1.00 18.47 ? 3727 LYS A N     1 
ATOM   16486 C  CA    . LYS A 1 3727 ? 181.015 207.464 272.587 1.00 15.56 ? 3727 LYS A CA    1 
ATOM   16487 C  C     . LYS A 1 3727 ? 182.108 206.505 272.137 1.00 20.42 ? 3727 LYS A C     1 
ATOM   16488 O  O     . LYS A 1 3727 ? 183.209 206.496 272.701 1.00 27.89 ? 3727 LYS A O     1 
ATOM   16489 C  CB    . LYS A 1 3727 ? 180.036 206.768 273.534 1.00 16.94 ? 3727 LYS A CB    1 
ATOM   16490 C  CG    . LYS A 1 3727 ? 180.679 205.799 274.509 1.00 21.54 ? 3727 LYS A CG    1 
ATOM   16491 C  CD    . LYS A 1 3727 ? 179.634 205.024 275.299 1.00 21.17 ? 3727 LYS A CD    1 
ATOM   16492 C  CE    . LYS A 1 3727 ? 178.877 205.923 276.258 1.00 18.44 ? 3727 LYS A CE    1 
ATOM   16493 N  NZ    . LYS A 1 3727 ? 179.781 206.521 277.278 1.00 29.49 ? 3727 LYS A NZ    1 
ATOM   16494 N  N     . ARG A 1 3728 ? 181.823 205.690 271.120 1.00 15.40 ? 3728 ARG A N     1 
ATOM   16495 C  CA    . ARG A 1 3728 ? 182.835 204.791 270.578 1.00 17.19 ? 3728 ARG A CA    1 
ATOM   16496 C  C     . ARG A 1 3728 ? 184.005 205.567 269.983 1.00 19.44 ? 3728 ARG A C     1 
ATOM   16497 O  O     . ARG A 1 3728 ? 185.168 205.200 270.182 1.00 20.71 ? 3728 ARG A O     1 
ATOM   16498 C  CB    . ARG A 1 3728 ? 182.203 203.874 269.529 1.00 14.55 ? 3728 ARG A CB    1 
ATOM   16499 C  CG    . ARG A 1 3728 ? 183.189 203.037 268.739 1.00 12.95 ? 3728 ARG A CG    1 
ATOM   16500 C  CD    . ARG A 1 3728 ? 182.588 202.583 267.418 1.00 13.73 ? 3728 ARG A CD    1 
ATOM   16501 N  NE    . ARG A 1 3728 ? 182.478 203.678 266.463 1.00 19.43 ? 3728 ARG A NE    1 
ATOM   16502 C  CZ    . ARG A 1 3728 ? 183.408 203.996 265.573 1.00 21.08 ? 3728 ARG A CZ    1 
ATOM   16503 N  NH1   . ARG A 1 3728 ? 184.535 203.311 265.477 1.00 16.40 ? 3728 ARG A NH1   1 
ATOM   16504 N  NH2   . ARG A 1 3728 ? 183.203 205.028 264.760 1.00 18.20 ? 3728 ARG A NH2   1 
ATOM   16505 N  N     . SER A 1 3729 ? 183.716 206.644 269.247 1.00 21.30 ? 3729 SER A N     1 
ATOM   16506 C  CA    . SER A 1 3729 ? 184.782 207.431 268.633 1.00 17.65 ? 3729 SER A CA    1 
ATOM   16507 C  C     . SER A 1 3729 ? 185.656 208.109 269.684 1.00 20.90 ? 3729 SER A C     1 
ATOM   16508 O  O     . SER A 1 3729 ? 186.885 208.134 269.550 1.00 17.47 ? 3729 SER A O     1 
ATOM   16509 C  CB    . SER A 1 3729 ? 184.186 208.467 267.682 1.00 21.02 ? 3729 SER A CB    1 
ATOM   16510 O  OG    . SER A 1 3729 ? 185.109 209.509 267.422 1.00 29.66 ? 3729 SER A OG    1 
ATOM   16511 N  N     . ASP A 1 3730 ? 185.042 208.673 270.728 1.00 20.23 ? 3730 ASP A N     1 
ATOM   16512 C  CA    . ASP A 1 3730 ? 185.822 209.331 271.771 1.00 17.50 ? 3730 ASP A CA    1 
ATOM   16513 C  C     . ASP A 1 3730 ? 186.723 208.343 272.499 1.00 16.69 ? 3730 ASP A C     1 
ATOM   16514 O  O     . ASP A 1 3730 ? 187.880 208.654 272.800 1.00 17.97 ? 3730 ASP A O     1 
ATOM   16515 C  CB    . ASP A 1 3730 ? 184.898 210.040 272.762 1.00 19.37 ? 3730 ASP A CB    1 
ATOM   16516 C  CG    . ASP A 1 3730 ? 183.865 210.907 272.079 1.00 29.69 ? 3730 ASP A CG    1 
ATOM   16517 O  OD1   . ASP A 1 3730 ? 182.690 210.877 272.500 1.00 32.01 ? 3730 ASP A OD1   1 
ATOM   16518 O  OD2   . ASP A 1 3730 ? 184.227 211.618 271.117 1.00 30.89 ? 3730 ASP A OD2   1 
ATOM   16519 N  N     . LEU A 1 3731 ? 186.207 207.148 272.794 1.00 16.22 ? 3731 LEU A N     1 
ATOM   16520 C  CA    . LEU A 1 3731 ? 187.006 206.155 273.503 1.00 14.72 ? 3731 LEU A CA    1 
ATOM   16521 C  C     . LEU A 1 3731 ? 188.210 205.717 272.681 1.00 14.82 ? 3731 LEU A C     1 
ATOM   16522 O  O     . LEU A 1 3731 ? 189.315 205.575 273.217 1.00 20.55 ? 3731 LEU A O     1 
ATOM   16523 C  CB    . LEU A 1 3731 ? 186.142 204.950 273.865 1.00 14.30 ? 3731 LEU A CB    1 
ATOM   16524 C  CG    . LEU A 1 3731 ? 185.179 205.150 275.034 1.00 17.94 ? 3731 LEU A CG    1 
ATOM   16525 C  CD1   . LEU A 1 3731 ? 184.425 203.871 275.299 1.00 18.88 ? 3731 LEU A CD1   1 
ATOM   16526 C  CD2   . LEU A 1 3731 ? 185.915 205.612 276.282 1.00 18.02 ? 3731 LEU A CD2   1 
ATOM   16527 N  N     . LEU A 1 3732 ? 188.018 205.497 271.379 1.00 10.88 ? 3732 LEU A N     1 
ATOM   16528 C  CA    . LEU A 1 3732 ? 189.135 205.096 270.530 1.00 12.76 ? 3732 LEU A CA    1 
ATOM   16529 C  C     . LEU A 1 3732 ? 190.206 206.176 270.488 1.00 14.89 ? 3732 LEU A C     1 
ATOM   16530 O  O     . LEU A 1 3732 ? 191.405 205.873 270.475 1.00 14.48 ? 3732 LEU A O     1 
ATOM   16531 C  CB    . LEU A 1 3732 ? 188.633 204.772 269.123 1.00 10.24 ? 3732 LEU A CB    1 
ATOM   16532 C  CG    . LEU A 1 3732 ? 187.716 203.554 269.016 1.00 12.57 ? 3732 LEU A CG    1 
ATOM   16533 C  CD1   . LEU A 1 3732 ? 187.167 203.408 267.607 1.00 14.24 ? 3732 LEU A CD1   1 
ATOM   16534 C  CD2   . LEU A 1 3732 ? 188.450 202.293 269.443 1.00 13.58 ? 3732 LEU A CD2   1 
ATOM   16535 N  N     . LYS A 1 3733 ? 189.793 207.444 270.466 1.00 15.03 ? 3733 LYS A N     1 
ATOM   16536 C  CA    . LYS A 1 3733 ? 190.759 208.531 270.569 1.00 15.54 ? 3733 LYS A CA    1 
ATOM   16537 C  C     . LYS A 1 3733 ? 191.419 208.550 271.942 1.00 14.20 ? 3733 LYS A C     1 
ATOM   16538 O  O     . LYS A 1 3733 ? 192.637 208.726 272.047 1.00 14.50 ? 3733 LYS A O     1 
ATOM   16539 C  CB    . LYS A 1 3733 ? 190.076 209.867 270.276 1.00 14.28 ? 3733 LYS A CB    1 
ATOM   16540 C  CG    . LYS A 1 3733 ? 191.010 211.061 270.320 1.00 15.17 ? 3733 LYS A CG    1 
ATOM   16541 C  CD    . LYS A 1 3733 ? 190.304 212.332 269.882 1.00 23.30 ? 3733 LYS A CD    1 
ATOM   16542 C  CE    . LYS A 1 3733 ? 189.310 212.798 270.932 1.00 22.53 ? 3733 LYS A CE    1 
ATOM   16543 N  NZ    . LYS A 1 3733 ? 189.989 213.271 272.169 1.00 21.57 ? 3733 LYS A NZ    1 
ATOM   16544 N  N     . LEU A 1 3734 ? 190.631 208.362 273.003 1.00 11.67 ? 3734 LEU A N     1 
ATOM   16545 C  CA    . LEU A 1 3734 ? 191.188 208.330 274.352 1.00 13.97 ? 3734 LEU A CA    1 
ATOM   16546 C  C     . LEU A 1 3734 ? 192.134 207.148 274.534 1.00 14.10 ? 3734 LEU A C     1 
ATOM   16547 O  O     . LEU A 1 3734 ? 193.231 207.296 275.085 1.00 17.62 ? 3734 LEU A O     1 
ATOM   16548 C  CB    . LEU A 1 3734 ? 190.061 208.281 275.386 1.00 15.89 ? 3734 LEU A CB    1 
ATOM   16549 C  CG    . LEU A 1 3734 ? 189.606 209.590 276.040 1.00 17.52 ? 3734 LEU A CG    1 
ATOM   16550 C  CD1   . LEU A 1 3734 ? 189.139 210.608 275.014 1.00 17.57 ? 3734 LEU A CD1   1 
ATOM   16551 C  CD2   . LEU A 1 3734 ? 188.509 209.311 277.052 1.00 16.76 ? 3734 LEU A CD2   1 
ATOM   16552 N  N     . GLN A 1 3735 ? 191.725 205.962 274.076 1.00 10.73 ? 3735 GLN A N     1 
ATOM   16553 C  CA    . GLN A 1 3735 ? 192.571 204.782 274.235 1.00 14.18 ? 3735 GLN A CA    1 
ATOM   16554 C  C     . GLN A 1 3735 ? 193.832 204.884 273.386 1.00 12.41 ? 3735 GLN A C     1 
ATOM   16555 O  O     . GLN A 1 3735 ? 194.892 204.386 273.780 1.00 14.04 ? 3735 GLN A O     1 
ATOM   16556 C  CB    . GLN A 1 3735 ? 191.787 203.515 273.892 1.00 15.72 ? 3735 GLN A CB    1 
ATOM   16557 C  CG    . GLN A 1 3735 ? 190.661 203.220 274.867 1.00 19.06 ? 3735 GLN A CG    1 
ATOM   16558 C  CD    . GLN A 1 3735 ? 189.880 201.974 274.511 1.00 20.82 ? 3735 GLN A CD    1 
ATOM   16559 O  OE1   . GLN A 1 3735 ? 188.977 201.561 275.238 1.00 25.25 ? 3735 GLN A OE1   1 
ATOM   16560 N  NE2   . GLN A 1 3735 ? 190.227 201.364 273.386 1.00 23.60 ? 3735 GLN A NE2   1 
ATOM   16561 N  N     . GLY A 1 3736 ? 193.737 205.516 272.216 1.00 11.61 ? 3736 GLY A N     1 
ATOM   16562 C  CA    . GLY A 1 3736 ? 194.928 205.741 271.416 1.00 10.65 ? 3736 GLY A CA    1 
ATOM   16563 C  C     . GLY A 1 3736 ? 195.934 206.633 272.116 1.00 17.88 ? 3736 GLY A C     1 
ATOM   16564 O  O     . GLY A 1 3736 ? 197.136 206.355 272.111 1.00 17.66 ? 3736 GLY A O     1 
ATOM   16565 N  N     . GLU A 1 3737 ? 195.458 207.717 272.730 1.00 16.38 ? 3737 GLU A N     1 
ATOM   16566 C  CA    . GLU A 1 3737 ? 196.344 208.586 273.496 1.00 17.00 ? 3737 GLU A CA    1 
ATOM   16567 C  C     . GLU A 1 3737 ? 196.870 207.885 274.741 1.00 15.96 ? 3737 GLU A C     1 
ATOM   16568 O  O     . GLU A 1 3737 ? 198.032 208.066 275.119 1.00 18.21 ? 3737 GLU A O     1 
ATOM   16569 C  CB    . GLU A 1 3737 ? 195.620 209.875 273.878 1.00 17.40 ? 3737 GLU A CB    1 
ATOM   16570 C  CG    . GLU A 1 3737 ? 195.166 210.713 272.701 1.00 16.81 ? 3737 GLU A CG    1 
ATOM   16571 C  CD    . GLU A 1 3737 ? 193.824 211.366 272.949 1.00 24.90 ? 3737 GLU A CD    1 
ATOM   16572 O  OE1   . GLU A 1 3737 ? 193.194 211.050 273.979 1.00 24.07 ? 3737 GLU A OE1   1 
ATOM   16573 O  OE2   . GLU A 1 3737 ? 193.402 212.197 272.118 1.00 26.41 ? 3737 GLU A OE2   1 
ATOM   16574 N  N     . PHE A 1 3738 ? 196.023 207.091 275.400 1.00 15.91 ? 3738 PHE A N     1 
ATOM   16575 C  CA    . PHE A 1 3738 ? 196.433 206.423 276.631 1.00 13.30 ? 3738 PHE A CA    1 
ATOM   16576 C  C     . PHE A 1 3738 ? 197.535 205.405 276.366 1.00 16.56 ? 3738 PHE A C     1 
ATOM   16577 O  O     . PHE A 1 3738 ? 198.522 205.344 277.108 1.00 19.85 ? 3738 PHE A O     1 
ATOM   16578 C  CB    . PHE A 1 3738 ? 195.227 205.751 277.281 1.00 12.98 ? 3738 PHE A CB    1 
ATOM   16579 C  CG    . PHE A 1 3738 ? 194.332 206.699 278.024 1.00 18.03 ? 3738 PHE A CG    1 
ATOM   16580 C  CD1   . PHE A 1 3738 ? 193.059 206.312 278.404 1.00 17.86 ? 3738 PHE A CD1   1 
ATOM   16581 C  CD2   . PHE A 1 3738 ? 194.755 207.982 278.326 1.00 16.68 ? 3738 PHE A CD2   1 
ATOM   16582 C  CE1   . PHE A 1 3738 ? 192.229 207.183 279.077 1.00 18.54 ? 3738 PHE A CE1   1 
ATOM   16583 C  CE2   . PHE A 1 3738 ? 193.930 208.858 279.000 1.00 19.09 ? 3738 PHE A CE2   1 
ATOM   16584 C  CZ    . PHE A 1 3738 ? 192.665 208.457 279.377 1.00 17.27 ? 3738 PHE A CZ    1 
ATOM   16585 N  N     . GLN A 1 3739 ? 197.387 204.601 275.310 1.00 14.54 ? 3739 GLN A N     1 
ATOM   16586 C  CA    . GLN A 1 3739 ? 198.431 203.644 274.957 1.00 16.26 ? 3739 GLN A CA    1 
ATOM   16587 C  C     . GLN A 1 3739 ? 199.694 204.355 274.492 1.00 15.92 ? 3739 GLN A C     1 
ATOM   16588 O  O     . GLN A 1 3739 ? 200.807 203.866 274.714 1.00 14.87 ? 3739 GLN A O     1 
ATOM   16589 C  CB    . GLN A 1 3739 ? 197.926 202.683 273.880 1.00 13.40 ? 3739 GLN A CB    1 
ATOM   16590 C  CG    . GLN A 1 3739 ? 196.785 201.793 274.332 1.00 12.84 ? 3739 GLN A CG    1 
ATOM   16591 C  CD    . GLN A 1 3739 ? 197.217 200.786 275.379 1.00 19.44 ? 3739 GLN A CD    1 
ATOM   16592 O  OE1   . GLN A 1 3739 ? 198.397 200.455 275.489 1.00 21.57 ? 3739 GLN A OE1   1 
ATOM   16593 N  NE2   . GLN A 1 3739 ? 196.262 200.300 276.161 1.00 22.34 ? 3739 GLN A NE2   1 
ATOM   16594 N  N     . LEU A 1 3740 ? 199.539 205.506 273.833 1.00 15.47 ? 3740 LEU A N     1 
ATOM   16595 C  CA    . LEU A 1 3740 ? 200.698 206.309 273.458 1.00 12.36 ? 3740 LEU A CA    1 
ATOM   16596 C  C     . LEU A 1 3740 ? 201.463 206.771 274.691 1.00 17.01 ? 3740 LEU A C     1 
ATOM   16597 O  O     . LEU A 1 3740 ? 202.692 206.664 274.748 1.00 22.04 ? 3740 LEU A O     1 
ATOM   16598 C  CB    . LEU A 1 3740 ? 200.250 207.512 272.629 1.00 12.82 ? 3740 LEU A CB    1 
ATOM   16599 C  CG    . LEU A 1 3740 ? 201.313 208.565 272.303 1.00 14.88 ? 3740 LEU A CG    1 
ATOM   16600 C  CD1   . LEU A 1 3740 ? 202.316 208.062 271.277 1.00 16.79 ? 3740 LEU A CD1   1 
ATOM   16601 C  CD2   . LEU A 1 3740 ? 200.665 209.862 271.849 1.00 11.31 ? 3740 LEU A CD2   1 
ATOM   16602 N  N     . ARG A 1 3741 ? 200.743 207.267 275.698 1.00 14.92 ? 3741 ARG A N     1 
ATOM   16603 C  CA    . ARG A 1 3741 ? 201.391 207.796 276.893 1.00 14.41 ? 3741 ARG A CA    1 
ATOM   16604 C  C     . ARG A 1 3741 ? 202.140 206.709 277.652 1.00 15.85 ? 3741 ARG A C     1 
ATOM   16605 O  O     . ARG A 1 3741 ? 203.242 206.945 278.161 1.00 23.16 ? 3741 ARG A O     1 
ATOM   16606 C  CB    . ARG A 1 3741 ? 200.351 208.465 277.791 1.00 15.89 ? 3741 ARG A CB    1 
ATOM   16607 C  CG    . ARG A 1 3741 ? 200.935 209.342 278.880 1.00 18.49 ? 3741 ARG A CG    1 
ATOM   16608 C  CD    . ARG A 1 3741 ? 201.824 210.432 278.309 1.00 19.24 ? 3741 ARG A CD    1 
ATOM   16609 N  NE    . ARG A 1 3741 ? 202.560 211.120 279.363 1.00 24.46 ? 3741 ARG A NE    1 
ATOM   16610 C  CZ    . ARG A 1 3741 ? 203.879 211.095 279.497 1.00 26.23 ? 3741 ARG A CZ    1 
ATOM   16611 N  NH1   . ARG A 1 3741 ? 204.647 210.425 278.655 1.00 27.26 ? 3741 ARG A NH1   1 
ATOM   16612 N  NH2   . ARG A 1 3741 ? 204.440 211.755 280.505 1.00 23.03 ? 3741 ARG A NH2   1 
ATOM   16613 N  N     . LEU A 1 3742 ? 201.556 205.514 277.744 1.00 14.02 ? 3742 LEU A N     1 
ATOM   16614 C  CA    . LEU A 1 3742 ? 202.218 204.417 278.444 1.00 13.85 ? 3742 LEU A CA    1 
ATOM   16615 C  C     . LEU A 1 3742 ? 203.526 204.037 277.761 1.00 16.70 ? 3742 LEU A C     1 
ATOM   16616 O  O     . LEU A 1 3742 ? 204.509 203.697 278.431 1.00 19.57 ? 3742 LEU A O     1 
ATOM   16617 C  CB    . LEU A 1 3742 ? 201.283 203.213 278.531 1.00 11.59 ? 3742 LEU A CB    1 
ATOM   16618 C  CG    . LEU A 1 3742 ? 200.167 203.289 279.577 1.00 17.75 ? 3742 LEU A CG    1 
ATOM   16619 C  CD1   . LEU A 1 3742 ? 199.595 201.908 279.845 1.00 18.94 ? 3742 LEU A CD1   1 
ATOM   16620 C  CD2   . LEU A 1 3742 ? 200.675 203.919 280.867 1.00 15.40 ? 3742 LEU A CD2   1 
ATOM   16621 N  N     . ARG A 1 3743 ? 203.554 204.073 276.427 1.00 18.35 ? 3743 ARG A N     1 
ATOM   16622 C  CA    . ARG A 1 3743 ? 204.787 203.767 275.709 1.00 16.12 ? 3743 ARG A CA    1 
ATOM   16623 C  C     . ARG A 1 3743 ? 205.871 204.798 276.002 1.00 18.02 ? 3743 ARG A C     1 
ATOM   16624 O  O     . ARG A 1 3743 ? 207.040 204.437 276.187 1.00 20.35 ? 3743 ARG A O     1 
ATOM   16625 C  CB    . ARG A 1 3743 ? 204.511 203.671 274.211 1.00 14.80 ? 3743 ARG A CB    1 
ATOM   16626 C  CG    . ARG A 1 3743 ? 204.025 202.303 273.776 1.00 11.90 ? 3743 ARG A CG    1 
ATOM   16627 C  CD    . ARG A 1 3743 ? 203.754 202.252 272.283 1.00 15.23 ? 3743 ARG A CD    1 
ATOM   16628 N  NE    . ARG A 1 3743 ? 202.349 202.491 271.977 1.00 15.09 ? 3743 ARG A NE    1 
ATOM   16629 C  CZ    . ARG A 1 3743 ? 201.890 203.576 271.370 1.00 16.81 ? 3743 ARG A CZ    1 
ATOM   16630 N  NH1   . ARG A 1 3743 ? 202.700 204.544 270.981 1.00 12.67 ? 3743 ARG A NH1   1 
ATOM   16631 N  NH2   . ARG A 1 3743 ? 200.584 203.692 271.150 1.00 17.20 ? 3743 ARG A NH2   1 
ATOM   16632 N  N     . GLN A 1 3744 ? 205.511 206.083 276.049 1.00 15.05 ? 3744 GLN A N     1 
ATOM   16633 C  CA    . GLN A 1 3744 ? 206.481 207.094 276.455 1.00 17.31 ? 3744 GLN A CA    1 
ATOM   16634 C  C     . GLN A 1 3744 ? 206.904 206.899 277.905 1.00 17.78 ? 3744 GLN A C     1 
ATOM   16635 O  O     . GLN A 1 3744 ? 208.074 207.107 278.249 1.00 23.47 ? 3744 GLN A O     1 
ATOM   16636 C  CB    . GLN A 1 3744 ? 205.912 208.499 276.252 1.00 17.99 ? 3744 GLN A CB    1 
ATOM   16637 C  CG    . GLN A 1 3744 ? 204.980 208.638 275.072 1.00 15.25 ? 3744 GLN A CG    1 
ATOM   16638 C  CD    . GLN A 1 3744 ? 204.781 210.079 274.650 1.00 21.55 ? 3744 GLN A CD    1 
ATOM   16639 O  OE1   . GLN A 1 3744 ? 204.410 210.928 275.459 1.00 21.55 ? 3744 GLN A OE1   1 
ATOM   16640 N  NE2   . GLN A 1 3744 ? 205.023 210.363 273.376 1.00 24.53 ? 3744 GLN A NE2   1 
ATOM   16641 N  N     . LEU A 1 3745 ? 205.965 206.510 278.770 1.00 16.39 ? 3745 LEU A N     1 
ATOM   16642 C  CA    . LEU A 1 3745 ? 206.285 206.336 280.184 1.00 20.25 ? 3745 LEU A CA    1 
ATOM   16643 C  C     . LEU A 1 3745 ? 207.289 205.211 280.399 1.00 18.75 ? 3745 LEU A C     1 
ATOM   16644 O  O     . LEU A 1 3745 ? 208.221 205.351 281.198 1.00 25.03 ? 3745 LEU A O     1 
ATOM   16645 C  CB    . LEU A 1 3745 ? 205.006 206.082 280.981 1.00 22.08 ? 3745 LEU A CB    1 
ATOM   16646 C  CG    . LEU A 1 3745 ? 204.190 207.346 281.253 1.00 19.61 ? 3745 LEU A CG    1 
ATOM   16647 C  CD1   . LEU A 1 3745 ? 202.773 207.007 281.668 1.00 19.86 ? 3745 LEU A CD1   1 
ATOM   16648 C  CD2   . LEU A 1 3745 ? 204.873 208.193 282.310 1.00 20.62 ? 3745 LEU A CD2   1 
ATOM   16649 N  N     . GLU A 1 3746 ? 207.117 204.087 279.700 1.00 19.99 ? 3746 GLU A N     1 
ATOM   16650 C  CA    . GLU A 1 3746 ? 208.077 202.997 279.845 1.00 21.27 ? 3746 GLU A CA    1 
ATOM   16651 C  C     . GLU A 1 3746 ? 209.398 203.326 279.163 1.00 24.63 ? 3746 GLU A C     1 
ATOM   16652 O  O     . GLU A 1 3746 ? 210.457 202.879 279.618 1.00 28.98 ? 3746 GLU A O     1 
ATOM   16653 C  CB    . GLU A 1 3746 ? 207.497 201.694 279.294 1.00 17.59 ? 3746 GLU A CB    1 
ATOM   16654 C  CG    . GLU A 1 3746 ? 207.260 201.687 277.797 1.00 24.21 ? 3746 GLU A CG    1 
ATOM   16655 C  CD    . GLU A 1 3746 ? 206.696 200.372 277.301 1.00 33.23 ? 3746 GLU A CD    1 
ATOM   16656 O  OE1   . GLU A 1 3746 ? 206.476 199.464 278.131 1.00 30.71 ? 3746 GLU A OE1   1 
ATOM   16657 O  OE2   . GLU A 1 3746 ? 206.473 200.246 276.078 1.00 33.03 ? 3746 GLU A OE2   1 
ATOM   16658 N  N     . LYS A 1 3747 ? 209.359 204.099 278.076 1.00 20.21 ? 3747 LYS A N     1 
ATOM   16659 C  CA    . LYS A 1 3747 ? 210.592 204.527 277.426 1.00 20.81 ? 3747 LYS A CA    1 
ATOM   16660 C  C     . LYS A 1 3747 ? 211.352 205.523 278.295 1.00 25.63 ? 3747 LYS A C     1 
ATOM   16661 O  O     . LYS A 1 3747 ? 212.561 205.379 278.507 1.00 32.25 ? 3747 LYS A O     1 
ATOM   16662 C  CB    . LYS A 1 3747 ? 210.279 205.133 276.057 1.00 18.67 ? 3747 LYS A CB    1 
ATOM   16663 C  CG    . LYS A 1 3747 ? 211.430 205.906 275.444 1.00 21.44 ? 3747 LYS A CG    1 
ATOM   16664 C  CD    . LYS A 1 3747 ? 211.096 206.381 274.039 1.00 22.02 ? 3747 LYS A CD    1 
ATOM   16665 C  CE    . LYS A 1 3747 ? 210.834 205.212 273.106 1.00 24.64 ? 3747 LYS A CE    1 
ATOM   16666 N  NZ    . LYS A 1 3747 ? 210.589 205.664 271.709 1.00 24.55 ? 3747 LYS A NZ    1 
ATOM   16667 N  N     . SER A 1 3748 ? 210.654 206.539 278.812 1.00 24.46 ? 3748 SER A N     1 
ATOM   16668 C  CA    . SER A 1 3748 ? 211.311 207.545 279.641 1.00 23.73 ? 3748 SER A CA    1 
ATOM   16669 C  C     . SER A 1 3748 ? 211.871 206.933 280.917 1.00 21.25 ? 3748 SER A C     1 
ATOM   16670 O  O     . SER A 1 3748 ? 212.984 207.266 281.339 1.00 24.11 ? 3748 SER A O     1 
ATOM   16671 C  CB    . SER A 1 3748 ? 210.334 208.672 279.976 1.00 26.74 ? 3748 SER A CB    1 
ATOM   16672 O  OG    . SER A 1 3748 ? 209.822 209.277 278.802 1.00 30.40 ? 3748 SER A OG    1 
ATOM   16673 N  N     . LEU A 1 3749 ? 211.113 206.034 281.548 1.00 18.31 ? 3749 LEU A N     1 
ATOM   16674 C  CA    . LEU A 1 3749 ? 211.579 205.409 282.781 1.00 19.89 ? 3749 LEU A CA    1 
ATOM   16675 C  C     . LEU A 1 3749 ? 212.811 204.553 282.518 1.00 18.43 ? 3749 LEU A C     1 
ATOM   16676 O  O     . LEU A 1 3749 ? 213.736 204.510 283.338 1.00 23.20 ? 3749 LEU A O     1 
ATOM   16677 C  CB    . LEU A 1 3749 ? 210.449 204.590 283.407 1.00 22.59 ? 3749 LEU A CB    1 
ATOM   16678 C  CG    . LEU A 1 3749 ? 210.605 203.971 284.801 1.00 22.99 ? 3749 LEU A CG    1 
ATOM   16679 C  CD1   . LEU A 1 3749 ? 209.233 203.818 285.430 1.00 24.36 ? 3749 LEU A CD1   1 
ATOM   16680 C  CD2   . LEU A 1 3749 ? 211.306 202.629 284.761 1.00 23.72 ? 3749 LEU A CD2   1 
ATOM   16681 N  N     . LEU A 1 3750 ? 212.841 203.861 281.377 1.00 23.04 ? 3750 LEU A N     1 
ATOM   16682 C  CA    . LEU A 1 3750 ? 214.038 203.126 280.986 1.00 22.83 ? 3750 LEU A CA    1 
ATOM   16683 C  C     . LEU A 1 3750 ? 215.207 204.069 280.730 1.00 23.60 ? 3750 LEU A C     1 
ATOM   16684 O  O     . LEU A 1 3750 ? 216.343 203.782 281.127 1.00 25.27 ? 3750 LEU A O     1 
ATOM   16685 C  CB    . LEU A 1 3750 ? 213.750 202.277 279.749 1.00 19.64 ? 3750 LEU A CB    1 
ATOM   16686 C  CG    . LEU A 1 3750 ? 214.586 201.008 279.575 1.00 20.99 ? 3750 LEU A CG    1 
ATOM   16687 C  CD1   . LEU A 1 3750 ? 214.583 200.186 280.848 1.00 23.21 ? 3750 LEU A CD1   1 
ATOM   16688 C  CD2   . LEU A 1 3750 ? 214.079 200.187 278.401 1.00 17.16 ? 3750 LEU A CD2   1 
ATOM   16689 N  N     . GLN A 1 3751 ? 214.950 205.204 280.073 1.00 19.88 ? 3751 GLN A N     1 
ATOM   16690 C  CA    . GLN A 1 3751 ? 216.019 206.159 279.796 1.00 22.08 ? 3751 GLN A CA    1 
ATOM   16691 C  C     . GLN A 1 3751 ? 216.614 206.714 281.085 1.00 27.12 ? 3751 GLN A C     1 
ATOM   16692 O  O     . GLN A 1 3751 ? 217.826 206.946 281.167 1.00 30.51 ? 3751 GLN A O     1 
ATOM   16693 C  CB    . GLN A 1 3751 ? 215.500 207.303 278.923 1.00 18.01 ? 3751 GLN A CB    1 
ATOM   16694 C  CG    . GLN A 1 3751 ? 215.144 206.917 277.498 1.00 26.78 ? 3751 GLN A CG    1 
ATOM   16695 C  CD    . GLN A 1 3751 ? 216.068 205.863 276.921 1.00 33.41 ? 3751 GLN A CD    1 
ATOM   16696 O  OE1   . GLN A 1 3751 ? 217.270 206.086 276.777 1.00 33.36 ? 3751 GLN A OE1   1 
ATOM   16697 N  NE2   . GLN A 1 3751 ? 215.507 204.707 276.583 1.00 30.84 ? 3751 GLN A NE2   1 
ATOM   16698 N  N     . ALA A 1 3752 ? 215.774 206.945 282.097 1.00 22.15 ? 3752 ALA A N     1 
ATOM   16699 C  CA    . ALA A 1 3752 ? 216.261 207.512 283.350 1.00 22.56 ? 3752 ALA A CA    1 
ATOM   16700 C  C     . ALA A 1 3752 ? 217.266 206.589 284.024 1.00 22.13 ? 3752 ALA A C     1 
ATOM   16701 O  O     . ALA A 1 3752 ? 218.277 207.051 284.564 1.00 28.62 ? 3752 ALA A O     1 
ATOM   16702 C  CB    . ALA A 1 3752 ? 215.086 207.802 284.285 1.00 23.42 ? 3752 ALA A CB    1 
ATOM   16703 N  N     . LEU A 1 3753 ? 217.004 205.282 284.007 1.00 20.34 ? 3753 LEU A N     1 
ATOM   16704 C  CA    . LEU A 1 3753 ? 217.950 204.328 284.569 1.00 20.98 ? 3753 LEU A CA    1 
ATOM   16705 C  C     . LEU A 1 3753 ? 219.152 204.104 283.665 1.00 25.48 ? 3753 LEU A C     1 
ATOM   16706 O  O     . LEU A 1 3753 ? 220.191 203.637 284.142 1.00 30.08 ? 3753 LEU A O     1 
ATOM   16707 C  CB    . LEU A 1 3753 ? 217.257 202.993 284.841 1.00 21.66 ? 3753 LEU A CB    1 
ATOM   16708 C  CG    . LEU A 1 3753 ? 216.529 202.839 286.176 1.00 19.11 ? 3753 LEU A CG    1 
ATOM   16709 C  CD1   . LEU A 1 3753 ? 215.230 203.623 286.182 1.00 18.44 ? 3753 LEU A CD1   1 
ATOM   16710 C  CD2   . LEU A 1 3753 ? 216.273 201.369 286.464 1.00 24.37 ? 3753 LEU A CD2   1 
ATOM   16711 N  N     . ASN A 1 3754 ? 219.035 204.415 282.375 1.00 28.93 ? 3754 ASN A N     1 
ATOM   16712 C  CA    . ASN A 1 3754 ? 220.119 204.203 281.427 1.00 21.85 ? 3754 ASN A CA    1 
ATOM   16713 C  C     . ASN A 1 3754 ? 221.007 205.426 281.251 1.00 26.13 ? 3754 ASN A C     1 
ATOM   16714 O  O     . ASN A 1 3754 ? 222.037 205.329 280.575 1.00 34.48 ? 3754 ASN A O     1 
ATOM   16715 C  CB    . ASN A 1 3754 ? 219.551 203.788 280.068 1.00 24.70 ? 3754 ASN A CB    1 
ATOM   16716 C  CG    . ASN A 1 3754 ? 218.878 202.431 280.107 1.00 25.67 ? 3754 ASN A CG    1 
ATOM   16717 O  OD1   . ASN A 1 3754 ? 219.461 201.448 280.560 1.00 24.10 ? 3754 ASN A OD1   1 
ATOM   16718 N  ND2   . ASN A 1 3754 ? 217.636 202.376 279.644 1.00 32.06 ? 3754 ASN A ND2   1 
ATOM   16719 N  N     . GLU A 1 3755 ? 220.642 206.564 281.837 1.00 28.47 ? 3755 GLU A N     1 
ATOM   16720 C  CA    . GLU A 1 3755 ? 221.415 207.790 281.707 1.00 27.24 ? 3755 GLU A CA    1 
ATOM   16721 C  C     . GLU A 1 3755 ? 221.941 208.313 283.035 1.00 27.26 ? 3755 GLU A C     1 
ATOM   16722 O  O     . GLU A 1 3755 ? 222.623 209.343 283.052 1.00 30.13 ? 3755 GLU A O     1 
ATOM   16723 C  CB    . GLU A 1 3755 ? 220.571 208.875 281.026 1.00 24.43 ? 3755 GLU A CB    1 
ATOM   16724 C  CG    . GLU A 1 3755 ? 220.234 208.577 279.575 1.00 26.79 ? 3755 GLU A CG    1 
ATOM   16725 C  CD    . GLU A 1 3755 ? 221.455 208.590 278.677 1.00 33.76 ? 3755 GLU A CD    1 
ATOM   16726 O  OE1   . GLU A 1 3755 ? 222.386 209.377 278.949 1.00 35.42 ? 3755 GLU A OE1   1 
ATOM   16727 O  OE2   . GLU A 1 3755 ? 221.484 207.813 277.700 1.00 37.40 ? 3755 GLU A OE2   1 
ATOM   16728 N  N     . VAL A 1 3756 ? 221.650 207.641 284.139 1.00 25.45 ? 3756 VAL A N     1 
ATOM   16729 C  CA    . VAL A 1 3756 ? 222.069 208.098 285.459 1.00 26.91 ? 3756 VAL A CA    1 
ATOM   16730 C  C     . VAL A 1 3756 ? 223.422 207.485 285.799 1.00 29.49 ? 3756 VAL A C     1 
ATOM   16731 O  O     . VAL A 1 3756 ? 223.664 206.296 285.562 1.00 33.96 ? 3756 VAL A O     1 
ATOM   16732 C  CB    . VAL A 1 3756 ? 221.006 207.753 286.521 1.00 29.60 ? 3756 VAL A CB    1 
ATOM   16733 C  CG1   . VAL A 1 3756 ? 220.719 206.256 286.537 1.00 26.37 ? 3756 VAL A CG1   1 
ATOM   16734 C  CG2   . VAL A 1 3756 ? 221.442 208.241 287.894 1.00 24.41 ? 3756 VAL A CG2   1 
ATOM   16735 N  N     . LYS A 1 3757 ? 224.314 208.306 286.342 1.00 29.85 ? 3757 LYS A N     1 
ATOM   16736 C  CA    . LYS A 1 3757 ? 225.649 207.873 286.721 1.00 31.11 ? 3757 LYS A CA    1 
ATOM   16737 C  C     . LYS A 1 3757 ? 225.711 207.582 288.215 1.00 31.80 ? 3757 LYS A C     1 
ATOM   16738 O  O     . LYS A 1 3757 ? 224.908 208.084 289.006 1.00 30.61 ? 3757 LYS A O     1 
ATOM   16739 C  CB    . LYS A 1 3757 ? 226.689 208.932 286.347 1.00 24.55 ? 3757 LYS A CB    1 
ATOM   16740 C  CG    . LYS A 1 3757 ? 226.522 209.499 284.945 1.00 29.79 ? 3757 LYS A CG    1 
ATOM   16741 C  CD    . LYS A 1 3757 ? 226.597 208.409 283.887 1.00 29.90 ? 3757 LYS A CD    1 
ATOM   16742 C  CE    . LYS A 1 3757 ? 227.973 207.767 283.846 1.00 32.63 ? 3757 LYS A CE    1 
ATOM   16743 N  NZ    . LYS A 1 3757 ? 228.029 206.642 282.872 1.00 31.61 ? 3757 LYS A NZ    1 
ATOM   16744 N  N     . GLY A 1 3758 ? 226.682 206.762 288.593 1.00 33.34 ? 3758 GLY A N     1 
ATOM   16745 C  CA    . GLY A 1 3758 ? 226.825 206.387 289.991 1.00 28.49 ? 3758 GLY A CA    1 
ATOM   16746 C  C     . GLY A 1 3758 ? 225.627 205.586 290.459 1.00 34.08 ? 3758 GLY A C     1 
ATOM   16747 O  O     . GLY A 1 3758 ? 225.260 204.565 289.864 1.00 35.54 ? 3758 GLY A O     1 
ATOM   16748 N  N     . ARG A 1 3759 ? 224.997 206.046 291.537 1.00 32.20 ? 3759 ARG A N     1 
ATOM   16749 C  CA    . ARG A 1 3759 ? 223.851 205.374 292.126 1.00 30.24 ? 3759 ARG A CA    1 
ATOM   16750 C  C     . ARG A 1 3759 ? 222.611 206.253 292.013 1.00 30.90 ? 3759 ARG A C     1 
ATOM   16751 O  O     . ARG A 1 3759 ? 222.702 207.482 291.960 1.00 31.84 ? 3759 ARG A O     1 
ATOM   16752 C  CB    . ARG A 1 3759 ? 224.109 205.020 293.596 1.00 32.34 ? 3759 ARG A CB    1 
ATOM   16753 C  CG    . ARG A 1 3759 ? 225.450 204.345 293.842 1.00 31.12 ? 3759 ARG A CG    1 
ATOM   16754 C  CD    . ARG A 1 3759 ? 225.815 204.350 295.317 1.00 30.13 ? 3759 ARG A CD    1 
ATOM   16755 N  NE    . ARG A 1 3759 ? 226.329 205.648 295.743 1.00 32.77 ? 3759 ARG A NE    1 
ATOM   16756 C  CZ    . ARG A 1 3759 ? 226.689 205.940 296.985 1.00 34.47 ? 3759 ARG A CZ    1 
ATOM   16757 N  NH1   . ARG A 1 3759 ? 226.606 205.047 297.957 1.00 32.33 ? 3759 ARG A NH1   1 
ATOM   16758 N  NH2   . ARG A 1 3759 ? 227.144 207.159 297.259 1.00 29.68 ? 3759 ARG A NH2   1 
ATOM   16759 N  N     . ILE A 1 3760 ? 221.449 205.599 291.962 1.00 29.52 ? 3760 ILE A N     1 
ATOM   16760 C  CA    . ILE A 1 3760 ? 220.184 206.321 291.873 1.00 30.56 ? 3760 ILE A CA    1 
ATOM   16761 C  C     . ILE A 1 3760 ? 219.943 207.144 293.134 1.00 33.58 ? 3760 ILE A C     1 
ATOM   16762 O  O     . ILE A 1 3760 ? 219.511 208.301 293.063 1.00 35.88 ? 3760 ILE A O     1 
ATOM   16763 C  CB    . ILE A 1 3760 ? 219.032 205.336 291.607 1.00 28.28 ? 3760 ILE A CB    1 
ATOM   16764 C  CG1   . ILE A 1 3760 ? 219.208 204.663 290.245 1.00 26.03 ? 3760 ILE A CG1   1 
ATOM   16765 C  CG2   . ILE A 1 3760 ? 217.686 206.041 291.690 1.00 30.06 ? 3760 ILE A CG2   1 
ATOM   16766 C  CD1   . ILE A 1 3760 ? 218.134 203.652 289.922 1.00 25.11 ? 3760 ILE A CD1   1 
ATOM   16767 N  N     . LEU A 1 3761 ? 220.228 206.566 294.305 1.00 28.24 ? 3761 LEU A N     1 
ATOM   16768 C  CA    . LEU A 1 3761 ? 219.939 207.243 295.565 1.00 29.91 ? 3761 LEU A CA    1 
ATOM   16769 C  C     . LEU A 1 3761 ? 220.759 208.515 295.734 1.00 34.98 ? 3761 LEU A C     1 
ATOM   16770 O  O     . LEU A 1 3761 ? 220.350 209.421 296.471 1.00 37.33 ? 3761 LEU A O     1 
ATOM   16771 C  CB    . LEU A 1 3761 ? 220.198 206.300 296.741 1.00 26.37 ? 3761 LEU A CB    1 
ATOM   16772 C  CG    . LEU A 1 3761 ? 219.168 205.206 297.014 1.00 25.49 ? 3761 LEU A CG    1 
ATOM   16773 C  CD1   . LEU A 1 3761 ? 219.490 203.965 296.204 1.00 30.96 ? 3761 LEU A CD1   1 
ATOM   16774 C  CD2   . LEU A 1 3761 ? 219.115 204.883 298.498 1.00 27.54 ? 3761 LEU A CD2   1 
ATOM   16775 N  N     . ASP A 1 3762 ? 221.917 208.603 295.074 1.00 34.56 ? 3762 ASP A N     1 
ATOM   16776 C  CA    . ASP A 1 3762 ? 222.772 209.775 295.237 1.00 33.42 ? 3762 ASP A CA    1 
ATOM   16777 C  C     . ASP A 1 3762 ? 222.083 211.042 294.742 1.00 36.28 ? 3762 ASP A C     1 
ATOM   16778 O  O     . ASP A 1 3762 ? 222.185 212.099 295.375 1.00 39.33 ? 3762 ASP A O     1 
ATOM   16779 C  CB    . ASP A 1 3762 ? 224.097 209.565 294.506 1.00 33.23 ? 3762 ASP A CB    1 
ATOM   16780 C  CG    . ASP A 1 3762 ? 224.982 208.543 295.190 1.00 36.01 ? 3762 ASP A CG    1 
ATOM   16781 O  OD1   . ASP A 1 3762 ? 225.063 208.566 296.436 1.00 33.54 ? 3762 ASP A OD1   1 
ATOM   16782 O  OD2   . ASP A 1 3762 ? 225.601 207.720 294.483 1.00 35.30 ? 3762 ASP A OD2   1 
ATOM   16783 N  N     . ASP A 1 3763 ? 221.382 210.957 293.616 1.00 34.67 ? 3763 ASP A N     1 
ATOM   16784 C  CA    . ASP A 1 3763 ? 220.691 212.100 293.031 1.00 35.48 ? 3763 ASP A CA    1 
ATOM   16785 C  C     . ASP A 1 3763 ? 219.199 211.968 293.319 1.00 35.34 ? 3763 ASP A C     1 
ATOM   16786 O  O     . ASP A 1 3763 ? 218.526 211.101 292.754 1.00 34.87 ? 3763 ASP A O     1 
ATOM   16787 C  CB    . ASP A 1 3763 ? 220.956 212.186 291.529 1.00 33.33 ? 3763 ASP A CB    1 
ATOM   16788 C  CG    . ASP A 1 3763 ? 220.288 213.387 290.889 1.00 39.54 ? 3763 ASP A CG    1 
ATOM   16789 O  OD1   . ASP A 1 3763 ? 220.544 214.524 291.340 1.00 38.21 ? 3763 ASP A OD1   1 
ATOM   16790 O  OD2   . ASP A 1 3763 ? 219.508 213.195 289.932 1.00 38.17 ? 3763 ASP A OD2   1 
ATOM   16791 N  N     . ASP A 1 3764 ? 218.687 212.834 294.198 1.00 37.64 ? 3764 ASP A N     1 
ATOM   16792 C  CA    . ASP A 1 3764 ? 217.270 212.803 294.537 1.00 33.53 ? 3764 ASP A CA    1 
ATOM   16793 C  C     . ASP A 1 3764 ? 216.383 213.189 293.362 1.00 33.26 ? 3764 ASP A C     1 
ATOM   16794 O  O     . ASP A 1 3764 ? 215.199 212.835 293.355 1.00 35.71 ? 3764 ASP A O     1 
ATOM   16795 C  CB    . ASP A 1 3764 ? 216.992 213.730 295.722 1.00 34.27 ? 3764 ASP A CB    1 
ATOM   16796 C  CG    . ASP A 1 3764 ? 217.588 213.214 297.017 1.00 39.45 ? 3764 ASP A CG    1 
ATOM   16797 O  OD1   . ASP A 1 3764 ? 218.267 212.166 296.986 1.00 39.24 ? 3764 ASP A OD1   1 
ATOM   16798 O  OD2   . ASP A 1 3764 ? 217.377 213.857 298.068 1.00 38.74 ? 3764 ASP A OD2   1 
ATOM   16799 N  N     . THR A 1 3765 ? 216.925 213.906 292.375 1.00 28.75 ? 3765 THR A N     1 
ATOM   16800 C  CA    . THR A 1 3765 ? 216.140 214.259 291.197 1.00 30.21 ? 3765 THR A CA    1 
ATOM   16801 C  C     . THR A 1 3765 ? 215.711 213.015 290.429 1.00 30.07 ? 3765 THR A C     1 
ATOM   16802 O  O     . THR A 1 3765 ? 214.555 212.908 290.003 1.00 32.63 ? 3765 THR A O     1 
ATOM   16803 C  CB    . THR A 1 3765 ? 216.939 215.199 290.294 1.00 29.54 ? 3765 THR A CB    1 
ATOM   16804 O  OG1   . THR A 1 3765 ? 217.314 216.368 291.032 1.00 32.13 ? 3765 THR A OG1   1 
ATOM   16805 C  CG2   . THR A 1 3765 ? 216.112 215.612 289.088 1.00 24.81 ? 3765 THR A CG2   1 
ATOM   16806 N  N     . ILE A 1 3766 ? 216.624 212.057 290.256 1.00 27.96 ? 3766 ILE A N     1 
ATOM   16807 C  CA    . ILE A 1 3766 ? 216.288 210.815 289.563 1.00 28.52 ? 3766 ILE A CA    1 
ATOM   16808 C  C     . ILE A 1 3766 ? 215.190 210.070 290.308 1.00 30.34 ? 3766 ILE A C     1 
ATOM   16809 O  O     . ILE A 1 3766 ? 214.270 209.514 289.694 1.00 30.20 ? 3766 ILE A O     1 
ATOM   16810 C  CB    . ILE A 1 3766 ? 217.547 209.946 289.383 1.00 29.48 ? 3766 ILE A CB    1 
ATOM   16811 C  CG1   . ILE A 1 3766 ? 218.466 210.554 288.325 1.00 25.21 ? 3766 ILE A CG1   1 
ATOM   16812 C  CG2   . ILE A 1 3766 ? 217.174 208.522 288.999 1.00 26.89 ? 3766 ILE A CG2   1 
ATOM   16813 C  CD1   . ILE A 1 3766 ? 217.843 210.620 286.949 1.00 28.47 ? 3766 ILE A CD1   1 
ATOM   16814 N  N     . ILE A 1 3767 ? 215.262 210.051 291.642 1.00 28.63 ? 3767 ILE A N     1 
ATOM   16815 C  CA    . ILE A 1 3767 ? 214.239 209.375 292.435 1.00 27.92 ? 3767 ILE A CA    1 
ATOM   16816 C  C     . ILE A 1 3767 ? 212.881 210.033 292.228 1.00 29.17 ? 3767 ILE A C     1 
ATOM   16817 O  O     . ILE A 1 3767 ? 211.865 209.351 292.052 1.00 32.39 ? 3767 ILE A O     1 
ATOM   16818 C  CB    . ILE A 1 3767 ? 214.639 209.355 293.920 1.00 29.39 ? 3767 ILE A CB    1 
ATOM   16819 C  CG1   . ILE A 1 3767 ? 215.985 208.650 294.100 1.00 30.82 ? 3767 ILE A CG1   1 
ATOM   16820 C  CG2   . ILE A 1 3767 ? 213.559 208.688 294.758 1.00 24.98 ? 3767 ILE A CG2   1 
ATOM   16821 C  CD1   . ILE A 1 3767 ? 216.419 208.520 295.545 1.00 31.42 ? 3767 ILE A CD1   1 
ATOM   16822 N  N     . THR A 1 3768 ? 212.841 211.367 292.243 1.00 28.79 ? 3768 THR A N     1 
ATOM   16823 C  CA    . THR A 1 3768 ? 211.580 212.071 292.030 1.00 26.73 ? 3768 THR A CA    1 
ATOM   16824 C  C     . THR A 1 3768 ? 211.021 211.801 290.640 1.00 27.58 ? 3768 THR A C     1 
ATOM   16825 O  O     . THR A 1 3768 ? 209.811 211.605 290.477 1.00 31.65 ? 3768 THR A O     1 
ATOM   16826 C  CB    . THR A 1 3768 ? 211.773 213.570 292.246 1.00 26.93 ? 3768 THR A CB    1 
ATOM   16827 O  OG1   . THR A 1 3768 ? 212.838 214.039 291.411 1.00 32.06 ? 3768 THR A OG1   1 
ATOM   16828 C  CG2   . THR A 1 3768 ? 212.106 213.860 293.701 1.00 25.45 ? 3768 THR A CG2   1 
ATOM   16829 N  N     . THR A 1 3769 ? 211.885 211.788 289.622 1.00 28.08 ? 3769 THR A N     1 
ATOM   16830 C  CA    . THR A 1 3769 ? 211.419 211.546 288.260 1.00 29.74 ? 3769 THR A CA    1 
ATOM   16831 C  C     . THR A 1 3769 ? 210.826 210.152 288.113 1.00 24.98 ? 3769 THR A C     1 
ATOM   16832 O  O     . THR A 1 3769 ? 209.792 209.977 287.458 1.00 30.48 ? 3769 THR A O     1 
ATOM   16833 C  CB    . THR A 1 3769 ? 212.561 211.744 287.266 1.00 27.69 ? 3769 THR A CB    1 
ATOM   16834 O  OG1   . THR A 1 3769 ? 213.657 210.889 287.617 1.00 31.91 ? 3769 THR A OG1   1 
ATOM   16835 C  CG2   . THR A 1 3769 ? 213.023 213.195 287.268 1.00 26.10 ? 3769 THR A CG2   1 
ATOM   16836 N  N     . LEU A 1 3770 ? 211.464 209.146 288.714 1.00 24.18 ? 3770 LEU A N     1 
ATOM   16837 C  CA    . LEU A 1 3770 ? 210.930 207.789 288.644 1.00 25.29 ? 3770 LEU A CA    1 
ATOM   16838 C  C     . LEU A 1 3770 ? 209.564 207.702 289.309 1.00 28.13 ? 3770 LEU A C     1 
ATOM   16839 O  O     . LEU A 1 3770 ? 208.650 207.056 288.785 1.00 30.63 ? 3770 LEU A O     1 
ATOM   16840 C  CB    . LEU A 1 3770 ? 211.902 206.804 289.292 1.00 22.43 ? 3770 LEU A CB    1 
ATOM   16841 C  CG    . LEU A 1 3770 ? 213.261 206.629 288.618 1.00 19.55 ? 3770 LEU A CG    1 
ATOM   16842 C  CD1   . LEU A 1 3770 ? 213.992 205.431 289.200 1.00 20.82 ? 3770 LEU A CD1   1 
ATOM   16843 C  CD2   . LEU A 1 3770 ? 213.095 206.483 287.116 1.00 21.91 ? 3770 LEU A CD2   1 
ATOM   16844 N  N     . GLU A 1 3771 ? 209.407 208.347 290.467 1.00 27.48 ? 3771 GLU A N     1 
ATOM   16845 C  CA    . GLU A 1 3771 ? 208.116 208.339 291.146 1.00 24.20 ? 3771 GLU A CA    1 
ATOM   16846 C  C     . GLU A 1 3771 ? 207.045 209.012 290.299 1.00 28.12 ? 3771 GLU A C     1 
ATOM   16847 O  O     . GLU A 1 3771 ? 205.922 208.508 290.190 1.00 30.17 ? 3771 GLU A O     1 
ATOM   16848 C  CB    . GLU A 1 3771 ? 208.239 209.026 292.504 1.00 29.20 ? 3771 GLU A CB    1 
ATOM   16849 C  CG    . GLU A 1 3771 ? 209.186 208.335 293.467 1.00 27.39 ? 3771 GLU A CG    1 
ATOM   16850 C  CD    . GLU A 1 3771 ? 209.550 209.209 294.649 1.00 30.10 ? 3771 GLU A CD    1 
ATOM   16851 O  OE1   . GLU A 1 3771 ? 209.981 210.360 294.426 1.00 33.11 ? 3771 GLU A OE1   1 
ATOM   16852 O  OE2   . GLU A 1 3771 ? 209.411 208.746 295.801 1.00 33.72 ? 3771 GLU A OE2   1 
ATOM   16853 N  N     . ASN A 1 3772 ? 207.375 210.153 289.688 1.00 24.90 ? 3772 ASN A N     1 
ATOM   16854 C  CA    . ASN A 1 3772 ? 206.404 210.856 288.857 1.00 23.16 ? 3772 ASN A CA    1 
ATOM   16855 C  C     . ASN A 1 3772 ? 206.034 210.041 287.623 1.00 24.10 ? 3772 ASN A C     1 
ATOM   16856 O  O     . ASN A 1 3772 ? 204.859 209.986 287.242 1.00 22.26 ? 3772 ASN A O     1 
ATOM   16857 C  CB    . ASN A 1 3772 ? 206.951 212.226 288.456 1.00 22.74 ? 3772 ASN A CB    1 
ATOM   16858 C  CG    . ASN A 1 3772 ? 207.240 213.111 289.653 1.00 27.39 ? 3772 ASN A CG    1 
ATOM   16859 O  OD1   . ASN A 1 3772 ? 207.086 212.692 290.800 1.00 26.63 ? 3772 ASN A OD1   1 
ATOM   16860 N  ND2   . ASN A 1 3772 ? 207.658 214.343 289.390 1.00 30.93 ? 3772 ASN A ND2   1 
ATOM   16861 N  N     . LEU A 1 3773 ? 207.021 209.410 286.984 1.00 24.89 ? 3773 LEU A N     1 
ATOM   16862 C  CA    . LEU A 1 3773 ? 206.722 208.534 285.855 1.00 23.53 ? 3773 LEU A CA    1 
ATOM   16863 C  C     . LEU A 1 3773 ? 205.901 207.330 286.295 1.00 23.10 ? 3773 LEU A C     1 
ATOM   16864 O  O     . LEU A 1 3773 ? 204.956 206.929 285.608 1.00 28.95 ? 3773 LEU A O     1 
ATOM   16865 C  CB    . LEU A 1 3773 ? 208.017 208.085 285.181 1.00 24.10 ? 3773 LEU A CB    1 
ATOM   16866 C  CG    . LEU A 1 3773 ? 208.838 209.186 284.508 1.00 24.03 ? 3773 LEU A CG    1 
ATOM   16867 C  CD1   . LEU A 1 3773 ? 210.094 208.608 283.882 1.00 19.36 ? 3773 LEU A CD1   1 
ATOM   16868 C  CD2   . LEU A 1 3773 ? 208.004 209.920 283.469 1.00 23.80 ? 3773 LEU A CD2   1 
ATOM   16869 N  N     . LYS A 1 3774 ? 206.247 206.739 287.440 1.00 22.90 ? 3774 LYS A N     1 
ATOM   16870 C  CA    . LYS A 1 3774 ? 205.452 205.636 287.969 1.00 23.26 ? 3774 LYS A CA    1 
ATOM   16871 C  C     . LYS A 1 3774 ? 204.057 206.097 288.369 1.00 23.53 ? 3774 LYS A C     1 
ATOM   16872 O  O     . LYS A 1 3774 ? 203.073 205.387 288.134 1.00 28.20 ? 3774 LYS A O     1 
ATOM   16873 C  CB    . LYS A 1 3774 ? 206.166 204.992 289.157 1.00 20.82 ? 3774 LYS A CB    1 
ATOM   16874 C  CG    . LYS A 1 3774 ? 207.286 204.048 288.762 1.00 22.74 ? 3774 LYS A CG    1 
ATOM   16875 C  CD    . LYS A 1 3774 ? 206.747 202.843 288.009 1.00 26.31 ? 3774 LYS A CD    1 
ATOM   16876 C  CE    . LYS A 1 3774 ? 205.626 202.158 288.778 1.00 27.61 ? 3774 LYS A CE    1 
ATOM   16877 N  NZ    . LYS A 1 3774 ? 205.199 200.882 288.146 1.00 28.37 ? 3774 LYS A NZ    1 
ATOM   16878 N  N     . ARG A 1 3775 ? 203.952 207.278 288.984 1.00 25.31 ? 3775 ARG A N     1 
ATOM   16879 C  CA    . ARG A 1 3775 ? 202.645 207.789 289.384 1.00 24.28 ? 3775 ARG A CA    1 
ATOM   16880 C  C     . ARG A 1 3775 ? 201.757 208.045 288.174 1.00 22.12 ? 3775 ARG A C     1 
ATOM   16881 O  O     . ARG A 1 3775 ? 200.570 207.700 288.182 1.00 24.60 ? 3775 ARG A O     1 
ATOM   16882 C  CB    . ARG A 1 3775 ? 202.811 209.066 290.206 1.00 22.22 ? 3775 ARG A CB    1 
ATOM   16883 C  CG    . ARG A 1 3775 ? 201.508 209.682 290.679 1.00 27.54 ? 3775 ARG A CG    1 
ATOM   16884 C  CD    . ARG A 1 3775 ? 201.760 211.001 291.386 1.00 28.60 ? 3775 ARG A CD    1 
ATOM   16885 N  NE    . ARG A 1 3775 ? 202.835 210.890 292.363 1.00 31.52 ? 3775 ARG A NE    1 
ATOM   16886 C  CZ    . ARG A 1 3775 ? 204.009 211.500 292.261 1.00 33.02 ? 3775 ARG A CZ    1 
ATOM   16887 N  NH1   . ARG A 1 3775 ? 204.296 212.277 291.229 1.00 28.11 ? 3775 ARG A NH1   1 
ATOM   16888 N  NH2   . ARG A 1 3775 ? 204.916 211.325 293.217 1.00 32.14 ? 3775 ARG A NH2   1 
ATOM   16889 N  N     . GLU A 1 3776 ? 202.312 208.644 287.121 1.00 22.36 ? 3776 GLU A N     1 
ATOM   16890 C  CA    . GLU A 1 3776 ? 201.532 208.848 285.907 1.00 21.47 ? 3776 GLU A CA    1 
ATOM   16891 C  C     . GLU A 1 3776 ? 201.248 207.529 285.204 1.00 24.78 ? 3776 GLU A C     1 
ATOM   16892 O  O     . GLU A 1 3776 ? 200.194 207.378 284.578 1.00 24.66 ? 3776 GLU A O     1 
ATOM   16893 C  CB    . GLU A 1 3776 ? 202.253 209.818 284.971 1.00 16.26 ? 3776 GLU A CB    1 
ATOM   16894 C  CG    . GLU A 1 3776 ? 201.337 210.506 283.972 1.00 19.79 ? 3776 GLU A CG    1 
ATOM   16895 C  CD    . GLU A 1 3776 ? 202.096 211.323 282.944 1.00 31.46 ? 3776 GLU A CD    1 
ATOM   16896 O  OE1   . GLU A 1 3776 ? 203.206 210.911 282.549 1.00 26.44 ? 3776 GLU A OE1   1 
ATOM   16897 O  OE2   . GLU A 1 3776 ? 201.581 212.384 282.532 1.00 34.08 ? 3776 GLU A OE2   1 
ATOM   16898 N  N     . ALA A 1 3777 ? 202.167 206.564 285.299 1.00 20.72 ? 3777 ALA A N     1 
ATOM   16899 C  CA    . ALA A 1 3777 ? 201.929 205.254 284.703 1.00 18.97 ? 3777 ALA A CA    1 
ATOM   16900 C  C     . ALA A 1 3777 ? 200.754 204.548 285.366 1.00 20.97 ? 3777 ALA A C     1 
ATOM   16901 O  O     . ALA A 1 3777 ? 199.950 203.897 284.691 1.00 24.41 ? 3777 ALA A O     1 
ATOM   16902 C  CB    . ALA A 1 3777 ? 203.191 204.395 284.792 1.00 23.36 ? 3777 ALA A CB    1 
ATOM   16903 N  N     . ALA A 1 3778 ? 200.641 204.659 286.691 1.00 21.75 ? 3778 ALA A N     1 
ATOM   16904 C  CA    . ALA A 1 3778 ? 199.541 204.005 287.393 1.00 19.73 ? 3778 ALA A CA    1 
ATOM   16905 C  C     . ALA A 1 3778 ? 198.206 204.671 287.080 1.00 23.24 ? 3778 ALA A C     1 
ATOM   16906 O  O     . ALA A 1 3778 ? 197.193 203.986 286.895 1.00 22.09 ? 3778 ALA A O     1 
ATOM   16907 C  CB    . ALA A 1 3778 ? 199.803 204.003 288.898 1.00 19.23 ? 3778 ALA A CB    1 
ATOM   16908 N  N     . GLU A 1 3779 ? 198.181 206.005 287.018 1.00 22.82 ? 3779 GLU A N     1 
ATOM   16909 C  CA    . GLU A 1 3779 ? 196.928 206.708 286.756 1.00 19.84 ? 3779 GLU A CA    1 
ATOM   16910 C  C     . GLU A 1 3779 ? 196.429 206.455 285.339 1.00 23.24 ? 3779 GLU A C     1 
ATOM   16911 O  O     . GLU A 1 3779 ? 195.229 206.248 285.129 1.00 26.95 ? 3779 GLU A O     1 
ATOM   16912 C  CB    . GLU A 1 3779 ? 197.100 208.205 287.002 1.00 19.82 ? 3779 GLU A CB    1 
ATOM   16913 C  CG    . GLU A 1 3779 ? 197.365 208.557 288.451 1.00 23.85 ? 3779 GLU A CG    1 
ATOM   16914 C  CD    . GLU A 1 3779 ? 196.177 208.263 289.347 1.00 31.28 ? 3779 GLU A CD    1 
ATOM   16915 O  OE1   . GLU A 1 3779 ? 195.026 208.369 288.871 1.00 32.77 ? 3779 GLU A OE1   1 
ATOM   16916 O  OE2   . GLU A 1 3779 ? 196.395 207.926 290.529 1.00 30.97 ? 3779 GLU A OE2   1 
ATOM   16917 N  N     . VAL A 1 3780 ? 197.328 206.474 284.354 1.00 22.90 ? 3780 VAL A N     1 
ATOM   16918 C  CA    . VAL A 1 3780 ? 196.919 206.169 282.988 1.00 20.75 ? 3780 VAL A CA    1 
ATOM   16919 C  C     . VAL A 1 3780 ? 196.442 204.726 282.893 1.00 19.95 ? 3780 VAL A C     1 
ATOM   16920 O  O     . VAL A 1 3780 ? 195.435 204.433 282.239 1.00 24.05 ? 3780 VAL A O     1 
ATOM   16921 C  CB    . VAL A 1 3780 ? 198.064 206.466 282.003 1.00 19.17 ? 3780 VAL A CB    1 
ATOM   16922 C  CG1   . VAL A 1 3780 ? 197.671 206.058 280.596 1.00 16.79 ? 3780 VAL A CG1   1 
ATOM   16923 C  CG2   . VAL A 1 3780 ? 198.415 207.939 282.036 1.00 18.55 ? 3780 VAL A CG2   1 
ATOM   16924 N  N     . THR A 1 3781 ? 197.146 203.806 283.554 1.00 20.85 ? 3781 THR A N     1 
ATOM   16925 C  CA    . THR A 1 3781 ? 196.681 202.425 283.624 1.00 19.32 ? 3781 THR A CA    1 
ATOM   16926 C  C     . THR A 1 3781 ? 195.322 202.333 284.302 1.00 20.88 ? 3781 THR A C     1 
ATOM   16927 O  O     . THR A 1 3781 ? 194.509 201.471 283.950 1.00 22.33 ? 3781 THR A O     1 
ATOM   16928 C  CB    . THR A 1 3781 ? 197.712 201.567 284.358 1.00 21.51 ? 3781 THR A CB    1 
ATOM   16929 O  OG1   . THR A 1 3781 ? 199.006 201.786 283.784 1.00 22.05 ? 3781 THR A OG1   1 
ATOM   16930 C  CG2   . THR A 1 3781 ? 197.363 200.094 284.249 1.00 19.86 ? 3781 THR A CG2   1 
ATOM   16931 N  N     . ARG A 1 3782 ? 195.055 203.211 285.272 1.00 28.73 ? 3782 ARG A N     1 
ATOM   16932 C  CA    . ARG A 1 3782 ? 193.718 203.294 285.853 1.00 22.09 ? 3782 ARG A CA    1 
ATOM   16933 C  C     . ARG A 1 3782 ? 192.711 203.839 284.846 1.00 21.27 ? 3782 ARG A C     1 
ATOM   16934 O  O     . ARG A 1 3782 ? 191.553 203.409 284.825 1.00 26.26 ? 3782 ARG A O     1 
ATOM   16935 C  CB    . ARG A 1 3782 ? 193.752 204.156 287.114 1.00 20.54 ? 3782 ARG A CB    1 
ATOM   16936 C  CG    . ARG A 1 3782 ? 192.438 204.223 287.873 1.00 26.83 ? 3782 ARG A CG    1 
ATOM   16937 C  CD    . ARG A 1 3782 ? 192.183 205.626 288.397 1.00 23.39 ? 3782 ARG A CD    1 
ATOM   16938 N  NE    . ARG A 1 3782 ? 192.052 206.599 287.318 1.00 28.16 ? 3782 ARG A NE    1 
ATOM   16939 C  CZ    . ARG A 1 3782 ? 191.796 207.887 287.499 1.00 32.36 ? 3782 ARG A CZ    1 
ATOM   16940 N  NH1   . ARG A 1 3782 ? 191.638 208.397 288.710 1.00 28.66 ? 3782 ARG A NH1   1 
ATOM   16941 N  NH2   . ARG A 1 3782 ? 191.697 208.686 286.440 1.00 32.74 ? 3782 ARG A NH2   1 
ATOM   16942 N  N     . LYS A 1 3783 ? 193.133 204.788 284.006 1.00 22.61 ? 3783 LYS A N     1 
ATOM   16943 C  CA    . LYS A 1 3783 ? 192.232 205.340 282.997 1.00 20.21 ? 3783 LYS A CA    1 
ATOM   16944 C  C     . LYS A 1 3783 ? 191.985 204.359 281.858 1.00 23.62 ? 3783 LYS A C     1 
ATOM   16945 O  O     . LYS A 1 3783 ? 190.936 204.422 281.208 1.00 29.90 ? 3783 LYS A O     1 
ATOM   16946 C  CB    . LYS A 1 3783 ? 192.790 206.652 282.447 1.00 18.10 ? 3783 LYS A CB    1 
ATOM   16947 C  CG    . LYS A 1 3783 ? 192.908 207.765 283.469 1.00 21.82 ? 3783 LYS A CG    1 
ATOM   16948 C  CD    . LYS A 1 3783 ? 193.888 208.832 283.008 1.00 20.57 ? 3783 LYS A CD    1 
ATOM   16949 C  CE    . LYS A 1 3783 ? 194.580 209.489 284.190 1.00 25.96 ? 3783 LYS A CE    1 
ATOM   16950 N  NZ    . LYS A 1 3783 ? 195.735 210.330 283.768 1.00 25.44 ? 3783 LYS A NZ    1 
ATOM   16951 N  N     . VAL A 1 3784 ? 192.938 203.468 281.581 1.00 20.73 ? 3784 VAL A N     1 
ATOM   16952 C  CA    . VAL A 1 3784 ? 192.728 202.464 280.541 1.00 25.08 ? 3784 VAL A CA    1 
ATOM   16953 C  C     . VAL A 1 3784 ? 191.687 201.445 280.984 1.00 23.65 ? 3784 VAL A C     1 
ATOM   16954 O  O     . VAL A 1 3784 ? 190.850 201.006 280.187 1.00 25.36 ? 3784 VAL A O     1 
ATOM   16955 C  CB    . VAL A 1 3784 ? 194.059 201.791 280.164 1.00 22.66 ? 3784 VAL A CB    1 
ATOM   16956 C  CG1   . VAL A 1 3784 ? 193.819 200.665 279.170 1.00 24.33 ? 3784 VAL A CG1   1 
ATOM   16957 C  CG2   . VAL A 1 3784 ? 195.011 202.808 279.572 1.00 19.87 ? 3784 VAL A CG2   1 
ATOM   16958 N  N     . GLU A 1 3785 ? 191.722 201.051 282.259 1.00 23.21 ? 3785 GLU A N     1 
ATOM   16959 C  CA    . GLU A 1 3785 ? 190.753 200.080 282.761 1.00 25.60 ? 3785 GLU A CA    1 
ATOM   16960 C  C     . GLU A 1 3785 ? 189.332 200.623 282.680 1.00 27.49 ? 3785 GLU A C     1 
ATOM   16961 O  O     . GLU A 1 3785 ? 188.400 199.892 282.322 1.00 26.10 ? 3785 GLU A O     1 
ATOM   16962 C  CB    . GLU A 1 3785 ? 191.098 199.688 284.198 1.00 25.59 ? 3785 GLU A CB    1 
ATOM   16963 C  CG    . GLU A 1 3785 ? 192.426 198.959 284.357 1.00 27.97 ? 3785 GLU A CG    1 
ATOM   16964 C  CD    . GLU A 1 3785 ? 192.388 197.532 283.835 1.00 34.63 ? 3785 GLU A CD    1 
ATOM   16965 O  OE1   . GLU A 1 3785 ? 191.300 197.061 283.441 1.00 34.08 ? 3785 GLU A OE1   1 
ATOM   16966 O  OE2   . GLU A 1 3785 ? 193.452 196.879 283.823 1.00 36.15 ? 3785 GLU A OE2   1 
ATOM   16967 N  N     . GLU A 1 3786 ? 189.143 201.903 283.013 1.00 23.93 ? 3786 GLU A N     1 
ATOM   16968 C  CA    . GLU A 1 3786 ? 187.804 202.477 282.975 1.00 24.60 ? 3786 GLU A CA    1 
ATOM   16969 C  C     . GLU A 1 3786 ? 187.315 202.675 281.545 1.00 26.88 ? 3786 GLU A C     1 
ATOM   16970 O  O     . GLU A 1 3786 ? 186.104 202.672 281.303 1.00 30.33 ? 3786 GLU A O     1 
ATOM   16971 C  CB    . GLU A 1 3786 ? 187.770 203.796 283.750 1.00 21.44 ? 3786 GLU A CB    1 
ATOM   16972 C  CG    . GLU A 1 3786 ? 188.534 204.936 283.101 1.00 30.70 ? 3786 GLU A CG    1 
ATOM   16973 C  CD    . GLU A 1 3786 ? 188.614 206.164 283.987 1.00 37.05 ? 3786 GLU A CD    1 
ATOM   16974 O  OE1   . GLU A 1 3786 ? 188.052 206.133 285.102 1.00 34.83 ? 3786 GLU A OE1   1 
ATOM   16975 O  OE2   . GLU A 1 3786 ? 189.242 207.161 283.569 1.00 34.98 ? 3786 GLU A OE2   1 
ATOM   16976 N  N     . THR A 1 3787 ? 188.229 202.854 280.588 1.00 24.35 ? 3787 THR A N     1 
ATOM   16977 C  CA    . THR A 1 3787 ? 187.817 202.909 279.190 1.00 22.60 ? 3787 THR A CA    1 
ATOM   16978 C  C     . THR A 1 3787 ? 187.532 201.526 278.623 1.00 26.98 ? 3787 THR A C     1 
ATOM   16979 O  O     . THR A 1 3787 ? 186.866 201.418 277.589 1.00 31.95 ? 3787 THR A O     1 
ATOM   16980 C  CB    . THR A 1 3787 ? 188.878 203.604 278.337 1.00 21.55 ? 3787 THR A CB    1 
ATOM   16981 O  OG1   . THR A 1 3787 ? 190.173 203.076 278.652 1.00 30.91 ? 3787 THR A OG1   1 
ATOM   16982 C  CG2   . THR A 1 3787 ? 188.866 205.103 278.583 1.00 22.53 ? 3787 THR A CG2   1 
ATOM   16983 N  N     . ASP A 1 3788 ? 188.027 200.468 279.269 1.00 22.22 ? 3788 ASP A N     1 
ATOM   16984 C  CA    . ASP A 1 3788 ? 187.736 199.118 278.800 1.00 24.09 ? 3788 ASP A CA    1 
ATOM   16985 C  C     . ASP A 1 3788 ? 186.282 198.744 279.054 1.00 23.00 ? 3788 ASP A C     1 
ATOM   16986 O  O     . ASP A 1 3788 ? 185.636 198.126 278.199 1.00 29.36 ? 3788 ASP A O     1 
ATOM   16987 C  CB    . ASP A 1 3788 ? 188.674 198.113 279.468 1.00 24.87 ? 3788 ASP A CB    1 
ATOM   16988 C  CG    . ASP A 1 3788 ? 190.071 198.146 278.886 1.00 32.05 ? 3788 ASP A CG    1 
ATOM   16989 O  OD1   . ASP A 1 3788 ? 190.303 198.923 277.936 1.00 27.44 ? 3788 ASP A OD1   1 
ATOM   16990 O  OD2   . ASP A 1 3788 ? 190.937 197.390 279.373 1.00 37.90 ? 3788 ASP A OD2   1 
ATOM   16991 N  N     . ILE A 1 3789 ? 185.748 199.105 280.224 1.00 26.13 ? 3789 ILE A N     1 
ATOM   16992 C  CA    . ILE A 1 3789 ? 184.377 198.726 280.553 1.00 24.08 ? 3789 ILE A CA    1 
ATOM   16993 C  C     . ILE A 1 3789 ? 183.378 199.493 279.695 1.00 25.75 ? 3789 ILE A C     1 
ATOM   16994 O  O     . ILE A 1 3789 ? 182.331 198.951 279.321 1.00 29.69 ? 3789 ILE A O     1 
ATOM   16995 C  CB    . ILE A 1 3789 ? 184.105 198.921 282.058 1.00 23.51 ? 3789 ILE A CB    1 
ATOM   16996 C  CG1   . ILE A 1 3789 ? 184.252 200.386 282.463 1.00 27.06 ? 3789 ILE A CG1   1 
ATOM   16997 C  CG2   . ILE A 1 3789 ? 185.046 198.056 282.881 1.00 23.20 ? 3789 ILE A CG2   1 
ATOM   16998 C  CD1   . ILE A 1 3789 ? 183.777 200.681 283.866 1.00 28.73 ? 3789 ILE A CD1   1 
ATOM   16999 N  N     . VAL A 1 3790 ? 183.672 200.754 279.369 1.00 24.51 ? 3790 VAL A N     1 
ATOM   17000 C  CA    . VAL A 1 3790 ? 182.731 201.548 278.586 1.00 22.50 ? 3790 VAL A CA    1 
ATOM   17001 C  C     . VAL A 1 3790 ? 182.676 201.052 277.143 1.00 22.73 ? 3790 VAL A C     1 
ATOM   17002 O  O     . VAL A 1 3790 ? 181.621 201.112 276.499 1.00 21.50 ? 3790 VAL A O     1 
ATOM   17003 C  CB    . VAL A 1 3790 ? 183.097 203.042 278.676 1.00 23.90 ? 3790 VAL A CB    1 
ATOM   17004 C  CG1   . VAL A 1 3790 ? 182.108 203.892 277.891 1.00 18.96 ? 3790 VAL A CG1   1 
ATOM   17005 C  CG2   . VAL A 1 3790 ? 183.151 203.485 280.128 1.00 18.89 ? 3790 VAL A CG2   1 
ATOM   17006 N  N     . MET A 1 3791 ? 183.798 200.554 276.608 1.00 23.14 ? 3791 MET A N     1 
ATOM   17007 C  CA    . MET A 1 3791 ? 183.765 199.871 275.316 1.00 21.17 ? 3791 MET A CA    1 
ATOM   17008 C  C     . MET A 1 3791 ? 182.849 198.655 275.346 1.00 24.68 ? 3791 MET A C     1 
ATOM   17009 O  O     . MET A 1 3791 ? 182.175 198.354 274.354 1.00 21.79 ? 3791 MET A O     1 
ATOM   17010 C  CB    . MET A 1 3791 ? 185.177 199.464 274.891 1.00 23.05 ? 3791 MET A CB    1 
ATOM   17011 C  CG    . MET A 1 3791 ? 185.340 199.158 273.397 1.00 24.74 ? 3791 MET A CG    1 
ATOM   17012 S  SD    . MET A 1 3791 ? 184.462 200.194 272.207 1.00 50.92 ? 3791 MET A SD    1 
ATOM   17013 C  CE    . MET A 1 3791 ? 185.144 201.805 272.552 1.00 15.97 ? 3791 MET A CE    1 
ATOM   17014 N  N     . GLN A 1 3792 ? 182.817 197.936 276.470 1.00 21.87 ? 3792 GLN A N     1 
ATOM   17015 C  CA    . GLN A 1 3792 ? 181.901 196.807 276.586 1.00 20.96 ? 3792 GLN A CA    1 
ATOM   17016 C  C     . GLN A 1 3792 ? 180.451 197.252 276.448 1.00 22.56 ? 3792 GLN A C     1 
ATOM   17017 O  O     . GLN A 1 3792 ? 179.620 196.503 275.924 1.00 26.59 ? 3792 GLN A O     1 
ATOM   17018 C  CB    . GLN A 1 3792 ? 182.124 196.081 277.912 1.00 23.16 ? 3792 GLN A CB    1 
ATOM   17019 C  CG    . GLN A 1 3792 ? 183.486 195.414 278.018 1.00 26.33 ? 3792 GLN A CG    1 
ATOM   17020 C  CD    . GLN A 1 3792 ? 183.892 195.131 279.451 1.00 34.19 ? 3792 GLN A CD    1 
ATOM   17021 O  OE1   . GLN A 1 3792 ? 184.949 195.569 279.905 1.00 35.96 ? 3792 GLN A OE1   1 
ATOM   17022 N  NE2   . GLN A 1 3792 ? 183.055 194.392 280.170 1.00 30.76 ? 3792 GLN A NE2   1 
ATOM   17023 N  N     . GLU A 1 3793 ? 180.130 198.463 276.908 1.00 21.55 ? 3793 GLU A N     1 
ATOM   17024 C  CA    . GLU A 1 3793 ? 178.814 199.030 276.639 1.00 22.43 ? 3793 GLU A CA    1 
ATOM   17025 C  C     . GLU A 1 3793 ? 178.629 199.308 275.151 1.00 24.04 ? 3793 GLU A C     1 
ATOM   17026 O  O     . GLU A 1 3793 ? 177.550 199.065 274.597 1.00 24.20 ? 3793 GLU A O     1 
ATOM   17027 C  CB    . GLU A 1 3793 ? 178.618 200.306 277.455 1.00 21.76 ? 3793 GLU A CB    1 
ATOM   17028 C  CG    . GLU A 1 3793 ? 177.256 200.964 277.282 1.00 29.15 ? 3793 GLU A CG    1 
ATOM   17029 C  CD    . GLU A 1 3793 ? 176.115 200.108 277.803 1.00 34.64 ? 3793 GLU A CD    1 
ATOM   17030 O  OE1   . GLU A 1 3793 ? 176.352 199.276 278.703 1.00 34.86 ? 3793 GLU A OE1   1 
ATOM   17031 O  OE2   . GLU A 1 3793 ? 174.979 200.271 277.310 1.00 35.03 ? 3793 GLU A OE2   1 
ATOM   17032 N  N     . VAL A 1 3794 ? 179.665 199.825 274.489 1.00 24.44 ? 3794 VAL A N     1 
ATOM   17033 C  CA    . VAL A 1 3794 ? 179.588 200.070 273.052 1.00 19.30 ? 3794 VAL A CA    1 
ATOM   17034 C  C     . VAL A 1 3794 ? 179.504 198.753 272.288 1.00 20.68 ? 3794 VAL A C     1 
ATOM   17035 O  O     . VAL A 1 3794 ? 178.724 198.618 271.338 1.00 24.22 ? 3794 VAL A O     1 
ATOM   17036 C  CB    . VAL A 1 3794 ? 180.786 200.920 272.591 1.00 16.41 ? 3794 VAL A CB    1 
ATOM   17037 C  CG1   . VAL A 1 3794 ? 180.954 200.844 271.083 1.00 14.23 ? 3794 VAL A CG1   1 
ATOM   17038 C  CG2   . VAL A 1 3794 ? 180.605 202.363 273.031 1.00 14.46 ? 3794 VAL A CG2   1 
ATOM   17039 N  N     . GLU A 1 3795 ? 180.303 197.763 272.692 1.00 25.47 ? 3795 GLU A N     1 
ATOM   17040 C  CA    . GLU A 1 3795 ? 180.344 196.495 271.970 1.00 22.53 ? 3795 GLU A CA    1 
ATOM   17041 C  C     . GLU A 1 3795 ? 179.006 195.769 272.042 1.00 20.03 ? 3795 GLU A C     1 
ATOM   17042 O  O     . GLU A 1 3795 ? 178.547 195.200 271.043 1.00 22.27 ? 3795 GLU A O     1 
ATOM   17043 C  CB    . GLU A 1 3795 ? 181.461 195.616 272.529 1.00 17.44 ? 3795 GLU A CB    1 
ATOM   17044 C  CG    . GLU A 1 3795 ? 181.638 194.281 271.825 1.00 22.61 ? 3795 GLU A CG    1 
ATOM   17045 C  CD    . GLU A 1 3795 ? 182.097 194.426 270.385 1.00 35.47 ? 3795 GLU A CD    1 
ATOM   17046 O  OE1   . GLU A 1 3795 ? 182.739 195.448 270.061 1.00 34.94 ? 3795 GLU A OE1   1 
ATOM   17047 O  OE2   . GLU A 1 3795 ? 181.820 193.515 269.578 1.00 41.72 ? 3795 GLU A OE2   1 
ATOM   17048 N  N     . THR A 1 3796 ? 178.363 195.775 273.212 1.00 18.41 ? 3796 THR A N     1 
ATOM   17049 C  CA    . THR A 1 3796 ? 177.107 195.046 273.360 1.00 21.14 ? 3796 THR A CA    1 
ATOM   17050 C  C     . THR A 1 3796 ? 175.970 195.719 272.597 1.00 20.22 ? 3796 THR A C     1 
ATOM   17051 O  O     . THR A 1 3796 ? 175.040 195.038 272.151 1.00 18.38 ? 3796 THR A O     1 
ATOM   17052 C  CB    . THR A 1 3796 ? 176.749 194.890 274.843 1.00 19.42 ? 3796 THR A CB    1 
ATOM   17053 O  OG1   . THR A 1 3796 ? 175.613 194.030 274.977 1.00 31.99 ? 3796 THR A OG1   1 
ATOM   17054 C  CG2   . THR A 1 3796 ? 176.429 196.233 275.473 1.00 18.79 ? 3796 THR A CG2   1 
ATOM   17055 N  N     . VAL A 1 3797 ? 176.023 197.044 272.437 1.00 19.04 ? 3797 VAL A N     1 
ATOM   17056 C  CA    . VAL A 1 3797 ? 175.057 197.725 271.583 1.00 15.85 ? 3797 VAL A CA    1 
ATOM   17057 C  C     . VAL A 1 3797 ? 175.318 197.394 270.118 1.00 17.03 ? 3797 VAL A C     1 
ATOM   17058 O  O     . VAL A 1 3797 ? 174.384 197.144 269.348 1.00 24.07 ? 3797 VAL A O     1 
ATOM   17059 C  CB    . VAL A 1 3797 ? 175.092 199.244 271.835 1.00 20.56 ? 3797 VAL A CB    1 
ATOM   17060 C  CG1   . VAL A 1 3797 ? 174.199 199.973 270.843 1.00 11.19 ? 3797 VAL A CG1   1 
ATOM   17061 C  CG2   . VAL A 1 3797 ? 174.665 199.554 273.258 1.00 21.50 ? 3797 VAL A CG2   1 
ATOM   17062 N  N     . SER A 1 3798 ? 176.590 197.380 269.715 1.00 15.60 ? 3798 SER A N     1 
ATOM   17063 C  CA    . SER A 1 3798 ? 176.962 197.109 268.332 1.00 17.60 ? 3798 SER A CA    1 
ATOM   17064 C  C     . SER A 1 3798 ? 176.678 195.677 267.907 1.00 14.49 ? 3798 SER A C     1 
ATOM   17065 O  O     . SER A 1 3798 ? 176.640 195.406 266.703 1.00 21.02 ? 3798 SER A O     1 
ATOM   17066 C  CB    . SER A 1 3798 ? 178.445 197.418 268.121 1.00 19.14 ? 3798 SER A CB    1 
ATOM   17067 O  OG    . SER A 1 3798 ? 178.752 198.744 268.506 1.00 18.05 ? 3798 SER A OG    1 
ATOM   17068 N  N     . GLN A 1 3799 ? 176.482 194.759 268.858 1.00 14.53 ? 3799 GLN A N     1 
ATOM   17069 C  CA    . GLN A 1 3799 ? 176.210 193.369 268.505 1.00 12.39 ? 3799 GLN A CA    1 
ATOM   17070 C  C     . GLN A 1 3799 ? 174.877 193.218 267.782 1.00 17.14 ? 3799 GLN A C     1 
ATOM   17071 O  O     . GLN A 1 3799 ? 174.710 192.288 266.985 1.00 21.77 ? 3799 GLN A O     1 
ATOM   17072 C  CB    . GLN A 1 3799 ? 176.228 192.498 269.762 1.00 13.67 ? 3799 GLN A CB    1 
ATOM   17073 C  CG    . GLN A 1 3799 ? 177.614 192.072 270.202 1.00 17.16 ? 3799 GLN A CG    1 
ATOM   17074 C  CD    . GLN A 1 3799 ? 178.276 191.132 269.214 1.00 29.20 ? 3799 GLN A CD    1 
ATOM   17075 O  OE1   . GLN A 1 3799 ? 179.325 191.444 268.651 1.00 33.17 ? 3799 GLN A OE1   1 
ATOM   17076 N  NE2   . GLN A 1 3799 ? 177.664 189.972 268.999 1.00 26.01 ? 3799 GLN A NE2   1 
ATOM   17077 N  N     . GLN A 1 3800 ? 173.919 194.107 268.051 1.00 15.03 ? 3800 GLN A N     1 
ATOM   17078 C  CA    . GLN A 1 3800 ? 172.623 194.022 267.387 1.00 10.35 ? 3800 GLN A CA    1 
ATOM   17079 C  C     . GLN A 1 3800 ? 172.730 194.319 265.898 1.00 12.03 ? 3800 GLN A C     1 
ATOM   17080 O  O     . GLN A 1 3800 ? 171.989 193.740 265.097 1.00 13.64 ? 3800 GLN A O     1 
ATOM   17081 C  CB    . GLN A 1 3800 ? 171.632 194.979 268.049 1.00 13.62 ? 3800 GLN A CB    1 
ATOM   17082 C  CG    . GLN A 1 3800 ? 170.179 194.684 267.731 1.00 14.89 ? 3800 GLN A CG    1 
ATOM   17083 C  CD    . GLN A 1 3800 ? 169.252 195.795 268.168 1.00 18.24 ? 3800 GLN A CD    1 
ATOM   17084 O  OE1   . GLN A 1 3800 ? 169.698 196.869 268.570 1.00 25.34 ? 3800 GLN A OE1   1 
ATOM   17085 N  NE2   . GLN A 1 3800 ? 167.951 195.546 268.094 1.00 20.26 ? 3800 GLN A NE2   1 
ATOM   17086 N  N     . TYR A 1 3801 ? 173.641 195.206 265.510 1.00 11.76 ? 3801 TYR A N     1 
ATOM   17087 C  CA    . TYR A 1 3801 ? 173.801 195.608 264.120 1.00 5.46  ? 3801 TYR A CA    1 
ATOM   17088 C  C     . TYR A 1 3801 ? 174.835 194.778 263.375 1.00 7.45  ? 3801 TYR A C     1 
ATOM   17089 O  O     . TYR A 1 3801 ? 175.101 195.055 262.201 1.00 12.44 ? 3801 TYR A O     1 
ATOM   17090 C  CB    . TYR A 1 3801 ? 174.182 197.089 264.049 1.00 5.21  ? 3801 TYR A CB    1 
ATOM   17091 C  CG    . TYR A 1 3801 ? 173.170 198.002 264.693 1.00 8.35  ? 3801 TYR A CG    1 
ATOM   17092 C  CD1   . TYR A 1 3801 ? 172.094 198.494 263.972 1.00 8.18  ? 3801 TYR A CD1   1 
ATOM   17093 C  CD2   . TYR A 1 3801 ? 173.285 198.366 266.028 1.00 11.72 ? 3801 TYR A CD2   1 
ATOM   17094 C  CE1   . TYR A 1 3801 ? 171.163 199.324 264.557 1.00 6.45  ? 3801 TYR A CE1   1 
ATOM   17095 C  CE2   . TYR A 1 3801 ? 172.359 199.197 266.622 1.00 10.70 ? 3801 TYR A CE2   1 
ATOM   17096 C  CZ    . TYR A 1 3801 ? 171.299 199.673 265.881 1.00 8.74  ? 3801 TYR A CZ    1 
ATOM   17097 O  OH    . TYR A 1 3801 ? 170.373 200.503 266.467 1.00 19.06 ? 3801 TYR A OH    1 
ATOM   17098 N  N     . LEU A 1 3802 ? 175.427 193.778 264.026 1.00 8.67  ? 3802 LEU A N     1 
ATOM   17099 C  CA    . LEU A 1 3802 ? 176.416 192.935 263.355 1.00 7.77  ? 3802 LEU A CA    1 
ATOM   17100 C  C     . LEU A 1 3802 ? 175.841 192.164 262.172 1.00 4.39  ? 3802 LEU A C     1 
ATOM   17101 O  O     . LEU A 1 3802 ? 176.501 192.119 261.120 1.00 4.26  ? 3802 LEU A O     1 
ATOM   17102 C  CB    . LEU A 1 3802 ? 177.070 192.004 264.380 1.00 10.93 ? 3802 LEU A CB    1 
ATOM   17103 C  CG    . LEU A 1 3802 ? 178.183 191.089 263.869 1.00 13.47 ? 3802 LEU A CG    1 
ATOM   17104 C  CD1   . LEU A 1 3802 ? 179.348 191.914 263.356 1.00 8.44  ? 3802 LEU A CD1   1 
ATOM   17105 C  CD2   . LEU A 1 3802 ? 178.642 190.146 264.968 1.00 17.30 ? 3802 LEU A CD2   1 
ATOM   17106 N  N     . PRO A 1 3803 ? 174.662 191.530 262.258 1.00 9.24  ? 3803 PRO A N     1 
ATOM   17107 C  CA    . PRO A 1 3803 ? 174.137 190.826 261.073 1.00 3.73  ? 3803 PRO A CA    1 
ATOM   17108 C  C     . PRO A 1 3803 ? 173.902 191.725 259.871 1.00 3.88  ? 3803 PRO A C     1 
ATOM   17109 O  O     . PRO A 1 3803 ? 174.057 191.266 258.733 1.00 2.83  ? 3803 PRO A O     1 
ATOM   17110 C  CB    . PRO A 1 3803 ? 172.827 190.215 261.588 1.00 2.19  ? 3803 PRO A CB    1 
ATOM   17111 C  CG    . PRO A 1 3803 ? 173.046 190.064 263.042 1.00 4.11  ? 3803 PRO A CG    1 
ATOM   17112 C  CD    . PRO A 1 3803 ? 173.802 191.291 263.432 1.00 7.48  ? 3803 PRO A CD    1 
ATOM   17113 N  N     . LEU A 1 3804 ? 173.518 192.986 260.083 1.00 3.53  ? 3804 LEU A N     1 
ATOM   17114 C  CA    . LEU A 1 3804 ? 173.344 193.900 258.959 1.00 2.74  ? 3804 LEU A CA    1 
ATOM   17115 C  C     . LEU A 1 3804 ? 174.667 194.169 258.251 1.00 3.48  ? 3804 LEU A C     1 
ATOM   17116 O  O     . LEU A 1 3804 ? 174.720 194.214 257.018 1.00 2.83  ? 3804 LEU A O     1 
ATOM   17117 C  CB    . LEU A 1 3804 ? 172.715 195.207 259.438 1.00 2.89  ? 3804 LEU A CB    1 
ATOM   17118 C  CG    . LEU A 1 3804 ? 172.526 196.287 258.372 1.00 2.75  ? 3804 LEU A CG    1 
ATOM   17119 C  CD1   . LEU A 1 3804 ? 171.455 195.881 257.374 1.00 3.19  ? 3804 LEU A CD1   1 
ATOM   17120 C  CD2   . LEU A 1 3804 ? 172.197 197.625 259.009 1.00 1.77  ? 3804 LEU A CD2   1 
ATOM   17121 N  N     . SER A 1 3805 ? 175.745 194.354 259.018 1.00 3.73  ? 3805 SER A N     1 
ATOM   17122 C  CA    . SER A 1 3805 ? 177.053 194.594 258.415 1.00 2.06  ? 3805 SER A CA    1 
ATOM   17123 C  C     . SER A 1 3805 ? 177.536 193.377 257.636 1.00 2.42  ? 3805 SER A C     1 
ATOM   17124 O  O     . SER A 1 3805 ? 178.160 193.517 256.578 1.00 1.55  ? 3805 SER A O     1 
ATOM   17125 C  CB    . SER A 1 3805 ? 178.063 194.986 259.494 1.00 3.16  ? 3805 SER A CB    1 
ATOM   17126 O  OG    . SER A 1 3805 ? 178.274 193.928 260.410 1.00 7.78  ? 3805 SER A OG    1 
ATOM   17127 N  N     . THR A 1 3806 ? 177.268 192.174 258.150 1.00 2.71  ? 3806 THR A N     1 
ATOM   17128 C  CA    . THR A 1 3806 ? 177.583 190.964 257.397 1.00 2.10  ? 3806 THR A CA    1 
ATOM   17129 C  C     . THR A 1 3806 ? 176.784 190.903 256.103 1.00 2.52  ? 3806 THR A C     1 
ATOM   17130 O  O     . THR A 1 3806 ? 177.313 190.517 255.054 1.00 3.88  ? 3806 THR A O     1 
ATOM   17131 C  CB    . THR A 1 3806 ? 177.313 189.726 258.253 1.00 1.96  ? 3806 THR A CB    1 
ATOM   17132 O  OG1   . THR A 1 3806 ? 178.009 189.843 259.499 1.00 6.68  ? 3806 THR A OG1   1 
ATOM   17133 C  CG2   . THR A 1 3806 ? 177.776 188.470 257.536 1.00 1.55  ? 3806 THR A CG2   1 
ATOM   17134 N  N     . ALA A 1 3807 ? 175.504 191.279 256.158 1.00 2.05  ? 3807 ALA A N     1 
ATOM   17135 C  CA    . ALA A 1 3807 ? 174.698 191.331 254.944 1.00 1.58  ? 3807 ALA A CA    1 
ATOM   17136 C  C     . ALA A 1 3807 ? 175.251 192.355 253.963 1.00 1.14  ? 3807 ALA A C     1 
ATOM   17137 O  O     . ALA A 1 3807 ? 175.268 192.118 252.750 1.00 1.05  ? 3807 ALA A O     1 
ATOM   17138 C  CB    . ALA A 1 3807 ? 173.244 191.650 255.292 1.00 1.30  ? 3807 ALA A CB    1 
ATOM   17139 N  N     . CYS A 1 3808 ? 175.717 193.498 254.470 1.00 1.09  ? 3808 CYS A N     1 
ATOM   17140 C  CA    . CYS A 1 3808 ? 176.273 194.528 253.600 1.00 1.13  ? 3808 CYS A CA    1 
ATOM   17141 C  C     . CYS A 1 3808 ? 177.493 194.020 252.841 1.00 1.18  ? 3808 CYS A C     1 
ATOM   17142 O  O     . CYS A 1 3808 ? 177.625 194.255 251.634 1.00 1.08  ? 3808 CYS A O     1 
ATOM   17143 C  CB    . CYS A 1 3808 ? 176.637 195.763 254.419 1.00 1.05  ? 3808 CYS A CB    1 
ATOM   17144 S  SG    . CYS A 1 3808 ? 175.254 196.830 254.838 1.00 7.26  ? 3808 CYS A SG    1 
ATOM   17145 N  N     . SER A 1 3809 ? 178.399 193.322 253.530 1.00 1.60  ? 3809 SER A N     1 
ATOM   17146 C  CA    . SER A 1 3809 ? 179.600 192.827 252.867 1.00 1.71  ? 3809 SER A CA    1 
ATOM   17147 C  C     . SER A 1 3809 ? 179.268 191.729 251.865 1.00 1.09  ? 3809 SER A C     1 
ATOM   17148 O  O     . SER A 1 3809 ? 179.853 191.677 250.778 1.00 0.97  ? 3809 SER A O     1 
ATOM   17149 C  CB    . SER A 1 3809 ? 180.614 192.336 253.902 1.00 2.58  ? 3809 SER A CB    1 
ATOM   17150 O  OG    . SER A 1 3809 ? 180.133 191.207 254.607 1.00 7.34  ? 3809 SER A OG    1 
ATOM   17151 N  N     . SER A 1 3810 ? 178.331 190.841 252.209 1.00 1.40  ? 3810 SER A N     1 
ATOM   17152 C  CA    . SER A 1 3810 ? 177.934 189.795 251.273 1.00 1.15  ? 3810 SER A CA    1 
ATOM   17153 C  C     . SER A 1 3810 ? 177.278 190.386 250.031 1.00 1.02  ? 3810 SER A C     1 
ATOM   17154 O  O     . SER A 1 3810 ? 177.506 189.908 248.915 1.00 1.31  ? 3810 SER A O     1 
ATOM   17155 C  CB    . SER A 1 3810 ? 176.993 188.799 251.953 1.00 1.48  ? 3810 SER A CB    1 
ATOM   17156 O  OG    . SER A 1 3810 ? 177.495 188.388 253.210 1.00 5.44  ? 3810 SER A OG    1 
ATOM   17157 N  N     . ILE A 1 3811 ? 176.456 191.423 250.208 1.00 0.73  ? 3811 ILE A N     1 
ATOM   17158 C  CA    . ILE A 1 3811 ? 175.779 192.040 249.070 1.00 0.75  ? 3811 ILE A CA    1 
ATOM   17159 C  C     . ILE A 1 3811 ? 176.790 192.685 248.132 1.00 0.78  ? 3811 ILE A C     1 
ATOM   17160 O  O     . ILE A 1 3811 ? 176.728 192.509 246.909 1.00 2.46  ? 3811 ILE A O     1 
ATOM   17161 C  CB    . ILE A 1 3811 ? 174.729 193.058 249.554 1.00 0.73  ? 3811 ILE A CB    1 
ATOM   17162 C  CG1   . ILE A 1 3811 ? 173.523 192.336 250.157 1.00 0.52  ? 3811 ILE A CG1   1 
ATOM   17163 C  CG2   . ILE A 1 3811 ? 174.289 193.965 248.412 1.00 0.49  ? 3811 ILE A CG2   1 
ATOM   17164 C  CD1   . ILE A 1 3811 ? 172.508 193.261 250.773 1.00 0.59  ? 3811 ILE A CD1   1 
ATOM   17165 N  N     . TYR A 1 3812 ? 177.743 193.439 248.689 1.00 0.88  ? 3812 TYR A N     1 
ATOM   17166 C  CA    . TYR A 1 3812 ? 178.724 194.112 247.843 1.00 0.61  ? 3812 TYR A CA    1 
ATOM   17167 C  C     . TYR A 1 3812 ? 179.603 193.111 247.110 1.00 0.52  ? 3812 TYR A C     1 
ATOM   17168 O  O     . TYR A 1 3812 ? 179.871 193.271 245.913 1.00 0.79  ? 3812 TYR A O     1 
ATOM   17169 C  CB    . TYR A 1 3812 ? 179.589 195.063 248.668 1.00 0.88  ? 3812 TYR A CB    1 
ATOM   17170 C  CG    . TYR A 1 3812 ? 180.771 195.588 247.885 1.00 1.08  ? 3812 TYR A CG    1 
ATOM   17171 C  CD1   . TYR A 1 3812 ? 180.599 196.568 246.918 1.00 0.68  ? 3812 TYR A CD1   1 
ATOM   17172 C  CD2   . TYR A 1 3812 ? 182.052 195.087 248.089 1.00 0.57  ? 3812 TYR A CD2   1 
ATOM   17173 C  CE1   . TYR A 1 3812 ? 181.664 197.042 246.188 1.00 1.04  ? 3812 TYR A CE1   1 
ATOM   17174 C  CE2   . TYR A 1 3812 ? 183.125 195.559 247.363 1.00 0.55  ? 3812 TYR A CE2   1 
ATOM   17175 C  CZ    . TYR A 1 3812 ? 182.926 196.539 246.415 1.00 1.26  ? 3812 TYR A CZ    1 
ATOM   17176 O  OH    . TYR A 1 3812 ? 183.986 197.022 245.683 1.00 2.03  ? 3812 TYR A OH    1 
ATOM   17177 N  N     . PHE A 1 3813 ? 180.068 192.076 247.809 1.00 0.93  ? 3813 PHE A N     1 
ATOM   17178 C  CA    . PHE A 1 3813 ? 180.915 191.080 247.167 1.00 0.88  ? 3813 PHE A CA    1 
ATOM   17179 C  C     . PHE A 1 3813 ? 180.143 190.236 246.163 1.00 1.14  ? 3813 PHE A C     1 
ATOM   17180 O  O     . PHE A 1 3813 ? 180.753 189.680 245.245 1.00 1.31  ? 3813 PHE A O     1 
ATOM   17181 C  CB    . PHE A 1 3813 ? 181.586 190.208 248.228 1.00 1.36  ? 3813 PHE A CB    1 
ATOM   17182 C  CG    . PHE A 1 3813 ? 182.864 190.795 248.758 1.00 1.98  ? 3813 PHE A CG    1 
ATOM   17183 C  CD1   . PHE A 1 3813 ? 182.847 191.673 249.827 1.00 2.70  ? 3813 PHE A CD1   1 
ATOM   17184 C  CD2   . PHE A 1 3813 ? 184.078 190.491 248.169 1.00 3.78  ? 3813 PHE A CD2   1 
ATOM   17185 C  CE1   . PHE A 1 3813 ? 184.017 192.230 250.307 1.00 1.67  ? 3813 PHE A CE1   1 
ATOM   17186 C  CE2   . PHE A 1 3813 ? 185.254 191.042 248.646 1.00 4.50  ? 3813 PHE A CE2   1 
ATOM   17187 C  CZ    . PHE A 1 3813 ? 185.222 191.913 249.717 1.00 2.53  ? 3813 PHE A CZ    1 
ATOM   17188 N  N     . THR A 1 3814 ? 178.822 190.127 246.318 1.00 1.38  ? 3814 THR A N     1 
ATOM   17189 C  CA    . THR A 1 3814 ? 178.000 189.570 245.250 1.00 1.03  ? 3814 THR A CA    1 
ATOM   17190 C  C     . THR A 1 3814 ? 177.948 190.516 244.055 1.00 0.89  ? 3814 THR A C     1 
ATOM   17191 O  O     . THR A 1 3814 ? 178.072 190.079 242.905 1.00 0.94  ? 3814 THR A O     1 
ATOM   17192 C  CB    . THR A 1 3814 ? 176.592 189.276 245.771 1.00 1.25  ? 3814 THR A CB    1 
ATOM   17193 O  OG1   . THR A 1 3814 ? 176.656 188.242 246.762 1.00 3.89  ? 3814 THR A OG1   1 
ATOM   17194 C  CG2   . THR A 1 3814 ? 175.683 188.825 244.641 1.00 1.25  ? 3814 THR A CG2   1 
ATOM   17195 N  N     . MET A 1 3815 ? 177.783 191.816 244.312 1.00 0.79  ? 3815 MET A N     1 
ATOM   17196 C  CA    . MET A 1 3815 ? 177.817 192.805 243.238 1.00 0.74  ? 3815 MET A CA    1 
ATOM   17197 C  C     . MET A 1 3815 ? 179.167 192.811 242.535 1.00 0.97  ? 3815 MET A C     1 
ATOM   17198 O  O     . MET A 1 3815 ? 179.236 192.912 241.306 1.00 2.09  ? 3815 MET A O     1 
ATOM   17199 C  CB    . MET A 1 3815 ? 177.512 194.194 243.798 1.00 0.62  ? 3815 MET A CB    1 
ATOM   17200 C  CG    . MET A 1 3815 ? 176.125 194.367 244.381 1.00 0.47  ? 3815 MET A CG    1 
ATOM   17201 S  SD    . MET A 1 3815 ? 175.939 195.965 245.197 1.00 12.79 ? 3815 MET A SD    1 
ATOM   17202 C  CE    . MET A 1 3815 ? 176.306 197.087 243.854 1.00 0.52  ? 3815 MET A CE    1 
ATOM   17203 N  N     . GLU A 1 3816 ? 180.252 192.708 243.305 1.00 1.75  ? 3816 GLU A N     1 
ATOM   17204 C  CA    . GLU A 1 3816 ? 181.589 192.728 242.726 1.00 1.81  ? 3816 GLU A CA    1 
ATOM   17205 C  C     . GLU A 1 3816 ? 181.820 191.538 241.804 1.00 1.76  ? 3816 GLU A C     1 
ATOM   17206 O  O     . GLU A 1 3816 ? 182.592 191.636 240.844 1.00 4.28  ? 3816 GLU A O     1 
ATOM   17207 C  CB    . GLU A 1 3816 ? 182.631 192.757 243.847 1.00 2.07  ? 3816 GLU A CB    1 
ATOM   17208 C  CG    . GLU A 1 3816 ? 184.077 192.826 243.383 1.00 6.35  ? 3816 GLU A CG    1 
ATOM   17209 C  CD    . GLU A 1 3816 ? 184.399 194.121 242.660 1.00 22.30 ? 3816 GLU A CD    1 
ATOM   17210 O  OE1   . GLU A 1 3816 ? 183.718 195.136 242.921 1.00 22.74 ? 3816 GLU A OE1   1 
ATOM   17211 O  OE2   . GLU A 1 3816 ? 185.339 194.124 241.837 1.00 18.20 ? 3816 GLU A OE2   1 
ATOM   17212 N  N     . SER A 1 3817 ? 181.159 190.414 242.069 1.00 1.77  ? 3817 SER A N     1 
ATOM   17213 C  CA    . SER A 1 3817 ? 181.309 189.215 241.258 1.00 2.05  ? 3817 SER A CA    1 
ATOM   17214 C  C     . SER A 1 3817 ? 180.400 189.201 240.036 1.00 2.18  ? 3817 SER A C     1 
ATOM   17215 O  O     . SER A 1 3817 ? 180.533 188.306 239.197 1.00 3.50  ? 3817 SER A O     1 
ATOM   17216 C  CB    . SER A 1 3817 ? 181.039 187.970 242.108 1.00 2.03  ? 3817 SER A CB    1 
ATOM   17217 O  OG    . SER A 1 3817 ? 179.856 188.125 242.872 1.00 12.12 ? 3817 SER A OG    1 
ATOM   17218 N  N     . LEU A 1 3818 ? 179.490 190.170 239.909 1.00 2.15  ? 3818 LEU A N     1 
ATOM   17219 C  CA    . LEU A 1 3818 ? 178.596 190.206 238.758 1.00 1.16  ? 3818 LEU A CA    1 
ATOM   17220 C  C     . LEU A 1 3818 ? 179.336 190.490 237.457 1.00 1.61  ? 3818 LEU A C     1 
ATOM   17221 O  O     . LEU A 1 3818 ? 178.791 190.226 236.381 1.00 1.99  ? 3818 LEU A O     1 
ATOM   17222 C  CB    . LEU A 1 3818 ? 177.497 191.245 238.976 1.00 1.11  ? 3818 LEU A CB    1 
ATOM   17223 C  CG    . LEU A 1 3818 ? 176.320 190.780 239.837 1.00 0.60  ? 3818 LEU A CG    1 
ATOM   17224 C  CD1   . LEU A 1 3818 ? 175.481 191.959 240.293 1.00 0.33  ? 3818 LEU A CD1   1 
ATOM   17225 C  CD2   . LEU A 1 3818 ? 175.469 189.768 239.088 1.00 0.71  ? 3818 LEU A CD2   1 
ATOM   17226 N  N     . LYS A 1 3819 ? 180.561 191.014 237.529 1.00 2.20  ? 3819 LYS A N     1 
ATOM   17227 C  CA    . LYS A 1 3819 ? 181.368 191.202 236.330 1.00 1.51  ? 3819 LYS A CA    1 
ATOM   17228 C  C     . LYS A 1 3819 ? 181.759 189.878 235.685 1.00 2.46  ? 3819 LYS A C     1 
ATOM   17229 O  O     . LYS A 1 3819 ? 182.149 189.868 234.513 1.00 3.03  ? 3819 LYS A O     1 
ATOM   17230 C  CB    . LYS A 1 3819 ? 182.628 192.003 236.663 1.00 1.35  ? 3819 LYS A CB    1 
ATOM   17231 C  CG    . LYS A 1 3819 ? 183.654 191.227 237.470 1.00 1.30  ? 3819 LYS A CG    1 
ATOM   17232 C  CD    . LYS A 1 3819 ? 185.011 191.903 237.461 1.00 1.31  ? 3819 LYS A CD    1 
ATOM   17233 C  CE    . LYS A 1 3819 ? 185.016 193.160 238.309 1.00 3.02  ? 3819 LYS A CE    1 
ATOM   17234 N  NZ    . LYS A 1 3819 ? 184.867 192.852 239.752 1.00 3.49  ? 3819 LYS A NZ    1 
ATOM   17235 N  N     . GLN A 1 3820 ? 181.663 188.766 236.418 1.00 3.34  ? 3820 GLN A N     1 
ATOM   17236 C  CA    . GLN A 1 3820 ? 182.012 187.468 235.857 1.00 3.30  ? 3820 GLN A CA    1 
ATOM   17237 C  C     . GLN A 1 3820 ? 180.985 186.970 234.850 1.00 3.32  ? 3820 GLN A C     1 
ATOM   17238 O  O     . GLN A 1 3820 ? 181.334 186.174 233.974 1.00 11.08 ? 3820 GLN A O     1 
ATOM   17239 C  CB    . GLN A 1 3820 ? 182.181 186.433 236.971 1.00 4.11  ? 3820 GLN A CB    1 
ATOM   17240 C  CG    . GLN A 1 3820 ? 183.216 186.791 238.024 1.00 2.66  ? 3820 GLN A CG    1 
ATOM   17241 C  CD    . GLN A 1 3820 ? 184.574 187.107 237.431 1.00 9.73  ? 3820 GLN A CD    1 
ATOM   17242 O  OE1   . GLN A 1 3820 ? 185.154 188.157 237.706 1.00 12.82 ? 3820 GLN A OE1   1 
ATOM   17243 N  NE2   . GLN A 1 3820 ? 185.088 186.199 236.610 1.00 13.57 ? 3820 GLN A NE2   1 
ATOM   17244 N  N     . ILE A 1 3821 ? 179.732 187.412 234.952 1.00 2.47  ? 3821 ILE A N     1 
ATOM   17245 C  CA    . ILE A 1 3821 ? 178.687 186.930 234.056 1.00 2.55  ? 3821 ILE A CA    1 
ATOM   17246 C  C     . ILE A 1 3821 ? 178.392 187.893 232.908 1.00 2.83  ? 3821 ILE A C     1 
ATOM   17247 O  O     . ILE A 1 3821 ? 177.803 187.470 231.903 1.00 3.71  ? 3821 ILE A O     1 
ATOM   17248 C  CB    . ILE A 1 3821 ? 177.391 186.621 234.835 1.00 2.03  ? 3821 ILE A CB    1 
ATOM   17249 C  CG1   . ILE A 1 3821 ? 176.745 187.909 235.345 1.00 2.84  ? 3821 ILE A CG1   1 
ATOM   17250 C  CG2   . ILE A 1 3821 ? 177.682 185.676 235.988 1.00 2.04  ? 3821 ILE A CG2   1 
ATOM   17251 C  CD1   . ILE A 1 3821 ? 175.365 187.708 235.918 1.00 1.69  ? 3821 ILE A CD1   1 
ATOM   17252 N  N     . HIS A 1 3822 ? 178.778 189.161 233.024 1.00 2.74  ? 3822 HIS A N     1 
ATOM   17253 C  CA    . HIS A 1 3822 ? 178.618 190.111 231.933 1.00 1.17  ? 3822 HIS A CA    1 
ATOM   17254 C  C     . HIS A 1 3822 ? 179.618 191.241 232.119 1.00 1.25  ? 3822 HIS A C     1 
ATOM   17255 O  O     . HIS A 1 3822 ? 179.796 191.738 233.233 1.00 3.99  ? 3822 HIS A O     1 
ATOM   17256 C  CB    . HIS A 1 3822 ? 177.191 190.667 231.872 1.00 1.26  ? 3822 HIS A CB    1 
ATOM   17257 C  CG    . HIS A 1 3822 ? 176.790 191.146 230.512 1.00 1.11  ? 3822 HIS A CG    1 
ATOM   17258 N  ND1   . HIS A 1 3822 ? 177.269 192.317 229.966 1.00 1.79  ? 3822 HIS A ND1   1 
ATOM   17259 C  CD2   . HIS A 1 3822 ? 175.959 190.611 229.588 1.00 1.17  ? 3822 HIS A CD2   1 
ATOM   17260 C  CE1   . HIS A 1 3822 ? 176.750 192.482 228.763 1.00 1.75  ? 3822 HIS A CE1   1 
ATOM   17261 N  NE2   . HIS A 1 3822 ? 175.951 191.462 228.511 1.00 4.69  ? 3822 HIS A NE2   1 
ATOM   17262 N  N     . PHE A 1 3823 ? 180.261 191.643 231.021 1.00 1.60  ? 3823 PHE A N     1 
ATOM   17263 C  CA    . PHE A 1 3823 ? 181.254 192.710 231.084 1.00 1.62  ? 3823 PHE A CA    1 
ATOM   17264 C  C     . PHE A 1 3823 ? 180.648 194.046 231.491 1.00 1.23  ? 3823 PHE A C     1 
ATOM   17265 O  O     . PHE A 1 3823 ? 181.371 194.915 231.987 1.00 3.13  ? 3823 PHE A O     1 
ATOM   17266 C  CB    . PHE A 1 3823 ? 181.970 192.848 229.737 1.00 1.43  ? 3823 PHE A CB    1 
ATOM   17267 C  CG    . PHE A 1 3823 ? 181.061 193.211 228.592 1.00 2.05  ? 3823 PHE A CG    1 
ATOM   17268 C  CD1   . PHE A 1 3823 ? 180.741 194.533 228.331 1.00 1.77  ? 3823 PHE A CD1   1 
ATOM   17269 C  CD2   . PHE A 1 3823 ? 180.534 192.229 227.773 1.00 2.23  ? 3823 PHE A CD2   1 
ATOM   17270 C  CE1   . PHE A 1 3823 ? 179.906 194.864 227.287 1.00 0.92  ? 3823 PHE A CE1   1 
ATOM   17271 C  CE2   . PHE A 1 3823 ? 179.703 192.557 226.723 1.00 1.25  ? 3823 PHE A CE2   1 
ATOM   17272 C  CZ    . PHE A 1 3823 ? 179.389 193.875 226.479 1.00 0.99  ? 3823 PHE A CZ    1 
ATOM   17273 N  N     . LEU A 1 3824 ? 179.344 194.231 231.293 1.00 0.83  ? 3824 LEU A N     1 
ATOM   17274 C  CA    . LEU A 1 3824 ? 178.698 195.493 231.620 1.00 0.89  ? 3824 LEU A CA    1 
ATOM   17275 C  C     . LEU A 1 3824 ? 178.474 195.678 233.115 1.00 0.54  ? 3824 LEU A C     1 
ATOM   17276 O  O     . LEU A 1 3824 ? 178.305 196.815 233.565 1.00 0.39  ? 3824 LEU A O     1 
ATOM   17277 C  CB    . LEU A 1 3824 ? 177.363 195.597 230.880 1.00 0.91  ? 3824 LEU A CB    1 
ATOM   17278 C  CG    . LEU A 1 3824 ? 176.669 196.960 230.845 1.00 0.42  ? 3824 LEU A CG    1 
ATOM   17279 C  CD1   . LEU A 1 3824 ? 177.471 197.949 230.018 1.00 0.98  ? 3824 LEU A CD1   1 
ATOM   17280 C  CD2   . LEU A 1 3824 ? 175.257 196.830 230.310 1.00 0.27  ? 3824 LEU A CD2   1 
ATOM   17281 N  N     . TYR A 1 3825 ? 178.487 194.599 233.897 1.00 1.38  ? 3825 TYR A N     1 
ATOM   17282 C  CA    . TYR A 1 3825 ? 178.122 194.671 235.313 1.00 0.83  ? 3825 TYR A CA    1 
ATOM   17283 C  C     . TYR A 1 3825 ? 179.348 195.080 236.124 1.00 0.57  ? 3825 TYR A C     1 
ATOM   17284 O  O     . TYR A 1 3825 ? 179.982 194.278 236.813 1.00 1.52  ? 3825 TYR A O     1 
ATOM   17285 C  CB    . TYR A 1 3825 ? 177.548 193.344 235.795 1.00 0.63  ? 3825 TYR A CB    1 
ATOM   17286 C  CG    . TYR A 1 3825 ? 176.358 192.838 235.004 1.00 0.94  ? 3825 TYR A CG    1 
ATOM   17287 C  CD1   . TYR A 1 3825 ? 175.646 193.678 234.155 1.00 0.91  ? 3825 TYR A CD1   1 
ATOM   17288 C  CD2   . TYR A 1 3825 ? 175.940 191.520 235.119 1.00 1.01  ? 3825 TYR A CD2   1 
ATOM   17289 C  CE1   . TYR A 1 3825 ? 174.568 193.214 233.435 1.00 0.66  ? 3825 TYR A CE1   1 
ATOM   17290 C  CE2   . TYR A 1 3825 ? 174.859 191.051 234.407 1.00 0.71  ? 3825 TYR A CE2   1 
ATOM   17291 C  CZ    . TYR A 1 3825 ? 174.175 191.901 233.567 1.00 0.54  ? 3825 TYR A CZ    1 
ATOM   17292 O  OH    . TYR A 1 3825 ? 173.097 191.433 232.857 1.00 0.86  ? 3825 TYR A OH    1 
ATOM   17293 N  N     . GLN A 1 3826 ? 179.679 196.364 236.039 1.00 0.72  ? 3826 GLN A N     1 
ATOM   17294 C  CA    . GLN A 1 3826 ? 180.781 196.955 236.786 1.00 0.39  ? 3826 GLN A CA    1 
ATOM   17295 C  C     . GLN A 1 3826 ? 180.199 197.848 237.871 1.00 0.58  ? 3826 GLN A C     1 
ATOM   17296 O  O     . GLN A 1 3826 ? 179.418 198.758 237.574 1.00 0.95  ? 3826 GLN A O     1 
ATOM   17297 C  CB    . GLN A 1 3826 ? 181.703 197.759 235.871 1.00 0.64  ? 3826 GLN A CB    1 
ATOM   17298 C  CG    . GLN A 1 3826 ? 182.203 197.013 234.645 1.00 0.61  ? 3826 GLN A CG    1 
ATOM   17299 C  CD    . GLN A 1 3826 ? 182.852 195.688 234.976 1.00 0.90  ? 3826 GLN A CD    1 
ATOM   17300 O  OE1   . GLN A 1 3826 ? 183.823 195.627 235.727 1.00 1.77  ? 3826 GLN A OE1   1 
ATOM   17301 N  NE2   . GLN A 1 3826 ? 182.328 194.617 234.397 1.00 0.99  ? 3826 GLN A NE2   1 
ATOM   17302 N  N     . TYR A 1 3827 ? 180.575 197.594 239.120 1.00 0.92  ? 3827 TYR A N     1 
ATOM   17303 C  CA    . TYR A 1 3827 ? 180.034 198.327 240.256 1.00 1.31  ? 3827 TYR A CA    1 
ATOM   17304 C  C     . TYR A 1 3827 ? 181.151 198.679 241.222 1.00 1.88  ? 3827 TYR A C     1 
ATOM   17305 O  O     . TYR A 1 3827 ? 181.875 197.796 241.690 1.00 5.72  ? 3827 TYR A O     1 
ATOM   17306 C  CB    . TYR A 1 3827 ? 178.948 197.514 240.962 1.00 0.89  ? 3827 TYR A CB    1 
ATOM   17307 C  CG    . TYR A 1 3827 ? 177.840 197.108 240.027 1.00 0.88  ? 3827 TYR A CG    1 
ATOM   17308 C  CD1   . TYR A 1 3827 ? 176.982 198.057 239.490 1.00 0.70  ? 3827 TYR A CD1   1 
ATOM   17309 C  CD2   . TYR A 1 3827 ? 177.671 195.785 239.651 1.00 0.78  ? 3827 TYR A CD2   1 
ATOM   17310 C  CE1   . TYR A 1 3827 ? 175.979 197.696 238.624 1.00 1.61  ? 3827 TYR A CE1   1 
ATOM   17311 C  CE2   . TYR A 1 3827 ? 176.668 195.415 238.786 1.00 0.66  ? 3827 TYR A CE2   1 
ATOM   17312 C  CZ    . TYR A 1 3827 ? 175.825 196.373 238.273 1.00 0.74  ? 3827 TYR A CZ    1 
ATOM   17313 O  OH    . TYR A 1 3827 ? 174.820 196.008 237.409 1.00 1.42  ? 3827 TYR A OH    1 
ATOM   17314 N  N     . SER A 1 3828 ? 181.282 199.966 241.518 1.00 2.13  ? 3828 SER A N     1 
ATOM   17315 C  CA    . SER A 1 3828 ? 182.274 200.430 242.468 1.00 1.16  ? 3828 SER A CA    1 
ATOM   17316 C  C     . SER A 1 3828 ? 181.760 200.259 243.895 1.00 1.57  ? 3828 SER A C     1 
ATOM   17317 O  O     . SER A 1 3828 ? 180.588 199.955 244.134 1.00 2.72  ? 3828 SER A O     1 
ATOM   17318 C  CB    . SER A 1 3828 ? 182.629 201.890 242.199 1.00 1.18  ? 3828 SER A CB    1 
ATOM   17319 O  OG    . SER A 1 3828 ? 181.532 202.739 242.481 1.00 1.22  ? 3828 SER A OG    1 
ATOM   17320 N  N     . LEU A 1 3829 ? 182.663 200.450 244.856 1.00 1.78  ? 3829 LEU A N     1 
ATOM   17321 C  CA    . LEU A 1 3829 ? 182.252 200.439 246.253 1.00 0.96  ? 3829 LEU A CA    1 
ATOM   17322 C  C     . LEU A 1 3829 ? 181.367 201.632 246.580 1.00 0.86  ? 3829 LEU A C     1 
ATOM   17323 O  O     . LEU A 1 3829 ? 180.451 201.516 247.402 1.00 1.43  ? 3829 LEU A O     1 
ATOM   17324 C  CB    . LEU A 1 3829 ? 183.477 200.411 247.166 1.00 1.54  ? 3829 LEU A CB    1 
ATOM   17325 C  CG    . LEU A 1 3829 ? 183.201 200.485 248.668 1.00 2.21  ? 3829 LEU A CG    1 
ATOM   17326 C  CD1   . LEU A 1 3829 ? 182.340 199.317 249.115 1.00 0.70  ? 3829 LEU A CD1   1 
ATOM   17327 C  CD2   . LEU A 1 3829 ? 184.497 200.534 249.450 1.00 3.18  ? 3829 LEU A CD2   1 
ATOM   17328 N  N     . GLN A 1 3830 ? 181.613 202.777 245.942 1.00 1.12  ? 3830 GLN A N     1 
ATOM   17329 C  CA    . GLN A 1 3830 ? 180.798 203.957 246.202 1.00 2.07  ? 3830 GLN A CA    1 
ATOM   17330 C  C     . GLN A 1 3830 ? 179.350 203.729 245.788 1.00 2.13  ? 3830 GLN A C     1 
ATOM   17331 O  O     . GLN A 1 3830 ? 178.428 204.261 246.416 1.00 2.81  ? 3830 GLN A O     1 
ATOM   17332 C  CB    . GLN A 1 3830 ? 181.379 205.170 245.476 1.00 1.81  ? 3830 GLN A CB    1 
ATOM   17333 C  CG    . GLN A 1 3830 ? 180.811 206.495 245.951 1.00 4.18  ? 3830 GLN A CG    1 
ATOM   17334 C  CD    . GLN A 1 3830 ? 180.784 206.601 247.463 1.00 9.31  ? 3830 GLN A CD    1 
ATOM   17335 O  OE1   . GLN A 1 3830 ? 181.820 206.517 248.121 1.00 10.17 ? 3830 GLN A OE1   1 
ATOM   17336 N  NE2   . GLN A 1 3830 ? 179.593 206.781 248.024 1.00 8.45  ? 3830 GLN A NE2   1 
ATOM   17337 N  N     . PHE A 1 3831 ? 179.131 202.942 244.732 1.00 1.60  ? 3831 PHE A N     1 
ATOM   17338 C  CA    . PHE A 1 3831 ? 177.771 202.651 244.290 1.00 1.29  ? 3831 PHE A CA    1 
ATOM   17339 C  C     . PHE A 1 3831 ? 177.000 201.891 245.363 1.00 1.43  ? 3831 PHE A C     1 
ATOM   17340 O  O     . PHE A 1 3831 ? 175.828 202.186 245.627 1.00 1.82  ? 3831 PHE A O     1 
ATOM   17341 C  CB    . PHE A 1 3831 ? 177.805 201.865 242.978 1.00 1.67  ? 3831 PHE A CB    1 
ATOM   17342 C  CG    . PHE A 1 3831 ? 176.446 201.511 242.446 1.00 1.63  ? 3831 PHE A CG    1 
ATOM   17343 C  CD1   . PHE A 1 3831 ? 176.074 200.191 242.285 1.00 1.77  ? 3831 PHE A CD1   1 
ATOM   17344 C  CD2   . PHE A 1 3831 ? 175.541 202.501 242.107 1.00 4.28  ? 3831 PHE A CD2   1 
ATOM   17345 C  CE1   . PHE A 1 3831 ? 174.824 199.862 241.793 1.00 3.14  ? 3831 PHE A CE1   1 
ATOM   17346 C  CE2   . PHE A 1 3831 ? 174.288 202.176 241.617 1.00 6.27  ? 3831 PHE A CE2   1 
ATOM   17347 C  CZ    . PHE A 1 3831 ? 173.932 200.855 241.460 1.00 1.47  ? 3831 PHE A CZ    1 
ATOM   17348 N  N     . PHE A 1 3832 ? 177.644 200.909 245.998 1.00 0.99  ? 3832 PHE A N     1 
ATOM   17349 C  CA    . PHE A 1 3832 ? 176.999 200.208 247.101 1.00 0.99  ? 3832 PHE A CA    1 
ATOM   17350 C  C     . PHE A 1 3832 ? 176.843 201.111 248.320 1.00 1.50  ? 3832 PHE A C     1 
ATOM   17351 O  O     . PHE A 1 3832 ? 175.832 201.040 249.024 1.00 1.89  ? 3832 PHE A O     1 
ATOM   17352 C  CB    . PHE A 1 3832 ? 177.777 198.944 247.469 1.00 0.77  ? 3832 PHE A CB    1 
ATOM   17353 C  CG    . PHE A 1 3832 ? 177.331 198.322 248.761 1.00 1.20  ? 3832 PHE A CG    1 
ATOM   17354 C  CD1   . PHE A 1 3832 ? 176.248 197.459 248.788 1.00 1.11  ? 3832 PHE A CD1   1 
ATOM   17355 C  CD2   . PHE A 1 3832 ? 177.990 198.601 249.948 1.00 0.65  ? 3832 PHE A CD2   1 
ATOM   17356 C  CE1   . PHE A 1 3832 ? 175.827 196.896 249.972 1.00 1.23  ? 3832 PHE A CE1   1 
ATOM   17357 C  CE2   . PHE A 1 3832 ? 177.572 198.041 251.135 1.00 0.47  ? 3832 PHE A CE2   1 
ATOM   17358 C  CZ    . PHE A 1 3832 ? 176.490 197.186 251.147 1.00 1.36  ? 3832 PHE A CZ    1 
ATOM   17359 N  N     . LEU A 1 3833 ? 177.842 201.953 248.593 1.00 1.93  ? 3833 LEU A N     1 
ATOM   17360 C  CA    . LEU A 1 3833 ? 177.739 202.867 249.726 1.00 1.75  ? 3833 LEU A CA    1 
ATOM   17361 C  C     . LEU A 1 3833 ? 176.630 203.888 249.520 1.00 2.35  ? 3833 LEU A C     1 
ATOM   17362 O  O     . LEU A 1 3833 ? 176.001 204.321 250.493 1.00 4.68  ? 3833 LEU A O     1 
ATOM   17363 C  CB    . LEU A 1 3833 ? 179.077 203.564 249.961 1.00 2.71  ? 3833 LEU A CB    1 
ATOM   17364 C  CG    . LEU A 1 3833 ? 180.215 202.664 250.442 1.00 1.53  ? 3833 LEU A CG    1 
ATOM   17365 C  CD1   . LEU A 1 3833 ? 181.509 203.449 250.556 1.00 2.77  ? 3833 LEU A CD1   1 
ATOM   17366 C  CD2   . LEU A 1 3833 ? 179.862 202.010 251.767 1.00 2.61  ? 3833 LEU A CD2   1 
ATOM   17367 N  N     . ASP A 1 3834 ? 176.380 204.288 248.273 1.00 2.07  ? 3834 ASP A N     1 
ATOM   17368 C  CA    . ASP A 1 3834 ? 175.227 205.133 247.985 1.00 2.60  ? 3834 ASP A CA    1 
ATOM   17369 C  C     . ASP A 1 3834 ? 173.925 204.395 248.269 1.00 4.70  ? 3834 ASP A C     1 
ATOM   17370 O  O     . ASP A 1 3834 ? 172.961 204.988 248.768 1.00 4.13  ? 3834 ASP A O     1 
ATOM   17371 C  CB    . ASP A 1 3834 ? 175.275 205.603 246.531 1.00 3.74  ? 3834 ASP A CB    1 
ATOM   17372 C  CG    . ASP A 1 3834 ? 176.457 206.506 246.248 1.00 6.92  ? 3834 ASP A CG    1 
ATOM   17373 O  OD1   . ASP A 1 3834 ? 177.151 206.908 247.205 1.00 11.38 ? 3834 ASP A OD1   1 
ATOM   17374 O  OD2   . ASP A 1 3834 ? 176.701 206.805 245.061 1.00 8.68  ? 3834 ASP A OD2   1 
ATOM   17375 N  N     . ILE A 1 3835 ? 173.874 203.102 247.944 1.00 2.64  ? 3835 ILE A N     1 
ATOM   17376 C  CA    . ILE A 1 3835 ? 172.704 202.287 248.264 1.00 1.44  ? 3835 ILE A CA    1 
ATOM   17377 C  C     . ILE A 1 3835 ? 172.526 202.194 249.774 1.00 3.29  ? 3835 ILE A C     1 
ATOM   17378 O  O     . ILE A 1 3835 ? 171.420 202.358 250.302 1.00 2.87  ? 3835 ILE A O     1 
ATOM   17379 C  CB    . ILE A 1 3835 ? 172.839 200.893 247.628 1.00 2.32  ? 3835 ILE A CB    1 
ATOM   17380 C  CG1   . ILE A 1 3835 ? 172.637 200.966 246.114 1.00 2.08  ? 3835 ILE A CG1   1 
ATOM   17381 C  CG2   . ILE A 1 3835 ? 171.871 199.903 248.267 1.00 1.15  ? 3835 ILE A CG2   1 
ATOM   17382 C  CD1   . ILE A 1 3835 ? 173.049 199.706 245.388 1.00 0.90  ? 3835 ILE A CD1   1 
ATOM   17383 N  N     . TYR A 1 3836 ? 173.623 201.933 250.488 1.00 5.54  ? 3836 TYR A N     1 
ATOM   17384 C  CA    . TYR A 1 3836 ? 173.566 201.810 251.940 1.00 2.06  ? 3836 TYR A CA    1 
ATOM   17385 C  C     . TYR A 1 3836 ? 173.154 203.122 252.591 1.00 2.72  ? 3836 TYR A C     1 
ATOM   17386 O  O     . TYR A 1 3836 ? 172.365 203.132 253.543 1.00 3.21  ? 3836 TYR A O     1 
ATOM   17387 C  CB    . TYR A 1 3836 ? 174.924 201.345 252.460 1.00 2.81  ? 3836 TYR A CB    1 
ATOM   17388 C  CG    . TYR A 1 3836 ? 174.922 200.879 253.893 1.00 3.26  ? 3836 TYR A CG    1 
ATOM   17389 C  CD1   . TYR A 1 3836 ? 173.835 200.199 254.423 1.00 3.39  ? 3836 TYR A CD1   1 
ATOM   17390 C  CD2   . TYR A 1 3836 ? 176.013 201.116 254.714 1.00 1.75  ? 3836 TYR A CD2   1 
ATOM   17391 C  CE1   . TYR A 1 3836 ? 173.836 199.775 255.735 1.00 3.19  ? 3836 TYR A CE1   1 
ATOM   17392 C  CE2   . TYR A 1 3836 ? 176.023 200.695 256.020 1.00 2.14  ? 3836 TYR A CE2   1 
ATOM   17393 C  CZ    . TYR A 1 3836 ? 174.936 200.025 256.528 1.00 3.15  ? 3836 TYR A CZ    1 
ATOM   17394 O  OH    . TYR A 1 3836 ? 174.952 199.604 257.832 1.00 2.98  ? 3836 TYR A OH    1 
ATOM   17395 N  N     . HIS A 1 3837 ? 173.677 204.241 252.089 1.00 2.90  ? 3837 HIS A N     1 
ATOM   17396 C  CA    . HIS A 1 3837 ? 173.281 205.547 252.602 1.00 3.68  ? 3837 HIS A CA    1 
ATOM   17397 C  C     . HIS A 1 3837 ? 171.801 205.809 252.356 1.00 5.91  ? 3837 HIS A C     1 
ATOM   17398 O  O     . HIS A 1 3837 ? 171.115 206.390 253.204 1.00 7.29  ? 3837 HIS A O     1 
ATOM   17399 C  CB    . HIS A 1 3837 ? 174.137 206.637 251.956 1.00 5.26  ? 3837 HIS A CB    1 
ATOM   17400 C  CG    . HIS A 1 3837 ? 173.780 208.025 252.384 1.00 10.20 ? 3837 HIS A CG    1 
ATOM   17401 N  ND1   . HIS A 1 3837 ? 174.434 208.680 253.404 1.00 14.46 ? 3837 HIS A ND1   1 
ATOM   17402 C  CD2   . HIS A 1 3837 ? 172.841 208.885 251.926 1.00 8.37  ? 3837 HIS A CD2   1 
ATOM   17403 C  CE1   . HIS A 1 3837 ? 173.912 209.884 253.557 1.00 11.69 ? 3837 HIS A CE1   1 
ATOM   17404 N  NE2   . HIS A 1 3837 ? 172.943 210.033 252.673 1.00 13.25 ? 3837 HIS A NE2   1 
ATOM   17405 N  N     . ASN A 1 3838 ? 171.294 205.390 251.194 1.00 4.53  ? 3838 ASN A N     1 
ATOM   17406 C  CA    . ASN A 1 3838 ? 169.886 205.594 250.871 1.00 4.50  ? 3838 ASN A CA    1 
ATOM   17407 C  C     . ASN A 1 3838 ? 168.979 204.848 251.844 1.00 5.36  ? 3838 ASN A C     1 
ATOM   17408 O  O     . ASN A 1 3838 ? 167.960 205.387 252.291 1.00 6.99  ? 3838 ASN A O     1 
ATOM   17409 C  CB    . ASN A 1 3838 ? 169.619 205.148 249.434 1.00 5.64  ? 3838 ASN A CB    1 
ATOM   17410 C  CG    . ASN A 1 3838 ? 168.190 205.382 249.007 1.00 6.03  ? 3838 ASN A CG    1 
ATOM   17411 O  OD1   . ASN A 1 3838 ? 167.447 204.441 248.740 1.00 4.98  ? 3838 ASN A OD1   1 
ATOM   17412 N  ND2   . ASN A 1 3838 ? 167.796 206.646 248.934 1.00 7.90  ? 3838 ASN A ND2   1 
ATOM   17413 N  N     . VAL A 1 3839 ? 169.331 203.606 252.177 1.00 3.78  ? 3839 VAL A N     1 
ATOM   17414 C  CA    . VAL A 1 3839 ? 168.522 202.814 253.097 1.00 4.05  ? 3839 VAL A CA    1 
ATOM   17415 C  C     . VAL A 1 3839 ? 168.560 203.399 254.504 1.00 5.15  ? 3839 VAL A C     1 
ATOM   17416 O  O     . VAL A 1 3839 ? 167.569 203.328 255.240 1.00 10.33 ? 3839 VAL A O     1 
ATOM   17417 C  CB    . VAL A 1 3839 ? 168.991 201.346 253.072 1.00 3.52  ? 3839 VAL A CB    1 
ATOM   17418 C  CG1   . VAL A 1 3839 ? 168.243 200.519 254.099 1.00 6.41  ? 3839 VAL A CG1   1 
ATOM   17419 C  CG2   . VAL A 1 3839 ? 168.797 200.762 251.687 1.00 5.19  ? 3839 VAL A CG2   1 
ATOM   17420 N  N     . LEU A 1 3840 ? 169.688 203.978 254.905 1.00 4.62  ? 3840 LEU A N     1 
ATOM   17421 C  CA    . LEU A 1 3840 ? 169.838 204.480 256.265 1.00 3.76  ? 3840 LEU A CA    1 
ATOM   17422 C  C     . LEU A 1 3840 ? 169.263 205.877 256.464 1.00 5.90  ? 3840 LEU A C     1 
ATOM   17423 O  O     . LEU A 1 3840 ? 168.779 206.183 257.560 1.00 16.60 ? 3840 LEU A O     1 
ATOM   17424 C  CB    . LEU A 1 3840 ? 171.315 204.482 256.661 1.00 3.86  ? 3840 LEU A CB    1 
ATOM   17425 C  CG    . LEU A 1 3840 ? 171.966 203.113 256.855 1.00 4.45  ? 3840 LEU A CG    1 
ATOM   17426 C  CD1   . LEU A 1 3840 ? 173.450 203.269 257.130 1.00 3.26  ? 3840 LEU A CD1   1 
ATOM   17427 C  CD2   . LEU A 1 3840 ? 171.283 202.341 257.973 1.00 3.52  ? 3840 LEU A CD2   1 
ATOM   17428 N  N     . TYR A 1 3841 ? 169.299 206.731 255.446 1.00 5.24  ? 3841 TYR A N     1 
ATOM   17429 C  CA    . TYR A 1 3841 ? 168.946 208.134 255.618 1.00 7.19  ? 3841 TYR A CA    1 
ATOM   17430 C  C     . TYR A 1 3841 ? 167.791 208.609 254.753 1.00 8.62  ? 3841 TYR A C     1 
ATOM   17431 O  O     . TYR A 1 3841 ? 167.130 209.581 255.121 1.00 12.16 ? 3841 TYR A O     1 
ATOM   17432 C  CB    . TYR A 1 3841 ? 170.165 209.026 255.338 1.00 6.55  ? 3841 TYR A CB    1 
ATOM   17433 C  CG    . TYR A 1 3841 ? 171.287 208.845 256.330 1.00 13.01 ? 3841 TYR A CG    1 
ATOM   17434 C  CD1   . TYR A 1 3841 ? 171.194 209.370 257.611 1.00 11.97 ? 3841 TYR A CD1   1 
ATOM   17435 C  CD2   . TYR A 1 3841 ? 172.436 208.147 255.989 1.00 10.99 ? 3841 TYR A CD2   1 
ATOM   17436 C  CE1   . TYR A 1 3841 ? 172.215 209.211 258.521 1.00 9.92  ? 3841 TYR A CE1   1 
ATOM   17437 C  CE2   . TYR A 1 3841 ? 173.464 207.982 256.895 1.00 10.61 ? 3841 TYR A CE2   1 
ATOM   17438 C  CZ    . TYR A 1 3841 ? 173.347 208.516 258.160 1.00 16.94 ? 3841 TYR A CZ    1 
ATOM   17439 O  OH    . TYR A 1 3841 ? 174.367 208.354 259.072 1.00 19.23 ? 3841 TYR A OH    1 
ATOM   17440 N  N     . GLU A 1 3842 ? 167.526 207.962 253.623 1.00 7.58  ? 3842 GLU A N     1 
ATOM   17441 C  CA    . GLU A 1 3842 ? 166.464 208.370 252.713 1.00 8.98  ? 3842 GLU A CA    1 
ATOM   17442 C  C     . GLU A 1 3842 ? 165.420 207.270 252.571 1.00 10.68 ? 3842 GLU A C     1 
ATOM   17443 O  O     . GLU A 1 3842 ? 164.961 206.957 251.471 1.00 16.10 ? 3842 GLU A O     1 
ATOM   17444 C  CB    . GLU A 1 3842 ? 167.036 208.757 251.353 1.00 8.38  ? 3842 GLU A CB    1 
ATOM   17445 C  CG    . GLU A 1 3842 ? 168.151 209.785 251.425 1.00 11.85 ? 3842 GLU A CG    1 
ATOM   17446 C  CD    . GLU A 1 3842 ? 169.247 209.534 250.410 1.00 14.15 ? 3842 GLU A CD    1 
ATOM   17447 O  OE1   . GLU A 1 3842 ? 169.150 208.541 249.659 1.00 18.36 ? 3842 GLU A OE1   1 
ATOM   17448 O  OE2   . GLU A 1 3842 ? 170.208 210.329 250.364 1.00 16.59 ? 3842 GLU A OE2   1 
ATOM   17449 N  N     . ASN A 1 3843 ? 165.031 206.670 253.694 1.00 9.06  ? 3843 ASN A N     1 
ATOM   17450 C  CA    . ASN A 1 3843 ? 164.105 205.551 253.688 1.00 12.91 ? 3843 ASN A CA    1 
ATOM   17451 C  C     . ASN A 1 3843 ? 162.735 206.023 254.144 1.00 16.19 ? 3843 ASN A C     1 
ATOM   17452 O  O     . ASN A 1 3843 ? 162.583 206.420 255.310 1.00 19.30 ? 3843 ASN A O     1 
ATOM   17453 C  CB    . ASN A 1 3843 ? 164.616 204.438 254.596 1.00 11.18 ? 3843 ASN A CB    1 
ATOM   17454 C  CG    . ASN A 1 3843 ? 163.761 203.188 254.532 1.00 12.82 ? 3843 ASN A CG    1 
ATOM   17455 O  OD1   . ASN A 1 3843 ? 162.732 203.152 253.860 1.00 17.59 ? 3843 ASN A OD1   1 
ATOM   17456 N  ND2   . ASN A 1 3843 ? 164.201 202.142 255.222 1.00 13.62 ? 3843 ASN A ND2   1 
ATOM   17457 N  N     . PRO A 1 3844 ? 161.718 205.997 253.277 1.00 17.68 ? 3844 PRO A N     1 
ATOM   17458 C  CA    . PRO A 1 3844 ? 160.378 206.434 253.704 1.00 13.01 ? 3844 PRO A CA    1 
ATOM   17459 C  C     . PRO A 1 3844 ? 159.746 205.534 254.747 1.00 15.55 ? 3844 PRO A C     1 
ATOM   17460 O  O     . PRO A 1 3844 ? 158.778 205.950 255.395 1.00 29.14 ? 3844 PRO A O     1 
ATOM   17461 C  CB    . PRO A 1 3844 ? 159.569 206.423 252.397 1.00 17.98 ? 3844 PRO A CB    1 
ATOM   17462 C  CG    . PRO A 1 3844 ? 160.592 206.328 251.293 1.00 15.73 ? 3844 PRO A CG    1 
ATOM   17463 C  CD    . PRO A 1 3844 ? 161.734 205.566 251.872 1.00 12.23 ? 3844 PRO A CD    1 
ATOM   17464 N  N     . ASN A 1 3845 ? 160.253 204.320 254.932 1.00 15.10 ? 3845 ASN A N     1 
ATOM   17465 C  CA    . ASN A 1 3845 ? 159.685 203.375 255.882 1.00 13.34 ? 3845 ASN A CA    1 
ATOM   17466 C  C     . ASN A 1 3845 ? 160.160 203.607 257.312 1.00 15.82 ? 3845 ASN A C     1 
ATOM   17467 O  O     . ASN A 1 3845 ? 159.714 202.898 258.218 1.00 14.29 ? 3845 ASN A O     1 
ATOM   17468 C  CB    . ASN A 1 3845 ? 160.015 201.944 255.452 1.00 12.48 ? 3845 ASN A CB    1 
ATOM   17469 C  CG    . ASN A 1 3845 ? 159.390 201.579 254.119 1.00 18.94 ? 3845 ASN A CG    1 
ATOM   17470 O  OD1   . ASN A 1 3845 ? 160.091 201.343 253.137 1.00 15.01 ? 3845 ASN A OD1   1 
ATOM   17471 N  ND2   . ASN A 1 3845 ? 158.065 201.532 254.080 1.00 23.97 ? 3845 ASN A ND2   1 
ATOM   17472 N  N     . LEU A 1 3846 ? 161.050 204.576 257.533 1.00 12.88 ? 3846 LEU A N     1 
ATOM   17473 C  CA    . LEU A 1 3846 ? 161.553 204.901 258.863 1.00 14.65 ? 3846 LEU A CA    1 
ATOM   17474 C  C     . LEU A 1 3846 ? 161.064 206.260 259.353 1.00 19.51 ? 3846 LEU A C     1 
ATOM   17475 O  O     . LEU A 1 3846 ? 161.626 206.806 260.307 1.00 19.95 ? 3846 LEU A O     1 
ATOM   17476 C  CB    . LEU A 1 3846 ? 163.082 204.865 258.873 1.00 15.56 ? 3846 LEU A CB    1 
ATOM   17477 C  CG    . LEU A 1 3846 ? 163.790 203.556 258.529 1.00 10.80 ? 3846 LEU A CG    1 
ATOM   17478 C  CD1   . LEU A 1 3846 ? 165.252 203.824 258.243 1.00 7.29  ? 3846 LEU A CD1   1 
ATOM   17479 C  CD2   . LEU A 1 3846 ? 163.640 202.556 259.659 1.00 11.71 ? 3846 LEU A CD2   1 
ATOM   17480 N  N     . LYS A 1 3847 ? 160.028 206.816 258.718 1.00 20.82 ? 3847 LYS A N     1 
ATOM   17481 C  CA    . LYS A 1 3847 ? 159.611 208.182 259.023 1.00 20.41 ? 3847 LYS A CA    1 
ATOM   17482 C  C     . LYS A 1 3847 ? 159.140 208.319 260.466 1.00 23.96 ? 3847 LYS A C     1 
ATOM   17483 O  O     . LYS A 1 3847 ? 159.535 209.254 261.173 1.00 32.38 ? 3847 LYS A O     1 
ATOM   17484 C  CB    . LYS A 1 3847 ? 158.509 208.619 258.056 1.00 23.94 ? 3847 LYS A CB    1 
ATOM   17485 C  CG    . LYS A 1 3847 ? 158.126 210.084 258.174 1.00 23.56 ? 3847 LYS A CG    1 
ATOM   17486 C  CD    . LYS A 1 3847 ? 159.251 210.994 257.711 1.00 24.67 ? 3847 LYS A CD    1 
ATOM   17487 C  CE    . LYS A 1 3847 ? 159.580 210.763 256.246 1.00 23.32 ? 3847 LYS A CE    1 
ATOM   17488 N  NZ    . LYS A 1 3847 ? 160.687 211.643 255.784 1.00 24.96 ? 3847 LYS A NZ    1 
ATOM   17489 N  N     . GLY A 1 3848 ? 158.303 207.395 260.926 1.00 17.02 ? 3848 GLY A N     1 
ATOM   17490 C  CA    . GLY A 1 3848 ? 157.750 207.503 262.263 1.00 14.80 ? 3848 GLY A CA    1 
ATOM   17491 C  C     . GLY A 1 3848 ? 158.219 206.424 263.214 1.00 19.95 ? 3848 GLY A C     1 
ATOM   17492 O  O     . GLY A 1 3848 ? 157.859 206.427 264.395 1.00 27.00 ? 3848 GLY A O     1 
ATOM   17493 N  N     . VAL A 1 3849 ? 159.028 205.494 262.712 1.00 17.34 ? 3849 VAL A N     1 
ATOM   17494 C  CA    . VAL A 1 3849 ? 159.454 204.360 263.519 1.00 15.40 ? 3849 VAL A CA    1 
ATOM   17495 C  C     . VAL A 1 3849 ? 160.488 204.818 264.540 1.00 21.18 ? 3849 VAL A C     1 
ATOM   17496 O  O     . VAL A 1 3849 ? 161.452 205.517 264.203 1.00 18.76 ? 3849 VAL A O     1 
ATOM   17497 C  CB    . VAL A 1 3849 ? 160.008 203.244 262.624 1.00 16.79 ? 3849 VAL A CB    1 
ATOM   17498 C  CG1   . VAL A 1 3849 ? 160.302 202.015 263.450 1.00 11.65 ? 3849 VAL A CG1   1 
ATOM   17499 C  CG2   . VAL A 1 3849 ? 159.029 202.928 261.502 1.00 21.12 ? 3849 VAL A CG2   1 
ATOM   17500 N  N     . THR A 1 3850 ? 160.289 204.423 265.799 1.00 21.75 ? 3850 THR A N     1 
ATOM   17501 C  CA    . THR A 1 3850 ? 161.190 204.794 266.880 1.00 14.94 ? 3850 THR A CA    1 
ATOM   17502 C  C     . THR A 1 3850 ? 161.886 203.615 267.541 1.00 20.58 ? 3850 THR A C     1 
ATOM   17503 O  O     . THR A 1 3850 ? 162.952 203.810 268.134 1.00 24.99 ? 3850 THR A O     1 
ATOM   17504 C  CB    . THR A 1 3850 ? 160.438 205.581 267.964 1.00 18.77 ? 3850 THR A CB    1 
ATOM   17505 O  OG1   . THR A 1 3850 ? 159.207 204.916 268.273 1.00 20.64 ? 3850 THR A OG1   1 
ATOM   17506 C  CG2   . THR A 1 3850 ? 160.141 206.994 267.489 1.00 20.04 ? 3850 THR A CG2   1 
ATOM   17507 N  N     . ASP A 1 3851 ? 161.327 202.411 267.460 1.00 20.12 ? 3851 ASP A N     1 
ATOM   17508 C  CA    . ASP A 1 3851 ? 161.952 201.260 268.092 1.00 17.18 ? 3851 ASP A CA    1 
ATOM   17509 C  C     . ASP A 1 3851 ? 163.168 200.818 267.288 1.00 19.98 ? 3851 ASP A C     1 
ATOM   17510 O  O     . ASP A 1 3851 ? 163.076 200.587 266.079 1.00 20.94 ? 3851 ASP A O     1 
ATOM   17511 C  CB    . ASP A 1 3851 ? 160.948 200.118 268.219 1.00 14.46 ? 3851 ASP A CB    1 
ATOM   17512 C  CG    . ASP A 1 3851 ? 161.601 198.806 268.590 1.00 21.05 ? 3851 ASP A CG    1 
ATOM   17513 O  OD1   . ASP A 1 3851 ? 162.344 198.779 269.592 1.00 23.66 ? 3851 ASP A OD1   1 
ATOM   17514 O  OD2   . ASP A 1 3851 ? 161.365 197.801 267.886 1.00 21.93 ? 3851 ASP A OD2   1 
ATOM   17515 N  N     . HIS A 1 3852 ? 164.310 200.694 267.971 1.00 19.12 ? 3852 HIS A N     1 
ATOM   17516 C  CA    . HIS A 1 3852 ? 165.560 200.382 267.283 1.00 13.14 ? 3852 HIS A CA    1 
ATOM   17517 C  C     . HIS A 1 3852 ? 165.491 199.028 266.590 1.00 13.16 ? 3852 HIS A C     1 
ATOM   17518 O  O     . HIS A 1 3852 ? 165.980 198.873 265.465 1.00 15.64 ? 3852 HIS A O     1 
ATOM   17519 C  CB    . HIS A 1 3852 ? 166.725 200.417 268.271 1.00 15.22 ? 3852 HIS A CB    1 
ATOM   17520 C  CG    . HIS A 1 3852 ? 166.953 201.760 268.890 1.00 18.50 ? 3852 HIS A CG    1 
ATOM   17521 N  ND1   . HIS A 1 3852 ? 166.558 202.935 268.287 1.00 17.50 ? 3852 HIS A ND1   1 
ATOM   17522 C  CD2   . HIS A 1 3852 ? 167.540 202.115 270.057 1.00 17.37 ? 3852 HIS A CD2   1 
ATOM   17523 C  CE1   . HIS A 1 3852 ? 166.888 203.955 269.058 1.00 13.83 ? 3852 HIS A CE1   1 
ATOM   17524 N  NE2   . HIS A 1 3852 ? 167.486 203.485 270.138 1.00 20.41 ? 3852 HIS A NE2   1 
ATOM   17525 N  N     . THR A 1 3853 ? 164.893 198.033 267.248 1.00 11.61 ? 3853 THR A N     1 
ATOM   17526 C  CA    . THR A 1 3853 ? 164.790 196.708 266.645 1.00 13.27 ? 3853 THR A CA    1 
ATOM   17527 C  C     . THR A 1 3853 ? 163.954 196.743 265.371 1.00 13.17 ? 3853 THR A C     1 
ATOM   17528 O  O     . THR A 1 3853 ? 164.321 196.130 264.362 1.00 16.01 ? 3853 THR A O     1 
ATOM   17529 C  CB    . THR A 1 3853 ? 164.197 195.721 267.649 1.00 12.40 ? 3853 THR A CB    1 
ATOM   17530 O  OG1   . THR A 1 3853 ? 165.076 195.597 268.775 1.00 19.61 ? 3853 THR A OG1   1 
ATOM   17531 C  CG2   . THR A 1 3853 ? 164.009 194.356 267.010 1.00 11.63 ? 3853 THR A CG2   1 
ATOM   17532 N  N     . GLN A 1 3854 ? 162.830 197.461 265.396 1.00 11.10 ? 3854 GLN A N     1 
ATOM   17533 C  CA    . GLN A 1 3854 ? 161.959 197.498 264.227 1.00 13.83 ? 3854 GLN A CA    1 
ATOM   17534 C  C     . GLN A 1 3854 ? 162.590 198.309 263.101 1.00 13.43 ? 3854 GLN A C     1 
ATOM   17535 O  O     . GLN A 1 3854 ? 162.431 197.971 261.921 1.00 15.67 ? 3854 GLN A O     1 
ATOM   17536 C  CB    . GLN A 1 3854 ? 160.589 198.056 264.617 1.00 14.86 ? 3854 GLN A CB    1 
ATOM   17537 C  CG    . GLN A 1 3854 ? 159.747 198.539 263.453 1.00 16.29 ? 3854 GLN A CG    1 
ATOM   17538 C  CD    . GLN A 1 3854 ? 158.401 199.074 263.895 1.00 24.00 ? 3854 GLN A CD    1 
ATOM   17539 O  OE1   . GLN A 1 3854 ? 158.182 199.340 265.076 1.00 16.52 ? 3854 GLN A OE1   1 
ATOM   17540 N  NE2   . GLN A 1 3854 ? 157.489 199.236 262.943 1.00 23.79 ? 3854 GLN A NE2   1 
ATOM   17541 N  N     . ARG A 1 3855 ? 163.320 199.373 263.443 1.00 11.73 ? 3855 ARG A N     1 
ATOM   17542 C  CA    . ARG A 1 3855 ? 164.067 200.114 262.431 1.00 7.78  ? 3855 ARG A CA    1 
ATOM   17543 C  C     . ARG A 1 3855 ? 165.121 199.236 261.775 1.00 9.63  ? 3855 ARG A C     1 
ATOM   17544 O  O     . ARG A 1 3855 ? 165.347 199.322 260.562 1.00 12.99 ? 3855 ARG A O     1 
ATOM   17545 C  CB    . ARG A 1 3855 ? 164.721 201.348 263.050 1.00 8.25  ? 3855 ARG A CB    1 
ATOM   17546 C  CG    . ARG A 1 3855 ? 163.753 202.373 263.586 1.00 9.36  ? 3855 ARG A CG    1 
ATOM   17547 C  CD    . ARG A 1 3855 ? 164.445 203.682 263.900 1.00 13.57 ? 3855 ARG A CD    1 
ATOM   17548 N  NE    . ARG A 1 3855 ? 165.250 204.158 262.783 1.00 12.05 ? 3855 ARG A NE    1 
ATOM   17549 C  CZ    . ARG A 1 3855 ? 165.034 205.293 262.137 1.00 13.71 ? 3855 ARG A CZ    1 
ATOM   17550 N  NH1   . ARG A 1 3855 ? 164.040 206.099 262.468 1.00 14.34 ? 3855 ARG A NH1   1 
ATOM   17551 N  NH2   . ARG A 1 3855 ? 165.839 205.629 261.131 1.00 19.32 ? 3855 ARG A NH2   1 
ATOM   17552 N  N     . LEU A 1 3856 ? 165.785 198.391 262.565 1.00 8.30  ? 3856 LEU A N     1 
ATOM   17553 C  CA    . LEU A 1 3856 ? 166.802 197.502 262.015 1.00 6.66  ? 3856 LEU A CA    1 
ATOM   17554 C  C     . LEU A 1 3856 ? 166.198 196.516 261.024 1.00 10.20 ? 3856 LEU A C     1 
ATOM   17555 O  O     . LEU A 1 3856 ? 166.791 196.236 259.976 1.00 10.52 ? 3856 LEU A O     1 
ATOM   17556 C  CB    . LEU A 1 3856 ? 167.515 196.766 263.146 1.00 6.20  ? 3856 LEU A CB    1 
ATOM   17557 C  CG    . LEU A 1 3856 ? 168.813 196.046 262.789 1.00 5.15  ? 3856 LEU A CG    1 
ATOM   17558 C  CD1   . LEU A 1 3856 ? 169.686 196.919 261.904 1.00 6.38  ? 3856 LEU A CD1   1 
ATOM   17559 C  CD2   . LEU A 1 3856 ? 169.555 195.651 264.054 1.00 7.00  ? 3856 LEU A CD2   1 
ATOM   17560 N  N     . SER A 1 3857 ? 165.021 195.970 261.340 1.00 9.50  ? 3857 SER A N     1 
ATOM   17561 C  CA    . SER A 1 3857 ? 164.353 195.069 260.407 1.00 10.27 ? 3857 SER A CA    1 
ATOM   17562 C  C     . SER A 1 3857 ? 163.981 195.792 259.119 1.00 7.98  ? 3857 SER A C     1 
ATOM   17563 O  O     . SER A 1 3857 ? 164.129 195.241 258.023 1.00 10.23 ? 3857 SER A O     1 
ATOM   17564 C  CB    . SER A 1 3857 ? 163.111 194.459 261.057 1.00 11.35 ? 3857 SER A CB    1 
ATOM   17565 O  OG    . SER A 1 3857 ? 162.117 195.442 261.278 1.00 13.15 ? 3857 SER A OG    1 
ATOM   17566 N  N     . ILE A 1 3858 ? 163.493 197.029 259.235 1.00 7.48  ? 3858 ILE A N     1 
ATOM   17567 C  CA    . ILE A 1 3858 ? 163.173 197.820 258.051 1.00 7.76  ? 3858 ILE A CA    1 
ATOM   17568 C  C     . ILE A 1 3858 ? 164.430 198.093 257.236 1.00 9.49  ? 3858 ILE A C     1 
ATOM   17569 O  O     . ILE A 1 3858 ? 164.430 197.963 256.006 1.00 11.50 ? 3858 ILE A O     1 
ATOM   17570 C  CB    . ILE A 1 3858 ? 162.468 199.126 258.458 1.00 9.12  ? 3858 ILE A CB    1 
ATOM   17571 C  CG1   . ILE A 1 3858 ? 161.079 198.831 259.024 1.00 8.97  ? 3858 ILE A CG1   1 
ATOM   17572 C  CG2   . ILE A 1 3858 ? 162.392 200.079 257.280 1.00 10.23 ? 3858 ILE A CG2   1 
ATOM   17573 C  CD1   . ILE A 1 3858 ? 160.479 199.984 259.788 1.00 12.89 ? 3858 ILE A CD1   1 
ATOM   17574 N  N     . ILE A 1 3859 ? 165.518 198.474 257.908 1.00 7.70  ? 3859 ILE A N     1 
ATOM   17575 C  CA    . ILE A 1 3859 ? 166.772 198.743 257.211 1.00 6.49  ? 3859 ILE A CA    1 
ATOM   17576 C  C     . ILE A 1 3859 ? 167.286 197.482 256.531 1.00 5.26  ? 3859 ILE A C     1 
ATOM   17577 O  O     . ILE A 1 3859 ? 167.720 197.516 255.374 1.00 7.24  ? 3859 ILE A O     1 
ATOM   17578 C  CB    . ILE A 1 3859 ? 167.808 199.329 258.189 1.00 5.49  ? 3859 ILE A CB    1 
ATOM   17579 C  CG1   . ILE A 1 3859 ? 167.482 200.790 258.499 1.00 5.49  ? 3859 ILE A CG1   1 
ATOM   17580 C  CG2   . ILE A 1 3859 ? 169.215 199.199 257.631 1.00 4.53  ? 3859 ILE A CG2   1 
ATOM   17581 C  CD1   . ILE A 1 3859 ? 168.174 201.321 259.730 1.00 5.80  ? 3859 ILE A CD1   1 
ATOM   17582 N  N     . THR A 1 3860 ? 167.238 196.349 257.237 1.00 4.96  ? 3860 THR A N     1 
ATOM   17583 C  CA    . THR A 1 3860 ? 167.711 195.094 256.661 1.00 5.64  ? 3860 THR A CA    1 
ATOM   17584 C  C     . THR A 1 3860 ? 166.881 194.693 255.450 1.00 9.01  ? 3860 THR A C     1 
ATOM   17585 O  O     . THR A 1 3860 ? 167.429 194.299 254.414 1.00 7.19  ? 3860 THR A O     1 
ATOM   17586 C  CB    . THR A 1 3860 ? 167.675 193.988 257.717 1.00 5.67  ? 3860 THR A CB    1 
ATOM   17587 O  OG1   . THR A 1 3860 ? 168.406 194.406 258.876 1.00 9.38  ? 3860 THR A OG1   1 
ATOM   17588 C  CG2   . THR A 1 3860 ? 168.285 192.707 257.170 1.00 3.81  ? 3860 THR A CG2   1 
ATOM   17589 N  N     . LYS A 1 3861 ? 165.556 194.786 255.563 1.00 8.90  ? 3861 LYS A N     1 
ATOM   17590 C  CA    . LYS A 1 3861 ? 164.687 194.460 254.438 1.00 6.27  ? 3861 LYS A CA    1 
ATOM   17591 C  C     . LYS A 1 3861 ? 164.918 195.410 253.270 1.00 4.72  ? 3861 LYS A C     1 
ATOM   17592 O  O     . LYS A 1 3861 ? 165.026 194.980 252.117 1.00 4.21  ? 3861 LYS A O     1 
ATOM   17593 C  CB    . LYS A 1 3861 ? 163.225 194.505 254.884 1.00 6.75  ? 3861 LYS A CB    1 
ATOM   17594 C  CG    . LYS A 1 3861 ? 162.229 194.132 253.804 1.00 6.33  ? 3861 LYS A CG    1 
ATOM   17595 C  CD    . LYS A 1 3861 ? 160.812 194.090 254.351 1.00 8.70  ? 3861 LYS A CD    1 
ATOM   17596 C  CE    . LYS A 1 3861 ? 159.801 193.867 253.242 1.00 18.23 ? 3861 LYS A CE    1 
ATOM   17597 N  NZ    . LYS A 1 3861 ? 159.948 192.523 252.617 1.00 13.24 ? 3861 LYS A NZ    1 
ATOM   17598 N  N     . ASP A 1 3862 ? 165.009 196.710 253.557 1.00 7.05  ? 3862 ASP A N     1 
ATOM   17599 C  CA    . ASP A 1 3862 ? 165.069 197.692 252.484 1.00 3.24  ? 3862 ASP A CA    1 
ATOM   17600 C  C     . ASP A 1 3862 ? 166.439 197.674 251.813 1.00 3.67  ? 3862 ASP A C     1 
ATOM   17601 O  O     . ASP A 1 3862 ? 166.562 198.030 250.636 1.00 4.76  ? 3862 ASP A O     1 
ATOM   17602 C  CB    . ASP A 1 3862 ? 164.738 199.077 253.048 1.00 6.33  ? 3862 ASP A CB    1 
ATOM   17603 C  CG    . ASP A 1 3862 ? 164.547 200.130 251.971 1.00 23.33 ? 3862 ASP A CG    1 
ATOM   17604 O  OD1   . ASP A 1 3862 ? 164.690 199.818 250.778 1.00 21.22 ? 3862 ASP A OD1   1 
ATOM   17605 O  OD2   . ASP A 1 3862 ? 164.241 201.285 252.324 1.00 21.89 ? 3862 ASP A OD2   1 
ATOM   17606 N  N     . LEU A 1 3863 ? 167.476 197.241 252.539 1.00 5.19  ? 3863 LEU A N     1 
ATOM   17607 C  CA    . LEU A 1 3863 ? 168.805 197.123 251.948 1.00 1.88  ? 3863 LEU A CA    1 
ATOM   17608 C  C     . LEU A 1 3863 ? 168.809 196.134 250.791 1.00 1.59  ? 3863 LEU A C     1 
ATOM   17609 O  O     . LEU A 1 3863 ? 169.407 196.397 249.741 1.00 2.50  ? 3863 LEU A O     1 
ATOM   17610 C  CB    . LEU A 1 3863 ? 169.816 196.699 253.013 1.00 1.99  ? 3863 LEU A CB    1 
ATOM   17611 C  CG    . LEU A 1 3863 ? 171.232 196.382 252.525 1.00 3.79  ? 3863 LEU A CG    1 
ATOM   17612 C  CD1   . LEU A 1 3863 ? 171.940 197.637 252.045 1.00 1.35  ? 3863 LEU A CD1   1 
ATOM   17613 C  CD2   . LEU A 1 3863 ? 172.038 195.684 253.608 1.00 1.82  ? 3863 LEU A CD2   1 
ATOM   17614 N  N     . PHE A 1 3864 ? 168.152 194.988 250.965 1.00 1.71  ? 3864 PHE A N     1 
ATOM   17615 C  CA    . PHE A 1 3864 ? 168.071 194.012 249.885 1.00 1.98  ? 3864 PHE A CA    1 
ATOM   17616 C  C     . PHE A 1 3864 ? 167.244 194.541 248.722 1.00 0.97  ? 3864 PHE A C     1 
ATOM   17617 O  O     . PHE A 1 3864 ? 167.552 194.264 247.557 1.00 0.35  ? 3864 PHE A O     1 
ATOM   17618 C  CB    . PHE A 1 3864 ? 167.488 192.700 250.408 1.00 1.18  ? 3864 PHE A CB    1 
ATOM   17619 C  CG    . PHE A 1 3864 ? 168.479 191.843 251.137 1.00 0.94  ? 3864 PHE A CG    1 
ATOM   17620 C  CD1   . PHE A 1 3864 ? 169.279 190.951 250.447 1.00 1.59  ? 3864 PHE A CD1   1 
ATOM   17621 C  CD2   . PHE A 1 3864 ? 168.611 191.928 252.512 1.00 1.00  ? 3864 PHE A CD2   1 
ATOM   17622 C  CE1   . PHE A 1 3864 ? 170.195 190.160 251.116 1.00 2.89  ? 3864 PHE A CE1   1 
ATOM   17623 C  CE2   . PHE A 1 3864 ? 169.525 191.142 253.185 1.00 1.14  ? 3864 PHE A CE2   1 
ATOM   17624 C  CZ    . PHE A 1 3864 ? 170.316 190.257 252.486 1.00 1.70  ? 3864 PHE A CZ    1 
ATOM   17625 N  N     . GLN A 1 3865 ? 166.189 195.305 249.017 1.00 0.97  ? 3865 GLN A N     1 
ATOM   17626 C  CA    . GLN A 1 3865 ? 165.295 195.780 247.968 1.00 0.65  ? 3865 GLN A CA    1 
ATOM   17627 C  C     . GLN A 1 3865 ? 165.966 196.840 247.100 1.00 0.55  ? 3865 GLN A C     1 
ATOM   17628 O  O     . GLN A 1 3865 ? 165.904 196.773 245.868 1.00 0.58  ? 3865 GLN A O     1 
ATOM   17629 C  CB    . GLN A 1 3865 ? 164.007 196.325 248.587 1.00 0.77  ? 3865 GLN A CB    1 
ATOM   17630 C  CG    . GLN A 1 3865 ? 162.944 196.686 247.568 1.00 1.37  ? 3865 GLN A CG    1 
ATOM   17631 C  CD    . GLN A 1 3865 ? 162.392 195.471 246.850 1.00 0.98  ? 3865 GLN A CD    1 
ATOM   17632 O  OE1   . GLN A 1 3865 ? 161.610 194.709 247.411 1.00 2.53  ? 3865 GLN A OE1   1 
ATOM   17633 N  NE2   . GLN A 1 3865 ? 162.811 195.276 245.608 1.00 0.60  ? 3865 GLN A NE2   1 
ATOM   17634 N  N     . VAL A 1 3866 ? 166.610 197.828 247.723 1.00 0.45  ? 3866 VAL A N     1 
ATOM   17635 C  CA    . VAL A 1 3866 ? 167.268 198.879 246.953 1.00 0.59  ? 3866 VAL A CA    1 
ATOM   17636 C  C     . VAL A 1 3866 ? 168.461 198.317 246.192 1.00 0.43  ? 3866 VAL A C     1 
ATOM   17637 O  O     . VAL A 1 3866 ? 168.749 198.737 245.065 1.00 0.55  ? 3866 VAL A O     1 
ATOM   17638 C  CB    . VAL A 1 3866 ? 167.670 200.052 247.864 1.00 1.67  ? 3866 VAL A CB    1 
ATOM   17639 C  CG1   . VAL A 1 3866 ? 168.436 201.100 247.080 1.00 1.39  ? 3866 VAL A CG1   1 
ATOM   17640 C  CG2   . VAL A 1 3866 ? 166.440 200.680 248.466 1.00 1.19  ? 3866 VAL A CG2   1 
ATOM   17641 N  N     . ALA A 1 3867 ? 169.171 197.357 246.790 1.00 0.36  ? 3867 ALA A N     1 
ATOM   17642 C  CA    . ALA A 1 3867 ? 170.294 196.740 246.096 1.00 0.37  ? 3867 ALA A CA    1 
ATOM   17643 C  C     . ALA A 1 3867 ? 169.839 196.067 244.809 1.00 0.47  ? 3867 ALA A C     1 
ATOM   17644 O  O     . ALA A 1 3867 ? 170.491 196.201 243.768 1.00 1.02  ? 3867 ALA A O     1 
ATOM   17645 C  CB    . ALA A 1 3867 ? 170.995 195.736 247.011 1.00 0.38  ? 3867 ALA A CB    1 
ATOM   17646 N  N     . PHE A 1 3868 ? 168.718 195.347 244.857 1.00 0.26  ? 3868 PHE A N     1 
ATOM   17647 C  CA    . PHE A 1 3868 ? 168.205 194.731 243.640 1.00 0.22  ? 3868 PHE A CA    1 
ATOM   17648 C  C     . PHE A 1 3868 ? 167.706 195.780 242.655 1.00 0.29  ? 3868 PHE A C     1 
ATOM   17649 O  O     . PHE A 1 3868 ? 167.944 195.663 241.450 1.00 0.49  ? 3868 PHE A O     1 
ATOM   17650 C  CB    . PHE A 1 3868 ? 167.090 193.740 243.970 1.00 0.24  ? 3868 PHE A CB    1 
ATOM   17651 C  CG    . PHE A 1 3868 ? 166.522 193.055 242.760 1.00 0.21  ? 3868 PHE A CG    1 
ATOM   17652 C  CD1   . PHE A 1 3868 ? 167.204 192.014 242.154 1.00 0.26  ? 3868 PHE A CD1   1 
ATOM   17653 C  CD2   . PHE A 1 3868 ? 165.316 193.461 242.217 1.00 0.17  ? 3868 PHE A CD2   1 
ATOM   17654 C  CE1   . PHE A 1 3868 ? 166.693 191.387 241.039 1.00 0.50  ? 3868 PHE A CE1   1 
ATOM   17655 C  CE2   . PHE A 1 3868 ? 164.798 192.836 241.101 1.00 0.39  ? 3868 PHE A CE2   1 
ATOM   17656 C  CZ    . PHE A 1 3868 ? 165.485 191.798 240.513 1.00 0.67  ? 3868 PHE A CZ    1 
ATOM   17657 N  N     . ASN A 1 3869 ? 167.017 196.809 243.148 1.00 0.26  ? 3869 ASN A N     1 
ATOM   17658 C  CA    . ASN A 1 3869 ? 166.404 197.788 242.258 1.00 0.36  ? 3869 ASN A CA    1 
ATOM   17659 C  C     . ASN A 1 3869 ? 167.454 198.547 241.457 1.00 1.23  ? 3869 ASN A C     1 
ATOM   17660 O  O     . ASN A 1 3869 ? 167.336 198.687 240.234 1.00 3.71  ? 3869 ASN A O     1 
ATOM   17661 C  CB    . ASN A 1 3869 ? 165.531 198.752 243.060 1.00 0.46  ? 3869 ASN A CB    1 
ATOM   17662 C  CG    . ASN A 1 3869 ? 164.223 198.124 243.497 1.00 1.17  ? 3869 ASN A CG    1 
ATOM   17663 O  OD1   . ASN A 1 3869 ? 163.896 197.007 243.104 1.00 2.15  ? 3869 ASN A OD1   1 
ATOM   17664 N  ND2   . ASN A 1 3869 ? 163.467 198.842 244.318 1.00 2.27  ? 3869 ASN A ND2   1 
ATOM   17665 N  N     . ARG A 1 3870 ? 168.499 199.034 242.124 1.00 0.73  ? 3870 ARG A N     1 
ATOM   17666 C  CA    . ARG A 1 3870 ? 169.489 199.843 241.424 1.00 0.67  ? 3870 ARG A CA    1 
ATOM   17667 C  C     . ARG A 1 3870 ? 170.406 198.996 240.547 1.00 0.59  ? 3870 ARG A C     1 
ATOM   17668 O  O     . ARG A 1 3870 ? 170.772 199.418 239.445 1.00 2.66  ? 3870 ARG A O     1 
ATOM   17669 C  CB    . ARG A 1 3870 ? 170.300 200.659 242.428 1.00 1.05  ? 3870 ARG A CB    1 
ATOM   17670 C  CG    . ARG A 1 3870 ? 169.447 201.575 243.288 1.00 1.16  ? 3870 ARG A CG    1 
ATOM   17671 C  CD    . ARG A 1 3870 ? 170.277 202.662 243.932 1.00 1.95  ? 3870 ARG A CD    1 
ATOM   17672 N  NE    . ARG A 1 3870 ? 169.463 203.601 244.692 1.00 6.94  ? 3870 ARG A NE    1 
ATOM   17673 C  CZ    . ARG A 1 3870 ? 169.938 204.678 245.301 1.00 5.89  ? 3870 ARG A CZ    1 
ATOM   17674 N  NH1   . ARG A 1 3870 ? 171.223 204.980 245.263 1.00 3.93  ? 3870 ARG A NH1   1 
ATOM   17675 N  NH2   . ARG A 1 3870 ? 169.099 205.474 245.956 1.00 7.59  ? 3870 ARG A NH2   1 
ATOM   17676 N  N     . VAL A 1 3871 ? 170.788 197.806 241.012 1.00 0.38  ? 3871 VAL A N     1 
ATOM   17677 C  CA    . VAL A 1 3871 ? 171.681 196.965 240.219 1.00 0.48  ? 3871 VAL A CA    1 
ATOM   17678 C  C     . VAL A 1 3871 ? 170.960 196.407 238.996 1.00 0.38  ? 3871 VAL A C     1 
ATOM   17679 O  O     . VAL A 1 3871 ? 171.505 196.409 237.886 1.00 0.45  ? 3871 VAL A O     1 
ATOM   17680 C  CB    . VAL A 1 3871 ? 172.279 195.847 241.092 1.00 0.32  ? 3871 VAL A CB    1 
ATOM   17681 C  CG1   . VAL A 1 3871 ? 172.978 194.812 240.231 1.00 0.49  ? 3871 VAL A CG1   1 
ATOM   17682 C  CG2   . VAL A 1 3871 ? 173.247 196.426 242.107 1.00 0.20  ? 3871 VAL A CG2   1 
ATOM   17683 N  N     . ALA A 1 3872 ? 169.723 195.931 239.172 1.00 0.32  ? 3872 ALA A N     1 
ATOM   17684 C  CA    . ALA A 1 3872 ? 169.010 195.277 238.078 1.00 0.28  ? 3872 ALA A CA    1 
ATOM   17685 C  C     . ALA A 1 3872 ? 168.599 196.245 236.977 1.00 0.36  ? 3872 ALA A C     1 
ATOM   17686 O  O     . ALA A 1 3872 ? 168.405 195.814 235.837 1.00 0.25  ? 3872 ALA A O     1 
ATOM   17687 C  CB    . ALA A 1 3872 ? 167.775 194.543 238.604 1.00 0.35  ? 3872 ALA A CB    1 
ATOM   17688 N  N     . ARG A 1 3873 ? 168.460 197.538 237.282 1.00 0.90  ? 3873 ARG A N     1 
ATOM   17689 C  CA    . ARG A 1 3873 ? 168.189 198.504 236.227 1.00 0.72  ? 3873 ARG A CA    1 
ATOM   17690 C  C     . ARG A 1 3873 ? 169.347 198.579 235.242 1.00 0.47  ? 3873 ARG A C     1 
ATOM   17691 O  O     . ARG A 1 3873 ? 169.161 198.982 234.089 1.00 0.59  ? 3873 ARG A O     1 
ATOM   17692 C  CB    . ARG A 1 3873 ? 167.909 199.882 236.823 1.00 1.49  ? 3873 ARG A CB    1 
ATOM   17693 C  CG    . ARG A 1 3873 ? 166.561 200.007 237.505 1.00 2.93  ? 3873 ARG A CG    1 
ATOM   17694 C  CD    . ARG A 1 3873 ? 165.415 199.575 236.612 1.00 4.18  ? 3873 ARG A CD    1 
ATOM   17695 N  NE    . ARG A 1 3873 ? 164.135 200.050 237.126 1.00 7.41  ? 3873 ARG A NE    1 
ATOM   17696 C  CZ    . ARG A 1 3873 ? 162.957 199.777 236.585 1.00 6.50  ? 3873 ARG A CZ    1 
ATOM   17697 N  NH1   . ARG A 1 3873 ? 162.850 199.014 235.511 1.00 5.32  ? 3873 ARG A NH1   1 
ATOM   17698 N  NH2   . ARG A 1 3873 ? 161.858 200.281 237.137 1.00 8.38  ? 3873 ARG A NH2   1 
ATOM   17699 N  N     . GLY A 1 3874 ? 170.542 198.192 235.678 1.00 0.21  ? 3874 GLY A N     1 
ATOM   17700 C  CA    . GLY A 1 3874 ? 171.694 198.122 234.806 1.00 0.22  ? 3874 GLY A CA    1 
ATOM   17701 C  C     . GLY A 1 3874 ? 172.080 196.711 234.425 1.00 0.24  ? 3874 GLY A C     1 
ATOM   17702 O  O     . GLY A 1 3874 ? 173.220 196.461 234.029 1.00 0.42  ? 3874 GLY A O     1 
ATOM   17703 N  N     . MET A 1 3875 ? 171.143 195.775 234.537 1.00 0.41  ? 3875 MET A N     1 
ATOM   17704 C  CA    . MET A 1 3875 ? 171.371 194.395 234.137 1.00 0.39  ? 3875 MET A CA    1 
ATOM   17705 C  C     . MET A 1 3875 ? 170.395 194.016 233.037 1.00 0.36  ? 3875 MET A C     1 
ATOM   17706 O  O     . MET A 1 3875 ? 169.312 194.594 232.918 1.00 0.87  ? 3875 MET A O     1 
ATOM   17707 C  CB    . MET A 1 3875 ? 171.213 193.408 235.307 1.00 0.45  ? 3875 MET A CB    1 
ATOM   17708 C  CG    . MET A 1 3875 ? 172.255 193.535 236.397 1.00 0.55  ? 3875 MET A CG    1 
ATOM   17709 S  SD    . MET A 1 3875 ? 171.964 192.405 237.776 1.00 7.22  ? 3875 MET A SD    1 
ATOM   17710 C  CE    . MET A 1 3875 ? 172.358 190.831 237.034 1.00 1.00  ? 3875 MET A CE    1 
ATOM   17711 N  N     . LEU A 1 3876 ? 170.802 193.051 232.220 1.00 0.47  ? 3876 LEU A N     1 
ATOM   17712 C  CA    . LEU A 1 3876 ? 169.873 192.413 231.303 1.00 0.68  ? 3876 LEU A CA    1 
ATOM   17713 C  C     . LEU A 1 3876 ? 168.810 191.665 232.094 1.00 0.99  ? 3876 LEU A C     1 
ATOM   17714 O  O     . LEU A 1 3876 ? 169.097 191.065 233.133 1.00 2.95  ? 3876 LEU A O     1 
ATOM   17715 C  CB    . LEU A 1 3876 ? 170.614 191.457 230.371 1.00 1.32  ? 3876 LEU A CB    1 
ATOM   17716 C  CG    . LEU A 1 3876 ? 171.607 192.102 229.401 1.00 1.21  ? 3876 LEU A CG    1 
ATOM   17717 C  CD1   . LEU A 1 3876 ? 172.370 191.040 228.630 1.00 2.11  ? 3876 LEU A CD1   1 
ATOM   17718 C  CD2   . LEU A 1 3876 ? 170.894 193.051 228.454 1.00 0.69  ? 3876 LEU A CD2   1 
ATOM   17719 N  N     . HIS A 1 3877 ? 167.571 191.708 231.599 1.00 1.17  ? 3877 HIS A N     1 
ATOM   17720 C  CA    . HIS A 1 3877 ? 166.458 191.119 232.338 1.00 1.20  ? 3877 HIS A CA    1 
ATOM   17721 C  C     . HIS A 1 3877 ? 166.657 189.628 232.575 1.00 1.36  ? 3877 HIS A C     1 
ATOM   17722 O  O     . HIS A 1 3877 ? 166.181 189.093 233.582 1.00 1.80  ? 3877 HIS A O     1 
ATOM   17723 C  CB    . HIS A 1 3877 ? 165.150 191.369 231.589 1.00 0.92  ? 3877 HIS A CB    1 
ATOM   17724 C  CG    . HIS A 1 3877 ? 163.929 190.979 232.360 1.00 1.45  ? 3877 HIS A CG    1 
ATOM   17725 N  ND1   . HIS A 1 3877 ? 163.357 189.731 232.265 1.00 1.38  ? 3877 HIS A ND1   1 
ATOM   17726 C  CD2   . HIS A 1 3877 ? 163.171 191.675 233.239 1.00 4.45  ? 3877 HIS A CD2   1 
ATOM   17727 C  CE1   . HIS A 1 3877 ? 162.299 189.672 233.053 1.00 2.25  ? 3877 HIS A CE1   1 
ATOM   17728 N  NE2   . HIS A 1 3877 ? 162.163 190.840 233.654 1.00 7.03  ? 3877 HIS A NE2   1 
ATOM   17729 N  N     . GLN A 1 3878 ? 167.362 188.946 231.669 1.00 1.31  ? 3878 GLN A N     1 
ATOM   17730 C  CA    . GLN A 1 3878 ? 167.616 187.521 231.841 1.00 1.78  ? 3878 GLN A CA    1 
ATOM   17731 C  C     . GLN A 1 3878 ? 168.474 187.241 233.069 1.00 3.65  ? 3878 GLN A C     1 
ATOM   17732 O  O     . GLN A 1 3878 ? 168.401 186.147 233.639 1.00 6.22  ? 3878 GLN A O     1 
ATOM   17733 C  CB    . GLN A 1 3878 ? 168.282 186.956 230.587 1.00 3.86  ? 3878 GLN A CB    1 
ATOM   17734 C  CG    . GLN A 1 3878 ? 169.744 187.330 230.440 1.00 7.62  ? 3878 GLN A CG    1 
ATOM   17735 C  CD    . GLN A 1 3878 ? 170.294 187.006 229.071 1.00 13.16 ? 3878 GLN A CD    1 
ATOM   17736 O  OE1   . GLN A 1 3878 ? 171.307 186.317 228.942 1.00 18.64 ? 3878 GLN A OE1   1 
ATOM   17737 N  NE2   . GLN A 1 3878 ? 169.628 187.499 228.034 1.00 13.55 ? 3878 GLN A NE2   1 
ATOM   17738 N  N     . ASP A 1 3879 ? 169.286 188.205 233.491 1.00 3.28  ? 3879 ASP A N     1 
ATOM   17739 C  CA    . ASP A 1 3879 ? 170.146 188.037 234.652 1.00 2.17  ? 3879 ASP A CA    1 
ATOM   17740 C  C     . ASP A 1 3879 ? 169.507 188.524 235.947 1.00 1.22  ? 3879 ASP A C     1 
ATOM   17741 O  O     . ASP A 1 3879 ? 170.128 188.405 237.006 1.00 1.84  ? 3879 ASP A O     1 
ATOM   17742 C  CB    . ASP A 1 3879 ? 171.477 188.759 234.430 1.00 1.76  ? 3879 ASP A CB    1 
ATOM   17743 C  CG    . ASP A 1 3879 ? 172.272 188.184 233.278 1.00 6.16  ? 3879 ASP A CG    1 
ATOM   17744 O  OD1   . ASP A 1 3879 ? 172.535 186.966 233.285 1.00 10.65 ? 3879 ASP A OD1   1 
ATOM   17745 O  OD2   . ASP A 1 3879 ? 172.649 188.955 232.372 1.00 8.37  ? 3879 ASP A OD2   1 
ATOM   17746 N  N     . HIS A 1 3880 ? 168.288 189.066 235.888 1.00 1.14  ? 3880 HIS A N     1 
ATOM   17747 C  CA    . HIS A 1 3880 ? 167.642 189.573 237.096 1.00 0.90  ? 3880 HIS A CA    1 
ATOM   17748 C  C     . HIS A 1 3880 ? 167.382 188.457 238.098 1.00 1.19  ? 3880 HIS A C     1 
ATOM   17749 O  O     . HIS A 1 3880 ? 167.562 188.645 239.307 1.00 1.60  ? 3880 HIS A O     1 
ATOM   17750 C  CB    . HIS A 1 3880 ? 166.336 190.281 236.737 1.00 0.63  ? 3880 HIS A CB    1 
ATOM   17751 C  CG    . HIS A 1 3880 ? 166.531 191.594 236.046 1.00 1.03  ? 3880 HIS A CG    1 
ATOM   17752 N  ND1   . HIS A 1 3880 ? 165.488 192.453 235.778 1.00 0.58  ? 3880 HIS A ND1   1 
ATOM   17753 C  CD2   . HIS A 1 3880 ? 167.645 192.195 235.571 1.00 0.46  ? 3880 HIS A CD2   1 
ATOM   17754 C  CE1   . HIS A 1 3880 ? 165.951 193.527 235.165 1.00 0.33  ? 3880 HIS A CE1   1 
ATOM   17755 N  NE2   . HIS A 1 3880 ? 167.258 193.394 235.027 1.00 0.51  ? 3880 HIS A NE2   1 
ATOM   17756 N  N     . ILE A 1 3881 ? 166.954 187.289 237.617 1.00 2.27  ? 3881 ILE A N     1 
ATOM   17757 C  CA    . ILE A 1 3881 ? 166.683 186.175 238.517 1.00 1.31  ? 3881 ILE A CA    1 
ATOM   17758 C  C     . ILE A 1 3881 ? 167.965 185.691 239.178 1.00 1.28  ? 3881 ILE A C     1 
ATOM   17759 O  O     . ILE A 1 3881 ? 167.950 185.272 240.340 1.00 1.44  ? 3881 ILE A O     1 
ATOM   17760 C  CB    . ILE A 1 3881 ? 165.953 185.042 237.764 1.00 1.17  ? 3881 ILE A CB    1 
ATOM   17761 C  CG1   . ILE A 1 3881 ? 165.471 183.966 238.742 1.00 3.08  ? 3881 ILE A CG1   1 
ATOM   17762 C  CG2   . ILE A 1 3881 ? 166.834 184.445 236.673 1.00 1.17  ? 3881 ILE A CG2   1 
ATOM   17763 C  CD1   . ILE A 1 3881 ? 164.579 184.491 239.839 1.00 0.92  ? 3881 ILE A CD1   1 
ATOM   17764 N  N     . THR A 1 3882 ? 169.093 185.746 238.465 1.00 1.26  ? 3882 THR A N     1 
ATOM   17765 C  CA    . THR A 1 3882 ? 170.356 185.286 239.029 1.00 2.08  ? 3882 THR A CA    1 
ATOM   17766 C  C     . THR A 1 3882 ? 170.774 186.140 240.220 1.00 1.25  ? 3882 THR A C     1 
ATOM   17767 O  O     . THR A 1 3882 ? 171.174 185.615 241.264 1.00 2.68  ? 3882 THR A O     1 
ATOM   17768 C  CB    . THR A 1 3882 ? 171.441 185.293 237.954 1.00 3.01  ? 3882 THR A CB    1 
ATOM   17769 O  OG1   . THR A 1 3882 ? 170.983 184.564 236.809 1.00 6.09  ? 3882 THR A OG1   1 
ATOM   17770 C  CG2   . THR A 1 3882 ? 172.711 184.650 238.476 1.00 2.14  ? 3882 THR A CG2   1 
ATOM   17771 N  N     . PHE A 1 3883 ? 170.691 187.465 240.079 1.00 1.10  ? 3883 PHE A N     1 
ATOM   17772 C  CA    . PHE A 1 3883 ? 171.035 188.350 241.187 1.00 0.78  ? 3883 PHE A CA    1 
ATOM   17773 C  C     . PHE A 1 3883 ? 170.051 188.207 242.343 1.00 0.68  ? 3883 PHE A C     1 
ATOM   17774 O  O     . PHE A 1 3883 ? 170.457 188.191 243.510 1.00 0.75  ? 3883 PHE A O     1 
ATOM   17775 C  CB    . PHE A 1 3883 ? 171.095 189.800 240.708 1.00 0.45  ? 3883 PHE A CB    1 
ATOM   17776 C  CG    . PHE A 1 3883 ? 171.613 190.757 241.740 1.00 0.29  ? 3883 PHE A CG    1 
ATOM   17777 C  CD1   . PHE A 1 3883 ? 172.678 190.412 242.551 1.00 0.35  ? 3883 PHE A CD1   1 
ATOM   17778 C  CD2   . PHE A 1 3883 ? 171.025 191.996 241.911 1.00 0.35  ? 3883 PHE A CD2   1 
ATOM   17779 C  CE1   . PHE A 1 3883 ? 173.151 191.287 243.507 1.00 0.40  ? 3883 PHE A CE1   1 
ATOM   17780 C  CE2   . PHE A 1 3883 ? 171.495 192.875 242.865 1.00 0.25  ? 3883 PHE A CE2   1 
ATOM   17781 C  CZ    . PHE A 1 3883 ? 172.559 192.520 243.663 1.00 0.22  ? 3883 PHE A CZ    1 
ATOM   17782 N  N     . ALA A 1 3884 ? 168.756 188.109 242.039 1.00 0.96  ? 3884 ALA A N     1 
ATOM   17783 C  CA    . ALA A 1 3884 ? 167.762 187.922 243.091 1.00 0.62  ? 3884 ALA A CA    1 
ATOM   17784 C  C     . ALA A 1 3884 ? 167.926 186.578 243.786 1.00 0.91  ? 3884 ALA A C     1 
ATOM   17785 O  O     . ALA A 1 3884 ? 167.649 186.465 244.984 1.00 0.84  ? 3884 ALA A O     1 
ATOM   17786 C  CB    . ALA A 1 3884 ? 166.354 188.060 242.517 1.00 0.59  ? 3884 ALA A CB    1 
ATOM   17787 N  N     . MET A 1 3885 ? 168.369 185.553 243.053 1.00 0.71  ? 3885 MET A N     1 
ATOM   17788 C  CA    . MET A 1 3885 ? 168.629 184.254 243.662 1.00 0.83  ? 3885 MET A CA    1 
ATOM   17789 C  C     . MET A 1 3885 ? 169.735 184.354 244.705 1.00 1.76  ? 3885 MET A C     1 
ATOM   17790 O  O     . MET A 1 3885 ? 169.657 183.735 245.772 1.00 2.05  ? 3885 MET A O     1 
ATOM   17791 C  CB    . MET A 1 3885 ? 169.011 183.238 242.586 1.00 3.43  ? 3885 MET A CB    1 
ATOM   17792 C  CG    . MET A 1 3885 ? 167.844 182.514 241.934 1.00 1.92  ? 3885 MET A CG    1 
ATOM   17793 S  SD    . MET A 1 3885 ? 166.781 181.636 243.087 1.00 16.65 ? 3885 MET A SD    1 
ATOM   17794 C  CE    . MET A 1 3885 ? 167.571 180.030 243.114 1.00 11.80 ? 3885 MET A CE    1 
ATOM   17795 N  N     . LEU A 1 3886 ? 170.780 185.130 244.408 1.00 1.30  ? 3886 LEU A N     1 
ATOM   17796 C  CA    . LEU A 1 3886 ? 171.893 185.272 245.338 1.00 1.05  ? 3886 LEU A CA    1 
ATOM   17797 C  C     . LEU A 1 3886 ? 171.509 186.120 246.542 1.00 1.42  ? 3886 LEU A C     1 
ATOM   17798 O  O     . LEU A 1 3886 ? 171.903 185.813 247.674 1.00 5.14  ? 3886 LEU A O     1 
ATOM   17799 C  CB    . LEU A 1 3886 ? 173.097 185.874 244.619 1.00 1.12  ? 3886 LEU A CB    1 
ATOM   17800 C  CG    . LEU A 1 3886 ? 173.644 185.050 243.453 1.00 1.45  ? 3886 LEU A CG    1 
ATOM   17801 C  CD1   . LEU A 1 3886 ? 174.567 185.898 242.604 1.00 1.59  ? 3886 LEU A CD1   1 
ATOM   17802 C  CD2   . LEU A 1 3886 ? 174.357 183.807 243.956 1.00 1.36  ? 3886 LEU A CD2   1 
ATOM   17803 N  N     . LEU A 1 3887 ? 170.743 187.192 246.324 1.00 0.86  ? 3887 LEU A N     1 
ATOM   17804 C  CA    . LEU A 1 3887 ? 170.295 188.012 247.446 1.00 1.39  ? 3887 LEU A CA    1 
ATOM   17805 C  C     . LEU A 1 3887 ? 169.409 187.206 248.386 1.00 1.84  ? 3887 LEU A C     1 
ATOM   17806 O  O     . LEU A 1 3887 ? 169.458 187.388 249.606 1.00 3.42  ? 3887 LEU A O     1 
ATOM   17807 C  CB    . LEU A 1 3887 ? 169.555 189.250 246.938 1.00 1.35  ? 3887 LEU A CB    1 
ATOM   17808 C  CG    . LEU A 1 3887 ? 170.356 190.266 246.124 1.00 1.07  ? 3887 LEU A CG    1 
ATOM   17809 C  CD1   . LEU A 1 3887 ? 169.466 191.423 245.698 1.00 0.35  ? 3887 LEU A CD1   1 
ATOM   17810 C  CD2   . LEU A 1 3887 ? 171.563 190.769 246.901 1.00 0.51  ? 3887 LEU A CD2   1 
ATOM   17811 N  N     . ALA A 1 3888 ? 168.590 186.311 247.829 1.00 2.17  ? 3888 ALA A N     1 
ATOM   17812 C  CA    . ALA A 1 3888 ? 167.790 185.420 248.661 1.00 2.50  ? 3888 ALA A CA    1 
ATOM   17813 C  C     . ALA A 1 3888 ? 168.673 184.490 249.480 1.00 3.16  ? 3888 ALA A C     1 
ATOM   17814 O  O     . ALA A 1 3888 ? 168.398 184.238 250.659 1.00 5.87  ? 3888 ALA A O     1 
ATOM   17815 C  CB    . ALA A 1 3888 ? 166.825 184.619 247.788 1.00 2.93  ? 3888 ALA A CB    1 
ATOM   17816 N  N     . ARG A 1 3889 ? 169.740 183.966 248.875 1.00 3.44  ? 3889 ARG A N     1 
ATOM   17817 C  CA    . ARG A 1 3889 ? 170.643 183.078 249.599 1.00 3.07  ? 3889 ARG A CA    1 
ATOM   17818 C  C     . ARG A 1 3889 ? 171.392 183.824 250.697 1.00 5.54  ? 3889 ARG A C     1 
ATOM   17819 O  O     . ARG A 1 3889 ? 171.658 183.261 251.763 1.00 12.10 ? 3889 ARG A O     1 
ATOM   17820 C  CB    . ARG A 1 3889 ? 171.620 182.419 248.627 1.00 4.44  ? 3889 ARG A CB    1 
ATOM   17821 C  CG    . ARG A 1 3889 ? 170.960 181.442 247.670 1.00 3.83  ? 3889 ARG A CG    1 
ATOM   17822 C  CD    . ARG A 1 3889 ? 171.839 180.240 247.398 1.00 3.81  ? 3889 ARG A CD    1 
ATOM   17823 N  NE    . ARG A 1 3889 ? 172.365 179.657 248.625 1.00 8.69  ? 3889 ARG A NE    1 
ATOM   17824 C  CZ    . ARG A 1 3889 ? 173.435 178.877 248.683 1.00 9.13  ? 3889 ARG A CZ    1 
ATOM   17825 N  NH1   . ARG A 1 3889 ? 174.130 178.575 247.598 1.00 5.19  ? 3889 ARG A NH1   1 
ATOM   17826 N  NH2   . ARG A 1 3889 ? 173.815 178.385 249.859 1.00 11.56 ? 3889 ARG A NH2   1 
ATOM   17827 N  N     . ILE A 1 3890 ? 171.751 185.086 250.449 1.00 3.33  ? 3890 ILE A N     1 
ATOM   17828 C  CA    . ILE A 1 3890 ? 172.355 185.904 251.496 1.00 2.97  ? 3890 ILE A CA    1 
ATOM   17829 C  C     . ILE A 1 3890 ? 171.363 186.145 252.625 1.00 4.24  ? 3890 ILE A C     1 
ATOM   17830 O  O     . ILE A 1 3890 ? 171.709 186.039 253.807 1.00 9.23  ? 3890 ILE A O     1 
ATOM   17831 C  CB    . ILE A 1 3890 ? 172.879 187.227 250.907 1.00 2.54  ? 3890 ILE A CB    1 
ATOM   17832 C  CG1   . ILE A 1 3890 ? 173.998 186.962 249.903 1.00 1.32  ? 3890 ILE A CG1   1 
ATOM   17833 C  CG2   . ILE A 1 3890 ? 173.365 188.153 252.009 1.00 2.00  ? 3890 ILE A CG2   1 
ATOM   17834 C  CD1   . ILE A 1 3890 ? 174.487 188.206 249.204 1.00 1.44  ? 3890 ILE A CD1   1 
ATOM   17835 N  N     . LYS A 1 3891 ? 170.114 186.474 252.285 1.00 3.66  ? 3891 LYS A N     1 
ATOM   17836 C  CA    . LYS A 1 3891 ? 169.098 186.690 253.311 1.00 3.54  ? 3891 LYS A CA    1 
ATOM   17837 C  C     . LYS A 1 3891 ? 168.798 185.412 254.081 1.00 8.81  ? 3891 LYS A C     1 
ATOM   17838 O  O     . LYS A 1 3891 ? 168.513 185.467 255.283 1.00 6.04  ? 3891 LYS A O     1 
ATOM   17839 C  CB    . LYS A 1 3891 ? 167.818 187.238 252.683 1.00 3.80  ? 3891 LYS A CB    1 
ATOM   17840 C  CG    . LYS A 1 3891 ? 166.862 187.863 253.686 1.00 3.36  ? 3891 LYS A CG    1 
ATOM   17841 C  CD    . LYS A 1 3891 ? 165.430 187.810 253.190 1.00 6.76  ? 3891 LYS A CD    1 
ATOM   17842 C  CE    . LYS A 1 3891 ? 164.476 188.455 254.182 1.00 9.23  ? 3891 LYS A CE    1 
ATOM   17843 N  NZ    . LYS A 1 3891 ? 163.165 188.782 253.556 1.00 9.56  ? 3891 LYS A NZ    1 
ATOM   17844 N  N     . LEU A 1 3892 ? 168.849 184.263 253.407 1.00 7.83  ? 3892 LEU A N     1 
ATOM   17845 C  CA    . LEU A 1 3892 ? 168.608 182.992 254.080 1.00 9.03  ? 3892 LEU A CA    1 
ATOM   17846 C  C     . LEU A 1 3892 ? 169.662 182.724 255.147 1.00 12.64 ? 3892 LEU A C     1 
ATOM   17847 O  O     . LEU A 1 3892 ? 169.343 182.227 256.233 1.00 18.84 ? 3892 LEU A O     1 
ATOM   17848 C  CB    . LEU A 1 3892 ? 168.576 181.864 253.049 1.00 10.91 ? 3892 LEU A CB    1 
ATOM   17849 C  CG    . LEU A 1 3892 ? 168.186 180.469 253.529 1.00 11.09 ? 3892 LEU A CG    1 
ATOM   17850 C  CD1   . LEU A 1 3892 ? 166.929 180.531 254.374 1.00 10.28 ? 3892 LEU A CD1   1 
ATOM   17851 C  CD2   . LEU A 1 3892 ? 167.987 179.557 252.334 1.00 11.23 ? 3892 LEU A CD2   1 
ATOM   17852 N  N     . LYS A 1 3893 ? 170.924 183.053 254.855 1.00 10.53 ? 3893 LYS A N     1 
ATOM   17853 C  CA    . LYS A 1 3893 ? 171.986 182.891 255.844 1.00 8.91  ? 3893 LYS A CA    1 
ATOM   17854 C  C     . LYS A 1 3893 ? 171.764 183.771 257.067 1.00 13.92 ? 3893 LYS A C     1 
ATOM   17855 O  O     . LYS A 1 3893 ? 172.207 183.425 258.167 1.00 25.43 ? 3893 LYS A O     1 
ATOM   17856 C  CB    . LYS A 1 3893 ? 173.340 183.202 255.208 1.00 11.48 ? 3893 LYS A CB    1 
ATOM   17857 C  CG    . LYS A 1 3893 ? 173.874 182.100 254.310 1.00 11.61 ? 3893 LYS A CG    1 
ATOM   17858 C  CD    . LYS A 1 3893 ? 175.284 182.408 253.851 1.00 10.27 ? 3893 LYS A CD    1 
ATOM   17859 C  CE    . LYS A 1 3893 ? 176.209 182.664 255.026 1.00 10.25 ? 3893 LYS A CE    1 
ATOM   17860 N  NZ    . LYS A 1 3893 ? 177.612 182.889 254.584 1.00 19.11 ? 3893 LYS A NZ    1 
ATOM   17861 N  N     . GLY A 1 3894 ? 171.093 184.911 256.900 1.00 14.16 ? 3894 GLY A N     1 
ATOM   17862 C  CA    . GLY A 1 3894 ? 170.842 185.795 258.023 1.00 12.21 ? 3894 GLY A CA    1 
ATOM   17863 C  C     . GLY A 1 3894 ? 169.790 185.290 258.986 1.00 17.24 ? 3894 GLY A C     1 
ATOM   17864 O  O     . GLY A 1 3894 ? 169.730 185.761 260.125 1.00 25.37 ? 3894 GLY A O     1 
ATOM   17865 N  N     . THR A 1 3895 ? 168.962 184.340 258.558 1.00 20.73 ? 3895 THR A N     1 
ATOM   17866 C  CA    . THR A 1 3895 ? 167.901 183.801 259.402 1.00 21.16 ? 3895 THR A CA    1 
ATOM   17867 C  C     . THR A 1 3895 ? 168.495 182.750 260.333 1.00 25.29 ? 3895 THR A C     1 
ATOM   17868 O  O     . THR A 1 3895 ? 168.967 181.702 259.879 1.00 25.69 ? 3895 THR A O     1 
ATOM   17869 C  CB    . THR A 1 3895 ? 166.788 183.204 258.547 1.00 21.10 ? 3895 THR A CB    1 
ATOM   17870 O  OG1   . THR A 1 3895 ? 166.246 184.216 257.689 1.00 18.37 ? 3895 THR A OG1   1 
ATOM   17871 C  CG2   . THR A 1 3895 ? 165.679 182.666 259.436 1.00 19.24 ? 3895 THR A CG2   1 
ATOM   17872 N  N     . VAL A 1 3896 ? 168.473 183.031 261.638 1.00 24.38 ? 3896 VAL A N     1 
ATOM   17873 C  CA    . VAL A 1 3896 ? 169.037 182.102 262.613 1.00 25.72 ? 3896 VAL A CA    1 
ATOM   17874 C  C     . VAL A 1 3896 ? 168.214 180.819 262.671 1.00 24.22 ? 3896 VAL A C     1 
ATOM   17875 O  O     . VAL A 1 3896 ? 168.760 179.722 262.833 1.00 28.09 ? 3896 VAL A O     1 
ATOM   17876 C  CB    . VAL A 1 3896 ? 169.137 182.777 263.992 1.00 27.19 ? 3896 VAL A CB    1 
ATOM   17877 C  CG1   . VAL A 1 3896 ? 169.740 181.824 265.013 1.00 27.09 ? 3896 VAL A CG1   1 
ATOM   17878 C  CG2   . VAL A 1 3896 ? 169.959 184.054 263.898 1.00 20.76 ? 3896 VAL A CG2   1 
ATOM   17879 N  N     . GLY A 1 3897 ? 166.897 180.932 262.527 1.00 23.13 ? 3897 GLY A N     1 
ATOM   17880 C  CA    . GLY A 1 3897 ? 166.013 179.788 262.588 1.00 21.82 ? 3897 GLY A CA    1 
ATOM   17881 C  C     . GLY A 1 3897 ? 165.977 178.914 261.356 1.00 25.95 ? 3897 GLY A C     1 
ATOM   17882 O  O     . GLY A 1 3897 ? 165.287 177.890 261.359 1.00 24.45 ? 3897 GLY A O     1 
ATOM   17883 N  N     . GLU A 1 3898 ? 166.702 179.282 260.289 1.00 21.54 ? 3898 GLU A N     1 
ATOM   17884 C  CA    . GLU A 1 3898 ? 166.674 178.430 259.114 1.00 19.21 ? 3898 GLU A CA    1 
ATOM   17885 C  C     . GLU A 1 3898 ? 167.936 177.579 259.029 1.00 19.90 ? 3898 GLU A C     1 
ATOM   17886 O  O     . GLU A 1 3898 ? 169.013 178.007 259.454 1.00 23.28 ? 3898 GLU A O     1 
ATOM   17887 C  CB    . GLU A 1 3898 ? 166.548 179.265 257.836 1.00 18.00 ? 3898 GLU A CB    1 
ATOM   17888 C  CG    . GLU A 1 3898 ? 165.132 179.720 257.522 1.00 17.86 ? 3898 GLU A CG    1 
ATOM   17889 C  CD    . GLU A 1 3898 ? 164.163 178.569 257.386 1.00 18.55 ? 3898 GLU A CD    1 
ATOM   17890 O  OE1   . GLU A 1 3898 ? 164.369 177.713 256.502 1.00 17.01 ? 3898 GLU A OE1   1 
ATOM   17891 O  OE2   . GLU A 1 3898 ? 163.191 178.523 258.168 1.00 24.41 ? 3898 GLU A OE2   1 
ATOM   17892 N  N     . PRO A 1 3899 ? 167.829 176.369 258.488 1.00 19.15 ? 3899 PRO A N     1 
ATOM   17893 C  CA    . PRO A 1 3899 ? 169.025 175.560 258.231 1.00 17.01 ? 3899 PRO A CA    1 
ATOM   17894 C  C     . PRO A 1 3899 ? 169.843 176.134 257.083 1.00 19.92 ? 3899 PRO A C     1 
ATOM   17895 O  O     . PRO A 1 3899 ? 169.444 177.076 256.396 1.00 21.33 ? 3899 PRO A O     1 
ATOM   17896 C  CB    . PRO A 1 3899 ? 168.467 174.177 257.878 1.00 11.58 ? 3899 PRO A CB    1 
ATOM   17897 C  CG    . PRO A 1 3899 ? 167.038 174.198 258.325 1.00 14.03 ? 3899 PRO A CG    1 
ATOM   17898 C  CD    . PRO A 1 3899 ? 166.590 175.619 258.232 1.00 16.05 ? 3899 PRO A CD    1 
ATOM   17899 N  N     . THR A 1 3900 ? 171.018 175.538 256.881 1.00 20.23 ? 3900 THR A N     1 
ATOM   17900 C  CA    . THR A 1 3900 ? 171.934 176.019 255.852 1.00 19.11 ? 3900 THR A CA    1 
ATOM   17901 C  C     . THR A 1 3900 ? 171.481 175.627 254.451 1.00 16.18 ? 3900 THR A C     1 
ATOM   17902 O  O     . THR A 1 3900 ? 171.664 176.399 253.502 1.00 16.65 ? 3900 THR A O     1 
ATOM   17903 C  CB    . THR A 1 3900 ? 173.344 175.487 256.114 1.00 17.93 ? 3900 THR A CB    1 
ATOM   17904 O  OG1   . THR A 1 3900 ? 173.429 174.125 255.678 1.00 19.77 ? 3900 THR A OG1   1 
ATOM   17905 C  CG2   . THR A 1 3900 ? 173.676 175.560 257.595 1.00 19.32 ? 3900 THR A CG2   1 
ATOM   17906 N  N     . TYR A 1 3901 ? 170.904 174.434 254.302 1.00 15.44 ? 3901 TYR A N     1 
ATOM   17907 C  CA    . TYR A 1 3901 ? 170.549 173.871 252.997 1.00 13.36 ? 3901 TYR A CA    1 
ATOM   17908 C  C     . TYR A 1 3901 ? 171.751 173.809 252.059 1.00 16.94 ? 3901 TYR A C     1 
ATOM   17909 O  O     . TYR A 1 3901 ? 171.605 173.915 250.839 1.00 19.10 ? 3901 TYR A O     1 
ATOM   17910 C  CB    . TYR A 1 3901 ? 169.406 174.646 252.335 1.00 11.24 ? 3901 TYR A CB    1 
ATOM   17911 C  CG    . TYR A 1 3901 ? 168.199 174.867 253.213 1.00 12.64 ? 3901 TYR A CG    1 
ATOM   17912 C  CD1   . TYR A 1 3901 ? 167.333 173.823 253.511 1.00 9.25  ? 3901 TYR A CD1   1 
ATOM   17913 C  CD2   . TYR A 1 3901 ? 167.915 176.123 253.731 1.00 11.07 ? 3901 TYR A CD2   1 
ATOM   17914 C  CE1   . TYR A 1 3901 ? 166.226 174.022 254.308 1.00 8.60  ? 3901 TYR A CE1   1 
ATOM   17915 C  CE2   . TYR A 1 3901 ? 166.809 176.332 254.525 1.00 12.37 ? 3901 TYR A CE2   1 
ATOM   17916 C  CZ    . TYR A 1 3901 ? 165.967 175.277 254.811 1.00 13.22 ? 3901 TYR A CZ    1 
ATOM   17917 O  OH    . TYR A 1 3901 ? 164.863 175.484 255.604 1.00 17.14 ? 3901 TYR A OH    1 
ATOM   17918 N  N     . ASP A 1 3902 ? 172.950 173.632 252.619 1.00 16.11 ? 3902 ASP A N     1 
ATOM   17919 C  CA    . ASP A 1 3902 ? 174.154 173.617 251.795 1.00 16.25 ? 3902 ASP A CA    1 
ATOM   17920 C  C     . ASP A 1 3902 ? 174.163 172.426 250.846 1.00 18.72 ? 3902 ASP A C     1 
ATOM   17921 O  O     . ASP A 1 3902 ? 174.569 172.553 249.686 1.00 21.46 ? 3902 ASP A O     1 
ATOM   17922 C  CB    . ASP A 1 3902 ? 175.398 173.611 252.683 1.00 21.74 ? 3902 ASP A CB    1 
ATOM   17923 C  CG    . ASP A 1 3902 ? 175.600 174.927 253.407 1.00 29.64 ? 3902 ASP A CG    1 
ATOM   17924 O  OD1   . ASP A 1 3902 ? 174.816 175.867 253.159 1.00 26.85 ? 3902 ASP A OD1   1 
ATOM   17925 O  OD2   . ASP A 1 3902 ? 176.541 175.021 254.222 1.00 31.50 ? 3902 ASP A OD2   1 
ATOM   17926 N  N     . ALA A 1 3903 ? 173.724 171.258 251.321 1.00 16.87 ? 3903 ALA A N     1 
ATOM   17927 C  CA    . ALA A 1 3903 ? 173.683 170.081 250.460 1.00 19.13 ? 3903 ALA A CA    1 
ATOM   17928 C  C     . ALA A 1 3903 ? 172.693 170.262 249.316 1.00 17.52 ? 3903 ALA A C     1 
ATOM   17929 O  O     . ALA A 1 3903 ? 172.990 169.911 248.168 1.00 19.93 ? 3903 ALA A O     1 
ATOM   17930 C  CB    . ALA A 1 3903 ? 173.330 168.843 251.285 1.00 15.49 ? 3903 ALA A CB    1 
ATOM   17931 N  N     . GLU A 1 3904 ? 171.510 170.805 249.610 1.00 15.16 ? 3904 GLU A N     1 
ATOM   17932 C  CA    . GLU A 1 3904 ? 170.515 171.022 248.563 1.00 14.43 ? 3904 GLU A CA    1 
ATOM   17933 C  C     . GLU A 1 3904 ? 170.988 172.047 247.539 1.00 16.42 ? 3904 GLU A C     1 
ATOM   17934 O  O     . GLU A 1 3904 ? 170.780 171.867 246.334 1.00 23.24 ? 3904 GLU A O     1 
ATOM   17935 C  CB    . GLU A 1 3904 ? 169.183 171.440 249.186 1.00 17.08 ? 3904 GLU A CB    1 
ATOM   17936 C  CG    . GLU A 1 3904 ? 168.508 170.344 250.006 1.00 20.28 ? 3904 GLU A CG    1 
ATOM   17937 C  CD    . GLU A 1 3904 ? 169.047 170.230 251.417 1.00 24.44 ? 3904 GLU A CD    1 
ATOM   17938 O  OE1   . GLU A 1 3904 ? 169.912 171.045 251.796 1.00 22.42 ? 3904 GLU A OE1   1 
ATOM   17939 O  OE2   . GLU A 1 3904 ? 168.604 169.320 252.149 1.00 26.53 ? 3904 GLU A OE2   1 
ATOM   17940 N  N     . PHE A 1 3905 ? 171.624 173.129 247.992 1.00 12.56 ? 3905 PHE A N     1 
ATOM   17941 C  CA    . PHE A 1 3905 ? 172.197 174.074 247.040 1.00 10.17 ? 3905 PHE A CA    1 
ATOM   17942 C  C     . PHE A 1 3905 ? 173.426 173.493 246.353 1.00 13.78 ? 3905 PHE A C     1 
ATOM   17943 O  O     . PHE A 1 3905 ? 173.731 173.866 245.215 1.00 18.47 ? 3905 PHE A O     1 
ATOM   17944 C  CB    . PHE A 1 3905 ? 172.540 175.394 247.729 1.00 13.24 ? 3905 PHE A CB    1 
ATOM   17945 C  CG    . PHE A 1 3905 ? 171.349 176.276 247.968 1.00 7.06  ? 3905 PHE A CG    1 
ATOM   17946 C  CD1   . PHE A 1 3905 ? 170.651 176.816 246.903 1.00 5.03  ? 3905 PHE A CD1   1 
ATOM   17947 C  CD2   . PHE A 1 3905 ? 170.935 176.569 249.254 1.00 7.15  ? 3905 PHE A CD2   1 
ATOM   17948 C  CE1   . PHE A 1 3905 ? 169.555 177.623 247.117 1.00 6.98  ? 3905 PHE A CE1   1 
ATOM   17949 C  CE2   . PHE A 1 3905 ? 169.841 177.380 249.474 1.00 8.41  ? 3905 PHE A CE2   1 
ATOM   17950 C  CZ    . PHE A 1 3905 ? 169.149 177.908 248.404 1.00 10.25 ? 3905 PHE A CZ    1 
ATOM   17951 N  N     . GLN A 1 3906 ? 174.140 172.588 247.025 1.00 16.31 ? 3906 GLN A N     1 
ATOM   17952 C  CA    . GLN A 1 3906 ? 175.226 171.873 246.365 1.00 14.87 ? 3906 GLN A CA    1 
ATOM   17953 C  C     . GLN A 1 3906 ? 174.697 171.024 245.219 1.00 17.32 ? 3906 GLN A C     1 
ATOM   17954 O  O     . GLN A 1 3906 ? 175.327 170.931 244.161 1.00 18.78 ? 3906 GLN A O     1 
ATOM   17955 C  CB    . GLN A 1 3906 ? 175.973 171.002 247.375 1.00 16.96 ? 3906 GLN A CB    1 
ATOM   17956 C  CG    . GLN A 1 3906 ? 177.174 170.264 246.811 1.00 18.38 ? 3906 GLN A CG    1 
ATOM   17957 C  CD    . GLN A 1 3906 ? 178.247 171.202 246.300 1.00 28.40 ? 3906 GLN A CD    1 
ATOM   17958 O  OE1   . GLN A 1 3906 ? 178.411 171.379 245.095 1.00 27.89 ? 3906 GLN A OE1   1 
ATOM   17959 N  NE2   . GLN A 1 3906 ? 178.988 171.810 247.219 1.00 24.72 ? 3906 GLN A NE2   1 
ATOM   17960 N  N     . HIS A 1 3907 ? 173.536 170.395 245.414 1.00 15.08 ? 3907 HIS A N     1 
ATOM   17961 C  CA    . HIS A 1 3907 ? 172.934 169.606 244.347 1.00 13.51 ? 3907 HIS A CA    1 
ATOM   17962 C  C     . HIS A 1 3907 ? 172.281 170.485 243.289 1.00 17.04 ? 3907 HIS A C     1 
ATOM   17963 O  O     . HIS A 1 3907 ? 172.287 170.137 242.104 1.00 20.96 ? 3907 HIS A O     1 
ATOM   17964 C  CB    . HIS A 1 3907 ? 171.910 168.630 244.922 1.00 20.07 ? 3907 HIS A CB    1 
ATOM   17965 C  CG    . HIS A 1 3907 ? 171.481 167.579 243.950 1.00 19.22 ? 3907 HIS A CG    1 
ATOM   17966 N  ND1   . HIS A 1 3907 ? 172.260 166.483 243.648 1.00 19.23 ? 3907 HIS A ND1   1 
ATOM   17967 C  CD2   . HIS A 1 3907 ? 170.365 167.468 243.193 1.00 17.67 ? 3907 HIS A CD2   1 
ATOM   17968 C  CE1   . HIS A 1 3907 ? 171.637 165.738 242.753 1.00 22.86 ? 3907 HIS A CE1   1 
ATOM   17969 N  NE2   . HIS A 1 3907 ? 170.485 166.313 242.460 1.00 24.61 ? 3907 HIS A NE2   1 
ATOM   17970 N  N     . PHE A 1 3908 ? 171.703 171.617 243.697 1.00 15.09 ? 3908 PHE A N     1 
ATOM   17971 C  CA    . PHE A 1 3908 ? 171.062 172.508 242.735 1.00 14.69 ? 3908 PHE A CA    1 
ATOM   17972 C  C     . PHE A 1 3908 ? 172.075 173.050 241.736 1.00 12.70 ? 3908 PHE A C     1 
ATOM   17973 O  O     . PHE A 1 3908 ? 171.820 173.076 240.527 1.00 13.63 ? 3908 PHE A O     1 
ATOM   17974 C  CB    . PHE A 1 3908 ? 170.353 173.644 243.471 1.00 11.81 ? 3908 PHE A CB    1 
ATOM   17975 C  CG    . PHE A 1 3908 ? 169.601 174.575 242.567 1.00 10.99 ? 3908 PHE A CG    1 
ATOM   17976 C  CD1   . PHE A 1 3908 ? 168.510 174.127 241.844 1.00 9.43  ? 3908 PHE A CD1   1 
ATOM   17977 C  CD2   . PHE A 1 3908 ? 169.968 175.906 242.462 1.00 11.32 ? 3908 PHE A CD2   1 
ATOM   17978 C  CE1   . PHE A 1 3908 ? 167.815 174.980 241.017 1.00 11.19 ? 3908 PHE A CE1   1 
ATOM   17979 C  CE2   . PHE A 1 3908 ? 169.268 176.767 241.642 1.00 13.55 ? 3908 PHE A CE2   1 
ATOM   17980 C  CZ    . PHE A 1 3908 ? 168.188 176.305 240.921 1.00 9.38  ? 3908 PHE A CZ    1 
ATOM   17981 N  N     . LEU A 1 3909 ? 173.233 173.481 242.223 1.00 10.26 ? 3909 LEU A N     1 
ATOM   17982 C  CA    . LEU A 1 3909 ? 174.337 173.816 241.344 1.00 10.25 ? 3909 LEU A CA    1 
ATOM   17983 C  C     . LEU A 1 3909 ? 175.075 172.543 240.940 1.00 17.73 ? 3909 LEU A C     1 
ATOM   17984 O  O     . LEU A 1 3909 ? 174.878 171.472 241.521 1.00 22.32 ? 3909 LEU A O     1 
ATOM   17985 C  CB    . LEU A 1 3909 ? 175.287 174.799 242.024 1.00 13.05 ? 3909 LEU A CB    1 
ATOM   17986 C  CG    . LEU A 1 3909 ? 174.657 176.055 242.629 1.00 13.56 ? 3909 LEU A CG    1 
ATOM   17987 C  CD1   . LEU A 1 3909 ? 175.731 176.979 243.174 1.00 16.38 ? 3909 LEU A CD1   1 
ATOM   17988 C  CD2   . LEU A 1 3909 ? 173.796 176.775 241.607 1.00 10.10 ? 3909 LEU A CD2   1 
ATOM   17989 N  N     . ARG A 1 3910 ? 175.931 172.666 239.925 1.00 19.10 ? 3910 ARG A N     1 
ATOM   17990 C  CA    . ARG A 1 3910 ? 176.695 171.528 239.422 1.00 26.49 ? 3910 ARG A CA    1 
ATOM   17991 C  C     . ARG A 1 3910 ? 175.758 170.371 239.096 1.00 32.31 ? 3910 ARG A C     1 
ATOM   17992 O  O     . ARG A 1 3910 ? 175.144 170.348 238.023 1.00 29.90 ? 3910 ARG A O     1 
ATOM   17993 C  CB    . ARG A 1 3910 ? 177.762 171.110 240.442 1.00 21.06 ? 3910 ARG A CB    1 
ATOM   17994 C  CG    . ARG A 1 3910 ? 178.679 172.256 240.840 1.00 26.55 ? 3910 ARG A CG    1 
ATOM   17995 C  CD    . ARG A 1 3910 ? 179.430 172.007 242.135 1.00 23.50 ? 3910 ARG A CD    1 
ATOM   17996 N  NE    . ARG A 1 3910 ? 180.487 171.014 241.988 1.00 36.38 ? 3910 ARG A NE    1 
ATOM   17997 C  CZ    . ARG A 1 3910 ? 181.403 170.755 242.910 1.00 37.67 ? 3910 ARG A CZ    1 
ATOM   17998 N  NH1   . ARG A 1 3910 ? 181.429 171.407 244.061 1.00 28.79 ? 3910 ARG A NH1   1 
ATOM   17999 N  NH2   . ARG A 1 3910 ? 182.318 169.819 242.672 1.00 38.44 ? 3910 ARG A NH2   1 
ATOM   18000 N  N     . GLY A 1 3911 ? 175.638 169.410 240.010 1.00 23.19 ? 3911 GLY A N     1 
ATOM   18001 C  CA    . GLY A 1 3911 ? 174.637 168.366 239.881 1.00 22.47 ? 3911 GLY A CA    1 
ATOM   18002 C  C     . GLY A 1 3911 ? 174.947 167.329 238.823 1.00 23.75 ? 3911 GLY A C     1 
ATOM   18003 O  O     . GLY A 1 3911 ? 174.868 166.124 239.083 1.00 28.10 ? 3911 GLY A O     1 
ATOM   18004 N  N     . ASN A 1 3912 ? 175.290 167.786 237.619 1.00 26.39 ? 3912 ASN A N     1 
ATOM   18005 C  CA    . ASN A 1 3912 ? 175.672 166.883 236.542 1.00 26.32 ? 3912 ASN A CA    1 
ATOM   18006 C  C     . ASN A 1 3912 ? 176.981 166.156 236.818 1.00 30.39 ? 3912 ASN A C     1 
ATOM   18007 O  O     . ASN A 1 3912 ? 177.285 165.183 236.120 1.00 39.00 ? 3912 ASN A O     1 
ATOM   18008 C  CB    . ASN A 1 3912 ? 175.779 167.659 235.227 1.00 22.44 ? 3912 ASN A CB    1 
ATOM   18009 C  CG    . ASN A 1 3912 ? 176.645 168.899 235.351 1.00 35.31 ? 3912 ASN A CG    1 
ATOM   18010 O  OD1   . ASN A 1 3912 ? 177.187 169.191 236.418 1.00 37.44 ? 3912 ASN A OD1   1 
ATOM   18011 N  ND2   . ASN A 1 3912 ? 176.778 169.639 234.256 1.00 37.61 ? 3912 ASN A ND2   1 
ATOM   18012 N  N     . GLU A 1 3913 ? 177.754 166.600 237.812 1.00 23.90 ? 3913 GLU A N     1 
ATOM   18013 C  CA    . GLU A 1 3913 ? 179.028 165.961 238.117 1.00 28.83 ? 3913 GLU A CA    1 
ATOM   18014 C  C     . GLU A 1 3913 ? 178.856 164.561 238.691 1.00 34.17 ? 3913 GLU A C     1 
ATOM   18015 O  O     . GLU A 1 3913 ? 179.825 163.795 238.720 1.00 35.21 ? 3913 GLU A O     1 
ATOM   18016 C  CB    . GLU A 1 3913 ? 179.826 166.828 239.091 1.00 32.48 ? 3913 GLU A CB    1 
ATOM   18017 C  CG    . GLU A 1 3913 ? 180.135 168.217 238.565 1.00 29.44 ? 3913 GLU A CG    1 
ATOM   18018 C  CD    . GLU A 1 3913 ? 180.858 169.075 239.580 1.00 35.38 ? 3913 GLU A CD    1 
ATOM   18019 O  OE1   . GLU A 1 3913 ? 181.024 168.623 240.732 1.00 37.72 ? 3913 GLU A OE1   1 
ATOM   18020 O  OE2   . GLU A 1 3913 ? 181.260 170.203 239.227 1.00 36.99 ? 3913 GLU A OE2   1 
ATOM   18021 N  N     . ILE A 1 3914 ? 177.654 164.209 239.143 1.00 28.08 ? 3914 ILE A N     1 
ATOM   18022 C  CA    . ILE A 1 3914 ? 177.396 162.875 239.666 1.00 24.43 ? 3914 ILE A CA    1 
ATOM   18023 C  C     . ILE A 1 3914 ? 177.252 161.916 238.493 1.00 28.77 ? 3914 ILE A C     1 
ATOM   18024 O  O     . ILE A 1 3914 ? 176.173 161.792 237.904 1.00 27.68 ? 3914 ILE A O     1 
ATOM   18025 C  CB    . ILE A 1 3914 ? 176.144 162.855 240.563 1.00 26.21 ? 3914 ILE A CB    1 
ATOM   18026 C  CG1   . ILE A 1 3914 ? 176.241 163.940 241.637 1.00 20.17 ? 3914 ILE A CG1   1 
ATOM   18027 C  CG2   . ILE A 1 3914 ? 175.959 161.483 241.191 1.00 24.66 ? 3914 ILE A CG2   1 
ATOM   18028 C  CD1   . ILE A 1 3914 ? 175.063 163.974 242.583 1.00 17.14 ? 3914 ILE A CD1   1 
ATOM   18029 N  N     . VAL A 1 3915 ? 178.344 161.233 238.149 1.00 30.17 ? 3915 VAL A N     1 
ATOM   18030 C  CA    . VAL A 1 3915 ? 178.363 160.373 236.973 1.00 25.66 ? 3915 VAL A CA    1 
ATOM   18031 C  C     . VAL A 1 3915 ? 177.544 159.118 237.240 1.00 30.83 ? 3915 VAL A C     1 
ATOM   18032 O  O     . VAL A 1 3915 ? 177.705 158.460 238.277 1.00 27.74 ? 3915 VAL A O     1 
ATOM   18033 C  CB    . VAL A 1 3915 ? 179.808 160.027 236.586 1.00 32.28 ? 3915 VAL A CB    1 
ATOM   18034 C  CG1   . VAL A 1 3915 ? 179.830 159.098 235.382 1.00 28.07 ? 3915 VAL A CG1   1 
ATOM   18035 C  CG2   . VAL A 1 3915 ? 180.595 161.297 236.300 1.00 30.55 ? 3915 VAL A CG2   1 
ATOM   18036 N  N     . LEU A 1 3916 ? 176.662 158.782 236.305 1.00 27.50 ? 3916 LEU A N     1 
ATOM   18037 C  CA    . LEU A 1 3916 ? 175.798 157.615 236.410 1.00 28.77 ? 3916 LEU A CA    1 
ATOM   18038 C  C     . LEU A 1 3916 ? 176.182 156.599 235.345 1.00 34.60 ? 3916 LEU A C     1 
ATOM   18039 O  O     . LEU A 1 3916 ? 176.281 156.941 234.162 1.00 36.99 ? 3916 LEU A O     1 
ATOM   18040 C  CB    . LEU A 1 3916 ? 174.328 158.006 236.255 1.00 28.93 ? 3916 LEU A CB    1 
ATOM   18041 C  CG    . LEU A 1 3916 ? 173.811 159.109 237.176 1.00 29.68 ? 3916 LEU A CG    1 
ATOM   18042 C  CD1   . LEU A 1 3916 ? 172.325 159.331 236.944 1.00 27.15 ? 3916 LEU A CD1   1 
ATOM   18043 C  CD2   . LEU A 1 3916 ? 174.090 158.767 238.629 1.00 27.69 ? 3916 LEU A CD2   1 
ATOM   18044 N  N     . SER A 1 3917 ? 176.395 155.355 235.767 1.00 32.55 ? 3917 SER A N     1 
ATOM   18045 C  CA    . SER A 1 3917 ? 176.680 154.278 234.835 1.00 33.84 ? 3917 SER A CA    1 
ATOM   18046 C  C     . SER A 1 3917 ? 175.392 153.803 234.162 1.00 38.29 ? 3917 SER A C     1 
ATOM   18047 O  O     . SER A 1 3917 ? 174.286 154.225 234.507 1.00 37.87 ? 3917 SER A O     1 
ATOM   18048 C  CB    . SER A 1 3917 ? 177.369 153.118 235.552 1.00 34.97 ? 3917 SER A CB    1 
ATOM   18049 O  OG    . SER A 1 3917 ? 178.566 153.544 236.178 1.00 33.72 ? 3917 SER A OG    1 
ATOM   18050 N  N     . ALA A 1 3918 ? 175.553 152.915 233.179 1.00 35.18 ? 3918 ALA A N     1 
ATOM   18051 C  CA    . ALA A 1 3918 ? 174.394 152.388 232.464 1.00 31.72 ? 3918 ALA A CA    1 
ATOM   18052 C  C     . ALA A 1 3918 ? 173.480 151.601 233.396 1.00 31.16 ? 3918 ALA A C     1 
ATOM   18053 O  O     . ALA A 1 3918 ? 172.252 151.746 233.343 1.00 35.85 ? 3918 ALA A O     1 
ATOM   18054 C  CB    . ALA A 1 3918 ? 174.849 151.515 231.295 1.00 27.24 ? 3918 ALA A CB    1 
ATOM   18055 N  N     . GLY A 1 3919 ? 174.059 150.763 234.258 1.00 29.92 ? 3919 GLY A N     1 
ATOM   18056 C  CA    . GLY A 1 3919 ? 173.249 150.026 235.213 1.00 29.32 ? 3919 GLY A CA    1 
ATOM   18057 C  C     . GLY A 1 3919 ? 172.764 150.879 236.366 1.00 33.40 ? 3919 GLY A C     1 
ATOM   18058 O  O     . GLY A 1 3919 ? 171.789 150.525 237.037 1.00 33.87 ? 3919 GLY A O     1 
ATOM   18059 N  N     . SER A 1 3920 ? 173.433 152.007 236.618 1.00 33.65 ? 3920 SER A N     1 
ATOM   18060 C  CA    . SER A 1 3920 ? 173.019 152.886 237.707 1.00 33.65 ? 3920 SER A CA    1 
ATOM   18061 C  C     . SER A 1 3920 ? 171.666 153.524 237.420 1.00 33.41 ? 3920 SER A C     1 
ATOM   18062 O  O     . SER A 1 3920 ? 170.849 153.702 238.331 1.00 31.21 ? 3920 SER A O     1 
ATOM   18063 C  CB    . SER A 1 3920 ? 174.080 153.960 237.947 1.00 32.45 ? 3920 SER A CB    1 
ATOM   18064 O  OG    . SER A 1 3920 ? 175.352 153.380 238.175 1.00 36.94 ? 3920 SER A OG    1 
ATOM   18065 N  N     . THR A 1 3921 ? 171.409 153.879 236.160 1.00 30.86 ? 3921 THR A N     1 
ATOM   18066 C  CA    . THR A 1 3921 ? 170.162 154.529 235.796 1.00 29.52 ? 3921 THR A CA    1 
ATOM   18067 C  C     . THR A 1 3921 ? 169.205 153.502 235.216 1.00 28.40 ? 3921 THR A C     1 
ATOM   18068 O  O     . THR A 1 3921 ? 169.449 153.000 234.109 1.00 29.08 ? 3921 THR A O     1 
ATOM   18069 C  CB    . THR A 1 3921 ? 170.408 155.651 234.790 1.00 28.10 ? 3921 THR A CB    1 
ATOM   18070 O  OG1   . THR A 1 3921 ? 171.285 156.628 235.365 1.00 30.51 ? 3921 THR A OG1   1 
ATOM   18071 C  CG2   . THR A 1 3921 ? 169.097 156.319 234.406 1.00 26.28 ? 3921 THR A CG2   1 
ATOM   18072 N  N     . PRO A 1 3922 ? 168.121 153.160 235.902 1.00 25.91 ? 3922 PRO A N     1 
ATOM   18073 C  CA    . PRO A 1 3922 ? 167.138 152.228 235.351 1.00 27.24 ? 3922 PRO A CA    1 
ATOM   18074 C  C     . PRO A 1 3922 ? 166.174 152.963 234.426 1.00 33.11 ? 3922 PRO A C     1 
ATOM   18075 O  O     . PRO A 1 3922 ? 166.334 154.146 234.130 1.00 37.21 ? 3922 PRO A O     1 
ATOM   18076 C  CB    . PRO A 1 3922 ? 166.434 151.697 236.600 1.00 31.92 ? 3922 PRO A CB    1 
ATOM   18077 C  CG    . PRO A 1 3922 ? 166.477 152.849 237.546 1.00 29.65 ? 3922 PRO A CG    1 
ATOM   18078 C  CD    . PRO A 1 3922 ? 167.780 153.574 237.275 1.00 29.63 ? 3922 PRO A CD    1 
ATOM   18079 N  N     . ARG A 1 3923 ? 165.160 152.235 233.965 1.00 32.60 ? 3923 ARG A N     1 
ATOM   18080 C  CA    . ARG A 1 3923 ? 164.115 152.799 233.114 1.00 30.09 ? 3923 ARG A CA    1 
ATOM   18081 C  C     . ARG A 1 3923 ? 162.841 152.908 233.943 1.00 34.03 ? 3923 ARG A C     1 
ATOM   18082 O  O     . ARG A 1 3923 ? 162.133 151.918 234.149 1.00 35.02 ? 3923 ARG A O     1 
ATOM   18083 C  CB    . ARG A 1 3923 ? 163.900 151.945 231.868 1.00 32.40 ? 3923 ARG A CB    1 
ATOM   18084 C  CG    . ARG A 1 3923 ? 162.774 152.437 230.973 1.00 33.62 ? 3923 ARG A CG    1 
ATOM   18085 C  CD    . ARG A 1 3923 ? 162.482 151.457 229.851 1.00 31.12 ? 3923 ARG A CD    1 
ATOM   18086 N  NE    . ARG A 1 3923 ? 162.064 150.157 230.360 1.00 42.52 ? 3923 ARG A NE    1 
ATOM   18087 C  CZ    . ARG A 1 3923 ? 161.712 149.132 229.597 1.00 42.29 ? 3923 ARG A CZ    1 
ATOM   18088 N  NH1   . ARG A 1 3923 ? 161.714 149.220 228.277 1.00 36.12 ? 3923 ARG A NH1   1 
ATOM   18089 N  NH2   . ARG A 1 3923 ? 161.347 147.990 230.173 1.00 39.72 ? 3923 ARG A NH2   1 
ATOM   18090 N  N     . ILE A 1 3924 ? 162.549 154.112 234.421 1.00 33.73 ? 3924 ILE A N     1 
ATOM   18091 C  CA    . ILE A 1 3924 ? 161.317 154.379 235.155 1.00 30.12 ? 3924 ILE A CA    1 
ATOM   18092 C  C     . ILE A 1 3924 ? 160.218 154.671 234.144 1.00 29.87 ? 3924 ILE A C     1 
ATOM   18093 O  O     . ILE A 1 3924 ? 160.344 155.586 233.323 1.00 33.07 ? 3924 ILE A O     1 
ATOM   18094 C  CB    . ILE A 1 3924 ? 161.484 155.549 236.137 1.00 31.62 ? 3924 ILE A CB    1 
ATOM   18095 C  CG1   . ILE A 1 3924 ? 162.569 155.246 237.174 1.00 30.56 ? 3924 ILE A CG1   1 
ATOM   18096 C  CG2   . ILE A 1 3924 ? 160.160 155.851 236.824 1.00 29.66 ? 3924 ILE A CG2   1 
ATOM   18097 C  CD1   . ILE A 1 3924 ? 163.931 155.808 236.826 1.00 25.26 ? 3924 ILE A CD1   1 
ATOM   18098 N  N     . GLN A 1 3925 ? 159.140 153.890 234.196 1.00 32.11 ? 3925 GLN A N     1 
ATOM   18099 C  CA    . GLN A 1 3925 ? 158.017 154.116 233.301 1.00 28.79 ? 3925 GLN A CA    1 
ATOM   18100 C  C     . GLN A 1 3925 ? 157.341 155.441 233.633 1.00 28.99 ? 3925 GLN A C     1 
ATOM   18101 O  O     . GLN A 1 3925 ? 157.048 155.731 234.797 1.00 23.96 ? 3925 GLN A O     1 
ATOM   18102 C  CB    . GLN A 1 3925 ? 157.016 152.965 233.406 1.00 29.70 ? 3925 GLN A CB    1 
ATOM   18103 C  CG    . GLN A 1 3925 ? 155.801 153.113 232.507 1.00 27.88 ? 3925 GLN A CG    1 
ATOM   18104 C  CD    . GLN A 1 3925 ? 154.719 152.098 232.818 1.00 34.24 ? 3925 GLN A CD    1 
ATOM   18105 O  OE1   . GLN A 1 3925 ? 154.853 151.291 233.738 1.00 34.20 ? 3925 GLN A OE1   1 
ATOM   18106 N  NE2   . GLN A 1 3925 ? 153.638 152.129 232.047 1.00 36.88 ? 3925 GLN A NE2   1 
ATOM   18107 N  N     . GLY A 1 3926 ? 157.087 156.243 232.603 1.00 26.47 ? 3926 GLY A N     1 
ATOM   18108 C  CA    . GLY A 1 3926 ? 156.520 157.563 232.764 1.00 25.07 ? 3926 GLY A CA    1 
ATOM   18109 C  C     . GLY A 1 3926 ? 157.520 158.699 232.705 1.00 25.65 ? 3926 GLY A C     1 
ATOM   18110 O  O     . GLY A 1 3926 ? 157.109 159.864 232.752 1.00 25.80 ? 3926 GLY A O     1 
ATOM   18111 N  N     . LEU A 1 3927 ? 158.813 158.399 232.607 1.00 24.08 ? 3927 LEU A N     1 
ATOM   18112 C  CA    . LEU A 1 3927 ? 159.850 159.414 232.504 1.00 25.33 ? 3927 LEU A CA    1 
ATOM   18113 C  C     . LEU A 1 3927 ? 160.765 159.089 231.333 1.00 26.64 ? 3927 LEU A C     1 
ATOM   18114 O  O     . LEU A 1 3927 ? 160.868 157.941 230.897 1.00 29.26 ? 3927 LEU A O     1 
ATOM   18115 C  CB    . LEU A 1 3927 ? 160.678 159.520 233.791 1.00 22.02 ? 3927 LEU A CB    1 
ATOM   18116 C  CG    . LEU A 1 3927 ? 159.938 159.454 235.126 1.00 23.15 ? 3927 LEU A CG    1 
ATOM   18117 C  CD1   . LEU A 1 3927 ? 160.931 159.328 236.268 1.00 23.64 ? 3927 LEU A CD1   1 
ATOM   18118 C  CD2   . LEU A 1 3927 ? 159.063 160.677 235.312 1.00 21.30 ? 3927 LEU A CD2   1 
ATOM   18119 N  N     . THR A 1 3928 ? 161.430 160.121 230.825 1.00 20.48 ? 3928 THR A N     1 
ATOM   18120 C  CA    . THR A 1 3928 ? 162.372 159.962 229.732 1.00 22.01 ? 3928 THR A CA    1 
ATOM   18121 C  C     . THR A 1 3928 ? 163.740 159.579 230.294 1.00 22.44 ? 3928 THR A C     1 
ATOM   18122 O  O     . THR A 1 3928 ? 163.915 159.414 231.504 1.00 23.76 ? 3928 THR A O     1 
ATOM   18123 C  CB    . THR A 1 3928 ? 162.442 161.236 228.892 1.00 21.61 ? 3928 THR A CB    1 
ATOM   18124 O  OG1   . THR A 1 3928 ? 162.902 162.321 229.706 1.00 31.34 ? 3928 THR A OG1   1 
ATOM   18125 C  CG2   . THR A 1 3928 ? 161.072 161.576 228.335 1.00 21.81 ? 3928 THR A CG2   1 
ATOM   18126 N  N     . VAL A 1 3929 ? 164.727 159.430 229.409 1.00 25.65 ? 3929 VAL A N     1 
ATOM   18127 C  CA    . VAL A 1 3929 ? 166.067 159.052 229.844 1.00 21.59 ? 3929 VAL A CA    1 
ATOM   18128 C  C     . VAL A 1 3929 ? 166.684 160.155 230.696 1.00 26.74 ? 3929 VAL A C     1 
ATOM   18129 O  O     . VAL A 1 3929 ? 167.227 159.895 231.777 1.00 28.24 ? 3929 VAL A O     1 
ATOM   18130 C  CB    . VAL A 1 3929 ? 166.951 158.718 228.628 1.00 28.64 ? 3929 VAL A CB    1 
ATOM   18131 C  CG1   . VAL A 1 3929 ? 168.384 158.461 229.067 1.00 26.11 ? 3929 VAL A CG1   1 
ATOM   18132 C  CG2   . VAL A 1 3929 ? 166.393 157.518 227.881 1.00 22.75 ? 3929 VAL A CG2   1 
ATOM   18133 N  N     . GLU A 1 3930 ? 166.609 161.402 230.224 1.00 27.53 ? 3930 GLU A N     1 
ATOM   18134 C  CA    . GLU A 1 3930 ? 167.192 162.512 230.973 1.00 24.19 ? 3930 GLU A CA    1 
ATOM   18135 C  C     . GLU A 1 3930 ? 166.479 162.724 232.303 1.00 24.18 ? 3930 GLU A C     1 
ATOM   18136 O  O     . GLU A 1 3930 ? 167.123 163.020 233.315 1.00 24.09 ? 3930 GLU A O     1 
ATOM   18137 C  CB    . GLU A 1 3930 ? 167.171 163.790 230.132 1.00 20.20 ? 3930 GLU A CB    1 
ATOM   18138 C  CG    . GLU A 1 3930 ? 165.794 164.223 229.649 1.00 25.47 ? 3930 GLU A CG    1 
ATOM   18139 C  CD    . GLU A 1 3930 ? 165.415 163.591 228.323 1.00 30.86 ? 3930 GLU A CD    1 
ATOM   18140 O  OE1   . GLU A 1 3930 ? 166.157 162.703 227.854 1.00 31.41 ? 3930 GLU A OE1   1 
ATOM   18141 O  OE2   . GLU A 1 3930 ? 164.378 163.986 227.750 1.00 33.14 ? 3930 GLU A OE2   1 
ATOM   18142 N  N     . GLN A 1 3931 ? 165.151 162.580 232.322 1.00 19.42 ? 3931 GLN A N     1 
ATOM   18143 C  CA    . GLN A 1 3931 ? 164.417 162.708 233.577 1.00 22.30 ? 3931 GLN A CA    1 
ATOM   18144 C  C     . GLN A 1 3931 ? 164.815 161.616 234.559 1.00 25.98 ? 3931 GLN A C     1 
ATOM   18145 O  O     . GLN A 1 3931 ? 164.976 161.876 235.756 1.00 27.35 ? 3931 GLN A O     1 
ATOM   18146 C  CB    . GLN A 1 3931 ? 162.912 162.672 233.317 1.00 20.01 ? 3931 GLN A CB    1 
ATOM   18147 C  CG    . GLN A 1 3931 ? 162.333 163.981 232.811 1.00 19.53 ? 3931 GLN A CG    1 
ATOM   18148 C  CD    . GLN A 1 3931 ? 160.829 163.921 232.640 1.00 22.97 ? 3931 GLN A CD    1 
ATOM   18149 O  OE1   . GLN A 1 3931 ? 160.227 162.852 232.737 1.00 27.96 ? 3931 GLN A OE1   1 
ATOM   18150 N  NE2   . GLN A 1 3931 ? 160.214 165.071 232.397 1.00 19.60 ? 3931 GLN A NE2   1 
ATOM   18151 N  N     . ALA A 1 3932 ? 164.979 160.385 234.071 1.00 26.55 ? 3932 ALA A N     1 
ATOM   18152 C  CA    . ALA A 1 3932 ? 165.370 159.285 234.947 1.00 25.75 ? 3932 ALA A CA    1 
ATOM   18153 C  C     . ALA A 1 3932 ? 166.741 159.531 235.563 1.00 25.97 ? 3932 ALA A C     1 
ATOM   18154 O  O     . ALA A 1 3932 ? 166.952 159.263 236.751 1.00 27.58 ? 3932 ALA A O     1 
ATOM   18155 C  CB    . ALA A 1 3932 ? 165.356 157.967 234.173 1.00 30.37 ? 3932 ALA A CB    1 
ATOM   18156 N  N     . GLU A 1 3933 ? 167.687 160.039 234.770 1.00 23.14 ? 3933 GLU A N     1 
ATOM   18157 C  CA    . GLU A 1 3933 ? 169.008 160.353 235.307 1.00 23.47 ? 3933 GLU A CA    1 
ATOM   18158 C  C     . GLU A 1 3933 ? 168.923 161.434 236.377 1.00 23.64 ? 3933 GLU A C     1 
ATOM   18159 O  O     . GLU A 1 3933 ? 169.591 161.347 237.413 1.00 28.88 ? 3933 GLU A O     1 
ATOM   18160 C  CB    . GLU A 1 3933 ? 169.943 160.790 234.178 1.00 24.84 ? 3933 GLU A CB    1 
ATOM   18161 C  CG    . GLU A 1 3933 ? 170.190 159.721 233.129 1.00 23.95 ? 3933 GLU A CG    1 
ATOM   18162 C  CD    . GLU A 1 3933 ? 171.614 159.732 232.611 1.00 34.01 ? 3933 GLU A CD    1 
ATOM   18163 O  OE1   . GLU A 1 3933 ? 172.546 159.861 233.431 1.00 39.33 ? 3933 GLU A OE1   1 
ATOM   18164 O  OE2   . GLU A 1 3933 ? 171.802 159.613 231.382 1.00 33.35 ? 3933 GLU A OE2   1 
ATOM   18165 N  N     . ALA A 1 3934 ? 168.102 162.460 236.145 1.00 24.58 ? 3934 ALA A N     1 
ATOM   18166 C  CA    . ALA A 1 3934 ? 167.917 163.499 237.150 1.00 24.44 ? 3934 ALA A CA    1 
ATOM   18167 C  C     . ALA A 1 3934 ? 167.299 162.936 238.421 1.00 25.61 ? 3934 ALA A C     1 
ATOM   18168 O  O     . ALA A 1 3934 ? 167.561 163.445 239.517 1.00 24.27 ? 3934 ALA A O     1 
ATOM   18169 C  CB    . ALA A 1 3934 ? 167.054 164.626 236.586 1.00 19.43 ? 3934 ALA A CB    1 
ATOM   18170 N  N     . VAL A 1 3935 ? 166.472 161.897 238.299 1.00 22.20 ? 3935 VAL A N     1 
ATOM   18171 C  CA    . VAL A 1 3935 ? 165.940 161.223 239.479 1.00 20.49 ? 3935 VAL A CA    1 
ATOM   18172 C  C     . VAL A 1 3935 ? 167.056 160.509 240.230 1.00 27.65 ? 3935 VAL A C     1 
ATOM   18173 O  O     . VAL A 1 3935 ? 167.156 160.598 241.460 1.00 26.41 ? 3935 VAL A O     1 
ATOM   18174 C  CB    . VAL A 1 3935 ? 164.817 160.251 239.078 1.00 21.11 ? 3935 VAL A CB    1 
ATOM   18175 C  CG1   . VAL A 1 3935 ? 164.396 159.408 240.262 1.00 21.38 ? 3935 VAL A CG1   1 
ATOM   18176 C  CG2   . VAL A 1 3935 ? 163.634 161.012 238.525 1.00 23.33 ? 3935 VAL A CG2   1 
ATOM   18177 N  N     . VAL A 1 3936 ? 167.911 159.788 239.502 1.00 25.71 ? 3936 VAL A N     1 
ATOM   18178 C  CA    . VAL A 1 3936 ? 168.974 159.022 240.145 1.00 24.70 ? 3936 VAL A CA    1 
ATOM   18179 C  C     . VAL A 1 3936 ? 169.959 159.951 240.842 1.00 28.51 ? 3936 VAL A C     1 
ATOM   18180 O  O     . VAL A 1 3936 ? 170.389 159.687 241.970 1.00 30.20 ? 3936 VAL A O     1 
ATOM   18181 C  CB    . VAL A 1 3936 ? 169.675 158.115 239.118 1.00 27.45 ? 3936 VAL A CB    1 
ATOM   18182 C  CG1   . VAL A 1 3936 ? 170.815 157.349 239.774 1.00 25.24 ? 3936 VAL A CG1   1 
ATOM   18183 C  CG2   . VAL A 1 3936 ? 168.678 157.156 238.492 1.00 23.37 ? 3936 VAL A CG2   1 
ATOM   18184 N  N     . ARG A 1 3937 ? 170.338 161.049 240.182 1.00 28.41 ? 3937 ARG A N     1 
ATOM   18185 C  CA    . ARG A 1 3937 ? 171.251 162.000 240.810 1.00 21.58 ? 3937 ARG A CA    1 
ATOM   18186 C  C     . ARG A 1 3937 ? 170.613 162.648 242.032 1.00 22.87 ? 3937 ARG A C     1 
ATOM   18187 O  O     . ARG A 1 3937 ? 171.263 162.797 243.074 1.00 31.71 ? 3937 ARG A O     1 
ATOM   18188 C  CB    . ARG A 1 3937 ? 171.689 163.057 239.799 1.00 21.47 ? 3937 ARG A CB    1 
ATOM   18189 C  CG    . ARG A 1 3937 ? 172.476 162.490 238.634 1.00 22.27 ? 3937 ARG A CG    1 
ATOM   18190 C  CD    . ARG A 1 3937 ? 172.907 163.565 237.657 1.00 22.29 ? 3937 ARG A CD    1 
ATOM   18191 N  NE    . ARG A 1 3937 ? 173.157 163.010 236.331 1.00 25.08 ? 3937 ARG A NE    1 
ATOM   18192 C  CZ    . ARG A 1 3937 ? 174.343 162.985 235.739 1.00 27.06 ? 3937 ARG A CZ    1 
ATOM   18193 N  NH1   . ARG A 1 3937 ? 175.423 163.466 236.332 1.00 28.71 ? 3937 ARG A NH1   1 
ATOM   18194 N  NH2   . ARG A 1 3937 ? 174.448 162.462 234.522 1.00 28.62 ? 3937 ARG A NH2   1 
ATOM   18195 N  N     . LEU A 1 3938 ? 169.340 163.033 241.929 1.00 23.01 ? 3938 LEU A N     1 
ATOM   18196 C  CA    . LEU A 1 3938 ? 168.645 163.606 243.074 1.00 19.52 ? 3938 LEU A CA    1 
ATOM   18197 C  C     . LEU A 1 3938 ? 168.448 162.588 244.190 1.00 22.12 ? 3938 LEU A C     1 
ATOM   18198 O  O     . LEU A 1 3938 ? 168.259 162.981 245.346 1.00 23.65 ? 3938 LEU A O     1 
ATOM   18199 C  CB    . LEU A 1 3938 ? 167.295 164.182 242.637 1.00 15.64 ? 3938 LEU A CB    1 
ATOM   18200 C  CG    . LEU A 1 3938 ? 166.483 164.970 243.670 1.00 18.73 ? 3938 LEU A CG    1 
ATOM   18201 C  CD1   . LEU A 1 3938 ? 167.223 166.223 244.106 1.00 19.45 ? 3938 LEU A CD1   1 
ATOM   18202 C  CD2   . LEU A 1 3938 ? 165.112 165.323 243.124 1.00 17.86 ? 3938 LEU A CD2   1 
ATOM   18203 N  N     . SER A 1 3939 ? 168.505 161.294 243.873 1.00 24.52 ? 3939 SER A N     1 
ATOM   18204 C  CA    . SER A 1 3939 ? 168.352 160.255 244.883 1.00 23.20 ? 3939 SER A CA    1 
ATOM   18205 C  C     . SER A 1 3939 ? 169.494 160.235 245.890 1.00 26.18 ? 3939 SER A C     1 
ATOM   18206 O  O     . SER A 1 3939 ? 169.348 159.618 246.950 1.00 27.70 ? 3939 SER A O     1 
ATOM   18207 C  CB    . SER A 1 3939 ? 168.235 158.887 244.212 1.00 23.41 ? 3939 SER A CB    1 
ATOM   18208 O  OG    . SER A 1 3939 ? 169.497 158.449 243.741 1.00 34.46 ? 3939 SER A OG    1 
ATOM   18209 N  N     . CYS A 1 3940 ? 170.617 160.893 245.590 1.00 23.50 ? 3940 CYS A N     1 
ATOM   18210 C  CA    . CYS A 1 3940 ? 171.744 160.916 246.512 1.00 20.75 ? 3940 CYS A CA    1 
ATOM   18211 C  C     . CYS A 1 3940 ? 171.444 161.713 247.775 1.00 27.75 ? 3940 CYS A C     1 
ATOM   18212 O  O     . CYS A 1 3940 ? 172.128 161.528 248.788 1.00 30.84 ? 3940 CYS A O     1 
ATOM   18213 C  CB    . CYS A 1 3940 ? 172.979 161.487 245.812 1.00 20.70 ? 3940 CYS A CB    1 
ATOM   18214 S  SG    . CYS A 1 3940 ? 174.527 161.290 246.726 1.00 64.87 ? 3940 CYS A SG    1 
ATOM   18215 N  N     . LEU A 1 3941 ? 170.452 162.599 247.739 1.00 23.19 ? 3941 LEU A N     1 
ATOM   18216 C  CA    . LEU A 1 3941 ? 170.153 163.267 248.999 1.00 22.47 ? 3941 LEU A CA    1 
ATOM   18217 C  C     . LEU A 1 3941 ? 169.349 162.342 249.908 1.00 23.60 ? 3941 LEU A C     1 
ATOM   18218 O  O     . LEU A 1 3941 ? 168.556 161.531 249.422 1.00 30.53 ? 3941 LEU A O     1 
ATOM   18219 C  CB    . LEU A 1 3941 ? 169.368 164.553 248.764 1.00 28.56 ? 3941 LEU A CB    1 
ATOM   18220 C  CG    . LEU A 1 3941 ? 170.041 165.674 247.970 1.00 24.28 ? 3941 LEU A CG    1 
ATOM   18221 C  CD1   . LEU A 1 3941 ? 169.360 166.998 248.268 1.00 17.23 ? 3941 LEU A CD1   1 
ATOM   18222 C  CD2   . LEU A 1 3941 ? 171.528 165.751 248.275 1.00 27.19 ? 3941 LEU A CD2   1 
ATOM   18223 N  N     . PRO A 1 3942 ? 169.551 162.446 251.224 1.00 24.61 ? 3942 PRO A N     1 
ATOM   18224 C  CA    . PRO A 1 3942 ? 168.733 161.643 252.147 1.00 21.09 ? 3942 PRO A CA    1 
ATOM   18225 C  C     . PRO A 1 3942 ? 167.243 161.907 252.019 1.00 21.45 ? 3942 PRO A C     1 
ATOM   18226 O  O     . PRO A 1 3942 ? 166.438 160.984 252.194 1.00 25.80 ? 3942 PRO A O     1 
ATOM   18227 C  CB    . PRO A 1 3942 ? 169.273 162.054 253.522 1.00 21.01 ? 3942 PRO A CB    1 
ATOM   18228 C  CG    . PRO A 1 3942 ? 170.688 162.437 253.255 1.00 20.97 ? 3942 PRO A CG    1 
ATOM   18229 C  CD    . PRO A 1 3942 ? 170.667 163.115 251.912 1.00 23.96 ? 3942 PRO A CD    1 
ATOM   18230 N  N     . ALA A 1 3943 ? 166.850 163.146 251.718 1.00 20.64 ? 3943 ALA A N     1 
ATOM   18231 C  CA    . ALA A 1 3943 ? 165.430 163.456 251.582 1.00 25.80 ? 3943 ALA A CA    1 
ATOM   18232 C  C     . ALA A 1 3943 ? 164.822 162.793 250.352 1.00 23.62 ? 3943 ALA A C     1 
ATOM   18233 O  O     . ALA A 1 3943 ? 163.642 162.426 250.367 1.00 26.56 ? 3943 ALA A O     1 
ATOM   18234 C  CB    . ALA A 1 3943 ? 165.221 164.968 251.528 1.00 19.80 ? 3943 ALA A CB    1 
ATOM   18235 N  N     . PHE A 1 3944 ? 165.603 162.632 249.285 1.00 19.48 ? 3944 PHE A N     1 
ATOM   18236 C  CA    . PHE A 1 3944 ? 165.126 162.011 248.057 1.00 24.79 ? 3944 PHE A CA    1 
ATOM   18237 C  C     . PHE A 1 3944 ? 165.684 160.606 247.860 1.00 27.36 ? 3944 PHE A C     1 
ATOM   18238 O  O     . PHE A 1 3944 ? 165.795 160.147 246.720 1.00 27.33 ? 3944 PHE A O     1 
ATOM   18239 C  CB    . PHE A 1 3944 ? 165.467 162.886 246.848 1.00 24.26 ? 3944 PHE A CB    1 
ATOM   18240 C  CG    . PHE A 1 3944 ? 164.837 164.250 246.883 1.00 22.16 ? 3944 PHE A CG    1 
ATOM   18241 C  CD1   . PHE A 1 3944 ? 163.512 164.423 246.527 1.00 21.12 ? 3944 PHE A CD1   1 
ATOM   18242 C  CD2   . PHE A 1 3944 ? 165.574 165.359 247.262 1.00 20.77 ? 3944 PHE A CD2   1 
ATOM   18243 C  CE1   . PHE A 1 3944 ? 162.931 165.674 246.553 1.00 22.73 ? 3944 PHE A CE1   1 
ATOM   18244 C  CE2   . PHE A 1 3944 ? 164.998 166.613 247.290 1.00 21.83 ? 3944 PHE A CE2   1 
ATOM   18245 C  CZ    . PHE A 1 3944 ? 163.675 166.771 246.936 1.00 21.78 ? 3944 PHE A CZ    1 
ATOM   18246 N  N     . LYS A 1 3945 ? 166.047 159.912 248.943 1.00 25.92 ? 3945 LYS A N     1 
ATOM   18247 C  CA    . LYS A 1 3945 ? 166.561 158.554 248.797 1.00 24.84 ? 3945 LYS A CA    1 
ATOM   18248 C  C     . LYS A 1 3945 ? 165.494 157.619 248.237 1.00 26.19 ? 3945 LYS A C     1 
ATOM   18249 O  O     . LYS A 1 3945 ? 165.786 156.775 247.382 1.00 23.33 ? 3945 LYS A O     1 
ATOM   18250 C  CB    . LYS A 1 3945 ? 167.105 158.040 250.135 1.00 26.87 ? 3945 LYS A CB    1 
ATOM   18251 C  CG    . LYS A 1 3945 ? 166.068 157.816 251.230 1.00 27.24 ? 3945 LYS A CG    1 
ATOM   18252 C  CD    . LYS A 1 3945 ? 166.723 157.330 252.512 1.00 25.52 ? 3945 LYS A CD    1 
ATOM   18253 C  CE    . LYS A 1 3945 ? 165.703 157.143 253.625 1.00 29.77 ? 3945 LYS A CE    1 
ATOM   18254 N  NZ    . LYS A 1 3945 ? 164.753 156.035 253.333 1.00 34.26 ? 3945 LYS A NZ    1 
ATOM   18255 N  N     . ASP A 1 3946 ? 164.253 157.758 248.699 1.00 24.22 ? 3946 ASP A N     1 
ATOM   18256 C  CA    . ASP A 1 3946 ? 163.132 156.978 248.174 1.00 22.40 ? 3946 ASP A CA    1 
ATOM   18257 C  C     . ASP A 1 3946 ? 162.380 157.763 247.094 1.00 26.95 ? 3946 ASP A C     1 
ATOM   18258 O  O     . ASP A 1 3946 ? 161.161 157.933 247.126 1.00 25.98 ? 3946 ASP A O     1 
ATOM   18259 C  CB    . ASP A 1 3946 ? 162.214 156.548 249.316 1.00 22.69 ? 3946 ASP A CB    1 
ATOM   18260 C  CG    . ASP A 1 3946 ? 161.583 157.722 250.048 1.00 37.13 ? 3946 ASP A CG    1 
ATOM   18261 O  OD1   . ASP A 1 3946 ? 161.880 158.888 249.708 1.00 37.34 ? 3946 ASP A OD1   1 
ATOM   18262 O  OD2   . ASP A 1 3946 ? 160.781 157.476 250.973 1.00 35.38 ? 3946 ASP A OD2   1 
ATOM   18263 N  N     . LEU A 1 3947 ? 163.142 158.228 246.104 1.00 29.23 ? 3947 LEU A N     1 
ATOM   18264 C  CA    . LEU A 1 3947 ? 162.596 159.052 245.032 1.00 23.40 ? 3947 LEU A CA    1 
ATOM   18265 C  C     . LEU A 1 3947 ? 161.947 158.218 243.932 1.00 26.14 ? 3947 LEU A C     1 
ATOM   18266 O  O     . LEU A 1 3947 ? 160.838 158.530 243.490 1.00 27.59 ? 3947 LEU A O     1 
ATOM   18267 C  CB    . LEU A 1 3947 ? 163.701 159.935 244.444 1.00 21.96 ? 3947 LEU A CB    1 
ATOM   18268 C  CG    . LEU A 1 3947 ? 163.311 160.983 243.400 1.00 25.55 ? 3947 LEU A CG    1 
ATOM   18269 C  CD1   . LEU A 1 3947 ? 162.288 161.941 243.958 1.00 18.51 ? 3947 LEU A CD1   1 
ATOM   18270 C  CD2   . LEU A 1 3947 ? 164.542 161.741 242.946 1.00 23.82 ? 3947 LEU A CD2   1 
ATOM   18271 N  N     . ILE A 1 3948 ? 162.628 157.161 243.478 1.00 22.23 ? 3948 ILE A N     1 
ATOM   18272 C  CA    . ILE A 1 3948 ? 162.086 156.325 242.410 1.00 23.33 ? 3948 ILE A CA    1 
ATOM   18273 C  C     . ILE A 1 3948 ? 160.786 155.668 242.855 1.00 25.49 ? 3948 ILE A C     1 
ATOM   18274 O  O     . ILE A 1 3948 ? 159.813 155.600 242.094 1.00 25.75 ? 3948 ILE A O     1 
ATOM   18275 C  CB    . ILE A 1 3948 ? 163.127 155.278 241.969 1.00 25.29 ? 3948 ILE A CB    1 
ATOM   18276 C  CG1   . ILE A 1 3948 ? 164.287 155.951 241.237 1.00 20.06 ? 3948 ILE A CG1   1 
ATOM   18277 C  CG2   . ILE A 1 3948 ? 162.486 154.213 241.089 1.00 26.37 ? 3948 ILE A CG2   1 
ATOM   18278 C  CD1   . ILE A 1 3948 ? 165.343 154.989 240.757 1.00 25.80 ? 3948 ILE A CD1   1 
ATOM   18279 N  N     . ALA A 1 3949 ? 160.752 155.173 244.094 1.00 24.30 ? 3949 ALA A N     1 
ATOM   18280 C  CA    . ALA A 1 3949 ? 159.543 154.539 244.607 1.00 23.27 ? 3949 ALA A CA    1 
ATOM   18281 C  C     . ALA A 1 3949 ? 158.394 155.531 244.715 1.00 27.55 ? 3949 ALA A C     1 
ATOM   18282 O  O     . ALA A 1 3949 ? 157.253 155.210 244.363 1.00 31.13 ? 3949 ALA A O     1 
ATOM   18283 C  CB    . ALA A 1 3949 ? 159.826 153.894 245.963 1.00 19.38 ? 3949 ALA A CB    1 
ATOM   18284 N  N     . LYS A 1 3950 ? 158.672 156.743 245.204 1.00 27.81 ? 3950 LYS A N     1 
ATOM   18285 C  CA    . LYS A 1 3950 ? 157.607 157.721 245.406 1.00 25.34 ? 3950 LYS A CA    1 
ATOM   18286 C  C     . LYS A 1 3950 ? 156.956 158.114 244.084 1.00 27.32 ? 3950 LYS A C     1 
ATOM   18287 O  O     . LYS A 1 3950 ? 155.734 158.288 244.014 1.00 27.35 ? 3950 LYS A O     1 
ATOM   18288 C  CB    . LYS A 1 3950 ? 158.148 158.952 246.130 1.00 26.75 ? 3950 LYS A CB    1 
ATOM   18289 C  CG    . LYS A 1 3950 ? 157.822 158.980 247.614 1.00 23.15 ? 3950 LYS A CG    1 
ATOM   18290 C  CD    . LYS A 1 3950 ? 158.651 160.022 248.347 1.00 23.67 ? 3950 LYS A CD    1 
ATOM   18291 C  CE    . LYS A 1 3950 ? 158.337 160.029 249.831 1.00 27.97 ? 3950 LYS A CE    1 
ATOM   18292 N  NZ    . LYS A 1 3950 ? 158.541 158.688 250.447 1.00 30.79 ? 3950 LYS A NZ    1 
ATOM   18293 N  N     . VAL A 1 3951 ? 157.759 158.274 243.030 1.00 25.92 ? 3951 VAL A N     1 
ATOM   18294 C  CA    . VAL A 1 3951 ? 157.196 158.531 241.708 1.00 23.41 ? 3951 VAL A CA    1 
ATOM   18295 C  C     . VAL A 1 3951 ? 156.392 157.332 241.224 1.00 27.49 ? 3951 VAL A C     1 
ATOM   18296 O  O     . VAL A 1 3951 ? 155.274 157.482 240.714 1.00 36.05 ? 3951 VAL A O     1 
ATOM   18297 C  CB    . VAL A 1 3951 ? 158.311 158.901 240.714 1.00 21.90 ? 3951 VAL A CB    1 
ATOM   18298 C  CG1   . VAL A 1 3951 ? 157.740 159.053 239.318 1.00 21.91 ? 3951 VAL A CG1   1 
ATOM   18299 C  CG2   . VAL A 1 3951 ? 158.998 160.182 241.147 1.00 24.86 ? 3951 VAL A CG2   1 
ATOM   18300 N  N     . GLN A 1 3952 ? 156.941 156.125 241.377 1.00 26.47 ? 3952 GLN A N     1 
ATOM   18301 C  CA    . GLN A 1 3952 ? 156.229 154.930 240.936 1.00 28.00 ? 3952 GLN A CA    1 
ATOM   18302 C  C     . GLN A 1 3952 ? 154.950 154.719 241.738 1.00 26.88 ? 3952 GLN A C     1 
ATOM   18303 O  O     . GLN A 1 3952 ? 153.921 154.321 241.182 1.00 31.03 ? 3952 GLN A O     1 
ATOM   18304 C  CB    . GLN A 1 3952 ? 157.142 153.708 241.037 1.00 25.16 ? 3952 GLN A CB    1 
ATOM   18305 C  CG    . GLN A 1 3952 ? 158.092 153.553 239.862 1.00 27.06 ? 3952 GLN A CG    1 
ATOM   18306 C  CD    . GLN A 1 3952 ? 159.235 152.603 240.154 1.00 31.51 ? 3952 GLN A CD    1 
ATOM   18307 O  OE1   . GLN A 1 3952 ? 159.413 152.157 241.287 1.00 32.18 ? 3952 GLN A OE1   1 
ATOM   18308 N  NE2   . GLN A 1 3952 ? 160.016 152.285 239.129 1.00 27.67 ? 3952 GLN A NE2   1 
ATOM   18309 N  N     . ALA A 1 3953 ? 154.993 154.988 243.045 1.00 25.45 ? 3953 ALA A N     1 
ATOM   18310 C  CA    . ALA A 1 3953 ? 153.798 154.855 243.868 1.00 28.51 ? 3953 ALA A CA    1 
ATOM   18311 C  C     . ALA A 1 3953 ? 152.743 155.904 243.540 1.00 30.18 ? 3953 ALA A C     1 
ATOM   18312 O  O     . ALA A 1 3953 ? 151.585 155.741 243.933 1.00 35.10 ? 3953 ALA A O     1 
ATOM   18313 C  CB    . ALA A 1 3953 ? 154.166 154.934 245.350 1.00 25.32 ? 3953 ALA A CB    1 
ATOM   18314 N  N     . ASP A 1 3954 ? 153.114 156.971 242.835 1.00 30.40 ? 3954 ASP A N     1 
ATOM   18315 C  CA    . ASP A 1 3954 ? 152.194 158.055 242.498 1.00 30.17 ? 3954 ASP A CA    1 
ATOM   18316 C  C     . ASP A 1 3954 ? 151.868 157.977 241.010 1.00 30.79 ? 3954 ASP A C     1 
ATOM   18317 O  O     . ASP A 1 3954 ? 152.658 158.407 240.166 1.00 33.61 ? 3954 ASP A O     1 
ATOM   18318 C  CB    . ASP A 1 3954 ? 152.800 159.407 242.862 1.00 29.16 ? 3954 ASP A CB    1 
ATOM   18319 C  CG    . ASP A 1 3954 ? 151.809 160.546 242.725 1.00 31.54 ? 3954 ASP A CG    1 
ATOM   18320 O  OD1   . ASP A 1 3954 ? 150.610 160.272 242.514 1.00 30.23 ? 3954 ASP A OD1   1 
ATOM   18321 O  OD2   . ASP A 1 3954 ? 152.232 161.717 242.823 1.00 36.44 ? 3954 ASP A OD2   1 
ATOM   18322 N  N     . GLU A 1 3955 ? 150.694 157.431 240.688 1.00 30.17 ? 3955 GLU A N     1 
ATOM   18323 C  CA    . GLU A 1 3955 ? 150.239 157.425 239.303 1.00 32.50 ? 3955 GLU A CA    1 
ATOM   18324 C  C     . GLU A 1 3955 ? 149.768 158.801 238.851 1.00 35.34 ? 3955 GLU A C     1 
ATOM   18325 O  O     . GLU A 1 3955 ? 149.758 159.073 237.646 1.00 33.95 ? 3955 GLU A O     1 
ATOM   18326 C  CB    . GLU A 1 3955 ? 149.119 156.398 239.110 1.00 29.47 ? 3955 GLU A CB    1 
ATOM   18327 C  CG    . GLU A 1 3955 ? 147.963 156.519 240.094 1.00 29.37 ? 3955 GLU A CG    1 
ATOM   18328 C  CD    . GLU A 1 3955 ? 148.239 155.833 241.418 1.00 37.69 ? 3955 GLU A CD    1 
ATOM   18329 O  OE1   . GLU A 1 3955 ? 149.327 155.236 241.566 1.00 35.51 ? 3955 GLU A OE1   1 
ATOM   18330 O  OE2   . GLU A 1 3955 ? 147.368 155.889 242.311 1.00 34.58 ? 3955 GLU A OE2   1 
ATOM   18331 N  N     . GLN A 1 3956 ? 149.379 159.670 239.787 1.00 29.95 ? 3956 GLN A N     1 
ATOM   18332 C  CA    . GLN A 1 3956 ? 149.044 161.048 239.451 1.00 28.43 ? 3956 GLN A CA    1 
ATOM   18333 C  C     . GLN A 1 3956 ? 150.271 161.872 239.086 1.00 27.22 ? 3956 GLN A C     1 
ATOM   18334 O  O     . GLN A 1 3956 ? 150.118 163.000 238.605 1.00 24.81 ? 3956 GLN A O     1 
ATOM   18335 C  CB    . GLN A 1 3956 ? 148.304 161.721 240.611 1.00 25.39 ? 3956 GLN A CB    1 
ATOM   18336 C  CG    . GLN A 1 3956 ? 146.872 161.244 240.839 1.00 29.80 ? 3956 GLN A CG    1 
ATOM   18337 C  CD    . GLN A 1 3956 ? 146.784 159.798 241.287 1.00 34.71 ? 3956 GLN A CD    1 
ATOM   18338 O  OE1   . GLN A 1 3956 ? 147.493 159.374 242.200 1.00 33.90 ? 3956 GLN A OE1   1 
ATOM   18339 N  NE2   . GLN A 1 3956 ? 145.905 159.034 240.650 1.00 36.41 ? 3956 GLN A NE2   1 
ATOM   18340 N  N     . PHE A 1 3957 ? 151.475 161.341 239.310 1.00 25.41 ? 3957 PHE A N     1 
ATOM   18341 C  CA    . PHE A 1 3957 ? 152.689 162.057 238.935 1.00 25.27 ? 3957 PHE A CA    1 
ATOM   18342 C  C     . PHE A 1 3957 ? 152.758 162.297 237.433 1.00 23.49 ? 3957 PHE A C     1 
ATOM   18343 O  O     . PHE A 1 3957 ? 153.353 163.287 236.991 1.00 27.94 ? 3957 PHE A O     1 
ATOM   18344 C  CB    . PHE A 1 3957 ? 153.917 161.280 239.411 1.00 20.15 ? 3957 PHE A CB    1 
ATOM   18345 C  CG    . PHE A 1 3957 ? 155.195 162.057 239.330 1.00 21.30 ? 3957 PHE A CG    1 
ATOM   18346 C  CD1   . PHE A 1 3957 ? 155.575 162.895 240.363 1.00 22.57 ? 3957 PHE A CD1   1 
ATOM   18347 C  CD2   . PHE A 1 3957 ? 156.024 161.942 238.227 1.00 13.88 ? 3957 PHE A CD2   1 
ATOM   18348 C  CE1   . PHE A 1 3957 ? 156.751 163.608 240.295 1.00 21.31 ? 3957 PHE A CE1   1 
ATOM   18349 C  CE2   . PHE A 1 3957 ? 157.202 162.652 238.155 1.00 16.68 ? 3957 PHE A CE2   1 
ATOM   18350 C  CZ    . PHE A 1 3957 ? 157.565 163.487 239.191 1.00 16.35 ? 3957 PHE A CZ    1 
ATOM   18351 N  N     . GLY A 1 3958 ? 152.159 161.411 236.636 1.00 21.11 ? 3958 GLY A N     1 
ATOM   18352 C  CA    . GLY A 1 3958 ? 152.138 161.620 235.198 1.00 15.61 ? 3958 GLY A CA    1 
ATOM   18353 C  C     . GLY A 1 3958 ? 151.348 162.850 234.798 1.00 23.18 ? 3958 GLY A C     1 
ATOM   18354 O  O     . GLY A 1 3958 ? 151.733 163.571 233.873 1.00 24.38 ? 3958 GLY A O     1 
ATOM   18355 N  N     . ILE A 1 3959 ? 150.231 163.105 235.482 1.00 23.05 ? 3959 ILE A N     1 
ATOM   18356 C  CA    . ILE A 1 3959 ? 149.430 164.289 235.183 1.00 17.80 ? 3959 ILE A CA    1 
ATOM   18357 C  C     . ILE A 1 3959 ? 150.188 165.559 235.552 1.00 23.77 ? 3959 ILE A C     1 
ATOM   18358 O  O     . ILE A 1 3959 ? 150.227 166.521 234.776 1.00 32.10 ? 3959 ILE A O     1 
ATOM   18359 C  CB    . ILE A 1 3959 ? 148.073 164.207 235.903 1.00 19.84 ? 3959 ILE A CB    1 
ATOM   18360 C  CG1   . ILE A 1 3959 ? 147.290 162.984 235.426 1.00 25.80 ? 3959 ILE A CG1   1 
ATOM   18361 C  CG2   . ILE A 1 3959 ? 147.271 165.477 235.679 1.00 16.62 ? 3959 ILE A CG2   1 
ATOM   18362 C  CD1   . ILE A 1 3959 ? 147.068 162.947 233.930 1.00 21.22 ? 3959 ILE A CD1   1 
ATOM   18363 N  N     . TRP A 1 3960 ? 150.800 165.585 236.739 1.00 24.48 ? 3960 TRP A N     1 
ATOM   18364 C  CA    . TRP A 1 3960 ? 151.561 166.758 237.154 1.00 15.57 ? 3960 TRP A CA    1 
ATOM   18365 C  C     . TRP A 1 3960 ? 152.773 166.985 236.261 1.00 15.90 ? 3960 TRP A C     1 
ATOM   18366 O  O     . TRP A 1 3960 ? 153.156 168.134 236.017 1.00 22.45 ? 3960 TRP A O     1 
ATOM   18367 C  CB    . TRP A 1 3960 ? 151.999 166.618 238.612 1.00 18.79 ? 3960 TRP A CB    1 
ATOM   18368 C  CG    . TRP A 1 3960 ? 152.975 167.672 239.054 1.00 18.26 ? 3960 TRP A CG    1 
ATOM   18369 C  CD1   . TRP A 1 3960 ? 152.680 168.908 239.542 1.00 15.81 ? 3960 TRP A CD1   1 
ATOM   18370 C  CD2   . TRP A 1 3960 ? 154.405 167.576 239.044 1.00 15.87 ? 3960 TRP A CD2   1 
ATOM   18371 N  NE1   . TRP A 1 3960 ? 153.833 169.590 239.837 1.00 15.92 ? 3960 TRP A NE1   1 
ATOM   18372 C  CE2   . TRP A 1 3960 ? 154.907 168.794 239.538 1.00 14.43 ? 3960 TRP A CE2   1 
ATOM   18373 C  CE3   . TRP A 1 3960 ? 155.308 166.580 238.665 1.00 12.91 ? 3960 TRP A CE3   1 
ATOM   18374 C  CZ2   . TRP A 1 3960 ? 156.271 169.043 239.665 1.00 16.69 ? 3960 TRP A CZ2   1 
ATOM   18375 C  CZ3   . TRP A 1 3960 ? 156.660 166.829 238.791 1.00 13.40 ? 3960 TRP A CZ3   1 
ATOM   18376 C  CH2   . TRP A 1 3960 ? 157.130 168.050 239.286 1.00 18.59 ? 3960 TRP A CH2   1 
ATOM   18377 N  N     . LEU A 1 3961 ? 153.382 165.907 235.766 1.00 20.19 ? 3961 LEU A N     1 
ATOM   18378 C  CA    . LEU A 1 3961 ? 154.570 166.033 234.930 1.00 18.58 ? 3961 LEU A CA    1 
ATOM   18379 C  C     . LEU A 1 3961 ? 154.282 166.740 233.612 1.00 20.65 ? 3961 LEU A C     1 
ATOM   18380 O  O     . LEU A 1 3961 ? 155.194 167.338 233.030 1.00 23.34 ? 3961 LEU A O     1 
ATOM   18381 C  CB    . LEU A 1 3961 ? 155.166 164.649 234.665 1.00 16.25 ? 3961 LEU A CB    1 
ATOM   18382 C  CG    . LEU A 1 3961 ? 156.554 164.607 234.027 1.00 20.94 ? 3961 LEU A CG    1 
ATOM   18383 C  CD1   . LEU A 1 3961 ? 157.576 165.223 234.958 1.00 17.61 ? 3961 LEU A CD1   1 
ATOM   18384 C  CD2   . LEU A 1 3961 ? 156.942 163.182 233.670 1.00 20.01 ? 3961 LEU A CD2   1 
ATOM   18385 N  N     . ASP A 1 3962 ? 153.043 166.691 233.127 1.00 20.09 ? 3962 ASP A N     1 
ATOM   18386 C  CA    . ASP A 1 3962 ? 152.680 167.293 231.850 1.00 20.77 ? 3962 ASP A CA    1 
ATOM   18387 C  C     . ASP A 1 3962 ? 151.682 168.433 232.024 1.00 23.78 ? 3962 ASP A C     1 
ATOM   18388 O  O     . ASP A 1 3962 ? 150.849 168.676 231.151 1.00 28.83 ? 3962 ASP A O     1 
ATOM   18389 C  CB    . ASP A 1 3962 ? 152.128 166.234 230.897 1.00 21.19 ? 3962 ASP A CB    1 
ATOM   18390 C  CG    . ASP A 1 3962 ? 153.093 165.087 230.685 1.00 25.03 ? 3962 ASP A CG    1 
ATOM   18391 O  OD1   . ASP A 1 3962 ? 154.218 165.338 230.207 1.00 26.71 ? 3962 ASP A OD1   1 
ATOM   18392 O  OD2   . ASP A 1 3962 ? 152.728 163.935 230.998 1.00 28.21 ? 3962 ASP A OD2   1 
ATOM   18393 N  N     . SER A 1 3963 ? 151.756 169.139 233.147 1.00 25.58 ? 3963 SER A N     1 
ATOM   18394 C  CA    . SER A 1 3963 ? 150.912 170.295 233.401 1.00 19.43 ? 3963 SER A CA    1 
ATOM   18395 C  C     . SER A 1 3963 ? 151.621 171.573 232.969 1.00 19.51 ? 3963 SER A C     1 
ATOM   18396 O  O     . SER A 1 3963 ? 152.850 171.628 232.862 1.00 23.34 ? 3963 SER A O     1 
ATOM   18397 C  CB    . SER A 1 3963 ? 150.531 170.374 234.881 1.00 18.90 ? 3963 SER A CB    1 
ATOM   18398 O  OG    . SER A 1 3963 ? 151.677 170.511 235.700 1.00 23.22 ? 3963 SER A OG    1 
ATOM   18399 N  N     . SER A 1 3964 ? 150.820 172.608 232.710 1.00 20.36 ? 3964 SER A N     1 
ATOM   18400 C  CA    . SER A 1 3964 ? 151.366 173.873 232.231 1.00 14.40 ? 3964 SER A CA    1 
ATOM   18401 C  C     . SER A 1 3964 ? 152.232 174.546 233.289 1.00 18.76 ? 3964 SER A C     1 
ATOM   18402 O  O     . SER A 1 3964 ? 153.270 175.134 232.967 1.00 18.24 ? 3964 SER A O     1 
ATOM   18403 C  CB    . SER A 1 3964 ? 150.234 174.802 231.797 1.00 12.31 ? 3964 SER A CB    1 
ATOM   18404 O  OG    . SER A 1 3964 ? 149.394 175.121 232.890 1.00 15.68 ? 3964 SER A OG    1 
ATOM   18405 N  N     . SER A 1 3965 ? 151.821 174.476 234.552 1.00 18.93 ? 3965 SER A N     1 
ATOM   18406 C  CA    . SER A 1 3965 ? 152.516 175.143 235.652 1.00 14.70 ? 3965 SER A CA    1 
ATOM   18407 C  C     . SER A 1 3965 ? 152.772 174.139 236.767 1.00 16.16 ? 3965 SER A C     1 
ATOM   18408 O  O     . SER A 1 3965 ? 152.174 174.220 237.845 1.00 22.34 ? 3965 SER A O     1 
ATOM   18409 C  CB    . SER A 1 3965 ? 151.704 176.334 236.162 1.00 17.89 ? 3965 SER A CB    1 
ATOM   18410 O  OG    . SER A 1 3965 ? 151.437 177.253 235.118 1.00 18.18 ? 3965 SER A OG    1 
ATOM   18411 N  N     . PRO A 1 3966 ? 153.673 173.177 236.543 1.00 11.93 ? 3966 PRO A N     1 
ATOM   18412 C  CA    . PRO A 1 3966 ? 153.953 172.181 237.586 1.00 13.66 ? 3966 PRO A CA    1 
ATOM   18413 C  C     . PRO A 1 3966 ? 154.618 172.763 238.820 1.00 16.84 ? 3966 PRO A C     1 
ATOM   18414 O  O     . PRO A 1 3966 ? 154.627 172.102 239.865 1.00 22.87 ? 3966 PRO A O     1 
ATOM   18415 C  CB    . PRO A 1 3966 ? 154.873 171.182 236.873 1.00 13.80 ? 3966 PRO A CB    1 
ATOM   18416 C  CG    . PRO A 1 3966 ? 155.565 172.004 235.852 1.00 11.09 ? 3966 PRO A CG    1 
ATOM   18417 C  CD    . PRO A 1 3966 ? 154.542 172.994 235.367 1.00 13.27 ? 3966 PRO A CD    1 
ATOM   18418 N  N     . GLU A 1 3967 ? 155.179 173.971 238.734 1.00 13.38 ? 3967 GLU A N     1 
ATOM   18419 C  CA    . GLU A 1 3967 ? 155.889 174.562 239.862 1.00 12.48 ? 3967 GLU A CA    1 
ATOM   18420 C  C     . GLU A 1 3967 ? 154.952 175.042 240.961 1.00 15.49 ? 3967 GLU A C     1 
ATOM   18421 O  O     . GLU A 1 3967 ? 155.402 175.247 242.093 1.00 23.01 ? 3967 GLU A O     1 
ATOM   18422 C  CB    . GLU A 1 3967 ? 156.758 175.726 239.386 1.00 9.43  ? 3967 GLU A CB    1 
ATOM   18423 C  CG    . GLU A 1 3967 ? 155.965 176.936 238.924 1.00 13.05 ? 3967 GLU A CG    1 
ATOM   18424 C  CD    . GLU A 1 3967 ? 155.481 176.808 237.493 1.00 13.76 ? 3967 GLU A CD    1 
ATOM   18425 O  OE1   . GLU A 1 3967 ? 155.919 175.869 236.798 1.00 14.28 ? 3967 GLU A OE1   1 
ATOM   18426 O  OE2   . GLU A 1 3967 ? 154.654 177.638 237.066 1.00 18.57 ? 3967 GLU A OE2   1 
ATOM   18427 N  N     . GLN A 1 3968 ? 153.671 175.236 240.659 1.00 14.57 ? 3968 GLN A N     1 
ATOM   18428 C  CA    . GLN A 1 3968 ? 152.718 175.711 241.651 1.00 14.76 ? 3968 GLN A CA    1 
ATOM   18429 C  C     . GLN A 1 3968 ? 152.024 174.586 242.405 1.00 18.28 ? 3968 GLN A C     1 
ATOM   18430 O  O     . GLN A 1 3968 ? 151.344 174.859 243.401 1.00 21.39 ? 3968 GLN A O     1 
ATOM   18431 C  CB    . GLN A 1 3968 ? 151.664 176.601 240.987 1.00 16.61 ? 3968 GLN A CB    1 
ATOM   18432 C  CG    . GLN A 1 3968 ? 152.235 177.813 240.272 1.00 16.95 ? 3968 GLN A CG    1 
ATOM   18433 C  CD    . GLN A 1 3968 ? 151.169 178.623 239.567 1.00 25.67 ? 3968 GLN A CD    1 
ATOM   18434 O  OE1   . GLN A 1 3968 ? 149.987 178.286 239.613 1.00 30.82 ? 3968 GLN A OE1   1 
ATOM   18435 N  NE2   . GLN A 1 3968 ? 151.581 179.699 238.909 1.00 23.51 ? 3968 GLN A NE2   1 
ATOM   18436 N  N     . THR A 1 3969 ? 152.171 173.342 241.961 1.00 18.53 ? 3969 THR A N     1 
ATOM   18437 C  CA    . THR A 1 3969 ? 151.536 172.187 242.586 1.00 15.74 ? 3969 THR A CA    1 
ATOM   18438 C  C     . THR A 1 3969 ? 152.519 171.031 242.695 1.00 18.12 ? 3969 THR A C     1 
ATOM   18439 O  O     . THR A 1 3969 ? 152.169 169.874 242.453 1.00 22.62 ? 3969 THR A O     1 
ATOM   18440 C  CB    . THR A 1 3969 ? 150.294 171.750 241.814 1.00 22.23 ? 3969 THR A CB    1 
ATOM   18441 O  OG1   . THR A 1 3969 ? 150.653 171.442 240.462 1.00 22.64 ? 3969 THR A OG1   1 
ATOM   18442 C  CG2   . THR A 1 3969 ? 149.228 172.842 241.825 1.00 18.44 ? 3969 THR A CG2   1 
ATOM   18443 N  N     . VAL A 1 3970 ? 153.778 171.364 242.997 1.00 22.70 ? 3970 VAL A N     1 
ATOM   18444 C  CA    . VAL A 1 3970 ? 154.844 170.321 243.089 1.00 17.78 ? 3970 VAL A CA    1 
ATOM   18445 C  C     . VAL A 1 3970 ? 154.448 169.321 244.184 1.00 20.23 ? 3970 VAL A C     1 
ATOM   18446 O  O     . VAL A 1 3970 ? 154.276 169.749 245.345 1.00 24.70 ? 3970 VAL A O     1 
ATOM   18447 C  CB    . VAL A 1 3970 ? 156.229 170.935 243.369 1.00 15.47 ? 3970 VAL A CB    1 
ATOM   18448 C  CG1   . VAL A 1 3970 ? 157.317 169.869 243.431 1.00 18.46 ? 3970 VAL A CG1   1 
ATOM   18449 C  CG2   . VAL A 1 3970 ? 156.591 172.011 242.355 1.00 12.54 ? 3970 VAL A CG2   1 
ATOM   18450 N  N     . PRO A 1 3971 ? 154.297 168.019 243.864 1.00 25.62 ? 3971 PRO A N     1 
ATOM   18451 C  CA    . PRO A 1 3971 ? 153.862 167.046 244.854 1.00 23.62 ? 3971 PRO A CA    1 
ATOM   18452 C  C     . PRO A 1 3971 ? 154.868 166.911 245.984 1.00 25.30 ? 3971 PRO A C     1 
ATOM   18453 O  O     . PRO A 1 3971 ? 156.083 167.043 245.731 1.00 30.73 ? 3971 PRO A O     1 
ATOM   18454 C  CB    . PRO A 1 3971 ? 153.736 165.753 244.033 1.00 19.09 ? 3971 PRO A CB    1 
ATOM   18455 C  CG    . PRO A 1 3971 ? 154.670 165.967 242.864 1.00 19.43 ? 3971 PRO A CG    1 
ATOM   18456 C  CD    . PRO A 1 3971 ? 154.549 167.448 242.552 1.00 17.37 ? 3971 PRO A CD    1 
ATOM   18457 N  N     . TYR A 1 3972 ? 154.384 166.649 247.200 1.00 23.44 ? 3972 TYR A N     1 
ATOM   18458 C  CA    . TYR A 1 3972 ? 155.301 166.421 248.349 1.00 23.21 ? 3972 TYR A CA    1 
ATOM   18459 C  C     . TYR A 1 3972 ? 155.966 165.069 248.135 1.00 26.33 ? 3972 TYR A C     1 
ATOM   18460 O  O     . TYR A 1 3972 ? 155.551 164.079 248.775 1.00 34.57 ? 3972 TYR A O     1 
ATOM   18461 C  CB    . TYR A 1 3972 ? 154.490 166.497 249.646 1.00 24.46 ? 3972 TYR A CB    1 
ATOM   18462 C  CG    . TYR A 1 3972 ? 155.294 166.283 250.920 1.00 26.69 ? 3972 TYR A CG    1 
ATOM   18463 C  CD1   . TYR A 1 3972 ? 156.623 166.680 251.008 1.00 25.45 ? 3972 TYR A CD1   1 
ATOM   18464 C  CD2   . TYR A 1 3972 ? 154.722 165.678 252.032 1.00 26.33 ? 3972 TYR A CD2   1 
ATOM   18465 C  CE1   . TYR A 1 3972 ? 157.355 166.487 252.168 1.00 25.52 ? 3972 TYR A CE1   1 
ATOM   18466 C  CE2   . TYR A 1 3972 ? 155.444 165.478 253.195 1.00 27.34 ? 3972 TYR A CE2   1 
ATOM   18467 C  CZ    . TYR A 1 3972 ? 156.764 165.883 253.263 1.00 26.76 ? 3972 TYR A CZ    1 
ATOM   18468 O  OH    . TYR A 1 3972 ? 157.475 165.684 254.409 1.00 32.46 ? 3972 TYR A OH    1 
ATOM   18469 N  N     . LEU A 1 3973 ? 156.969 165.021 247.256 1.00 25.13 ? 3973 LEU A N     1 
ATOM   18470 C  CA    . LEU A 1 3973 ? 157.616 163.730 246.906 1.00 21.68 ? 3973 LEU A CA    1 
ATOM   18471 C  C     . LEU A 1 3973 ? 158.978 163.602 247.609 1.00 24.62 ? 3973 LEU A C     1 
ATOM   18472 O  O     . LEU A 1 3973 ? 159.826 162.831 247.109 1.00 26.30 ? 3973 LEU A O     1 
ATOM   18473 C  CB    . LEU A 1 3973 ? 157.755 163.709 245.387 1.00 20.01 ? 3973 LEU A CB    1 
ATOM   18474 C  CG    . LEU A 1 3973 ? 157.890 162.332 244.731 1.00 24.80 ? 3973 LEU A CG    1 
ATOM   18475 C  CD1   . LEU A 1 3973 ? 156.556 161.609 244.736 1.00 22.14 ? 3973 LEU A CD1   1 
ATOM   18476 C  CD2   . LEU A 1 3973 ? 158.401 162.507 243.314 1.00 24.20 ? 3973 LEU A CD2   1 
ATOM   18477 N  N     . TRP A 1 3974 ? 159.182 164.326 248.714 1.00 22.83 ? 3974 TRP A N     1 
ATOM   18478 C  CA    . TRP A 1 3974 ? 160.452 164.199 249.479 1.00 21.87 ? 3974 TRP A CA    1 
ATOM   18479 C  C     . TRP A 1 3974 ? 160.162 163.759 250.916 1.00 25.59 ? 3974 TRP A C     1 
ATOM   18480 O  O     . TRP A 1 3974 ? 159.174 164.246 251.508 1.00 27.53 ? 3974 TRP A O     1 
ATOM   18481 C  CB    . TRP A 1 3974 ? 161.250 165.511 249.445 1.00 21.98 ? 3974 TRP A CB    1 
ATOM   18482 C  CG    . TRP A 1 3974 ? 160.579 166.669 250.133 1.00 21.19 ? 3974 TRP A CG    1 
ATOM   18483 C  CD1   . TRP A 1 3974 ? 160.707 167.034 251.442 1.00 20.98 ? 3974 TRP A CD1   1 
ATOM   18484 C  CD2   . TRP A 1 3974 ? 159.681 167.628 249.534 1.00 21.39 ? 3974 TRP A CD2   1 
ATOM   18485 N  NE1   . TRP A 1 3974 ? 159.951 168.146 251.701 1.00 23.47 ? 3974 TRP A NE1   1 
ATOM   18486 C  CE2   . TRP A 1 3974 ? 159.311 168.534 250.552 1.00 23.78 ? 3974 TRP A CE2   1 
ATOM   18487 C  CE3   . TRP A 1 3974 ? 159.158 167.807 248.250 1.00 20.21 ? 3974 TRP A CE3   1 
ATOM   18488 C  CZ2   . TRP A 1 3974 ? 158.443 169.597 250.318 1.00 21.47 ? 3974 TRP A CZ2   1 
ATOM   18489 C  CZ3   . TRP A 1 3974 ? 158.299 168.859 248.021 1.00 21.55 ? 3974 TRP A CZ3   1 
ATOM   18490 C  CH2   . TRP A 1 3974 ? 157.949 169.741 249.043 1.00 19.88 ? 3974 TRP A CH2   1 
ATOM   18491 N  N     . SER A 1 3975 ? 160.997 162.868 251.457 1.00 23.87 ? 3975 SER A N     1 
ATOM   18492 C  CA    . SER A 1 3975 ? 160.807 162.376 252.848 1.00 28.16 ? 3975 SER A CA    1 
ATOM   18493 C  C     . SER A 1 3975 ? 161.536 163.299 253.833 1.00 28.01 ? 3975 SER A C     1 
ATOM   18494 O  O     . SER A 1 3975 ? 162.503 163.968 253.407 1.00 27.13 ? 3975 SER A O     1 
ATOM   18495 C  CB    . SER A 1 3975 ? 161.279 160.952 252.984 1.00 29.88 ? 3975 SER A CB    1 
ATOM   18496 O  OG    . SER A 1 3975 ? 162.642 160.834 252.601 1.00 30.03 ? 3975 SER A OG    1 
ATOM   18497 N  N     . GLU A 1 3976 ? 161.091 163.329 255.094 1.00 29.52 ? 3976 GLU A N     1 
ATOM   18498 C  CA    . GLU A 1 3976 ? 161.747 164.170 256.131 1.00 28.56 ? 3976 GLU A CA    1 
ATOM   18499 C  C     . GLU A 1 3976 ? 161.274 163.727 257.524 1.00 34.16 ? 3976 GLU A C     1 
ATOM   18500 O  O     . GLU A 1 3976 ? 160.259 163.000 257.599 1.00 26.83 ? 3976 GLU A O     1 
ATOM   18501 C  CB    . GLU A 1 3976 ? 161.441 165.648 255.894 1.00 27.29 ? 3976 GLU A CB    1 
ATOM   18502 C  CG    . GLU A 1 3976 ? 159.960 165.985 256.036 1.00 24.24 ? 3976 GLU A CG    1 
ATOM   18503 C  CD    . GLU A 1 3976 ? 159.616 167.416 255.665 1.00 30.90 ? 3976 GLU A CD    1 
ATOM   18504 O  OE1   . GLU A 1 3976 ? 159.884 167.803 254.508 1.00 33.13 ? 3976 GLU A OE1   1 
ATOM   18505 O  OE2   . GLU A 1 3976 ? 159.074 168.137 256.526 1.00 30.05 ? 3976 GLU A OE2   1 
ATOM   18506 N  N     . GLU A 1 3977 ? 161.978 164.147 258.580 1.00 33.07 ? 3977 GLU A N     1 
ATOM   18507 C  CA    . GLU A 1 3977 ? 161.612 163.768 259.942 1.00 32.49 ? 3977 GLU A CA    1 
ATOM   18508 C  C     . GLU A 1 3977 ? 160.742 164.833 260.604 1.00 31.38 ? 3977 GLU A C     1 
ATOM   18509 O  O     . GLU A 1 3977 ? 159.599 164.562 260.987 1.00 35.92 ? 3977 GLU A O     1 
ATOM   18510 C  CB    . GLU A 1 3977 ? 162.873 163.511 260.775 1.00 32.39 ? 3977 GLU A CB    1 
ATOM   18511 C  CG    . GLU A 1 3977 ? 163.697 162.315 260.319 1.00 33.83 ? 3977 GLU A CG    1 
ATOM   18512 C  CD    . GLU A 1 3977 ? 164.609 162.639 259.150 1.00 41.07 ? 3977 GLU A CD    1 
ATOM   18513 O  OE1   . GLU A 1 3977 ? 164.638 163.814 258.723 1.00 35.48 ? 3977 GLU A OE1   1 
ATOM   18514 O  OE2   . GLU A 1 3977 ? 165.297 161.720 258.659 1.00 41.16 ? 3977 GLU A OE2   1 
ATOM   18515 N  N     . THR A 1 3978 ? 161.264 166.034 260.741 1.00 33.42 ? 3978 THR A N     1 
ATOM   18516 C  CA    . THR A 1 3978 ? 160.513 167.151 261.292 1.00 32.32 ? 3978 THR A CA    1 
ATOM   18517 C  C     . THR A 1 3978 ? 159.824 167.924 260.170 1.00 31.08 ? 3978 THR A C     1 
ATOM   18518 O  O     . THR A 1 3978 ? 160.304 167.931 259.032 1.00 29.07 ? 3978 THR A O     1 
ATOM   18519 C  CB    . THR A 1 3978 ? 161.441 168.084 262.070 1.00 35.03 ? 3978 THR A CB    1 
ATOM   18520 O  OG1   . THR A 1 3978 ? 160.715 169.236 262.514 1.00 36.32 ? 3978 THR A OG1   1 
ATOM   18521 C  CG2   . THR A 1 3978 ? 162.608 168.529 261.199 1.00 28.02 ? 3978 THR A CG2   1 
ATOM   18522 N  N     . PRO A 1 3979 ? 158.685 168.555 260.451 1.00 32.34 ? 3979 PRO A N     1 
ATOM   18523 C  CA    . PRO A 1 3979 ? 158.031 169.377 259.421 1.00 29.52 ? 3979 PRO A CA    1 
ATOM   18524 C  C     . PRO A 1 3979 ? 158.973 170.453 258.902 1.00 28.90 ? 3979 PRO A C     1 
ATOM   18525 O  O     . PRO A 1 3979 ? 159.648 171.138 259.672 1.00 31.39 ? 3979 PRO A O     1 
ATOM   18526 C  CB    . PRO A 1 3979 ? 156.834 169.978 260.162 1.00 29.04 ? 3979 PRO A CB    1 
ATOM   18527 C  CG    . PRO A 1 3979 ? 156.511 168.970 261.206 1.00 29.58 ? 3979 PRO A CG    1 
ATOM   18528 C  CD    . PRO A 1 3979 ? 157.831 168.381 261.638 1.00 31.77 ? 3979 PRO A CD    1 
ATOM   18529 N  N     . ALA A 1 3980 ? 159.007 170.599 257.580 1.00 29.17 ? 3980 ALA A N     1 
ATOM   18530 C  CA    . ALA A 1 3980 ? 159.934 171.518 256.945 1.00 25.53 ? 3980 ALA A CA    1 
ATOM   18531 C  C     . ALA A 1 3980 ? 159.422 172.952 257.032 1.00 23.00 ? 3980 ALA A C     1 
ATOM   18532 O  O     . ALA A 1 3980 ? 158.257 173.214 257.352 1.00 25.29 ? 3980 ALA A O     1 
ATOM   18533 C  CB    . ALA A 1 3980 ? 160.166 171.125 255.487 1.00 22.32 ? 3980 ALA A CB    1 
ATOM   18534 N  N     . THR A 1 3981 ? 160.308 173.882 256.748 1.00 18.58 ? 3981 THR A N     1 
ATOM   18535 C  CA    . THR A 1 3981 ? 160.009 175.303 256.734 1.00 17.58 ? 3981 THR A CA    1 
ATOM   18536 C  C     . THR A 1 3981 ? 159.537 175.732 255.347 1.00 16.29 ? 3981 THR A C     1 
ATOM   18537 O  O     . THR A 1 3981 ? 159.852 175.076 254.350 1.00 18.03 ? 3981 THR A O     1 
ATOM   18538 C  CB    . THR A 1 3981 ? 161.243 176.108 257.133 1.00 17.89 ? 3981 THR A CB    1 
ATOM   18539 O  OG1   . THR A 1 3981 ? 162.293 175.883 256.185 1.00 20.51 ? 3981 THR A OG1   1 
ATOM   18540 C  CG2   . THR A 1 3981 ? 161.719 175.683 258.510 1.00 14.65 ? 3981 THR A CG2   1 
ATOM   18541 N  N     . PRO A 1 3982 ? 158.771 176.827 255.254 1.00 17.23 ? 3982 PRO A N     1 
ATOM   18542 C  CA    . PRO A 1 3982 ? 158.337 177.294 253.925 1.00 13.78 ? 3982 PRO A CA    1 
ATOM   18543 C  C     . PRO A 1 3982 ? 159.490 177.559 252.974 1.00 13.67 ? 3982 PRO A C     1 
ATOM   18544 O  O     . PRO A 1 3982 ? 159.375 177.280 251.775 1.00 15.16 ? 3982 PRO A O     1 
ATOM   18545 C  CB    . PRO A 1 3982 ? 157.555 178.573 254.247 1.00 13.27 ? 3982 PRO A CB    1 
ATOM   18546 C  CG    . PRO A 1 3982 ? 157.101 178.389 255.651 1.00 8.38  ? 3982 PRO A CG    1 
ATOM   18547 C  CD    . PRO A 1 3982 ? 158.211 177.653 256.336 1.00 17.34 ? 3982 PRO A CD    1 
ATOM   18548 N  N     . ILE A 1 3983 ? 160.605 178.088 253.477 1.00 13.79 ? 3983 ILE A N     1 
ATOM   18549 C  CA    . ILE A 1 3983 ? 161.794 178.238 252.644 1.00 14.08 ? 3983 ILE A CA    1 
ATOM   18550 C  C     . ILE A 1 3983 ? 162.383 176.871 252.314 1.00 13.02 ? 3983 ILE A C     1 
ATOM   18551 O  O     . ILE A 1 3983 ? 162.822 176.620 251.186 1.00 13.39 ? 3983 ILE A O     1 
ATOM   18552 C  CB    . ILE A 1 3983 ? 162.822 179.151 253.336 1.00 12.88 ? 3983 ILE A CB    1 
ATOM   18553 C  CG1   . ILE A 1 3983 ? 162.240 180.554 253.518 1.00 8.68  ? 3983 ILE A CG1   1 
ATOM   18554 C  CG2   . ILE A 1 3983 ? 164.105 179.214 252.533 1.00 9.29  ? 3983 ILE A CG2   1 
ATOM   18555 C  CD1   . ILE A 1 3983 ? 163.060 181.446 254.415 1.00 17.19 ? 3983 ILE A CD1   1 
ATOM   18556 N  N     . GLY A 1 3984 ? 162.397 175.965 253.295 1.00 14.70 ? 3984 GLY A N     1 
ATOM   18557 C  CA    . GLY A 1 3984 ? 162.892 174.624 253.045 1.00 11.61 ? 3984 GLY A CA    1 
ATOM   18558 C  C     . GLY A 1 3984 ? 162.039 173.844 252.065 1.00 16.57 ? 3984 GLY A C     1 
ATOM   18559 O  O     . GLY A 1 3984 ? 162.561 173.047 251.280 1.00 11.66 ? 3984 GLY A O     1 
ATOM   18560 N  N     . GLN A 1 3985 ? 160.720 174.047 252.103 1.00 15.33 ? 3985 GLN A N     1 
ATOM   18561 C  CA    . GLN A 1 3985 ? 159.842 173.391 251.139 1.00 15.24 ? 3985 GLN A CA    1 
ATOM   18562 C  C     . GLN A 1 3985 ? 160.088 173.906 249.727 1.00 14.05 ? 3985 GLN A C     1 
ATOM   18563 O  O     . GLN A 1 3985 ? 160.037 173.137 248.760 1.00 16.95 ? 3985 GLN A O     1 
ATOM   18564 C  CB    . GLN A 1 3985 ? 158.380 173.593 251.531 1.00 14.52 ? 3985 GLN A CB    1 
ATOM   18565 C  CG    . GLN A 1 3985 ? 157.965 172.907 252.814 1.00 20.34 ? 3985 GLN A CG    1 
ATOM   18566 C  CD    . GLN A 1 3985 ? 156.511 173.163 253.156 1.00 27.54 ? 3985 GLN A CD    1 
ATOM   18567 O  OE1   . GLN A 1 3985 ? 155.822 173.912 252.464 1.00 22.89 ? 3985 GLN A OE1   1 
ATOM   18568 N  NE2   . GLN A 1 3985 ? 156.037 172.541 254.229 1.00 30.69 ? 3985 GLN A NE2   1 
ATOM   18569 N  N     . ALA A 1 3986 ? 160.343 175.208 249.588 1.00 15.82 ? 3986 ALA A N     1 
ATOM   18570 C  CA    . ALA A 1 3986 ? 160.615 175.778 248.272 1.00 9.91  ? 3986 ALA A CA    1 
ATOM   18571 C  C     . ALA A 1 3986 ? 161.886 175.193 247.668 1.00 9.45  ? 3986 ALA A C     1 
ATOM   18572 O  O     . ALA A 1 3986 ? 161.942 174.935 246.460 1.00 12.94 ? 3986 ALA A O     1 
ATOM   18573 C  CB    . ALA A 1 3986 ? 160.717 177.299 248.372 1.00 6.12  ? 3986 ALA A CB    1 
ATOM   18574 N  N     . ILE A 1 3987 ? 162.915 174.981 248.490 1.00 8.42  ? 3987 ILE A N     1 
ATOM   18575 C  CA    . ILE A 1 3987 ? 164.168 174.427 247.987 1.00 11.44 ? 3987 ILE A CA    1 
ATOM   18576 C  C     . ILE A 1 3987 ? 163.961 172.998 247.502 1.00 13.20 ? 3987 ILE A C     1 
ATOM   18577 O  O     . ILE A 1 3987 ? 164.530 172.586 246.483 1.00 11.73 ? 3987 ILE A O     1 
ATOM   18578 C  CB    . ILE A 1 3987 ? 165.256 174.510 249.071 1.00 13.05 ? 3987 ILE A CB    1 
ATOM   18579 C  CG1   . ILE A 1 3987 ? 165.531 175.969 249.416 1.00 11.93 ? 3987 ILE A CG1   1 
ATOM   18580 C  CG2   . ILE A 1 3987 ? 166.540 173.863 248.589 1.00 12.05 ? 3987 ILE A CG2   1 
ATOM   18581 C  CD1   . ILE A 1 3987 ? 166.381 176.151 250.629 1.00 14.14 ? 3987 ILE A CD1   1 
ATOM   18582 N  N     . HIS A 1 3988 ? 163.156 172.217 248.224 1.00 15.24 ? 3988 HIS A N     1 
ATOM   18583 C  CA    . HIS A 1 3988 ? 162.836 170.866 247.774 1.00 12.92 ? 3988 HIS A CA    1 
ATOM   18584 C  C     . HIS A 1 3988 ? 162.048 170.889 246.472 1.00 14.08 ? 3988 HIS A C     1 
ATOM   18585 O  O     . HIS A 1 3988 ? 162.307 170.087 245.568 1.00 18.60 ? 3988 HIS A O     1 
ATOM   18586 C  CB    . HIS A 1 3988 ? 162.067 170.120 248.864 1.00 13.43 ? 3988 HIS A CB    1 
ATOM   18587 C  CG    . HIS A 1 3988 ? 162.909 169.737 250.040 1.00 16.70 ? 3988 HIS A CG    1 
ATOM   18588 N  ND1   . HIS A 1 3988 ? 162.432 169.752 251.333 1.00 22.16 ? 3988 HIS A ND1   1 
ATOM   18589 C  CD2   . HIS A 1 3988 ? 164.195 169.327 250.119 1.00 16.92 ? 3988 HIS A CD2   1 
ATOM   18590 C  CE1   . HIS A 1 3988 ? 163.390 169.370 252.158 1.00 17.27 ? 3988 HIS A CE1   1 
ATOM   18591 N  NE2   . HIS A 1 3988 ? 164.471 169.106 251.446 1.00 18.78 ? 3988 HIS A NE2   1 
ATOM   18592 N  N     . ARG A 1 3989 ? 161.076 171.799 246.358 1.00 14.36 ? 3989 ARG A N     1 
ATOM   18593 C  CA    . ARG A 1 3989 ? 160.373 171.954 245.089 1.00 11.82 ? 3989 ARG A CA    1 
ATOM   18594 C  C     . ARG A 1 3989 ? 161.313 172.418 243.985 1.00 8.11  ? 3989 ARG A C     1 
ATOM   18595 O  O     . ARG A 1 3989 ? 161.139 172.034 242.824 1.00 13.91 ? 3989 ARG A O     1 
ATOM   18596 C  CB    . ARG A 1 3989 ? 159.211 172.938 245.226 1.00 8.04  ? 3989 ARG A CB    1 
ATOM   18597 C  CG    . ARG A 1 3989 ? 158.065 172.460 246.098 1.00 8.83  ? 3989 ARG A CG    1 
ATOM   18598 C  CD    . ARG A 1 3989 ? 156.971 173.510 246.155 1.00 10.89 ? 3989 ARG A CD    1 
ATOM   18599 N  NE    . ARG A 1 3989 ? 155.830 173.088 246.958 1.00 18.15 ? 3989 ARG A NE    1 
ATOM   18600 C  CZ    . ARG A 1 3989 ? 155.695 173.318 248.256 1.00 18.96 ? 3989 ARG A CZ    1 
ATOM   18601 N  NH1   . ARG A 1 3989 ? 156.594 174.012 248.931 1.00 25.03 ? 3989 ARG A NH1   1 
ATOM   18602 N  NH2   . ARG A 1 3989 ? 154.620 172.855 248.888 1.00 24.21 ? 3989 ARG A NH2   1 
ATOM   18603 N  N     . LEU A 1 3990 ? 162.298 173.247 244.326 1.00 7.53  ? 3990 LEU A N     1 
ATOM   18604 C  CA    . LEU A 1 3990 ? 163.246 173.725 243.327 1.00 8.46  ? 3990 LEU A CA    1 
ATOM   18605 C  C     . LEU A 1 3990 ? 164.083 172.578 242.773 1.00 11.21 ? 3990 LEU A C     1 
ATOM   18606 O  O     . LEU A 1 3990 ? 164.347 172.517 241.566 1.00 14.81 ? 3990 LEU A O     1 
ATOM   18607 C  CB    . LEU A 1 3990 ? 164.129 174.808 243.941 1.00 8.83  ? 3990 LEU A CB    1 
ATOM   18608 C  CG    . LEU A 1 3990 ? 165.144 175.503 243.044 1.00 6.45  ? 3990 LEU A CG    1 
ATOM   18609 C  CD1   . LEU A 1 3990 ? 164.441 176.251 241.923 1.00 6.90  ? 3990 LEU A CD1   1 
ATOM   18610 C  CD2   . LEU A 1 3990 ? 165.998 176.445 243.868 1.00 9.50  ? 3990 LEU A CD2   1 
ATOM   18611 N  N     . LEU A 1 3991 ? 164.511 171.660 243.642 1.00 15.90 ? 3991 LEU A N     1 
ATOM   18612 C  CA    . LEU A 1 3991 ? 165.244 170.485 243.181 1.00 9.85  ? 3991 LEU A CA    1 
ATOM   18613 C  C     . LEU A 1 3991 ? 164.348 169.555 242.372 1.00 11.14 ? 3991 LEU A C     1 
ATOM   18614 O  O     . LEU A 1 3991 ? 164.793 168.968 241.379 1.00 11.69 ? 3991 LEU A O     1 
ATOM   18615 C  CB    . LEU A 1 3991 ? 165.848 169.747 244.373 1.00 10.01 ? 3991 LEU A CB    1 
ATOM   18616 C  CG    . LEU A 1 3991 ? 166.999 170.433 245.108 1.00 10.95 ? 3991 LEU A CG    1 
ATOM   18617 C  CD1   . LEU A 1 3991 ? 167.280 169.729 246.420 1.00 16.84 ? 3991 LEU A CD1   1 
ATOM   18618 C  CD2   . LEU A 1 3991 ? 168.244 170.463 244.240 1.00 13.66 ? 3991 LEU A CD2   1 
ATOM   18619 N  N     . LEU A 1 3992 ? 163.089 169.398 242.790 1.00 11.12 ? 3992 LEU A N     1 
ATOM   18620 C  CA    . LEU A 1 3992 ? 162.165 168.542 242.051 1.00 9.61  ? 3992 LEU A CA    1 
ATOM   18621 C  C     . LEU A 1 3992 ? 161.880 169.099 240.663 1.00 11.83 ? 3992 LEU A C     1 
ATOM   18622 O  O     . LEU A 1 3992 ? 161.857 168.349 239.682 1.00 14.64 ? 3992 LEU A O     1 
ATOM   18623 C  CB    . LEU A 1 3992 ? 160.865 168.371 242.835 1.00 10.94 ? 3992 LEU A CB    1 
ATOM   18624 C  CG    . LEU A 1 3992 ? 160.913 167.382 243.999 1.00 14.23 ? 3992 LEU A CG    1 
ATOM   18625 C  CD1   . LEU A 1 3992 ? 159.656 167.483 244.843 1.00 12.71 ? 3992 LEU A CD1   1 
ATOM   18626 C  CD2   . LEU A 1 3992 ? 161.107 165.963 243.485 1.00 10.13 ? 3992 LEU A CD2   1 
ATOM   18627 N  N     . ILE A 1 3993 ? 161.662 170.411 240.559 1.00 11.52 ? 3993 ILE A N     1 
ATOM   18628 C  CA    . ILE A 1 3993 ? 161.382 171.015 239.260 1.00 10.28 ? 3993 ILE A CA    1 
ATOM   18629 C  C     . ILE A 1 3993 ? 162.581 170.867 238.334 1.00 10.18 ? 3993 ILE A C     1 
ATOM   18630 O  O     . ILE A 1 3993 ? 162.437 170.516 237.159 1.00 11.92 ? 3993 ILE A O     1 
ATOM   18631 C  CB    . ILE A 1 3993 ? 160.970 172.489 239.433 1.00 11.22 ? 3993 ILE A CB    1 
ATOM   18632 C  CG1   . ILE A 1 3993 ? 159.544 172.578 239.976 1.00 9.17  ? 3993 ILE A CG1   1 
ATOM   18633 C  CG2   . ILE A 1 3993 ? 161.093 173.241 238.118 1.00 4.37  ? 3993 ILE A CG2   1 
ATOM   18634 C  CD1   . ILE A 1 3993 ? 158.504 171.975 239.061 1.00 9.46  ? 3993 ILE A CD1   1 
ATOM   18635 N  N     . GLN A 1 3994 ? 163.786 171.112 238.856 1.00 11.19 ? 3994 GLN A N     1 
ATOM   18636 C  CA    . GLN A 1 3994 ? 164.988 170.961 238.043 1.00 8.02  ? 3994 GLN A CA    1 
ATOM   18637 C  C     . GLN A 1 3994 ? 165.151 169.532 237.542 1.00 10.53 ? 3994 GLN A C     1 
ATOM   18638 O  O     . GLN A 1 3994 ? 165.658 169.315 236.435 1.00 12.86 ? 3994 GLN A O     1 
ATOM   18639 C  CB    . GLN A 1 3994 ? 166.213 171.388 238.851 1.00 9.20  ? 3994 GLN A CB    1 
ATOM   18640 C  CG    . GLN A 1 3994 ? 167.548 171.088 238.193 1.00 10.60 ? 3994 GLN A CG    1 
ATOM   18641 C  CD    . GLN A 1 3994 ? 168.718 171.567 239.023 1.00 11.80 ? 3994 GLN A CD    1 
ATOM   18642 O  OE1   . GLN A 1 3994 ? 168.900 171.139 240.161 1.00 19.16 ? 3994 GLN A OE1   1 
ATOM   18643 N  NE2   . GLN A 1 3994 ? 169.516 172.464 238.459 1.00 10.78 ? 3994 GLN A NE2   1 
ATOM   18644 N  N     . ALA A 1 3995 ? 164.723 168.549 238.335 1.00 14.45 ? 3995 ALA A N     1 
ATOM   18645 C  CA    . ALA A 1 3995 ? 164.857 167.158 237.919 1.00 15.50 ? 3995 ALA A CA    1 
ATOM   18646 C  C     . ALA A 1 3995 ? 163.837 166.792 236.846 1.00 15.96 ? 3995 ALA A C     1 
ATOM   18647 O  O     . ALA A 1 3995 ? 164.174 166.117 235.868 1.00 19.39 ? 3995 ALA A O     1 
ATOM   18648 C  CB    . ALA A 1 3995 ? 164.721 166.234 239.129 1.00 13.41 ? 3995 ALA A CB    1 
ATOM   18649 N  N     . PHE A 1 3996 ? 162.591 167.233 237.003 1.00 13.25 ? 3996 PHE A N     1 
ATOM   18650 C  CA    . PHE A 1 3996 ? 161.501 166.786 236.144 1.00 13.04 ? 3996 PHE A CA    1 
ATOM   18651 C  C     . PHE A 1 3996 ? 161.088 167.802 235.088 1.00 18.76 ? 3996 PHE A C     1 
ATOM   18652 O  O     . PHE A 1 3996 ? 160.834 167.420 233.943 1.00 23.54 ? 3996 PHE A O     1 
ATOM   18653 C  CB    . PHE A 1 3996 ? 160.285 166.415 236.995 1.00 13.99 ? 3996 PHE A CB    1 
ATOM   18654 C  CG    . PHE A 1 3996 ? 160.522 165.248 237.903 1.00 18.42 ? 3996 PHE A CG    1 
ATOM   18655 C  CD1   . PHE A 1 3996 ? 160.537 163.960 237.401 1.00 17.79 ? 3996 PHE A CD1   1 
ATOM   18656 C  CD2   . PHE A 1 3996 ? 160.737 165.437 239.257 1.00 16.68 ? 3996 PHE A CD2   1 
ATOM   18657 C  CE1   . PHE A 1 3996 ? 160.756 162.883 238.232 1.00 19.94 ? 3996 PHE A CE1   1 
ATOM   18658 C  CE2   . PHE A 1 3996 ? 160.957 164.365 240.092 1.00 17.25 ? 3996 PHE A CE2   1 
ATOM   18659 C  CZ    . PHE A 1 3996 ? 160.966 163.086 239.581 1.00 21.11 ? 3996 PHE A CZ    1 
ATOM   18660 N  N     . ARG A 1 3997 ? 161.013 169.086 235.431 1.00 11.02 ? 3997 ARG A N     1 
ATOM   18661 C  CA    . ARG A 1 3997 ? 160.553 170.123 234.508 1.00 10.00 ? 3997 ARG A CA    1 
ATOM   18662 C  C     . ARG A 1 3997 ? 161.560 171.265 234.471 1.00 8.13  ? 3997 ARG A C     1 
ATOM   18663 O  O     . ARG A 1 3997 ? 161.306 172.354 234.996 1.00 11.96 ? 3997 ARG A O     1 
ATOM   18664 C  CB    . ARG A 1 3997 ? 159.167 170.630 234.907 1.00 10.25 ? 3997 ARG A CB    1 
ATOM   18665 C  CG    . ARG A 1 3997 ? 158.064 169.598 234.749 1.00 14.08 ? 3997 ARG A CG    1 
ATOM   18666 C  CD    . ARG A 1 3997 ? 158.009 169.067 233.326 1.00 12.25 ? 3997 ARG A CD    1 
ATOM   18667 N  NE    . ARG A 1 3997 ? 157.666 170.111 232.367 1.00 15.04 ? 3997 ARG A NE    1 
ATOM   18668 C  CZ    . ARG A 1 3997 ? 156.460 170.647 232.237 1.00 15.19 ? 3997 ARG A CZ    1 
ATOM   18669 N  NH1   . ARG A 1 3997 ? 155.436 170.236 232.967 1.00 15.51 ? 3997 ARG A NH1   1 
ATOM   18670 N  NH2   . ARG A 1 3997 ? 156.276 171.618 231.349 1.00 18.41 ? 3997 ARG A NH2   1 
ATOM   18671 N  N     . PRO A 1 3998 ? 162.722 171.048 233.850 1.00 7.79  ? 3998 PRO A N     1 
ATOM   18672 C  CA    . PRO A 1 3998 ? 163.725 172.122 233.787 1.00 8.18  ? 3998 PRO A CA    1 
ATOM   18673 C  C     . PRO A 1 3998 ? 163.258 173.348 233.020 1.00 8.28  ? 3998 PRO A C     1 
ATOM   18674 O  O     . PRO A 1 3998 ? 163.821 174.430 233.216 1.00 11.15 ? 3998 PRO A O     1 
ATOM   18675 C  CB    . PRO A 1 3998 ? 164.923 171.446 233.104 1.00 5.81  ? 3998 PRO A CB    1 
ATOM   18676 C  CG    . PRO A 1 3998 ? 164.331 170.314 232.343 1.00 7.81  ? 3998 PRO A CG    1 
ATOM   18677 C  CD    . PRO A 1 3998 ? 163.175 169.829 233.160 1.00 8.60  ? 3998 PRO A CD    1 
ATOM   18678 N  N     . ASP A 1 3999 ? 162.251 173.217 232.154 1.00 6.86  ? 3999 ASP A N     1 
ATOM   18679 C  CA    . ASP A 1 3999 ? 161.691 174.384 231.484 1.00 5.44  ? 3999 ASP A CA    1 
ATOM   18680 C  C     . ASP A 1 3999 ? 160.958 175.304 232.450 1.00 5.68  ? 3999 ASP A C     1 
ATOM   18681 O  O     . ASP A 1 3999 ? 160.786 176.489 232.149 1.00 7.23  ? 3999 ASP A O     1 
ATOM   18682 C  CB    . ASP A 1 3999 ? 160.750 173.946 230.362 1.00 7.46  ? 3999 ASP A CB    1 
ATOM   18683 C  CG    . ASP A 1 3999 ? 159.786 172.862 230.797 1.00 13.45 ? 3999 ASP A CG    1 
ATOM   18684 O  OD1   . ASP A 1 3999 ? 160.253 171.798 231.250 1.00 12.82 ? 3999 ASP A OD1   1 
ATOM   18685 O  OD2   . ASP A 1 3999 ? 158.561 173.074 230.685 1.00 13.60 ? 3999 ASP A OD2   1 
ATOM   18686 N  N     . ARG A 1 4000 ? 160.530 174.790 233.601 1.00 6.23  ? 4000 ARG A N     1 
ATOM   18687 C  CA    . ARG A 1 4000 ? 159.889 175.588 234.633 1.00 4.40  ? 4000 ARG A CA    1 
ATOM   18688 C  C     . ARG A 1 4000 ? 160.849 175.980 235.748 1.00 3.51  ? 4000 ARG A C     1 
ATOM   18689 O  O     . ARG A 1 4000 ? 160.406 176.465 236.792 1.00 4.68  ? 4000 ARG A O     1 
ATOM   18690 C  CB    . ARG A 1 4000 ? 158.691 174.834 235.209 1.00 6.26  ? 4000 ARG A CB    1 
ATOM   18691 C  CG    . ARG A 1 4000 ? 157.702 174.371 234.158 1.00 7.38  ? 4000 ARG A CG    1 
ATOM   18692 C  CD    . ARG A 1 4000 ? 157.162 175.540 233.362 1.00 8.73  ? 4000 ARG A CD    1 
ATOM   18693 N  NE    . ARG A 1 4000 ? 156.428 176.479 234.199 1.00 11.29 ? 4000 ARG A NE    1 
ATOM   18694 C  CZ    . ARG A 1 4000 ? 155.919 177.625 233.767 1.00 9.06  ? 4000 ARG A CZ    1 
ATOM   18695 N  NH1   . ARG A 1 4000 ? 156.063 178.015 232.511 1.00 10.14 ? 4000 ARG A NH1   1 
ATOM   18696 N  NH2   . ARG A 1 4000 ? 155.252 178.399 234.617 1.00 7.53  ? 4000 ARG A NH2   1 
ATOM   18697 N  N     . LEU A 1 4001 ? 162.152 175.777 235.547 1.00 3.79  ? 4001 LEU A N     1 
ATOM   18698 C  CA    . LEU A 1 4001 ? 163.125 176.086 236.589 1.00 4.53  ? 4001 LEU A CA    1 
ATOM   18699 C  C     . LEU A 1 4001 ? 163.155 177.578 236.900 1.00 3.09  ? 4001 LEU A C     1 
ATOM   18700 O  O     . LEU A 1 4001 ? 163.297 177.973 238.063 1.00 4.70  ? 4001 LEU A O     1 
ATOM   18701 C  CB    . LEU A 1 4001 ? 164.509 175.591 236.174 1.00 5.04  ? 4001 LEU A CB    1 
ATOM   18702 C  CG    . LEU A 1 4001 ? 165.608 175.699 237.229 1.00 3.66  ? 4001 LEU A CG    1 
ATOM   18703 C  CD1   . LEU A 1 4001 ? 165.192 174.970 238.496 1.00 6.19  ? 4001 LEU A CD1   1 
ATOM   18704 C  CD2   . LEU A 1 4001 ? 166.909 175.147 236.689 1.00 4.96  ? 4001 LEU A CD2   1 
ATOM   18705 N  N     . LEU A 1 4002 ? 163.033 178.422 235.873 1.00 2.36  ? 4002 LEU A N     1 
ATOM   18706 C  CA    . LEU A 1 4002 ? 162.957 179.861 236.106 1.00 2.19  ? 4002 LEU A CA    1 
ATOM   18707 C  C     . LEU A 1 4002 ? 161.709 180.228 236.899 1.00 2.41  ? 4002 LEU A C     1 
ATOM   18708 O  O     . LEU A 1 4002 ? 161.767 181.060 237.811 1.00 4.39  ? 4002 LEU A O     1 
ATOM   18709 C  CB    . LEU A 1 4002 ? 162.980 180.614 234.778 1.00 2.48  ? 4002 LEU A CB    1 
ATOM   18710 C  CG    . LEU A 1 4002 ? 164.283 180.576 233.985 1.00 2.78  ? 4002 LEU A CG    1 
ATOM   18711 C  CD1   . LEU A 1 4002 ? 164.142 181.409 232.726 1.00 1.87  ? 4002 LEU A CD1   1 
ATOM   18712 C  CD2   . LEU A 1 4002 ? 165.449 181.062 234.835 1.00 1.77  ? 4002 LEU A CD2   1 
ATOM   18713 N  N     . ALA A 1 4003 ? 160.570 179.620 236.561 1.00 2.89  ? 4003 ALA A N     1 
ATOM   18714 C  CA    . ALA A 1 4003 ? 159.340 179.895 237.294 1.00 3.07  ? 4003 ALA A CA    1 
ATOM   18715 C  C     . ALA A 1 4003 ? 159.461 179.463 238.752 1.00 3.21  ? 4003 ALA A C     1 
ATOM   18716 O  O     . ALA A 1 4003 ? 159.001 180.169 239.656 1.00 3.14  ? 4003 ALA A O     1 
ATOM   18717 C  CB    . ALA A 1 4003 ? 158.160 179.197 236.620 1.00 2.66  ? 4003 ALA A CB    1 
ATOM   18718 N  N     . MET A 1 4004 ? 160.076 178.305 238.995 1.00 4.05  ? 4004 MET A N     1 
ATOM   18719 C  CA    . MET A 1 4004 ? 160.300 177.861 240.366 1.00 4.54  ? 4004 MET A CA    1 
ATOM   18720 C  C     . MET A 1 4004 ? 161.310 178.747 241.084 1.00 3.87  ? 4004 MET A C     1 
ATOM   18721 O  O     . MET A 1 4004 ? 161.174 178.992 242.287 1.00 3.99  ? 4004 MET A O     1 
ATOM   18722 C  CB    . MET A 1 4004 ? 160.764 176.404 240.374 1.00 5.00  ? 4004 MET A CB    1 
ATOM   18723 C  CG    . MET A 1 4004 ? 160.734 175.745 241.738 1.00 4.87  ? 4004 MET A CG    1 
ATOM   18724 S  SD    . MET A 1 4004 ? 159.102 175.747 242.495 1.00 14.52 ? 4004 MET A SD    1 
ATOM   18725 C  CE    . MET A 1 4004 ? 159.423 176.661 243.997 1.00 6.42  ? 4004 MET A CE    1 
ATOM   18726 N  N     . ALA A 1 4005 ? 162.328 179.233 240.367 1.00 2.64  ? 4005 ALA A N     1 
ATOM   18727 C  CA    . ALA A 1 4005 ? 163.303 180.133 240.974 1.00 1.71  ? 4005 ALA A CA    1 
ATOM   18728 C  C     . ALA A 1 4005 ? 162.650 181.436 241.412 1.00 3.69  ? 4005 ALA A C     1 
ATOM   18729 O  O     . ALA A 1 4005 ? 162.982 181.981 242.472 1.00 3.44  ? 4005 ALA A O     1 
ATOM   18730 C  CB    . ALA A 1 4005 ? 164.447 180.406 240.000 1.00 1.59  ? 4005 ALA A CB    1 
ATOM   18731 N  N     . HIS A 1 4006 ? 161.723 181.955 240.605 1.00 2.64  ? 4006 HIS A N     1 
ATOM   18732 C  CA    . HIS A 1 4006 ? 160.996 183.162 240.989 1.00 2.21  ? 4006 HIS A CA    1 
ATOM   18733 C  C     . HIS A 1 4006 ? 160.159 182.923 242.238 1.00 2.75  ? 4006 HIS A C     1 
ATOM   18734 O  O     . HIS A 1 4006 ? 160.021 183.816 243.083 1.00 4.17  ? 4006 HIS A O     1 
ATOM   18735 C  CB    . HIS A 1 4006 ? 160.119 183.638 239.831 1.00 1.74  ? 4006 HIS A CB    1 
ATOM   18736 C  CG    . HIS A 1 4006 ? 160.847 184.487 238.836 1.00 3.06  ? 4006 HIS A CG    1 
ATOM   18737 N  ND1   . HIS A 1 4006 ? 161.577 183.955 237.795 1.00 4.66  ? 4006 HIS A ND1   1 
ATOM   18738 C  CD2   . HIS A 1 4006 ? 160.958 185.832 238.724 1.00 1.38  ? 4006 HIS A CD2   1 
ATOM   18739 C  CE1   . HIS A 1 4006 ? 162.108 184.934 237.086 1.00 2.47  ? 4006 HIS A CE1   1 
ATOM   18740 N  NE2   . HIS A 1 4006 ? 161.748 186.083 237.629 1.00 1.56  ? 4006 HIS A NE2   1 
ATOM   18741 N  N     . MET A 1 4007 ? 159.586 181.725 242.370 1.00 2.68  ? 4007 MET A N     1 
ATOM   18742 C  CA    . MET A 1 4007 ? 158.834 181.397 243.577 1.00 3.69  ? 4007 MET A CA    1 
ATOM   18743 C  C     . MET A 1 4007 ? 159.758 181.269 244.783 1.00 3.85  ? 4007 MET A C     1 
ATOM   18744 O  O     . MET A 1 4007 ? 159.385 181.643 245.900 1.00 3.50  ? 4007 MET A O     1 
ATOM   18745 C  CB    . MET A 1 4007 ? 158.037 180.111 243.364 1.00 4.91  ? 4007 MET A CB    1 
ATOM   18746 C  CG    . MET A 1 4007 ? 156.726 180.320 242.631 1.00 4.92  ? 4007 MET A CG    1 
ATOM   18747 S  SD    . MET A 1 4007 ? 155.960 178.778 242.105 1.00 26.38 ? 4007 MET A SD    1 
ATOM   18748 C  CE    . MET A 1 4007 ? 155.332 178.163 243.664 1.00 11.79 ? 4007 MET A CE    1 
ATOM   18749 N  N     . PHE A 1 4008 ? 160.966 180.738 244.577 1.00 4.91  ? 4008 PHE A N     1 
ATOM   18750 C  CA    . PHE A 1 4008 ? 161.945 180.685 245.659 1.00 4.59  ? 4008 PHE A CA    1 
ATOM   18751 C  C     . PHE A 1 4008 ? 162.327 182.085 246.121 1.00 3.73  ? 4008 PHE A C     1 
ATOM   18752 O  O     . PHE A 1 4008 ? 162.457 182.334 247.326 1.00 8.33  ? 4008 PHE A O     1 
ATOM   18753 C  CB    . PHE A 1 4008 ? 163.182 179.907 245.208 1.00 5.19  ? 4008 PHE A CB    1 
ATOM   18754 C  CG    . PHE A 1 4008 ? 164.328 179.967 246.177 1.00 6.54  ? 4008 PHE A CG    1 
ATOM   18755 C  CD1   . PHE A 1 4008 ? 164.389 179.104 247.256 1.00 8.87  ? 4008 PHE A CD1   1 
ATOM   18756 C  CD2   . PHE A 1 4008 ? 165.352 180.881 246.003 1.00 9.75  ? 4008 PHE A CD2   1 
ATOM   18757 C  CE1   . PHE A 1 4008 ? 165.444 179.162 248.145 1.00 8.97  ? 4008 PHE A CE1   1 
ATOM   18758 C  CE2   . PHE A 1 4008 ? 166.410 180.940 246.887 1.00 7.91  ? 4008 PHE A CE2   1 
ATOM   18759 C  CZ    . PHE A 1 4008 ? 166.455 180.079 247.959 1.00 6.32  ? 4008 PHE A CZ    1 
ATOM   18760 N  N     . VAL A 1 4009 ? 162.516 183.010 245.179 1.00 3.07  ? 4009 VAL A N     1 
ATOM   18761 C  CA    . VAL A 1 4009 ? 162.814 184.393 245.541 1.00 2.96  ? 4009 VAL A CA    1 
ATOM   18762 C  C     . VAL A 1 4009 ? 161.627 185.016 246.264 1.00 3.37  ? 4009 VAL A C     1 
ATOM   18763 O  O     . VAL A 1 4009 ? 161.791 185.761 247.237 1.00 4.06  ? 4009 VAL A O     1 
ATOM   18764 C  CB    . VAL A 1 4009 ? 163.211 185.197 244.289 1.00 2.67  ? 4009 VAL A CB    1 
ATOM   18765 C  CG1   . VAL A 1 4009 ? 163.326 186.679 244.610 1.00 1.22  ? 4009 VAL A CG1   1 
ATOM   18766 C  CG2   . VAL A 1 4009 ? 164.515 184.671 243.716 1.00 1.27  ? 4009 VAL A CG2   1 
ATOM   18767 N  N     . SER A 1 4010 ? 160.412 184.711 245.803 1.00 6.95  ? 4010 SER A N     1 
ATOM   18768 C  CA    . SER A 1 4010 ? 159.212 185.219 246.462 1.00 3.81  ? 4010 SER A CA    1 
ATOM   18769 C  C     . SER A 1 4010 ? 159.094 184.689 247.886 1.00 4.43  ? 4010 SER A C     1 
ATOM   18770 O  O     . SER A 1 4010 ? 158.650 185.407 248.789 1.00 6.28  ? 4010 SER A O     1 
ATOM   18771 C  CB    . SER A 1 4010 ? 157.976 184.847 245.646 1.00 4.05  ? 4010 SER A CB    1 
ATOM   18772 O  OG    . SER A 1 4010 ? 156.823 185.505 246.133 1.00 14.46 ? 4010 SER A OG    1 
ATOM   18773 N  N     . THR A 1 4011 ? 159.468 183.427 248.105 1.00 6.70  ? 4011 THR A N     1 
ATOM   18774 C  CA    . THR A 1 4011 ? 159.410 182.863 249.449 1.00 6.74  ? 4011 THR A CA    1 
ATOM   18775 C  C     . THR A 1 4011 ? 160.391 183.559 250.386 1.00 7.35  ? 4011 THR A C     1 
ATOM   18776 O  O     . THR A 1 4011 ? 160.059 183.846 251.541 1.00 4.89  ? 4011 THR A O     1 
ATOM   18777 C  CB    . THR A 1 4011 ? 159.689 181.361 249.397 1.00 6.15  ? 4011 THR A CB    1 
ATOM   18778 O  OG1   . THR A 1 4011 ? 158.712 180.721 248.569 1.00 9.84  ? 4011 THR A OG1   1 
ATOM   18779 C  CG2   . THR A 1 4011 ? 159.629 180.758 250.788 1.00 6.87  ? 4011 THR A CG2   1 
ATOM   18780 N  N     . ASN A 1 4012 ? 161.600 183.845 249.902 1.00 6.86  ? 4012 ASN A N     1 
ATOM   18781 C  CA    . ASN A 1 4012 ? 162.624 184.441 250.753 1.00 5.35  ? 4012 ASN A CA    1 
ATOM   18782 C  C     . ASN A 1 4012 ? 162.471 185.953 250.868 1.00 2.17  ? 4012 ASN A C     1 
ATOM   18783 O  O     . ASN A 1 4012 ? 162.558 186.503 251.969 1.00 3.73  ? 4012 ASN A O     1 
ATOM   18784 C  CB    . ASN A 1 4012 ? 164.013 184.091 250.217 1.00 4.90  ? 4012 ASN A CB    1 
ATOM   18785 C  CG    . ASN A 1 4012 ? 164.560 182.811 250.806 1.00 7.26  ? 4012 ASN A CG    1 
ATOM   18786 O  OD1   . ASN A 1 4012 ? 164.837 182.733 252.002 1.00 14.12 ? 4012 ASN A OD1   1 
ATOM   18787 N  ND2   . ASN A 1 4012 ? 164.716 181.795 249.970 1.00 11.43 ? 4012 ASN A ND2   1 
ATOM   18788 N  N     . LEU A 1 4013 ? 162.232 186.639 249.751 1.00 3.40  ? 4013 LEU A N     1 
ATOM   18789 C  CA    . LEU A 1 4013 ? 162.275 188.094 249.718 1.00 3.02  ? 4013 LEU A CA    1 
ATOM   18790 C  C     . LEU A 1 4013 ? 160.913 188.759 249.572 1.00 2.52  ? 4013 LEU A C     1 
ATOM   18791 O  O     . LEU A 1 4013 ? 160.824 189.979 249.742 1.00 4.76  ? 4013 LEU A O     1 
ATOM   18792 C  CB    . LEU A 1 4013 ? 163.193 188.564 248.580 1.00 1.06  ? 4013 LEU A CB    1 
ATOM   18793 C  CG    . LEU A 1 4013 ? 164.659 188.144 248.714 1.00 0.98  ? 4013 LEU A CG    1 
ATOM   18794 C  CD1   . LEU A 1 4013 ? 165.378 188.241 247.384 1.00 0.92  ? 4013 LEU A CD1   1 
ATOM   18795 C  CD2   . LEU A 1 4013 ? 165.364 188.987 249.761 1.00 1.23  ? 4013 LEU A CD2   1 
ATOM   18796 N  N     . GLY A 1 4014 ? 159.863 188.011 249.267 1.00 2.67  ? 4014 GLY A N     1 
ATOM   18797 C  CA    . GLY A 1 4014 ? 158.538 188.581 249.147 1.00 3.45  ? 4014 GLY A CA    1 
ATOM   18798 C  C     . GLY A 1 4014 ? 158.035 188.567 247.709 1.00 5.89  ? 4014 GLY A C     1 
ATOM   18799 O  O     . GLY A 1 4014 ? 158.799 188.461 246.745 1.00 5.97  ? 4014 GLY A O     1 
ATOM   18800 N  N     . GLU A 1 4015 ? 156.711 188.691 247.578 1.00 9.64  ? 4015 GLU A N     1 
ATOM   18801 C  CA    . GLU A 1 4015 ? 156.073 188.583 246.269 1.00 6.16  ? 4015 GLU A CA    1 
ATOM   18802 C  C     . GLU A 1 4015 ? 156.382 189.782 245.383 1.00 7.11  ? 4015 GLU A C     1 
ATOM   18803 O  O     . GLU A 1 4015 ? 156.501 189.633 244.162 1.00 11.35 ? 4015 GLU A O     1 
ATOM   18804 C  CB    . GLU A 1 4015 ? 154.559 188.420 246.440 1.00 8.66  ? 4015 GLU A CB    1 
ATOM   18805 C  CG    . GLU A 1 4015 ? 153.800 188.061 245.164 1.00 19.16 ? 4015 GLU A CG    1 
ATOM   18806 C  CD    . GLU A 1 4015 ? 153.459 189.270 244.307 1.00 26.83 ? 4015 GLU A CD    1 
ATOM   18807 O  OE1   . GLU A 1 4015 ? 153.294 190.374 244.868 1.00 24.03 ? 4015 GLU A OE1   1 
ATOM   18808 O  OE2   . GLU A 1 4015 ? 153.365 189.115 243.071 1.00 24.55 ? 4015 GLU A OE2   1 
ATOM   18809 N  N     . SER A 1 4016 ? 156.526 190.967 245.970 1.00 7.48  ? 4016 SER A N     1 
ATOM   18810 C  CA    . SER A 1 4016 ? 156.740 192.193 245.218 1.00 5.88  ? 4016 SER A CA    1 
ATOM   18811 C  C     . SER A 1 4016 ? 158.209 192.581 245.122 1.00 6.71  ? 4016 SER A C     1 
ATOM   18812 O  O     . SER A 1 4016 ? 158.515 193.708 244.726 1.00 7.92  ? 4016 SER A O     1 
ATOM   18813 C  CB    . SER A 1 4016 ? 155.938 193.336 245.843 1.00 10.70 ? 4016 SER A CB    1 
ATOM   18814 O  OG    . SER A 1 4016 ? 156.034 193.306 247.255 1.00 19.27 ? 4016 SER A OG    1 
ATOM   18815 N  N     . PHE A 1 4017 ? 159.122 191.675 245.479 1.00 8.41  ? 4017 PHE A N     1 
ATOM   18816 C  CA    . PHE A 1 4017 ? 160.541 192.010 245.472 1.00 2.35  ? 4017 PHE A CA    1 
ATOM   18817 C  C     . PHE A 1 4017 ? 161.033 192.341 244.067 1.00 2.39  ? 4017 PHE A C     1 
ATOM   18818 O  O     . PHE A 1 4017 ? 161.787 193.300 243.877 1.00 1.95  ? 4017 PHE A O     1 
ATOM   18819 C  CB    . PHE A 1 4017 ? 161.352 190.861 246.070 1.00 1.14  ? 4017 PHE A CB    1 
ATOM   18820 C  CG    . PHE A 1 4017 ? 162.820 191.148 246.173 1.00 1.23  ? 4017 PHE A CG    1 
ATOM   18821 C  CD1   . PHE A 1 4017 ? 163.328 191.844 247.253 1.00 0.51  ? 4017 PHE A CD1   1 
ATOM   18822 C  CD2   . PHE A 1 4017 ? 163.693 190.724 245.184 1.00 0.92  ? 4017 PHE A CD2   1 
ATOM   18823 C  CE1   . PHE A 1 4017 ? 164.677 192.112 247.348 1.00 0.50  ? 4017 PHE A CE1   1 
ATOM   18824 C  CE2   . PHE A 1 4017 ? 165.042 190.992 245.274 1.00 0.50  ? 4017 PHE A CE2   1 
ATOM   18825 C  CZ    . PHE A 1 4017 ? 165.534 191.686 246.360 1.00 0.57  ? 4017 PHE A CZ    1 
ATOM   18826 N  N     . MET A 1 4018 ? 160.614 191.563 243.072 1.00 2.28  ? 4018 MET A N     1 
ATOM   18827 C  CA    . MET A 1 4018 ? 161.067 191.741 241.700 1.00 1.38  ? 4018 MET A CA    1 
ATOM   18828 C  C     . MET A 1 4018 ? 160.085 192.541 240.853 1.00 4.22  ? 4018 MET A C     1 
ATOM   18829 O  O     . MET A 1 4018 ? 160.267 192.636 239.636 1.00 7.92  ? 4018 MET A O     1 
ATOM   18830 C  CB    . MET A 1 4018 ? 161.326 190.379 241.058 1.00 1.46  ? 4018 MET A CB    1 
ATOM   18831 C  CG    . MET A 1 4018 ? 162.574 189.684 241.569 1.00 1.69  ? 4018 MET A CG    1 
ATOM   18832 S  SD    . MET A 1 4018 ? 162.852 188.086 240.788 1.00 13.64 ? 4018 MET A SD    1 
ATOM   18833 C  CE    . MET A 1 4018 ? 164.062 188.529 239.546 1.00 1.18  ? 4018 MET A CE    1 
ATOM   18834 N  N     . SER A 1 4019 ? 159.059 193.129 241.472 1.00 5.71  ? 4019 SER A N     1 
ATOM   18835 C  CA    . SER A 1 4019 ? 157.985 193.762 240.719 1.00 5.50  ? 4019 SER A CA    1 
ATOM   18836 C  C     . SER A 1 4019 ? 158.397 195.084 240.082 1.00 7.52  ? 4019 SER A C     1 
ATOM   18837 O  O     . SER A 1 4019 ? 157.746 195.521 239.128 1.00 14.85 ? 4019 SER A O     1 
ATOM   18838 C  CB    . SER A 1 4019 ? 156.776 193.977 241.629 1.00 8.68  ? 4019 SER A CB    1 
ATOM   18839 O  OG    . SER A 1 4019 ? 156.141 192.745 241.925 1.00 14.84 ? 4019 SER A OG    1 
ATOM   18840 N  N     . ILE A 1 4020 ? 159.453 195.730 240.578 1.00 6.74  ? 4020 ILE A N     1 
ATOM   18841 C  CA    . ILE A 1 4020 ? 159.862 197.018 240.023 1.00 4.67  ? 4020 ILE A CA    1 
ATOM   18842 C  C     . ILE A 1 4020 ? 160.362 196.853 238.594 1.00 7.51  ? 4020 ILE A C     1 
ATOM   18843 O  O     . ILE A 1 4020 ? 160.126 197.711 237.735 1.00 11.73 ? 4020 ILE A O     1 
ATOM   18844 C  CB    . ILE A 1 4020 ? 160.923 197.676 240.926 1.00 5.71  ? 4020 ILE A CB    1 
ATOM   18845 C  CG1   . ILE A 1 4020 ? 160.364 197.882 242.333 1.00 8.18  ? 4020 ILE A CG1   1 
ATOM   18846 C  CG2   . ILE A 1 4020 ? 161.382 199.005 240.349 1.00 3.27  ? 4020 ILE A CG2   1 
ATOM   18847 C  CD1   . ILE A 1 4020 ? 159.154 198.786 242.379 1.00 3.84  ? 4020 ILE A CD1   1 
ATOM   18848 N  N     . MET A 1 4021 ? 161.052 195.748 238.310 1.00 7.11  ? 4021 MET A N     1 
ATOM   18849 C  CA    . MET A 1 4021 ? 161.601 195.538 236.978 1.00 6.02  ? 4021 MET A CA    1 
ATOM   18850 C  C     . MET A 1 4021 ? 160.515 195.385 235.921 1.00 9.87  ? 4021 MET A C     1 
ATOM   18851 O  O     . MET A 1 4021 ? 160.780 195.619 234.737 1.00 15.57 ? 4021 MET A O     1 
ATOM   18852 C  CB    . MET A 1 4021 ? 162.511 194.310 236.979 1.00 5.72  ? 4021 MET A CB    1 
ATOM   18853 C  CG    . MET A 1 4021 ? 163.847 194.503 237.689 1.00 6.34  ? 4021 MET A CG    1 
ATOM   18854 S  SD    . MET A 1 4021 ? 164.595 196.138 237.524 1.00 12.12 ? 4021 MET A SD    1 
ATOM   18855 C  CE    . MET A 1 4021 ? 164.118 196.901 239.074 1.00 2.74  ? 4021 MET A CE    1 
ATOM   18856 N  N     . GLU A 1 4022 ? 159.302 195.000 236.318 1.00 11.79 ? 4022 GLU A N     1 
ATOM   18857 C  CA    . GLU A 1 4022 ? 158.192 194.905 235.378 1.00 8.03  ? 4022 GLU A CA    1 
ATOM   18858 C  C     . GLU A 1 4022 ? 157.630 196.268 234.999 1.00 8.05  ? 4022 GLU A C     1 
ATOM   18859 O  O     . GLU A 1 4022 ? 157.019 196.396 233.933 1.00 6.82  ? 4022 GLU A O     1 
ATOM   18860 C  CB    . GLU A 1 4022 ? 157.074 194.043 235.970 1.00 11.50 ? 4022 GLU A CB    1 
ATOM   18861 C  CG    . GLU A 1 4022 ? 157.309 192.544 235.870 1.00 11.79 ? 4022 GLU A CG    1 
ATOM   18862 C  CD    . GLU A 1 4022 ? 158.106 192.155 234.645 1.00 17.93 ? 4022 GLU A CD    1 
ATOM   18863 O  OE1   . GLU A 1 4022 ? 159.277 191.748 234.801 1.00 20.91 ? 4022 GLU A OE1   1 
ATOM   18864 O  OE2   . GLU A 1 4022 ? 157.560 192.255 233.526 1.00 18.17 ? 4022 GLU A OE2   1 
ATOM   18865 N  N     . GLN A 1 4023 ? 157.818 197.280 235.845 1.00 11.18 ? 4023 GLN A N     1 
ATOM   18866 C  CA    . GLN A 1 4023 ? 157.319 198.619 235.588 1.00 7.79  ? 4023 GLN A CA    1 
ATOM   18867 C  C     . GLN A 1 4023 ? 158.251 199.374 234.641 1.00 6.91  ? 4023 GLN A C     1 
ATOM   18868 O  O     . GLN A 1 4023 ? 159.445 199.075 234.564 1.00 7.87  ? 4023 GLN A O     1 
ATOM   18869 C  CB    . GLN A 1 4023 ? 157.185 199.396 236.893 1.00 8.93  ? 4023 GLN A CB    1 
ATOM   18870 C  CG    . GLN A 1 4023 ? 156.013 198.972 237.757 1.00 12.21 ? 4023 GLN A CG    1 
ATOM   18871 C  CD    . GLN A 1 4023 ? 154.690 199.079 237.031 1.00 20.30 ? 4023 GLN A CD    1 
ATOM   18872 O  OE1   . GLN A 1 4023 ? 154.347 200.131 236.495 1.00 19.90 ? 4023 GLN A OE1   1 
ATOM   18873 N  NE2   . GLN A 1 4023 ? 153.935 197.987 237.010 1.00 16.60 ? 4023 GLN A NE2   1 
ATOM   18874 N  N     . PRO A 1 4024 ? 157.725 200.348 233.896 1.00 7.40  ? 4024 PRO A N     1 
ATOM   18875 C  CA    . PRO A 1 4024 ? 158.597 201.197 233.080 1.00 6.28  ? 4024 PRO A CA    1 
ATOM   18876 C  C     . PRO A 1 4024 ? 159.532 202.027 233.948 1.00 9.02  ? 4024 PRO A C     1 
ATOM   18877 O  O     . PRO A 1 4024 ? 159.205 202.401 235.077 1.00 11.29 ? 4024 PRO A O     1 
ATOM   18878 C  CB    . PRO A 1 4024 ? 157.611 202.083 232.308 1.00 7.37  ? 4024 PRO A CB    1 
ATOM   18879 C  CG    . PRO A 1 4024 ? 156.352 202.035 233.104 1.00 8.93  ? 4024 PRO A CG    1 
ATOM   18880 C  CD    . PRO A 1 4024 ? 156.301 200.664 233.691 1.00 8.51  ? 4024 PRO A CD    1 
ATOM   18881 N  N     . LEU A 1 4025 ? 160.711 202.309 233.401 1.00 6.44  ? 4025 LEU A N     1 
ATOM   18882 C  CA    . LEU A 1 4025 ? 161.750 203.002 234.152 1.00 6.68  ? 4025 LEU A CA    1 
ATOM   18883 C  C     . LEU A 1 4025 ? 161.318 204.424 234.493 1.00 10.76 ? 4025 LEU A C     1 
ATOM   18884 O  O     . LEU A 1 4025 ? 160.885 205.181 233.620 1.00 12.16 ? 4025 LEU A O     1 
ATOM   18885 C  CB    . LEU A 1 4025 ? 163.049 203.020 233.347 1.00 5.51  ? 4025 LEU A CB    1 
ATOM   18886 C  CG    . LEU A 1 4025 ? 164.286 203.607 234.026 1.00 7.24  ? 4025 LEU A CG    1 
ATOM   18887 C  CD1   . LEU A 1 4025 ? 164.626 202.821 235.275 1.00 10.52 ? 4025 LEU A CD1   1 
ATOM   18888 C  CD2   . LEU A 1 4025 ? 165.458 203.615 233.063 1.00 5.28  ? 4025 LEU A CD2   1 
ATOM   18889 N  N     . ASP A 1 4026 ? 161.450 204.785 235.767 1.00 13.22 ? 4026 ASP A N     1 
ATOM   18890 C  CA    . ASP A 1 4026 ? 161.099 206.118 236.256 1.00 11.30 ? 4026 ASP A CA    1 
ATOM   18891 C  C     . ASP A 1 4026 ? 162.367 206.965 236.203 1.00 14.54 ? 4026 ASP A C     1 
ATOM   18892 O  O     . ASP A 1 4026 ? 163.025 207.200 237.217 1.00 15.52 ? 4026 ASP A O     1 
ATOM   18893 C  CB    . ASP A 1 4026 ? 160.521 206.045 237.665 1.00 13.93 ? 4026 ASP A CB    1 
ATOM   18894 C  CG    . ASP A 1 4026 ? 159.942 207.366 238.133 1.00 20.14 ? 4026 ASP A CG    1 
ATOM   18895 O  OD1   . ASP A 1 4026 ? 160.036 208.366 237.390 1.00 20.11 ? 4026 ASP A OD1   1 
ATOM   18896 O  OD2   . ASP A 1 4026 ? 159.389 207.404 239.251 1.00 28.61 ? 4026 ASP A OD2   1 
ATOM   18897 N  N     . LEU A 1 4027 ? 162.707 207.427 234.998 1.00 12.88 ? 4027 LEU A N     1 
ATOM   18898 C  CA    . LEU A 1 4027 ? 163.937 208.188 234.814 1.00 9.86  ? 4027 LEU A CA    1 
ATOM   18899 C  C     . LEU A 1 4027 ? 163.886 209.532 235.530 1.00 14.65 ? 4027 LEU A C     1 
ATOM   18900 O  O     . LEU A 1 4027 ? 164.933 210.073 235.900 1.00 17.97 ? 4027 LEU A O     1 
ATOM   18901 C  CB    . LEU A 1 4027 ? 164.202 208.386 233.322 1.00 9.11  ? 4027 LEU A CB    1 
ATOM   18902 C  CG    . LEU A 1 4027 ? 165.663 208.438 232.876 1.00 15.37 ? 4027 LEU A CG    1 
ATOM   18903 C  CD1   . LEU A 1 4027 ? 166.353 207.122 233.166 1.00 12.18 ? 4027 LEU A CD1   1 
ATOM   18904 C  CD2   . LEU A 1 4027 ? 165.750 208.773 231.397 1.00 11.92 ? 4027 LEU A CD2   1 
ATOM   18905 N  N     . THR A 1 4028 ? 162.686 210.077 235.739 1.00 11.88 ? 4028 THR A N     1 
ATOM   18906 C  CA    . THR A 1 4028 ? 162.562 211.371 236.402 1.00 13.95 ? 4028 THR A CA    1 
ATOM   18907 C  C     . THR A 1 4028 ? 163.051 211.304 237.844 1.00 14.83 ? 4028 THR A C     1 
ATOM   18908 O  O     . THR A 1 4028 ? 163.860 212.131 238.278 1.00 19.04 ? 4028 THR A O     1 
ATOM   18909 C  CB    . THR A 1 4028 ? 161.109 211.844 236.356 1.00 14.30 ? 4028 THR A CB    1 
ATOM   18910 O  OG1   . THR A 1 4028 ? 160.689 211.975 234.992 1.00 16.75 ? 4028 THR A OG1   1 
ATOM   18911 C  CG2   . THR A 1 4028 ? 160.959 213.179 237.063 1.00 10.28 ? 4028 THR A CG2   1 
ATOM   18912 N  N     . HIS A 1 4029 ? 162.566 210.320 238.603 1.00 14.90 ? 4029 HIS A N     1 
ATOM   18913 C  CA    . HIS A 1 4029 ? 162.918 210.234 240.015 1.00 14.10 ? 4029 HIS A CA    1 
ATOM   18914 C  C     . HIS A 1 4029 ? 164.395 209.909 240.206 1.00 12.56 ? 4029 HIS A C     1 
ATOM   18915 O  O     . HIS A 1 4029 ? 165.049 210.468 241.093 1.00 13.73 ? 4029 HIS A O     1 
ATOM   18916 C  CB    . HIS A 1 4029 ? 162.044 209.188 240.707 1.00 18.48 ? 4029 HIS A CB    1 
ATOM   18917 C  CG    . HIS A 1 4029 ? 162.361 209.002 242.157 1.00 17.10 ? 4029 HIS A CG    1 
ATOM   18918 N  ND1   . HIS A 1 4029 ? 162.634 210.058 242.999 1.00 14.45 ? 4029 HIS A ND1   1 
ATOM   18919 C  CD2   . HIS A 1 4029 ? 162.457 207.882 242.912 1.00 17.43 ? 4029 HIS A CD2   1 
ATOM   18920 C  CE1   . HIS A 1 4029 ? 162.879 209.597 244.213 1.00 18.35 ? 4029 HIS A CE1   1 
ATOM   18921 N  NE2   . HIS A 1 4029 ? 162.779 208.280 244.187 1.00 23.78 ? 4029 HIS A NE2   1 
ATOM   18922 N  N     . ILE A 1 4030 ? 164.935 209.007 239.386 1.00 14.22 ? 4030 ILE A N     1 
ATOM   18923 C  CA    . ILE A 1 4030 ? 166.317 208.574 239.566 1.00 14.39 ? 4030 ILE A CA    1 
ATOM   18924 C  C     . ILE A 1 4030 ? 167.289 209.706 239.262 1.00 9.95  ? 4030 ILE A C     1 
ATOM   18925 O  O     . ILE A 1 4030 ? 168.239 209.942 240.018 1.00 11.74 ? 4030 ILE A O     1 
ATOM   18926 C  CB    . ILE A 1 4030 ? 166.603 207.335 238.699 1.00 9.20  ? 4030 ILE A CB    1 
ATOM   18927 C  CG1   . ILE A 1 4030 ? 165.589 206.230 239.003 1.00 4.08  ? 4030 ILE A CG1   1 
ATOM   18928 C  CG2   . ILE A 1 4030 ? 168.019 206.851 238.930 1.00 8.59  ? 4030 ILE A CG2   1 
ATOM   18929 C  CD1   . ILE A 1 4030 ? 165.725 205.018 238.124 1.00 5.98  ? 4030 ILE A CD1   1 
ATOM   18930 N  N     . VAL A 1 4031 ? 167.077 210.421 238.157 1.00 12.04 ? 4031 VAL A N     1 
ATOM   18931 C  CA    . VAL A 1 4031 ? 167.998 211.488 237.779 1.00 8.82  ? 4031 VAL A CA    1 
ATOM   18932 C  C     . VAL A 1 4031 ? 167.931 212.636 238.779 1.00 8.34  ? 4031 VAL A C     1 
ATOM   18933 O  O     . VAL A 1 4031 ? 168.955 213.235 239.126 1.00 15.27 ? 4031 VAL A O     1 
ATOM   18934 C  CB    . VAL A 1 4031 ? 167.705 211.960 236.341 1.00 10.45 ? 4031 VAL A CB    1 
ATOM   18935 C  CG1   . VAL A 1 4031 ? 168.442 213.256 236.034 1.00 10.44 ? 4031 VAL A CG1   1 
ATOM   18936 C  CG2   . VAL A 1 4031 ? 168.094 210.882 235.346 1.00 4.90  ? 4031 VAL A CG2   1 
ATOM   18937 N  N     . GLY A 1 4032 ? 166.730 212.954 239.269 1.00 10.46 ? 4032 GLY A N     1 
ATOM   18938 C  CA    . GLY A 1 4032 ? 166.580 214.085 240.166 1.00 10.53 ? 4032 GLY A CA    1 
ATOM   18939 C  C     . GLY A 1 4032 ? 167.052 213.849 241.584 1.00 15.31 ? 4032 GLY A C     1 
ATOM   18940 O  O     . GLY A 1 4032 ? 167.401 214.805 242.282 1.00 20.02 ? 4032 GLY A O     1 
ATOM   18941 N  N     . THR A 1 4033 ? 167.070 212.598 242.038 1.00 16.96 ? 4033 THR A N     1 
ATOM   18942 C  CA    . THR A 1 4033 ? 167.366 212.311 243.437 1.00 12.12 ? 4033 THR A CA    1 
ATOM   18943 C  C     . THR A 1 4033 ? 168.516 211.340 243.644 1.00 11.82 ? 4033 THR A C     1 
ATOM   18944 O  O     . THR A 1 4033 ? 169.288 211.506 244.592 1.00 18.74 ? 4033 THR A O     1 
ATOM   18945 C  CB    . THR A 1 4033 ? 166.116 211.757 244.144 1.00 15.35 ? 4033 THR A CB    1 
ATOM   18946 O  OG1   . THR A 1 4033 ? 165.711 210.533 243.518 1.00 19.76 ? 4033 THR A OG1   1 
ATOM   18947 C  CG2   . THR A 1 4033 ? 164.975 212.757 244.086 1.00 17.42 ? 4033 THR A CG2   1 
ATOM   18948 N  N     . GLU A 1 4034 ? 168.657 210.326 242.794 1.00 11.21 ? 4034 GLU A N     1 
ATOM   18949 C  CA    . GLU A 1 4034 ? 169.633 209.273 243.041 1.00 8.28  ? 4034 GLU A CA    1 
ATOM   18950 C  C     . GLU A 1 4034 ? 170.969 209.500 242.346 1.00 9.51  ? 4034 GLU A C     1 
ATOM   18951 O  O     . GLU A 1 4034 ? 171.972 208.910 242.762 1.00 13.38 ? 4034 GLU A O     1 
ATOM   18952 C  CB    . GLU A 1 4034 ? 169.071 207.917 242.605 1.00 8.27  ? 4034 GLU A CB    1 
ATOM   18953 C  CG    . GLU A 1 4034 ? 167.900 207.427 243.435 1.00 10.94 ? 4034 GLU A CG    1 
ATOM   18954 C  CD    . GLU A 1 4034 ? 167.363 206.091 242.957 1.00 14.83 ? 4034 GLU A CD    1 
ATOM   18955 O  OE1   . GLU A 1 4034 ? 167.823 205.607 241.905 1.00 13.73 ? 4034 GLU A OE1   1 
ATOM   18956 O  OE2   . GLU A 1 4034 ? 166.479 205.525 243.632 1.00 25.10 ? 4034 GLU A OE2   1 
ATOM   18957 N  N     . VAL A 1 4035 ? 171.016 210.329 241.310 1.00 11.60 ? 4035 VAL A N     1 
ATOM   18958 C  CA    . VAL A 1 4035 ? 172.218 210.502 240.502 1.00 8.56  ? 4035 VAL A CA    1 
ATOM   18959 C  C     . VAL A 1 4035 ? 172.934 211.770 240.946 1.00 7.42  ? 4035 VAL A C     1 
ATOM   18960 O  O     . VAL A 1 4035 ? 172.336 212.852 240.984 1.00 10.23 ? 4035 VAL A O     1 
ATOM   18961 C  CB    . VAL A 1 4035 ? 171.885 210.550 239.003 1.00 4.86  ? 4035 VAL A CB    1 
ATOM   18962 C  CG1   . VAL A 1 4035 ? 173.090 211.021 238.208 1.00 5.06  ? 4035 VAL A CG1   1 
ATOM   18963 C  CG2   . VAL A 1 4035 ? 171.429 209.184 238.522 1.00 5.57  ? 4035 VAL A CG2   1 
ATOM   18964 N  N     . LYS A 1 4036 ? 174.208 211.634 241.289 1.00 6.64  ? 4036 LYS A N     1 
ATOM   18965 C  CA    . LYS A 1 4036 ? 175.040 212.784 241.593 1.00 7.62  ? 4036 LYS A CA    1 
ATOM   18966 C  C     . LYS A 1 4036 ? 175.462 213.481 240.302 1.00 5.63  ? 4036 LYS A C     1 
ATOM   18967 O  O     . LYS A 1 4036 ? 175.617 212.835 239.263 1.00 8.00  ? 4036 LYS A O     1 
ATOM   18968 C  CB    . LYS A 1 4036 ? 176.275 212.355 242.374 1.00 8.18  ? 4036 LYS A CB    1 
ATOM   18969 C  CG    . LYS A 1 4036 ? 175.966 211.711 243.710 1.00 9.02  ? 4036 LYS A CG    1 
ATOM   18970 C  CD    . LYS A 1 4036 ? 175.393 212.705 244.696 1.00 9.13  ? 4036 LYS A CD    1 
ATOM   18971 C  CE    . LYS A 1 4036 ? 175.084 212.032 246.023 1.00 21.95 ? 4036 LYS A CE    1 
ATOM   18972 N  NZ    . LYS A 1 4036 ? 176.322 211.605 246.729 1.00 19.75 ? 4036 LYS A NZ    1 
ATOM   18973 N  N     . PRO A 1 4037 ? 175.646 214.803 240.339 1.00 5.86  ? 4037 PRO A N     1 
ATOM   18974 C  CA    . PRO A 1 4037 ? 176.062 215.515 239.118 1.00 4.69  ? 4037 PRO A CA    1 
ATOM   18975 C  C     . PRO A 1 4037 ? 177.387 215.034 238.556 1.00 5.32  ? 4037 PRO A C     1 
ATOM   18976 O  O     . PRO A 1 4037 ? 177.563 215.027 237.331 1.00 9.28  ? 4037 PRO A O     1 
ATOM   18977 C  CB    . PRO A 1 4037 ? 176.133 216.981 239.571 1.00 5.13  ? 4037 PRO A CB    1 
ATOM   18978 C  CG    . PRO A 1 4037 ? 176.182 216.934 241.064 1.00 7.92  ? 4037 PRO A CG    1 
ATOM   18979 C  CD    . PRO A 1 4037 ? 175.424 215.717 241.469 1.00 5.21  ? 4037 PRO A CD    1 
ATOM   18980 N  N     . ASN A 1 4038 ? 178.326 214.625 239.410 1.00 7.13  ? 4038 ASN A N     1 
ATOM   18981 C  CA    . ASN A 1 4038 ? 179.600 214.097 238.936 1.00 6.94  ? 4038 ASN A CA    1 
ATOM   18982 C  C     . ASN A 1 4038 ? 179.474 212.701 238.342 1.00 4.50  ? 4038 ASN A C     1 
ATOM   18983 O  O     . ASN A 1 4038 ? 180.413 212.241 237.683 1.00 4.56  ? 4038 ASN A O     1 
ATOM   18984 C  CB    . ASN A 1 4038 ? 180.616 214.076 240.080 1.00 7.71  ? 4038 ASN A CB    1 
ATOM   18985 C  CG    . ASN A 1 4038 ? 180.101 213.338 241.300 1.00 19.60 ? 4038 ASN A CG    1 
ATOM   18986 O  OD1   . ASN A 1 4038 ? 180.300 212.131 241.440 1.00 18.25 ? 4038 ASN A OD1   1 
ATOM   18987 N  ND2   . ASN A 1 4038 ? 179.430 214.059 242.191 1.00 15.21 ? 4038 ASN A ND2   1 
ATOM   18988 N  N     . THR A 1 4039 ? 178.351 212.021 238.556 1.00 3.75  ? 4039 THR A N     1 
ATOM   18989 C  CA    . THR A 1 4039 ? 178.171 210.664 238.062 1.00 3.09  ? 4039 THR A CA    1 
ATOM   18990 C  C     . THR A 1 4039 ? 177.481 210.695 236.706 1.00 3.02  ? 4039 THR A C     1 
ATOM   18991 O  O     . THR A 1 4039 ? 176.334 211.155 236.620 1.00 8.32  ? 4039 THR A O     1 
ATOM   18992 C  CB    . THR A 1 4039 ? 177.350 209.843 239.041 1.00 3.29  ? 4039 THR A CB    1 
ATOM   18993 O  OG1   . THR A 1 4039 ? 178.065 209.713 240.277 1.00 10.34 ? 4039 THR A OG1   1 
ATOM   18994 C  CG2   . THR A 1 4039 ? 177.072 208.462 238.478 1.00 1.62  ? 4039 THR A CG2   1 
ATOM   18995 N  N     . PRO A 1 4040 ? 178.125 210.237 235.638 1.00 1.06  ? 4040 PRO A N     1 
ATOM   18996 C  CA    . PRO A 1 4040 ? 177.439 210.164 234.344 1.00 0.37  ? 4040 PRO A CA    1 
ATOM   18997 C  C     . PRO A 1 4040 ? 176.326 209.129 234.365 1.00 0.39  ? 4040 PRO A C     1 
ATOM   18998 O  O     . PRO A 1 4040 ? 176.385 208.128 235.082 1.00 0.34  ? 4040 PRO A O     1 
ATOM   18999 C  CB    . PRO A 1 4040 ? 178.555 209.763 233.374 1.00 0.25  ? 4040 PRO A CB    1 
ATOM   19000 C  CG    . PRO A 1 4040 ? 179.563 209.079 234.224 1.00 0.36  ? 4040 PRO A CG    1 
ATOM   19001 C  CD    . PRO A 1 4040 ? 179.516 209.764 235.557 1.00 0.71  ? 4040 PRO A CD    1 
ATOM   19002 N  N     . VAL A 1 4041 ? 175.297 209.384 233.565 1.00 0.53  ? 4041 VAL A N     1 
ATOM   19003 C  CA    . VAL A 1 4041 ? 174.178 208.465 233.417 1.00 0.24  ? 4041 VAL A CA    1 
ATOM   19004 C  C     . VAL A 1 4041 ? 174.389 207.701 232.118 1.00 0.24  ? 4041 VAL A C     1 
ATOM   19005 O  O     . VAL A 1 4041 ? 174.280 208.269 231.026 1.00 0.31  ? 4041 VAL A O     1 
ATOM   19006 C  CB    . VAL A 1 4041 ? 172.831 209.199 233.424 1.00 0.33  ? 4041 VAL A CB    1 
ATOM   19007 C  CG1   . VAL A 1 4041 ? 171.701 208.208 233.265 1.00 0.28  ? 4041 VAL A CG1   1 
ATOM   19008 C  CG2   . VAL A 1 4041 ? 172.670 210.002 234.701 1.00 0.96  ? 4041 VAL A CG2   1 
ATOM   19009 N  N     . LEU A 1 4042 ? 174.685 206.411 232.229 1.00 0.36  ? 4042 LEU A N     1 
ATOM   19010 C  CA    . LEU A 1 4042 ? 175.001 205.583 231.074 1.00 0.46  ? 4042 LEU A CA    1 
ATOM   19011 C  C     . LEU A 1 4042 ? 173.722 204.953 230.536 1.00 0.61  ? 4042 LEU A C     1 
ATOM   19012 O  O     . LEU A 1 4042 ? 173.076 204.159 231.225 1.00 0.57  ? 4042 LEU A O     1 
ATOM   19013 C  CB    . LEU A 1 4042 ? 176.024 204.510 231.443 1.00 0.44  ? 4042 LEU A CB    1 
ATOM   19014 C  CG    . LEU A 1 4042 ? 177.237 204.985 232.250 1.00 0.68  ? 4042 LEU A CG    1 
ATOM   19015 C  CD1   . LEU A 1 4042 ? 178.210 203.845 232.483 1.00 0.83  ? 4042 LEU A CD1   1 
ATOM   19016 C  CD2   . LEU A 1 4042 ? 177.932 206.154 231.566 1.00 0.24  ? 4042 LEU A CD2   1 
ATOM   19017 N  N     . MET A 1 4043 ? 173.361 205.312 229.308 1.00 1.42  ? 4043 MET A N     1 
ATOM   19018 C  CA    . MET A 1 4043 ? 172.172 204.785 228.642 1.00 0.78  ? 4043 MET A CA    1 
ATOM   19019 C  C     . MET A 1 4043 ? 172.634 203.660 227.722 1.00 0.91  ? 4043 MET A C     1 
ATOM   19020 O  O     . MET A 1 4043 ? 172.929 203.876 226.547 1.00 1.91  ? 4043 MET A O     1 
ATOM   19021 C  CB    . MET A 1 4043 ? 171.450 205.881 227.867 1.00 1.36  ? 4043 MET A CB    1 
ATOM   19022 C  CG    . MET A 1 4043 ? 170.859 207.007 228.703 1.00 0.78  ? 4043 MET A CG    1 
ATOM   19023 S  SD    . MET A 1 4043 ? 169.558 206.475 229.823 1.00 33.78 ? 4043 MET A SD    1 
ATOM   19024 C  CE    . MET A 1 4043 ? 169.274 207.958 230.772 1.00 18.30 ? 4043 MET A CE    1 
ATOM   19025 N  N     . CYS A 1 4044 ? 172.708 202.448 228.266 1.00 1.05  ? 4044 CYS A N     1 
ATOM   19026 C  CA    . CYS A 1 4044 ? 173.163 201.280 227.524 1.00 0.59  ? 4044 CYS A CA    1 
ATOM   19027 C  C     . CYS A 1 4044 ? 171.961 200.547 226.944 1.00 0.71  ? 4044 CYS A C     1 
ATOM   19028 O  O     . CYS A 1 4044 ? 171.009 200.239 227.668 1.00 1.04  ? 4044 CYS A O     1 
ATOM   19029 C  CB    . CYS A 1 4044 ? 173.970 200.341 228.420 1.00 0.81  ? 4044 CYS A CB    1 
ATOM   19030 S  SG    . CYS A 1 4044 ? 175.255 201.143 229.398 1.00 6.85  ? 4044 CYS A SG    1 
ATOM   19031 N  N     . SER A 1 4045 ? 172.007 200.266 225.647 1.00 1.00  ? 4045 SER A N     1 
ATOM   19032 C  CA    . SER A 1 4045 ? 170.882 199.652 224.962 1.00 1.65  ? 4045 SER A CA    1 
ATOM   19033 C  C     . SER A 1 4045 ? 171.357 198.515 224.071 1.00 1.51  ? 4045 SER A C     1 
ATOM   19034 O  O     . SER A 1 4045 ? 172.477 198.530 223.555 1.00 1.80  ? 4045 SER A O     1 
ATOM   19035 C  CB    . SER A 1 4045 ? 170.109 200.683 224.129 1.00 1.27  ? 4045 SER A CB    1 
ATOM   19036 O  OG    . SER A 1 4045 ? 170.947 201.297 223.172 1.00 5.16  ? 4045 SER A OG    1 
ATOM   19037 N  N     . VAL A 1 4046 ? 170.489 197.523 223.911 1.00 2.22  ? 4046 VAL A N     1 
ATOM   19038 C  CA    . VAL A 1 4046 ? 170.706 196.425 222.973 1.00 4.55  ? 4046 VAL A CA    1 
ATOM   19039 C  C     . VAL A 1 4046 ? 170.434 196.949 221.567 1.00 5.11  ? 4046 VAL A C     1 
ATOM   19040 O  O     . VAL A 1 4046 ? 169.768 197.985 221.420 1.00 6.92  ? 4046 VAL A O     1 
ATOM   19041 C  CB    . VAL A 1 4046 ? 169.818 195.218 223.318 1.00 4.23  ? 4046 VAL A CB    1 
ATOM   19042 C  CG1   . VAL A 1 4046 ? 170.091 194.752 224.741 1.00 1.34  ? 4046 VAL A CG1   1 
ATOM   19043 C  CG2   . VAL A 1 4046 ? 168.353 195.571 223.137 1.00 4.84  ? 4046 VAL A CG2   1 
ATOM   19044 N  N     . PRO A 1 4047 ? 170.932 196.293 220.518 1.00 6.02  ? 4047 PRO A N     1 
ATOM   19045 C  CA    . PRO A 1 4047 ? 170.705 196.800 219.159 1.00 5.31  ? 4047 PRO A CA    1 
ATOM   19046 C  C     . PRO A 1 4047 ? 169.223 196.937 218.840 1.00 8.70  ? 4047 PRO A C     1 
ATOM   19047 O  O     . PRO A 1 4047 ? 168.406 196.087 219.200 1.00 14.05 ? 4047 PRO A O     1 
ATOM   19048 C  CB    . PRO A 1 4047 ? 171.373 195.741 218.280 1.00 7.29  ? 4047 PRO A CB    1 
ATOM   19049 C  CG    . PRO A 1 4047 ? 172.463 195.205 219.137 1.00 9.24  ? 4047 PRO A CG    1 
ATOM   19050 C  CD    . PRO A 1 4047 ? 171.897 195.180 220.530 1.00 6.69  ? 4047 PRO A CD    1 
ATOM   19051 N  N     . GLY A 1 4048 ? 168.887 198.022 218.148 1.00 12.00 ? 4048 GLY A N     1 
ATOM   19052 C  CA    . GLY A 1 4048 ? 167.513 198.359 217.855 1.00 10.70 ? 4048 GLY A CA    1 
ATOM   19053 C  C     . GLY A 1 4048 ? 166.845 199.240 218.884 1.00 11.02 ? 4048 GLY A C     1 
ATOM   19054 O  O     . GLY A 1 4048 ? 165.736 199.728 218.634 1.00 13.22 ? 4048 GLY A O     1 
ATOM   19055 N  N     . TYR A 1 4049 ? 167.482 199.466 220.027 1.00 8.49  ? 4049 TYR A N     1 
ATOM   19056 C  CA    . TYR A 1 4049 ? 166.947 200.313 221.080 1.00 5.81  ? 4049 TYR A CA    1 
ATOM   19057 C  C     . TYR A 1 4049 ? 167.909 201.463 221.332 1.00 10.92 ? 4049 TYR A C     1 
ATOM   19058 O  O     . TYR A 1 4049 ? 169.128 201.314 221.210 1.00 11.51 ? 4049 TYR A O     1 
ATOM   19059 C  CB    . TYR A 1 4049 ? 166.695 199.511 222.366 1.00 5.97  ? 4049 TYR A CB    1 
ATOM   19060 C  CG    . TYR A 1 4049 ? 165.491 198.601 222.260 1.00 7.55  ? 4049 TYR A CG    1 
ATOM   19061 C  CD1   . TYR A 1 4049 ? 165.500 197.503 221.409 1.00 5.81  ? 4049 TYR A CD1   1 
ATOM   19062 C  CD2   . TYR A 1 4049 ? 164.340 198.850 222.993 1.00 3.06  ? 4049 TYR A CD2   1 
ATOM   19063 C  CE1   . TYR A 1 4049 ? 164.401 196.682 221.291 1.00 6.49  ? 4049 TYR A CE1   1 
ATOM   19064 C  CE2   . TYR A 1 4049 ? 163.235 198.030 222.885 1.00 4.41  ? 4049 TYR A CE2   1 
ATOM   19065 C  CZ    . TYR A 1 4049 ? 163.273 196.947 222.034 1.00 8.36  ? 4049 TYR A CZ    1 
ATOM   19066 O  OH    . TYR A 1 4049 ? 162.177 196.124 221.920 1.00 8.00  ? 4049 TYR A OH    1 
ATOM   19067 N  N     . ASP A 1 4050 ? 167.346 202.622 221.657 1.00 11.61 ? 4050 ASP A N     1 
ATOM   19068 C  CA    . ASP A 1 4050 ? 168.135 203.835 221.825 1.00 11.03 ? 4050 ASP A CA    1 
ATOM   19069 C  C     . ASP A 1 4050 ? 167.415 204.728 222.821 1.00 8.03  ? 4050 ASP A C     1 
ATOM   19070 O  O     . ASP A 1 4050 ? 166.256 205.092 222.603 1.00 7.78  ? 4050 ASP A O     1 
ATOM   19071 C  CB    . ASP A 1 4050 ? 168.331 204.550 220.484 1.00 8.29  ? 4050 ASP A CB    1 
ATOM   19072 C  CG    . ASP A 1 4050 ? 168.838 205.967 220.642 1.00 15.20 ? 4050 ASP A CG    1 
ATOM   19073 O  OD1   . ASP A 1 4050 ? 169.927 206.148 221.225 1.00 14.92 ? 4050 ASP A OD1   1 
ATOM   19074 O  OD2   . ASP A 1 4050 ? 168.149 206.900 220.179 1.00 15.59 ? 4050 ASP A OD2   1 
ATOM   19075 N  N     . ALA A 1 4051 ? 168.099 205.073 223.907 1.00 7.02  ? 4051 ALA A N     1 
ATOM   19076 C  CA    . ALA A 1 4051 ? 167.508 205.826 225.003 1.00 6.66  ? 4051 ALA A CA    1 
ATOM   19077 C  C     . ALA A 1 4051 ? 167.628 207.332 224.819 1.00 5.65  ? 4051 ALA A C     1 
ATOM   19078 O  O     . ALA A 1 4051 ? 167.248 208.084 225.722 1.00 7.95  ? 4051 ALA A O     1 
ATOM   19079 C  CB    . ALA A 1 4051 ? 168.150 205.413 226.329 1.00 4.36  ? 4051 ALA A CB    1 
ATOM   19080 N  N     . SER A 1 4052 ? 168.147 207.785 223.676 1.00 5.69  ? 4052 SER A N     1 
ATOM   19081 C  CA    . SER A 1 4052 ? 168.318 209.217 223.454 1.00 7.08  ? 4052 SER A CA    1 
ATOM   19082 C  C     . SER A 1 4052 ? 166.983 209.946 223.503 1.00 8.99  ? 4052 SER A C     1 
ATOM   19083 O  O     . SER A 1 4052 ? 166.882 211.032 224.084 1.00 5.02  ? 4052 SER A O     1 
ATOM   19084 C  CB    . SER A 1 4052 ? 169.009 209.458 222.112 1.00 9.21  ? 4052 SER A CB    1 
ATOM   19085 O  OG    . SER A 1 4052 ? 170.127 208.601 221.954 1.00 9.31  ? 4052 SER A OG    1 
ATOM   19086 N  N     . GLY A 1 4053 ? 165.945 209.359 222.903 1.00 7.18  ? 4053 GLY A N     1 
ATOM   19087 C  CA    . GLY A 1 4053 ? 164.633 209.984 222.934 1.00 5.11  ? 4053 GLY A CA    1 
ATOM   19088 C  C     . GLY A 1 4053 ? 164.078 210.119 224.338 1.00 10.18 ? 4053 GLY A C     1 
ATOM   19089 O  O     . GLY A 1 4053 ? 163.450 211.127 224.670 1.00 13.63 ? 4053 GLY A O     1 
ATOM   19090 N  N     . HIS A 1 4054 ? 164.304 209.110 225.183 1.00 7.53  ? 4054 HIS A N     1 
ATOM   19091 C  CA    . HIS A 1 4054 ? 163.826 209.183 226.561 1.00 8.65  ? 4054 HIS A CA    1 
ATOM   19092 C  C     . HIS A 1 4054 ? 164.450 210.361 227.299 1.00 9.33  ? 4054 HIS A C     1 
ATOM   19093 O  O     . HIS A 1 4054 ? 163.762 211.072 228.041 1.00 15.14 ? 4054 HIS A O     1 
ATOM   19094 C  CB    . HIS A 1 4054 ? 164.122 207.876 227.297 1.00 6.72  ? 4054 HIS A CB    1 
ATOM   19095 C  CG    . HIS A 1 4054 ? 163.647 206.655 226.575 1.00 15.32 ? 4054 HIS A CG    1 
ATOM   19096 N  ND1   . HIS A 1 4054 ? 162.431 206.597 225.933 1.00 22.85 ? 4054 HIS A ND1   1 
ATOM   19097 C  CD2   . HIS A 1 4054 ? 164.228 205.446 226.392 1.00 14.10 ? 4054 HIS A CD2   1 
ATOM   19098 C  CE1   . HIS A 1 4054 ? 162.280 205.403 225.388 1.00 21.62 ? 4054 HIS A CE1   1 
ATOM   19099 N  NE2   . HIS A 1 4054 ? 163.356 204.685 225.651 1.00 15.59 ? 4054 HIS A NE2   1 
ATOM   19100 N  N     . VAL A 1 4055 ? 165.753 210.580 227.111 1.00 5.23  ? 4055 VAL A N     1 
ATOM   19101 C  CA    . VAL A 1 4055 ? 166.408 211.726 227.732 1.00 8.16  ? 4055 VAL A CA    1 
ATOM   19102 C  C     . VAL A 1 4055 ? 165.846 213.027 227.176 1.00 6.88  ? 4055 VAL A C     1 
ATOM   19103 O  O     . VAL A 1 4055 ? 165.587 213.978 227.922 1.00 7.08  ? 4055 VAL A O     1 
ATOM   19104 C  CB    . VAL A 1 4055 ? 167.933 211.641 227.537 1.00 6.16  ? 4055 VAL A CB    1 
ATOM   19105 C  CG1   . VAL A 1 4055 ? 168.623 212.775 228.275 1.00 1.50  ? 4055 VAL A CG1   1 
ATOM   19106 C  CG2   . VAL A 1 4055 ? 168.455 210.294 228.005 1.00 4.86  ? 4055 VAL A CG2   1 
ATOM   19107 N  N     . GLU A 1 4056 ? 165.650 213.090 225.857 1.00 10.41 ? 4056 GLU A N     1 
ATOM   19108 C  CA    . GLU A 1 4056 ? 165.097 214.289 225.238 1.00 9.99  ? 4056 GLU A CA    1 
ATOM   19109 C  C     . GLU A 1 4056 ? 163.701 214.589 225.764 1.00 12.17 ? 4056 GLU A C     1 
ATOM   19110 O  O     . GLU A 1 4056 ? 163.370 215.747 226.048 1.00 14.21 ? 4056 GLU A O     1 
ATOM   19111 C  CB    . GLU A 1 4056 ? 165.079 214.123 223.719 1.00 8.14  ? 4056 GLU A CB    1 
ATOM   19112 C  CG    . GLU A 1 4056 ? 166.463 214.064 223.100 1.00 11.70 ? 4056 GLU A CG    1 
ATOM   19113 C  CD    . GLU A 1 4056 ? 166.427 213.876 221.599 1.00 16.63 ? 4056 GLU A CD    1 
ATOM   19114 O  OE1   . GLU A 1 4056 ? 165.325 213.665 221.048 1.00 14.57 ? 4056 GLU A OE1   1 
ATOM   19115 O  OE2   . GLU A 1 4056 ? 167.505 213.928 220.971 1.00 19.81 ? 4056 GLU A OE2   1 
ATOM   19116 N  N     . ASP A 1 4057 ? 162.865 213.558 225.899 1.00 11.26 ? 4057 ASP A N     1 
ATOM   19117 C  CA    . ASP A 1 4057 ? 161.545 213.752 226.491 1.00 13.64 ? 4057 ASP A CA    1 
ATOM   19118 C  C     . ASP A 1 4057 ? 161.653 214.141 227.960 1.00 14.11 ? 4057 ASP A C     1 
ATOM   19119 O  O     . ASP A 1 4057 ? 160.900 214.996 228.437 1.00 18.23 ? 4057 ASP A O     1 
ATOM   19120 C  CB    . ASP A 1 4057 ? 160.704 212.486 226.331 1.00 12.67 ? 4057 ASP A CB    1 
ATOM   19121 C  CG    . ASP A 1 4057 ? 160.571 212.056 224.886 1.00 18.89 ? 4057 ASP A CG    1 
ATOM   19122 O  OD1   . ASP A 1 4057 ? 160.414 212.934 224.014 1.00 21.54 ? 4057 ASP A OD1   1 
ATOM   19123 O  OD2   . ASP A 1 4057 ? 160.618 210.836 224.622 1.00 22.48 ? 4057 ASP A OD2   1 
ATOM   19124 N  N     . LEU A 1 4058 ? 162.591 213.530 228.687 1.00 13.04 ? 4058 LEU A N     1 
ATOM   19125 C  CA    . LEU A 1 4058 ? 162.754 213.831 230.105 1.00 12.48 ? 4058 LEU A CA    1 
ATOM   19126 C  C     . LEU A 1 4058 ? 163.118 215.294 230.322 1.00 15.72 ? 4058 LEU A C     1 
ATOM   19127 O  O     . LEU A 1 4058 ? 162.625 215.932 231.259 1.00 16.85 ? 4058 LEU A O     1 
ATOM   19128 C  CB    . LEU A 1 4058 ? 163.819 212.919 230.712 1.00 13.05 ? 4058 LEU A CB    1 
ATOM   19129 C  CG    . LEU A 1 4058 ? 164.327 213.289 232.106 1.00 17.12 ? 4058 LEU A CG    1 
ATOM   19130 C  CD1   . LEU A 1 4058 ? 163.229 213.115 233.144 1.00 7.09  ? 4058 LEU A CD1   1 
ATOM   19131 C  CD2   . LEU A 1 4058 ? 165.554 212.468 232.464 1.00 10.96 ? 4058 LEU A CD2   1 
ATOM   19132 N  N     . ALA A 1 4059 ? 163.990 215.840 229.472 1.00 14.15 ? 4059 ALA A N     1 
ATOM   19133 C  CA    . ALA A 1 4059 ? 164.333 217.253 229.576 1.00 12.02 ? 4059 ALA A CA    1 
ATOM   19134 C  C     . ALA A 1 4059 ? 163.121 218.136 229.306 1.00 17.47 ? 4059 ALA A C     1 
ATOM   19135 O  O     . ALA A 1 4059 ? 162.956 219.186 229.936 1.00 15.78 ? 4059 ALA A O     1 
ATOM   19136 C  CB    . ALA A 1 4059 ? 165.474 217.587 228.616 1.00 7.00  ? 4059 ALA A CB    1 
ATOM   19137 N  N     . ALA A 1 4060 ? 162.268 217.730 228.363 1.00 16.19 ? 4060 ALA A N     1 
ATOM   19138 C  CA    . ALA A 1 4060 ? 161.058 218.494 228.081 1.00 16.53 ? 4060 ALA A CA    1 
ATOM   19139 C  C     . ALA A 1 4060 ? 160.111 218.505 229.276 1.00 19.58 ? 4060 ALA A C     1 
ATOM   19140 O  O     . ALA A 1 4060 ? 159.539 219.549 229.612 1.00 24.13 ? 4060 ALA A O     1 
ATOM   19141 C  CB    . ALA A 1 4060 ? 160.358 217.928 226.847 1.00 13.79 ? 4060 ALA A CB    1 
ATOM   19142 N  N     . GLU A 1 4061 ? 159.934 217.354 229.932 1.00 17.94 ? 4061 GLU A N     1 
ATOM   19143 C  CA    . GLU A 1 4061 ? 159.055 217.291 231.097 1.00 19.93 ? 4061 GLU A CA    1 
ATOM   19144 C  C     . GLU A 1 4061 ? 159.552 218.203 232.209 1.00 20.35 ? 4061 GLU A C     1 
ATOM   19145 O  O     . GLU A 1 4061 ? 158.772 218.945 232.820 1.00 29.14 ? 4061 GLU A O     1 
ATOM   19146 C  CB    . GLU A 1 4061 ? 158.948 215.850 231.601 1.00 23.86 ? 4061 GLU A CB    1 
ATOM   19147 C  CG    . GLU A 1 4061 ? 158.581 214.830 230.538 1.00 21.35 ? 4061 GLU A CG    1 
ATOM   19148 C  CD    . GLU A 1 4061 ? 159.183 213.466 230.813 1.00 29.84 ? 4061 GLU A CD    1 
ATOM   19149 O  OE1   . GLU A 1 4061 ? 159.863 213.313 231.850 1.00 31.13 ? 4061 GLU A OE1   1 
ATOM   19150 O  OE2   . GLU A 1 4061 ? 158.981 212.548 229.993 1.00 30.83 ? 4061 GLU A OE2   1 
ATOM   19151 N  N     . GLN A 1 4062 ? 160.855 218.169 232.481 1.00 18.42 ? 4062 GLN A N     1 
ATOM   19152 C  CA    . GLN A 1 4062 ? 161.439 219.017 233.509 1.00 22.17 ? 4062 GLN A CA    1 
ATOM   19153 C  C     . GLN A 1 4062 ? 161.584 220.465 233.064 1.00 22.95 ? 4062 GLN A C     1 
ATOM   19154 O  O     . GLN A 1 4062 ? 161.960 221.310 233.883 1.00 23.94 ? 4062 GLN A O     1 
ATOM   19155 C  CB    . GLN A 1 4062 ? 162.805 218.467 233.927 1.00 20.24 ? 4062 GLN A CB    1 
ATOM   19156 C  CG    . GLN A 1 4062 ? 162.739 217.106 234.604 1.00 14.92 ? 4062 GLN A CG    1 
ATOM   19157 C  CD    . GLN A 1 4062 ? 161.957 217.135 235.899 1.00 24.49 ? 4062 GLN A CD    1 
ATOM   19158 O  OE1   . GLN A 1 4062 ? 160.852 216.599 235.982 1.00 28.62 ? 4062 GLN A OE1   1 
ATOM   19159 N  NE2   . GLN A 1 4062 ? 162.525 217.768 236.921 1.00 30.51 ? 4062 GLN A NE2   1 
ATOM   19160 N  N     . ASN A 1 4063 ? 161.298 220.763 231.793 1.00 22.74 ? 4063 ASN A N     1 
ATOM   19161 C  CA    . ASN A 1 4063 ? 161.480 222.099 231.225 1.00 19.76 ? 4063 ASN A CA    1 
ATOM   19162 C  C     . ASN A 1 4063 ? 162.913 222.585 231.428 1.00 22.60 ? 4063 ASN A C     1 
ATOM   19163 O  O     . ASN A 1 4063 ? 163.160 223.761 231.701 1.00 32.15 ? 4063 ASN A O     1 
ATOM   19164 C  CB    . ASN A 1 4063 ? 160.473 223.097 231.802 1.00 20.16 ? 4063 ASN A CB    1 
ATOM   19165 C  CG    . ASN A 1 4063 ? 159.169 223.118 231.032 1.00 28.95 ? 4063 ASN A CG    1 
ATOM   19166 O  OD1   . ASN A 1 4063 ? 158.147 222.618 231.503 1.00 29.66 ? 4063 ASN A OD1   1 
ATOM   19167 N  ND2   . ASN A 1 4063 ? 159.199 223.695 229.836 1.00 32.38 ? 4063 ASN A ND2   1 
ATOM   19168 N  N     . THR A 1 4064 ? 163.860 221.663 231.303 1.00 17.22 ? 4064 THR A N     1 
ATOM   19169 C  CA    . THR A 1 4064 ? 165.280 221.959 231.401 1.00 13.76 ? 4064 THR A CA    1 
ATOM   19170 C  C     . THR A 1 4064 ? 165.918 221.914 230.019 1.00 18.63 ? 4064 THR A C     1 
ATOM   19171 O  O     . THR A 1 4064 ? 165.442 221.224 229.113 1.00 17.75 ? 4064 THR A O     1 
ATOM   19172 C  CB    . THR A 1 4064 ? 165.982 220.976 232.345 1.00 16.68 ? 4064 THR A CB    1 
ATOM   19173 O  OG1   . THR A 1 4064 ? 167.339 221.386 232.554 1.00 18.02 ? 4064 THR A OG1   1 
ATOM   19174 C  CG2   . THR A 1 4064 ? 165.963 219.569 231.781 1.00 14.23 ? 4064 THR A CG2   1 
ATOM   19175 N  N     . GLN A 1 4065 ? 166.995 222.673 229.860 1.00 14.40 ? 4065 GLN A N     1 
ATOM   19176 C  CA    . GLN A 1 4065 ? 167.700 222.760 228.592 1.00 15.05 ? 4065 GLN A CA    1 
ATOM   19177 C  C     . GLN A 1 4065 ? 168.752 221.665 228.506 1.00 11.67 ? 4065 GLN A C     1 
ATOM   19178 O  O     . GLN A 1 4065 ? 169.403 221.333 229.500 1.00 16.26 ? 4065 GLN A O     1 
ATOM   19179 C  CB    . GLN A 1 4065 ? 168.347 224.135 228.433 1.00 15.17 ? 4065 GLN A CB    1 
ATOM   19180 C  CG    . GLN A 1 4065 ? 167.354 225.280 228.407 1.00 16.69 ? 4065 GLN A CG    1 
ATOM   19181 C  CD    . GLN A 1 4065 ? 166.247 225.061 227.395 1.00 24.90 ? 4065 GLN A CD    1 
ATOM   19182 O  OE1   . GLN A 1 4065 ? 166.490 225.032 226.190 1.00 27.46 ? 4065 GLN A OE1   1 
ATOM   19183 N  NE2   . GLN A 1 4065 ? 165.021 224.901 227.883 1.00 22.75 ? 4065 GLN A NE2   1 
ATOM   19184 N  N     . ILE A 1 4066 ? 168.906 221.093 227.315 1.00 8.69  ? 4066 ILE A N     1 
ATOM   19185 C  CA    . ILE A 1 4066 ? 169.838 219.995 227.098 1.00 6.58  ? 4066 ILE A CA    1 
ATOM   19186 C  C     . ILE A 1 4066 ? 170.551 220.195 225.768 1.00 8.22  ? 4066 ILE A C     1 
ATOM   19187 O  O     . ILE A 1 4066 ? 169.942 220.616 224.778 1.00 14.71 ? 4066 ILE A O     1 
ATOM   19188 C  CB    . ILE A 1 4066 ? 169.124 218.626 227.150 1.00 6.44  ? 4066 ILE A CB    1 
ATOM   19189 C  CG1   . ILE A 1 4066 ? 170.125 217.488 226.936 1.00 3.98  ? 4066 ILE A CG1   1 
ATOM   19190 C  CG2   . ILE A 1 4066 ? 167.990 218.565 226.139 1.00 5.02  ? 4066 ILE A CG2   1 
ATOM   19191 C  CD1   . ILE A 1 4066 ? 169.711 216.187 227.564 1.00 2.96  ? 4066 ILE A CD1   1 
ATOM   19192 N  N     . THR A 1 4067 ? 171.848 219.904 225.752 1.00 7.13  ? 4067 THR A N     1 
ATOM   19193 C  CA    . THR A 1 4067 ? 172.658 219.922 224.542 1.00 4.94  ? 4067 THR A CA    1 
ATOM   19194 C  C     . THR A 1 4067 ? 172.985 218.481 224.170 1.00 4.32  ? 4067 THR A C     1 
ATOM   19195 O  O     . THR A 1 4067 ? 173.589 217.755 224.967 1.00 3.08  ? 4067 THR A O     1 
ATOM   19196 C  CB    . THR A 1 4067 ? 173.940 220.731 224.747 1.00 7.80  ? 4067 THR A CB    1 
ATOM   19197 O  OG1   . THR A 1 4067 ? 173.614 222.116 224.899 1.00 17.27 ? 4067 THR A OG1   1 
ATOM   19198 C  CG2   . THR A 1 4067 ? 174.878 220.565 223.558 1.00 2.02  ? 4067 THR A CG2   1 
ATOM   19199 N  N     . SER A 1 4068 ? 172.586 218.075 222.969 1.00 3.15  ? 4068 SER A N     1 
ATOM   19200 C  CA    . SER A 1 4068 ? 172.795 216.718 222.484 1.00 1.61  ? 4068 SER A CA    1 
ATOM   19201 C  C     . SER A 1 4068 ? 173.860 216.735 221.399 1.00 1.35  ? 4068 SER A C     1 
ATOM   19202 O  O     . SER A 1 4068 ? 173.801 217.556 220.478 1.00 2.21  ? 4068 SER A O     1 
ATOM   19203 C  CB    . SER A 1 4068 ? 171.495 216.122 221.941 1.00 2.83  ? 4068 SER A CB    1 
ATOM   19204 O  OG    . SER A 1 4068 ? 170.456 216.227 222.894 1.00 8.40  ? 4068 SER A OG    1 
ATOM   19205 N  N     . ILE A 1 4069 ? 174.835 215.838 221.514 1.00 1.75  ? 4069 ILE A N     1 
ATOM   19206 C  CA    . ILE A 1 4069 ? 175.974 215.790 220.607 1.00 1.04  ? 4069 ILE A CA    1 
ATOM   19207 C  C     . ILE A 1 4069 ? 176.230 214.346 220.202 1.00 0.78  ? 4069 ILE A C     1 
ATOM   19208 O  O     . ILE A 1 4069 ? 176.279 213.456 221.057 1.00 1.46  ? 4069 ILE A O     1 
ATOM   19209 C  CB    . ILE A 1 4069 ? 177.236 216.399 221.249 1.00 2.23  ? 4069 ILE A CB    1 
ATOM   19210 C  CG1   . ILE A 1 4069 ? 176.951 217.821 221.737 1.00 1.73  ? 4069 ILE A CG1   1 
ATOM   19211 C  CG2   . ILE A 1 4069 ? 178.392 216.391 220.271 1.00 1.37  ? 4069 ILE A CG2   1 
ATOM   19212 C  CD1   . ILE A 1 4069 ? 178.068 218.430 222.511 1.00 3.42  ? 4069 ILE A CD1   1 
ATOM   19213 N  N     . ALA A 1 4070 ? 176.384 214.116 218.901 1.00 1.98  ? 4070 ALA A N     1 
ATOM   19214 C  CA    . ALA A 1 4070 ? 176.942 212.866 218.407 1.00 0.93  ? 4070 ALA A CA    1 
ATOM   19215 C  C     . ALA A 1 4070 ? 178.463 212.912 218.495 1.00 3.04  ? 4070 ALA A C     1 
ATOM   19216 O  O     . ALA A 1 4070 ? 179.080 213.975 218.388 1.00 9.36  ? 4070 ALA A O     1 
ATOM   19217 C  CB    . ALA A 1 4070 ? 176.500 212.609 216.970 1.00 1.50  ? 4070 ALA A CB    1 
ATOM   19218 N  N     . ILE A 1 4071 ? 179.071 211.742 218.674 1.00 1.50  ? 4071 ILE A N     1 
ATOM   19219 C  CA    . ILE A 1 4071 ? 180.443 211.670 219.169 1.00 4.91  ? 4071 ILE A CA    1 
ATOM   19220 C  C     . ILE A 1 4071 ? 181.469 211.460 218.060 1.00 9.66  ? 4071 ILE A C     1 
ATOM   19221 O  O     . ILE A 1 4071 ? 182.615 211.912 218.173 1.00 10.07 ? 4071 ILE A O     1 
ATOM   19222 C  CB    . ILE A 1 4071 ? 180.540 210.572 220.248 1.00 2.77  ? 4071 ILE A CB    1 
ATOM   19223 C  CG1   . ILE A 1 4071 ? 179.836 211.048 221.517 1.00 3.87  ? 4071 ILE A CG1   1 
ATOM   19224 C  CG2   . ILE A 1 4071 ? 181.974 210.198 220.552 1.00 1.16  ? 4071 ILE A CG2   1 
ATOM   19225 C  CD1   . ILE A 1 4071 ? 180.261 212.433 221.953 1.00 5.29  ? 4071 ILE A CD1   1 
ATOM   19226 N  N     . GLY A 1 4072 ? 181.058 210.819 216.964 1.00 2.84  ? 4072 GLY A N     1 
ATOM   19227 C  CA    . GLY A 1 4072 ? 182.023 210.308 216.001 1.00 1.57  ? 4072 GLY A CA    1 
ATOM   19228 C  C     . GLY A 1 4072 ? 182.937 211.355 215.389 1.00 2.91  ? 4072 GLY A C     1 
ATOM   19229 O  O     . GLY A 1 4072 ? 184.114 211.083 215.141 1.00 5.69  ? 4072 GLY A O     1 
ATOM   19230 N  N     . SER A 1 4073 ? 182.419 212.550 215.125 1.00 4.21  ? 4073 SER A N     1 
ATOM   19231 C  CA    . SER A 1 4073 ? 183.205 213.571 214.443 1.00 3.05  ? 4073 SER A CA    1 
ATOM   19232 C  C     . SER A 1 4073 ? 184.299 214.132 215.346 1.00 7.65  ? 4073 SER A C     1 
ATOM   19233 O  O     . SER A 1 4073 ? 184.191 214.124 216.575 1.00 9.06  ? 4073 SER A O     1 
ATOM   19234 C  CB    . SER A 1 4073 ? 182.301 214.710 213.968 1.00 3.47  ? 4073 SER A CB    1 
ATOM   19235 O  OG    . SER A 1 4073 ? 183.059 215.792 213.463 1.00 7.93  ? 4073 SER A OG    1 
ATOM   19236 N  N     . ALA A 1 4074 ? 185.367 214.624 214.714 1.00 9.55  ? 4074 ALA A N     1 
ATOM   19237 C  CA    . ALA A 1 4074 ? 186.391 215.356 215.451 1.00 4.39  ? 4074 ALA A CA    1 
ATOM   19238 C  C     . ALA A 1 4074 ? 185.825 216.645 216.032 1.00 7.25  ? 4074 ALA A C     1 
ATOM   19239 O  O     . ALA A 1 4074 ? 186.173 217.035 217.153 1.00 15.22 ? 4074 ALA A O     1 
ATOM   19240 C  CB    . ALA A 1 4074 ? 187.585 215.651 214.546 1.00 2.82  ? 4074 ALA A CB    1 
ATOM   19241 N  N     . GLU A 1 4075 ? 184.958 217.324 215.278 1.00 5.57  ? 4075 GLU A N     1 
ATOM   19242 C  CA    . GLU A 1 4075 ? 184.277 218.501 215.807 1.00 8.43  ? 4075 GLU A CA    1 
ATOM   19243 C  C     . GLU A 1 4075 ? 183.352 218.141 216.961 1.00 7.82  ? 4075 GLU A C     1 
ATOM   19244 O  O     . GLU A 1 4075 ? 183.131 218.961 217.859 1.00 9.25  ? 4075 GLU A O     1 
ATOM   19245 C  CB    . GLU A 1 4075 ? 183.497 219.196 214.690 1.00 8.11  ? 4075 GLU A CB    1 
ATOM   19246 C  CG    . GLU A 1 4075 ? 182.777 220.465 215.119 1.00 8.66  ? 4075 GLU A CG    1 
ATOM   19247 C  CD    . GLU A 1 4075 ? 183.731 221.566 215.544 1.00 20.96 ? 4075 GLU A CD    1 
ATOM   19248 O  OE1   . GLU A 1 4075 ? 184.890 221.571 215.077 1.00 21.29 ? 4075 GLU A OE1   1 
ATOM   19249 O  OE2   . GLU A 1 4075 ? 183.320 222.426 216.351 1.00 21.58 ? 4075 GLU A OE2   1 
ATOM   19250 N  N     . GLY A 1 4076 ? 182.804 216.923 216.956 1.00 6.37  ? 4076 GLY A N     1 
ATOM   19251 C  CA    . GLY A 1 4076 ? 181.948 216.507 218.054 1.00 3.40  ? 4076 GLY A CA    1 
ATOM   19252 C  C     . GLY A 1 4076 ? 182.686 216.444 219.377 1.00 5.29  ? 4076 GLY A C     1 
ATOM   19253 O  O     . GLY A 1 4076 ? 182.129 216.777 220.425 1.00 4.23  ? 4076 GLY A O     1 
ATOM   19254 N  N     . PHE A 1 4077 ? 183.948 216.008 219.347 1.00 8.34  ? 4077 PHE A N     1 
ATOM   19255 C  CA    . PHE A 1 4077 ? 184.753 215.978 220.565 1.00 4.46  ? 4077 PHE A CA    1 
ATOM   19256 C  C     . PHE A 1 4077 ? 184.972 217.380 221.115 1.00 6.01  ? 4077 PHE A C     1 
ATOM   19257 O  O     . PHE A 1 4077 ? 184.842 217.608 222.323 1.00 9.13  ? 4077 PHE A O     1 
ATOM   19258 C  CB    . PHE A 1 4077 ? 186.090 215.296 220.287 1.00 2.40  ? 4077 PHE A CB    1 
ATOM   19259 C  CG    . PHE A 1 4077 ? 185.972 213.832 219.998 1.00 3.45  ? 4077 PHE A CG    1 
ATOM   19260 C  CD1   . PHE A 1 4077 ? 185.250 213.003 220.837 1.00 2.52  ? 4077 PHE A CD1   1 
ATOM   19261 C  CD2   . PHE A 1 4077 ? 186.563 213.288 218.871 1.00 5.73  ? 4077 PHE A CD2   1 
ATOM   19262 C  CE1   . PHE A 1 4077 ? 185.139 211.657 220.568 1.00 4.20  ? 4077 PHE A CE1   1 
ATOM   19263 C  CE2   . PHE A 1 4077 ? 186.449 211.944 218.595 1.00 4.20  ? 4077 PHE A CE2   1 
ATOM   19264 C  CZ    . PHE A 1 4077 ? 185.736 211.127 219.443 1.00 4.80  ? 4077 PHE A CZ    1 
ATOM   19265 N  N     . ASN A 1 4078 ? 185.308 218.333 220.243 1.00 6.37  ? 4078 ASN A N     1 
ATOM   19266 C  CA    . ASN A 1 4078 ? 185.484 219.710 220.690 1.00 5.36  ? 4078 ASN A CA    1 
ATOM   19267 C  C     . ASN A 1 4078 ? 184.181 220.280 221.229 1.00 5.16  ? 4078 ASN A C     1 
ATOM   19268 O  O     . ASN A 1 4078 ? 184.168 220.952 222.267 1.00 5.86  ? 4078 ASN A O     1 
ATOM   19269 C  CB    . ASN A 1 4078 ? 186.010 220.578 219.545 1.00 5.92  ? 4078 ASN A CB    1 
ATOM   19270 C  CG    . ASN A 1 4078 ? 187.299 220.048 218.953 1.00 13.40 ? 4078 ASN A CG    1 
ATOM   19271 O  OD1   . ASN A 1 4078 ? 188.145 219.504 219.662 1.00 17.61 ? 4078 ASN A OD1   1 
ATOM   19272 N  ND2   . ASN A 1 4078 ? 187.458 220.212 217.645 1.00 19.38 ? 4078 ASN A ND2   1 
ATOM   19273 N  N     . GLN A 1 4079 ? 183.071 220.019 220.535 1.00 6.59  ? 4079 GLN A N     1 
ATOM   19274 C  CA    . GLN A 1 4079 ? 181.782 220.525 220.989 1.00 6.63  ? 4079 GLN A CA    1 
ATOM   19275 C  C     . GLN A 1 4079 ? 181.379 219.897 222.317 1.00 5.34  ? 4079 GLN A C     1 
ATOM   19276 O  O     . GLN A 1 4079 ? 180.794 220.570 223.174 1.00 6.08  ? 4079 GLN A O     1 
ATOM   19277 C  CB    . GLN A 1 4079 ? 180.715 220.268 219.926 1.00 6.01  ? 4079 GLN A CB    1 
ATOM   19278 C  CG    . GLN A 1 4079 ? 179.361 220.841 220.276 1.00 11.21 ? 4079 GLN A CG    1 
ATOM   19279 C  CD    . GLN A 1 4079 ? 178.330 220.627 219.189 1.00 19.56 ? 4079 GLN A CD    1 
ATOM   19280 O  OE1   . GLN A 1 4079 ? 178.609 220.007 218.165 1.00 14.26 ? 4079 GLN A OE1   1 
ATOM   19281 N  NE2   . GLN A 1 4079 ? 177.126 221.142 219.409 1.00 27.68 ? 4079 GLN A NE2   1 
ATOM   19282 N  N     . ALA A 1 4080 ? 181.683 218.611 222.506 1.00 5.01  ? 4080 ALA A N     1 
ATOM   19283 C  CA    . ALA A 1 4080 ? 181.332 217.939 223.754 1.00 3.51  ? 4080 ALA A CA    1 
ATOM   19284 C  C     . ALA A 1 4080 ? 182.047 218.571 224.939 1.00 4.51  ? 4080 ALA A C     1 
ATOM   19285 O  O     . ALA A 1 4080 ? 181.443 218.806 225.990 1.00 6.82  ? 4080 ALA A O     1 
ATOM   19286 C  CB    . ALA A 1 4080 ? 181.656 216.448 223.659 1.00 2.35  ? 4080 ALA A CB    1 
ATOM   19287 N  N     . ASP A 1 4081 ? 183.340 218.863 224.782 1.00 5.53  ? 4081 ASP A N     1 
ATOM   19288 C  CA    . ASP A 1 4081 ? 184.097 219.465 225.873 1.00 4.50  ? 4081 ASP A CA    1 
ATOM   19289 C  C     . ASP A 1 4081 ? 183.562 220.848 226.225 1.00 9.39  ? 4081 ASP A C     1 
ATOM   19290 O  O     . ASP A 1 4081 ? 183.403 221.175 227.407 1.00 9.18  ? 4081 ASP A O     1 
ATOM   19291 C  CB    . ASP A 1 4081 ? 185.578 219.537 225.505 1.00 6.98  ? 4081 ASP A CB    1 
ATOM   19292 C  CG    . ASP A 1 4081 ? 186.409 220.220 226.570 1.00 15.79 ? 4081 ASP A CG    1 
ATOM   19293 O  OD1   . ASP A 1 4081 ? 186.664 221.436 226.435 1.00 20.66 ? 4081 ASP A OD1   1 
ATOM   19294 O  OD2   . ASP A 1 4081 ? 186.808 219.544 227.540 1.00 14.26 ? 4081 ASP A OD2   1 
ATOM   19295 N  N     . LYS A 1 4082 ? 183.270 221.673 225.216 1.00 7.06  ? 4082 LYS A N     1 
ATOM   19296 C  CA    . LYS A 1 4082 ? 182.726 222.999 225.493 1.00 6.36  ? 4082 LYS A CA    1 
ATOM   19297 C  C     . LYS A 1 4082 ? 181.344 222.912 226.129 1.00 7.10  ? 4082 LYS A C     1 
ATOM   19298 O  O     . LYS A 1 4082 ? 181.037 223.663 227.061 1.00 8.37  ? 4082 LYS A O     1 
ATOM   19299 C  CB    . LYS A 1 4082 ? 182.676 223.845 224.220 1.00 9.13  ? 4082 LYS A CB    1 
ATOM   19300 C  CG    . LYS A 1 4082 ? 184.032 224.156 223.607 1.00 13.78 ? 4082 LYS A CG    1 
ATOM   19301 C  CD    . LYS A 1 4082 ? 183.893 225.065 222.389 1.00 15.58 ? 4082 LYS A CD    1 
ATOM   19302 C  CE    . LYS A 1 4082 ? 183.267 224.360 221.197 1.00 13.57 ? 4082 LYS A CE    1 
ATOM   19303 N  NZ    . LYS A 1 4082 ? 184.135 223.280 220.665 1.00 10.96 ? 4082 LYS A NZ    1 
ATOM   19304 N  N     . ALA A 1 4083 ? 180.493 222.007 225.636 1.00 7.79  ? 4083 ALA A N     1 
ATOM   19305 C  CA    . ALA A 1 4083 ? 179.161 221.859 226.213 1.00 5.51  ? 4083 ALA A CA    1 
ATOM   19306 C  C     . ALA A 1 4083 ? 179.238 221.399 227.663 1.00 6.03  ? 4083 ALA A C     1 
ATOM   19307 O  O     . ALA A 1 4083 ? 178.510 221.908 228.522 1.00 5.83  ? 4083 ALA A O     1 
ATOM   19308 C  CB    . ALA A 1 4083 ? 178.332 220.881 225.382 1.00 3.91  ? 4083 ALA A CB    1 
ATOM   19309 N  N     . ILE A 1 4084 ? 180.119 220.441 227.952 1.00 4.32  ? 4084 ILE A N     1 
ATOM   19310 C  CA    . ILE A 1 4084 ? 180.275 219.950 229.319 1.00 3.95  ? 4084 ILE A CA    1 
ATOM   19311 C  C     . ILE A 1 4084 ? 180.811 221.053 230.224 1.00 7.21  ? 4084 ILE A C     1 
ATOM   19312 O  O     . ILE A 1 4084 ? 180.315 221.263 231.337 1.00 9.31  ? 4084 ILE A O     1 
ATOM   19313 C  CB    . ILE A 1 4084 ? 181.183 218.707 229.336 1.00 4.63  ? 4084 ILE A CB    1 
ATOM   19314 C  CG1   . ILE A 1 4084 ? 180.421 217.490 228.805 1.00 2.26  ? 4084 ILE A CG1   1 
ATOM   19315 C  CG2   . ILE A 1 4084 ? 181.724 218.448 230.732 1.00 3.60  ? 4084 ILE A CG2   1 
ATOM   19316 C  CD1   . ILE A 1 4084 ? 181.294 216.288 228.554 1.00 2.46  ? 4084 ILE A CD1   1 
ATOM   19317 N  N     . ASN A 1 4085 ? 181.825 221.783 229.755 1.00 6.49  ? 4085 ASN A N     1 
ATOM   19318 C  CA    . ASN A 1 4085 ? 182.420 222.841 230.565 1.00 5.00  ? 4085 ASN A CA    1 
ATOM   19319 C  C     . ASN A 1 4085 ? 181.415 223.945 230.863 1.00 7.12  ? 4085 ASN A C     1 
ATOM   19320 O  O     . ASN A 1 4085 ? 181.387 224.489 231.973 1.00 12.86 ? 4085 ASN A O     1 
ATOM   19321 C  CB    . ASN A 1 4085 ? 183.652 223.412 229.862 1.00 6.85  ? 4085 ASN A CB    1 
ATOM   19322 C  CG    . ASN A 1 4085 ? 184.806 222.432 229.825 1.00 6.28  ? 4085 ASN A CG    1 
ATOM   19323 O  OD1   . ASN A 1 4085 ? 184.807 221.429 230.537 1.00 6.85  ? 4085 ASN A OD1   1 
ATOM   19324 N  ND2   . ASN A 1 4085 ? 185.794 222.714 228.986 1.00 6.89  ? 4085 ASN A ND2   1 
ATOM   19325 N  N     . THR A 1 4086 ? 180.593 224.306 229.877 1.00 7.76  ? 4086 THR A N     1 
ATOM   19326 C  CA    . THR A 1 4086 ? 179.550 225.297 230.115 1.00 7.38  ? 4086 THR A CA    1 
ATOM   19327 C  C     . THR A 1 4086 ? 178.480 224.759 231.058 1.00 5.94  ? 4086 THR A C     1 
ATOM   19328 O  O     . THR A 1 4086 ? 177.989 225.485 231.930 1.00 6.89  ? 4086 THR A O     1 
ATOM   19329 C  CB    . THR A 1 4086 ? 178.925 225.731 228.790 1.00 5.54  ? 4086 THR A CB    1 
ATOM   19330 O  OG1   . THR A 1 4086 ? 179.960 226.078 227.864 1.00 8.59  ? 4086 THR A OG1   1 
ATOM   19331 C  CG2   . THR A 1 4086 ? 178.023 226.933 228.997 1.00 6.84  ? 4086 THR A CG2   1 
ATOM   19332 N  N     . ALA A 1 4087 ? 178.111 223.486 230.899 1.00 8.07  ? 4087 ALA A N     1 
ATOM   19333 C  CA    . ALA A 1 4087 ? 177.008 222.924 231.669 1.00 6.92  ? 4087 ALA A CA    1 
ATOM   19334 C  C     . ALA A 1 4087 ? 177.361 222.746 233.140 1.00 9.30  ? 4087 ALA A C     1 
ATOM   19335 O  O     . ALA A 1 4087 ? 176.497 222.923 234.005 1.00 9.92  ? 4087 ALA A O     1 
ATOM   19336 C  CB    . ALA A 1 4087 ? 176.575 221.590 231.066 1.00 7.01  ? 4087 ALA A CB    1 
ATOM   19337 N  N     . VAL A 1 4088 ? 178.611 222.393 233.445 1.00 6.84  ? 4088 VAL A N     1 
ATOM   19338 C  CA    . VAL A 1 4088 ? 178.999 222.157 234.831 1.00 5.88  ? 4088 VAL A CA    1 
ATOM   19339 C  C     . VAL A 1 4088 ? 179.028 223.432 235.657 1.00 11.89 ? 4088 VAL A C     1 
ATOM   19340 O  O     . VAL A 1 4088 ? 179.152 223.361 236.884 1.00 18.26 ? 4088 VAL A O     1 
ATOM   19341 C  CB    . VAL A 1 4088 ? 180.371 221.459 234.906 1.00 8.19  ? 4088 VAL A CB    1 
ATOM   19342 C  CG1   . VAL A 1 4088 ? 180.296 220.080 234.271 1.00 3.33  ? 4088 VAL A CG1   1 
ATOM   19343 C  CG2   . VAL A 1 4088 ? 181.445 222.307 234.256 1.00 7.92  ? 4088 VAL A CG2   1 
ATOM   19344 N  N     . LYS A 1 4089 ? 178.917 224.594 235.017 1.00 10.18 ? 4089 LYS A N     1 
ATOM   19345 C  CA    . LYS A 1 4089 ? 178.844 225.863 235.722 1.00 8.83  ? 4089 LYS A CA    1 
ATOM   19346 C  C     . LYS A 1 4089 ? 177.456 226.483 235.716 1.00 9.67  ? 4089 LYS A C     1 
ATOM   19347 O  O     . LYS A 1 4089 ? 177.263 227.524 236.351 1.00 23.73 ? 4089 LYS A O     1 
ATOM   19348 C  CB    . LYS A 1 4089 ? 179.842 226.866 235.122 1.00 10.31 ? 4089 LYS A CB    1 
ATOM   19349 C  CG    . LYS A 1 4089 ? 181.297 226.501 235.327 1.00 13.51 ? 4089 LYS A CG    1 
ATOM   19350 C  CD    . LYS A 1 4089 ? 182.202 227.623 234.850 1.00 11.92 ? 4089 LYS A CD    1 
ATOM   19351 C  CE    . LYS A 1 4089 ? 182.247 227.693 233.334 1.00 18.93 ? 4089 LYS A CE    1 
ATOM   19352 N  NZ    . LYS A 1 4089 ? 183.214 228.717 232.854 1.00 26.90 ? 4089 LYS A NZ    1 
ATOM   19353 N  N     . SER A 1 4090 ? 176.489 225.883 235.018 1.00 8.63  ? 4090 SER A N     1 
ATOM   19354 C  CA    . SER A 1 4090 ? 175.150 226.444 234.913 1.00 9.50  ? 4090 SER A CA    1 
ATOM   19355 C  C     . SER A 1 4090 ? 174.028 225.468 235.233 1.00 13.39 ? 4090 SER A C     1 
ATOM   19356 O  O     . SER A 1 4090 ? 172.863 225.880 235.219 1.00 19.35 ? 4090 SER A O     1 
ATOM   19357 C  CB    . SER A 1 4090 ? 174.913 227.009 233.502 1.00 7.86  ? 4090 SER A CB    1 
ATOM   19358 O  OG    . SER A 1 4090 ? 174.982 225.988 232.524 1.00 12.93 ? 4090 SER A OG    1 
ATOM   19359 N  N     . GLY A 1 4091 ? 174.331 224.203 235.510 1.00 9.74  ? 4091 GLY A N     1 
ATOM   19360 C  CA    . GLY A 1 4091 ? 173.300 223.208 235.725 1.00 6.42  ? 4091 GLY A CA    1 
ATOM   19361 C  C     . GLY A 1 4091 ? 172.676 222.659 234.465 1.00 8.55  ? 4091 GLY A C     1 
ATOM   19362 O  O     . GLY A 1 4091 ? 171.676 221.938 234.549 1.00 10.13 ? 4091 GLY A O     1 
ATOM   19363 N  N     . ARG A 1 4092 ? 173.232 222.986 233.302 1.00 13.21 ? 4092 ARG A N     1 
ATOM   19364 C  CA    . ARG A 1 4092 ? 172.745 222.526 232.013 1.00 7.23  ? 4092 ARG A CA    1 
ATOM   19365 C  C     . ARG A 1 4092 ? 172.943 221.013 231.883 1.00 6.50  ? 4092 ARG A C     1 
ATOM   19366 O  O     . ARG A 1 4092 ? 173.816 220.416 232.517 1.00 9.16  ? 4092 ARG A O     1 
ATOM   19367 C  CB    . ARG A 1 4092 ? 173.480 223.286 230.905 1.00 12.44 ? 4092 ARG A CB    1 
ATOM   19368 C  CG    . ARG A 1 4092 ? 173.124 222.963 229.465 1.00 15.70 ? 4092 ARG A CG    1 
ATOM   19369 C  CD    . ARG A 1 4092 ? 171.726 223.416 229.132 1.00 17.17 ? 4092 ARG A CD    1 
ATOM   19370 N  NE    . ARG A 1 4092 ? 171.381 223.133 227.744 1.00 22.77 ? 4092 ARG A NE    1 
ATOM   19371 C  CZ    . ARG A 1 4092 ? 171.599 223.969 226.740 1.00 12.39 ? 4092 ARG A CZ    1 
ATOM   19372 N  NH1   . ARG A 1 4092 ? 172.141 225.159 226.939 1.00 15.54 ? 4092 ARG A NH1   1 
ATOM   19373 N  NH2   . ARG A 1 4092 ? 171.263 223.604 225.507 1.00 10.11 ? 4092 ARG A NH2   1 
ATOM   19374 N  N     . TRP A 1 4093 ? 172.105 220.387 231.063 1.00 8.64  ? 4093 TRP A N     1 
ATOM   19375 C  CA    . TRP A 1 4093 ? 172.188 218.962 230.777 1.00 3.02  ? 4093 TRP A CA    1 
ATOM   19376 C  C     . TRP A 1 4093 ? 172.912 218.732 229.456 1.00 2.71  ? 4093 TRP A C     1 
ATOM   19377 O  O     . TRP A 1 4093 ? 172.708 219.470 228.488 1.00 4.19  ? 4093 TRP A O     1 
ATOM   19378 C  CB    . TRP A 1 4093 ? 170.796 218.328 230.723 1.00 2.67  ? 4093 TRP A CB    1 
ATOM   19379 C  CG    . TRP A 1 4093 ? 170.190 218.053 232.064 1.00 3.25  ? 4093 TRP A CG    1 
ATOM   19380 C  CD1   . TRP A 1 4093 ? 170.615 218.525 233.269 1.00 2.47  ? 4093 TRP A CD1   1 
ATOM   19381 C  CD2   . TRP A 1 4093 ? 169.016 217.277 232.331 1.00 2.92  ? 4093 TRP A CD2   1 
ATOM   19382 N  NE1   . TRP A 1 4093 ? 169.797 218.073 234.271 1.00 1.67  ? 4093 TRP A NE1   1 
ATOM   19383 C  CE2   . TRP A 1 4093 ? 168.804 217.307 233.721 1.00 1.36  ? 4093 TRP A CE2   1 
ATOM   19384 C  CE3   . TRP A 1 4093 ? 168.128 216.554 231.529 1.00 2.29  ? 4093 TRP A CE3   1 
ATOM   19385 C  CZ2   . TRP A 1 4093 ? 167.744 216.641 234.328 1.00 2.85  ? 4093 TRP A CZ2   1 
ATOM   19386 C  CZ3   . TRP A 1 4093 ? 167.078 215.893 232.133 1.00 3.38  ? 4093 TRP A CZ3   1 
ATOM   19387 C  CH2   . TRP A 1 4093 ? 166.893 215.941 233.519 1.00 5.56  ? 4093 TRP A CH2   1 
ATOM   19388 N  N     . VAL A 1 4094 ? 173.764 217.711 229.426 1.00 1.15  ? 4094 VAL A N     1 
ATOM   19389 C  CA    . VAL A 1 4094 ? 174.507 217.326 228.231 1.00 1.48  ? 4094 VAL A CA    1 
ATOM   19390 C  C     . VAL A 1 4094 ? 174.281 215.842 227.983 1.00 0.81  ? 4094 VAL A C     1 
ATOM   19391 O  O     . VAL A 1 4094 ? 174.446 215.026 228.896 1.00 0.74  ? 4094 VAL A O     1 
ATOM   19392 C  CB    . VAL A 1 4094 ? 176.011 217.632 228.370 1.00 0.95  ? 4094 VAL A CB    1 
ATOM   19393 C  CG1   . VAL A 1 4094 ? 176.777 217.099 227.172 1.00 0.57  ? 4094 VAL A CG1   1 
ATOM   19394 C  CG2   . VAL A 1 4094 ? 176.242 219.119 228.526 1.00 1.35  ? 4094 VAL A CG2   1 
ATOM   19395 N  N     . MET A 1 4095 ? 173.907 215.494 226.754 1.00 0.67  ? 4095 MET A N     1 
ATOM   19396 C  CA    . MET A 1 4095 ? 173.782 214.101 226.344 1.00 0.41  ? 4095 MET A CA    1 
ATOM   19397 C  C     . MET A 1 4095 ? 174.715 213.843 225.171 1.00 0.32  ? 4095 MET A C     1 
ATOM   19398 O  O     . MET A 1 4095 ? 174.676 214.564 224.170 1.00 0.51  ? 4095 MET A O     1 
ATOM   19399 C  CB    . MET A 1 4095 ? 172.341 213.745 225.974 1.00 0.71  ? 4095 MET A CB    1 
ATOM   19400 C  CG    . MET A 1 4095 ? 172.211 212.373 225.326 1.00 0.51  ? 4095 MET A CG    1 
ATOM   19401 S  SD    . MET A 1 4095 ? 170.519 211.880 224.960 1.00 8.70  ? 4095 MET A SD    1 
ATOM   19402 C  CE    . MET A 1 4095 ? 169.906 213.340 224.134 1.00 2.96  ? 4095 MET A CE    1 
ATOM   19403 N  N     . LEU A 1 4096 ? 175.549 212.815 225.298 1.00 0.31  ? 4096 LEU A N     1 
ATOM   19404 C  CA    . LEU A 1 4096 ? 176.465 212.396 224.248 1.00 0.24  ? 4096 LEU A CA    1 
ATOM   19405 C  C     . LEU A 1 4096 ? 176.031 211.023 223.752 1.00 0.43  ? 4096 LEU A C     1 
ATOM   19406 O  O     . LEU A 1 4096 ? 175.933 210.077 224.540 1.00 0.42  ? 4096 LEU A O     1 
ATOM   19407 C  CB    . LEU A 1 4096 ? 177.903 212.373 224.763 1.00 0.27  ? 4096 LEU A CB    1 
ATOM   19408 C  CG    . LEU A 1 4096 ? 178.350 213.670 225.450 1.00 0.29  ? 4096 LEU A CG    1 
ATOM   19409 C  CD1   . LEU A 1 4096 ? 179.785 213.584 225.921 1.00 0.30  ? 4096 LEU A CD1   1 
ATOM   19410 C  CD2   . LEU A 1 4096 ? 178.162 214.869 224.534 1.00 0.33  ? 4096 LEU A CD2   1 
ATOM   19411 N  N     . LYS A 1 4097 ? 175.772 210.918 222.453 1.00 0.70  ? 4097 LYS A N     1 
ATOM   19412 C  CA    . LYS A 1 4097 ? 175.218 209.709 221.863 1.00 0.48  ? 4097 LYS A CA    1 
ATOM   19413 C  C     . LYS A 1 4097 ? 176.296 208.904 221.154 1.00 0.43  ? 4097 LYS A C     1 
ATOM   19414 O  O     . LYS A 1 4097 ? 177.241 209.458 220.587 1.00 1.25  ? 4097 LYS A O     1 
ATOM   19415 C  CB    . LYS A 1 4097 ? 174.099 210.045 220.875 1.00 0.84  ? 4097 LYS A CB    1 
ATOM   19416 C  CG    . LYS A 1 4097 ? 173.163 211.142 221.328 1.00 1.56  ? 4097 LYS A CG    1 
ATOM   19417 C  CD    . LYS A 1 4097 ? 172.125 211.432 220.257 1.00 5.14  ? 4097 LYS A CD    1 
ATOM   19418 C  CE    . LYS A 1 4097 ? 171.763 212.902 220.219 1.00 4.20  ? 4097 LYS A CE    1 
ATOM   19419 N  NZ    . LYS A 1 4097 ? 170.858 213.211 219.081 1.00 5.79  ? 4097 LYS A NZ    1 
ATOM   19420 N  N     . ASN A 1 4098 ? 176.133 207.580 221.185 1.00 0.45  ? 4098 ASN A N     1 
ATOM   19421 C  CA    . ASN A 1 4098 ? 177.022 206.643 220.495 1.00 0.69  ? 4098 ASN A CA    1 
ATOM   19422 C  C     . ASN A 1 4098 ? 178.466 206.787 220.967 1.00 0.65  ? 4098 ASN A C     1 
ATOM   19423 O  O     . ASN A 1 4098 ? 179.403 206.770 220.169 1.00 1.26  ? 4098 ASN A O     1 
ATOM   19424 C  CB    . ASN A 1 4098 ? 176.926 206.809 218.976 1.00 0.74  ? 4098 ASN A CB    1 
ATOM   19425 C  CG    . ASN A 1 4098 ? 175.495 206.837 218.480 1.00 0.39  ? 4098 ASN A CG    1 
ATOM   19426 O  OD1   . ASN A 1 4098 ? 174.768 205.856 218.602 1.00 0.87  ? 4098 ASN A OD1   1 
ATOM   19427 N  ND2   . ASN A 1 4098 ? 175.086 207.964 217.914 1.00 0.28  ? 4098 ASN A ND2   1 
ATOM   19428 N  N     . VAL A 1 4099 ? 178.651 206.921 222.282 1.00 0.61  ? 4099 VAL A N     1 
ATOM   19429 C  CA    . VAL A 1 4099 ? 179.993 207.093 222.828 1.00 0.56  ? 4099 VAL A CA    1 
ATOM   19430 C  C     . VAL A 1 4099 ? 180.811 205.814 222.731 1.00 0.77  ? 4099 VAL A C     1 
ATOM   19431 O  O     . VAL A 1 4099 ? 182.039 205.860 222.859 1.00 0.88  ? 4099 VAL A O     1 
ATOM   19432 C  CB    . VAL A 1 4099 ? 179.927 207.591 224.283 1.00 0.31  ? 4099 VAL A CB    1 
ATOM   19433 C  CG1   . VAL A 1 4099 ? 179.110 208.868 224.365 1.00 0.36  ? 4099 VAL A CG1   1 
ATOM   19434 C  CG2   . VAL A 1 4099 ? 179.356 206.520 225.194 1.00 0.52  ? 4099 VAL A CG2   1 
ATOM   19435 N  N     . HIS A 1 4100 ? 180.164 204.669 222.502 1.00 0.53  ? 4100 HIS A N     1 
ATOM   19436 C  CA    . HIS A 1 4100 ? 180.886 203.423 222.280 1.00 0.63  ? 4100 HIS A CA    1 
ATOM   19437 C  C     . HIS A 1 4100 ? 181.718 203.451 221.005 1.00 0.98  ? 4100 HIS A C     1 
ATOM   19438 O  O     . HIS A 1 4100 ? 182.583 202.589 220.831 1.00 2.95  ? 4100 HIS A O     1 
ATOM   19439 C  CB    . HIS A 1 4100 ? 179.908 202.249 222.235 1.00 1.08  ? 4100 HIS A CB    1 
ATOM   19440 C  CG    . HIS A 1 4100 ? 178.973 202.285 221.066 1.00 1.44  ? 4100 HIS A CG    1 
ATOM   19441 N  ND1   . HIS A 1 4100 ? 177.857 203.092 221.032 1.00 0.85  ? 4100 HIS A ND1   1 
ATOM   19442 C  CD2   . HIS A 1 4100 ? 178.989 201.615 219.890 1.00 1.63  ? 4100 HIS A CD2   1 
ATOM   19443 C  CE1   . HIS A 1 4100 ? 177.226 202.918 219.885 1.00 0.70  ? 4100 HIS A CE1   1 
ATOM   19444 N  NE2   . HIS A 1 4100 ? 177.893 202.028 219.175 1.00 3.07  ? 4100 HIS A NE2   1 
ATOM   19445 N  N     . LEU A 1 4101 ? 181.473 204.412 220.116 1.00 0.85  ? 4101 LEU A N     1 
ATOM   19446 C  CA    . LEU A 1 4101 ? 182.271 204.569 218.909 1.00 0.97  ? 4101 LEU A CA    1 
ATOM   19447 C  C     . LEU A 1 4101 ? 183.617 205.229 219.169 1.00 1.96  ? 4101 LEU A C     1 
ATOM   19448 O  O     . LEU A 1 4101 ? 184.466 205.236 218.272 1.00 4.23  ? 4101 LEU A O     1 
ATOM   19449 C  CB    . LEU A 1 4101 ? 181.490 205.379 217.872 1.00 1.49  ? 4101 LEU A CB    1 
ATOM   19450 C  CG    . LEU A 1 4101 ? 180.162 204.780 217.408 1.00 2.03  ? 4101 LEU A CG    1 
ATOM   19451 C  CD1   . LEU A 1 4101 ? 179.468 205.706 216.423 1.00 1.16  ? 4101 LEU A CD1   1 
ATOM   19452 C  CD2   . LEU A 1 4101 ? 180.368 203.404 216.798 1.00 0.53  ? 4101 LEU A CD2   1 
ATOM   19453 N  N     . ALA A 1 4102 ? 183.836 205.781 220.360 1.00 2.76  ? 4102 ALA A N     1 
ATOM   19454 C  CA    . ALA A 1 4102 ? 185.099 206.423 220.725 1.00 1.62  ? 4102 ALA A CA    1 
ATOM   19455 C  C     . ALA A 1 4102 ? 185.565 205.900 222.079 1.00 2.60  ? 4102 ALA A C     1 
ATOM   19456 O  O     . ALA A 1 4102 ? 185.559 206.630 223.077 1.00 2.42  ? 4102 ALA A O     1 
ATOM   19457 C  CB    . ALA A 1 4102 ? 184.949 207.943 220.749 1.00 0.76  ? 4102 ALA A CB    1 
ATOM   19458 N  N     . PRO A 1 4103 ? 185.974 204.629 222.149 1.00 4.00  ? 4103 PRO A N     1 
ATOM   19459 C  CA    . PRO A 1 4103 ? 186.423 204.084 223.443 1.00 4.15  ? 4103 PRO A CA    1 
ATOM   19460 C  C     . PRO A 1 4103 ? 187.620 204.813 224.028 1.00 3.65  ? 4103 PRO A C     1 
ATOM   19461 O  O     . PRO A 1 4103 ? 187.695 204.988 225.249 1.00 4.94  ? 4103 PRO A O     1 
ATOM   19462 C  CB    . PRO A 1 4103 ? 186.752 202.622 223.110 1.00 4.04  ? 4103 PRO A CB    1 
ATOM   19463 C  CG    . PRO A 1 4103 ? 186.988 202.608 221.644 1.00 4.43  ? 4103 PRO A CG    1 
ATOM   19464 C  CD    . PRO A 1 4103 ? 186.072 203.634 221.070 1.00 2.94  ? 4103 PRO A CD    1 
ATOM   19465 N  N     . GLY A 1 4104 ? 188.558 205.252 223.186 1.00 3.80  ? 4104 GLY A N     1 
ATOM   19466 C  CA    . GLY A 1 4104 ? 189.721 205.959 223.694 1.00 1.45  ? 4104 GLY A CA    1 
ATOM   19467 C  C     . GLY A 1 4104 ? 189.373 207.300 224.310 1.00 2.46  ? 4104 GLY A C     1 
ATOM   19468 O  O     . GLY A 1 4104 ? 189.889 207.659 225.371 1.00 8.42  ? 4104 GLY A O     1 
ATOM   19469 N  N     . TRP A 1 4105 ? 188.493 208.058 223.653 1.00 1.87  ? 4105 TRP A N     1 
ATOM   19470 C  CA    . TRP A 1 4105 ? 188.076 209.345 224.196 1.00 1.45  ? 4105 TRP A CA    1 
ATOM   19471 C  C     . TRP A 1 4105 ? 187.238 209.170 225.457 1.00 2.21  ? 4105 TRP A C     1 
ATOM   19472 O  O     . TRP A 1 4105 ? 187.223 210.056 226.319 1.00 2.04  ? 4105 TRP A O     1 
ATOM   19473 C  CB    . TRP A 1 4105 ? 187.308 210.126 223.128 1.00 1.45  ? 4105 TRP A CB    1 
ATOM   19474 C  CG    . TRP A 1 4105 ? 186.491 211.257 223.656 1.00 1.03  ? 4105 TRP A CG    1 
ATOM   19475 C  CD1   . TRP A 1 4105 ? 186.917 212.528 223.910 1.00 0.92  ? 4105 TRP A CD1   1 
ATOM   19476 C  CD2   . TRP A 1 4105 ? 185.102 211.226 223.995 1.00 1.23  ? 4105 TRP A CD2   1 
ATOM   19477 N  NE1   . TRP A 1 4105 ? 185.878 213.290 224.384 1.00 1.64  ? 4105 TRP A NE1   1 
ATOM   19478 C  CE2   . TRP A 1 4105 ? 184.753 212.511 224.448 1.00 1.23  ? 4105 TRP A CE2   1 
ATOM   19479 C  CE3   . TRP A 1 4105 ? 184.118 210.233 223.960 1.00 2.17  ? 4105 TRP A CE3   1 
ATOM   19480 C  CZ2   . TRP A 1 4105 ? 183.464 212.830 224.862 1.00 1.90  ? 4105 TRP A CZ2   1 
ATOM   19481 C  CZ3   . TRP A 1 4105 ? 182.842 210.551 224.370 1.00 2.42  ? 4105 TRP A CZ3   1 
ATOM   19482 C  CH2   . TRP A 1 4105 ? 182.525 211.839 224.815 1.00 2.01  ? 4105 TRP A CH2   1 
ATOM   19483 N  N     . LEU A 1 4106 ? 186.548 208.033 225.585 1.00 3.19  ? 4106 LEU A N     1 
ATOM   19484 C  CA    . LEU A 1 4106 ? 185.734 207.773 226.770 1.00 2.41  ? 4106 LEU A CA    1 
ATOM   19485 C  C     . LEU A 1 4106 ? 186.590 207.662 228.024 1.00 5.53  ? 4106 LEU A C     1 
ATOM   19486 O  O     . LEU A 1 4106 ? 186.183 208.113 229.100 1.00 10.30 ? 4106 LEU A O     1 
ATOM   19487 C  CB    . LEU A 1 4106 ? 184.910 206.502 226.570 1.00 2.93  ? 4106 LEU A CB    1 
ATOM   19488 C  CG    . LEU A 1 4106 ? 183.484 206.685 226.049 1.00 1.01  ? 4106 LEU A CG    1 
ATOM   19489 C  CD1   . LEU A 1 4106 ? 182.745 205.360 226.060 1.00 0.61  ? 4106 LEU A CD1   1 
ATOM   19490 C  CD2   . LEU A 1 4106 ? 182.740 207.727 226.863 1.00 0.49  ? 4106 LEU A CD2   1 
ATOM   19491 N  N     . MET A 1 4107 ? 187.773 207.049 227.912 1.00 5.24  ? 4107 MET A N     1 
ATOM   19492 C  CA    . MET A 1 4107 ? 188.672 206.967 229.059 1.00 4.82  ? 4107 MET A CA    1 
ATOM   19493 C  C     . MET A 1 4107 ? 189.086 208.353 229.529 1.00 5.01  ? 4107 MET A C     1 
ATOM   19494 O  O     . MET A 1 4107 ? 189.163 208.613 230.736 1.00 8.65  ? 4107 MET A O     1 
ATOM   19495 C  CB    . MET A 1 4107 ? 189.905 206.135 228.712 1.00 8.13  ? 4107 MET A CB    1 
ATOM   19496 C  CG    . MET A 1 4107 ? 189.604 204.753 228.168 1.00 12.60 ? 4107 MET A CG    1 
ATOM   19497 S  SD    . MET A 1 4107 ? 191.057 203.974 227.441 1.00 42.64 ? 4107 MET A SD    1 
ATOM   19498 C  CE    . MET A 1 4107 ? 190.343 203.200 225.995 1.00 13.27 ? 4107 MET A CE    1 
ATOM   19499 N  N     . GLN A 1 4108 ? 189.362 209.256 228.590 1.00 4.71  ? 4108 GLN A N     1 
ATOM   19500 C  CA    . GLN A 1 4108 ? 189.750 210.611 228.960 1.00 3.60  ? 4108 GLN A CA    1 
ATOM   19501 C  C     . GLN A 1 4108 ? 188.584 211.385 229.560 1.00 4.33  ? 4108 GLN A C     1 
ATOM   19502 O  O     . GLN A 1 4108 ? 188.797 212.270 230.395 1.00 4.77  ? 4108 GLN A O     1 
ATOM   19503 C  CB    . GLN A 1 4108 ? 190.315 211.337 227.741 1.00 5.29  ? 4108 GLN A CB    1 
ATOM   19504 C  CG    . GLN A 1 4108 ? 191.621 210.746 227.237 1.00 9.04  ? 4108 GLN A CG    1 
ATOM   19505 C  CD    . GLN A 1 4108 ? 192.512 210.251 228.363 1.00 18.20 ? 4108 GLN A CD    1 
ATOM   19506 O  OE1   . GLN A 1 4108 ? 193.007 211.035 229.173 1.00 14.25 ? 4108 GLN A OE1   1 
ATOM   19507 N  NE2   . GLN A 1 4108 ? 192.718 208.941 228.417 1.00 12.64 ? 4108 GLN A NE2   1 
ATOM   19508 N  N     . LEU A 1 4109 ? 187.354 211.073 229.146 1.00 9.18  ? 4109 LEU A N     1 
ATOM   19509 C  CA    . LEU A 1 4109 ? 186.188 211.721 229.737 1.00 3.87  ? 4109 LEU A CA    1 
ATOM   19510 C  C     . LEU A 1 4109 ? 185.986 211.277 231.180 1.00 2.94  ? 4109 LEU A C     1 
ATOM   19511 O  O     . LEU A 1 4109 ? 185.581 212.077 232.031 1.00 4.61  ? 4109 LEU A O     1 
ATOM   19512 C  CB    . LEU A 1 4109 ? 184.943 211.426 228.902 1.00 4.47  ? 4109 LEU A CB    1 
ATOM   19513 C  CG    . LEU A 1 4109 ? 183.639 212.013 229.450 1.00 2.68  ? 4109 LEU A CG    1 
ATOM   19514 C  CD1   . LEU A 1 4109 ? 183.621 213.516 229.249 1.00 1.60  ? 4109 LEU A CD1   1 
ATOM   19515 C  CD2   . LEU A 1 4109 ? 182.426 211.359 228.815 1.00 1.88  ? 4109 LEU A CD2   1 
ATOM   19516 N  N     . GLU A 1 4110 ? 186.258 210.003 231.472 1.00 4.53  ? 4110 GLU A N     1 
ATOM   19517 C  CA    . GLU A 1 4110 ? 186.128 209.510 232.840 1.00 4.06  ? 4110 GLU A CA    1 
ATOM   19518 C  C     . GLU A 1 4110 ? 187.096 210.225 233.774 1.00 4.77  ? 4110 GLU A C     1 
ATOM   19519 O  O     . GLU A 1 4110 ? 186.738 210.572 234.905 1.00 7.39  ? 4110 GLU A O     1 
ATOM   19520 C  CB    . GLU A 1 4110 ? 186.353 207.998 232.871 1.00 3.04  ? 4110 GLU A CB    1 
ATOM   19521 C  CG    . GLU A 1 4110 ? 185.985 207.318 234.183 1.00 5.48  ? 4110 GLU A CG    1 
ATOM   19522 C  CD    . GLU A 1 4110 ? 187.087 207.396 235.224 1.00 7.74  ? 4110 GLU A CD    1 
ATOM   19523 O  OE1   . GLU A 1 4110 ? 188.243 207.060 234.892 1.00 9.47  ? 4110 GLU A OE1   1 
ATOM   19524 O  OE2   . GLU A 1 4110 ? 186.797 207.788 236.374 1.00 4.50  ? 4110 GLU A OE2   1 
ATOM   19525 N  N     . LYS A 1 4111 ? 188.330 210.452 233.317 1.00 4.56  ? 4111 LYS A N     1 
ATOM   19526 C  CA    . LYS A 1 4111 ? 189.293 211.198 234.119 1.00 4.74  ? 4111 LYS A CA    1 
ATOM   19527 C  C     . LYS A 1 4111 ? 188.869 212.653 234.281 1.00 3.19  ? 4111 LYS A C     1 
ATOM   19528 O  O     . LYS A 1 4111 ? 189.082 213.251 235.342 1.00 5.69  ? 4111 LYS A O     1 
ATOM   19529 C  CB    . LYS A 1 4111 ? 190.682 211.097 233.491 1.00 5.72  ? 4111 LYS A CB    1 
ATOM   19530 C  CG    . LYS A 1 4111 ? 191.369 209.764 233.737 1.00 8.42  ? 4111 LYS A CG    1 
ATOM   19531 C  CD    . LYS A 1 4111 ? 192.230 209.354 232.558 1.00 11.55 ? 4111 LYS A CD    1 
ATOM   19532 C  CE    . LYS A 1 4111 ? 193.161 208.207 232.916 1.00 7.89  ? 4111 LYS A CE    1 
ATOM   19533 N  NZ    . LYS A 1 4111 ? 192.440 207.016 233.433 1.00 8.21  ? 4111 LYS A NZ    1 
ATOM   19534 N  N     . LYS A 1 4112 ? 188.274 213.241 233.241 1.00 4.07  ? 4112 LYS A N     1 
ATOM   19535 C  CA    . LYS A 1 4112 ? 187.802 214.620 233.334 1.00 3.22  ? 4112 LYS A CA    1 
ATOM   19536 C  C     . LYS A 1 4112 ? 186.669 214.756 234.343 1.00 4.66  ? 4112 LYS A C     1 
ATOM   19537 O  O     . LYS A 1 4112 ? 186.634 215.714 235.123 1.00 6.00  ? 4112 LYS A O     1 
ATOM   19538 C  CB    . LYS A 1 4112 ? 187.353 215.114 231.959 1.00 3.93  ? 4112 LYS A CB    1 
ATOM   19539 C  CG    . LYS A 1 4112 ? 186.628 216.445 231.995 1.00 5.03  ? 4112 LYS A CG    1 
ATOM   19540 C  CD    . LYS A 1 4112 ? 186.157 216.866 230.618 1.00 4.33  ? 4112 LYS A CD    1 
ATOM   19541 C  CE    . LYS A 1 4112 ? 185.483 218.225 230.675 1.00 7.29  ? 4112 LYS A CE    1 
ATOM   19542 N  NZ    . LYS A 1 4112 ? 185.099 218.724 229.328 1.00 6.97  ? 4112 LYS A NZ    1 
ATOM   19543 N  N     . LEU A 1 4113 ? 185.727 213.810 234.339 1.00 7.00  ? 4113 LEU A N     1 
ATOM   19544 C  CA    . LEU A 1 4113 ? 184.594 213.885 235.254 1.00 5.99  ? 4113 LEU A CA    1 
ATOM   19545 C  C     . LEU A 1 4113 ? 185.021 213.698 236.702 1.00 7.16  ? 4113 LEU A C     1 
ATOM   19546 O  O     . LEU A 1 4113 ? 184.401 214.270 237.607 1.00 9.03  ? 4113 LEU A O     1 
ATOM   19547 C  CB    . LEU A 1 4113 ? 183.548 212.838 234.880 1.00 4.96  ? 4113 LEU A CB    1 
ATOM   19548 C  CG    . LEU A 1 4113 ? 182.834 213.034 233.546 1.00 6.96  ? 4113 LEU A CG    1 
ATOM   19549 C  CD1   . LEU A 1 4113 ? 182.034 211.793 233.192 1.00 4.35  ? 4113 LEU A CD1   1 
ATOM   19550 C  CD2   . LEU A 1 4113 ? 181.942 214.263 233.609 1.00 7.07  ? 4113 LEU A CD2   1 
ATOM   19551 N  N     . HIS A 1 4114 ? 186.064 212.903 236.941 1.00 8.93  ? 4114 HIS A N     1 
ATOM   19552 C  CA    . HIS A 1 4114 ? 186.488 212.618 238.306 1.00 7.34  ? 4114 HIS A CA    1 
ATOM   19553 C  C     . HIS A 1 4114 ? 186.928 213.884 239.030 1.00 8.54  ? 4114 HIS A C     1 
ATOM   19554 O  O     . HIS A 1 4114 ? 186.568 214.100 240.193 1.00 8.61  ? 4114 HIS A O     1 
ATOM   19555 C  CB    . HIS A 1 4114 ? 187.617 211.588 238.293 1.00 7.09  ? 4114 HIS A CB    1 
ATOM   19556 C  CG    . HIS A 1 4114 ? 188.064 211.164 239.656 1.00 6.15  ? 4114 HIS A CG    1 
ATOM   19557 N  ND1   . HIS A 1 4114 ? 187.435 210.166 240.368 1.00 5.76  ? 4114 HIS A ND1   1 
ATOM   19558 C  CD2   . HIS A 1 4114 ? 189.075 211.606 240.440 1.00 4.85  ? 4114 HIS A CD2   1 
ATOM   19559 C  CE1   . HIS A 1 4114 ? 188.039 210.010 241.532 1.00 8.25  ? 4114 HIS A CE1   1 
ATOM   19560 N  NE2   . HIS A 1 4114 ? 189.038 210.872 241.600 1.00 7.67  ? 4114 HIS A NE2   1 
ATOM   19561 N  N     . SER A 1 4115 ? 187.700 214.734 238.358 1.00 9.60  ? 4115 SER A N     1 
ATOM   19562 C  CA    . SER A 1 4115 ? 188.207 215.965 238.957 1.00 10.14 ? 4115 SER A CA    1 
ATOM   19563 C  C     . SER A 1 4115 ? 187.311 217.137 238.562 1.00 14.74 ? 4115 SER A C     1 
ATOM   19564 O  O     . SER A 1 4115 ? 187.704 218.052 237.838 1.00 17.48 ? 4115 SER A O     1 
ATOM   19565 C  CB    . SER A 1 4115 ? 189.653 216.199 238.536 1.00 9.24  ? 4115 SER A CB    1 
ATOM   19566 O  OG    . SER A 1 4115 ? 189.764 216.252 237.125 1.00 17.12 ? 4115 SER A OG    1 
ATOM   19567 N  N     . LEU A 1 4116 ? 186.080 217.098 239.065 1.00 13.45 ? 4116 LEU A N     1 
ATOM   19568 C  CA    . LEU A 1 4116 ? 185.100 218.111 238.704 1.00 12.58 ? 4116 LEU A CA    1 
ATOM   19569 C  C     . LEU A 1 4116 ? 183.981 218.119 239.735 1.00 15.91 ? 4116 LEU A C     1 
ATOM   19570 O  O     . LEU A 1 4116 ? 183.509 217.061 240.156 1.00 21.12 ? 4116 LEU A O     1 
ATOM   19571 C  CB    . LEU A 1 4116 ? 184.549 217.845 237.300 1.00 12.87 ? 4116 LEU A CB    1 
ATOM   19572 C  CG    . LEU A 1 4116 ? 183.469 218.758 236.732 1.00 15.75 ? 4116 LEU A CG    1 
ATOM   19573 C  CD1   . LEU A 1 4116 ? 183.873 220.217 236.866 1.00 14.08 ? 4116 LEU A CD1   1 
ATOM   19574 C  CD2   . LEU A 1 4116 ? 183.261 218.397 235.279 1.00 9.78  ? 4116 LEU A CD2   1 
ATOM   19575 N  N     . GLN A 1 4117 ? 183.567 219.321 240.137 1.00 12.52 ? 4117 GLN A N     1 
ATOM   19576 C  CA    . GLN A 1 4117 ? 182.482 219.518 241.100 1.00 15.35 ? 4117 GLN A CA    1 
ATOM   19577 C  C     . GLN A 1 4117 ? 181.452 220.422 240.442 1.00 15.19 ? 4117 GLN A C     1 
ATOM   19578 O  O     . GLN A 1 4117 ? 181.440 221.640 240.663 1.00 18.21 ? 4117 GLN A O     1 
ATOM   19579 C  CB    . GLN A 1 4117 ? 182.988 220.118 242.414 1.00 17.71 ? 4117 GLN A CB    1 
ATOM   19580 C  CG    . GLN A 1 4117 ? 183.790 219.170 243.297 1.00 19.72 ? 4117 GLN A CG    1 
ATOM   19581 C  CD    . GLN A 1 4117 ? 185.146 218.819 242.714 1.00 27.43 ? 4117 GLN A CD    1 
ATOM   19582 O  OE1   . GLN A 1 4117 ? 185.440 217.654 242.452 1.00 32.12 ? 4117 GLN A OE1   1 
ATOM   19583 N  NE2   . GLN A 1 4117 ? 185.981 219.832 242.511 1.00 22.70 ? 4117 GLN A NE2   1 
ATOM   19584 N  N     . PRO A 1 4118 ? 180.570 219.861 239.630 1.00 14.65 ? 4118 PRO A N     1 
ATOM   19585 C  CA    . PRO A 1 4118 ? 179.668 220.674 238.812 1.00 10.92 ? 4118 PRO A CA    1 
ATOM   19586 C  C     . PRO A 1 4118 ? 178.513 221.243 239.629 1.00 10.22 ? 4118 PRO A C     1 
ATOM   19587 O  O     . PRO A 1 4118 ? 178.407 221.049 240.838 1.00 13.85 ? 4118 PRO A O     1 
ATOM   19588 C  CB    . PRO A 1 4118 ? 179.172 219.683 237.759 1.00 6.82  ? 4118 PRO A CB    1 
ATOM   19589 C  CG    . PRO A 1 4118 ? 179.256 218.358 238.417 1.00 11.07 ? 4118 PRO A CG    1 
ATOM   19590 C  CD    . PRO A 1 4118 ? 180.389 218.416 239.399 1.00 8.99  ? 4118 PRO A CD    1 
ATOM   19591 N  N     . HIS A 1 4119 ? 177.648 221.972 238.931 1.00 9.85  ? 4119 HIS A N     1 
ATOM   19592 C  CA    . HIS A 1 4119 ? 176.433 222.494 239.535 1.00 9.96  ? 4119 HIS A CA    1 
ATOM   19593 C  C     . HIS A 1 4119 ? 175.529 221.347 239.968 1.00 11.53 ? 4119 HIS A C     1 
ATOM   19594 O  O     . HIS A 1 4119 ? 175.528 220.273 239.361 1.00 14.56 ? 4119 HIS A O     1 
ATOM   19595 C  CB    . HIS A 1 4119 ? 175.714 223.404 238.539 1.00 9.04  ? 4119 HIS A CB    1 
ATOM   19596 C  CG    . HIS A 1 4119 ? 174.529 224.118 239.106 1.00 11.90 ? 4119 HIS A CG    1 
ATOM   19597 N  ND1   . HIS A 1 4119 ? 173.267 223.567 239.126 1.00 16.86 ? 4119 HIS A ND1   1 
ATOM   19598 C  CD2   . HIS A 1 4119 ? 174.412 225.345 239.666 1.00 14.70 ? 4119 HIS A CD2   1 
ATOM   19599 C  CE1   . HIS A 1 4119 ? 172.423 224.421 239.676 1.00 17.39 ? 4119 HIS A CE1   1 
ATOM   19600 N  NE2   . HIS A 1 4119 ? 173.093 225.508 240.012 1.00 21.91 ? 4119 HIS A NE2   1 
ATOM   19601 N  N     . ALA A 1 4120 ? 174.759 221.578 241.035 1.00 8.63  ? 4120 ALA A N     1 
ATOM   19602 C  CA    . ALA A 1 4120 ? 173.939 220.513 241.603 1.00 7.55  ? 4120 ALA A CA    1 
ATOM   19603 C  C     . ALA A 1 4120 ? 172.919 219.980 240.604 1.00 10.28 ? 4120 ALA A C     1 
ATOM   19604 O  O     . ALA A 1 4120 ? 172.517 218.814 240.692 1.00 14.81 ? 4120 ALA A O     1 
ATOM   19605 C  CB    . ALA A 1 4120 ? 173.236 221.009 242.864 1.00 10.84 ? 4120 ALA A CB    1 
ATOM   19606 N  N     . CYS A 1 4121 ? 172.492 220.807 239.654 1.00 9.22  ? 4121 CYS A N     1 
ATOM   19607 C  CA    . CYS A 1 4121 ? 171.517 220.395 238.653 1.00 6.62  ? 4121 CYS A CA    1 
ATOM   19608 C  C     . CYS A 1 4121 ? 172.148 219.817 237.394 1.00 4.55  ? 4121 CYS A C     1 
ATOM   19609 O  O     . CYS A 1 4121 ? 171.418 219.317 236.533 1.00 3.72  ? 4121 CYS A O     1 
ATOM   19610 C  CB    . CYS A 1 4121 ? 170.621 221.579 238.271 1.00 9.21  ? 4121 CYS A CB    1 
ATOM   19611 S  SG    . CYS A 1 4121 ? 169.200 221.823 239.351 1.00 38.83 ? 4121 CYS A SG    1 
ATOM   19612 N  N     . PHE A 1 4122 ? 173.472 219.867 237.260 1.00 4.81  ? 4122 PHE A N     1 
ATOM   19613 C  CA    . PHE A 1 4122 ? 174.115 219.347 236.061 1.00 3.08  ? 4122 PHE A CA    1 
ATOM   19614 C  C     . PHE A 1 4122 ? 173.950 217.837 235.970 1.00 2.55  ? 4122 PHE A C     1 
ATOM   19615 O  O     . PHE A 1 4122 ? 174.116 217.112 236.954 1.00 3.64  ? 4122 PHE A O     1 
ATOM   19616 C  CB    . PHE A 1 4122 ? 175.602 219.701 236.043 1.00 1.83  ? 4122 PHE A CB    1 
ATOM   19617 C  CG    . PHE A 1 4122 ? 176.409 218.864 235.086 1.00 1.98  ? 4122 PHE A CG    1 
ATOM   19618 C  CD1   . PHE A 1 4122 ? 176.395 219.135 233.729 1.00 1.58  ? 4122 PHE A CD1   1 
ATOM   19619 C  CD2   . PHE A 1 4122 ? 177.169 217.800 235.540 1.00 1.44  ? 4122 PHE A CD2   1 
ATOM   19620 C  CE1   . PHE A 1 4122 ? 177.125 218.368 232.847 1.00 0.84  ? 4122 PHE A CE1   1 
ATOM   19621 C  CE2   . PHE A 1 4122 ? 177.900 217.030 234.660 1.00 0.59  ? 4122 PHE A CE2   1 
ATOM   19622 C  CZ    . PHE A 1 4122 ? 177.879 217.314 233.313 1.00 0.57  ? 4122 PHE A CZ    1 
ATOM   19623 N  N     . ARG A 1 4123 ? 173.632 217.363 234.770 1.00 1.55  ? 4123 ARG A N     1 
ATOM   19624 C  CA    . ARG A 1 4123 ? 173.557 215.939 234.490 1.00 1.23  ? 4123 ARG A CA    1 
ATOM   19625 C  C     . ARG A 1 4123 ? 174.221 215.666 233.151 1.00 0.50  ? 4123 ARG A C     1 
ATOM   19626 O  O     . ARG A 1 4123 ? 174.041 216.426 232.196 1.00 0.45  ? 4123 ARG A O     1 
ATOM   19627 C  CB    . ARG A 1 4123 ? 172.106 215.441 234.474 1.00 0.97  ? 4123 ARG A CB    1 
ATOM   19628 C  CG    . ARG A 1 4123 ? 171.422 215.478 235.827 1.00 1.44  ? 4123 ARG A CG    1 
ATOM   19629 C  CD    . ARG A 1 4123 ? 172.085 214.528 236.812 1.00 2.74  ? 4123 ARG A CD    1 
ATOM   19630 N  NE    . ARG A 1 4123 ? 171.483 214.602 238.136 1.00 6.51  ? 4123 ARG A NE    1 
ATOM   19631 C  CZ    . ARG A 1 4123 ? 171.658 215.602 238.991 1.00 4.73  ? 4123 ARG A CZ    1 
ATOM   19632 N  NH1   . ARG A 1 4123 ? 172.454 216.620 238.712 1.00 3.24  ? 4123 ARG A NH1   1 
ATOM   19633 N  NH2   . ARG A 1 4123 ? 171.022 215.575 240.157 1.00 7.65  ? 4123 ARG A NH2   1 
ATOM   19634 N  N     . LEU A 1 4124 ? 174.997 214.590 233.089 1.00 0.67  ? 4124 LEU A N     1 
ATOM   19635 C  CA    . LEU A 1 4124 ? 175.624 214.140 231.852 1.00 0.38  ? 4124 LEU A CA    1 
ATOM   19636 C  C     . LEU A 1 4124 ? 175.052 212.780 231.483 1.00 0.22  ? 4124 LEU A C     1 
ATOM   19637 O  O     . LEU A 1 4124 ? 175.131 211.835 232.274 1.00 0.41  ? 4124 LEU A O     1 
ATOM   19638 C  CB    . LEU A 1 4124 ? 177.144 214.065 231.996 1.00 0.25  ? 4124 LEU A CB    1 
ATOM   19639 C  CG    . LEU A 1 4124 ? 177.870 213.467 230.790 1.00 0.37  ? 4124 LEU A CG    1 
ATOM   19640 C  CD1   . LEU A 1 4124 ? 177.754 214.386 229.583 1.00 0.24  ? 4124 LEU A CD1   1 
ATOM   19641 C  CD2   . LEU A 1 4124 ? 179.322 213.173 231.113 1.00 0.55  ? 4124 LEU A CD2   1 
ATOM   19642 N  N     . PHE A 1 4125 ? 174.479 212.684 230.288 1.00 0.18  ? 4125 PHE A N     1 
ATOM   19643 C  CA    . PHE A 1 4125 ? 173.917 211.442 229.777 1.00 0.41  ? 4125 PHE A CA    1 
ATOM   19644 C  C     . PHE A 1 4125 ? 174.810 210.909 228.668 1.00 0.15  ? 4125 PHE A C     1 
ATOM   19645 O  O     . PHE A 1 4125 ? 175.153 211.640 227.735 1.00 0.15  ? 4125 PHE A O     1 
ATOM   19646 C  CB    . PHE A 1 4125 ? 172.493 211.645 229.251 1.00 0.43  ? 4125 PHE A CB    1 
ATOM   19647 C  CG    . PHE A 1 4125 ? 171.512 212.089 230.297 1.00 0.48  ? 4125 PHE A CG    1 
ATOM   19648 C  CD1   . PHE A 1 4125 ? 171.356 213.431 230.599 1.00 0.42  ? 4125 PHE A CD1   1 
ATOM   19649 C  CD2   . PHE A 1 4125 ? 170.739 211.162 230.974 1.00 0.23  ? 4125 PHE A CD2   1 
ATOM   19650 C  CE1   . PHE A 1 4125 ? 170.452 213.838 231.559 1.00 0.47  ? 4125 PHE A CE1   1 
ATOM   19651 C  CE2   . PHE A 1 4125 ? 169.833 211.562 231.934 1.00 0.24  ? 4125 PHE A CE2   1 
ATOM   19652 C  CZ    . PHE A 1 4125 ? 169.689 212.901 232.226 1.00 0.93  ? 4125 PHE A CZ    1 
ATOM   19653 N  N     . LEU A 1 4126 ? 175.193 209.643 228.778 1.00 0.27  ? 4126 LEU A N     1 
ATOM   19654 C  CA    . LEU A 1 4126 ? 175.992 208.978 227.758 1.00 0.43  ? 4126 LEU A CA    1 
ATOM   19655 C  C     . LEU A 1 4126 ? 175.164 207.855 227.157 1.00 0.56  ? 4126 LEU A C     1 
ATOM   19656 O  O     . LEU A 1 4126 ? 174.705 206.962 227.875 1.00 0.97  ? 4126 LEU A O     1 
ATOM   19657 C  CB    . LEU A 1 4126 ? 177.301 208.442 228.339 1.00 0.43  ? 4126 LEU A CB    1 
ATOM   19658 C  CG    . LEU A 1 4126 ? 178.211 209.462 229.027 1.00 0.25  ? 4126 LEU A CG    1 
ATOM   19659 C  CD1   . LEU A 1 4126 ? 179.517 208.812 229.455 1.00 0.13  ? 4126 LEU A CD1   1 
ATOM   19660 C  CD2   . LEU A 1 4126 ? 178.469 210.648 228.118 1.00 0.12  ? 4126 LEU A CD2   1 
ATOM   19661 N  N     . THR A 1 4127 ? 174.976 207.907 225.845 1.00 1.38  ? 4127 THR A N     1 
ATOM   19662 C  CA    . THR A 1 4127 ? 174.248 206.885 225.111 1.00 0.62  ? 4127 THR A CA    1 
ATOM   19663 C  C     . THR A 1 4127 ? 175.247 205.996 224.389 1.00 0.61  ? 4127 THR A C     1 
ATOM   19664 O  O     . THR A 1 4127 ? 176.124 206.492 223.673 1.00 2.04  ? 4127 THR A O     1 
ATOM   19665 C  CB    . THR A 1 4127 ? 173.273 207.517 224.116 1.00 0.98  ? 4127 THR A CB    1 
ATOM   19666 O  OG1   . THR A 1 4127 ? 172.204 208.153 224.827 1.00 1.71  ? 4127 THR A OG1   1 
ATOM   19667 C  CG2   . THR A 1 4127 ? 172.708 206.474 223.174 1.00 5.74  ? 4127 THR A CG2   1 
ATOM   19668 N  N     . MET A 1 4128 ? 175.129 204.690 224.596 1.00 1.01  ? 4128 MET A N     1 
ATOM   19669 C  CA    . MET A 1 4128 ? 176.003 203.740 223.932 1.00 1.10  ? 4128 MET A CA    1 
ATOM   19670 C  C     . MET A 1 4128 ? 175.262 202.426 223.757 1.00 1.04  ? 4128 MET A C     1 
ATOM   19671 O  O     . MET A 1 4128 ? 174.295 202.134 224.464 1.00 1.70  ? 4128 MET A O     1 
ATOM   19672 C  CB    . MET A 1 4128 ? 177.302 203.516 224.716 1.00 1.12  ? 4128 MET A CB    1 
ATOM   19673 C  CG    . MET A 1 4128 ? 177.123 202.703 225.985 1.00 1.90  ? 4128 MET A CG    1 
ATOM   19674 S  SD    . MET A 1 4128 ? 176.193 203.597 227.241 1.00 31.07 ? 4128 MET A SD    1 
ATOM   19675 C  CE    . MET A 1 4128 ? 177.360 204.875 227.682 1.00 4.24  ? 4128 MET A CE    1 
ATOM   19676 N  N     . GLU A 1 4129 ? 175.720 201.645 222.789 1.00 1.37  ? 4129 GLU A N     1 
ATOM   19677 C  CA    . GLU A 1 4129 ? 175.284 200.268 222.677 1.00 1.70  ? 4129 GLU A CA    1 
ATOM   19678 C  C     . GLU A 1 4129 ? 176.017 199.418 223.708 1.00 2.99  ? 4129 GLU A C     1 
ATOM   19679 O  O     . GLU A 1 4129 ? 177.069 199.797 224.229 1.00 8.77  ? 4129 GLU A O     1 
ATOM   19680 C  CB    . GLU A 1 4129 ? 175.541 199.730 221.270 1.00 4.16  ? 4129 GLU A CB    1 
ATOM   19681 C  CG    . GLU A 1 4129 ? 174.758 200.434 220.183 1.00 7.20  ? 4129 GLU A CG    1 
ATOM   19682 C  CD    . GLU A 1 4129 ? 174.833 199.711 218.852 1.00 18.36 ? 4129 GLU A CD    1 
ATOM   19683 O  OE1   . GLU A 1 4129 ? 175.830 199.001 218.616 1.00 20.86 ? 4129 GLU A OE1   1 
ATOM   19684 O  OE2   . GLU A 1 4129 ? 173.894 199.855 218.041 1.00 16.50 ? 4129 GLU A OE2   1 
ATOM   19685 N  N     . ILE A 1 4130 ? 175.451 198.252 224.004 1.00 2.27  ? 4130 ILE A N     1 
ATOM   19686 C  CA    . ILE A 1 4130 ? 176.106 197.332 224.924 1.00 2.47  ? 4130 ILE A CA    1 
ATOM   19687 C  C     . ILE A 1 4130 ? 177.291 196.727 224.187 1.00 2.95  ? 4130 ILE A C     1 
ATOM   19688 O  O     . ILE A 1 4130 ? 177.139 195.795 223.391 1.00 10.47 ? 4130 ILE A O     1 
ATOM   19689 C  CB    . ILE A 1 4130 ? 175.135 196.258 225.444 1.00 3.42  ? 4130 ILE A CB    1 
ATOM   19690 C  CG1   . ILE A 1 4130 ? 173.975 196.924 226.190 1.00 1.25  ? 4130 ILE A CG1   1 
ATOM   19691 C  CG2   . ILE A 1 4130 ? 175.863 195.267 226.335 1.00 1.17  ? 4130 ILE A CG2   1 
ATOM   19692 C  CD1   . ILE A 1 4130 ? 173.029 195.956 226.855 1.00 0.56  ? 4130 ILE A CD1   1 
ATOM   19693 N  N     . ASN A 1 4131 ? 178.477 197.270 224.443 1.00 2.80  ? 4131 ASN A N     1 
ATOM   19694 C  CA    . ASN A 1 4131 ? 179.669 196.961 223.676 1.00 3.53  ? 4131 ASN A CA    1 
ATOM   19695 C  C     . ASN A 1 4131 ? 180.820 196.679 224.632 1.00 2.64  ? 4131 ASN A C     1 
ATOM   19696 O  O     . ASN A 1 4131 ? 181.045 197.454 225.577 1.00 3.15  ? 4131 ASN A O     1 
ATOM   19697 C  CB    . ASN A 1 4131 ? 180.020 198.129 222.741 1.00 3.56  ? 4131 ASN A CB    1 
ATOM   19698 C  CG    . ASN A 1 4131 ? 180.897 197.708 221.582 1.00 6.70  ? 4131 ASN A CG    1 
ATOM   19699 O  OD1   . ASN A 1 4131 ? 181.968 197.136 221.775 1.00 10.94 ? 4131 ASN A OD1   1 
ATOM   19700 N  ND2   . ASN A 1 4131 ? 180.449 197.994 220.369 1.00 10.11 ? 4131 ASN A ND2   1 
ATOM   19701 N  N     . PRO A 1 4132 ? 181.571 195.595 224.428 1.00 2.69  ? 4132 PRO A N     1 
ATOM   19702 C  CA    . PRO A 1 4132 ? 182.750 195.345 225.274 1.00 2.21  ? 4132 PRO A CA    1 
ATOM   19703 C  C     . PRO A 1 4132 ? 183.839 196.396 225.129 1.00 4.75  ? 4132 PRO A C     1 
ATOM   19704 O  O     . PRO A 1 4132 ? 184.738 196.445 225.978 1.00 7.22  ? 4132 PRO A O     1 
ATOM   19705 C  CB    . PRO A 1 4132 ? 183.235 193.965 224.805 1.00 2.41  ? 4132 PRO A CB    1 
ATOM   19706 C  CG    . PRO A 1 4132 ? 182.644 193.789 223.447 1.00 2.36  ? 4132 PRO A CG    1 
ATOM   19707 C  CD    . PRO A 1 4132 ? 181.330 194.497 223.477 1.00 2.18  ? 4132 PRO A CD    1 
ATOM   19708 N  N     . LYS A 1 4133 ? 183.796 197.223 224.084 1.00 5.64  ? 4133 LYS A N     1 
ATOM   19709 C  CA    . LYS A 1 4133 ? 184.790 198.275 223.913 1.00 4.69  ? 4133 LYS A CA    1 
ATOM   19710 C  C     . LYS A 1 4133 ? 184.651 199.389 224.943 1.00 5.70  ? 4133 LYS A C     1 
ATOM   19711 O  O     . LYS A 1 4133 ? 185.615 200.131 225.162 1.00 11.84 ? 4133 LYS A O     1 
ATOM   19712 C  CB    . LYS A 1 4133 ? 184.695 198.864 222.504 1.00 8.60  ? 4133 LYS A CB    1 
ATOM   19713 C  CG    . LYS A 1 4133 ? 185.214 197.946 221.411 1.00 8.35  ? 4133 LYS A CG    1 
ATOM   19714 C  CD    . LYS A 1 4133 ? 186.695 197.663 221.584 1.00 11.04 ? 4133 LYS A CD    1 
ATOM   19715 C  CE    . LYS A 1 4133 ? 187.517 198.937 221.496 1.00 16.94 ? 4133 LYS A CE    1 
ATOM   19716 N  NZ    . LYS A 1 4133 ? 187.325 199.625 220.190 1.00 16.56 ? 4133 LYS A NZ    1 
ATOM   19717 N  N     . VAL A 1 4134 ? 183.485 199.529 225.568 1.00 2.43  ? 4134 VAL A N     1 
ATOM   19718 C  CA    . VAL A 1 4134 ? 183.296 200.597 226.558 1.00 1.68  ? 4134 VAL A CA    1 
ATOM   19719 C  C     . VAL A 1 4134 ? 184.225 200.353 227.742 1.00 2.10  ? 4134 VAL A C     1 
ATOM   19720 O  O     . VAL A 1 4134 ? 184.257 199.230 228.283 1.00 5.20  ? 4134 VAL A O     1 
ATOM   19721 C  CB    . VAL A 1 4134 ? 181.827 200.663 227.011 1.00 2.53  ? 4134 VAL A CB    1 
ATOM   19722 C  CG1   . VAL A 1 4134 ? 181.686 201.527 228.254 1.00 0.97  ? 4134 VAL A CG1   1 
ATOM   19723 C  CG2   . VAL A 1 4134 ? 180.949 201.200 225.889 1.00 1.38  ? 4134 VAL A CG2   1 
ATOM   19724 N  N     . PRO A 1 4135 ? 185.002 201.345 228.176 1.00 2.82  ? 4135 PRO A N     1 
ATOM   19725 C  CA    . PRO A 1 4135 ? 185.970 201.113 229.254 1.00 2.82  ? 4135 PRO A CA    1 
ATOM   19726 C  C     . PRO A 1 4135 ? 185.289 200.743 230.564 1.00 2.20  ? 4135 PRO A C     1 
ATOM   19727 O  O     . PRO A 1 4135 ? 184.208 201.234 230.891 1.00 1.68  ? 4135 PRO A O     1 
ATOM   19728 C  CB    . PRO A 1 4135 ? 186.704 202.454 229.369 1.00 2.16  ? 4135 PRO A CB    1 
ATOM   19729 C  CG    . PRO A 1 4135 ? 186.376 203.195 228.115 1.00 3.20  ? 4135 PRO A CG    1 
ATOM   19730 C  CD    . PRO A 1 4135 ? 185.019 202.740 227.713 1.00 1.37  ? 4135 PRO A CD    1 
ATOM   19731 N  N     . VAL A 1 4136 ? 185.955 199.868 231.320 1.00 2.84  ? 4136 VAL A N     1 
ATOM   19732 C  CA    . VAL A 1 4136 ? 185.459 199.481 232.637 1.00 2.46  ? 4136 VAL A CA    1 
ATOM   19733 C  C     . VAL A 1 4136 ? 185.443 200.676 233.579 1.00 1.59  ? 4136 VAL A C     1 
ATOM   19734 O  O     . VAL A 1 4136 ? 184.506 200.851 234.367 1.00 1.92  ? 4136 VAL A O     1 
ATOM   19735 C  CB    . VAL A 1 4136 ? 186.306 198.325 233.203 1.00 3.88  ? 4136 VAL A CB    1 
ATOM   19736 C  CG1   . VAL A 1 4136 ? 185.871 197.987 234.618 1.00 6.22  ? 4136 VAL A CG1   1 
ATOM   19737 C  CG2   . VAL A 1 4136 ? 186.191 197.103 232.312 1.00 2.35  ? 4136 VAL A CG2   1 
ATOM   19738 N  N     . ASN A 1 4137 ? 186.474 201.520 233.511 1.00 1.99  ? 4137 ASN A N     1 
ATOM   19739 C  CA    . ASN A 1 4137 ? 186.582 202.639 234.440 1.00 2.08  ? 4137 ASN A CA    1 
ATOM   19740 C  C     . ASN A 1 4137 ? 185.418 203.609 234.280 1.00 1.76  ? 4137 ASN A C     1 
ATOM   19741 O  O     . ASN A 1 4137 ? 184.922 204.161 235.268 1.00 3.49  ? 4137 ASN A O     1 
ATOM   19742 C  CB    . ASN A 1 4137 ? 187.917 203.358 234.243 1.00 3.53  ? 4137 ASN A CB    1 
ATOM   19743 C  CG    . ASN A 1 4137 ? 188.592 203.698 235.555 1.00 11.36 ? 4137 ASN A CG    1 
ATOM   19744 O  OD1   . ASN A 1 4137 ? 188.393 203.017 236.562 1.00 10.95 ? 4137 ASN A OD1   1 
ATOM   19745 N  ND2   . ASN A 1 4137 ? 189.395 204.755 235.553 1.00 10.80 ? 4137 ASN A ND2   1 
ATOM   19746 N  N     . LEU A 1 4138 ? 184.978 203.842 233.042 1.00 2.25  ? 4138 LEU A N     1 
ATOM   19747 C  CA    . LEU A 1 4138 ? 183.797 204.669 232.826 1.00 0.85  ? 4138 LEU A CA    1 
ATOM   19748 C  C     . LEU A 1 4138 ? 182.548 204.009 233.397 1.00 0.82  ? 4138 LEU A C     1 
ATOM   19749 O  O     . LEU A 1 4138 ? 181.703 204.679 234.000 1.00 1.15  ? 4138 LEU A O     1 
ATOM   19750 C  CB    . LEU A 1 4138 ? 183.613 204.955 231.338 1.00 1.97  ? 4138 LEU A CB    1 
ATOM   19751 C  CG    . LEU A 1 4138 ? 182.340 205.744 231.022 1.00 0.60  ? 4138 LEU A CG    1 
ATOM   19752 C  CD1   . LEU A 1 4138 ? 182.568 207.234 231.209 1.00 0.38  ? 4138 LEU A CD1   1 
ATOM   19753 C  CD2   . LEU A 1 4138 ? 181.829 205.432 229.630 1.00 0.42  ? 4138 LEU A CD2   1 
ATOM   19754 N  N     . LEU A 1 4139 ? 182.417 202.693 233.218 1.00 0.74  ? 4139 LEU A N     1 
ATOM   19755 C  CA    . LEU A 1 4139 ? 181.240 201.985 233.711 1.00 0.48  ? 4139 LEU A CA    1 
ATOM   19756 C  C     . LEU A 1 4139 ? 181.133 202.076 235.229 1.00 0.97  ? 4139 LEU A C     1 
ATOM   19757 O  O     . LEU A 1 4139 ? 180.039 202.265 235.771 1.00 2.07  ? 4139 LEU A O     1 
ATOM   19758 C  CB    . LEU A 1 4139 ? 181.279 200.526 233.265 1.00 0.61  ? 4139 LEU A CB    1 
ATOM   19759 C  CG    . LEU A 1 4139 ? 181.088 200.246 231.773 1.00 1.15  ? 4139 LEU A CG    1 
ATOM   19760 C  CD1   . LEU A 1 4139 ? 181.296 198.773 231.479 1.00 0.45  ? 4139 LEU A CD1   1 
ATOM   19761 C  CD2   . LEU A 1 4139 ? 179.715 200.697 231.307 1.00 0.68  ? 4139 LEU A CD2   1 
ATOM   19762 N  N     . ARG A 1 4140 ? 182.259 201.937 235.931 1.00 0.77  ? 4140 ARG A N     1 
ATOM   19763 C  CA    . ARG A 1 4140 ? 182.239 202.035 237.386 1.00 0.99  ? 4140 ARG A CA    1 
ATOM   19764 C  C     . ARG A 1 4140 ? 181.884 203.440 237.855 1.00 0.87  ? 4140 ARG A C     1 
ATOM   19765 O  O     . ARG A 1 4140 ? 181.181 203.597 238.859 1.00 0.89  ? 4140 ARG A O     1 
ATOM   19766 C  CB    . ARG A 1 4140 ? 183.590 201.607 237.957 1.00 1.56  ? 4140 ARG A CB    1 
ATOM   19767 C  CG    . ARG A 1 4140 ? 183.974 200.179 237.617 1.00 1.77  ? 4140 ARG A CG    1 
ATOM   19768 C  CD    . ARG A 1 4140 ? 185.359 199.835 238.129 1.00 1.49  ? 4140 ARG A CD    1 
ATOM   19769 N  NE    . ARG A 1 4140 ? 185.656 200.503 239.388 1.00 5.75  ? 4140 ARG A NE    1 
ATOM   19770 C  CZ    . ARG A 1 4140 ? 185.682 199.899 240.568 1.00 4.95  ? 4140 ARG A CZ    1 
ATOM   19771 N  NH1   . ARG A 1 4140 ? 185.431 198.606 240.686 1.00 4.99  ? 4140 ARG A NH1   1 
ATOM   19772 N  NH2   . ARG A 1 4140 ? 185.959 200.612 241.655 1.00 1.87  ? 4140 ARG A NH2   1 
ATOM   19773 N  N     . ALA A 1 4141 ? 182.354 204.466 237.146 1.00 1.13  ? 4141 ALA A N     1 
ATOM   19774 C  CA    . ALA A 1 4141 ? 182.108 205.846 237.545 1.00 0.95  ? 4141 ALA A CA    1 
ATOM   19775 C  C     . ALA A 1 4141 ? 180.658 206.269 237.366 1.00 1.43  ? 4141 ALA A C     1 
ATOM   19776 O  O     . ALA A 1 4141 ? 180.178 207.120 238.122 1.00 3.03  ? 4141 ALA A O     1 
ATOM   19777 C  CB    . ALA A 1 4141 ? 183.016 206.788 236.755 1.00 1.05  ? 4141 ALA A CB    1 
ATOM   19778 N  N     . GLY A 1 4142 ? 179.952 205.705 236.388 1.00 0.59  ? 4142 GLY A N     1 
ATOM   19779 C  CA    . GLY A 1 4142 ? 178.584 206.073 236.108 1.00 0.77  ? 4142 GLY A CA    1 
ATOM   19780 C  C     . GLY A 1 4142 ? 177.596 205.048 236.643 1.00 0.59  ? 4142 GLY A C     1 
ATOM   19781 O  O     . GLY A 1 4142 ? 177.958 203.995 237.160 1.00 0.74  ? 4142 GLY A O     1 
ATOM   19782 N  N     . ARG A 1 4143 ? 176.320 205.389 236.518 1.00 0.39  ? 4143 ARG A N     1 
ATOM   19783 C  CA    . ARG A 1 4143 ? 175.241 204.471 236.851 1.00 0.40  ? 4143 ARG A CA    1 
ATOM   19784 C  C     . ARG A 1 4143 ? 174.628 203.953 235.557 1.00 0.26  ? 4143 ARG A C     1 
ATOM   19785 O  O     . ARG A 1 4143 ? 174.243 204.739 234.686 1.00 0.91  ? 4143 ARG A O     1 
ATOM   19786 C  CB    . ARG A 1 4143 ? 174.190 205.127 237.741 1.00 0.56  ? 4143 ARG A CB    1 
ATOM   19787 C  CG    . ARG A 1 4143 ? 173.109 204.153 238.169 1.00 2.52  ? 4143 ARG A CG    1 
ATOM   19788 C  CD    . ARG A 1 4143 ? 172.115 204.767 239.124 1.00 7.27  ? 4143 ARG A CD    1 
ATOM   19789 N  NE    . ARG A 1 4143 ? 171.070 203.816 239.481 1.00 8.71  ? 4143 ARG A NE    1 
ATOM   19790 C  CZ    . ARG A 1 4143 ? 170.074 204.075 240.315 1.00 7.39  ? 4143 ARG A CZ    1 
ATOM   19791 N  NH1   . ARG A 1 4143 ? 170.014 205.212 240.986 1.00 5.18  ? 4143 ARG A NH1   1 
ATOM   19792 N  NH2   . ARG A 1 4143 ? 169.112 203.173 240.478 1.00 9.84  ? 4143 ARG A NH2   1 
ATOM   19793 N  N     . ILE A 1 4144 ? 174.543 202.637 235.441 1.00 0.24  ? 4144 ILE A N     1 
ATOM   19794 C  CA    . ILE A 1 4144 ? 174.183 201.974 234.196 1.00 0.44  ? 4144 ILE A CA    1 
ATOM   19795 C  C     . ILE A 1 4144 ? 172.684 201.720 234.174 1.00 0.38  ? 4144 ILE A C     1 
ATOM   19796 O  O     . ILE A 1 4144 ? 172.107 201.252 235.163 1.00 0.30  ? 4144 ILE A O     1 
ATOM   19797 C  CB    . ILE A 1 4144 ? 174.970 200.663 234.039 1.00 0.38  ? 4144 ILE A CB    1 
ATOM   19798 C  CG1   . ILE A 1 4144 ? 176.470 200.941 234.159 1.00 0.56  ? 4144 ILE A CG1   1 
ATOM   19799 C  CG2   . ILE A 1 4144 ? 174.627 199.978 232.729 1.00 0.45  ? 4144 ILE A CG2   1 
ATOM   19800 C  CD1   . ILE A 1 4144 ? 177.301 199.725 234.468 1.00 0.97  ? 4144 ILE A CD1   1 
ATOM   19801 N  N     . PHE A 1 4145 ? 172.047 202.046 233.053 1.00 0.66  ? 4145 PHE A N     1 
ATOM   19802 C  CA    . PHE A 1 4145 ? 170.653 201.707 232.802 1.00 0.24  ? 4145 PHE A CA    1 
ATOM   19803 C  C     . PHE A 1 4145 ? 170.581 200.939 231.493 1.00 0.29  ? 4145 PHE A C     1 
ATOM   19804 O  O     . PHE A 1 4145 ? 171.014 201.443 230.451 1.00 1.56  ? 4145 PHE A O     1 
ATOM   19805 C  CB    . PHE A 1 4145 ? 169.775 202.957 232.752 1.00 0.52  ? 4145 PHE A CB    1 
ATOM   19806 C  CG    . PHE A 1 4145 ? 169.730 203.709 234.044 1.00 1.59  ? 4145 PHE A CG    1 
ATOM   19807 C  CD1   . PHE A 1 4145 ? 168.835 203.353 235.037 1.00 1.86  ? 4145 PHE A CD1   1 
ATOM   19808 C  CD2   . PHE A 1 4145 ? 170.590 204.770 234.269 1.00 1.60  ? 4145 PHE A CD2   1 
ATOM   19809 C  CE1   . PHE A 1 4145 ? 168.800 204.042 236.230 1.00 5.21  ? 4145 PHE A CE1   1 
ATOM   19810 C  CE2   . PHE A 1 4145 ? 170.557 205.462 235.458 1.00 1.13  ? 4145 PHE A CE2   1 
ATOM   19811 C  CZ    . PHE A 1 4145 ? 169.662 205.098 236.439 1.00 4.80  ? 4145 PHE A CZ    1 
ATOM   19812 N  N     . VAL A 1 4146 ? 170.049 199.727 231.547 1.00 0.25  ? 4146 VAL A N     1 
ATOM   19813 C  CA    . VAL A 1 4146 ? 169.942 198.872 230.372 1.00 0.44  ? 4146 VAL A CA    1 
ATOM   19814 C  C     . VAL A 1 4146 ? 168.578 199.084 229.732 1.00 0.31  ? 4146 VAL A C     1 
ATOM   19815 O  O     . VAL A 1 4146 ? 167.546 199.025 230.409 1.00 0.23  ? 4146 VAL A O     1 
ATOM   19816 C  CB    . VAL A 1 4146 ? 170.160 197.395 230.741 1.00 0.30  ? 4146 VAL A CB    1 
ATOM   19817 C  CG1   . VAL A 1 4146 ? 169.670 196.486 229.621 1.00 0.59  ? 4146 VAL A CG1   1 
ATOM   19818 C  CG2   . VAL A 1 4146 ? 171.621 197.135 231.032 1.00 0.14  ? 4146 VAL A CG2   1 
ATOM   19819 N  N     . PHE A 1 4147 ? 168.574 199.342 228.430 1.00 0.46  ? 4147 PHE A N     1 
ATOM   19820 C  CA    . PHE A 1 4147 ? 167.348 199.483 227.656 1.00 0.64  ? 4147 PHE A CA    1 
ATOM   19821 C  C     . PHE A 1 4147 ? 167.269 198.342 226.655 1.00 0.60  ? 4147 PHE A C     1 
ATOM   19822 O  O     . PHE A 1 4147 ? 168.180 198.151 225.846 1.00 0.94  ? 4147 PHE A O     1 
ATOM   19823 C  CB    . PHE A 1 4147 ? 167.294 200.842 226.962 1.00 0.91  ? 4147 PHE A CB    1 
ATOM   19824 C  CG    . PHE A 1 4147 ? 167.125 201.979 227.913 1.00 1.09  ? 4147 PHE A CG    1 
ATOM   19825 C  CD1   . PHE A 1 4147 ? 168.222 202.550 228.527 1.00 0.88  ? 4147 PHE A CD1   1 
ATOM   19826 C  CD2   . PHE A 1 4147 ? 165.866 202.468 228.212 1.00 1.04  ? 4147 PHE A CD2   1 
ATOM   19827 C  CE1   . PHE A 1 4147 ? 168.070 203.584 229.415 1.00 0.59  ? 4147 PHE A CE1   1 
ATOM   19828 C  CE2   . PHE A 1 4147 ? 165.708 203.511 229.098 1.00 1.89  ? 4147 PHE A CE2   1 
ATOM   19829 C  CZ    . PHE A 1 4147 ? 166.812 204.072 229.700 1.00 2.12  ? 4147 PHE A CZ    1 
ATOM   19830 N  N     . GLU A 1 4148 ? 166.180 197.591 226.722 1.00 0.94  ? 4148 GLU A N     1 
ATOM   19831 C  CA    . GLU A 1 4148 ? 166.027 196.362 225.961 1.00 1.56  ? 4148 GLU A CA    1 
ATOM   19832 C  C     . GLU A 1 4148 ? 164.543 196.158 225.721 1.00 2.66  ? 4148 GLU A C     1 
ATOM   19833 O  O     . GLU A 1 4148 ? 163.715 196.928 226.222 1.00 4.18  ? 4148 GLU A O     1 
ATOM   19834 C  CB    . GLU A 1 4148 ? 166.646 195.173 226.709 1.00 2.26  ? 4148 GLU A CB    1 
ATOM   19835 C  CG    . GLU A 1 4148 ? 165.933 194.783 227.989 1.00 2.95  ? 4148 GLU A CG    1 
ATOM   19836 C  CD    . GLU A 1 4148 ? 166.702 193.749 228.788 1.00 6.17  ? 4148 GLU A CD    1 
ATOM   19837 O  OE1   . GLU A 1 4148 ? 167.054 192.695 228.217 1.00 3.92  ? 4148 GLU A OE1   1 
ATOM   19838 O  OE2   . GLU A 1 4148 ? 166.951 193.987 229.987 1.00 9.18  ? 4148 GLU A OE2   1 
ATOM   19839 N  N     . PRO A 1 4149 ? 164.168 195.155 224.928 1.00 3.72  ? 4149 PRO A N     1 
ATOM   19840 C  CA    . PRO A 1 4149 ? 162.747 194.839 224.772 1.00 3.52  ? 4149 PRO A CA    1 
ATOM   19841 C  C     . PRO A 1 4149 ? 162.100 194.570 226.118 1.00 3.49  ? 4149 PRO A C     1 
ATOM   19842 O  O     . PRO A 1 4149 ? 162.712 193.947 226.997 1.00 5.88  ? 4149 PRO A O     1 
ATOM   19843 C  CB    . PRO A 1 4149 ? 162.763 193.575 223.902 1.00 5.03  ? 4149 PRO A CB    1 
ATOM   19844 C  CG    . PRO A 1 4149 ? 163.982 193.713 223.092 1.00 5.56  ? 4149 PRO A CG    1 
ATOM   19845 C  CD    . PRO A 1 4149 ? 164.992 194.425 223.946 1.00 3.91  ? 4149 PRO A CD    1 
ATOM   19846 N  N     . PRO A 1 4150 ? 160.873 195.044 226.324 1.00 3.04  ? 4150 PRO A N     1 
ATOM   19847 C  CA    . PRO A 1 4150 ? 160.197 194.779 227.589 1.00 3.86  ? 4150 PRO A CA    1 
ATOM   19848 C  C     . PRO A 1 4150 ? 160.014 193.293 227.797 1.00 3.95  ? 4150 PRO A C     1 
ATOM   19849 O  O     . PRO A 1 4150 ? 159.855 192.523 226.829 1.00 4.15  ? 4150 PRO A O     1 
ATOM   19850 C  CB    . PRO A 1 4150 ? 158.852 195.501 227.430 1.00 3.35  ? 4150 PRO A CB    1 
ATOM   19851 C  CG    . PRO A 1 4150 ? 159.083 196.523 226.382 1.00 2.14  ? 4150 PRO A CG    1 
ATOM   19852 C  CD    . PRO A 1 4150 ? 160.103 195.945 225.453 1.00 2.44  ? 4150 PRO A CD    1 
ATOM   19853 N  N     . PRO A 1 4151 ? 160.046 192.832 229.049 1.00 6.99  ? 4151 PRO A N     1 
ATOM   19854 C  CA    . PRO A 1 4151 ? 160.028 191.382 229.306 1.00 6.79  ? 4151 PRO A CA    1 
ATOM   19855 C  C     . PRO A 1 4151 ? 158.803 190.657 228.767 1.00 9.58  ? 4151 PRO A C     1 
ATOM   19856 O  O     . PRO A 1 4151 ? 158.907 189.468 228.442 1.00 21.82 ? 4151 PRO A O     1 
ATOM   19857 C  CB    . PRO A 1 4151 ? 160.110 191.293 230.837 1.00 5.63  ? 4151 PRO A CB    1 
ATOM   19858 C  CG    . PRO A 1 4151 ? 159.877 192.684 231.345 1.00 7.11  ? 4151 PRO A CG    1 
ATOM   19859 C  CD    . PRO A 1 4151 ? 160.302 193.613 230.270 1.00 4.78  ? 4151 PRO A CD    1 
ATOM   19860 N  N     . GLY A 1 4152 ? 157.654 191.313 228.662 1.00 4.04  ? 4152 GLY A N     1 
ATOM   19861 C  CA    . GLY A 1 4152 ? 156.478 190.626 228.178 1.00 1.65  ? 4152 GLY A CA    1 
ATOM   19862 C  C     . GLY A 1 4152 ? 155.430 191.575 227.642 1.00 1.30  ? 4152 GLY A C     1 
ATOM   19863 O  O     . GLY A 1 4152 ? 155.651 192.782 227.534 1.00 3.79  ? 4152 GLY A O     1 
ATOM   19864 N  N     . VAL A 1 4153 ? 154.272 190.998 227.306 1.00 1.11  ? 4153 VAL A N     1 
ATOM   19865 C  CA    . VAL A 1 4153 ? 153.184 191.769 226.708 1.00 0.70  ? 4153 VAL A CA    1 
ATOM   19866 C  C     . VAL A 1 4153 ? 152.686 192.836 227.672 1.00 0.53  ? 4153 VAL A C     1 
ATOM   19867 O  O     . VAL A 1 4153 ? 152.463 193.988 227.283 1.00 0.73  ? 4153 VAL A O     1 
ATOM   19868 C  CB    . VAL A 1 4153 ? 152.044 190.828 226.268 1.00 0.77  ? 4153 VAL A CB    1 
ATOM   19869 C  CG1   . VAL A 1 4153 ? 150.798 191.625 225.909 1.00 0.52  ? 4153 VAL A CG1   1 
ATOM   19870 C  CG2   . VAL A 1 4153 ? 152.489 189.971 225.100 1.00 0.37  ? 4153 VAL A CG2   1 
ATOM   19871 N  N     . LYS A 1 4154 ? 152.496 192.471 228.941 1.00 1.29  ? 4154 LYS A N     1 
ATOM   19872 C  CA    . LYS A 1 4154 ? 152.049 193.439 229.937 1.00 1.21  ? 4154 LYS A CA    1 
ATOM   19873 C  C     . LYS A 1 4154 ? 153.050 194.577 230.085 1.00 0.79  ? 4154 LYS A C     1 
ATOM   19874 O  O     . LYS A 1 4154 ? 152.675 195.755 230.083 1.00 1.10  ? 4154 LYS A O     1 
ATOM   19875 C  CB    . LYS A 1 4154 ? 151.828 192.739 231.277 1.00 1.93  ? 4154 LYS A CB    1 
ATOM   19876 C  CG    . LYS A 1 4154 ? 151.393 193.657 232.399 1.00 2.33  ? 4154 LYS A CG    1 
ATOM   19877 C  CD    . LYS A 1 4154 ? 151.158 192.875 233.675 1.00 4.80  ? 4154 LYS A CD    1 
ATOM   19878 C  CE    . LYS A 1 4154 ? 150.547 193.745 234.755 1.00 6.93  ? 4154 LYS A CE    1 
ATOM   19879 N  NZ    . LYS A 1 4154 ? 150.179 192.945 235.949 1.00 12.41 ? 4154 LYS A NZ    1 
ATOM   19880 N  N     . ALA A 1 4155 ? 154.336 194.243 230.199 1.00 1.07  ? 4155 ALA A N     1 
ATOM   19881 C  CA    . ALA A 1 4155 ? 155.355 195.273 230.358 1.00 1.43  ? 4155 ALA A CA    1 
ATOM   19882 C  C     . ALA A 1 4155 ? 155.504 196.108 229.092 1.00 2.70  ? 4155 ALA A C     1 
ATOM   19883 O  O     . ALA A 1 4155 ? 155.759 197.315 229.167 1.00 5.24  ? 4155 ALA A O     1 
ATOM   19884 C  CB    . ALA A 1 4155 ? 156.688 194.634 230.743 1.00 2.80  ? 4155 ALA A CB    1 
ATOM   19885 N  N     . ASN A 1 4156 ? 155.349 195.482 227.923 1.00 1.42  ? 4156 ASN A N     1 
ATOM   19886 C  CA    . ASN A 1 4156 ? 155.437 196.218 226.667 1.00 0.71  ? 4156 ASN A CA    1 
ATOM   19887 C  C     . ASN A 1 4156 ? 154.342 197.269 226.564 1.00 0.79  ? 4156 ASN A C     1 
ATOM   19888 O  O     . ASN A 1 4156 ? 154.599 198.409 226.158 1.00 1.38  ? 4156 ASN A O     1 
ATOM   19889 C  CB    . ASN A 1 4156 ? 155.361 195.245 225.488 1.00 0.94  ? 4156 ASN A CB    1 
ATOM   19890 C  CG    . ASN A 1 4156 ? 155.825 195.861 224.183 1.00 0.63  ? 4156 ASN A CG    1 
ATOM   19891 O  OD1   . ASN A 1 4156 ? 155.284 196.864 223.725 1.00 0.60  ? 4156 ASN A OD1   1 
ATOM   19892 N  ND2   . ASN A 1 4156 ? 156.827 195.248 223.570 1.00 1.26  ? 4156 ASN A ND2   1 
ATOM   19893 N  N     . MET A 1 4157 ? 153.116 196.909 226.935 1.00 0.52  ? 4157 MET A N     1 
ATOM   19894 C  CA    . MET A 1 4157 ? 151.994 197.825 226.781 1.00 0.50  ? 4157 MET A CA    1 
ATOM   19895 C  C     . MET A 1 4157 ? 152.012 198.929 227.828 1.00 1.87  ? 4157 MET A C     1 
ATOM   19896 O  O     . MET A 1 4157 ? 151.589 200.054 227.541 1.00 2.59  ? 4157 MET A O     1 
ATOM   19897 C  CB    . MET A 1 4157 ? 150.683 197.044 226.839 1.00 0.42  ? 4157 MET A CB    1 
ATOM   19898 C  CG    . MET A 1 4157 ? 150.162 196.657 225.466 1.00 0.38  ? 4157 MET A CG    1 
ATOM   19899 S  SD    . MET A 1 4157 ? 148.784 195.507 225.515 1.00 1.69  ? 4157 MET A SD    1 
ATOM   19900 C  CE    . MET A 1 4157 ? 147.423 196.651 225.392 1.00 0.79  ? 4157 MET A CE    1 
ATOM   19901 N  N     . LEU A 1 4158 ? 152.495 198.634 229.036 1.00 3.40  ? 4158 LEU A N     1 
ATOM   19902 C  CA    . LEU A 1 4158 ? 152.627 199.673 230.051 1.00 2.17  ? 4158 LEU A CA    1 
ATOM   19903 C  C     . LEU A 1 4158 ? 153.684 200.696 229.656 1.00 3.82  ? 4158 LEU A C     1 
ATOM   19904 O  O     . LEU A 1 4158 ? 153.530 201.893 229.926 1.00 6.28  ? 4158 LEU A O     1 
ATOM   19905 C  CB    . LEU A 1 4158 ? 152.956 199.046 231.404 1.00 3.44  ? 4158 LEU A CB    1 
ATOM   19906 C  CG    . LEU A 1 4158 ? 151.786 198.351 232.101 1.00 1.88  ? 4158 LEU A CG    1 
ATOM   19907 C  CD1   . LEU A 1 4158 ? 152.255 197.587 233.325 1.00 2.61  ? 4158 LEU A CD1   1 
ATOM   19908 C  CD2   . LEU A 1 4158 ? 150.709 199.356 232.470 1.00 3.52  ? 4158 LEU A CD2   1 
ATOM   19909 N  N     . ARG A 1 4159 ? 154.768 200.242 229.023 1.00 2.25  ? 4159 ARG A N     1 
ATOM   19910 C  CA    . ARG A 1 4159 ? 155.782 201.167 228.533 1.00 2.39  ? 4159 ARG A CA    1 
ATOM   19911 C  C     . ARG A 1 4159 ? 155.222 202.059 227.433 1.00 3.60  ? 4159 ARG A C     1 
ATOM   19912 O  O     . ARG A 1 4159 ? 155.550 203.249 227.358 1.00 9.02  ? 4159 ARG A O     1 
ATOM   19913 C  CB    . ARG A 1 4159 ? 157.001 200.394 228.029 1.00 4.62  ? 4159 ARG A CB    1 
ATOM   19914 C  CG    . ARG A 1 4159 ? 158.140 201.280 227.560 1.00 8.01  ? 4159 ARG A CG    1 
ATOM   19915 C  CD    . ARG A 1 4159 ? 159.353 200.469 227.140 1.00 11.92 ? 4159 ARG A CD    1 
ATOM   19916 N  NE    . ARG A 1 4159 ? 159.978 199.795 228.274 1.00 16.13 ? 4159 ARG A NE    1 
ATOM   19917 C  CZ    . ARG A 1 4159 ? 160.948 198.898 228.171 1.00 11.36 ? 4159 ARG A CZ    1 
ATOM   19918 N  NH1   . ARG A 1 4159 ? 161.494 198.601 227.003 1.00 7.22  ? 4159 ARG A NH1   1 
ATOM   19919 N  NH2   . ARG A 1 4159 ? 161.389 198.291 229.269 1.00 6.22  ? 4159 ARG A NH2   1 
ATOM   19920 N  N     . THR A 1 4160 ? 154.379 201.497 226.565 1.00 4.01  ? 4160 THR A N     1 
ATOM   19921 C  CA    . THR A 1 4160 ? 153.792 202.279 225.481 1.00 3.61  ? 4160 THR A CA    1 
ATOM   19922 C  C     . THR A 1 4160 ? 152.870 203.368 226.014 1.00 5.18  ? 4160 THR A C     1 
ATOM   19923 O  O     . THR A 1 4160 ? 152.921 204.515 225.554 1.00 5.19  ? 4160 THR A O     1 
ATOM   19924 C  CB    . THR A 1 4160 ? 153.036 201.357 224.524 1.00 1.72  ? 4160 THR A CB    1 
ATOM   19925 O  OG1   . THR A 1 4160 ? 153.969 200.527 223.824 1.00 2.25  ? 4160 THR A OG1   1 
ATOM   19926 C  CG2   . THR A 1 4160 ? 152.228 202.163 223.521 1.00 1.04  ? 4160 THR A CG2   1 
ATOM   19927 N  N     . PHE A 1 4161 ? 152.021 203.032 226.986 1.00 7.05  ? 4161 PHE A N     1 
ATOM   19928 C  CA    . PHE A 1 4161 ? 151.056 204.008 227.478 1.00 6.69  ? 4161 PHE A CA    1 
ATOM   19929 C  C     . PHE A 1 4161 ? 151.724 205.098 228.305 1.00 8.30  ? 4161 PHE A C     1 
ATOM   19930 O  O     . PHE A 1 4161 ? 151.190 206.208 228.408 1.00 14.48 ? 4161 PHE A O     1 
ATOM   19931 C  CB    . PHE A 1 4161 ? 149.963 203.309 228.283 1.00 3.55  ? 4161 PHE A CB    1 
ATOM   19932 C  CG    . PHE A 1 4161 ? 148.819 202.825 227.444 1.00 2.28  ? 4161 PHE A CG    1 
ATOM   19933 C  CD1   . PHE A 1 4161 ? 147.846 203.707 227.008 1.00 4.68  ? 4161 PHE A CD1   1 
ATOM   19934 C  CD2   . PHE A 1 4161 ? 148.722 201.494 227.082 1.00 2.37  ? 4161 PHE A CD2   1 
ATOM   19935 C  CE1   . PHE A 1 4161 ? 146.791 203.266 226.230 1.00 6.97  ? 4161 PHE A CE1   1 
ATOM   19936 C  CE2   . PHE A 1 4161 ? 147.673 201.048 226.307 1.00 2.38  ? 4161 PHE A CE2   1 
ATOM   19937 C  CZ    . PHE A 1 4161 ? 146.706 201.935 225.879 1.00 4.96  ? 4161 PHE A CZ    1 
ATOM   19938 N  N     . SER A 1 4162 ? 152.881 204.808 228.900 1.00 6.57  ? 4162 SER A N     1 
ATOM   19939 C  CA    . SER A 1 4162 ? 153.622 205.843 229.608 1.00 6.58  ? 4162 SER A CA    1 
ATOM   19940 C  C     . SER A 1 4162 ? 154.361 206.772 228.653 1.00 11.57 ? 4162 SER A C     1 
ATOM   19941 O  O     . SER A 1 4162 ? 154.511 207.963 228.948 1.00 19.32 ? 4162 SER A O     1 
ATOM   19942 C  CB    . SER A 1 4162 ? 154.606 205.209 230.592 1.00 6.98  ? 4162 SER A CB    1 
ATOM   19943 O  OG    . SER A 1 4162 ? 155.617 204.487 229.913 1.00 13.26 ? 4162 SER A OG    1 
ATOM   19944 N  N     . SER A 1 4163 ? 154.820 206.254 227.513 1.00 9.59  ? 4163 SER A N     1 
ATOM   19945 C  CA    . SER A 1 4163 ? 155.593 207.066 226.580 1.00 7.22  ? 4163 SER A CA    1 
ATOM   19946 C  C     . SER A 1 4163 ? 154.725 208.049 225.803 1.00 9.06  ? 4163 SER A C     1 
ATOM   19947 O  O     . SER A 1 4163 ? 155.217 209.105 225.391 1.00 18.45 ? 4163 SER A O     1 
ATOM   19948 C  CB    . SER A 1 4163 ? 156.364 206.167 225.613 1.00 5.33  ? 4163 SER A CB    1 
ATOM   19949 O  OG    . SER A 1 4163 ? 155.488 205.348 224.860 1.00 13.82 ? 4163 SER A OG    1 
ATOM   19950 N  N     . ILE A 1 4164 ? 153.454 207.731 225.587 1.00 7.46  ? 4164 ILE A N     1 
ATOM   19951 C  CA    . ILE A 1 4164 ? 152.554 208.581 224.814 1.00 8.69  ? 4164 ILE A CA    1 
ATOM   19952 C  C     . ILE A 1 4164 ? 151.834 209.511 225.785 1.00 14.37 ? 4164 ILE A C     1 
ATOM   19953 O  O     . ILE A 1 4164 ? 151.221 209.023 226.749 1.00 18.38 ? 4164 ILE A O     1 
ATOM   19954 C  CB    . ILE A 1 4164 ? 151.551 207.755 224.001 1.00 11.50 ? 4164 ILE A CB    1 
ATOM   19955 C  CG1   . ILE A 1 4164 ? 152.280 206.718 223.149 1.00 6.71  ? 4164 ILE A CG1   1 
ATOM   19956 C  CG2   . ILE A 1 4164 ? 150.752 208.659 223.092 1.00 12.74 ? 4164 ILE A CG2   1 
ATOM   19957 C  CD1   . ILE A 1 4164 ? 151.358 205.733 222.480 1.00 5.15  ? 4164 ILE A CD1   1 
ATOM   19958 N  N     . PRO A 1 4165 ? 151.889 210.828 225.586 1.00 15.61 ? 4165 PRO A N     1 
ATOM   19959 C  CA    . PRO A 1 4165 ? 151.202 211.750 226.499 1.00 9.56  ? 4165 PRO A CA    1 
ATOM   19960 C  C     . PRO A 1 4165 ? 149.703 211.498 226.544 1.00 11.32 ? 4165 PRO A C     1 
ATOM   19961 O  O     . PRO A 1 4165 ? 149.087 211.102 225.556 1.00 14.55 ? 4165 PRO A O     1 
ATOM   19962 C  CB    . PRO A 1 4165 ? 151.512 213.127 225.905 1.00 10.84 ? 4165 PRO A CB    1 
ATOM   19963 C  CG    . PRO A 1 4165 ? 152.796 212.933 225.175 1.00 12.27 ? 4165 PRO A CG    1 
ATOM   19964 C  CD    . PRO A 1 4165 ? 152.736 211.541 224.615 1.00 12.14 ? 4165 PRO A CD    1 
ATOM   19965 N  N     . VAL A 1 4166 ? 149.115 211.746 227.718 1.00 12.49 ? 4166 VAL A N     1 
ATOM   19966 C  CA    . VAL A 1 4166 ? 147.696 211.467 227.925 1.00 14.41 ? 4166 VAL A CA    1 
ATOM   19967 C  C     . VAL A 1 4166 ? 146.834 212.322 227.004 1.00 17.98 ? 4166 VAL A C     1 
ATOM   19968 O  O     . VAL A 1 4166 ? 145.850 211.842 226.429 1.00 18.39 ? 4166 VAL A O     1 
ATOM   19969 C  CB    . VAL A 1 4166 ? 147.324 211.671 229.405 1.00 12.81 ? 4166 VAL A CB    1 
ATOM   19970 C  CG1   . VAL A 1 4166 ? 145.832 211.488 229.610 1.00 12.10 ? 4166 VAL A CG1   1 
ATOM   19971 C  CG2   . VAL A 1 4166 ? 148.101 210.707 230.279 1.00 10.32 ? 4166 VAL A CG2   1 
ATOM   19972 N  N     . SER A 1 4167 ? 147.183 213.603 226.855 1.00 13.41 ? 4167 SER A N     1 
ATOM   19973 C  CA    . SER A 1 4167 ? 146.408 214.486 225.987 1.00 10.84 ? 4167 SER A CA    1 
ATOM   19974 C  C     . SER A 1 4167 ? 146.406 214.000 224.545 1.00 16.76 ? 4167 SER A C     1 
ATOM   19975 O  O     . SER A 1 4167 ? 145.469 214.291 223.791 1.00 18.13 ? 4167 SER A O     1 
ATOM   19976 C  CB    . SER A 1 4167 ? 146.960 215.909 226.064 1.00 13.57 ? 4167 SER A CB    1 
ATOM   19977 O  OG    . SER A 1 4167 ? 148.363 215.917 225.880 1.00 23.95 ? 4167 SER A OG    1 
ATOM   19978 N  N     . ARG A 1 4168 ? 147.446 213.267 224.142 1.00 17.16 ? 4168 ARG A N     1 
ATOM   19979 C  CA    . ARG A 1 4168 ? 147.485 212.681 222.807 1.00 12.84 ? 4168 ARG A CA    1 
ATOM   19980 C  C     . ARG A 1 4168 ? 146.334 211.700 222.603 1.00 12.86 ? 4168 ARG A C     1 
ATOM   19981 O  O     . ARG A 1 4168 ? 145.638 211.756 221.582 1.00 17.41 ? 4168 ARG A O     1 
ATOM   19982 C  CB    . ARG A 1 4168 ? 148.830 211.984 222.602 1.00 11.70 ? 4168 ARG A CB    1 
ATOM   19983 C  CG    . ARG A 1 4168 ? 149.057 211.322 221.257 1.00 10.31 ? 4168 ARG A CG    1 
ATOM   19984 C  CD    . ARG A 1 4168 ? 149.196 212.325 220.138 1.00 10.08 ? 4168 ARG A CD    1 
ATOM   19985 N  NE    . ARG A 1 4168 ? 149.423 211.658 218.861 1.00 17.82 ? 4168 ARG A NE    1 
ATOM   19986 C  CZ    . ARG A 1 4168 ? 150.619 211.337 218.384 1.00 9.18  ? 4168 ARG A CZ    1 
ATOM   19987 N  NH1   . ARG A 1 4168 ? 151.724 211.580 219.069 1.00 6.48  ? 4168 ARG A NH1   1 
ATOM   19988 N  NH2   . ARG A 1 4168 ? 150.705 210.756 217.192 1.00 3.39  ? 4168 ARG A NH2   1 
ATOM   19989 N  N     . ILE A 1 4169 ? 146.113 210.803 223.567 1.00 11.72 ? 4169 ILE A N     1 
ATOM   19990 C  CA    . ILE A 1 4169 ? 145.056 209.802 223.436 1.00 12.11 ? 4169 ILE A CA    1 
ATOM   19991 C  C     . ILE A 1 4169 ? 143.680 210.434 223.612 1.00 12.52 ? 4169 ILE A C     1 
ATOM   19992 O  O     . ILE A 1 4169 ? 142.716 210.050 222.942 1.00 16.47 ? 4169 ILE A O     1 
ATOM   19993 C  CB    . ILE A 1 4169 ? 145.269 208.641 224.429 1.00 12.30 ? 4169 ILE A CB    1 
ATOM   19994 C  CG1   . ILE A 1 4169 ? 146.570 207.884 224.155 1.00 10.09 ? 4169 ILE A CG1   1 
ATOM   19995 C  CG2   . ILE A 1 4169 ? 144.106 207.678 224.402 1.00 13.42 ? 4169 ILE A CG2   1 
ATOM   19996 C  CD1   . ILE A 1 4169 ? 147.761 208.427 224.864 1.00 13.68 ? 4169 ILE A CD1   1 
ATOM   19997 N  N     . CYS A 1 4170 ? 143.568 211.421 224.502 1.00 17.55 ? 4170 CYS A N     1 
ATOM   19998 C  CA    . CYS A 1 4170 ? 142.276 211.919 224.958 1.00 15.20 ? 4170 CYS A CA    1 
ATOM   19999 C  C     . CYS A 1 4170 ? 141.743 213.068 224.108 1.00 19.12 ? 4170 CYS A C     1 
ATOM   20000 O  O     . CYS A 1 4170 ? 141.021 213.930 224.628 1.00 23.74 ? 4170 CYS A O     1 
ATOM   20001 C  CB    . CYS A 1 4170 ? 142.373 212.344 226.423 1.00 14.43 ? 4170 CYS A CB    1 
ATOM   20002 S  SG    . CYS A 1 4170 ? 142.854 211.017 227.551 1.00 43.43 ? 4170 CYS A SG    1 
ATOM   20003 N  N     . LYS A 1 4171 ? 142.073 213.109 222.819 1.00 20.80 ? 4171 LYS A N     1 
ATOM   20004 C  CA    . LYS A 1 4171 ? 141.559 214.159 221.952 1.00 15.75 ? 4171 LYS A CA    1 
ATOM   20005 C  C     . LYS A 1 4171 ? 140.065 213.949 221.692 1.00 21.93 ? 4171 LYS A C     1 
ATOM   20006 O  O     . LYS A 1 4171 ? 139.444 213.003 222.185 1.00 27.51 ? 4171 LYS A O     1 
ATOM   20007 C  CB    . LYS A 1 4171 ? 142.356 214.215 220.652 1.00 14.10 ? 4171 LYS A CB    1 
ATOM   20008 C  CG    . LYS A 1 4171 ? 143.374 215.346 220.618 1.00 7.12  ? 4171 LYS A CG    1 
ATOM   20009 C  CD    . LYS A 1 4171 ? 144.386 215.182 219.496 1.00 13.35 ? 4171 LYS A CD    1 
ATOM   20010 C  CE    . LYS A 1 4171 ? 143.718 215.092 218.135 1.00 15.37 ? 4171 LYS A CE    1 
ATOM   20011 N  NZ    . LYS A 1 4171 ? 143.020 216.349 217.756 1.00 10.97 ? 4171 LYS A NZ    1 
ATOM   20012 N  N     . SER A 1 4172 ? 139.485 214.855 220.900 1.00 21.01 ? 4172 SER A N     1 
ATOM   20013 C  CA    . SER A 1 4172 ? 138.039 214.995 220.736 1.00 17.70 ? 4172 SER A CA    1 
ATOM   20014 C  C     . SER A 1 4172 ? 137.335 213.697 220.339 1.00 23.45 ? 4172 SER A C     1 
ATOM   20015 O  O     . SER A 1 4172 ? 136.300 213.371 220.933 1.00 27.17 ? 4172 SER A O     1 
ATOM   20016 C  CB    . SER A 1 4172 ? 137.728 216.096 219.718 1.00 23.70 ? 4172 SER A CB    1 
ATOM   20017 O  OG    . SER A 1 4172 ? 138.295 217.334 220.112 1.00 31.43 ? 4172 SER A OG    1 
ATOM   20018 N  N     . PRO A 1 4173 ? 137.825 212.932 219.360 1.00 22.33 ? 4173 PRO A N     1 
ATOM   20019 C  CA    . PRO A 1 4173 ? 137.178 211.643 219.067 1.00 14.49 ? 4173 PRO A CA    1 
ATOM   20020 C  C     . PRO A 1 4173 ? 137.411 210.652 220.196 1.00 20.17 ? 4173 PRO A C     1 
ATOM   20021 O  O     . PRO A 1 4173 ? 138.548 210.281 220.494 1.00 21.90 ? 4173 PRO A O     1 
ATOM   20022 C  CB    . PRO A 1 4173 ? 137.849 211.194 217.763 1.00 10.31 ? 4173 PRO A CB    1 
ATOM   20023 C  CG    . PRO A 1 4173 ? 138.461 212.416 217.196 1.00 15.85 ? 4173 PRO A CG    1 
ATOM   20024 C  CD    . PRO A 1 4173 ? 138.874 213.233 218.370 1.00 17.09 ? 4173 PRO A CD    1 
ATOM   20025 N  N     . ASN A 1 4174 ? 136.315 210.224 220.829 1.00 17.75 ? 4174 ASN A N     1 
ATOM   20026 C  CA    . ASN A 1 4174 ? 136.416 209.293 221.946 1.00 17.66 ? 4174 ASN A CA    1 
ATOM   20027 C  C     . ASN A 1 4174 ? 136.939 207.931 221.518 1.00 15.38 ? 4174 ASN A C     1 
ATOM   20028 O  O     . ASN A 1 4174 ? 137.514 207.212 222.341 1.00 17.04 ? 4174 ASN A O     1 
ATOM   20029 C  CB    . ASN A 1 4174 ? 135.054 209.133 222.621 1.00 19.74 ? 4174 ASN A CB    1 
ATOM   20030 C  CG    . ASN A 1 4174 ? 134.638 210.368 223.388 1.00 19.81 ? 4174 ASN A CG    1 
ATOM   20031 O  OD1   . ASN A 1 4174 ? 135.392 211.335 223.483 1.00 22.37 ? 4174 ASN A OD1   1 
ATOM   20032 N  ND2   . ASN A 1 4174 ? 133.430 210.345 223.936 1.00 19.87 ? 4174 ASN A ND2   1 
ATOM   20033 N  N     . GLU A 1 4175 ? 136.756 207.566 220.251 1.00 13.13 ? 4175 GLU A N     1 
ATOM   20034 C  CA    . GLU A 1 4175 ? 137.225 206.290 219.733 1.00 11.67 ? 4175 GLU A CA    1 
ATOM   20035 C  C     . GLU A 1 4175 ? 138.735 206.251 219.545 1.00 10.94 ? 4175 GLU A C     1 
ATOM   20036 O  O     . GLU A 1 4175 ? 139.279 205.182 219.255 1.00 15.29 ? 4175 GLU A O     1 
ATOM   20037 C  CB    . GLU A 1 4175 ? 136.525 205.980 218.406 1.00 10.39 ? 4175 GLU A CB    1 
ATOM   20038 C  CG    . GLU A 1 4175 ? 135.036 205.665 218.535 1.00 12.07 ? 4175 GLU A CG    1 
ATOM   20039 C  CD    . GLU A 1 4175 ? 134.184 206.882 218.867 1.00 17.52 ? 4175 GLU A CD    1 
ATOM   20040 O  OE1   . GLU A 1 4175 ? 134.724 208.008 218.907 1.00 21.37 ? 4175 GLU A OE1   1 
ATOM   20041 O  OE2   . GLU A 1 4175 ? 132.970 206.710 219.095 1.00 18.95 ? 4175 GLU A OE2   1 
ATOM   20042 N  N     . ARG A 1 4176 ? 139.415 207.388 219.706 1.00 8.42  ? 4176 ARG A N     1 
ATOM   20043 C  CA    . ARG A 1 4176 ? 140.867 207.421 219.555 1.00 8.34  ? 4176 ARG A CA    1 
ATOM   20044 C  C     . ARG A 1 4176 ? 141.550 206.571 220.618 1.00 8.16  ? 4176 ARG A C     1 
ATOM   20045 O  O     . ARG A 1 4176 ? 142.599 205.970 220.361 1.00 9.18  ? 4176 ARG A O     1 
ATOM   20046 C  CB    . ARG A 1 4176 ? 141.358 208.868 219.619 1.00 8.75  ? 4176 ARG A CB    1 
ATOM   20047 C  CG    . ARG A 1 4176 ? 142.852 209.041 219.419 1.00 7.95  ? 4176 ARG A CG    1 
ATOM   20048 C  CD    . ARG A 1 4176 ? 143.247 210.506 219.476 1.00 9.34  ? 4176 ARG A CD    1 
ATOM   20049 N  NE    . ARG A 1 4176 ? 142.336 211.349 218.711 1.00 13.24 ? 4176 ARG A NE    1 
ATOM   20050 C  CZ    . ARG A 1 4176 ? 142.643 211.937 217.565 1.00 13.28 ? 4176 ARG A CZ    1 
ATOM   20051 N  NH1   . ARG A 1 4176 ? 143.835 211.792 217.011 1.00 11.78 ? 4176 ARG A NH1   1 
ATOM   20052 N  NH2   . ARG A 1 4176 ? 141.734 212.692 216.956 1.00 11.84 ? 4176 ARG A NH2   1 
ATOM   20053 N  N     . ALA A 1 4177 ? 140.969 206.508 221.819 1.00 12.25 ? 4177 ALA A N     1 
ATOM   20054 C  CA    . ALA A 1 4177 ? 141.582 205.747 222.903 1.00 7.85  ? 4177 ALA A CA    1 
ATOM   20055 C  C     . ALA A 1 4177 ? 141.646 204.261 222.579 1.00 3.47  ? 4177 ALA A C     1 
ATOM   20056 O  O     . ALA A 1 4177 ? 142.655 203.601 222.852 1.00 3.42  ? 4177 ALA A O     1 
ATOM   20057 C  CB    . ALA A 1 4177 ? 140.819 205.981 224.205 1.00 9.64  ? 4177 ALA A CB    1 
ATOM   20058 N  N     . ARG A 1 4178 ? 140.577 203.713 222.002 1.00 2.53  ? 4178 ARG A N     1 
ATOM   20059 C  CA    . ARG A 1 4178 ? 140.566 202.294 221.668 1.00 3.77  ? 4178 ARG A CA    1 
ATOM   20060 C  C     . ARG A 1 4178 ? 141.529 201.978 220.531 1.00 4.46  ? 4178 ARG A C     1 
ATOM   20061 O  O     . ARG A 1 4178 ? 142.121 200.893 220.508 1.00 3.53  ? 4178 ARG A O     1 
ATOM   20062 C  CB    . ARG A 1 4178 ? 139.146 201.857 221.314 1.00 5.75  ? 4178 ARG A CB    1 
ATOM   20063 C  CG    . ARG A 1 4178 ? 138.944 200.358 221.251 1.00 3.53  ? 4178 ARG A CG    1 
ATOM   20064 C  CD    . ARG A 1 4178 ? 137.468 200.018 221.248 1.00 8.92  ? 4178 ARG A CD    1 
ATOM   20065 N  NE    . ARG A 1 4178 ? 137.194 198.749 221.911 1.00 14.24 ? 4178 ARG A NE    1 
ATOM   20066 C  CZ    . ARG A 1 4178 ? 136.561 198.631 223.070 1.00 16.17 ? 4178 ARG A CZ    1 
ATOM   20067 N  NH1   . ARG A 1 4178 ? 136.132 199.691 223.733 1.00 12.41 ? 4178 ARG A NH1   1 
ATOM   20068 N  NH2   . ARG A 1 4178 ? 136.360 197.419 223.576 1.00 20.56 ? 4178 ARG A NH2   1 
ATOM   20069 N  N     . LEU A 1 4179 ? 141.696 202.904 219.583 1.00 3.56  ? 4179 LEU A N     1 
ATOM   20070 C  CA    . LEU A 1 4179 ? 142.674 202.706 218.518 1.00 2.63  ? 4179 LEU A CA    1 
ATOM   20071 C  C     . LEU A 1 4179 ? 144.087 202.627 219.078 1.00 2.08  ? 4179 LEU A C     1 
ATOM   20072 O  O     . LEU A 1 4179 ? 144.884 201.781 218.656 1.00 1.99  ? 4179 LEU A O     1 
ATOM   20073 C  CB    . LEU A 1 4179 ? 142.573 203.833 217.492 1.00 5.62  ? 4179 LEU A CB    1 
ATOM   20074 C  CG    . LEU A 1 4179 ? 141.247 203.987 216.747 1.00 4.07  ? 4179 LEU A CG    1 
ATOM   20075 C  CD1   . LEU A 1 4179 ? 141.331 205.135 215.764 1.00 4.79  ? 4179 LEU A CD1   1 
ATOM   20076 C  CD2   . LEU A 1 4179 ? 140.888 202.703 216.035 1.00 3.56  ? 4179 LEU A CD2   1 
ATOM   20077 N  N     . TYR A 1 4180 ? 144.417 203.502 220.028 1.00 3.73  ? 4180 TYR A N     1 
ATOM   20078 C  CA    . TYR A 1 4180 ? 145.739 203.463 220.645 1.00 2.17  ? 4180 TYR A CA    1 
ATOM   20079 C  C     . TYR A 1 4180 ? 145.946 202.170 221.421 1.00 1.48  ? 4180 TYR A C     1 
ATOM   20080 O  O     . TYR A 1 4180 ? 147.046 201.608 221.422 1.00 1.54  ? 4180 TYR A O     1 
ATOM   20081 C  CB    . TYR A 1 4180 ? 145.932 204.677 221.550 1.00 3.13  ? 4180 TYR A CB    1 
ATOM   20082 C  CG    . TYR A 1 4180 ? 146.497 205.877 220.832 1.00 3.96  ? 4180 TYR A CG    1 
ATOM   20083 C  CD1   . TYR A 1 4180 ? 145.687 206.688 220.050 1.00 5.34  ? 4180 TYR A CD1   1 
ATOM   20084 C  CD2   . TYR A 1 4180 ? 147.843 206.195 220.929 1.00 4.85  ? 4180 TYR A CD2   1 
ATOM   20085 C  CE1   . TYR A 1 4180 ? 146.203 207.784 219.387 1.00 6.85  ? 4180 TYR A CE1   1 
ATOM   20086 C  CE2   . TYR A 1 4180 ? 148.366 207.286 220.273 1.00 6.38  ? 4180 TYR A CE2   1 
ATOM   20087 C  CZ    . TYR A 1 4180 ? 147.542 208.077 219.503 1.00 6.87  ? 4180 TYR A CZ    1 
ATOM   20088 O  OH    . TYR A 1 4180 ? 148.064 209.166 218.849 1.00 8.99  ? 4180 TYR A OH    1 
ATOM   20089 N  N     . PHE A 1 4181 ? 144.899 201.688 222.095 1.00 1.98  ? 4181 PHE A N     1 
ATOM   20090 C  CA    . PHE A 1 4181 ? 144.998 200.404 222.779 1.00 1.16  ? 4181 PHE A CA    1 
ATOM   20091 C  C     . PHE A 1 4181 ? 145.267 199.277 221.791 1.00 0.60  ? 4181 PHE A C     1 
ATOM   20092 O  O     . PHE A 1 4181 ? 146.121 198.418 222.036 1.00 0.50  ? 4181 PHE A O     1 
ATOM   20093 C  CB    . PHE A 1 4181 ? 143.719 200.129 223.571 1.00 1.59  ? 4181 PHE A CB    1 
ATOM   20094 C  CG    . PHE A 1 4181 ? 143.680 198.765 224.190 1.00 2.86  ? 4181 PHE A CG    1 
ATOM   20095 C  CD1   . PHE A 1 4181 ? 144.194 198.553 225.455 1.00 3.10  ? 4181 PHE A CD1   1 
ATOM   20096 C  CD2   . PHE A 1 4181 ? 143.142 197.688 223.503 1.00 2.30  ? 4181 PHE A CD2   1 
ATOM   20097 C  CE1   . PHE A 1 4181 ? 144.164 197.304 226.024 1.00 4.05  ? 4181 PHE A CE1   1 
ATOM   20098 C  CE2   . PHE A 1 4181 ? 143.119 196.433 224.068 1.00 3.29  ? 4181 PHE A CE2   1 
ATOM   20099 C  CZ    . PHE A 1 4181 ? 143.631 196.241 225.328 1.00 3.51  ? 4181 PHE A CZ    1 
ATOM   20100 N  N     . LEU A 1 4182 ? 144.544 199.263 220.669 1.00 0.73  ? 4182 LEU A N     1 
ATOM   20101 C  CA    . LEU A 1 4182 ? 144.772 198.244 219.651 1.00 0.82  ? 4182 LEU A CA    1 
ATOM   20102 C  C     . LEU A 1 4182 ? 146.182 198.339 219.093 1.00 0.42  ? 4182 LEU A C     1 
ATOM   20103 O  O     . LEU A 1 4182 ? 146.840 197.319 218.862 1.00 0.44  ? 4182 LEU A O     1 
ATOM   20104 C  CB    . LEU A 1 4182 ? 143.745 198.386 218.531 1.00 1.07  ? 4182 LEU A CB    1 
ATOM   20105 C  CG    . LEU A 1 4182 ? 142.321 197.944 218.859 1.00 2.48  ? 4182 LEU A CG    1 
ATOM   20106 C  CD1   . LEU A 1 4182 ? 141.361 198.492 217.821 1.00 5.38  ? 4182 LEU A CD1   1 
ATOM   20107 C  CD2   . LEU A 1 4182 ? 142.236 196.428 218.942 1.00 2.17  ? 4182 LEU A CD2   1 
ATOM   20108 N  N     . LEU A 1 4183 ? 146.661 199.562 218.870 1.00 0.40  ? 4183 LEU A N     1 
ATOM   20109 C  CA    . LEU A 1 4183 ? 148.035 199.756 218.432 1.00 0.38  ? 4183 LEU A CA    1 
ATOM   20110 C  C     . LEU A 1 4183 ? 149.025 199.274 219.485 1.00 0.42  ? 4183 LEU A C     1 
ATOM   20111 O  O     . LEU A 1 4183 ? 150.034 198.642 219.154 1.00 0.50  ? 4183 LEU A O     1 
ATOM   20112 C  CB    . LEU A 1 4183 ? 148.264 201.230 218.105 1.00 1.35  ? 4183 LEU A CB    1 
ATOM   20113 C  CG    . LEU A 1 4183 ? 149.612 201.601 217.494 1.00 2.76  ? 4183 LEU A CG    1 
ATOM   20114 C  CD1   . LEU A 1 4183 ? 149.925 200.689 216.321 1.00 1.50  ? 4183 LEU A CD1   1 
ATOM   20115 C  CD2   . LEU A 1 4183 ? 149.593 203.054 217.067 1.00 5.33  ? 4183 LEU A CD2   1 
ATOM   20116 N  N     . ALA A 1 4184 ? 148.755 199.564 220.761 1.00 0.29  ? 4184 ALA A N     1 
ATOM   20117 C  CA    . ALA A 1 4184 ? 149.640 199.102 221.825 1.00 0.30  ? 4184 ALA A CA    1 
ATOM   20118 C  C     . ALA A 1 4184 ? 149.645 197.582 221.918 1.00 0.26  ? 4184 ALA A C     1 
ATOM   20119 O  O     . ALA A 1 4184 ? 150.706 196.965 222.067 1.00 0.29  ? 4184 ALA A O     1 
ATOM   20120 C  CB    . ALA A 1 4184 ? 149.229 199.720 223.162 1.00 0.60  ? 4184 ALA A CB    1 
ATOM   20121 N  N     . TRP A 1 4185 ? 148.468 196.960 221.833 1.00 0.24  ? 4185 TRP A N     1 
ATOM   20122 C  CA    . TRP A 1 4185 ? 148.406 195.504 221.833 1.00 0.30  ? 4185 TRP A CA    1 
ATOM   20123 C  C     . TRP A 1 4185 ? 149.113 194.927 220.614 1.00 0.45  ? 4185 TRP A C     1 
ATOM   20124 O  O     . TRP A 1 4185 ? 149.878 193.964 220.730 1.00 0.53  ? 4185 TRP A O     1 
ATOM   20125 C  CB    . TRP A 1 4185 ? 146.950 195.037 221.878 1.00 0.90  ? 4185 TRP A CB    1 
ATOM   20126 C  CG    . TRP A 1 4185 ? 146.806 193.556 221.718 1.00 0.93  ? 4185 TRP A CG    1 
ATOM   20127 C  CD1   . TRP A 1 4185 ? 146.592 192.873 220.558 1.00 0.66  ? 4185 TRP A CD1   1 
ATOM   20128 C  CD2   . TRP A 1 4185 ? 146.877 192.571 222.754 1.00 1.58  ? 4185 TRP A CD2   1 
ATOM   20129 N  NE1   . TRP A 1 4185 ? 146.523 191.525 220.806 1.00 1.19  ? 4185 TRP A NE1   1 
ATOM   20130 C  CE2   . TRP A 1 4185 ? 146.694 191.314 222.148 1.00 1.83  ? 4185 TRP A CE2   1 
ATOM   20131 C  CE3   . TRP A 1 4185 ? 147.074 192.632 224.137 1.00 0.91  ? 4185 TRP A CE3   1 
ATOM   20132 C  CZ2   . TRP A 1 4185 ? 146.703 190.127 222.876 1.00 1.53  ? 4185 TRP A CZ2   1 
ATOM   20133 C  CZ3   . TRP A 1 4185 ? 147.085 191.455 224.855 1.00 1.25  ? 4185 TRP A CZ3   1 
ATOM   20134 C  CH2   . TRP A 1 4185 ? 146.900 190.219 224.224 1.00 1.59  ? 4185 TRP A CH2   1 
ATOM   20135 N  N     . PHE A 1 4186 ? 148.873 195.509 219.437 1.00 0.27  ? 4186 PHE A N     1 
ATOM   20136 C  CA    . PHE A 1 4186 ? 149.522 195.023 218.228 1.00 0.12  ? 4186 PHE A CA    1 
ATOM   20137 C  C     . PHE A 1 4186 ? 151.033 195.180 218.321 1.00 0.09  ? 4186 PHE A C     1 
ATOM   20138 O  O     . PHE A 1 4186 ? 151.783 194.283 217.926 1.00 0.12  ? 4186 PHE A O     1 
ATOM   20139 C  CB    . PHE A 1 4186 ? 148.970 195.762 217.005 1.00 0.19  ? 4186 PHE A CB    1 
ATOM   20140 C  CG    . PHE A 1 4186 ? 149.754 195.528 215.746 1.00 0.10  ? 4186 PHE A CG    1 
ATOM   20141 C  CD1   . PHE A 1 4186 ? 149.491 194.431 214.946 1.00 0.14  ? 4186 PHE A CD1   1 
ATOM   20142 C  CD2   . PHE A 1 4186 ? 150.752 196.410 215.357 1.00 0.23  ? 4186 PHE A CD2   1 
ATOM   20143 C  CE1   . PHE A 1 4186 ? 150.211 194.213 213.790 1.00 0.19  ? 4186 PHE A CE1   1 
ATOM   20144 C  CE2   . PHE A 1 4186 ? 151.474 196.194 214.202 1.00 0.21  ? 4186 PHE A CE2   1 
ATOM   20145 C  CZ    . PHE A 1 4186 ? 151.200 195.096 213.419 1.00 0.17  ? 4186 PHE A CZ    1 
ATOM   20146 N  N     . HIS A 1 4187 ? 151.495 196.314 218.847 1.00 0.23  ? 4187 HIS A N     1 
ATOM   20147 C  CA    . HIS A 1 4187 ? 152.930 196.535 218.984 1.00 0.13  ? 4187 HIS A CA    1 
ATOM   20148 C  C     . HIS A 1 4187 ? 153.549 195.559 219.979 1.00 0.13  ? 4187 HIS A C     1 
ATOM   20149 O  O     . HIS A 1 4187 ? 154.684 195.110 219.789 1.00 0.16  ? 4187 HIS A O     1 
ATOM   20150 C  CB    . HIS A 1 4187 ? 153.195 197.981 219.393 1.00 0.14  ? 4187 HIS A CB    1 
ATOM   20151 C  CG    . HIS A 1 4187 ? 154.646 198.325 219.495 1.00 0.31  ? 4187 HIS A CG    1 
ATOM   20152 N  ND1   . HIS A 1 4187 ? 155.426 198.593 218.392 1.00 0.23  ? 4187 HIS A ND1   1 
ATOM   20153 C  CD2   . HIS A 1 4187 ? 155.461 198.447 220.570 1.00 0.22  ? 4187 HIS A CD2   1 
ATOM   20154 C  CE1   . HIS A 1 4187 ? 156.659 198.860 218.782 1.00 0.34  ? 4187 HIS A CE1   1 
ATOM   20155 N  NE2   . HIS A 1 4187 ? 156.706 198.781 220.100 1.00 0.28  ? 4187 HIS A NE2   1 
ATOM   20156 N  N     . ALA A 1 4188 ? 152.826 195.227 221.049 1.00 0.12  ? 4188 ALA A N     1 
ATOM   20157 C  CA    . ALA A 1 4188 ? 153.349 194.275 222.023 1.00 0.15  ? 4188 ALA A CA    1 
ATOM   20158 C  C     . ALA A 1 4188 ? 153.439 192.873 221.437 1.00 0.34  ? 4188 ALA A C     1 
ATOM   20159 O  O     . ALA A 1 4188 ? 154.449 192.185 221.620 1.00 0.67  ? 4188 ALA A O     1 
ATOM   20160 C  CB    . ALA A 1 4188 ? 152.484 194.276 223.282 1.00 0.23  ? 4188 ALA A CB    1 
ATOM   20161 N  N     . ILE A 1 4189 ? 152.396 192.435 220.728 1.00 0.27  ? 4189 ILE A N     1 
ATOM   20162 C  CA    . ILE A 1 4189 ? 152.389 191.089 220.161 1.00 0.39  ? 4189 ILE A CA    1 
ATOM   20163 C  C     . ILE A 1 4189 ? 153.500 190.936 219.132 1.00 0.46  ? 4189 ILE A C     1 
ATOM   20164 O  O     . ILE A 1 4189 ? 154.216 189.928 219.115 1.00 1.94  ? 4189 ILE A O     1 
ATOM   20165 C  CB    . ILE A 1 4189 ? 151.010 190.766 219.557 1.00 0.57  ? 4189 ILE A CB    1 
ATOM   20166 C  CG1   . ILE A 1 4189 ? 149.915 190.859 220.622 1.00 1.13  ? 4189 ILE A CG1   1 
ATOM   20167 C  CG2   . ILE A 1 4189 ? 151.015 189.392 218.907 1.00 0.59  ? 4189 ILE A CG2   1 
ATOM   20168 C  CD1   . ILE A 1 4189 ? 150.231 190.139 221.907 1.00 0.48  ? 4189 ILE A CD1   1 
ATOM   20169 N  N     . ILE A 1 4190 ? 153.665 191.935 218.264 1.00 0.26  ? 4190 ILE A N     1 
ATOM   20170 C  CA    . ILE A 1 4190 ? 154.677 191.851 217.215 1.00 0.46  ? 4190 ILE A CA    1 
ATOM   20171 C  C     . ILE A 1 4190 ? 156.077 191.823 217.816 1.00 0.42  ? 4190 ILE A C     1 
ATOM   20172 O  O     . ILE A 1 4190 ? 156.939 191.051 217.381 1.00 0.47  ? 4190 ILE A O     1 
ATOM   20173 C  CB    . ILE A 1 4190 ? 154.502 193.012 216.215 1.00 0.29  ? 4190 ILE A CB    1 
ATOM   20174 C  CG1   . ILE A 1 4190 ? 153.143 192.924 215.519 1.00 0.29  ? 4190 ILE A CG1   1 
ATOM   20175 C  CG2   . ILE A 1 4190 ? 155.614 193.019 215.191 1.00 0.38  ? 4190 ILE A CG2   1 
ATOM   20176 C  CD1   . ILE A 1 4190 ? 152.745 191.532 215.106 1.00 0.96  ? 4190 ILE A CD1   1 
ATOM   20177 N  N     . GLN A 1 4191 ? 156.327 192.662 218.823 1.00 0.73  ? 4191 GLN A N     1 
ATOM   20178 C  CA    . GLN A 1 4191 ? 157.652 192.704 219.435 1.00 1.10  ? 4191 GLN A CA    1 
ATOM   20179 C  C     . GLN A 1 4191 ? 157.948 191.436 220.225 1.00 0.85  ? 4191 GLN A C     1 
ATOM   20180 O  O     . GLN A 1 4191 ? 159.077 190.932 220.195 1.00 2.76  ? 4191 GLN A O     1 
ATOM   20181 C  CB    . GLN A 1 4191 ? 157.782 193.935 220.329 1.00 0.77  ? 4191 GLN A CB    1 
ATOM   20182 C  CG    . GLN A 1 4191 ? 157.977 195.234 219.568 1.00 0.82  ? 4191 GLN A CG    1 
ATOM   20183 C  CD    . GLN A 1 4191 ? 158.625 196.312 220.411 1.00 2.40  ? 4191 GLN A CD    1 
ATOM   20184 O  OE1   . GLN A 1 4191 ? 158.123 196.670 221.474 1.00 7.40  ? 4191 GLN A OE1   1 
ATOM   20185 N  NE2   . GLN A 1 4191 ? 159.745 196.840 219.936 1.00 1.86  ? 4191 GLN A NE2   1 
ATOM   20186 N  N     . GLU A 1 4192 ? 156.938 190.905 220.918 1.00 0.59  ? 4192 GLU A N     1 
ATOM   20187 C  CA    . GLU A 1 4192 ? 157.154 189.708 221.778 1.00 0.88  ? 4192 GLU A CA    1 
ATOM   20188 C  C     . GLU A 1 4192 ? 157.447 188.470 220.910 1.00 1.75  ? 4192 GLU A C     1 
ATOM   20189 O  O     . GLU A 1 4192 ? 158.149 187.560 221.402 1.00 5.62  ? 4192 GLU A O     1 
ATOM   20190 C  CB    . GLU A 1 4192 ? 155.948 189.491 222.693 1.00 0.81  ? 4192 GLU A CB    1 
ATOM   20191 C  CG    . GLU A 1 4192 ? 155.939 190.414 223.908 1.00 0.84  ? 4192 GLU A CG    1 
ATOM   20192 C  CD    . GLU A 1 4192 ? 157.045 190.109 224.902 1.00 10.12 ? 4192 GLU A CD    1 
ATOM   20193 O  OE1   . GLU A 1 4192 ? 157.070 188.975 225.422 1.00 14.74 ? 4192 GLU A OE1   1 
ATOM   20194 O  OE2   . GLU A 1 4192 ? 157.881 191.000 225.156 1.00 11.24 ? 4192 GLU A OE2   1 
ATOM   20195 N  N     . ARG A 1 4193 ? 156.928 188.438 219.680 1.00 1.03  ? 4193 ARG A N     1 
ATOM   20196 C  CA    . ARG A 1 4193 ? 157.147 187.278 218.775 1.00 0.85  ? 4193 ARG A CA    1 
ATOM   20197 C  C     . ARG A 1 4193 ? 158.630 187.213 218.374 1.00 1.39  ? 4193 ARG A C     1 
ATOM   20198 O  O     . ARG A 1 4193 ? 159.098 186.110 218.020 1.00 3.98  ? 4193 ARG A O     1 
ATOM   20199 C  CB    . ARG A 1 4193 ? 156.224 187.359 217.553 1.00 0.75  ? 4193 ARG A CB    1 
ATOM   20200 C  CG    . ARG A 1 4193 ? 154.755 187.138 217.879 1.00 0.97  ? 4193 ARG A CG    1 
ATOM   20201 C  CD    . ARG A 1 4193 ? 153.906 186.992 216.627 1.00 1.47  ? 4193 ARG A CD    1 
ATOM   20202 N  NE    . ARG A 1 4193 ? 154.376 185.888 215.784 1.00 1.11  ? 4193 ARG A NE    1 
ATOM   20203 C  CZ    . ARG A 1 4193 ? 153.662 184.812 215.480 1.00 0.77  ? 4193 ARG A CZ    1 
ATOM   20204 N  NH1   . ARG A 1 4193 ? 152.441 184.669 215.963 1.00 0.70  ? 4193 ARG A NH1   1 
ATOM   20205 N  NH2   . ARG A 1 4193 ? 154.174 183.880 214.697 1.00 1.09  ? 4193 ARG A NH2   1 
ATOM   20206 N  N     . LEU A 1 4194 ? 159.339 188.344 218.439 1.00 2.15  ? 4194 LEU A N     1 
ATOM   20207 C  CA    . LEU A 1 4194 ? 160.787 188.372 218.110 1.00 1.87  ? 4194 LEU A CA    1 
ATOM   20208 C  C     . LEU A 1 4194 ? 161.553 187.486 219.106 1.00 2.94  ? 4194 LEU A C     1 
ATOM   20209 O  O     . LEU A 1 4194 ? 162.590 186.912 218.711 1.00 3.91  ? 4194 LEU A O     1 
ATOM   20210 C  CB    . LEU A 1 4194 ? 161.291 189.815 218.124 1.00 1.93  ? 4194 LEU A CB    1 
ATOM   20211 C  CG    . LEU A 1 4194 ? 160.698 190.739 217.055 1.00 3.56  ? 4194 LEU A CG    1 
ATOM   20212 C  CD1   . LEU A 1 4194 ? 161.097 192.184 217.298 1.00 2.48  ? 4194 LEU A CD1   1 
ATOM   20213 C  CD2   . LEU A 1 4194 ? 161.120 190.294 215.665 1.00 1.47  ? 4194 LEU A CD2   1 
ATOM   20214 N  N     . ARG A 1 4195 ? 161.055 187.377 220.342 1.00 2.88  ? 4195 ARG A N     1 
ATOM   20215 C  CA    . ARG A 1 4195 ? 161.706 186.512 221.361 1.00 2.92  ? 4195 ARG A CA    1 
ATOM   20216 C  C     . ARG A 1 4195 ? 161.779 185.082 220.807 1.00 4.49  ? 4195 ARG A C     1 
ATOM   20217 O  O     . ARG A 1 4195 ? 162.801 184.406 221.049 1.00 6.99  ? 4195 ARG A O     1 
ATOM   20218 C  CB    . ARG A 1 4195 ? 160.945 186.596 222.690 1.00 3.32  ? 4195 ARG A CB    1 
ATOM   20219 C  CG    . ARG A 1 4195 ? 160.986 187.983 223.313 1.00 8.06  ? 4195 ARG A CG    1 
ATOM   20220 C  CD    . ARG A 1 4195 ? 160.112 188.097 224.553 1.00 6.82  ? 4195 ARG A CD    1 
ATOM   20221 N  NE    . ARG A 1 4195 ? 160.313 189.375 225.246 1.00 18.64 ? 4195 ARG A NE    1 
ATOM   20222 C  CZ    . ARG A 1 4195 ? 161.468 189.764 225.774 1.00 10.31 ? 4195 ARG A CZ    1 
ATOM   20223 N  NH1   . ARG A 1 4195 ? 162.366 188.865 226.132 1.00 6.56  ? 4195 ARG A NH1   1 
ATOM   20224 N  NH2   . ARG A 1 4195 ? 161.717 191.049 225.945 1.00 8.84  ? 4195 ARG A NH2   1 
ATOM   20225 N  N     . TYR A 1 4196 ? 160.736 184.641 220.099 1.00 3.63  ? 4196 TYR A N     1 
ATOM   20226 C  CA    . TYR A 1 4196 ? 160.775 183.305 219.444 1.00 4.04  ? 4196 TYR A CA    1 
ATOM   20227 C  C     . TYR A 1 4196 ? 161.489 183.498 218.113 1.00 7.21  ? 4196 TYR A C     1 
ATOM   20228 O  O     . TYR A 1 4196 ? 160.854 183.329 217.050 1.00 4.89  ? 4196 TYR A O     1 
ATOM   20229 C  CB    . TYR A 1 4196 ? 159.334 182.786 219.408 1.00 3.77  ? 4196 TYR A CB    1 
ATOM   20230 C  CG    . TYR A 1 4196 ? 158.707 182.758 220.796 1.00 5.05  ? 4196 TYR A CG    1 
ATOM   20231 C  CD1   . TYR A 1 4196 ? 158.814 181.637 221.608 1.00 5.10  ? 4196 TYR A CD1   1 
ATOM   20232 C  CD2   . TYR A 1 4196 ? 158.038 183.865 221.304 1.00 3.89  ? 4196 TYR A CD2   1 
ATOM   20233 C  CE1   . TYR A 1 4196 ? 158.257 181.610 222.875 1.00 8.03  ? 4196 TYR A CE1   1 
ATOM   20234 C  CE2   . TYR A 1 4196 ? 157.478 183.850 222.570 1.00 4.55  ? 4196 TYR A CE2   1 
ATOM   20235 C  CZ    . TYR A 1 4196 ? 157.588 182.719 223.359 1.00 5.86  ? 4196 TYR A CZ    1 
ATOM   20236 O  OH    . TYR A 1 4196 ? 157.037 182.696 224.607 1.00 7.12  ? 4196 TYR A OH    1 
ATOM   20237 N  N     . ALA A 1 4197 ? 162.781 183.835 218.172 1.00 16.48 ? 4197 ALA A N     1 
ATOM   20238 C  CA    . ALA A 1 4197 ? 163.578 184.138 216.955 1.00 8.60  ? 4197 ALA A CA    1 
ATOM   20239 C  C     . ALA A 1 4197 ? 162.957 183.551 215.684 1.00 7.10  ? 4197 ALA A C     1 
ATOM   20240 O  O     . ALA A 1 4197 ? 162.520 184.362 214.845 1.00 8.44  ? 4197 ALA A O     1 
ATOM   20241 C  CB    . ALA A 1 4197 ? 165.012 183.679 217.148 1.00 8.34  ? 4197 ALA A CB    1 
ATOM   20242 N  N     . PRO A 1 4198 ? 162.902 182.216 215.476 1.00 30.00 ? 4198 PRO A N     1 
ATOM   20243 C  CA    . PRO A 1 4198 ? 162.423 181.671 214.205 1.00 30.00 ? 4198 PRO A CA    1 
ATOM   20244 C  C     . PRO A 1 4198 ? 160.911 181.546 213.998 1.00 30.00 ? 4198 PRO A C     1 
ATOM   20245 O  O     . PRO A 1 4198 ? 160.440 181.886 212.896 1.00 30.00 ? 4198 PRO A O     1 
ATOM   20246 C  CB    . PRO A 1 4198 ? 163.118 180.294 214.221 1.00 30.00 ? 4198 PRO A CB    1 
ATOM   20247 C  CG    . PRO A 1 4198 ? 163.080 179.888 215.675 1.00 30.00 ? 4198 PRO A CG    1 
ATOM   20248 C  CD    . PRO A 1 4198 ? 163.265 181.187 216.442 1.00 30.00 ? 4198 PRO A CD    1 
ATOM   20249 N  N     . LEU A 1 4199 ? 160.176 181.067 215.005 1.00 2.46  ? 4199 LEU A N     1 
ATOM   20250 C  CA    . LEU A 1 4199 ? 158.718 180.821 214.835 1.00 2.37  ? 4199 LEU A CA    1 
ATOM   20251 C  C     . LEU A 1 4199 ? 157.934 182.146 214.786 1.00 3.82  ? 4199 LEU A C     1 
ATOM   20252 O  O     . LEU A 1 4199 ? 157.103 182.300 213.867 1.00 5.74  ? 4199 LEU A O     1 
ATOM   20253 C  CB    . LEU A 1 4199 ? 158.232 179.918 215.969 1.00 3.87  ? 4199 LEU A CB    1 
ATOM   20254 C  CG    . LEU A 1 4199 ? 157.013 179.046 215.653 1.00 3.83  ? 4199 LEU A CG    1 
ATOM   20255 C  CD1   . LEU A 1 4199 ? 157.313 178.132 214.481 1.00 4.08  ? 4199 LEU A CD1   1 
ATOM   20256 C  CD2   . LEU A 1 4199 ? 156.604 178.236 216.870 1.00 2.85  ? 4199 LEU A CD2   1 
ATOM   20257 N  N     . GLY A 1 4200 ? 158.180 183.055 215.734 1.00 2.34  ? 4200 GLY A N     1 
ATOM   20258 C  CA    . GLY A 1 4200 ? 157.428 184.325 215.780 1.00 1.50  ? 4200 GLY A CA    1 
ATOM   20259 C  C     . GLY A 1 4200 ? 157.592 185.081 214.481 1.00 1.34  ? 4200 GLY A C     1 
ATOM   20260 O  O     . GLY A 1 4200 ? 156.576 185.582 213.958 1.00 1.16  ? 4200 GLY A O     1 
ATOM   20261 N  N     . TRP A 1 4201 ? 158.825 185.170 213.978 1.00 1.55  ? 4201 TRP A N     1 
ATOM   20262 C  CA    . TRP A 1 4201 ? 159.092 185.814 212.671 1.00 1.07  ? 4201 TRP A CA    1 
ATOM   20263 C  C     . TRP A 1 4201 ? 160.281 185.095 212.039 1.00 1.71  ? 4201 TRP A C     1 
ATOM   20264 O  O     . TRP A 1 4201 ? 161.169 184.655 212.790 1.00 4.86  ? 4201 TRP A O     1 
ATOM   20265 C  CB    . TRP A 1 4201 ? 159.389 187.310 212.842 1.00 1.40  ? 4201 TRP A CB    1 
ATOM   20266 C  CG    . TRP A 1 4201 ? 158.251 188.115 213.410 1.00 0.59  ? 4201 TRP A CG    1 
ATOM   20267 C  CD1   . TRP A 1 4201 ? 158.046 188.447 214.717 1.00 0.61  ? 4201 TRP A CD1   1 
ATOM   20268 C  CD2   . TRP A 1 4201 ? 157.147 188.685 212.674 1.00 0.76  ? 4201 TRP A CD2   1 
ATOM   20269 N  NE1   . TRP A 1 4201 ? 156.903 189.188 214.845 1.00 0.41  ? 4201 TRP A NE1   1 
ATOM   20270 C  CE2   . TRP A 1 4201 ? 156.328 189.349 213.612 1.00 0.56  ? 4201 TRP A CE2   1 
ATOM   20271 C  CE3   . TRP A 1 4201 ? 156.777 188.699 211.324 1.00 0.61  ? 4201 TRP A CE3   1 
ATOM   20272 C  CZ2   . TRP A 1 4201 ? 155.164 190.016 213.239 1.00 0.44  ? 4201 TRP A CZ2   1 
ATOM   20273 C  CZ3   . TRP A 1 4201 ? 155.625 189.359 210.959 1.00 0.66  ? 4201 TRP A CZ3   1 
ATOM   20274 C  CH2   . TRP A 1 4201 ? 154.832 190.009 211.905 1.00 0.50  ? 4201 TRP A CH2   1 
ATOM   20275 N  N     . SER A 1 4202 ? 160.297 184.967 210.712 1.00 2.65  ? 4202 SER A N     1 
ATOM   20276 C  CA    . SER A 1 4202 ? 161.401 184.240 210.037 1.00 2.54  ? 4202 SER A CA    1 
ATOM   20277 C  C     . SER A 1 4202 ? 162.723 184.954 210.346 1.00 1.48  ? 4202 SER A C     1 
ATOM   20278 O  O     . SER A 1 4202 ? 163.770 184.274 210.375 1.00 7.15  ? 4202 SER A O     1 
ATOM   20279 C  CB    . SER A 1 4202 ? 161.169 184.134 208.554 1.00 2.84  ? 4202 SER A CB    1 
ATOM   20280 O  OG    . SER A 1 4202 ? 161.427 185.372 207.906 1.00 5.05  ? 4202 SER A OG    1 
ATOM   20281 N  N     . LYS A 1 4203 ? 162.670 186.268 210.576 1.00 3.30  ? 4203 LYS A N     1 
ATOM   20282 C  CA    . LYS A 1 4203 ? 163.911 187.050 210.809 1.00 2.67  ? 4203 LYS A CA    1 
ATOM   20283 C  C     . LYS A 1 4203 ? 163.755 187.934 212.054 1.00 2.78  ? 4203 LYS A C     1 
ATOM   20284 O  O     . LYS A 1 4203 ? 162.606 188.121 212.507 1.00 4.17  ? 4203 LYS A O     1 
ATOM   20285 C  CB    . LYS A 1 4203 ? 164.210 187.915 209.579 1.00 3.70  ? 4203 LYS A CB    1 
ATOM   20286 C  CG    . LYS A 1 4203 ? 164.031 187.203 208.246 1.00 8.54  ? 4203 LYS A CG    1 
ATOM   20287 C  CD    . LYS A 1 4203 ? 164.435 188.043 207.042 1.00 7.88  ? 4203 LYS A CD    1 
ATOM   20288 C  CE    . LYS A 1 4203 ? 165.881 188.420 207.087 1.00 12.22 ? 4203 LYS A CE    1 
ATOM   20289 N  NZ    . LYS A 1 4203 ? 166.298 189.124 205.873 1.00 20.16 ? 4203 LYS A NZ    1 
ATOM   20290 N  N     . LYS A 1 4204 ? 164.868 188.456 212.575 1.00 4.11  ? 4204 LYS A N     1 
ATOM   20291 C  CA    . LYS A 1 4204 ? 164.836 189.336 213.741 1.00 2.85  ? 4204 LYS A CA    1 
ATOM   20292 C  C     . LYS A 1 4204 ? 164.679 190.786 213.276 1.00 4.14  ? 4204 LYS A C     1 
ATOM   20293 O  O     . LYS A 1 4204 ? 165.627 191.570 213.222 1.00 14.52 ? 4204 LYS A O     1 
ATOM   20294 C  CB    . LYS A 1 4204 ? 166.092 189.147 214.579 1.00 4.95  ? 4204 LYS A CB    1 
ATOM   20295 C  CG    . LYS A 1 4204 ? 166.132 189.978 215.845 1.00 9.70  ? 4204 LYS A CG    1 
ATOM   20296 C  CD    . LYS A 1 4204 ? 165.002 189.593 216.773 1.00 11.87 ? 4204 LYS A CD    1 
ATOM   20297 C  CE    . LYS A 1 4204 ? 165.191 188.172 217.260 1.00 9.20  ? 4204 LYS A CE    1 
ATOM   20298 N  NZ    . LYS A 1 4204 ? 166.373 188.060 218.159 1.00 18.69 ? 4204 LYS A NZ    1 
ATOM   20299 N  N     . TYR A 1 4205 ? 163.444 191.133 212.920 1.00 3.02  ? 4205 TYR A N     1 
ATOM   20300 C  CA    . TYR A 1 4205 ? 163.164 192.494 212.485 1.00 3.92  ? 4205 TYR A CA    1 
ATOM   20301 C  C     . TYR A 1 4205 ? 163.279 193.467 213.650 1.00 3.36  ? 4205 TYR A C     1 
ATOM   20302 O  O     . TYR A 1 4205 ? 163.059 193.116 214.812 1.00 4.16  ? 4205 TYR A O     1 
ATOM   20303 C  CB    . TYR A 1 4205 ? 161.772 192.602 211.869 1.00 1.51  ? 4205 TYR A CB    1 
ATOM   20304 C  CG    . TYR A 1 4205 ? 161.521 191.666 210.718 1.00 1.60  ? 4205 TYR A CG    1 
ATOM   20305 C  CD1   . TYR A 1 4205 ? 162.053 191.924 209.461 1.00 1.21  ? 4205 TYR A CD1   1 
ATOM   20306 C  CD2   . TYR A 1 4205 ? 160.726 190.543 210.878 1.00 1.37  ? 4205 TYR A CD2   1 
ATOM   20307 C  CE1   . TYR A 1 4205 ? 161.819 191.075 208.404 1.00 1.56  ? 4205 TYR A CE1   1 
ATOM   20308 C  CE2   . TYR A 1 4205 ? 160.484 189.692 209.827 1.00 1.69  ? 4205 TYR A CE2   1 
ATOM   20309 C  CZ    . TYR A 1 4205 ? 161.033 189.961 208.591 1.00 4.41  ? 4205 TYR A CZ    1 
ATOM   20310 O  OH    . TYR A 1 4205 ? 160.793 189.110 207.539 1.00 5.77  ? 4205 TYR A OH    1 
ATOM   20311 N  N     . GLU A 1 4206 ? 163.630 194.707 213.325 1.00 3.34  ? 4206 GLU A N     1 
ATOM   20312 C  CA    . GLU A 1 4206 ? 163.777 195.755 214.332 1.00 3.93  ? 4206 GLU A CA    1 
ATOM   20313 C  C     . GLU A 1 4206 ? 162.495 196.583 214.444 1.00 2.05  ? 4206 GLU A C     1 
ATOM   20314 O  O     . GLU A 1 4206 ? 162.481 197.794 214.234 1.00 5.07  ? 4206 GLU A O     1 
ATOM   20315 C  CB    . GLU A 1 4206 ? 164.980 196.631 214.009 1.00 2.88  ? 4206 GLU A CB    1 
ATOM   20316 C  CG    . GLU A 1 4206 ? 166.311 195.907 214.081 1.00 3.40  ? 4206 GLU A CG    1 
ATOM   20317 C  CD    . GLU A 1 4206 ? 167.481 196.852 214.273 1.00 14.86 ? 4206 GLU A CD    1 
ATOM   20318 O  OE1   . GLU A 1 4206 ? 167.565 197.854 213.532 1.00 23.29 ? 4206 GLU A OE1   1 
ATOM   20319 O  OE2   . GLU A 1 4206 ? 168.318 196.591 215.163 1.00 15.05 ? 4206 GLU A OE2   1 
ATOM   20320 N  N     . PHE A 1 4207 ? 161.399 195.905 214.774 1.00 1.68  ? 4207 PHE A N     1 
ATOM   20321 C  CA    . PHE A 1 4207 ? 160.188 196.616 215.160 1.00 1.60  ? 4207 PHE A CA    1 
ATOM   20322 C  C     . PHE A 1 4207 ? 160.458 197.366 216.458 1.00 3.07  ? 4207 PHE A C     1 
ATOM   20323 O  O     . PHE A 1 4207 ? 160.787 196.753 217.478 1.00 8.97  ? 4207 PHE A O     1 
ATOM   20324 C  CB    . PHE A 1 4207 ? 159.010 195.660 215.337 1.00 1.06  ? 4207 PHE A CB    1 
ATOM   20325 C  CG    . PHE A 1 4207 ? 158.732 194.791 214.147 1.00 0.98  ? 4207 PHE A CG    1 
ATOM   20326 C  CD1   . PHE A 1 4207 ? 158.265 195.338 212.964 1.00 0.76  ? 4207 PHE A CD1   1 
ATOM   20327 C  CD2   . PHE A 1 4207 ? 158.885 193.416 214.226 1.00 1.28  ? 4207 PHE A CD2   1 
ATOM   20328 C  CE1   . PHE A 1 4207 ? 157.989 194.536 211.876 1.00 0.59  ? 4207 PHE A CE1   1 
ATOM   20329 C  CE2   . PHE A 1 4207 ? 158.603 192.608 213.144 1.00 0.67  ? 4207 PHE A CE2   1 
ATOM   20330 C  CZ    . PHE A 1 4207 ? 158.158 193.169 211.965 1.00 0.78  ? 4207 PHE A CZ    1 
ATOM   20331 N  N     . GLY A 1 4208 ? 160.324 198.687 216.425 1.00 1.80  ? 4208 GLY A N     1 
ATOM   20332 C  CA    . GLY A 1 4208 ? 160.701 199.482 217.573 1.00 1.18  ? 4208 GLY A CA    1 
ATOM   20333 C  C     . GLY A 1 4208 ? 159.859 200.716 217.805 1.00 1.23  ? 4208 GLY A C     1 
ATOM   20334 O  O     . GLY A 1 4208 ? 158.723 200.807 217.334 1.00 2.57  ? 4208 GLY A O     1 
ATOM   20335 N  N     . GLU A 1 4209 ? 160.423 201.676 218.540 1.00 2.16  ? 4209 GLU A N     1 
ATOM   20336 C  CA    . GLU A 1 4209 ? 159.678 202.871 218.918 1.00 3.09  ? 4209 GLU A CA    1 
ATOM   20337 C  C     . GLU A 1 4209 ? 159.346 203.725 217.701 1.00 2.58  ? 4209 GLU A C     1 
ATOM   20338 O  O     . GLU A 1 4209 ? 158.274 204.342 217.643 1.00 1.73  ? 4209 GLU A O     1 
ATOM   20339 C  CB    . GLU A 1 4209 ? 160.481 203.670 219.948 1.00 3.10  ? 4209 GLU A CB    1 
ATOM   20340 C  CG    . GLU A 1 4209 ? 160.080 205.134 220.127 1.00 5.99  ? 4209 GLU A CG    1 
ATOM   20341 C  CD    . GLU A 1 4209 ? 158.716 205.321 220.787 1.00 14.81 ? 4209 GLU A CD    1 
ATOM   20342 O  OE1   . GLU A 1 4209 ? 157.968 204.336 220.956 1.00 5.10  ? 4209 GLU A OE1   1 
ATOM   20343 O  OE2   . GLU A 1 4209 ? 158.397 206.470 221.158 1.00 23.81 ? 4209 GLU A OE2   1 
ATOM   20344 N  N     . SER A 1 4210 ? 160.249 203.774 216.719 1.00 2.01  ? 4210 SER A N     1 
ATOM   20345 C  CA    . SER A 1 4210 ? 159.994 204.565 215.520 1.00 1.75  ? 4210 SER A CA    1 
ATOM   20346 C  C     . SER A 1 4210 ? 158.782 204.043 214.762 1.00 1.61  ? 4210 SER A C     1 
ATOM   20347 O  O     . SER A 1 4210 ? 157.967 204.827 214.262 1.00 2.58  ? 4210 SER A O     1 
ATOM   20348 C  CB    . SER A 1 4210 ? 161.231 204.572 214.620 1.00 2.17  ? 4210 SER A CB    1 
ATOM   20349 O  OG    . SER A 1 4210 ? 161.512 203.275 214.131 1.00 4.35  ? 4210 SER A OG    1 
ATOM   20350 N  N     . ASP A 1 4211 ? 158.646 202.720 214.663 1.00 1.48  ? 4211 ASP A N     1 
ATOM   20351 C  CA    . ASP A 1 4211 ? 157.461 202.144 214.039 1.00 1.40  ? 4211 ASP A CA    1 
ATOM   20352 C  C     . ASP A 1 4211 ? 156.204 202.490 214.824 1.00 1.68  ? 4211 ASP A C     1 
ATOM   20353 O  O     . ASP A 1 4211 ? 155.166 202.814 214.236 1.00 4.55  ? 4211 ASP A O     1 
ATOM   20354 C  CB    . ASP A 1 4211 ? 157.616 200.629 213.915 1.00 1.39  ? 4211 ASP A CB    1 
ATOM   20355 C  CG    . ASP A 1 4211 ? 158.635 200.229 212.869 1.00 4.31  ? 4211 ASP A CG    1 
ATOM   20356 O  OD1   . ASP A 1 4211 ? 159.203 201.125 212.213 1.00 7.84  ? 4211 ASP A OD1   1 
ATOM   20357 O  OD2   . ASP A 1 4211 ? 158.869 199.017 212.703 1.00 9.31  ? 4211 ASP A OD2   1 
ATOM   20358 N  N     . LEU A 1 4212 ? 156.279 202.433 216.154 1.00 1.45  ? 4212 LEU A N     1 
ATOM   20359 C  CA    . LEU A 1 4212 ? 155.120 202.754 216.979 1.00 0.71  ? 4212 LEU A CA    1 
ATOM   20360 C  C     . LEU A 1 4212 ? 154.733 204.224 216.853 1.00 0.89  ? 4212 LEU A C     1 
ATOM   20361 O  O     . LEU A 1 4212 ? 153.546 204.550 216.745 1.00 0.96  ? 4212 LEU A O     1 
ATOM   20362 C  CB    . LEU A 1 4212 ? 155.401 202.384 218.434 1.00 0.58  ? 4212 LEU A CB    1 
ATOM   20363 C  CG    . LEU A 1 4212 ? 154.314 202.692 219.465 1.00 0.49  ? 4212 LEU A CG    1 
ATOM   20364 C  CD1   . LEU A 1 4212 ? 153.039 201.924 219.161 1.00 0.34  ? 4212 LEU A CD1   1 
ATOM   20365 C  CD2   . LEU A 1 4212 ? 154.816 202.374 220.860 1.00 0.54  ? 4212 LEU A CD2   1 
ATOM   20366 N  N     . ARG A 1 4213 ? 155.718 205.129 216.869 1.00 1.70  ? 4213 ARG A N     1 
ATOM   20367 C  CA    . ARG A 1 4213 ? 155.404 206.550 216.726 1.00 1.77  ? 4213 ARG A CA    1 
ATOM   20368 C  C     . ARG A 1 4213 ? 154.804 206.859 215.361 1.00 1.77  ? 4213 ARG A C     1 
ATOM   20369 O  O     . ARG A 1 4213 ? 153.855 207.645 215.263 1.00 2.92  ? 4213 ARG A O     1 
ATOM   20370 C  CB    . ARG A 1 4213 ? 156.644 207.414 216.961 1.00 2.89  ? 4213 ARG A CB    1 
ATOM   20371 C  CG    . ARG A 1 4213 ? 157.173 207.416 218.381 1.00 5.93  ? 4213 ARG A CG    1 
ATOM   20372 C  CD    . ARG A 1 4213 ? 158.399 208.311 218.484 1.00 15.22 ? 4213 ARG A CD    1 
ATOM   20373 N  NE    . ARG A 1 4213 ? 158.965 208.339 219.827 1.00 10.51 ? 4213 ARG A NE    1 
ATOM   20374 C  CZ    . ARG A 1 4213 ? 160.065 209.001 220.160 1.00 22.36 ? 4213 ARG A CZ    1 
ATOM   20375 N  NH1   . ARG A 1 4213 ? 160.747 209.702 219.269 1.00 30.10 ? 4213 ARG A NH1   1 
ATOM   20376 N  NH2   . ARG A 1 4213 ? 160.494 208.956 221.419 1.00 24.98 ? 4213 ARG A NH2   1 
ATOM   20377 N  N     . SER A 1 4214 ? 155.345 206.261 214.298 1.00 1.63  ? 4214 SER A N     1 
ATOM   20378 C  CA    . SER A 1 4214 ? 154.777 206.467 212.970 1.00 1.11  ? 4214 SER A CA    1 
ATOM   20379 C  C     . SER A 1 4214 ? 153.347 205.949 212.901 1.00 1.50  ? 4214 SER A C     1 
ATOM   20380 O  O     . SER A 1 4214 ? 152.477 206.584 212.295 1.00 2.21  ? 4214 SER A O     1 
ATOM   20381 C  CB    . SER A 1 4214 ? 155.646 205.790 211.910 1.00 1.67  ? 4214 SER A CB    1 
ATOM   20382 O  OG    . SER A 1 4214 ? 156.928 206.383 211.847 1.00 5.86  ? 4214 SER A OG    1 
ATOM   20383 N  N     . ALA A 1 4215 ? 153.087 204.798 213.519 1.00 1.33  ? 4215 ALA A N     1 
ATOM   20384 C  CA    . ALA A 1 4215 ? 151.730 204.264 213.553 1.00 1.75  ? 4215 ALA A CA    1 
ATOM   20385 C  C     . ALA A 1 4215 ? 150.794 205.179 214.334 1.00 2.96  ? 4215 ALA A C     1 
ATOM   20386 O  O     . ALA A 1 4215 ? 149.624 205.337 213.968 1.00 4.25  ? 4215 ALA A O     1 
ATOM   20387 C  CB    . ALA A 1 4215 ? 151.738 202.858 214.148 1.00 1.00  ? 4215 ALA A CB    1 
ATOM   20388 N  N     . CYS A 1 4216 ? 151.289 205.787 215.416 1.00 2.84  ? 4216 CYS A N     1 
ATOM   20389 C  CA    . CYS A 1 4216 ? 150.469 206.729 216.173 1.00 2.58  ? 4216 CYS A CA    1 
ATOM   20390 C  C     . CYS A 1 4216 ? 150.145 207.972 215.355 1.00 3.36  ? 4216 CYS A C     1 
ATOM   20391 O  O     . CYS A 1 4216 ? 149.015 208.472 215.401 1.00 2.75  ? 4216 CYS A O     1 
ATOM   20392 C  CB    . CYS A 1 4216 ? 151.166 207.111 217.479 1.00 4.69  ? 4216 CYS A CB    1 
ATOM   20393 S  SG    . CYS A 1 4216 ? 151.296 205.770 218.685 1.00 8.86  ? 4216 CYS A SG    1 
ATOM   20394 N  N     . ASP A 1 4217 ? 151.122 208.493 214.606 1.00 4.66  ? 4217 ASP A N     1 
ATOM   20395 C  CA    . ASP A 1 4217 ? 150.855 209.642 213.747 1.00 3.05  ? 4217 ASP A CA    1 
ATOM   20396 C  C     . ASP A 1 4217 ? 149.855 209.290 212.654 1.00 2.72  ? 4217 ASP A C     1 
ATOM   20397 O  O     . ASP A 1 4217 ? 148.968 210.089 212.332 1.00 4.33  ? 4217 ASP A O     1 
ATOM   20398 C  CB    . ASP A 1 4217 ? 152.152 210.170 213.132 1.00 2.86  ? 4217 ASP A CB    1 
ATOM   20399 C  CG    . ASP A 1 4217 ? 153.153 210.628 214.175 1.00 12.53 ? 4217 ASP A CG    1 
ATOM   20400 O  OD1   . ASP A 1 4217 ? 152.792 211.476 215.017 1.00 19.90 ? 4217 ASP A OD1   1 
ATOM   20401 O  OD2   . ASP A 1 4217 ? 154.311 210.164 214.134 1.00 19.72 ? 4217 ASP A OD2   1 
ATOM   20402 N  N     . THR A 1 4218 ? 149.987 208.099 212.068 1.00 1.69  ? 4218 THR A N     1 
ATOM   20403 C  CA    . THR A 1 4218 ? 149.056 207.671 211.030 1.00 1.51  ? 4218 THR A CA    1 
ATOM   20404 C  C     . THR A 1 4218 ? 147.642 207.533 211.580 1.00 1.59  ? 4218 THR A C     1 
ATOM   20405 O  O     . THR A 1 4218 ? 146.669 207.934 210.931 1.00 1.71  ? 4218 THR A O     1 
ATOM   20406 C  CB    . THR A 1 4218 ? 149.533 206.355 210.415 1.00 1.24  ? 4218 THR A CB    1 
ATOM   20407 O  OG1   . THR A 1 4218 ? 150.772 206.574 209.734 1.00 4.16  ? 4218 THR A OG1   1 
ATOM   20408 C  CG2   . THR A 1 4218 ? 148.510 205.813 209.434 1.00 0.99  ? 4218 THR A CG2   1 
ATOM   20409 N  N     . VAL A 1 4219 ? 147.510 206.974 212.783 1.00 2.22  ? 4219 VAL A N     1 
ATOM   20410 C  CA    . VAL A 1 4219 ? 146.195 206.853 213.406 1.00 2.90  ? 4219 VAL A CA    1 
ATOM   20411 C  C     . VAL A 1 4219 ? 145.583 208.230 213.617 1.00 4.20  ? 4219 VAL A C     1 
ATOM   20412 O  O     . VAL A 1 4219 ? 144.405 208.458 213.324 1.00 10.11 ? 4219 VAL A O     1 
ATOM   20413 C  CB    . VAL A 1 4219 ? 146.296 206.068 214.728 1.00 2.98  ? 4219 VAL A CB    1 
ATOM   20414 C  CG1   . VAL A 1 4219 ? 145.079 206.329 215.602 1.00 5.36  ? 4219 VAL A CG1   1 
ATOM   20415 C  CG2   . VAL A 1 4219 ? 146.435 204.586 214.451 1.00 2.71  ? 4219 VAL A CG2   1 
ATOM   20416 N  N     . ASP A 1 4220 ? 146.383 209.176 214.114 1.00 3.14  ? 4220 ASP A N     1 
ATOM   20417 C  CA    . ASP A 1 4220 ? 145.871 210.516 214.379 1.00 3.43  ? 4220 ASP A CA    1 
ATOM   20418 C  C     . ASP A 1 4220 ? 145.559 211.258 213.085 1.00 5.05  ? 4220 ASP A C     1 
ATOM   20419 O  O     . ASP A 1 4220 ? 144.566 211.989 213.000 1.00 9.46  ? 4220 ASP A O     1 
ATOM   20420 C  CB    . ASP A 1 4220 ? 146.874 211.299 215.223 1.00 5.29  ? 4220 ASP A CB    1 
ATOM   20421 C  CG    . ASP A 1 4220 ? 146.843 210.896 216.679 1.00 10.97 ? 4220 ASP A CG    1 
ATOM   20422 O  OD1   . ASP A 1 4220 ? 147.916 210.874 217.308 1.00 12.99 ? 4220 ASP A OD1   1 
ATOM   20423 O  OD2   . ASP A 1 4220 ? 145.749 210.594 217.195 1.00 10.71 ? 4220 ASP A OD2   1 
ATOM   20424 N  N     . THR A 1 4221 ? 146.405 211.091 212.066 1.00 4.57  ? 4221 THR A N     1 
ATOM   20425 C  CA    . THR A 1 4221 ? 146.193 211.789 210.801 1.00 3.33  ? 4221 THR A CA    1 
ATOM   20426 C  C     . THR A 1 4221 ? 144.871 211.385 210.163 1.00 3.24  ? 4221 THR A C     1 
ATOM   20427 O  O     . THR A 1 4221 ? 144.068 212.239 209.770 1.00 5.43  ? 4221 THR A O     1 
ATOM   20428 C  CB    . THR A 1 4221 ? 147.356 211.511 209.847 1.00 2.99  ? 4221 THR A CB    1 
ATOM   20429 O  OG1   . THR A 1 4221 ? 148.555 212.104 210.360 1.00 6.80  ? 4221 THR A OG1   1 
ATOM   20430 C  CG2   . THR A 1 4221 ? 147.068 212.075 208.467 1.00 1.44  ? 4221 THR A CG2   1 
ATOM   20431 N  N     . TRP A 1 4222 ? 144.618 210.080 210.066 1.00 2.89  ? 4222 TRP A N     1 
ATOM   20432 C  CA    . TRP A 1 4222 ? 143.440 209.602 209.354 1.00 3.39  ? 4222 TRP A CA    1 
ATOM   20433 C  C     . TRP A 1 4222 ? 142.179 209.650 210.205 1.00 6.85  ? 4222 TRP A C     1 
ATOM   20434 O  O     . TRP A 1 4222 ? 141.080 209.791 209.660 1.00 7.12  ? 4222 TRP A O     1 
ATOM   20435 C  CB    . TRP A 1 4222 ? 143.696 208.189 208.834 1.00 1.81  ? 4222 TRP A CB    1 
ATOM   20436 C  CG    . TRP A 1 4222 ? 144.739 208.185 207.771 1.00 1.59  ? 4222 TRP A CG    1 
ATOM   20437 C  CD1   . TRP A 1 4222 ? 146.080 208.025 207.938 1.00 1.05  ? 4222 TRP A CD1   1 
ATOM   20438 C  CD2   . TRP A 1 4222 ? 144.529 208.376 206.369 1.00 0.87  ? 4222 TRP A CD2   1 
ATOM   20439 N  NE1   . TRP A 1 4222 ? 146.720 208.098 206.728 1.00 0.91  ? 4222 TRP A NE1   1 
ATOM   20440 C  CE2   . TRP A 1 4222 ? 145.790 208.310 205.746 1.00 0.91  ? 4222 TRP A CE2   1 
ATOM   20441 C  CE3   . TRP A 1 4222 ? 143.396 208.590 205.580 1.00 0.69  ? 4222 TRP A CE3   1 
ATOM   20442 C  CZ2   . TRP A 1 4222 ? 145.950 208.451 204.371 1.00 0.91  ? 4222 TRP A CZ2   1 
ATOM   20443 C  CZ3   . TRP A 1 4222 ? 143.557 208.730 204.216 1.00 0.97  ? 4222 TRP A CZ3   1 
ATOM   20444 C  CH2   . TRP A 1 4222 ? 144.824 208.660 203.625 1.00 1.30  ? 4222 TRP A CH2   1 
ATOM   20445 N  N     . LEU A 1 4223 ? 142.306 209.532 211.527 1.00 7.41  ? 4223 LEU A N     1 
ATOM   20446 C  CA    . LEU A 1 4223 ? 141.138 209.703 212.382 1.00 6.80  ? 4223 LEU A CA    1 
ATOM   20447 C  C     . LEU A 1 4223 ? 140.669 211.153 212.381 1.00 7.97  ? 4223 LEU A C     1 
ATOM   20448 O  O     . LEU A 1 4223 ? 139.463 211.421 212.348 1.00 11.52 ? 4223 LEU A O     1 
ATOM   20449 C  CB    . LEU A 1 4223 ? 141.449 209.239 213.802 1.00 11.22 ? 4223 LEU A CB    1 
ATOM   20450 C  CG    . LEU A 1 4223 ? 140.277 209.260 214.778 1.00 10.07 ? 4223 LEU A CG    1 
ATOM   20451 C  CD1   . LEU A 1 4223 ? 139.109 208.464 214.223 1.00 11.94 ? 4223 LEU A CD1   1 
ATOM   20452 C  CD2   . LEU A 1 4223 ? 140.718 208.714 216.116 1.00 8.03  ? 4223 LEU A CD2   1 
ATOM   20453 N  N     . ASP A 1 4224 ? 141.608 212.098 212.411 1.00 7.87  ? 4224 ASP A N     1 
ATOM   20454 C  CA    . ASP A 1 4224 ? 141.248 213.508 212.319 1.00 9.85  ? 4224 ASP A CA    1 
ATOM   20455 C  C     . ASP A 1 4224 ? 140.650 213.833 210.956 1.00 10.82 ? 4224 ASP A C     1 
ATOM   20456 O  O     . ASP A 1 4224 ? 139.749 214.672 210.852 1.00 20.04 ? 4224 ASP A O     1 
ATOM   20457 C  CB    . ASP A 1 4224 ? 142.472 214.382 212.592 1.00 10.93 ? 4224 ASP A CB    1 
ATOM   20458 C  CG    . ASP A 1 4224 ? 142.728 214.583 214.074 1.00 19.61 ? 4224 ASP A CG    1 
ATOM   20459 O  OD1   . ASP A 1 4224 ? 143.889 214.428 214.505 1.00 17.62 ? 4224 ASP A OD1   1 
ATOM   20460 O  OD2   . ASP A 1 4224 ? 141.768 214.902 214.806 1.00 24.65 ? 4224 ASP A OD2   1 
ATOM   20461 N  N     . ASP A 1 4225 ? 141.147 213.182 209.902 1.00 11.09 ? 4225 ASP A N     1 
ATOM   20462 C  CA    . ASP A 1 4225 ? 140.616 213.415 208.564 1.00 11.89 ? 4225 ASP A CA    1 
ATOM   20463 C  C     . ASP A 1 4225 ? 139.160 212.978 208.460 1.00 11.35 ? 4225 ASP A C     1 
ATOM   20464 O  O     . ASP A 1 4225 ? 138.339 213.671 207.848 1.00 21.31 ? 4225 ASP A O     1 
ATOM   20465 C  CB    . ASP A 1 4225 ? 141.477 212.688 207.530 1.00 14.69 ? 4225 ASP A CB    1 
ATOM   20466 C  CG    . ASP A 1 4225 ? 140.780 212.533 206.194 1.00 21.89 ? 4225 ASP A CG    1 
ATOM   20467 O  OD1   . ASP A 1 4225 ? 140.318 211.414 205.890 1.00 28.85 ? 4225 ASP A OD1   1 
ATOM   20468 O  OD2   . ASP A 1 4225 ? 140.697 213.528 205.445 1.00 27.99 ? 4225 ASP A OD2   1 
ATOM   20469 N  N     . THR A 1 4226 ? 138.816 211.835 209.053 1.00 10.66 ? 4226 THR A N     1 
ATOM   20470 C  CA    . THR A 1 4226 ? 137.447 211.335 208.958 1.00 16.25 ? 4226 THR A CA    1 
ATOM   20471 C  C     . THR A 1 4226 ? 136.541 212.004 209.987 1.00 21.55 ? 4226 THR A C     1 
ATOM   20472 O  O     . THR A 1 4226 ? 135.505 212.578 209.637 1.00 19.63 ? 4226 THR A O     1 
ATOM   20473 C  CB    . THR A 1 4226 ? 137.427 209.816 209.126 1.00 14.84 ? 4226 THR A CB    1 
ATOM   20474 O  OG1   . THR A 1 4226 ? 138.047 209.202 207.992 1.00 22.41 ? 4226 THR A OG1   1 
ATOM   20475 C  CG2   . THR A 1 4226 ? 135.998 209.326 209.224 1.00 16.04 ? 4226 THR A CG2   1 
ATOM   20476 N  N     . ALA A 1 4227 ? 136.915 211.936 211.262 1.00 19.67 ? 4227 ALA A N     1 
ATOM   20477 C  CA    . ALA A 1 4227 ? 136.168 212.608 212.324 1.00 18.53 ? 4227 ALA A CA    1 
ATOM   20478 C  C     . ALA A 1 4227 ? 136.585 214.071 212.326 1.00 23.21 ? 4227 ALA A C     1 
ATOM   20479 O  O     . ALA A 1 4227 ? 137.506 214.479 213.034 1.00 27.83 ? 4227 ALA A O     1 
ATOM   20480 C  CB    . ALA A 1 4227 ? 136.421 211.946 213.673 1.00 19.32 ? 4227 ALA A CB    1 
ATOM   20481 N  N     . LYS A 1 4228 ? 135.898 214.871 211.512 1.00 23.42 ? 4228 LYS A N     1 
ATOM   20482 C  CA    . LYS A 1 4228 ? 136.254 216.276 211.320 1.00 21.42 ? 4228 LYS A CA    1 
ATOM   20483 C  C     . LYS A 1 4228 ? 135.791 217.068 212.539 1.00 22.17 ? 4228 LYS A C     1 
ATOM   20484 O  O     . LYS A 1 4228 ? 134.726 217.690 212.556 1.00 23.11 ? 4228 LYS A O     1 
ATOM   20485 C  CB    . LYS A 1 4228 ? 135.645 216.813 210.032 1.00 14.34 ? 4228 LYS A CB    1 
ATOM   20486 C  CG    . LYS A 1 4228 ? 136.164 216.141 208.777 1.00 16.26 ? 4228 LYS A CG    1 
ATOM   20487 C  CD    . LYS A 1 4228 ? 135.997 217.036 207.561 1.00 26.05 ? 4228 LYS A CD    1 
ATOM   20488 C  CE    . LYS A 1 4228 ? 136.519 216.360 206.305 1.00 21.20 ? 4228 LYS A CE    1 
ATOM   20489 N  NZ    . LYS A 1 4228 ? 136.135 214.922 206.252 1.00 21.66 ? 4228 LYS A NZ    1 
ATOM   20490 N  N     . GLY A 1 4229 ? 136.621 217.039 213.576 1.00 20.06 ? 4229 GLY A N     1 
ATOM   20491 C  CA    . GLY A 1 4229 ? 136.323 217.771 214.798 1.00 21.62 ? 4229 GLY A CA    1 
ATOM   20492 C  C     . GLY A 1 4229 ? 135.042 217.337 215.476 1.00 21.95 ? 4229 GLY A C     1 
ATOM   20493 O  O     . GLY A 1 4229 ? 134.249 218.188 215.899 1.00 27.83 ? 4229 GLY A O     1 
ATOM   20494 N  N     . ARG A 1 4230 ? 134.817 216.033 215.584 1.00 22.25 ? 4230 ARG A N     1 
ATOM   20495 C  CA    . ARG A 1 4230 ? 133.609 215.489 216.184 1.00 20.83 ? 4230 ARG A CA    1 
ATOM   20496 C  C     . ARG A 1 4230 ? 133.948 214.775 217.486 1.00 22.39 ? 4230 ARG A C     1 
ATOM   20497 O  O     . ARG A 1 4230 ? 135.106 214.464 217.775 1.00 24.18 ? 4230 ARG A O     1 
ATOM   20498 C  CB    . ARG A 1 4230 ? 132.892 214.538 215.218 1.00 19.01 ? 4230 ARG A CB    1 
ATOM   20499 C  CG    . ARG A 1 4230 ? 131.895 215.232 214.303 1.00 14.18 ? 4230 ARG A CG    1 
ATOM   20500 C  CD    . ARG A 1 4230 ? 130.933 214.244 213.662 1.00 15.50 ? 4230 ARG A CD    1 
ATOM   20501 N  NE    . ARG A 1 4230 ? 131.400 213.788 212.358 1.00 28.38 ? 4230 ARG A NE    1 
ATOM   20502 C  CZ    . ARG A 1 4230 ? 132.187 212.739 212.162 1.00 28.21 ? 4230 ARG A CZ    1 
ATOM   20503 N  NH1   . ARG A 1 4230 ? 132.615 211.996 213.170 1.00 24.55 ? 4230 ARG A NH1   1 
ATOM   20504 N  NH2   . ARG A 1 4230 ? 132.553 212.424 210.924 1.00 27.65 ? 4230 ARG A NH2   1 
ATOM   20505 N  N     . GLN A 1 4231 ? 132.909 214.518 218.279 1.00 24.92 ? 4231 GLN A N     1 
ATOM   20506 C  CA    . GLN A 1 4231 ? 133.083 213.921 219.596 1.00 24.05 ? 4231 GLN A CA    1 
ATOM   20507 C  C     . GLN A 1 4231 ? 133.085 212.399 219.556 1.00 25.06 ? 4231 GLN A C     1 
ATOM   20508 O  O     . GLN A 1 4231 ? 133.894 211.764 220.240 1.00 26.32 ? 4231 GLN A O     1 
ATOM   20509 C  CB    . GLN A 1 4231 ? 131.982 214.411 220.541 1.00 18.64 ? 4231 GLN A CB    1 
ATOM   20510 C  CG    . GLN A 1 4231 ? 132.344 214.350 222.017 1.00 22.39 ? 4231 GLN A CG    1 
ATOM   20511 C  CD    . GLN A 1 4231 ? 133.804 214.663 222.283 1.00 24.71 ? 4231 GLN A CD    1 
ATOM   20512 O  OE1   . GLN A 1 4231 ? 134.515 213.887 222.921 1.00 26.23 ? 4231 GLN A OE1   1 
ATOM   20513 N  NE2   . GLN A 1 4231 ? 134.257 215.812 221.796 1.00 23.21 ? 4231 GLN A NE2   1 
ATOM   20514 N  N     . ASN A 1 4232 ? 132.196 211.796 218.768 1.00 22.49 ? 4232 ASN A N     1 
ATOM   20515 C  CA    . ASN A 1 4232 ? 132.051 210.341 218.724 1.00 19.28 ? 4232 ASN A CA    1 
ATOM   20516 C  C     . ASN A 1 4232 ? 131.902 209.916 217.268 1.00 24.47 ? 4232 ASN A C     1 
ATOM   20517 O  O     . ASN A 1 4232 ? 130.850 210.122 216.657 1.00 34.28 ? 4232 ASN A O     1 
ATOM   20518 C  CB    . ASN A 1 4232 ? 130.861 209.885 219.559 1.00 16.36 ? 4232 ASN A CB    1 
ATOM   20519 C  CG    . ASN A 1 4232 ? 131.071 210.113 221.041 1.00 24.87 ? 4232 ASN A CG    1 
ATOM   20520 O  OD1   . ASN A 1 4232 ? 131.879 209.436 221.676 1.00 28.18 ? 4232 ASN A OD1   1 
ATOM   20521 N  ND2   . ASN A 1 4232 ? 130.353 211.080 221.598 1.00 25.19 ? 4232 ASN A ND2   1 
ATOM   20522 N  N     . ILE A 1 4233 ? 132.947 209.321 216.724 1.00 21.70 ? 4233 ILE A N     1 
ATOM   20523 C  CA    . ILE A 1 4233 ? 132.931 208.792 215.366 1.00 18.87 ? 4233 ILE A CA    1 
ATOM   20524 C  C     . ILE A 1 4233 ? 132.393 207.370 215.400 1.00 18.33 ? 4233 ILE A C     1 
ATOM   20525 O  O     . ILE A 1 4233 ? 132.719 206.585 216.299 1.00 21.05 ? 4233 ILE A O     1 
ATOM   20526 C  CB    . ILE A 1 4233 ? 134.339 208.852 214.741 1.00 18.30 ? 4233 ILE A CB    1 
ATOM   20527 C  CG1   . ILE A 1 4233 ? 134.317 208.330 213.304 1.00 11.72 ? 4233 ILE A CG1   1 
ATOM   20528 C  CG2   . ILE A 1 4233 ? 135.350 208.091 215.591 1.00 16.18 ? 4233 ILE A CG2   1 
ATOM   20529 C  CD1   . ILE A 1 4233 ? 135.655 208.393 212.625 1.00 15.52 ? 4233 ILE A CD1   1 
ATOM   20530 N  N     . SER A 1 4234 ? 131.549 207.037 214.431 1.00 21.34 ? 4234 SER A N     1 
ATOM   20531 C  CA    . SER A 1 4234 ? 131.021 205.683 214.357 1.00 13.91 ? 4234 SER A CA    1 
ATOM   20532 C  C     . SER A 1 4234 ? 132.157 204.700 214.084 1.00 17.27 ? 4234 SER A C     1 
ATOM   20533 O  O     . SER A 1 4234 ? 133.041 204.985 213.268 1.00 26.78 ? 4234 SER A O     1 
ATOM   20534 C  CB    . SER A 1 4234 ? 129.959 205.578 213.263 1.00 19.14 ? 4234 SER A CB    1 
ATOM   20535 O  OG    . SER A 1 4234 ? 129.605 204.226 213.030 1.00 23.45 ? 4234 SER A OG    1 
ATOM   20536 N  N     . PRO A 1 4235 ? 132.175 203.547 214.758 1.00 18.05 ? 4235 PRO A N     1 
ATOM   20537 C  CA    . PRO A 1 4235 ? 133.272 202.588 214.540 1.00 15.39 ? 4235 PRO A CA    1 
ATOM   20538 C  C     . PRO A 1 4235 ? 133.399 202.122 213.103 1.00 14.41 ? 4235 PRO A C     1 
ATOM   20539 O  O     . PRO A 1 4235 ? 134.521 201.906 212.629 1.00 19.04 ? 4235 PRO A O     1 
ATOM   20540 C  CB    . PRO A 1 4235 ? 132.908 201.431 215.479 1.00 10.26 ? 4235 PRO A CB    1 
ATOM   20541 C  CG    . PRO A 1 4235 ? 132.065 202.064 216.536 1.00 14.33 ? 4235 PRO A CG    1 
ATOM   20542 C  CD    . PRO A 1 4235 ? 131.256 203.098 215.815 1.00 13.97 ? 4235 PRO A CD    1 
ATOM   20543 N  N     . ASP A 1 4236 ? 132.286 201.961 212.391 1.00 18.33 ? 4236 ASP A N     1 
ATOM   20544 C  CA    . ASP A 1 4236 ? 132.342 201.540 210.999 1.00 18.51 ? 4236 ASP A CA    1 
ATOM   20545 C  C     . ASP A 1 4236 ? 132.789 202.653 210.061 1.00 17.04 ? 4236 ASP A C     1 
ATOM   20546 O  O     . ASP A 1 4236 ? 133.115 202.370 208.904 1.00 20.02 ? 4236 ASP A O     1 
ATOM   20547 C  CB    . ASP A 1 4236 ? 130.981 200.986 210.567 1.00 13.64 ? 4236 ASP A CB    1 
ATOM   20548 C  CG    . ASP A 1 4236 ? 129.873 202.024 210.630 1.00 27.84 ? 4236 ASP A CG    1 
ATOM   20549 O  OD1   . ASP A 1 4236 ? 130.136 203.171 211.046 1.00 27.28 ? 4236 ASP A OD1   1 
ATOM   20550 O  OD2   . ASP A 1 4236 ? 128.726 201.684 210.272 1.00 31.45 ? 4236 ASP A OD2   1 
ATOM   20551 N  N     . LYS A 1 4237 ? 132.807 203.900 210.526 1.00 15.00 ? 4237 LYS A N     1 
ATOM   20552 C  CA    . LYS A 1 4237 ? 133.331 205.017 209.755 1.00 10.82 ? 4237 LYS A CA    1 
ATOM   20553 C  C     . LYS A 1 4237 ? 134.812 205.260 210.011 1.00 10.05 ? 4237 LYS A C     1 
ATOM   20554 O  O     . LYS A 1 4237 ? 135.407 206.121 209.355 1.00 13.68 ? 4237 LYS A O     1 
ATOM   20555 C  CB    . LYS A 1 4237 ? 132.539 206.293 210.062 1.00 12.41 ? 4237 LYS A CB    1 
ATOM   20556 C  CG    . LYS A 1 4237 ? 131.043 206.235 209.739 1.00 15.94 ? 4237 LYS A CG    1 
ATOM   20557 C  CD    . LYS A 1 4237 ? 130.744 206.221 208.242 1.00 16.29 ? 4237 LYS A CD    1 
ATOM   20558 C  CE    . LYS A 1 4237 ? 130.590 204.810 207.687 1.00 23.00 ? 4237 LYS A CE    1 
ATOM   20559 N  NZ    . LYS A 1 4237 ? 130.193 204.824 206.252 1.00 24.00 ? 4237 LYS A NZ    1 
ATOM   20560 N  N     . ILE A 1 4238 ? 135.411 204.535 210.945 1.00 12.61 ? 4238 ILE A N     1 
ATOM   20561 C  CA    . ILE A 1 4238 ? 136.858 204.619 211.163 1.00 10.06 ? 4238 ILE A CA    1 
ATOM   20562 C  C     . ILE A 1 4238 ? 137.577 204.097 209.923 1.00 11.49 ? 4238 ILE A C     1 
ATOM   20563 O  O     . ILE A 1 4238 ? 137.206 203.034 209.397 1.00 10.77 ? 4238 ILE A O     1 
ATOM   20564 C  CB    . ILE A 1 4238 ? 137.253 203.821 212.410 1.00 8.66  ? 4238 ILE A CB    1 
ATOM   20565 C  CG1   . ILE A 1 4238 ? 136.560 204.400 213.648 1.00 11.11 ? 4238 ILE A CG1   1 
ATOM   20566 C  CG2   . ILE A 1 4238 ? 138.762 203.800 212.589 1.00 5.79  ? 4238 ILE A CG2   1 
ATOM   20567 C  CD1   . ILE A 1 4238 ? 136.827 203.632 214.918 1.00 12.26 ? 4238 ILE A CD1   1 
ATOM   20568 N  N     . PRO A 1 4239 ? 138.587 204.800 209.411 1.00 11.30 ? 4239 PRO A N     1 
ATOM   20569 C  CA    . PRO A 1 4239 ? 139.266 204.332 208.196 1.00 7.09  ? 4239 PRO A CA    1 
ATOM   20570 C  C     . PRO A 1 4239 ? 140.142 203.114 208.443 1.00 6.69  ? 4239 PRO A C     1 
ATOM   20571 O  O     . PRO A 1 4239 ? 141.372 203.220 208.489 1.00 3.53  ? 4239 PRO A O     1 
ATOM   20572 C  CB    . PRO A 1 4239 ? 140.093 205.552 207.776 1.00 6.89  ? 4239 PRO A CB    1 
ATOM   20573 C  CG    . PRO A 1 4239 ? 140.368 206.258 209.054 1.00 5.51  ? 4239 PRO A CG    1 
ATOM   20574 C  CD    . PRO A 1 4239 ? 139.123 206.088 209.881 1.00 5.97  ? 4239 PRO A CD    1 
ATOM   20575 N  N     . TRP A 1 4240 ? 139.509 201.950 208.598 1.00 5.50  ? 4240 TRP A N     1 
ATOM   20576 C  CA    . TRP A 1 4240 ? 140.256 200.721 208.849 1.00 3.42  ? 4240 TRP A CA    1 
ATOM   20577 C  C     . TRP A 1 4240 ? 141.141 200.360 207.666 1.00 2.89  ? 4240 TRP A C     1 
ATOM   20578 O  O     . TRP A 1 4240 ? 142.270 199.887 207.847 1.00 2.41  ? 4240 TRP A O     1 
ATOM   20579 C  CB    . TRP A 1 4240 ? 139.293 199.579 209.167 1.00 3.85  ? 4240 TRP A CB    1 
ATOM   20580 C  CG    . TRP A 1 4240 ? 138.454 199.832 210.367 1.00 3.31  ? 4240 TRP A CG    1 
ATOM   20581 C  CD1   . TRP A 1 4240 ? 137.108 200.041 210.396 1.00 3.98  ? 4240 TRP A CD1   1 
ATOM   20582 C  CD2   . TRP A 1 4240 ? 138.902 199.912 211.724 1.00 5.26  ? 4240 TRP A CD2   1 
ATOM   20583 N  NE1   . TRP A 1 4240 ? 136.689 200.247 211.684 1.00 8.58  ? 4240 TRP A NE1   1 
ATOM   20584 C  CE2   . TRP A 1 4240 ? 137.772 200.171 212.520 1.00 5.69  ? 4240 TRP A CE2   1 
ATOM   20585 C  CE3   . TRP A 1 4240 ? 140.148 199.789 212.341 1.00 3.78  ? 4240 TRP A CE3   1 
ATOM   20586 C  CZ2   . TRP A 1 4240 ? 137.851 200.313 213.900 1.00 5.99  ? 4240 TRP A CZ2   1 
ATOM   20587 C  CZ3   . TRP A 1 4240 ? 140.224 199.927 213.711 1.00 3.59  ? 4240 TRP A CZ3   1 
ATOM   20588 C  CH2   . TRP A 1 4240 ? 139.082 200.182 214.476 1.00 4.60  ? 4240 TRP A CH2   1 
ATOM   20589 N  N     . SER A 1 4241 ? 140.641 200.566 206.447 1.00 5.85  ? 4241 SER A N     1 
ATOM   20590 C  CA    . SER A 1 4241 ? 141.431 200.258 205.261 1.00 3.20  ? 4241 SER A CA    1 
ATOM   20591 C  C     . SER A 1 4241 ? 142.687 201.116 205.195 1.00 2.01  ? 4241 SER A C     1 
ATOM   20592 O  O     . SER A 1 4241 ? 143.766 200.621 204.854 1.00 1.91  ? 4241 SER A O     1 
ATOM   20593 C  CB    . SER A 1 4241 ? 140.580 200.447 204.005 1.00 3.76  ? 4241 SER A CB    1 
ATOM   20594 O  OG    . SER A 1 4241 ? 141.332 200.187 202.836 1.00 14.94 ? 4241 SER A OG    1 
ATOM   20595 N  N     . ALA A 1 4242 ? 142.567 202.404 205.517 1.00 2.34  ? 4242 ALA A N     1 
ATOM   20596 C  CA    . ALA A 1 4242 ? 143.732 203.281 205.505 1.00 1.30  ? 4242 ALA A CA    1 
ATOM   20597 C  C     . ALA A 1 4242 ? 144.752 202.863 206.558 1.00 3.55  ? 4242 ALA A C     1 
ATOM   20598 O  O     . ALA A 1 4242 ? 145.955 202.810 206.279 1.00 4.22  ? 4242 ALA A O     1 
ATOM   20599 C  CB    . ALA A 1 4242 ? 143.302 204.730 205.728 1.00 1.38  ? 4242 ALA A CB    1 
ATOM   20600 N  N     . LEU A 1 4243 ? 144.289 202.564 207.776 1.00 2.08  ? 4243 LEU A N     1 
ATOM   20601 C  CA    . LEU A 1 4243 ? 145.212 202.205 208.849 1.00 1.06  ? 4243 LEU A CA    1 
ATOM   20602 C  C     . LEU A 1 4243 ? 145.903 200.879 208.569 1.00 1.32  ? 4243 LEU A C     1 
ATOM   20603 O  O     . LEU A 1 4243 ? 147.120 200.759 208.749 1.00 3.83  ? 4243 LEU A O     1 
ATOM   20604 C  CB    . LEU A 1 4243 ? 144.472 202.150 210.185 1.00 2.70  ? 4243 LEU A CB    1 
ATOM   20605 C  CG    . LEU A 1 4243 ? 143.797 203.435 210.662 1.00 3.18  ? 4243 LEU A CG    1 
ATOM   20606 C  CD1   . LEU A 1 4243 ? 143.131 203.216 212.010 1.00 1.69  ? 4243 LEU A CD1   1 
ATOM   20607 C  CD2   . LEU A 1 4243 ? 144.789 204.589 210.724 1.00 1.48  ? 4243 LEU A CD2   1 
ATOM   20608 N  N     . LYS A 1 4244 ? 145.146 199.872 208.129 1.00 1.50  ? 4244 LYS A N     1 
ATOM   20609 C  CA    . LYS A 1 4244 ? 145.724 198.550 207.913 1.00 0.98  ? 4244 LYS A CA    1 
ATOM   20610 C  C     . LYS A 1 4244 ? 146.730 198.565 206.771 1.00 0.66  ? 4244 LYS A C     1 
ATOM   20611 O  O     . LYS A 1 4244 ? 147.835 198.028 206.900 1.00 1.01  ? 4244 LYS A O     1 
ATOM   20612 C  CB    . LYS A 1 4244 ? 144.618 197.530 207.642 1.00 1.77  ? 4244 LYS A CB    1 
ATOM   20613 C  CG    . LYS A 1 4244 ? 143.930 197.016 208.891 1.00 2.47  ? 4244 LYS A CG    1 
ATOM   20614 C  CD    . LYS A 1 4244 ? 142.893 195.959 208.551 1.00 3.57  ? 4244 LYS A CD    1 
ATOM   20615 C  CE    . LYS A 1 4244 ? 141.845 196.506 207.599 1.00 6.04  ? 4244 LYS A CE    1 
ATOM   20616 N  NZ    . LYS A 1 4244 ? 140.741 195.538 207.385 1.00 10.30 ? 4244 LYS A NZ    1 
ATOM   20617 N  N     . THR A 1 4245 ? 146.365 199.180 205.643 1.00 0.88  ? 4245 THR A N     1 
ATOM   20618 C  CA    . THR A 1 4245 ? 147.249 199.189 204.483 1.00 0.65  ? 4245 THR A CA    1 
ATOM   20619 C  C     . THR A 1 4245 ? 148.549 199.925 204.778 1.00 0.46  ? 4245 THR A C     1 
ATOM   20620 O  O     . THR A 1 4245 ? 149.633 199.455 204.414 1.00 0.45  ? 4245 THR A O     1 
ATOM   20621 C  CB    . THR A 1 4245 ? 146.543 199.826 203.289 1.00 0.92  ? 4245 THR A CB    1 
ATOM   20622 O  OG1   . THR A 1 4245 ? 145.244 199.240 203.127 1.00 3.46  ? 4245 THR A OG1   1 
ATOM   20623 C  CG2   . THR A 1 4245 ? 147.354 199.631 202.018 1.00 0.40  ? 4245 THR A CG2   1 
ATOM   20624 N  N     . LEU A 1 4246 ? 148.463 201.082 205.437 1.00 0.57  ? 4246 LEU A N     1 
ATOM   20625 C  CA    . LEU A 1 4246 ? 149.667 201.845 205.739 1.00 0.48  ? 4246 LEU A CA    1 
ATOM   20626 C  C     . LEU A 1 4246 ? 150.578 201.078 206.686 1.00 0.53  ? 4246 LEU A C     1 
ATOM   20627 O  O     . LEU A 1 4246 ? 151.805 201.115 206.545 1.00 0.73  ? 4246 LEU A O     1 
ATOM   20628 C  CB    . LEU A 1 4246 ? 149.292 203.210 206.317 1.00 0.58  ? 4246 LEU A CB    1 
ATOM   20629 C  CG    . LEU A 1 4246 ? 148.934 204.231 205.235 1.00 0.50  ? 4246 LEU A CG    1 
ATOM   20630 C  CD1   . LEU A 1 4246 ? 148.552 205.565 205.832 1.00 0.69  ? 4246 LEU A CD1   1 
ATOM   20631 C  CD2   . LEU A 1 4246 ? 150.087 204.395 204.254 1.00 0.16  ? 4246 LEU A CD2   1 
ATOM   20632 N  N     . MET A 1 4247 ? 149.997 200.370 207.653 1.00 0.99  ? 4247 MET A N     1 
ATOM   20633 C  CA    . MET A 1 4247 ? 150.792 199.498 208.506 1.00 0.80  ? 4247 MET A CA    1 
ATOM   20634 C  C     . MET A 1 4247 ? 151.207 198.217 207.788 1.00 0.82  ? 4247 MET A C     1 
ATOM   20635 O  O     . MET A 1 4247 ? 152.244 197.634 208.115 1.00 2.88  ? 4247 MET A O     1 
ATOM   20636 C  CB    . MET A 1 4247 ? 150.023 199.168 209.784 1.00 1.12  ? 4247 MET A CB    1 
ATOM   20637 C  CG    . MET A 1 4247 ? 150.099 200.258 210.838 1.00 1.46  ? 4247 MET A CG    1 
ATOM   20638 S  SD    . MET A 1 4247 ? 149.380 199.776 212.414 1.00 23.95 ? 4247 MET A SD    1 
ATOM   20639 C  CE    . MET A 1 4247 ? 147.662 200.189 212.131 1.00 3.57  ? 4247 MET A CE    1 
ATOM   20640 N  N     . ALA A 1 4248 ? 150.426 197.754 206.816 1.00 0.47  ? 4248 ALA A N     1 
ATOM   20641 C  CA    . ALA A 1 4248 ? 150.831 196.562 206.084 1.00 0.47  ? 4248 ALA A CA    1 
ATOM   20642 C  C     . ALA A 1 4248 ? 152.017 196.850 205.173 1.00 0.68  ? 4248 ALA A C     1 
ATOM   20643 O  O     . ALA A 1 4248 ? 152.905 196.004 205.016 1.00 1.54  ? 4248 ALA A O     1 
ATOM   20644 C  CB    . ALA A 1 4248 ? 149.657 196.009 205.281 1.00 2.47  ? 4248 ALA A CB    1 
ATOM   20645 N  N     . GLN A 1 4249 ? 152.057 198.037 204.576 1.00 0.50  ? 4249 GLN A N     1 
ATOM   20646 C  CA    . GLN A 1 4249 ? 153.028 198.362 203.539 1.00 0.72  ? 4249 GLN A CA    1 
ATOM   20647 C  C     . GLN A 1 4249 ? 154.168 199.249 204.009 1.00 1.00  ? 4249 GLN A C     1 
ATOM   20648 O  O     . GLN A 1 4249 ? 155.294 199.091 203.536 1.00 1.48  ? 4249 GLN A O     1 
ATOM   20649 C  CB    . GLN A 1 4249 ? 152.322 199.041 202.359 1.00 1.02  ? 4249 GLN A CB    1 
ATOM   20650 C  CG    . GLN A 1 4249 ? 151.221 198.200 201.735 1.00 0.83  ? 4249 GLN A CG    1 
ATOM   20651 C  CD    . GLN A 1 4249 ? 151.709 196.828 201.314 1.00 2.79  ? 4249 GLN A CD    1 
ATOM   20652 O  OE1   . GLN A 1 4249 ? 152.502 196.699 200.382 1.00 6.22  ? 4249 GLN A OE1   1 
ATOM   20653 N  NE2   . GLN A 1 4249 ? 151.247 195.798 202.011 1.00 2.19  ? 4249 GLN A NE2   1 
ATOM   20654 N  N     . SER A 1 4250 ? 153.914 200.181 204.929 1.00 1.57  ? 4250 SER A N     1 
ATOM   20655 C  CA    . SER A 1 4250 ? 154.887 201.210 205.271 1.00 1.32  ? 4250 SER A CA    1 
ATOM   20656 C  C     . SER A 1 4250 ? 155.351 201.128 206.720 1.00 2.16  ? 4250 SER A C     1 
ATOM   20657 O  O     . SER A 1 4250 ? 156.556 201.142 206.980 1.00 7.82  ? 4250 SER A O     1 
ATOM   20658 C  CB    . SER A 1 4250 ? 154.292 202.592 204.975 1.00 1.12  ? 4250 SER A CB    1 
ATOM   20659 O  OG    . SER A 1 4250 ? 153.848 202.668 203.633 1.00 1.03  ? 4250 SER A OG    1 
ATOM   20660 N  N     . ILE A 1 4251 ? 154.430 201.046 207.674 1.00 2.10  ? 4251 ILE A N     1 
ATOM   20661 C  CA    . ILE A 1 4251 ? 154.756 201.047 209.095 1.00 1.49  ? 4251 ILE A CA    1 
ATOM   20662 C  C     . ILE A 1 4251 ? 154.702 199.610 209.590 1.00 7.46  ? 4251 ILE A C     1 
ATOM   20663 O  O     . ILE A 1 4251 ? 153.622 199.019 209.641 1.00 17.96 ? 4251 ILE A O     1 
ATOM   20664 C  CB    . ILE A 1 4251 ? 153.775 201.920 209.888 1.00 2.01  ? 4251 ILE A CB    1 
ATOM   20665 C  CG1   . ILE A 1 4251 ? 153.838 203.366 209.421 1.00 1.74  ? 4251 ILE A CG1   1 
ATOM   20666 C  CG2   . ILE A 1 4251 ? 154.099 201.862 211.364 1.00 3.14  ? 4251 ILE A CG2   1 
ATOM   20667 C  CD1   . ILE A 1 4251 ? 152.723 204.192 209.969 1.00 0.97  ? 4251 ILE A CD1   1 
ATOM   20668 N  N     . TYR A 1 4252 ? 155.854 199.070 209.994 1.00 2.51  ? 4252 TYR A N     1 
ATOM   20669 C  CA    . TYR A 1 4252 ? 156.061 197.658 210.333 1.00 1.93  ? 4252 TYR A CA    1 
ATOM   20670 C  C     . TYR A 1 4252 ? 156.121 196.792 209.080 1.00 2.47  ? 4252 TYR A C     1 
ATOM   20671 O  O     . TYR A 1 4252 ? 156.488 195.616 209.156 1.00 8.60  ? 4252 TYR A O     1 
ATOM   20672 C  CB    . TYR A 1 4252 ? 154.966 197.090 211.249 1.00 0.57  ? 4252 TYR A CB    1 
ATOM   20673 C  CG    . TYR A 1 4252 ? 154.726 197.803 212.558 1.00 0.79  ? 4252 TYR A CG    1 
ATOM   20674 C  CD1   . TYR A 1 4252 ? 155.508 197.535 213.673 1.00 0.45  ? 4252 TYR A CD1   1 
ATOM   20675 C  CD2   . TYR A 1 4252 ? 153.677 198.703 212.695 1.00 0.98  ? 4252 TYR A CD2   1 
ATOM   20676 C  CE1   . TYR A 1 4252 ? 155.274 198.169 214.873 1.00 0.60  ? 4252 TYR A CE1   1 
ATOM   20677 C  CE2   . TYR A 1 4252 ? 153.438 199.343 213.890 1.00 0.87  ? 4252 TYR A CE2   1 
ATOM   20678 C  CZ    . TYR A 1 4252 ? 154.239 199.072 214.976 1.00 0.46  ? 4252 TYR A CZ    1 
ATOM   20679 O  OH    . TYR A 1 4252 ? 154.003 199.708 216.170 1.00 0.46  ? 4252 TYR A OH    1 
ATOM   20680 N  N     . GLY A 1 4253 ? 155.791 197.360 207.927 1.00 5.57  ? 4253 GLY A N     1 
ATOM   20681 C  CA    . GLY A 1 4253 ? 155.762 196.592 206.700 1.00 0.87  ? 4253 GLY A CA    1 
ATOM   20682 C  C     . GLY A 1 4253 ? 157.013 196.790 205.876 1.00 1.01  ? 4253 GLY A C     1 
ATOM   20683 O  O     . GLY A 1 4253 ? 157.443 195.886 205.155 1.00 3.47  ? 4253 GLY A O     1 
ATOM   20684 N  N     . GLY A 1 4254 ? 157.615 197.975 205.993 1.00 1.11  ? 4254 GLY A N     1 
ATOM   20685 C  CA    . GLY A 1 4254 ? 158.824 198.276 205.253 1.00 0.61  ? 4254 GLY A CA    1 
ATOM   20686 C  C     . GLY A 1 4254 ? 160.013 197.424 205.639 1.00 1.08  ? 4254 GLY A C     1 
ATOM   20687 O  O     . GLY A 1 4254 ? 160.923 197.243 204.825 1.00 5.76  ? 4254 GLY A O     1 
ATOM   20688 N  N     . ARG A 1 4255 ? 160.026 196.896 206.862 1.00 1.59  ? 4255 ARG A N     1 
ATOM   20689 C  CA    . ARG A 1 4255 ? 161.128 196.058 207.307 1.00 2.00  ? 4255 ARG A CA    1 
ATOM   20690 C  C     . ARG A 1 4255 ? 161.041 194.635 206.775 1.00 1.54  ? 4255 ARG A C     1 
ATOM   20691 O  O     . ARG A 1 4255 ? 162.057 193.934 206.759 1.00 3.77  ? 4255 ARG A O     1 
ATOM   20692 C  CB    . ARG A 1 4255 ? 161.172 196.026 208.834 1.00 1.47  ? 4255 ARG A CB    1 
ATOM   20693 C  CG    . ARG A 1 4255 ? 161.076 197.394 209.466 1.00 3.06  ? 4255 ARG A CG    1 
ATOM   20694 C  CD    . ARG A 1 4255 ? 161.042 197.307 210.979 1.00 3.56  ? 4255 ARG A CD    1 
ATOM   20695 N  NE    . ARG A 1 4255 ? 161.189 198.617 211.600 1.00 2.44  ? 4255 ARG A NE    1 
ATOM   20696 C  CZ    . ARG A 1 4255 ? 162.301 199.340 211.581 1.00 2.40  ? 4255 ARG A CZ    1 
ATOM   20697 N  NH1   . ARG A 1 4255 ? 163.403 198.899 210.995 1.00 2.20  ? 4255 ARG A NH1   1 
ATOM   20698 N  NH2   . ARG A 1 4255 ? 162.310 200.529 212.173 1.00 2.48  ? 4255 ARG A NH2   1 
ATOM   20699 N  N     . VAL A 1 4256 ? 159.868 194.202 206.333 1.00 1.08  ? 4256 VAL A N     1 
ATOM   20700 C  CA    . VAL A 1 4256 ? 159.646 192.801 205.994 1.00 1.68  ? 4256 VAL A CA    1 
ATOM   20701 C  C     . VAL A 1 4256 ? 160.135 192.533 204.578 1.00 1.54  ? 4256 VAL A C     1 
ATOM   20702 O  O     . VAL A 1 4256 ? 159.723 193.205 203.625 1.00 3.01  ? 4256 VAL A O     1 
ATOM   20703 C  CB    . VAL A 1 4256 ? 158.162 192.435 206.151 1.00 1.93  ? 4256 VAL A CB    1 
ATOM   20704 C  CG1   . VAL A 1 4256 ? 157.946 190.963 205.862 1.00 1.31  ? 4256 VAL A CG1   1 
ATOM   20705 C  CG2   . VAL A 1 4256 ? 157.681 192.784 207.550 1.00 0.90  ? 4256 VAL A CG2   1 
ATOM   20706 N  N     . ASP A 1 4257 ? 161.015 191.543 204.438 1.00 1.84  ? 4257 ASP A N     1 
ATOM   20707 C  CA    . ASP A 1 4257 ? 161.546 191.123 203.147 1.00 4.26  ? 4257 ASP A CA    1 
ATOM   20708 C  C     . ASP A 1 4257 ? 161.179 189.672 202.849 1.00 4.09  ? 4257 ASP A C     1 
ATOM   20709 O  O     . ASP A 1 4257 ? 161.851 188.999 202.065 1.00 4.64  ? 4257 ASP A O     1 
ATOM   20710 C  CB    . ASP A 1 4257 ? 163.060 191.316 203.098 1.00 4.50  ? 4257 ASP A CB    1 
ATOM   20711 C  CG    . ASP A 1 4257 ? 163.766 190.731 204.306 1.00 8.46  ? 4257 ASP A CG    1 
ATOM   20712 O  OD1   . ASP A 1 4257 ? 163.086 190.150 205.176 1.00 9.36  ? 4257 ASP A OD1   1 
ATOM   20713 O  OD2   . ASP A 1 4257 ? 165.005 190.852 204.387 1.00 20.93 ? 4257 ASP A OD2   1 
ATOM   20714 N  N     . ASN A 1 4258 ? 160.112 189.183 203.475 1.00 3.34  ? 4258 ASN A N     1 
ATOM   20715 C  CA    . ASN A 1 4258 ? 159.692 187.793 203.373 1.00 3.59  ? 4258 ASN A CA    1 
ATOM   20716 C  C     . ASN A 1 4258 ? 158.181 187.774 203.209 1.00 2.72  ? 4258 ASN A C     1 
ATOM   20717 O  O     . ASN A 1 4258 ? 157.469 188.427 203.976 1.00 5.09  ? 4258 ASN A O     1 
ATOM   20718 C  CB    . ASN A 1 4258 ? 160.137 187.010 204.621 1.00 2.64  ? 4258 ASN A CB    1 
ATOM   20719 C  CG    . ASN A 1 4258 ? 159.639 185.577 204.639 1.00 5.22  ? 4258 ASN A CG    1 
ATOM   20720 O  OD1   . ASN A 1 4258 ? 158.439 185.320 204.679 1.00 10.75 ? 4258 ASN A OD1   1 
ATOM   20721 N  ND2   . ASN A 1 4258 ? 160.570 184.633 204.634 1.00 4.76  ? 4258 ASN A ND2   1 
ATOM   20722 N  N     . GLU A 1 4259 ? 157.692 187.032 202.213 1.00 3.36  ? 4259 GLU A N     1 
ATOM   20723 C  CA    . GLU A 1 4259 ? 156.259 187.047 201.931 1.00 3.59  ? 4259 GLU A CA    1 
ATOM   20724 C  C     . GLU A 1 4259 ? 155.462 186.369 203.039 1.00 1.79  ? 4259 GLU A C     1 
ATOM   20725 O  O     . GLU A 1 4259 ? 154.322 186.756 203.318 1.00 1.51  ? 4259 GLU A O     1 
ATOM   20726 C  CB    . GLU A 1 4259 ? 155.974 186.387 200.580 1.00 3.35  ? 4259 GLU A CB    1 
ATOM   20727 C  CG    . GLU A 1 4259 ? 156.292 184.903 200.519 1.00 6.60  ? 4259 GLU A CG    1 
ATOM   20728 C  CD    . GLU A 1 4259 ? 156.052 184.308 199.145 1.00 19.69 ? 4259 GLU A CD    1 
ATOM   20729 O  OE1   . GLU A 1 4259 ? 155.657 185.062 198.230 1.00 25.07 ? 4259 GLU A OE1   1 
ATOM   20730 O  OE2   . GLU A 1 4259 ? 156.259 183.088 198.981 1.00 21.82 ? 4259 GLU A OE2   1 
ATOM   20731 N  N     . PHE A 1 4260 ? 156.040 185.352 203.678 1.00 2.56  ? 4260 PHE A N     1 
ATOM   20732 C  CA    . PHE A 1 4260 ? 155.325 184.646 204.735 1.00 3.59  ? 4260 PHE A CA    1 
ATOM   20733 C  C     . PHE A 1 4260 ? 155.299 185.464 206.019 1.00 2.25  ? 4260 PHE A C     1 
ATOM   20734 O  O     . PHE A 1 4260 ? 154.331 185.400 206.785 1.00 1.53  ? 4260 PHE A O     1 
ATOM   20735 C  CB    . PHE A 1 4260 ? 155.965 183.278 204.958 1.00 3.82  ? 4260 PHE A CB    1 
ATOM   20736 C  CG    . PHE A 1 4260 ? 155.953 182.416 203.734 1.00 6.01  ? 4260 PHE A CG    1 
ATOM   20737 C  CD1   . PHE A 1 4260 ? 154.840 181.666 203.413 1.00 6.15  ? 4260 PHE A CD1   1 
ATOM   20738 C  CD2   . PHE A 1 4260 ? 157.043 182.388 202.884 1.00 4.02  ? 4260 PHE A CD2   1 
ATOM   20739 C  CE1   . PHE A 1 4260 ? 154.820 180.888 202.282 1.00 6.71  ? 4260 PHE A CE1   1 
ATOM   20740 C  CE2   . PHE A 1 4260 ? 157.027 181.614 201.751 1.00 4.16  ? 4260 PHE A CE2   1 
ATOM   20741 C  CZ    . PHE A 1 4260 ? 155.914 180.860 201.450 1.00 5.40  ? 4260 PHE A CZ    1 
ATOM   20742 N  N     . ASP A 1 4261 ? 156.355 186.240 206.267 1.00 1.93  ? 4261 ASP A N     1 
ATOM   20743 C  CA    . ASP A 1 4261 ? 156.317 187.210 207.353 1.00 1.47  ? 4261 ASP A CA    1 
ATOM   20744 C  C     . ASP A 1 4261 ? 155.363 188.352 207.028 1.00 1.28  ? 4261 ASP A C     1 
ATOM   20745 O  O     . ASP A 1 4261 ? 154.715 188.901 207.927 1.00 1.57  ? 4261 ASP A O     1 
ATOM   20746 C  CB    . ASP A 1 4261 ? 157.723 187.731 207.633 1.00 1.86  ? 4261 ASP A CB    1 
ATOM   20747 C  CG    . ASP A 1 4261 ? 158.557 186.753 208.433 1.00 2.59  ? 4261 ASP A CG    1 
ATOM   20748 O  OD1   . ASP A 1 4261 ? 158.026 185.692 208.822 1.00 2.64  ? 4261 ASP A OD1   1 
ATOM   20749 O  OD2   . ASP A 1 4261 ? 159.750 187.030 208.659 1.00 3.18  ? 4261 ASP A OD2   1 
ATOM   20750 N  N     . GLN A 1 4262 ? 155.270 188.729 205.751 1.00 1.27  ? 4262 GLN A N     1 
ATOM   20751 C  CA    . GLN A 1 4262 ? 154.296 189.733 205.336 1.00 0.94  ? 4262 GLN A CA    1 
ATOM   20752 C  C     . GLN A 1 4262 ? 152.871 189.234 205.527 1.00 1.14  ? 4262 GLN A C     1 
ATOM   20753 O  O     . GLN A 1 4262 ? 151.995 189.991 205.963 1.00 1.82  ? 4262 GLN A O     1 
ATOM   20754 C  CB    . GLN A 1 4262 ? 154.538 190.129 203.879 1.00 1.21  ? 4262 GLN A CB    1 
ATOM   20755 C  CG    . GLN A 1 4262 ? 153.634 191.240 203.364 1.00 1.05  ? 4262 GLN A CG    1 
ATOM   20756 C  CD    . GLN A 1 4262 ? 153.847 192.556 204.086 1.00 2.28  ? 4262 GLN A CD    1 
ATOM   20757 O  OE1   . GLN A 1 4262 ? 154.957 193.083 204.127 1.00 3.18  ? 4262 GLN A OE1   1 
ATOM   20758 N  NE2   . GLN A 1 4262 ? 152.776 193.101 204.649 1.00 1.09  ? 4262 GLN A NE2   1 
ATOM   20759 N  N     . ARG A 1 4263 ? 152.615 187.966 205.196 1.00 1.32  ? 4263 ARG A N     1 
ATOM   20760 C  CA    . ARG A 1 4263 ? 151.286 187.400 205.398 1.00 1.29  ? 4263 ARG A CA    1 
ATOM   20761 C  C     . ARG A 1 4263 ? 150.928 187.369 206.876 1.00 2.37  ? 4263 ARG A C     1 
ATOM   20762 O  O     . ARG A 1 4263 ? 149.783 187.640 207.255 1.00 3.21  ? 4263 ARG A O     1 
ATOM   20763 C  CB    . ARG A 1 4263 ? 151.217 185.996 204.802 1.00 3.58  ? 4263 ARG A CB    1 
ATOM   20764 C  CG    . ARG A 1 4263 ? 149.982 185.210 205.200 1.00 4.91  ? 4263 ARG A CG    1 
ATOM   20765 C  CD    . ARG A 1 4263 ? 149.991 183.830 204.583 1.00 7.17  ? 4263 ARG A CD    1 
ATOM   20766 N  NE    . ARG A 1 4263 ? 151.115 183.029 205.051 1.00 6.61  ? 4263 ARG A NE    1 
ATOM   20767 C  CZ    . ARG A 1 4263 ? 151.394 181.809 204.619 1.00 10.34 ? 4263 ARG A CZ    1 
ATOM   20768 N  NH1   . ARG A 1 4263 ? 150.714 181.254 203.628 1.00 7.83  ? 4263 ARG A NH1   1 
ATOM   20769 N  NH2   . ARG A 1 4263 ? 152.376 181.124 205.196 1.00 9.08  ? 4263 ARG A NH2   1 
ATOM   20770 N  N     . LEU A 1 4264 ? 151.898 187.028 207.725 1.00 1.23  ? 4264 LEU A N     1 
ATOM   20771 C  CA    . LEU A 1 4264 ? 151.673 187.029 209.165 1.00 0.91  ? 4264 LEU A CA    1 
ATOM   20772 C  C     . LEU A 1 4264 ? 151.340 188.429 209.664 1.00 1.35  ? 4264 LEU A C     1 
ATOM   20773 O  O     . LEU A 1 4264 ? 150.434 188.610 210.485 1.00 1.30  ? 4264 LEU A O     1 
ATOM   20774 C  CB    . LEU A 1 4264 ? 152.905 186.476 209.878 1.00 2.38  ? 4264 LEU A CB    1 
ATOM   20775 C  CG    . LEU A 1 4264 ? 152.804 186.352 211.394 1.00 1.31  ? 4264 LEU A CG    1 
ATOM   20776 C  CD1   . LEU A 1 4264 ? 151.682 185.409 211.750 1.00 0.90  ? 4264 LEU A CD1   1 
ATOM   20777 C  CD2   . LEU A 1 4264 ? 154.120 185.869 211.964 1.00 0.88  ? 4264 LEU A CD2   1 
ATOM   20778 N  N     . LEU A 1 4265 ? 152.063 189.435 209.169 1.00 1.92  ? 4265 LEU A N     1 
ATOM   20779 C  CA    . LEU A 1 4265 ? 151.764 190.817 209.530 1.00 0.73  ? 4265 LEU A CA    1 
ATOM   20780 C  C     . LEU A 1 4265 ? 150.366 191.214 209.068 1.00 1.00  ? 4265 LEU A C     1 
ATOM   20781 O  O     . LEU A 1 4265 ? 149.638 191.900 209.794 1.00 0.96  ? 4265 LEU A O     1 
ATOM   20782 C  CB    . LEU A 1 4265 ? 152.816 191.747 208.931 1.00 0.43  ? 4265 LEU A CB    1 
ATOM   20783 C  CG    . LEU A 1 4265 ? 152.628 193.248 209.144 1.00 0.71  ? 4265 LEU A CG    1 
ATOM   20784 C  CD1   . LEU A 1 4265 ? 152.718 193.589 210.620 1.00 1.08  ? 4265 LEU A CD1   1 
ATOM   20785 C  CD2   . LEU A 1 4265 ? 153.653 194.030 208.345 1.00 0.56  ? 4265 LEU A CD2   1 
ATOM   20786 N  N     . ASN A 1 4266 ? 149.976 190.791 207.863 1.00 0.89  ? 4266 ASN A N     1 
ATOM   20787 C  CA    . ASN A 1 4266 ? 148.634 191.083 207.371 1.00 1.56  ? 4266 ASN A CA    1 
ATOM   20788 C  C     . ASN A 1 4266 ? 147.570 190.397 208.216 1.00 1.54  ? 4266 ASN A C     1 
ATOM   20789 O  O     . ASN A 1 4266 ? 146.497 190.964 208.450 1.00 2.55  ? 4266 ASN A O     1 
ATOM   20790 C  CB    . ASN A 1 4266 ? 148.502 190.656 205.908 1.00 2.06  ? 4266 ASN A CB    1 
ATOM   20791 C  CG    . ASN A 1 4266 ? 149.238 191.578 204.964 1.00 2.71  ? 4266 ASN A CG    1 
ATOM   20792 O  OD1   . ASN A 1 4266 ? 149.177 192.797 205.099 1.00 8.52  ? 4266 ASN A OD1   1 
ATOM   20793 N  ND2   . ASN A 1 4266 ? 149.937 191.000 203.996 1.00 3.13  ? 4266 ASN A ND2   1 
ATOM   20794 N  N     . THR A 1 4267 ? 147.845 189.173 208.669 1.00 1.97  ? 4267 THR A N     1 
ATOM   20795 C  CA    . THR A 1 4267 ? 146.859 188.418 209.437 1.00 1.80  ? 4267 THR A CA    1 
ATOM   20796 C  C     . THR A 1 4267 ? 146.521 189.119 210.748 1.00 1.61  ? 4267 THR A C     1 
ATOM   20797 O  O     . THR A 1 4267 ? 145.346 189.239 211.114 1.00 3.93  ? 4267 THR A O     1 
ATOM   20798 C  CB    . THR A 1 4267 ? 147.378 187.002 209.694 1.00 3.07  ? 4267 THR A CB    1 
ATOM   20799 O  OG1   . THR A 1 4267 ? 147.548 186.322 208.446 1.00 5.34  ? 4267 THR A OG1   1 
ATOM   20800 C  CG2   . THR A 1 4267 ? 146.404 186.216 210.557 1.00 4.91  ? 4267 THR A CG2   1 
ATOM   20801 N  N     . PHE A 1 4268 ? 147.538 189.601 211.466 1.00 1.61  ? 4268 PHE A N     1 
ATOM   20802 C  CA    . PHE A 1 4268 ? 147.289 190.302 212.722 1.00 1.51  ? 4268 PHE A CA    1 
ATOM   20803 C  C     . PHE A 1 4268 ? 146.545 191.610 212.488 1.00 1.83  ? 4268 PHE A C     1 
ATOM   20804 O  O     . PHE A 1 4268 ? 145.600 191.939 213.213 1.00 3.49  ? 4268 PHE A O     1 
ATOM   20805 C  CB    . PHE A 1 4268 ? 148.603 190.562 213.459 1.00 1.06  ? 4268 PHE A CB    1 
ATOM   20806 C  CG    . PHE A 1 4268 ? 149.115 189.377 214.220 1.00 3.02  ? 4268 PHE A CG    1 
ATOM   20807 C  CD1   . PHE A 1 4268 ? 148.593 189.061 215.462 1.00 3.47  ? 4268 PHE A CD1   1 
ATOM   20808 C  CD2   . PHE A 1 4268 ? 150.134 188.595 213.710 1.00 4.21  ? 4268 PHE A CD2   1 
ATOM   20809 C  CE1   . PHE A 1 4268 ? 149.063 187.972 216.168 1.00 4.70  ? 4268 PHE A CE1   1 
ATOM   20810 C  CE2   . PHE A 1 4268 ? 150.611 187.508 214.416 1.00 3.03  ? 4268 PHE A CE2   1 
ATOM   20811 C  CZ    . PHE A 1 4268 ? 150.075 187.196 215.645 1.00 3.05  ? 4268 PHE A CZ    1 
ATOM   20812 N  N     . LEU A 1 4269 ? 146.963 192.373 211.475 1.00 2.01  ? 4269 LEU A N     1 
ATOM   20813 C  CA    . LEU A 1 4269 ? 146.314 193.649 211.195 1.00 1.46  ? 4269 LEU A CA    1 
ATOM   20814 C  C     . LEU A 1 4269 ? 144.859 193.451 210.797 1.00 2.08  ? 4269 LEU A C     1 
ATOM   20815 O  O     . LEU A 1 4269 ? 143.987 194.232 211.194 1.00 3.06  ? 4269 LEU A O     1 
ATOM   20816 C  CB    . LEU A 1 4269 ? 147.074 194.397 210.099 1.00 1.31  ? 4269 LEU A CB    1 
ATOM   20817 C  CG    . LEU A 1 4269 ? 148.432 194.988 210.480 1.00 0.91  ? 4269 LEU A CG    1 
ATOM   20818 C  CD1   . LEU A 1 4269 ? 149.182 195.449 209.239 1.00 0.62  ? 4269 LEU A CD1   1 
ATOM   20819 C  CD2   . LEU A 1 4269 ? 148.266 196.133 211.466 1.00 0.58  ? 4269 LEU A CD2   1 
ATOM   20820 N  N     . GLU A 1 4270 ? 144.576 192.411 210.010 1.00 1.84  ? 4270 GLU A N     1 
ATOM   20821 C  CA    . GLU A 1 4270 ? 143.200 192.159 209.601 1.00 3.87  ? 4270 GLU A CA    1 
ATOM   20822 C  C     . GLU A 1 4270 ? 142.334 191.732 210.778 1.00 5.43  ? 4270 GLU A C     1 
ATOM   20823 O  O     . GLU A 1 4270 ? 141.148 192.070 210.823 1.00 7.28  ? 4270 GLU A O     1 
ATOM   20824 C  CB    . GLU A 1 4270 ? 143.162 191.102 208.498 1.00 4.77  ? 4270 GLU A CB    1 
ATOM   20825 C  CG    . GLU A 1 4270 ? 141.787 190.914 207.876 1.00 9.24  ? 4270 GLU A CG    1 
ATOM   20826 C  CD    . GLU A 1 4270 ? 141.133 192.233 207.509 1.00 17.04 ? 4270 GLU A CD    1 
ATOM   20827 O  OE1   . GLU A 1 4270 ? 141.711 192.978 206.690 1.00 17.50 ? 4270 GLU A OE1   1 
ATOM   20828 O  OE2   . GLU A 1 4270 ? 140.046 192.527 208.045 1.00 15.46 ? 4270 GLU A OE2   1 
ATOM   20829 N  N     . ARG A 1 4271 ? 142.898 190.998 211.737 1.00 6.77  ? 4271 ARG A N     1 
ATOM   20830 C  CA    . ARG A 1 4271 ? 142.136 190.556 212.896 1.00 5.24  ? 4271 ARG A CA    1 
ATOM   20831 C  C     . ARG A 1 4271 ? 141.903 191.653 213.924 1.00 5.04  ? 4271 ARG A C     1 
ATOM   20832 O  O     . ARG A 1 4271 ? 140.846 191.663 214.562 1.00 11.26 ? 4271 ARG A O     1 
ATOM   20833 C  CB    . ARG A 1 4271 ? 142.837 189.376 213.579 1.00 4.81  ? 4271 ARG A CB    1 
ATOM   20834 C  CG    . ARG A 1 4271 ? 141.960 188.665 214.598 1.00 5.58  ? 4271 ARG A CG    1 
ATOM   20835 C  CD    . ARG A 1 4271 ? 142.460 187.267 214.924 1.00 9.38  ? 4271 ARG A CD    1 
ATOM   20836 N  NE    . ARG A 1 4271 ? 143.891 187.200 215.194 1.00 17.30 ? 4271 ARG A NE    1 
ATOM   20837 C  CZ    . ARG A 1 4271 ? 144.513 187.832 216.182 1.00 14.43 ? 4271 ARG A CZ    1 
ATOM   20838 N  NH1   . ARG A 1 4271 ? 143.852 188.572 217.056 1.00 13.48 ? 4271 ARG A NH1   1 
ATOM   20839 N  NH2   . ARG A 1 4271 ? 145.829 187.702 216.306 1.00 13.19 ? 4271 ARG A NH2   1 
ATOM   20840 N  N     . LEU A 1 4272 ? 142.851 192.575 214.097 1.00 2.39  ? 4272 LEU A N     1 
ATOM   20841 C  CA    . LEU A 1 4272 ? 142.789 193.538 215.189 1.00 3.56  ? 4272 LEU A CA    1 
ATOM   20842 C  C     . LEU A 1 4272 ? 142.174 194.878 214.811 1.00 3.76  ? 4272 LEU A C     1 
ATOM   20843 O  O     . LEU A 1 4272 ? 141.665 195.571 215.697 1.00 4.27  ? 4272 LEU A O     1 
ATOM   20844 C  CB    . LEU A 1 4272 ? 144.190 193.787 215.762 1.00 2.44  ? 4272 LEU A CB    1 
ATOM   20845 C  CG    . LEU A 1 4272 ? 144.865 192.602 216.452 1.00 3.09  ? 4272 LEU A CG    1 
ATOM   20846 C  CD1   . LEU A 1 4272 ? 146.297 192.942 216.819 1.00 1.29  ? 4272 LEU A CD1   1 
ATOM   20847 C  CD2   . LEU A 1 4272 ? 144.076 192.192 217.684 1.00 4.44  ? 4272 LEU A CD2   1 
ATOM   20848 N  N     . PHE A 1 4273 ? 142.214 195.272 213.541 1.00 5.38  ? 4273 PHE A N     1 
ATOM   20849 C  CA    . PHE A 1 4273 ? 141.741 196.593 213.131 1.00 3.45  ? 4273 PHE A CA    1 
ATOM   20850 C  C     . PHE A 1 4273 ? 140.525 196.426 212.226 1.00 4.35  ? 4273 PHE A C     1 
ATOM   20851 O  O     . PHE A 1 4273 ? 140.628 196.474 210.999 1.00 8.91  ? 4273 PHE A O     1 
ATOM   20852 C  CB    . PHE A 1 4273 ? 142.871 197.377 212.449 1.00 2.75  ? 4273 PHE A CB    1 
ATOM   20853 C  CG    . PHE A 1 4273 ? 143.990 197.751 213.379 1.00 1.51  ? 4273 PHE A CG    1 
ATOM   20854 C  CD1   . PHE A 1 4273 ? 143.941 198.931 214.106 1.00 2.88  ? 4273 PHE A CD1   1 
ATOM   20855 C  CD2   . PHE A 1 4273 ? 145.081 196.918 213.544 1.00 2.48  ? 4273 PHE A CD2   1 
ATOM   20856 C  CE1   . PHE A 1 4273 ? 144.963 199.274 214.972 1.00 1.17  ? 4273 PHE A CE1   1 
ATOM   20857 C  CE2   . PHE A 1 4273 ? 146.108 197.254 214.407 1.00 3.80  ? 4273 PHE A CE2   1 
ATOM   20858 C  CZ    . PHE A 1 4273 ? 146.048 198.435 215.121 1.00 1.03  ? 4273 PHE A CZ    1 
ATOM   20859 N  N     . THR A 1 4274 ? 139.361 196.249 212.852 1.00 4.53  ? 4274 THR A N     1 
ATOM   20860 C  CA    . THR A 1 4274 ? 138.071 196.187 212.178 1.00 3.13  ? 4274 THR A CA    1 
ATOM   20861 C  C     . THR A 1 4274 ? 137.039 196.869 213.063 1.00 7.42  ? 4274 THR A C     1 
ATOM   20862 O  O     . THR A 1 4274 ? 137.344 197.333 214.165 1.00 17.08 ? 4274 THR A O     1 
ATOM   20863 C  CB    . THR A 1 4274 ? 137.618 194.746 211.889 1.00 7.72  ? 4274 THR A CB    1 
ATOM   20864 O  OG1   . THR A 1 4274 ? 137.290 194.089 213.120 1.00 17.71 ? 4274 THR A OG1   1 
ATOM   20865 C  CG2   . THR A 1 4274 ? 138.680 193.952 211.156 1.00 7.45  ? 4274 THR A CG2   1 
ATOM   20866 N  N     . THR A 1 4275 ? 135.798 196.914 212.579 1.00 11.24 ? 4275 THR A N     1 
ATOM   20867 C  CA    . THR A 1 4275 ? 134.699 197.393 213.409 1.00 11.32 ? 4275 THR A CA    1 
ATOM   20868 C  C     . THR A 1 4275 ? 134.392 196.438 214.558 1.00 14.59 ? 4275 THR A C     1 
ATOM   20869 O  O     . THR A 1 4275 ? 133.862 196.872 215.585 1.00 18.69 ? 4275 THR A O     1 
ATOM   20870 C  CB    . THR A 1 4275 ? 133.449 197.607 212.553 1.00 12.04 ? 4275 THR A CB    1 
ATOM   20871 O  OG1   . THR A 1 4275 ? 133.817 198.239 211.322 1.00 13.10 ? 4275 THR A OG1   1 
ATOM   20872 C  CG2   . THR A 1 4275 ? 132.456 198.495 213.278 1.00 13.90 ? 4275 THR A CG2   1 
ATOM   20873 N  N     . ARG A 1 4276 ? 134.720 195.151 214.411 1.00 11.07 ? 4276 ARG A N     1 
ATOM   20874 C  CA    . ARG A 1 4276 ? 134.468 194.181 215.471 1.00 14.66 ? 4276 ARG A CA    1 
ATOM   20875 C  C     . ARG A 1 4276 ? 135.290 194.453 216.722 1.00 11.72 ? 4276 ARG A C     1 
ATOM   20876 O  O     . ARG A 1 4276 ? 134.931 193.970 217.800 1.00 12.55 ? 4276 ARG A O     1 
ATOM   20877 C  CB    . ARG A 1 4276 ? 134.746 192.764 214.967 1.00 10.88 ? 4276 ARG A CB    1 
ATOM   20878 C  CG    . ARG A 1 4276 ? 133.852 192.318 213.820 1.00 15.80 ? 4276 ARG A CG    1 
ATOM   20879 C  CD    . ARG A 1 4276 ? 132.441 191.968 214.285 1.00 18.05 ? 4276 ARG A CD    1 
ATOM   20880 N  NE    . ARG A 1 4276 ? 131.651 193.151 214.605 1.00 22.18 ? 4276 ARG A NE    1 
ATOM   20881 C  CZ    . ARG A 1 4276 ? 131.081 193.942 213.707 1.00 26.16 ? 4276 ARG A CZ    1 
ATOM   20882 N  NH1   . ARG A 1 4276 ? 131.172 193.693 212.410 1.00 22.43 ? 4276 ARG A NH1   1 
ATOM   20883 N  NH2   . ARG A 1 4276 ? 130.410 195.013 214.119 1.00 24.42 ? 4276 ARG A NH2   1 
ATOM   20884 N  N     . SER A 1 4277 ? 136.381 195.213 216.606 1.00 14.23 ? 4277 SER A N     1 
ATOM   20885 C  CA    . SER A 1 4277 ? 137.185 195.545 217.775 1.00 11.18 ? 4277 SER A CA    1 
ATOM   20886 C  C     . SER A 1 4277 ? 136.425 196.406 218.771 1.00 10.83 ? 4277 SER A C     1 
ATOM   20887 O  O     . SER A 1 4277 ? 136.795 196.444 219.949 1.00 17.47 ? 4277 SER A O     1 
ATOM   20888 C  CB    . SER A 1 4277 ? 138.468 196.254 217.345 1.00 10.92 ? 4277 SER A CB    1 
ATOM   20889 O  OG    . SER A 1 4277 ? 139.375 195.345 216.752 1.00 14.06 ? 4277 SER A OG    1 
ATOM   20890 N  N     . PHE A 1 4278 ? 135.380 197.097 218.329 1.00 10.88 ? 4278 PHE A N     1 
ATOM   20891 C  CA    . PHE A 1 4278 ? 134.559 197.924 219.199 1.00 11.00 ? 4278 PHE A CA    1 
ATOM   20892 C  C     . PHE A 1 4278 ? 133.348 197.181 219.750 1.00 16.41 ? 4278 PHE A C     1 
ATOM   20893 O  O     . PHE A 1 4278 ? 132.556 197.779 220.484 1.00 15.03 ? 4278 PHE A O     1 
ATOM   20894 C  CB    . PHE A 1 4278 ? 134.107 199.182 218.453 1.00 10.09 ? 4278 PHE A CB    1 
ATOM   20895 C  CG    . PHE A 1 4278 ? 135.153 200.255 218.395 1.00 7.94  ? 4278 PHE A CG    1 
ATOM   20896 C  CD1   . PHE A 1 4278 ? 136.284 200.097 217.613 1.00 11.65 ? 4278 PHE A CD1   1 
ATOM   20897 C  CD2   . PHE A 1 4278 ? 135.009 201.420 219.127 1.00 8.42  ? 4278 PHE A CD2   1 
ATOM   20898 C  CE1   . PHE A 1 4278 ? 137.249 201.078 217.563 1.00 7.73  ? 4278 PHE A CE1   1 
ATOM   20899 C  CE2   . PHE A 1 4278 ? 135.974 202.403 219.080 1.00 7.43  ? 4278 PHE A CE2   1 
ATOM   20900 C  CZ    . PHE A 1 4278 ? 137.094 202.232 218.296 1.00 9.65  ? 4278 PHE A CZ    1 
ATOM   20901 N  N     . ASP A 1 4279 ? 133.189 195.905 219.414 1.00 17.15 ? 4279 ASP A N     1 
ATOM   20902 C  CA    . ASP A 1 4279 ? 132.127 195.094 219.985 1.00 17.44 ? 4279 ASP A CA    1 
ATOM   20903 C  C     . ASP A 1 4279 ? 132.464 194.700 221.418 1.00 26.93 ? 4279 ASP A C     1 
ATOM   20904 O  O     . ASP A 1 4279 ? 133.626 194.698 221.837 1.00 27.20 ? 4279 ASP A O     1 
ATOM   20905 C  CB    . ASP A 1 4279 ? 131.885 193.840 219.145 1.00 16.47 ? 4279 ASP A CB    1 
ATOM   20906 C  CG    . ASP A 1 4279 ? 131.507 194.160 217.716 1.00 18.30 ? 4279 ASP A CG    1 
ATOM   20907 O  OD1   . ASP A 1 4279 ? 131.506 195.353 217.350 1.00 23.40 ? 4279 ASP A OD1   1 
ATOM   20908 O  OD2   . ASP A 1 4279 ? 131.201 193.216 216.962 1.00 19.49 ? 4279 ASP A OD2   1 
ATOM   20909 N  N     . SER A 1 4280 ? 131.416 194.364 222.175 1.00 27.58 ? 4280 SER A N     1 
ATOM   20910 C  CA    . SER A 1 4280 ? 131.593 194.019 223.581 1.00 23.00 ? 4280 SER A CA    1 
ATOM   20911 C  C     . SER A 1 4280 ? 132.407 192.741 223.750 1.00 28.81 ? 4280 SER A C     1 
ATOM   20912 O  O     . SER A 1 4280 ? 133.240 192.646 224.657 1.00 32.57 ? 4280 SER A O     1 
ATOM   20913 C  CB    . SER A 1 4280 ? 130.228 193.874 224.256 1.00 27.86 ? 4280 SER A CB    1 
ATOM   20914 O  OG    . SER A 1 4280 ? 129.463 195.057 224.120 1.00 33.83 ? 4280 SER A OG    1 
ATOM   20915 N  N     . GLU A 1 4281 ? 132.182 191.746 222.890 1.00 25.73 ? 4281 GLU A N     1 
ATOM   20916 C  CA    . GLU A 1 4281 ? 132.781 190.426 223.044 1.00 27.49 ? 4281 GLU A CA    1 
ATOM   20917 C  C     . GLU A 1 4281 ? 133.974 190.204 222.116 1.00 23.05 ? 4281 GLU A C     1 
ATOM   20918 O  O     . GLU A 1 4281 ? 134.253 189.062 221.736 1.00 18.08 ? 4281 GLU A O     1 
ATOM   20919 C  CB    . GLU A 1 4281 ? 131.731 189.339 222.817 1.00 26.68 ? 4281 GLU A CB    1 
ATOM   20920 C  CG    . GLU A 1 4281 ? 130.594 189.353 223.825 1.00 31.28 ? 4281 GLU A CG    1 
ATOM   20921 C  CD    . GLU A 1 4281 ? 131.088 189.288 225.255 1.00 38.71 ? 4281 GLU A CD    1 
ATOM   20922 O  OE1   . GLU A 1 4281 ? 131.771 188.303 225.604 1.00 37.79 ? 4281 GLU A OE1   1 
ATOM   20923 O  OE2   . GLU A 1 4281 ? 130.793 190.223 226.030 1.00 44.44 ? 4281 GLU A OE2   1 
ATOM   20924 N  N     . PHE A 1 4282 ? 134.682 191.268 221.744 1.00 18.68 ? 4282 PHE A N     1 
ATOM   20925 C  CA    . PHE A 1 4282 ? 135.866 191.113 220.909 1.00 12.00 ? 4282 PHE A CA    1 
ATOM   20926 C  C     . PHE A 1 4282 ? 136.952 190.355 221.663 1.00 14.61 ? 4282 PHE A C     1 
ATOM   20927 O  O     . PHE A 1 4282 ? 137.112 190.508 222.877 1.00 14.37 ? 4282 PHE A O     1 
ATOM   20928 C  CB    . PHE A 1 4282 ? 136.388 192.476 220.457 1.00 11.30 ? 4282 PHE A CB    1 
ATOM   20929 C  CG    . PHE A 1 4282 ? 137.538 192.392 219.498 1.00 8.40  ? 4282 PHE A CG    1 
ATOM   20930 C  CD1   . PHE A 1 4282 ? 137.409 191.707 218.302 1.00 9.92  ? 4282 PHE A CD1   1 
ATOM   20931 C  CD2   . PHE A 1 4282 ? 138.748 192.992 219.793 1.00 10.27 ? 4282 PHE A CD2   1 
ATOM   20932 C  CE1   . PHE A 1 4282 ? 138.464 191.623 217.418 1.00 10.53 ? 4282 PHE A CE1   1 
ATOM   20933 C  CE2   . PHE A 1 4282 ? 139.809 192.913 218.911 1.00 11.19 ? 4282 PHE A CE2   1 
ATOM   20934 C  CZ    . PHE A 1 4282 ? 139.665 192.227 217.723 1.00 15.93 ? 4282 PHE A CZ    1 
ATOM   20935 N  N     . LYS A 1 4283 ? 137.708 189.538 220.934 1.00 15.15 ? 4283 LYS A N     1 
ATOM   20936 C  CA    . LYS A 1 4283 ? 138.615 188.561 221.528 1.00 12.01 ? 4283 LYS A CA    1 
ATOM   20937 C  C     . LYS A 1 4283 ? 140.021 188.822 221.004 1.00 10.21 ? 4283 LYS A C     1 
ATOM   20938 O  O     . LYS A 1 4283 ? 140.328 188.495 219.853 1.00 19.43 ? 4283 LYS A O     1 
ATOM   20939 C  CB    . LYS A 1 4283 ? 138.150 187.145 221.191 1.00 16.10 ? 4283 LYS A CB    1 
ATOM   20940 C  CG    . LYS A 1 4283 ? 137.258 186.528 222.250 1.00 17.25 ? 4283 LYS A CG    1 
ATOM   20941 C  CD    . LYS A 1 4283 ? 136.824 185.126 221.871 1.00 22.21 ? 4283 LYS A CD    1 
ATOM   20942 C  CE    . LYS A 1 4283 ? 136.081 184.458 223.013 1.00 25.92 ? 4283 LYS A CE    1 
ATOM   20943 N  NZ    . LYS A 1 4283 ? 136.062 182.978 222.876 1.00 26.57 ? 4283 LYS A NZ    1 
ATOM   20944 N  N     . LEU A 1 4284 ? 140.874 189.417 221.844 1.00 9.81  ? 4284 LEU A N     1 
ATOM   20945 C  CA    . LEU A 1 4284 ? 142.243 189.707 221.426 1.00 10.73 ? 4284 LEU A CA    1 
ATOM   20946 C  C     . LEU A 1 4284 ? 143.028 188.427 221.159 1.00 10.74 ? 4284 LEU A C     1 
ATOM   20947 O  O     . LEU A 1 4284 ? 143.773 188.344 220.177 1.00 9.46  ? 4284 LEU A O     1 
ATOM   20948 C  CB    . LEU A 1 4284 ? 142.947 190.562 222.479 1.00 4.27  ? 4284 LEU A CB    1 
ATOM   20949 C  CG    . LEU A 1 4284 ? 142.431 191.995 222.624 1.00 5.98  ? 4284 LEU A CG    1 
ATOM   20950 C  CD1   . LEU A 1 4284 ? 142.588 192.490 224.053 1.00 5.88  ? 4284 LEU A CD1   1 
ATOM   20951 C  CD2   . LEU A 1 4284 ? 143.135 192.923 221.649 1.00 4.71  ? 4284 LEU A CD2   1 
ATOM   20952 N  N     . ALA A 1 4285 ? 142.878 187.428 222.023 1.00 10.43 ? 4285 ALA A N     1 
ATOM   20953 C  CA    . ALA A 1 4285 ? 143.510 186.131 221.839 1.00 7.58  ? 4285 ALA A CA    1 
ATOM   20954 C  C     . ALA A 1 4285 ? 142.521 185.048 222.241 1.00 14.45 ? 4285 ALA A C     1 
ATOM   20955 O  O     . ALA A 1 4285 ? 141.675 185.258 223.114 1.00 17.43 ? 4285 ALA A O     1 
ATOM   20956 C  CB    . ALA A 1 4285 ? 144.804 186.009 222.653 1.00 5.29  ? 4285 ALA A CB    1 
ATOM   20957 N  N     . CYS A 1 4286 ? 142.630 183.889 221.597 1.00 13.94 ? 4286 CYS A N     1 
ATOM   20958 C  CA    . CYS A 1 4286 ? 141.671 182.803 221.769 1.00 20.94 ? 4286 CYS A CA    1 
ATOM   20959 C  C     . CYS A 1 4286 ? 142.374 181.568 222.315 1.00 19.02 ? 4286 CYS A C     1 
ATOM   20960 O  O     . CYS A 1 4286 ? 143.339 181.084 221.717 1.00 16.18 ? 4286 CYS A O     1 
ATOM   20961 C  CB    . CYS A 1 4286 ? 140.972 182.481 220.446 1.00 23.30 ? 4286 CYS A CB    1 
ATOM   20962 S  SG    . CYS A 1 4286 ? 139.956 183.823 219.796 1.00 47.31 ? 4286 CYS A SG    1 
ATOM   20963 N  N     . LYS A 1 4287 ? 141.877 181.063 223.448 1.00 25.76 ? 4287 LYS A N     1 
ATOM   20964 C  CA    . LYS A 1 4287 ? 142.320 179.800 224.043 1.00 26.89 ? 4287 LYS A CA    1 
ATOM   20965 C  C     . LYS A 1 4287 ? 143.827 179.806 224.309 1.00 25.41 ? 4287 LYS A C     1 
ATOM   20966 O  O     . LYS A 1 4287 ? 144.599 179.051 223.716 1.00 25.56 ? 4287 LYS A O     1 
ATOM   20967 C  CB    . LYS A 1 4287 ? 141.911 178.610 223.165 1.00 28.33 ? 4287 LYS A CB    1 
ATOM   20968 C  CG    . LYS A 1 4287 ? 140.543 178.017 223.496 1.00 30.47 ? 4287 LYS A CG    1 
ATOM   20969 C  CD    . LYS A 1 4287 ? 139.425 179.045 223.402 1.00 30.63 ? 4287 LYS A CD    1 
ATOM   20970 C  CE    . LYS A 1 4287 ? 139.218 179.516 221.971 1.00 29.36 ? 4287 LYS A CE    1 
ATOM   20971 N  NZ    . LYS A 1 4287 ? 138.138 180.538 221.876 1.00 33.20 ? 4287 LYS A NZ    1 
ATOM   20972 N  N     . VAL A 1 4288 ? 144.236 180.693 225.217 1.00 22.89 ? 4288 VAL A N     1 
ATOM   20973 C  CA    . VAL A 1 4288 ? 145.647 180.787 225.573 1.00 20.28 ? 4288 VAL A CA    1 
ATOM   20974 C  C     . VAL A 1 4288 ? 146.082 179.566 226.378 1.00 26.71 ? 4288 VAL A C     1 
ATOM   20975 O  O     . VAL A 1 4288 ? 147.127 178.964 226.108 1.00 24.48 ? 4288 VAL A O     1 
ATOM   20976 C  CB    . VAL A 1 4288 ? 145.921 182.102 226.328 1.00 12.31 ? 4288 VAL A CB    1 
ATOM   20977 C  CG1   . VAL A 1 4288 ? 145.896 183.270 225.362 1.00 12.64 ? 4288 VAL A CG1   1 
ATOM   20978 C  CG2   . VAL A 1 4288 ? 144.893 182.316 227.426 1.00 19.22 ? 4288 VAL A CG2   1 
ATOM   20979 N  N     . ASP A 1 4289 ? 145.282 179.172 227.368 1.00 26.22 ? 4289 ASP A N     1 
ATOM   20980 C  CA    . ASP A 1 4289 ? 145.568 178.008 228.194 1.00 26.31 ? 4289 ASP A CA    1 
ATOM   20981 C  C     . ASP A 1 4289 ? 144.636 176.839 227.895 1.00 24.89 ? 4289 ASP A C     1 
ATOM   20982 O  O     . ASP A 1 4289 ? 144.458 175.962 228.746 1.00 31.91 ? 4289 ASP A O     1 
ATOM   20983 C  CB    . ASP A 1 4289 ? 145.508 178.382 229.677 1.00 28.49 ? 4289 ASP A CB    1 
ATOM   20984 C  CG    . ASP A 1 4289 ? 144.135 178.868 230.108 1.00 32.24 ? 4289 ASP A CG    1 
ATOM   20985 O  OD1   . ASP A 1 4289 ? 143.227 178.965 229.258 1.00 34.55 ? 4289 ASP A OD1   1 
ATOM   20986 O  OD2   . ASP A 1 4289 ? 143.964 179.157 231.311 1.00 36.54 ? 4289 ASP A OD2   1 
ATOM   20987 N  N     . GLY A 1 4290 ? 144.036 176.817 226.707 1.00 28.18 ? 4290 GLY A N     1 
ATOM   20988 C  CA    . GLY A 1 4290 ? 143.094 175.796 226.322 1.00 29.17 ? 4290 GLY A CA    1 
ATOM   20989 C  C     . GLY A 1 4290 ? 141.648 176.122 226.636 1.00 35.89 ? 4290 GLY A C     1 
ATOM   20990 O  O     . GLY A 1 4290 ? 140.758 175.761 225.858 1.00 37.64 ? 4290 GLY A O     1 
ATOM   20991 N  N     . HIS A 1 4291 ? 141.390 176.794 227.757 1.00 32.69 ? 4291 HIS A N     1 
ATOM   20992 C  CA    . HIS A 1 4291 ? 140.035 177.143 228.161 1.00 36.28 ? 4291 HIS A CA    1 
ATOM   20993 C  C     . HIS A 1 4291 ? 139.817 178.645 228.237 1.00 35.85 ? 4291 HIS A C     1 
ATOM   20994 O  O     . HIS A 1 4291 ? 138.890 179.166 227.605 1.00 35.80 ? 4291 HIS A O     1 
ATOM   20995 C  CB    . HIS A 1 4291 ? 139.710 176.497 229.517 1.00 29.59 ? 4291 HIS A CB    1 
ATOM   20996 C  CG    . HIS A 1 4291 ? 139.672 175.002 229.479 1.00 36.37 ? 4291 HIS A CG    1 
ATOM   20997 N  ND1   . HIS A 1 4291 ? 140.790 174.224 229.683 1.00 36.74 ? 4291 HIS A ND1   1 
ATOM   20998 C  CD2   . HIS A 1 4291 ? 138.649 174.141 229.262 1.00 40.94 ? 4291 HIS A CD2   1 
ATOM   20999 C  CE1   . HIS A 1 4291 ? 140.460 172.948 229.594 1.00 36.14 ? 4291 HIS A CE1   1 
ATOM   21000 N  NE2   . HIS A 1 4291 ? 139.167 172.870 229.339 1.00 42.03 ? 4291 HIS A NE2   1 
ATOM   21001 N  N     . LYS A 1 4292 ? 140.649 179.359 228.989 1.00 30.98 ? 4292 LYS A N     1 
ATOM   21002 C  CA    . LYS A 1 4292 ? 140.497 180.799 229.134 1.00 28.10 ? 4292 LYS A CA    1 
ATOM   21003 C  C     . LYS A 1 4292 ? 141.099 181.521 227.938 1.00 27.86 ? 4292 LYS A C     1 
ATOM   21004 O  O     . LYS A 1 4292 ? 141.907 180.957 227.195 1.00 28.23 ? 4292 LYS A O     1 
ATOM   21005 C  CB    . LYS A 1 4292 ? 141.161 181.281 230.424 1.00 29.88 ? 4292 LYS A CB    1 
ATOM   21006 C  CG    . LYS A 1 4292 ? 140.740 180.517 231.667 1.00 32.05 ? 4292 LYS A CG    1 
ATOM   21007 C  CD    . LYS A 1 4292 ? 141.486 181.015 232.896 1.00 34.72 ? 4292 LYS A CD    1 
ATOM   21008 C  CE    . LYS A 1 4292 ? 141.320 180.063 234.070 1.00 36.07 ? 4292 LYS A CE    1 
ATOM   21009 N  NZ    . LYS A 1 4292 ? 141.845 178.704 233.763 1.00 34.05 ? 4292 LYS A NZ    1 
ATOM   21010 N  N     . ASP A 1 4293 ? 140.697 182.775 227.752 1.00 26.20 ? 4293 ASP A N     1 
ATOM   21011 C  CA    . ASP A 1 4293 ? 141.218 183.608 226.681 1.00 20.61 ? 4293 ASP A CA    1 
ATOM   21012 C  C     . ASP A 1 4293 ? 141.073 185.083 227.032 1.00 19.63 ? 4293 ASP A C     1 
ATOM   21013 O  O     . ASP A 1 4293 ? 140.371 185.449 227.980 1.00 22.96 ? 4293 ASP A O     1 
ATOM   21014 C  CB    . ASP A 1 4293 ? 140.553 183.249 225.330 1.00 21.83 ? 4293 ASP A CB    1 
ATOM   21015 C  CG    . ASP A 1 4293 ? 139.099 183.688 225.222 1.00 22.30 ? 4293 ASP A CG    1 
ATOM   21016 O  OD1   . ASP A 1 4293 ? 138.643 184.609 225.925 1.00 27.94 ? 4293 ASP A OD1   1 
ATOM   21017 O  OD2   . ASP A 1 4293 ? 138.393 183.069 224.405 1.00 24.31 ? 4293 ASP A OD2   1 
ATOM   21018 N  N     . ILE A 1 4294 ? 141.755 185.923 226.264 1.00 16.45 ? 4294 ILE A N     1 
ATOM   21019 C  CA    . ILE A 1 4294 ? 141.895 187.335 226.602 1.00 12.10 ? 4294 ILE A CA    1 
ATOM   21020 C  C     . ILE A 1 4294 ? 140.804 188.134 225.903 1.00 13.31 ? 4294 ILE A C     1 
ATOM   21021 O  O     . ILE A 1 4294 ? 140.702 188.126 224.672 1.00 15.59 ? 4294 ILE A O     1 
ATOM   21022 C  CB    . ILE A 1 4294 ? 143.295 187.839 226.220 1.00 8.30  ? 4294 ILE A CB    1 
ATOM   21023 C  CG1   . ILE A 1 4294 ? 144.358 186.918 226.823 1.00 12.29 ? 4294 ILE A CG1   1 
ATOM   21024 C  CG2   . ILE A 1 4294 ? 143.494 189.269 226.687 1.00 7.68  ? 4294 ILE A CG2   1 
ATOM   21025 C  CD1   . ILE A 1 4294 ? 145.777 187.319 226.515 1.00 7.55  ? 4294 ILE A CD1   1 
ATOM   21026 N  N     . GLN A 1 4295 ? 139.991 188.832 226.691 1.00 15.18 ? 4295 GLN A N     1 
ATOM   21027 C  CA    . GLN A 1 4295 ? 138.874 189.616 226.183 1.00 13.39 ? 4295 GLN A CA    1 
ATOM   21028 C  C     . GLN A 1 4295 ? 139.285 191.064 225.962 1.00 9.27  ? 4295 GLN A C     1 
ATOM   21029 O  O     . GLN A 1 4295 ? 140.159 191.597 226.649 1.00 15.15 ? 4295 GLN A O     1 
ATOM   21030 C  CB    . GLN A 1 4295 ? 137.685 189.568 227.147 1.00 14.17 ? 4295 GLN A CB    1 
ATOM   21031 C  CG    . GLN A 1 4295 ? 137.056 188.200 227.312 1.00 17.58 ? 4295 GLN A CG    1 
ATOM   21032 C  CD    . GLN A 1 4295 ? 136.469 187.671 226.020 1.00 24.26 ? 4295 GLN A CD    1 
ATOM   21033 O  OE1   . GLN A 1 4295 ? 136.996 186.735 225.426 1.00 28.18 ? 4295 GLN A OE1   1 
ATOM   21034 N  NE2   . GLN A 1 4295 ? 135.366 188.265 225.581 1.00 23.07 ? 4295 GLN A NE2   1 
ATOM   21035 N  N     . MET A 1 4296 ? 138.642 191.693 224.994 1.00 12.50 ? 4296 MET A N     1 
ATOM   21036 C  CA    . MET A 1 4296 ? 138.864 193.108 224.733 1.00 11.51 ? 4296 MET A CA    1 
ATOM   21037 C  C     . MET A 1 4296 ? 138.199 193.943 225.820 1.00 11.43 ? 4296 MET A C     1 
ATOM   21038 O  O     . MET A 1 4296 ? 137.003 193.774 226.077 1.00 20.19 ? 4296 MET A O     1 
ATOM   21039 C  CB    . MET A 1 4296 ? 138.309 193.489 223.366 1.00 11.90 ? 4296 MET A CB    1 
ATOM   21040 C  CG    . MET A 1 4296 ? 138.481 194.948 223.010 1.00 12.79 ? 4296 MET A CG    1 
ATOM   21041 S  SD    . MET A 1 4296 ? 140.175 195.340 222.546 1.00 7.43  ? 4296 MET A SD    1 
ATOM   21042 C  CE    . MET A 1 4296 ? 139.933 196.888 221.690 1.00 9.99  ? 4296 MET A CE    1 
ATOM   21043 N  N     . PRO A 1 4297 ? 138.933 194.833 226.485 1.00 8.99  ? 4297 PRO A N     1 
ATOM   21044 C  CA    . PRO A 1 4297 ? 138.308 195.690 227.498 1.00 10.86 ? 4297 PRO A CA    1 
ATOM   21045 C  C     . PRO A 1 4297 ? 137.233 196.578 226.890 1.00 18.16 ? 4297 PRO A C     1 
ATOM   21046 O  O     . PRO A 1 4297 ? 137.365 197.065 225.765 1.00 22.82 ? 4297 PRO A O     1 
ATOM   21047 C  CB    . PRO A 1 4297 ? 139.481 196.519 228.038 1.00 6.08  ? 4297 PRO A CB    1 
ATOM   21048 C  CG    . PRO A 1 4297 ? 140.526 196.444 226.974 1.00 9.45  ? 4297 PRO A CG    1 
ATOM   21049 C  CD    . PRO A 1 4297 ? 140.372 195.103 226.332 1.00 7.00  ? 4297 PRO A CD    1 
ATOM   21050 N  N     . ASP A 1 4298 ? 136.161 196.782 227.647 1.00 19.04 ? 4298 ASP A N     1 
ATOM   21051 C  CA    . ASP A 1 4298 ? 135.046 197.619 227.210 1.00 20.39 ? 4298 ASP A CA    1 
ATOM   21052 C  C     . ASP A 1 4298 ? 135.210 199.068 227.666 1.00 20.58 ? 4298 ASP A C     1 
ATOM   21053 O  O     . ASP A 1 4298 ? 134.293 199.700 228.184 1.00 21.95 ? 4298 ASP A O     1 
ATOM   21054 C  CB    . ASP A 1 4298 ? 133.733 197.014 227.700 1.00 23.18 ? 4298 ASP A CB    1 
ATOM   21055 C  CG    . ASP A 1 4298 ? 133.586 197.062 229.213 1.00 31.98 ? 4298 ASP A CG    1 
ATOM   21056 O  OD1   . ASP A 1 4298 ? 134.075 196.128 229.882 1.00 31.33 ? 4298 ASP A OD1   1 
ATOM   21057 O  OD2   . ASP A 1 4298 ? 132.959 198.010 229.730 1.00 35.99 ? 4298 ASP A OD2   1 
ATOM   21058 N  N     . GLY A 1 4299 ? 136.393 199.623 227.423 1.00 17.69 ? 4299 GLY A N     1 
ATOM   21059 C  CA    . GLY A 1 4299 ? 136.687 200.976 227.839 1.00 21.52 ? 4299 GLY A CA    1 
ATOM   21060 C  C     . GLY A 1 4299 ? 136.467 201.998 226.737 1.00 23.45 ? 4299 GLY A C     1 
ATOM   21061 O  O     . GLY A 1 4299 ? 136.607 201.707 225.552 1.00 22.96 ? 4299 GLY A O     1 
ATOM   21062 N  N     . ILE A 1 4300 ? 136.105 203.210 227.152 1.00 18.77 ? 4300 ILE A N     1 
ATOM   21063 C  CA    . ILE A 1 4300 ? 135.992 204.354 226.259 1.00 14.02 ? 4300 ILE A CA    1 
ATOM   21064 C  C     . ILE A 1 4300 ? 136.988 205.450 226.595 1.00 19.80 ? 4300 ILE A C     1 
ATOM   21065 O  O     . ILE A 1 4300 ? 137.061 206.448 225.871 1.00 26.09 ? 4300 ILE A O     1 
ATOM   21066 C  CB    . ILE A 1 4300 ? 134.558 204.922 226.249 1.00 16.84 ? 4300 ILE A CB    1 
ATOM   21067 C  CG1   . ILE A 1 4300 ? 134.190 205.473 227.626 1.00 25.10 ? 4300 ILE A CG1   1 
ATOM   21068 C  CG2   . ILE A 1 4300 ? 133.566 203.858 225.808 1.00 20.39 ? 4300 ILE A CG2   1 
ATOM   21069 C  CD1   . ILE A 1 4300 ? 132.792 206.048 227.702 1.00 28.64 ? 4300 ILE A CD1   1 
ATOM   21070 N  N     . ARG A 1 4301 ? 137.759 205.296 227.670 1.00 16.29 ? 4301 ARG A N     1 
ATOM   21071 C  CA    . ARG A 1 4301 ? 138.738 206.283 228.094 1.00 17.02 ? 4301 ARG A CA    1 
ATOM   21072 C  C     . ARG A 1 4301 ? 140.085 205.602 228.291 1.00 15.53 ? 4301 ARG A C     1 
ATOM   21073 O  O     . ARG A 1 4301 ? 140.166 204.387 228.490 1.00 11.48 ? 4301 ARG A O     1 
ATOM   21074 C  CB    . ARG A 1 4301 ? 138.304 206.989 229.389 1.00 20.00 ? 4301 ARG A CB    1 
ATOM   21075 C  CG    . ARG A 1 4301 ? 137.017 207.787 229.258 1.00 22.40 ? 4301 ARG A CG    1 
ATOM   21076 C  CD    . ARG A 1 4301 ? 136.434 208.129 230.621 1.00 24.53 ? 4301 ARG A CD    1 
ATOM   21077 N  NE    . ARG A 1 4301 ? 135.957 206.944 231.325 1.00 29.73 ? 4301 ARG A NE    1 
ATOM   21078 C  CZ    . ARG A 1 4301 ? 136.437 206.521 232.486 1.00 29.78 ? 4301 ARG A CZ    1 
ATOM   21079 N  NH1   . ARG A 1 4301 ? 137.416 207.160 233.104 1.00 20.31 ? 4301 ARG A NH1   1 
ATOM   21080 N  NH2   . ARG A 1 4301 ? 135.922 205.428 233.040 1.00 32.23 ? 4301 ARG A NH2   1 
ATOM   21081 N  N     . ARG A 1 4302 ? 141.149 206.407 228.229 1.00 13.17 ? 4302 ARG A N     1 
ATOM   21082 C  CA    . ARG A 1 4302 ? 142.500 205.857 228.304 1.00 11.40 ? 4302 ARG A CA    1 
ATOM   21083 C  C     . ARG A 1 4302 ? 142.747 205.147 229.630 1.00 12.72 ? 4302 ARG A C     1 
ATOM   21084 O  O     . ARG A 1 4302 ? 143.327 204.056 229.658 1.00 17.05 ? 4302 ARG A O     1 
ATOM   21085 C  CB    . ARG A 1 4302 ? 143.532 206.963 228.101 1.00 11.76 ? 4302 ARG A CB    1 
ATOM   21086 C  CG    . ARG A 1 4302 ? 144.942 206.539 228.472 1.00 10.54 ? 4302 ARG A CG    1 
ATOM   21087 C  CD    . ARG A 1 4302 ? 145.932 207.679 228.357 1.00 13.28 ? 4302 ARG A CD    1 
ATOM   21088 N  NE    . ARG A 1 4302 ? 147.225 207.331 228.933 1.00 18.19 ? 4302 ARG A NE    1 
ATOM   21089 C  CZ    . ARG A 1 4302 ? 147.457 207.182 230.230 1.00 13.83 ? 4302 ARG A CZ    1 
ATOM   21090 N  NH1   . ARG A 1 4302 ? 146.509 207.387 231.130 1.00 11.03 ? 4302 ARG A NH1   1 
ATOM   21091 N  NH2   . ARG A 1 4302 ? 148.672 206.825 230.635 1.00 12.06 ? 4302 ARG A NH2   1 
ATOM   21092 N  N     . GLU A 1 4303 ? 142.311 205.751 230.738 1.00 17.50 ? 4303 GLU A N     1 
ATOM   21093 C  CA    . GLU A 1 4303 ? 142.587 205.183 232.055 1.00 13.85 ? 4303 GLU A CA    1 
ATOM   21094 C  C     . GLU A 1 4303 ? 141.963 203.805 232.222 1.00 16.44 ? 4303 GLU A C     1 
ATOM   21095 O  O     . GLU A 1 4303 ? 142.499 202.968 232.958 1.00 15.22 ? 4303 GLU A O     1 
ATOM   21096 C  CB    . GLU A 1 4303 ? 142.092 206.130 233.149 1.00 12.87 ? 4303 GLU A CB    1 
ATOM   21097 C  CG    . GLU A 1 4303 ? 140.671 206.622 232.950 1.00 20.97 ? 4303 GLU A CG    1 
ATOM   21098 C  CD    . GLU A 1 4303 ? 140.604 207.912 232.156 1.00 31.25 ? 4303 GLU A CD    1 
ATOM   21099 O  OE1   . GLU A 1 4303 ? 141.050 207.918 230.988 1.00 28.19 ? 4303 GLU A OE1   1 
ATOM   21100 O  OE2   . GLU A 1 4303 ? 140.104 208.920 232.698 1.00 35.90 ? 4303 GLU A OE2   1 
ATOM   21101 N  N     . GLU A 1 4304 ? 140.833 203.547 231.560 1.00 17.30 ? 4304 GLU A N     1 
ATOM   21102 C  CA    . GLU A 1 4304 ? 140.234 202.219 231.614 1.00 13.91 ? 4304 GLU A CA    1 
ATOM   21103 C  C     . GLU A 1 4304 ? 141.128 201.177 230.951 1.00 15.01 ? 4304 GLU A C     1 
ATOM   21104 O  O     . GLU A 1 4304 ? 141.270 200.060 231.461 1.00 22.30 ? 4304 GLU A O     1 
ATOM   21105 C  CB    . GLU A 1 4304 ? 138.855 202.234 230.960 1.00 19.08 ? 4304 GLU A CB    1 
ATOM   21106 C  CG    . GLU A 1 4304 ? 138.024 203.464 231.283 1.00 22.88 ? 4304 GLU A CG    1 
ATOM   21107 C  CD    . GLU A 1 4304 ? 136.651 203.414 230.643 1.00 26.82 ? 4304 GLU A CD    1 
ATOM   21108 O  OE1   . GLU A 1 4304 ? 135.990 202.360 230.738 1.00 30.94 ? 4304 GLU A OE1   1 
ATOM   21109 O  OE2   . GLU A 1 4304 ? 136.236 204.428 230.044 1.00 24.61 ? 4304 GLU A OE2   1 
ATOM   21110 N  N     . PHE A 1 4305 ? 141.730 201.521 229.808 1.00 13.61 ? 4305 PHE A N     1 
ATOM   21111 C  CA    . PHE A 1 4305 ? 142.620 200.582 229.135 1.00 8.64  ? 4305 PHE A CA    1 
ATOM   21112 C  C     . PHE A 1 4305 ? 143.885 200.338 229.948 1.00 8.94  ? 4305 PHE A C     1 
ATOM   21113 O  O     . PHE A 1 4305 ? 144.382 199.206 230.003 1.00 16.07 ? 4305 PHE A O     1 
ATOM   21114 C  CB    . PHE A 1 4305 ? 142.969 201.090 227.735 1.00 9.41  ? 4305 PHE A CB    1 
ATOM   21115 C  CG    . PHE A 1 4305 ? 141.798 201.138 226.795 1.00 6.50  ? 4305 PHE A CG    1 
ATOM   21116 C  CD1   . PHE A 1 4305 ? 141.238 199.970 226.305 1.00 8.23  ? 4305 PHE A CD1   1 
ATOM   21117 C  CD2   . PHE A 1 4305 ? 141.267 202.348 226.388 1.00 5.96  ? 4305 PHE A CD2   1 
ATOM   21118 C  CE1   . PHE A 1 4305 ? 140.164 200.011 225.437 1.00 8.05  ? 4305 PHE A CE1   1 
ATOM   21119 C  CE2   . PHE A 1 4305 ? 140.194 202.396 225.521 1.00 5.87  ? 4305 PHE A CE2   1 
ATOM   21120 C  CZ    . PHE A 1 4305 ? 139.643 201.226 225.046 1.00 10.88 ? 4305 PHE A CZ    1 
ATOM   21121 N  N     . VAL A 1 4306 ? 144.424 201.383 230.578 1.00 9.51  ? 4306 VAL A N     1 
ATOM   21122 C  CA    . VAL A 1 4306 ? 145.629 201.218 231.386 1.00 10.96 ? 4306 VAL A CA    1 
ATOM   21123 C  C     . VAL A 1 4306 ? 145.337 200.356 232.610 1.00 11.52 ? 4306 VAL A C     1 
ATOM   21124 O  O     . VAL A 1 4306 ? 146.186 199.573 233.051 1.00 11.06 ? 4306 VAL A O     1 
ATOM   21125 C  CB    . VAL A 1 4306 ? 146.205 202.593 231.772 1.00 13.39 ? 4306 VAL A CB    1 
ATOM   21126 C  CG1   . VAL A 1 4306 ? 147.528 202.435 232.496 1.00 8.12  ? 4306 VAL A CG1   1 
ATOM   21127 C  CG2   . VAL A 1 4306 ? 146.389 203.454 230.530 1.00 11.76 ? 4306 VAL A CG2   1 
ATOM   21128 N  N     . GLN A 1 4307 ? 144.136 200.487 233.179 1.00 11.71 ? 4307 GLN A N     1 
ATOM   21129 C  CA    . GLN A 1 4307 ? 143.740 199.603 234.271 1.00 10.59 ? 4307 GLN A CA    1 
ATOM   21130 C  C     . GLN A 1 4307 ? 143.662 198.155 233.800 1.00 10.02 ? 4307 GLN A C     1 
ATOM   21131 O  O     . GLN A 1 4307 ? 144.076 197.238 234.517 1.00 12.61 ? 4307 GLN A O     1 
ATOM   21132 C  CB    . GLN A 1 4307 ? 142.399 200.049 234.853 1.00 14.53 ? 4307 GLN A CB    1 
ATOM   21133 C  CG    . GLN A 1 4307 ? 142.500 201.199 235.839 1.00 21.86 ? 4307 GLN A CG    1 
ATOM   21134 C  CD    . GLN A 1 4307 ? 141.172 201.896 236.057 1.00 27.78 ? 4307 GLN A CD    1 
ATOM   21135 O  OE1   . GLN A 1 4307 ? 140.447 202.190 235.107 1.00 28.50 ? 4307 GLN A OE1   1 
ATOM   21136 N  NE2   . GLN A 1 4307 ? 140.845 202.164 237.316 1.00 30.98 ? 4307 GLN A NE2   1 
ATOM   21137 N  N     . TRP A 1 4308 ? 143.131 197.936 232.596 1.00 10.93 ? 4308 TRP A N     1 
ATOM   21138 C  CA    . TRP A 1 4308 ? 143.038 196.583 232.056 1.00 4.72  ? 4308 TRP A CA    1 
ATOM   21139 C  C     . TRP A 1 4308 ? 144.420 195.971 231.861 1.00 5.56  ? 4308 TRP A C     1 
ATOM   21140 O  O     . TRP A 1 4308 ? 144.624 194.783 232.138 1.00 9.23  ? 4308 TRP A O     1 
ATOM   21141 C  CB    . TRP A 1 4308 ? 142.262 196.609 230.739 1.00 6.27  ? 4308 TRP A CB    1 
ATOM   21142 C  CG    . TRP A 1 4308 ? 142.122 195.278 230.067 1.00 7.42  ? 4308 TRP A CG    1 
ATOM   21143 C  CD1   . TRP A 1 4308 ? 141.085 194.404 230.191 1.00 3.42  ? 4308 TRP A CD1   1 
ATOM   21144 C  CD2   . TRP A 1 4308 ? 143.046 194.674 229.155 1.00 4.11  ? 4308 TRP A CD2   1 
ATOM   21145 N  NE1   . TRP A 1 4308 ? 141.305 193.293 229.417 1.00 4.76  ? 4308 TRP A NE1   1 
ATOM   21146 C  CE2   . TRP A 1 4308 ? 142.503 193.434 228.770 1.00 4.49  ? 4308 TRP A CE2   1 
ATOM   21147 C  CE3   . TRP A 1 4308 ? 144.281 195.060 228.628 1.00 3.56  ? 4308 TRP A CE3   1 
ATOM   21148 C  CZ2   . TRP A 1 4308 ? 143.152 192.580 227.884 1.00 4.57  ? 4308 TRP A CZ2   1 
ATOM   21149 C  CZ3   . TRP A 1 4308 ? 144.922 194.210 227.750 1.00 2.80  ? 4308 TRP A CZ3   1 
ATOM   21150 C  CH2   . TRP A 1 4308 ? 144.358 192.985 227.387 1.00 3.83  ? 4308 TRP A CH2   1 
ATOM   21151 N  N     . VAL A 1 4309 ? 145.378 196.765 231.380 1.00 4.17  ? 4309 VAL A N     1 
ATOM   21152 C  CA    . VAL A 1 4309 ? 146.731 196.256 231.175 1.00 5.01  ? 4309 VAL A CA    1 
ATOM   21153 C  C     . VAL A 1 4309 ? 147.375 195.891 232.508 1.00 5.01  ? 4309 VAL A C     1 
ATOM   21154 O  O     . VAL A 1 4309 ? 148.051 194.862 232.622 1.00 8.13  ? 4309 VAL A O     1 
ATOM   21155 C  CB    . VAL A 1 4309 ? 147.572 197.283 230.394 1.00 6.86  ? 4309 VAL A CB    1 
ATOM   21156 C  CG1   . VAL A 1 4309 ? 149.012 196.817 230.272 1.00 2.01  ? 4309 VAL A CG1   1 
ATOM   21157 C  CG2   . VAL A 1 4309 ? 146.973 197.519 229.019 1.00 2.38  ? 4309 VAL A CG2   1 
ATOM   21158 N  N     . GLU A 1 4310 ? 147.176 196.723 233.535 1.00 10.69 ? 4310 GLU A N     1 
ATOM   21159 C  CA    . GLU A 1 4310 ? 147.743 196.435 234.848 1.00 5.72  ? 4310 GLU A CA    1 
ATOM   21160 C  C     . GLU A 1 4310 ? 147.121 195.207 235.497 1.00 9.31  ? 4310 GLU A C     1 
ATOM   21161 O  O     . GLU A 1 4310 ? 147.757 194.592 236.357 1.00 14.56 ? 4310 GLU A O     1 
ATOM   21162 C  CB    . GLU A 1 4310 ? 147.579 197.638 235.776 1.00 8.46  ? 4310 GLU A CB    1 
ATOM   21163 C  CG    . GLU A 1 4310 ? 148.408 198.848 235.398 1.00 8.23  ? 4310 GLU A CG    1 
ATOM   21164 C  CD    . GLU A 1 4310 ? 147.703 200.147 235.722 1.00 17.81 ? 4310 GLU A CD    1 
ATOM   21165 O  OE1   . GLU A 1 4310 ? 146.607 200.093 236.320 1.00 19.17 ? 4310 GLU A OE1   1 
ATOM   21166 O  OE2   . GLU A 1 4310 ? 148.243 201.221 235.387 1.00 16.97 ? 4310 GLU A OE2   1 
ATOM   21167 N  N     . LEU A 1 4311 ? 145.903 194.837 235.112 1.00 6.52  ? 4311 LEU A N     1 
ATOM   21168 C  CA    . LEU A 1 4311 ? 145.229 193.678 235.677 1.00 5.63  ? 4311 LEU A CA    1 
ATOM   21169 C  C     . LEU A 1 4311 ? 145.504 192.395 234.905 1.00 10.49 ? 4311 LEU A C     1 
ATOM   21170 O  O     . LEU A 1 4311 ? 144.925 191.357 235.236 1.00 14.02 ? 4311 LEU A O     1 
ATOM   21171 C  CB    . LEU A 1 4311 ? 143.719 193.921 235.749 1.00 6.67  ? 4311 LEU A CB    1 
ATOM   21172 C  CG    . LEU A 1 4311 ? 143.234 194.956 236.768 1.00 9.98  ? 4311 LEU A CG    1 
ATOM   21173 C  CD1   . LEU A 1 4311 ? 141.752 194.775 237.043 1.00 8.70  ? 4311 LEU A CD1   1 
ATOM   21174 C  CD2   . LEU A 1 4311 ? 144.034 194.878 238.057 1.00 9.42  ? 4311 LEU A CD2   1 
ATOM   21175 N  N     . LEU A 1 4312 ? 146.352 192.444 233.884 1.00 7.98  ? 4312 LEU A N     1 
ATOM   21176 C  CA    . LEU A 1 4312 ? 146.729 191.227 233.185 1.00 7.22  ? 4312 LEU A CA    1 
ATOM   21177 C  C     . LEU A 1 4312 ? 147.526 190.320 234.120 1.00 10.29 ? 4312 LEU A C     1 
ATOM   21178 O  O     . LEU A 1 4312 ? 148.352 190.801 234.901 1.00 11.00 ? 4312 LEU A O     1 
ATOM   21179 C  CB    . LEU A 1 4312 ? 147.556 191.546 231.941 1.00 6.34  ? 4312 LEU A CB    1 
ATOM   21180 C  CG    . LEU A 1 4312 ? 146.817 192.093 230.718 1.00 4.08  ? 4312 LEU A CG    1 
ATOM   21181 C  CD1   . LEU A 1 4312 ? 147.804 192.565 229.667 1.00 1.90  ? 4312 LEU A CD1   1 
ATOM   21182 C  CD2   . LEU A 1 4312 ? 145.873 191.051 230.138 1.00 2.87  ? 4312 LEU A CD2   1 
ATOM   21183 N  N     . PRO A 1 4313 ? 147.302 189.011 234.069 1.00 12.87 ? 4313 PRO A N     1 
ATOM   21184 C  CA    . PRO A 1 4313 ? 148.051 188.099 234.937 1.00 9.96  ? 4313 PRO A CA    1 
ATOM   21185 C  C     . PRO A 1 4313 ? 149.512 188.020 234.523 1.00 8.36  ? 4313 PRO A C     1 
ATOM   21186 O  O     . PRO A 1 4313 ? 149.903 188.400 233.419 1.00 15.42 ? 4313 PRO A O     1 
ATOM   21187 C  CB    . PRO A 1 4313 ? 147.338 186.760 234.738 1.00 11.01 ? 4313 PRO A CB    1 
ATOM   21188 C  CG    . PRO A 1 4313 ? 146.752 186.862 233.371 1.00 6.68  ? 4313 PRO A CG    1 
ATOM   21189 C  CD    . PRO A 1 4313 ? 146.334 188.296 233.221 1.00 6.30  ? 4313 PRO A CD    1 
ATOM   21190 N  N     . ASP A 1 4314 ? 150.330 187.511 235.444 1.00 10.57 ? 4314 ASP A N     1 
ATOM   21191 C  CA    . ASP A 1 4314 ? 151.741 187.267 235.180 1.00 13.36 ? 4314 ASP A CA    1 
ATOM   21192 C  C     . ASP A 1 4314 ? 151.970 185.858 234.645 1.00 13.84 ? 4314 ASP A C     1 
ATOM   21193 O  O     . ASP A 1 4314 ? 153.010 185.242 234.907 1.00 20.74 ? 4314 ASP A O     1 
ATOM   21194 C  CB    . ASP A 1 4314 ? 152.561 187.519 236.450 1.00 14.26 ? 4314 ASP A CB    1 
ATOM   21195 C  CG    . ASP A 1 4314 ? 154.062 187.587 236.189 1.00 21.82 ? 4314 ASP A CG    1 
ATOM   21196 O  OD1   . ASP A 1 4314 ? 154.489 187.438 235.026 1.00 18.02 ? 4314 ASP A OD1   1 
ATOM   21197 O  OD2   . ASP A 1 4314 ? 154.821 187.793 237.161 1.00 24.22 ? 4314 ASP A OD2   1 
ATOM   21198 N  N     . THR A 1 4315 ? 150.995 185.321 233.921 1.00 12.85 ? 4315 THR A N     1 
ATOM   21199 C  CA    . THR A 1 4315 ? 151.038 183.971 233.378 1.00 9.80  ? 4315 THR A CA    1 
ATOM   21200 C  C     . THR A 1 4315 ? 151.075 183.991 231.854 1.00 9.61  ? 4315 THR A C     1 
ATOM   21201 O  O     . THR A 1 4315 ? 150.403 183.200 231.190 1.00 16.02 ? 4315 THR A O     1 
ATOM   21202 C  CB    . THR A 1 4315 ? 149.845 183.158 233.871 1.00 18.37 ? 4315 THR A CB    1 
ATOM   21203 O  OG1   . THR A 1 4315 ? 148.650 183.633 233.239 1.00 17.66 ? 4315 THR A OG1   1 
ATOM   21204 C  CG2   . THR A 1 4315 ? 149.699 183.298 235.377 1.00 11.71 ? 4315 THR A CG2   1 
ATOM   21205 N  N     . GLN A 1 4316 ? 151.851 184.910 231.287 1.00 11.34 ? 4316 GLN A N     1 
ATOM   21206 C  CA    . GLN A 1 4316 ? 151.957 185.009 229.839 1.00 3.46  ? 4316 GLN A CA    1 
ATOM   21207 C  C     . GLN A 1 4316 ? 152.603 183.761 229.257 1.00 4.48  ? 4316 GLN A C     1 
ATOM   21208 O  O     . GLN A 1 4316 ? 153.605 183.257 229.770 1.00 8.39  ? 4316 GLN A O     1 
ATOM   21209 C  CB    . GLN A 1 4316 ? 152.767 186.241 229.441 1.00 3.44  ? 4316 GLN A CB    1 
ATOM   21210 C  CG    . GLN A 1 4316 ? 152.917 186.418 227.938 1.00 2.71  ? 4316 GLN A CG    1 
ATOM   21211 C  CD    . GLN A 1 4316 ? 153.871 187.534 227.568 1.00 5.47  ? 4316 GLN A CD    1 
ATOM   21212 O  OE1   . GLN A 1 4316 ? 153.751 188.655 228.057 1.00 7.07  ? 4316 GLN A OE1   1 
ATOM   21213 N  NE2   . GLN A 1 4316 ? 154.823 187.234 226.695 1.00 4.98  ? 4316 GLN A NE2   1 
ATOM   21214 N  N     . THR A 1 4317 ? 152.022 183.272 228.174 1.00 6.46  ? 4317 THR A N     1 
ATOM   21215 C  CA    . THR A 1 4317 ? 152.514 182.140 227.410 1.00 4.55  ? 4317 THR A CA    1 
ATOM   21216 C  C     . THR A 1 4317 ? 152.595 182.562 225.953 1.00 4.43  ? 4317 THR A C     1 
ATOM   21217 O  O     . THR A 1 4317 ? 151.953 183.536 225.549 1.00 5.95  ? 4317 THR A O     1 
ATOM   21218 C  CB    . THR A 1 4317 ? 151.590 180.922 227.559 1.00 9.34  ? 4317 THR A CB    1 
ATOM   21219 O  OG1   . THR A 1 4317 ? 150.253 181.287 227.199 1.00 8.38  ? 4317 THR A OG1   1 
ATOM   21220 C  CG2   . THR A 1 4317 ? 151.605 180.409 228.988 1.00 3.35  ? 4317 THR A CG2   1 
ATOM   21221 N  N     . PRO A 1 4318 ? 153.388 181.862 225.139 1.00 7.69  ? 4318 PRO A N     1 
ATOM   21222 C  CA    . PRO A 1 4318 ? 153.444 182.209 223.710 1.00 4.50  ? 4318 PRO A CA    1 
ATOM   21223 C  C     . PRO A 1 4318 ? 152.104 182.096 223.002 1.00 2.83  ? 4318 PRO A C     1 
ATOM   21224 O  O     . PRO A 1 4318 ? 151.955 182.647 221.905 1.00 4.63  ? 4318 PRO A O     1 
ATOM   21225 C  CB    . PRO A 1 4318 ? 154.474 181.220 223.141 1.00 6.90  ? 4318 PRO A CB    1 
ATOM   21226 C  CG    . PRO A 1 4318 ? 154.666 180.184 224.197 1.00 5.52  ? 4318 PRO A CG    1 
ATOM   21227 C  CD    . PRO A 1 4318 ? 154.392 180.850 225.498 1.00 4.87  ? 4318 PRO A CD    1 
ATOM   21228 N  N     . SER A 1 4319 ? 151.125 181.403 223.589 1.00 1.94  ? 4319 SER A N     1 
ATOM   21229 C  CA    . SER A 1 4319 ? 149.778 181.389 223.032 1.00 3.00  ? 4319 SER A CA    1 
ATOM   21230 C  C     . SER A 1 4319 ? 149.119 182.762 223.073 1.00 3.56  ? 4319 SER A C     1 
ATOM   21231 O  O     . SER A 1 4319 ? 148.164 182.999 222.326 1.00 6.56  ? 4319 SER A O     1 
ATOM   21232 C  CB    . SER A 1 4319 ? 148.910 180.370 223.772 1.00 6.03  ? 4319 SER A CB    1 
ATOM   21233 O  OG    . SER A 1 4319 ? 148.830 180.676 225.152 1.00 7.12  ? 4319 SER A OG    1 
ATOM   21234 N  N     . TRP A 1 4320 ? 149.595 183.666 223.933 1.00 3.21  ? 4320 TRP A N     1 
ATOM   21235 C  CA    . TRP A 1 4320 ? 149.141 185.052 223.871 1.00 2.97  ? 4320 TRP A CA    1 
ATOM   21236 C  C     . TRP A 1 4320 ? 149.460 185.672 222.520 1.00 2.80  ? 4320 TRP A C     1 
ATOM   21237 O  O     . TRP A 1 4320 ? 148.728 186.546 222.046 1.00 2.08  ? 4320 TRP A O     1 
ATOM   21238 C  CB    . TRP A 1 4320 ? 149.799 185.880 224.976 1.00 6.58  ? 4320 TRP A CB    1 
ATOM   21239 C  CG    . TRP A 1 4320 ? 149.291 185.619 226.354 1.00 4.40  ? 4320 TRP A CG    1 
ATOM   21240 C  CD1   . TRP A 1 4320 ? 148.802 184.446 226.844 1.00 4.94  ? 4320 TRP A CD1   1 
ATOM   21241 C  CD2   . TRP A 1 4320 ? 149.230 186.560 227.430 1.00 3.79  ? 4320 TRP A CD2   1 
ATOM   21242 N  NE1   . TRP A 1 4320 ? 148.437 184.598 228.157 1.00 5.83  ? 4320 TRP A NE1   1 
ATOM   21243 C  CE2   . TRP A 1 4320 ? 148.690 185.887 228.542 1.00 3.77  ? 4320 TRP A CE2   1 
ATOM   21244 C  CE3   . TRP A 1 4320 ? 149.579 187.907 227.559 1.00 5.11  ? 4320 TRP A CE3   1 
ATOM   21245 C  CZ2   . TRP A 1 4320 ? 148.490 186.515 229.768 1.00 5.25  ? 4320 TRP A CZ2   1 
ATOM   21246 C  CZ3   . TRP A 1 4320 ? 149.377 188.530 228.777 1.00 4.61  ? 4320 TRP A CZ3   1 
ATOM   21247 C  CH2   . TRP A 1 4320 ? 148.840 187.833 229.865 1.00 5.78  ? 4320 TRP A CH2   1 
ATOM   21248 N  N     . LEU A 1 4321 ? 150.546 185.230 221.897 1.00 3.40  ? 4321 LEU A N     1 
ATOM   21249 C  CA    . LEU A 1 4321 ? 151.024 185.769 220.634 1.00 1.13  ? 4321 LEU A CA    1 
ATOM   21250 C  C     . LEU A 1 4321 ? 150.498 185.003 219.430 1.00 2.55  ? 4321 LEU A C     1 
ATOM   21251 O  O     . LEU A 1 4321 ? 150.848 185.345 218.297 1.00 8.02  ? 4321 LEU A O     1 
ATOM   21252 C  CB    . LEU A 1 4321 ? 152.554 185.755 220.623 1.00 1.18  ? 4321 LEU A CB    1 
ATOM   21253 C  CG    . LEU A 1 4321 ? 153.228 186.248 221.905 1.00 0.96  ? 4321 LEU A CG    1 
ATOM   21254 C  CD1   . LEU A 1 4321 ? 154.731 186.073 221.823 1.00 0.51  ? 4321 LEU A CD1   1 
ATOM   21255 C  CD2   . LEU A 1 4321 ? 152.869 187.691 222.198 1.00 0.83  ? 4321 LEU A CD2   1 
ATOM   21256 N  N     . GLY A 1 4322 ? 149.670 183.982 219.645 1.00 1.31  ? 4322 GLY A N     1 
ATOM   21257 C  CA    . GLY A 1 4322 ? 149.241 183.099 218.583 1.00 1.75  ? 4322 GLY A CA    1 
ATOM   21258 C  C     . GLY A 1 4322 ? 150.163 181.929 218.316 1.00 2.28  ? 4322 GLY A C     1 
ATOM   21259 O  O     . GLY A 1 4322 ? 149.856 181.107 217.445 1.00 2.67  ? 4322 GLY A O     1 
ATOM   21260 N  N     . LEU A 1 4323 ? 151.273 181.831 219.030 1.00 1.99  ? 4323 LEU A N     1 
ATOM   21261 C  CA    . LEU A 1 4323 ? 152.248 180.761 218.908 1.00 2.03  ? 4323 LEU A CA    1 
ATOM   21262 C  C     . LEU A 1 4323 ? 151.828 179.556 219.736 1.00 2.32  ? 4323 LEU A C     1 
ATOM   21263 O  O     . LEU A 1 4323 ? 151.021 179.674 220.661 1.00 4.46  ? 4323 LEU A O     1 
ATOM   21264 C  CB    . LEU A 1 4323 ? 153.619 181.258 219.361 1.00 1.80  ? 4323 LEU A CB    1 
ATOM   21265 C  CG    . LEU A 1 4323 ? 154.361 182.178 218.390 1.00 1.36  ? 4323 LEU A CG    1 
ATOM   21266 C  CD1   . LEU A 1 4323 ? 155.538 182.843 219.076 1.00 1.83  ? 4323 LEU A CD1   1 
ATOM   21267 C  CD2   . LEU A 1 4323 ? 154.824 181.400 217.170 1.00 1.65  ? 4323 LEU A CD2   1 
ATOM   21268 N  N     . PRO A 1 4324 ? 152.336 178.367 219.415 1.00 3.76  ? 4324 PRO A N     1 
ATOM   21269 C  CA    . PRO A 1 4324 ? 152.120 177.221 220.304 1.00 4.68  ? 4324 PRO A CA    1 
ATOM   21270 C  C     . PRO A 1 4324 ? 152.841 177.410 221.629 1.00 4.55  ? 4324 PRO A C     1 
ATOM   21271 O  O     . PRO A 1 4324 ? 153.887 178.059 221.709 1.00 4.53  ? 4324 PRO A O     1 
ATOM   21272 C  CB    . PRO A 1 4324 ? 152.698 176.043 219.513 1.00 3.26  ? 4324 PRO A CB    1 
ATOM   21273 C  CG    . PRO A 1 4324 ? 153.672 176.657 218.572 1.00 3.82  ? 4324 PRO A CG    1 
ATOM   21274 C  CD    . PRO A 1 4324 ? 153.112 178.001 218.217 1.00 2.16  ? 4324 PRO A CD    1 
ATOM   21275 N  N     . ASN A 1 4325 ? 152.264 176.830 222.681 1.00 4.34  ? 4325 ASN A N     1 
ATOM   21276 C  CA    . ASN A 1 4325 ? 152.818 176.984 224.021 1.00 4.42  ? 4325 ASN A CA    1 
ATOM   21277 C  C     . ASN A 1 4325 ? 154.154 176.278 224.208 1.00 6.67  ? 4325 ASN A C     1 
ATOM   21278 O  O     . ASN A 1 4325 ? 154.861 176.581 225.174 1.00 16.37 ? 4325 ASN A O     1 
ATOM   21279 C  CB    . ASN A 1 4325 ? 151.813 176.488 225.058 1.00 7.25  ? 4325 ASN A CB    1 
ATOM   21280 C  CG    . ASN A 1 4325 ? 150.919 177.595 225.563 1.00 6.76  ? 4325 ASN A CG    1 
ATOM   21281 O  OD1   . ASN A 1 4325 ? 151.149 178.765 225.272 1.00 9.78  ? 4325 ASN A OD1   1 
ATOM   21282 N  ND2   . ASN A 1 4325 ? 149.885 177.232 226.306 1.00 9.30  ? 4325 ASN A ND2   1 
ATOM   21283 N  N     . ASN A 1 4326 ? 154.522 175.365 223.314 1.00 6.68  ? 4326 ASN A N     1 
ATOM   21284 C  CA    . ASN A 1 4326 ? 155.821 174.710 223.384 1.00 5.10  ? 4326 ASN A CA    1 
ATOM   21285 C  C     . ASN A 1 4326 ? 156.944 175.559 222.803 1.00 6.75  ? 4326 ASN A C     1 
ATOM   21286 O  O     . ASN A 1 4326 ? 158.106 175.146 222.869 1.00 11.38 ? 4326 ASN A O     1 
ATOM   21287 C  CB    . ASN A 1 4326 ? 155.773 173.360 222.663 1.00 6.15  ? 4326 ASN A CB    1 
ATOM   21288 C  CG    . ASN A 1 4326 ? 155.367 173.488 221.209 1.00 8.54  ? 4326 ASN A CG    1 
ATOM   21289 O  OD1   . ASN A 1 4326 ? 156.129 173.980 220.379 1.00 9.98  ? 4326 ASN A OD1   1 
ATOM   21290 N  ND2   . ASN A 1 4326 ? 154.160 173.040 220.894 1.00 11.52 ? 4326 ASN A ND2   1 
ATOM   21291 N  N     . ALA A 1 4327 ? 156.625 176.723 222.231 1.00 4.20  ? 4327 ALA A N     1 
ATOM   21292 C  CA    . ALA A 1 4327 ? 157.652 177.563 221.623 1.00 4.21  ? 4327 ALA A CA    1 
ATOM   21293 C  C     . ALA A 1 4327 ? 158.660 178.060 222.649 1.00 6.06  ? 4327 ALA A C     1 
ATOM   21294 O  O     . ALA A 1 4327 ? 159.820 178.307 222.305 1.00 10.16 ? 4327 ALA A O     1 
ATOM   21295 C  CB    . ALA A 1 4327 ? 157.004 178.744 220.902 1.00 5.13  ? 4327 ALA A CB    1 
ATOM   21296 N  N     . GLU A 1 4328 ? 158.241 178.218 223.901 1.00 7.23  ? 4328 GLU A N     1 
ATOM   21297 C  CA    . GLU A 1 4328 ? 159.123 178.703 224.952 1.00 5.29  ? 4328 GLU A CA    1 
ATOM   21298 C  C     . GLU A 1 4328 ? 159.839 177.588 225.705 1.00 7.27  ? 4328 GLU A C     1 
ATOM   21299 O  O     . GLU A 1 4328 ? 160.700 177.888 226.536 1.00 10.02 ? 4328 GLU A O     1 
ATOM   21300 C  CB    . GLU A 1 4328 ? 158.330 179.561 225.945 1.00 6.11  ? 4328 GLU A CB    1 
ATOM   21301 C  CG    . GLU A 1 4328 ? 157.578 178.759 226.996 1.00 6.44  ? 4328 GLU A CG    1 
ATOM   21302 C  CD    . GLU A 1 4328 ? 156.610 179.603 227.800 1.00 11.65 ? 4328 GLU A CD    1 
ATOM   21303 O  OE1   . GLU A 1 4328 ? 156.915 180.787 228.054 1.00 10.92 ? 4328 GLU A OE1   1 
ATOM   21304 O  OE2   . GLU A 1 4328 ? 155.541 179.082 228.182 1.00 18.41 ? 4328 GLU A OE2   1 
ATOM   21305 N  N     . ARG A 1 4329 ? 159.525 176.321 225.423 1.00 5.13  ? 4329 ARG A N     1 
ATOM   21306 C  CA    . ARG A 1 4329 ? 160.063 175.223 226.222 1.00 6.13  ? 4329 ARG A CA    1 
ATOM   21307 C  C     . ARG A 1 4329 ? 161.582 175.153 226.132 1.00 6.74  ? 4329 ARG A C     1 
ATOM   21308 O  O     . ARG A 1 4329 ? 162.272 175.079 227.154 1.00 10.81 ? 4329 ARG A O     1 
ATOM   21309 C  CB    . ARG A 1 4329 ? 159.438 173.900 225.783 1.00 5.14  ? 4329 ARG A CB    1 
ATOM   21310 C  CG    . ARG A 1 4329 ? 159.241 172.912 226.915 1.00 5.12  ? 4329 ARG A CG    1 
ATOM   21311 C  CD    . ARG A 1 4329 ? 158.921 171.525 226.388 1.00 11.28 ? 4329 ARG A CD    1 
ATOM   21312 N  NE    . ARG A 1 4329 ? 158.689 170.559 227.456 1.00 17.14 ? 4329 ARG A NE    1 
ATOM   21313 C  CZ    . ARG A 1 4329 ? 157.623 170.549 228.244 1.00 12.06 ? 4329 ARG A CZ    1 
ATOM   21314 N  NH1   . ARG A 1 4329 ? 156.659 171.445 228.120 1.00 10.66 ? 4329 ARG A NH1   1 
ATOM   21315 N  NH2   . ARG A 1 4329 ? 157.519 169.607 229.179 1.00 14.09 ? 4329 ARG A NH2   1 
ATOM   21316 N  N     . VAL A 1 4330 ? 162.123 175.166 224.914 1.00 5.83  ? 4330 VAL A N     1 
ATOM   21317 C  CA    . VAL A 1 4330 ? 163.571 175.104 224.749 1.00 7.01  ? 4330 VAL A CA    1 
ATOM   21318 C  C     . VAL A 1 4330 ? 164.220 176.393 225.240 1.00 7.93  ? 4330 VAL A C     1 
ATOM   21319 O  O     . VAL A 1 4330 ? 165.264 176.369 225.901 1.00 7.02  ? 4330 VAL A O     1 
ATOM   21320 C  CB    . VAL A 1 4330 ? 163.924 174.809 223.281 1.00 2.88  ? 4330 VAL A CB    1 
ATOM   21321 C  CG1   . VAL A 1 4330 ? 165.399 175.053 223.022 1.00 1.55  ? 4330 VAL A CG1   1 
ATOM   21322 C  CG2   . VAL A 1 4330 ? 163.540 173.382 222.924 1.00 2.74  ? 4330 VAL A CG2   1 
ATOM   21323 N  N     . LEU A 1 4331 ? 163.604 177.536 224.931 1.00 7.46  ? 4331 LEU A N     1 
ATOM   21324 C  CA    . LEU A 1 4331 ? 164.153 178.823 225.344 1.00 7.04  ? 4331 LEU A CA    1 
ATOM   21325 C  C     . LEU A 1 4331 ? 164.195 178.947 226.864 1.00 6.90  ? 4331 LEU A C     1 
ATOM   21326 O  O     . LEU A 1 4331 ? 165.174 179.453 227.424 1.00 8.01  ? 4331 LEU A O     1 
ATOM   21327 C  CB    . LEU A 1 4331 ? 163.330 179.949 224.712 1.00 11.67 ? 4331 LEU A CB    1 
ATOM   21328 C  CG    . LEU A 1 4331 ? 163.740 181.419 224.808 1.00 15.57 ? 4331 LEU A CG    1 
ATOM   21329 C  CD1   . LEU A 1 4331 ? 163.185 182.169 223.617 1.00 11.69 ? 4331 LEU A CD1   1 
ATOM   21330 C  CD2   . LEU A 1 4331 ? 163.194 182.039 226.070 1.00 12.69 ? 4331 LEU A CD2   1 
ATOM   21331 N  N     . LEU A 1 4332 ? 163.142 178.493 227.546 1.00 5.46  ? 4332 LEU A N     1 
ATOM   21332 C  CA    . LEU A 1 4332 ? 163.142 178.517 229.007 1.00 5.74  ? 4332 LEU A CA    1 
ATOM   21333 C  C     . LEU A 1 4332 ? 164.160 177.540 229.580 1.00 6.46  ? 4332 LEU A C     1 
ATOM   21334 O  O     . LEU A 1 4332 ? 164.841 177.851 230.563 1.00 6.98  ? 4332 LEU A O     1 
ATOM   21335 C  CB    . LEU A 1 4332 ? 161.746 178.208 229.541 1.00 6.79  ? 4332 LEU A CB    1 
ATOM   21336 C  CG    . LEU A 1 4332 ? 160.692 179.305 229.395 1.00 3.85  ? 4332 LEU A CG    1 
ATOM   21337 C  CD1   . LEU A 1 4332 ? 159.404 178.903 230.090 1.00 2.55  ? 4332 LEU A CD1   1 
ATOM   21338 C  CD2   . LEU A 1 4332 ? 161.215 180.623 229.933 1.00 1.74  ? 4332 LEU A CD2   1 
ATOM   21339 N  N     . THR A 1 4333 ? 164.270 176.350 228.984 1.00 8.61  ? 4333 THR A N     1 
ATOM   21340 C  CA    . THR A 1 4333 ? 165.190 175.339 229.495 1.00 6.68  ? 4333 THR A CA    1 
ATOM   21341 C  C     . THR A 1 4333 ? 166.636 175.810 229.408 1.00 5.54  ? 4333 THR A C     1 
ATOM   21342 O  O     . THR A 1 4333 ? 167.428 175.578 230.329 1.00 6.70  ? 4333 THR A O     1 
ATOM   21343 C  CB    . THR A 1 4333 ? 164.998 174.029 228.729 1.00 6.48  ? 4333 THR A CB    1 
ATOM   21344 O  OG1   . THR A 1 4333 ? 163.627 173.623 228.818 1.00 6.19  ? 4333 THR A OG1   1 
ATOM   21345 C  CG2   . THR A 1 4333 ? 165.877 172.933 229.305 1.00 4.85  ? 4333 THR A CG2   1 
ATOM   21346 N  N     . THR A 1 4334 ? 167.000 176.472 228.308 1.00 3.81  ? 4334 THR A N     1 
ATOM   21347 C  CA    . THR A 1 4334 ? 168.360 176.981 228.168 1.00 4.04  ? 4334 THR A CA    1 
ATOM   21348 C  C     . THR A 1 4334 ? 168.659 178.059 229.205 1.00 7.73  ? 4334 THR A C     1 
ATOM   21349 O  O     . THR A 1 4334 ? 169.745 178.073 229.794 1.00 6.92  ? 4334 THR A O     1 
ATOM   21350 C  CB    . THR A 1 4334 ? 168.578 177.521 226.755 1.00 5.97  ? 4334 THR A CB    1 
ATOM   21351 O  OG1   . THR A 1 4334 ? 168.184 176.533 225.797 1.00 8.21  ? 4334 THR A OG1   1 
ATOM   21352 C  CG2   . THR A 1 4334 ? 170.040 177.865 226.539 1.00 5.09  ? 4334 THR A CG2   1 
ATOM   21353 N  N     . GLN A 1 4335 ? 167.709 178.967 229.443 1.00 9.22  ? 4335 GLN A N     1 
ATOM   21354 C  CA    . GLN A 1 4335 ? 167.932 180.021 230.429 1.00 4.92  ? 4335 GLN A CA    1 
ATOM   21355 C  C     . GLN A 1 4335 ? 168.085 179.448 231.830 1.00 4.79  ? 4335 GLN A C     1 
ATOM   21356 O  O     . GLN A 1 4335 ? 168.924 179.914 232.610 1.00 8.43  ? 4335 GLN A O     1 
ATOM   21357 C  CB    . GLN A 1 4335 ? 166.792 181.037 230.404 1.00 7.32  ? 4335 GLN A CB    1 
ATOM   21358 C  CG    . GLN A 1 4335 ? 166.882 182.078 229.313 1.00 5.37  ? 4335 GLN A CG    1 
ATOM   21359 C  CD    . GLN A 1 4335 ? 165.718 183.046 229.359 1.00 16.23 ? 4335 GLN A CD    1 
ATOM   21360 O  OE1   . GLN A 1 4335 ? 165.837 184.151 229.890 1.00 12.65 ? 4335 GLN A OE1   1 
ATOM   21361 N  NE2   . GLN A 1 4335 ? 164.575 182.622 228.839 1.00 10.43 ? 4335 GLN A NE2   1 
ATOM   21362 N  N     . GLY A 1 4336 ? 167.272 178.447 232.174 1.00 5.57  ? 4336 GLY A N     1 
ATOM   21363 C  CA    . GLY A 1 4336 ? 167.405 177.817 233.476 1.00 4.61  ? 4336 GLY A CA    1 
ATOM   21364 C  C     . GLY A 1 4336 ? 168.776 177.206 233.684 1.00 6.90  ? 4336 GLY A C     1 
ATOM   21365 O  O     . GLY A 1 4336 ? 169.370 177.337 234.756 1.00 8.63  ? 4336 GLY A O     1 
ATOM   21366 N  N     . VAL A 1 4337 ? 169.298 176.530 232.658 1.00 5.99  ? 4337 VAL A N     1 
ATOM   21367 C  CA    . VAL A 1 4337 ? 170.670 176.038 232.715 1.00 6.75  ? 4337 VAL A CA    1 
ATOM   21368 C  C     . VAL A 1 4337 ? 171.650 177.206 232.720 1.00 7.54  ? 4337 VAL A C     1 
ATOM   21369 O  O     . VAL A 1 4337 ? 172.690 177.161 233.387 1.00 7.98  ? 4337 VAL A O     1 
ATOM   21370 C  CB    . VAL A 1 4337 ? 170.931 175.071 231.547 1.00 4.01  ? 4337 VAL A CB    1 
ATOM   21371 C  CG1   . VAL A 1 4337 ? 172.394 174.678 231.484 1.00 7.18  ? 4337 VAL A CG1   1 
ATOM   21372 C  CG2   . VAL A 1 4337 ? 170.049 173.841 231.676 1.00 4.85  ? 4337 VAL A CG2   1 
ATOM   21373 N  N     . ASP A 1 4338 ? 171.326 178.273 231.986 1.00 7.87  ? 4338 ASP A N     1 
ATOM   21374 C  CA    . ASP A 1 4338 ? 172.170 179.463 231.983 1.00 5.70  ? 4338 ASP A CA    1 
ATOM   21375 C  C     . ASP A 1 4338 ? 172.229 180.104 233.366 1.00 7.48  ? 4338 ASP A C     1 
ATOM   21376 O  O     . ASP A 1 4338 ? 173.286 180.579 233.793 1.00 6.13  ? 4338 ASP A O     1 
ATOM   21377 C  CB    . ASP A 1 4338 ? 171.657 180.457 230.940 1.00 8.21  ? 4338 ASP A CB    1 
ATOM   21378 C  CG    . ASP A 1 4338 ? 172.463 181.737 230.902 1.00 20.85 ? 4338 ASP A CG    1 
ATOM   21379 O  OD1   . ASP A 1 4338 ? 173.672 181.677 230.597 1.00 21.50 ? 4338 ASP A OD1   1 
ATOM   21380 O  OD2   . ASP A 1 4338 ? 171.878 182.809 231.171 1.00 26.54 ? 4338 ASP A OD2   1 
ATOM   21381 N  N     . MET A 1 4339 ? 171.100 180.126 234.080 1.00 7.96  ? 4339 MET A N     1 
ATOM   21382 C  CA    . MET A 1 4339 ? 171.094 180.660 235.439 1.00 5.73  ? 4339 MET A CA    1 
ATOM   21383 C  C     . MET A 1 4339 ? 171.968 179.825 236.367 1.00 9.02  ? 4339 MET A C     1 
ATOM   21384 O  O     . MET A 1 4339 ? 172.672 180.371 237.224 1.00 9.85  ? 4339 MET A O     1 
ATOM   21385 C  CB    . MET A 1 4339 ? 169.663 180.733 235.971 1.00 6.62  ? 4339 MET A CB    1 
ATOM   21386 C  CG    . MET A 1 4339 ? 169.574 180.974 237.468 1.00 8.27  ? 4339 MET A CG    1 
ATOM   21387 S  SD    . MET A 1 4339 ? 167.887 181.059 238.088 1.00 21.56 ? 4339 MET A SD    1 
ATOM   21388 C  CE    . MET A 1 4339 ? 167.465 179.321 238.143 1.00 4.85  ? 4339 MET A CE    1 
ATOM   21389 N  N     . ILE A 1 4340 ? 171.932 178.498 236.216 1.00 10.86 ? 4340 ILE A N     1 
ATOM   21390 C  CA    . ILE A 1 4340 ? 172.779 177.634 237.035 1.00 8.64  ? 4340 ILE A CA    1 
ATOM   21391 C  C     . ILE A 1 4340 ? 174.249 177.913 236.762 1.00 7.80  ? 4340 ILE A C     1 
ATOM   21392 O  O     . ILE A 1 4340 ? 175.059 178.023 237.690 1.00 9.48  ? 4340 ILE A O     1 
ATOM   21393 C  CB    . ILE A 1 4340 ? 172.437 176.153 236.786 1.00 12.01 ? 4340 ILE A CB    1 
ATOM   21394 C  CG1   . ILE A 1 4340 ? 170.972 175.876 237.108 1.00 8.09  ? 4340 ILE A CG1   1 
ATOM   21395 C  CG2   . ILE A 1 4340 ? 173.337 175.254 237.621 1.00 9.46  ? 4340 ILE A CG2   1 
ATOM   21396 C  CD1   . ILE A 1 4340 ? 170.620 176.139 238.531 1.00 8.86  ? 4340 ILE A CD1   1 
ATOM   21397 N  N     . SER A 1 4341 ? 174.617 178.029 235.484 1.00 6.56  ? 4341 SER A N     1 
ATOM   21398 C  CA    . SER A 1 4341 ? 176.010 178.282 235.131 1.00 5.56  ? 4341 SER A CA    1 
ATOM   21399 C  C     . SER A 1 4341 ? 176.485 179.621 235.678 1.00 8.64  ? 4341 SER A C     1 
ATOM   21400 O  O     . SER A 1 4341 ? 177.613 179.736 236.167 1.00 9.58  ? 4341 SER A O     1 
ATOM   21401 C  CB    . SER A 1 4341 ? 176.181 178.232 233.613 1.00 8.21  ? 4341 SER A CB    1 
ATOM   21402 O  OG    . SER A 1 4341 ? 175.899 176.938 233.113 1.00 20.12 ? 4341 SER A OG    1 
ATOM   21403 N  N     . LYS A 1 4342 ? 175.638 180.648 235.591 1.00 8.56  ? 4342 LYS A N     1 
ATOM   21404 C  CA    . LYS A 1 4342 ? 176.011 181.963 236.099 1.00 5.59  ? 4342 LYS A CA    1 
ATOM   21405 C  C     . LYS A 1 4342 ? 176.131 181.961 237.617 1.00 8.13  ? 4342 LYS A C     1 
ATOM   21406 O  O     . LYS A 1 4342 ? 177.058 182.560 238.172 1.00 7.80  ? 4342 LYS A O     1 
ATOM   21407 C  CB    . LYS A 1 4342 ? 174.999 183.008 235.633 1.00 4.60  ? 4342 LYS A CB    1 
ATOM   21408 C  CG    . LYS A 1 4342 ? 175.302 183.584 234.263 1.00 5.34  ? 4342 LYS A CG    1 
ATOM   21409 C  CD    . LYS A 1 4342 ? 174.038 183.957 233.513 1.00 8.05  ? 4342 LYS A CD    1 
ATOM   21410 C  CE    . LYS A 1 4342 ? 174.370 184.525 232.143 1.00 9.82  ? 4342 LYS A CE    1 
ATOM   21411 N  NZ    . LYS A 1 4342 ? 173.182 185.153 231.504 1.00 11.52 ? 4342 LYS A NZ    1 
ATOM   21412 N  N     . MET A 1 4343 ? 175.202 181.293 238.306 1.00 7.34  ? 4343 MET A N     1 
ATOM   21413 C  CA    . MET A 1 4343 ? 175.288 181.196 239.760 1.00 5.49  ? 4343 MET A CA    1 
ATOM   21414 C  C     . MET A 1 4343 ? 176.535 180.435 240.185 1.00 9.93  ? 4343 MET A C     1 
ATOM   21415 O  O     . MET A 1 4343 ? 177.225 180.835 241.129 1.00 15.34 ? 4343 MET A O     1 
ATOM   21416 C  CB    . MET A 1 4343 ? 174.037 180.519 240.320 1.00 5.94  ? 4343 MET A CB    1 
ATOM   21417 C  CG    . MET A 1 4343 ? 172.906 181.471 240.664 1.00 4.04  ? 4343 MET A CG    1 
ATOM   21418 S  SD    . MET A 1 4343 ? 171.385 180.598 241.079 1.00 14.49 ? 4343 MET A SD    1 
ATOM   21419 C  CE    . MET A 1 4343 ? 171.873 179.771 242.590 1.00 9.12  ? 4343 MET A CE    1 
ATOM   21420 N  N     . LEU A 1 4344 ? 176.838 179.332 239.497 1.00 11.76 ? 4344 LEU A N     1 
ATOM   21421 C  CA    . LEU A 1 4344 ? 178.017 178.541 239.829 1.00 13.22 ? 4344 LEU A CA    1 
ATOM   21422 C  C     . LEU A 1 4344 ? 179.298 179.331 239.601 1.00 12.83 ? 4344 LEU A C     1 
ATOM   21423 O  O     . LEU A 1 4344 ? 180.241 179.237 240.394 1.00 17.02 ? 4344 LEU A O     1 
ATOM   21424 C  CB    . LEU A 1 4344 ? 178.029 177.255 239.007 1.00 11.49 ? 4344 LEU A CB    1 
ATOM   21425 C  CG    . LEU A 1 4344 ? 179.100 176.222 239.356 1.00 18.43 ? 4344 LEU A CG    1 
ATOM   21426 C  CD1   . LEU A 1 4344 ? 179.092 175.902 240.845 1.00 14.71 ? 4344 LEU A CD1   1 
ATOM   21427 C  CD2   . LEU A 1 4344 ? 178.901 174.967 238.524 1.00 18.11 ? 4344 LEU A CD2   1 
ATOM   21428 N  N     . LYS A 1 4345 ? 179.352 180.104 238.516 1.00 8.45  ? 4345 LYS A N     1 
ATOM   21429 C  CA    . LYS A 1 4345 ? 180.558 180.861 238.201 1.00 8.52  ? 4345 LYS A CA    1 
ATOM   21430 C  C     . LYS A 1 4345 ? 180.855 181.903 239.273 1.00 15.62 ? 4345 LYS A C     1 
ATOM   21431 O  O     . LYS A 1 4345 ? 182.019 182.130 239.621 1.00 24.37 ? 4345 LYS A O     1 
ATOM   21432 C  CB    . LYS A 1 4345 ? 180.416 181.514 236.828 1.00 8.34  ? 4345 LYS A CB    1 
ATOM   21433 C  CG    . LYS A 1 4345 ? 181.619 182.325 236.396 1.00 14.75 ? 4345 LYS A CG    1 
ATOM   21434 C  CD    . LYS A 1 4345 ? 181.375 183.017 235.067 1.00 17.13 ? 4345 LYS A CD    1 
ATOM   21435 C  CE    . LYS A 1 4345 ? 180.856 182.042 234.023 1.00 17.16 ? 4345 LYS A CE    1 
ATOM   21436 N  NZ    . LYS A 1 4345 ? 180.501 182.729 232.751 1.00 18.07 ? 4345 LYS A NZ    1 
ATOM   21437 N  N     . MET A 1 4346 ? 179.818 182.550 239.809 1.00 10.37 ? 4346 MET A N     1 
ATOM   21438 C  CA    . MET A 1 4346 ? 180.040 183.551 240.846 1.00 10.14 ? 4346 MET A CA    1 
ATOM   21439 C  C     . MET A 1 4346 ? 180.345 182.938 242.209 1.00 13.13 ? 4346 MET A C     1 
ATOM   21440 O  O     . MET A 1 4346 ? 180.774 183.664 243.111 1.00 17.05 ? 4346 MET A O     1 
ATOM   21441 C  CB    . MET A 1 4346 ? 178.840 184.494 240.951 1.00 7.76  ? 4346 MET A CB    1 
ATOM   21442 C  CG    . MET A 1 4346 ? 178.851 185.609 239.918 1.00 8.37  ? 4346 MET A CG    1 
ATOM   21443 S  SD    . MET A 1 4346 ? 177.341 186.589 239.856 1.00 13.73 ? 4346 MET A SD    1 
ATOM   21444 C  CE    . MET A 1 4346 ? 176.139 185.339 239.442 1.00 6.00  ? 4346 MET A CE    1 
ATOM   21445 N  N     . GLN A 1 4347 ? 180.137 181.636 242.386 1.00 15.79 ? 4347 GLN A N     1 
ATOM   21446 C  CA    . GLN A 1 4347 ? 180.513 180.988 243.641 1.00 14.66 ? 4347 GLN A CA    1 
ATOM   21447 C  C     . GLN A 1 4347 ? 182.029 180.884 243.748 1.00 17.72 ? 4347 GLN A C     1 
ATOM   21448 O  O     . GLN A 1 4347 ? 182.714 180.636 242.756 1.00 25.57 ? 4347 GLN A O     1 
ATOM   21449 C  CB    . GLN A 1 4347 ? 179.885 179.597 243.767 1.00 14.76 ? 4347 GLN A CB    1 
ATOM   21450 C  CG    . GLN A 1 4347 ? 178.370 179.586 243.861 1.00 21.77 ? 4347 GLN A CG    1 
ATOM   21451 C  CD    . GLN A 1 4347 ? 177.855 180.303 245.093 1.00 27.16 ? 4347 GLN A CD    1 
ATOM   21452 O  OE1   . GLN A 1 4347 ? 177.272 181.383 244.998 1.00 23.78 ? 4347 GLN A OE1   1 
ATOM   21453 N  NE2   . GLN A 1 4347 ? 178.074 179.708 246.259 1.00 25.08 ? 4347 GLN A NE2   1 
ATOM   21454 N  N     . PRO A 1 4374 ? 202.567 165.295 220.995 1.00 28.80 ? 4374 PRO A N     1 
ATOM   21455 C  CA    . PRO A 1 4374 ? 201.607 165.999 221.854 1.00 27.17 ? 4374 PRO A CA    1 
ATOM   21456 C  C     . PRO A 1 4374 ? 200.269 165.271 221.961 1.00 31.60 ? 4374 PRO A C     1 
ATOM   21457 O  O     . PRO A 1 4374 ? 199.980 164.397 221.146 1.00 34.84 ? 4374 PRO A O     1 
ATOM   21458 C  CB    . PRO A 1 4374 ? 201.435 167.354 221.158 1.00 28.26 ? 4374 PRO A CB    1 
ATOM   21459 C  CG    . PRO A 1 4374 ? 202.650 167.508 220.306 1.00 28.60 ? 4374 PRO A CG    1 
ATOM   21460 C  CD    . PRO A 1 4374 ? 203.003 166.126 219.862 1.00 32.59 ? 4374 PRO A CD    1 
ATOM   21461 N  N     . ALA A 1 4375 ? 199.474 165.631 222.969 1.00 27.35 ? 4375 ALA A N     1 
ATOM   21462 C  CA    . ALA A 1 4375 ? 198.171 164.997 223.150 1.00 28.87 ? 4375 ALA A CA    1 
ATOM   21463 C  C     . ALA A 1 4375 ? 197.237 165.307 221.988 1.00 36.31 ? 4375 ALA A C     1 
ATOM   21464 O  O     . ALA A 1 4375 ? 196.504 164.427 221.523 1.00 35.68 ? 4375 ALA A O     1 
ATOM   21465 C  CB    . ALA A 1 4375 ? 197.550 165.442 224.474 1.00 30.19 ? 4375 ALA A CB    1 
ATOM   21466 N  N     . TRP A 1 4376 ? 197.245 166.554 221.511 1.00 35.34 ? 4376 TRP A N     1 
ATOM   21467 C  CA    . TRP A 1 4376 ? 196.401 166.917 220.376 1.00 27.87 ? 4376 TRP A CA    1 
ATOM   21468 C  C     . TRP A 1 4376 ? 196.809 166.161 219.119 1.00 28.33 ? 4376 TRP A C     1 
ATOM   21469 O  O     . TRP A 1 4376 ? 195.955 165.790 218.306 1.00 29.74 ? 4376 TRP A O     1 
ATOM   21470 C  CB    . TRP A 1 4376 ? 196.458 168.431 220.146 1.00 26.45 ? 4376 TRP A CB    1 
ATOM   21471 C  CG    . TRP A 1 4376 ? 197.738 168.912 219.524 1.00 28.68 ? 4376 TRP A CG    1 
ATOM   21472 C  CD1   . TRP A 1 4376 ? 198.816 169.430 220.177 1.00 31.83 ? 4376 TRP A CD1   1 
ATOM   21473 C  CD2   . TRP A 1 4376 ? 198.069 168.929 218.128 1.00 34.56 ? 4376 TRP A CD2   1 
ATOM   21474 N  NE1   . TRP A 1 4376 ? 199.800 169.761 219.278 1.00 32.93 ? 4376 TRP A NE1   1 
ATOM   21475 C  CE2   . TRP A 1 4376 ? 199.366 169.463 218.014 1.00 30.99 ? 4376 TRP A CE2   1 
ATOM   21476 C  CE3   . TRP A 1 4376 ? 197.396 168.538 216.966 1.00 26.84 ? 4376 TRP A CE3   1 
ATOM   21477 C  CZ2   . TRP A 1 4376 ? 200.004 169.619 216.786 1.00 27.23 ? 4376 TRP A CZ2   1 
ATOM   21478 C  CZ3   . TRP A 1 4376 ? 198.032 168.689 215.750 1.00 26.15 ? 4376 TRP A CZ3   1 
ATOM   21479 C  CH2   . TRP A 1 4376 ? 199.322 169.227 215.669 1.00 31.72 ? 4376 TRP A CH2   1 
ATOM   21480 N  N     . MET A 1 4377 ? 198.110 165.926 218.941 1.00 28.90 ? 4377 MET A N     1 
ATOM   21481 C  CA    . MET A 1 4377 ? 198.587 165.274 217.727 1.00 31.85 ? 4377 MET A CA    1 
ATOM   21482 C  C     . MET A 1 4377 ? 198.067 163.844 217.630 1.00 29.33 ? 4377 MET A C     1 
ATOM   21483 O  O     . MET A 1 4377 ? 197.725 163.373 216.539 1.00 31.06 ? 4377 MET A O     1 
ATOM   21484 C  CB    . MET A 1 4377 ? 200.114 165.313 217.690 1.00 27.30 ? 4377 MET A CB    1 
ATOM   21485 C  CG    . MET A 1 4377 ? 200.748 164.755 216.426 1.00 32.12 ? 4377 MET A CG    1 
ATOM   21486 S  SD    . MET A 1 4377 ? 202.541 164.961 216.471 1.00 53.08 ? 4377 MET A SD    1 
ATOM   21487 C  CE    . MET A 1 4377 ? 203.037 164.155 214.953 1.00 33.00 ? 4377 MET A CE    1 
ATOM   21488 N  N     . ARG A 1 4378 ? 197.999 163.138 218.761 1.00 29.78 ? 4378 ARG A N     1 
ATOM   21489 C  CA    . ARG A 1 4378 ? 197.472 161.776 218.752 1.00 27.30 ? 4378 ARG A CA    1 
ATOM   21490 C  C     . ARG A 1 4378 ? 195.953 161.762 218.609 1.00 26.83 ? 4378 ARG A C     1 
ATOM   21491 O  O     . ARG A 1 4378 ? 195.405 160.953 217.852 1.00 21.17 ? 4378 ARG A O     1 
ATOM   21492 C  CB    . ARG A 1 4378 ? 197.901 161.032 220.019 1.00 27.71 ? 4378 ARG A CB    1 
ATOM   21493 C  CG    . ARG A 1 4378 ? 199.272 160.357 219.941 1.00 27.51 ? 4378 ARG A CG    1 
ATOM   21494 C  CD    . ARG A 1 4378 ? 200.400 161.338 219.658 1.00 32.59 ? 4378 ARG A CD    1 
ATOM   21495 N  NE    . ARG A 1 4378 ? 201.677 160.662 219.455 1.00 34.52 ? 4378 ARG A NE    1 
ATOM   21496 C  CZ    . ARG A 1 4378 ? 202.816 161.280 219.176 1.00 37.22 ? 4378 ARG A CZ    1 
ATOM   21497 N  NH1   . ARG A 1 4378 ? 202.879 162.596 219.059 1.00 36.46 ? 4378 ARG A NH1   1 
ATOM   21498 N  NH2   . ARG A 1 4378 ? 203.922 160.558 219.010 1.00 30.14 ? 4378 ARG A NH2   1 
ATOM   21499 N  N     . THR A 1 4379 ? 195.256 162.645 219.330 1.00 26.96 ? 4379 THR A N     1 
ATOM   21500 C  CA    . THR A 1 4379 ? 193.796 162.660 219.273 1.00 26.64 ? 4379 THR A CA    1 
ATOM   21501 C  C     . THR A 1 4379 ? 193.293 163.043 217.886 1.00 26.99 ? 4379 THR A C     1 
ATOM   21502 O  O     . THR A 1 4379 ? 192.324 162.457 217.389 1.00 27.46 ? 4379 THR A O     1 
ATOM   21503 C  CB    . THR A 1 4379 ? 193.232 163.614 220.326 1.00 26.87 ? 4379 THR A CB    1 
ATOM   21504 O  OG1   . THR A 1 4379 ? 193.804 164.916 220.150 1.00 26.07 ? 4379 THR A OG1   1 
ATOM   21505 C  CG2   . THR A 1 4379 ? 193.539 163.108 221.730 1.00 30.30 ? 4379 THR A CG2   1 
ATOM   21506 N  N     . LEU A 1 4380 ? 193.934 164.025 217.251 1.00 24.54 ? 4380 LEU A N     1 
ATOM   21507 C  CA    . LEU A 1 4380 ? 193.510 164.439 215.919 1.00 21.53 ? 4380 LEU A CA    1 
ATOM   21508 C  C     . LEU A 1 4380 ? 193.795 163.363 214.877 1.00 19.90 ? 4380 LEU A C     1 
ATOM   21509 O  O     . LEU A 1 4380 ? 193.077 163.267 213.877 1.00 22.19 ? 4380 LEU A O     1 
ATOM   21510 C  CB    . LEU A 1 4380 ? 194.194 165.754 215.540 1.00 22.91 ? 4380 LEU A CB    1 
ATOM   21511 C  CG    . LEU A 1 4380 ? 193.822 166.414 214.209 1.00 18.77 ? 4380 LEU A CG    1 
ATOM   21512 C  CD1   . LEU A 1 4380 ? 192.317 166.451 214.027 1.00 14.91 ? 4380 LEU A CD1   1 
ATOM   21513 C  CD2   . LEU A 1 4380 ? 194.405 167.817 214.133 1.00 18.10 ? 4380 LEU A CD2   1 
ATOM   21514 N  N     . HIS A 1 4381 ? 194.834 162.551 215.091 1.00 20.68 ? 4381 HIS A N     1 
ATOM   21515 C  CA    . HIS A 1 4381 ? 195.134 161.478 214.149 1.00 27.62 ? 4381 HIS A CA    1 
ATOM   21516 C  C     . HIS A 1 4381 ? 194.009 160.453 214.098 1.00 22.73 ? 4381 HIS A C     1 
ATOM   21517 O  O     . HIS A 1 4381 ? 193.614 160.008 213.013 1.00 24.60 ? 4381 HIS A O     1 
ATOM   21518 C  CB    . HIS A 1 4381 ? 196.455 160.804 214.520 1.00 22.69 ? 4381 HIS A CB    1 
ATOM   21519 C  CG    . HIS A 1 4381 ? 196.816 159.658 213.629 1.00 23.95 ? 4381 HIS A CG    1 
ATOM   21520 N  ND1   . HIS A 1 4381 ? 196.323 158.384 213.816 1.00 32.87 ? 4381 HIS A ND1   1 
ATOM   21521 C  CD2   . HIS A 1 4381 ? 197.616 159.593 212.538 1.00 25.26 ? 4381 HIS A CD2   1 
ATOM   21522 C  CE1   . HIS A 1 4381 ? 196.806 157.585 212.882 1.00 26.92 ? 4381 HIS A CE1   1 
ATOM   21523 N  NE2   . HIS A 1 4381 ? 197.594 158.294 212.095 1.00 27.03 ? 4381 HIS A NE2   1 
ATOM   21524 N  N     . THR A 1 4382 ? 193.482 160.064 215.260 1.00 23.16 ? 4382 THR A N     1 
ATOM   21525 C  CA    . THR A 1 4382 ? 192.379 159.109 215.286 1.00 27.36 ? 4382 THR A CA    1 
ATOM   21526 C  C     . THR A 1 4382 ? 191.138 159.687 214.620 1.00 31.78 ? 4382 THR A C     1 
ATOM   21527 O  O     . THR A 1 4382 ? 190.453 158.994 213.859 1.00 31.91 ? 4382 THR A O     1 
ATOM   21528 C  CB    . THR A 1 4382 ? 192.068 158.702 216.726 1.00 27.48 ? 4382 THR A CB    1 
ATOM   21529 O  OG1   . THR A 1 4382 ? 191.778 159.872 217.500 1.00 31.37 ? 4382 THR A OG1   1 
ATOM   21530 C  CG2   . THR A 1 4382 ? 193.256 157.975 217.341 1.00 21.73 ? 4382 THR A CG2   1 
ATOM   21531 N  N     . THR A 1 4383 ? 190.839 160.959 214.891 1.00 23.27 ? 4383 THR A N     1 
ATOM   21532 C  CA    . THR A 1 4383 ? 189.640 161.581 214.339 1.00 22.89 ? 4383 THR A CA    1 
ATOM   21533 C  C     . THR A 1 4383 ? 189.706 161.671 212.819 1.00 25.72 ? 4383 THR A C     1 
ATOM   21534 O  O     . THR A 1 4383 ? 188.727 161.362 212.130 1.00 30.66 ? 4383 THR A O     1 
ATOM   21535 C  CB    . THR A 1 4383 ? 189.450 162.970 214.949 1.00 23.53 ? 4383 THR A CB    1 
ATOM   21536 O  OG1   . THR A 1 4383 ? 189.310 162.852 216.370 1.00 25.33 ? 4383 THR A OG1   1 
ATOM   21537 C  CG2   . THR A 1 4383 ? 188.205 163.632 214.384 1.00 19.64 ? 4383 THR A CG2   1 
ATOM   21538 N  N     . ALA A 1 4384 ? 190.850 162.093 212.279 1.00 27.56 ? 4384 ALA A N     1 
ATOM   21539 C  CA    . ALA A 1 4384 ? 190.978 162.228 210.831 1.00 23.39 ? 4384 ALA A CA    1 
ATOM   21540 C  C     . ALA A 1 4384 ? 190.931 160.871 210.140 1.00 26.45 ? 4384 ALA A C     1 
ATOM   21541 O  O     . ALA A 1 4384 ? 190.304 160.729 209.082 1.00 29.05 ? 4384 ALA A O     1 
ATOM   21542 C  CB    . ALA A 1 4384 ? 192.268 162.967 210.488 1.00 26.44 ? 4384 ALA A CB    1 
ATOM   21543 N  N     . SER A 1 4385 ? 191.591 159.863 210.714 1.00 29.10 ? 4385 SER A N     1 
ATOM   21544 C  CA    . SER A 1 4385 ? 191.530 158.521 210.143 1.00 29.93 ? 4385 SER A CA    1 
ATOM   21545 C  C     . SER A 1 4385 ? 190.108 157.974 210.182 1.00 29.86 ? 4385 SER A C     1 
ATOM   21546 O  O     . SER A 1 4385 ? 189.657 157.331 209.228 1.00 31.97 ? 4385 SER A O     1 
ATOM   21547 C  CB    . SER A 1 4385 ? 192.486 157.588 210.886 1.00 25.55 ? 4385 SER A CB    1 
ATOM   21548 O  OG    . SER A 1 4385 ? 193.823 158.045 210.794 1.00 29.63 ? 4385 SER A OG    1 
ATOM   21549 N  N     . ASN A 1 4386 ? 189.392 158.217 211.282 1.00 27.54 ? 4386 ASN A N     1 
ATOM   21550 C  CA    . ASN A 1 4386 ? 188.008 157.766 211.380 1.00 25.54 ? 4386 ASN A CA    1 
ATOM   21551 C  C     . ASN A 1 4386 ? 187.127 158.461 210.350 1.00 31.74 ? 4386 ASN A C     1 
ATOM   21552 O  O     . ASN A 1 4386 ? 186.257 157.829 209.741 1.00 34.18 ? 4386 ASN A O     1 
ATOM   21553 C  CB    . ASN A 1 4386 ? 187.477 158.008 212.793 1.00 23.82 ? 4386 ASN A CB    1 
ATOM   21554 C  CG    . ASN A 1 4386 ? 188.100 157.079 213.815 1.00 30.40 ? 4386 ASN A CG    1 
ATOM   21555 O  OD1   . ASN A 1 4386 ? 188.836 156.156 213.466 1.00 37.06 ? 4386 ASN A OD1   1 
ATOM   21556 N  ND2   . ASN A 1 4386 ? 187.813 157.323 215.087 1.00 31.13 ? 4386 ASN A ND2   1 
ATOM   21557 N  N     . TRP A 1 4387 ? 187.339 159.764 210.142 1.00 29.36 ? 4387 TRP A N     1 
ATOM   21558 C  CA    . TRP A 1 4387 ? 186.545 160.494 209.160 1.00 21.93 ? 4387 TRP A CA    1 
ATOM   21559 C  C     . TRP A 1 4387 ? 186.767 159.952 207.752 1.00 24.63 ? 4387 TRP A C     1 
ATOM   21560 O  O     . TRP A 1 4387 ? 185.832 159.907 206.944 1.00 33.54 ? 4387 TRP A O     1 
ATOM   21561 C  CB    . TRP A 1 4387 ? 186.874 161.985 209.218 1.00 18.72 ? 4387 TRP A CB    1 
ATOM   21562 C  CG    . TRP A 1 4387 ? 186.234 162.699 210.369 1.00 19.30 ? 4387 TRP A CG    1 
ATOM   21563 C  CD1   . TRP A 1 4387 ? 185.220 162.239 211.155 1.00 18.77 ? 4387 TRP A CD1   1 
ATOM   21564 C  CD2   . TRP A 1 4387 ? 186.555 164.007 210.853 1.00 18.47 ? 4387 TRP A CD2   1 
ATOM   21565 N  NE1   . TRP A 1 4387 ? 184.893 163.177 212.102 1.00 17.64 ? 4387 TRP A NE1   1 
ATOM   21566 C  CE2   . TRP A 1 4387 ? 185.698 164.272 211.938 1.00 15.98 ? 4387 TRP A CE2   1 
ATOM   21567 C  CE3   . TRP A 1 4387 ? 187.486 164.978 210.475 1.00 16.80 ? 4387 TRP A CE3   1 
ATOM   21568 C  CZ2   . TRP A 1 4387 ? 185.744 165.467 212.649 1.00 15.46 ? 4387 TRP A CZ2   1 
ATOM   21569 C  CZ3   . TRP A 1 4387 ? 187.529 166.163 211.182 1.00 18.32 ? 4387 TRP A CZ3   1 
ATOM   21570 C  CH2   . TRP A 1 4387 ? 186.666 166.397 212.257 1.00 21.01 ? 4387 TRP A CH2   1 
ATOM   21571 N  N     . LEU A 1 4388 ? 187.998 159.545 207.437 1.00 24.01 ? 4388 LEU A N     1 
ATOM   21572 C  CA    . LEU A 1 4388 ? 188.263 158.963 206.124 1.00 25.48 ? 4388 LEU A CA    1 
ATOM   21573 C  C     . LEU A 1 4388 ? 187.537 157.639 205.941 1.00 28.37 ? 4388 LEU A C     1 
ATOM   21574 O  O     . LEU A 1 4388 ? 187.265 157.234 204.805 1.00 28.62 ? 4388 LEU A O     1 
ATOM   21575 C  CB    . LEU A 1 4388 ? 189.765 158.779 205.919 1.00 23.10 ? 4388 LEU A CB    1 
ATOM   21576 C  CG    . LEU A 1 4388 ? 190.539 160.037 205.524 1.00 24.06 ? 4388 LEU A CG    1 
ATOM   21577 C  CD1   . LEU A 1 4388 ? 191.973 159.691 205.161 1.00 23.32 ? 4388 LEU A CD1   1 
ATOM   21578 C  CD2   . LEU A 1 4388 ? 189.846 160.747 204.373 1.00 27.84 ? 4388 LEU A CD2   1 
ATOM   21579 N  N     . HIS A 1 4389 ? 187.227 156.947 207.038 1.00 27.38 ? 4389 HIS A N     1 
ATOM   21580 C  CA    . HIS A 1 4389 ? 186.431 155.730 206.939 1.00 30.39 ? 4389 HIS A CA    1 
ATOM   21581 C  C     . HIS A 1 4389 ? 184.972 156.047 206.630 1.00 27.36 ? 4389 HIS A C     1 
ATOM   21582 O  O     . HIS A 1 4389 ? 184.359 155.396 205.777 1.00 28.17 ? 4389 HIS A O     1 
ATOM   21583 C  CB    . HIS A 1 4389 ? 186.545 154.923 208.232 1.00 27.90 ? 4389 HIS A CB    1 
ATOM   21584 C  CG    . HIS A 1 4389 ? 187.956 154.650 208.649 1.00 34.33 ? 4389 HIS A CG    1 
ATOM   21585 N  ND1   . HIS A 1 4389 ? 188.341 154.581 209.971 1.00 35.38 ? 4389 HIS A ND1   1 
ATOM   21586 C  CD2   . HIS A 1 4389 ? 189.073 154.422 207.919 1.00 33.90 ? 4389 HIS A CD2   1 
ATOM   21587 C  CE1   . HIS A 1 4389 ? 189.636 154.327 210.037 1.00 35.60 ? 4389 HIS A CE1   1 
ATOM   21588 N  NE2   . HIS A 1 4389 ? 190.104 154.225 208.806 1.00 39.97 ? 4389 HIS A NE2   1 
ATOM   21589 N  N     . LEU A 1 4390 ? 184.401 157.040 207.314 1.00 27.73 ? 4390 LEU A N     1 
ATOM   21590 C  CA    . LEU A 1 4390 ? 182.989 157.359 207.121 1.00 30.19 ? 4390 LEU A CA    1 
ATOM   21591 C  C     . LEU A 1 4390 ? 182.744 157.996 205.759 1.00 27.77 ? 4390 LEU A C     1 
ATOM   21592 O  O     . LEU A 1 4390 ? 181.820 157.605 205.037 1.00 31.74 ? 4390 LEU A O     1 
ATOM   21593 C  CB    . LEU A 1 4390 ? 182.502 158.284 208.238 1.00 24.19 ? 4390 LEU A CB    1 
ATOM   21594 C  CG    . LEU A 1 4390 ? 182.908 157.927 209.666 1.00 26.69 ? 4390 LEU A CG    1 
ATOM   21595 C  CD1   . LEU A 1 4390 ? 182.406 158.985 210.637 1.00 26.57 ? 4390 LEU A CD1   1 
ATOM   21596 C  CD2   . LEU A 1 4390 ? 182.386 156.550 210.050 1.00 24.74 ? 4390 LEU A CD2   1 
ATOM   21597 N  N     . ILE A 1 4391 ? 183.559 158.978 205.393 1.00 26.24 ? 4391 ILE A N     1 
ATOM   21598 C  CA    . ILE A 1 4391 ? 183.345 159.702 204.136 1.00 22.86 ? 4391 ILE A CA    1 
ATOM   21599 C  C     . ILE A 1 4391 ? 183.591 158.758 202.962 1.00 23.01 ? 4391 ILE A C     1 
ATOM   21600 O  O     . ILE A 1 4391 ? 184.602 158.035 202.954 1.00 25.69 ? 4391 ILE A O     1 
ATOM   21601 C  CB    . ILE A 1 4391 ? 184.261 160.927 204.065 1.00 21.76 ? 4391 ILE A CB    1 
ATOM   21602 C  CG1   . ILE A 1 4391 ? 183.918 161.912 205.184 1.00 21.22 ? 4391 ILE A CG1   1 
ATOM   21603 C  CG2   . ILE A 1 4391 ? 184.145 161.609 202.715 1.00 23.59 ? 4391 ILE A CG2   1 
ATOM   21604 C  CD1   . ILE A 1 4391 ? 184.927 163.026 205.356 1.00 25.23 ? 4391 ILE A CD1   1 
ATOM   21605 N  N     . PRO A 1 4392 ? 182.705 158.716 201.971 1.00 28.64 ? 4392 PRO A N     1 
ATOM   21606 C  CA    . PRO A 1 4392 ? 182.931 157.855 200.805 1.00 24.29 ? 4392 PRO A CA    1 
ATOM   21607 C  C     . PRO A 1 4392 ? 184.122 158.332 199.985 1.00 22.58 ? 4392 PRO A C     1 
ATOM   21608 O  O     . PRO A 1 4392 ? 184.644 159.434 200.162 1.00 30.43 ? 4392 PRO A O     1 
ATOM   21609 C  CB    . PRO A 1 4392 ? 181.623 157.972 200.018 1.00 26.82 ? 4392 PRO A CB    1 
ATOM   21610 C  CG    . PRO A 1 4392 ? 180.616 158.456 201.019 1.00 24.85 ? 4392 PRO A CG    1 
ATOM   21611 C  CD    . PRO A 1 4392 ? 181.382 159.358 201.928 1.00 27.76 ? 4392 PRO A CD    1 
ATOM   21612 N  N     . GLN A 1 4393 ? 184.548 157.470 199.061 1.00 24.24 ? 4393 GLN A N     1 
ATOM   21613 C  CA    . GLN A 1 4393 ? 185.784 157.685 198.325 1.00 23.31 ? 4393 GLN A CA    1 
ATOM   21614 C  C     . GLN A 1 4393 ? 185.607 157.876 196.825 1.00 27.76 ? 4393 GLN A C     1 
ATOM   21615 O  O     . GLN A 1 4393 ? 186.545 158.350 196.174 1.00 30.61 ? 4393 GLN A O     1 
ATOM   21616 C  CB    . GLN A 1 4393 ? 186.747 156.510 198.559 1.00 18.57 ? 4393 GLN A CB    1 
ATOM   21617 C  CG    . GLN A 1 4393 ? 186.648 155.899 199.946 1.00 24.48 ? 4393 GLN A CG    1 
ATOM   21618 C  CD    . GLN A 1 4393 ? 187.765 154.917 200.233 1.00 30.88 ? 4393 GLN A CD    1 
ATOM   21619 O  OE1   . GLN A 1 4393 ? 188.653 154.708 199.406 1.00 34.79 ? 4393 GLN A OE1   1 
ATOM   21620 N  NE2   . GLN A 1 4393 ? 187.726 154.304 201.409 1.00 26.22 ? 4393 GLN A NE2   1 
ATOM   21621 N  N     . THR A 1 4394 ? 184.450 157.539 196.257 1.00 24.20 ? 4394 THR A N     1 
ATOM   21622 C  CA    . THR A 1 4394 ? 184.262 157.560 194.813 1.00 25.92 ? 4394 THR A CA    1 
ATOM   21623 C  C     . THR A 1 4394 ? 183.064 158.422 194.442 1.00 24.61 ? 4394 THR A C     1 
ATOM   21624 O  O     . THR A 1 4394 ? 182.045 158.421 195.137 1.00 28.03 ? 4394 THR A O     1 
ATOM   21625 C  CB    . THR A 1 4394 ? 184.061 156.143 194.254 1.00 32.09 ? 4394 THR A CB    1 
ATOM   21626 O  OG1   . THR A 1 4394 ? 182.857 155.580 194.791 1.00 31.42 ? 4394 THR A OG1   1 
ATOM   21627 C  CG2   . THR A 1 4394 ? 185.239 155.251 194.622 1.00 25.83 ? 4394 THR A CG2   1 
ATOM   21628 N  N     . LEU A 1 4395 ? 183.195 159.159 193.336 1.00 21.76 ? 4395 LEU A N     1 
ATOM   21629 C  CA    . LEU A 1 4395 ? 182.080 159.935 192.793 1.00 24.22 ? 4395 LEU A CA    1 
ATOM   21630 C  C     . LEU A 1 4395 ? 182.358 160.138 191.303 1.00 29.48 ? 4395 LEU A C     1 
ATOM   21631 O  O     . LEU A 1 4395 ? 183.212 160.950 190.937 1.00 31.84 ? 4395 LEU A O     1 
ATOM   21632 C  CB    . LEU A 1 4395 ? 181.918 161.261 193.516 1.00 24.33 ? 4395 LEU A CB    1 
ATOM   21633 C  CG    . LEU A 1 4395 ? 180.533 161.903 193.409 1.00 23.03 ? 4395 LEU A CG    1 
ATOM   21634 C  CD1   . LEU A 1 4395 ? 179.445 160.862 193.634 1.00 25.94 ? 4395 LEU A CD1   1 
ATOM   21635 C  CD2   . LEU A 1 4395 ? 180.387 163.054 194.384 1.00 18.19 ? 4395 LEU A CD2   1 
ATOM   21636 N  N     . SER A 1 4396 ? 181.635 159.401 190.461 1.00 24.92 ? 4396 SER A N     1 
ATOM   21637 C  CA    . SER A 1 4396 ? 181.847 159.444 189.021 1.00 20.41 ? 4396 SER A CA    1 
ATOM   21638 C  C     . SER A 1 4396 ? 180.957 160.507 188.389 1.00 33.77 ? 4396 SER A C     1 
ATOM   21639 O  O     . SER A 1 4396 ? 179.749 160.548 188.643 1.00 34.85 ? 4396 SER A O     1 
ATOM   21640 C  CB    . SER A 1 4396 ? 181.565 158.077 188.397 1.00 23.65 ? 4396 SER A CB    1 
ATOM   21641 O  OG    . SER A 1 4396 ? 180.243 157.649 188.680 1.00 37.27 ? 4396 SER A OG    1 
ATOM   21642 N  N     . HIS A 1 4397 ? 181.559 161.361 187.564 1.00 26.56 ? 4397 HIS A N     1 
ATOM   21643 C  CA    . HIS A 1 4397 ? 180.810 162.404 186.882 1.00 21.31 ? 4397 HIS A CA    1 
ATOM   21644 C  C     . HIS A 1 4397 ? 179.804 161.799 185.910 1.00 33.21 ? 4397 HIS A C     1 
ATOM   21645 O  O     . HIS A 1 4397 ? 180.013 160.718 185.354 1.00 36.11 ? 4397 HIS A O     1 
ATOM   21646 C  CB    . HIS A 1 4397 ? 181.755 163.338 186.126 1.00 22.76 ? 4397 HIS A CB    1 
ATOM   21647 C  CG    . HIS A 1 4397 ? 182.501 164.292 187.006 1.00 29.92 ? 4397 HIS A CG    1 
ATOM   21648 N  ND1   . HIS A 1 4397 ? 182.769 165.591 186.633 1.00 34.59 ? 4397 HIS A ND1   1 
ATOM   21649 C  CD2   . HIS A 1 4397 ? 183.037 164.136 188.240 1.00 30.11 ? 4397 HIS A CD2   1 
ATOM   21650 C  CE1   . HIS A 1 4397 ? 183.437 166.195 187.599 1.00 29.47 ? 4397 HIS A CE1   1 
ATOM   21651 N  NE2   . HIS A 1 4397 ? 183.613 165.334 188.585 1.00 30.44 ? 4397 HIS A NE2   1 
ATOM   21652 N  N     . LEU A 1 4398 ? 178.695 162.508 185.719 1.00 29.60 ? 4398 LEU A N     1 
ATOM   21653 C  CA    . LEU A 1 4398 ? 177.696 162.082 184.750 1.00 24.69 ? 4398 LEU A CA    1 
ATOM   21654 C  C     . LEU A 1 4398 ? 178.245 162.216 183.335 1.00 25.43 ? 4398 LEU A C     1 
ATOM   21655 O  O     . LEU A 1 4398 ? 178.876 163.219 182.989 1.00 28.66 ? 4398 LEU A O     1 
ATOM   21656 C  CB    . LEU A 1 4398 ? 176.419 162.909 184.898 1.00 27.49 ? 4398 LEU A CB    1 
ATOM   21657 C  CG    . LEU A 1 4398 ? 175.717 162.934 186.259 1.00 28.48 ? 4398 LEU A CG    1 
ATOM   21658 C  CD1   . LEU A 1 4398 ? 174.349 163.586 186.136 1.00 22.45 ? 4398 LEU A CD1   1 
ATOM   21659 C  CD2   . LEU A 1 4398 ? 175.597 161.534 186.838 1.00 21.21 ? 4398 LEU A CD2   1 
ATOM   21660 N  N     . LYS A 1 4399 ? 177.999 161.201 182.513 1.00 30.00 ? 4399 LYS A N     1 
ATOM   21661 C  CA    . LYS A 1 4399 ? 178.488 161.197 181.140 1.00 26.14 ? 4399 LYS A CA    1 
ATOM   21662 C  C     . LYS A 1 4399 ? 177.592 162.074 180.276 1.00 25.76 ? 4399 LYS A C     1 
ATOM   21663 O  O     . LYS A 1 4399 ? 176.415 161.761 180.075 1.00 25.02 ? 4399 LYS A O     1 
ATOM   21664 C  CB    . LYS A 1 4399 ? 178.540 159.772 180.595 1.00 24.26 ? 4399 LYS A CB    1 
ATOM   21665 C  CG    . LYS A 1 4399 ? 179.049 159.677 179.166 1.00 22.39 ? 4399 LYS A CG    1 
ATOM   21666 C  CD    . LYS A 1 4399 ? 178.557 158.410 178.490 1.00 26.49 ? 4399 LYS A CD    1 
ATOM   21667 C  CE    . LYS A 1 4399 ? 177.044 158.400 178.360 1.00 25.59 ? 4399 LYS A CE    1 
ATOM   21668 N  NZ    . LYS A 1 4399 ? 176.554 157.169 177.684 1.00 29.58 ? 4399 LYS A NZ    1 
ATOM   21669 N  N     . ARG A 1 4400 ? 178.149 163.170 179.764 1.00 26.52 ? 4400 ARG A N     1 
ATOM   21670 C  CA    . ARG A 1 4400 ? 177.379 164.080 178.929 1.00 23.67 ? 4400 ARG A CA    1 
ATOM   21671 C  C     . ARG A 1 4400 ? 177.091 163.443 177.576 1.00 26.54 ? 4400 ARG A C     1 
ATOM   21672 O  O     . ARG A 1 4400 ? 177.974 162.846 176.952 1.00 33.06 ? 4400 ARG A O     1 
ATOM   21673 C  CB    . ARG A 1 4400 ? 178.125 165.401 178.756 1.00 18.35 ? 4400 ARG A CB    1 
ATOM   21674 C  CG    . ARG A 1 4400 ? 178.459 166.083 180.070 1.00 20.72 ? 4400 ARG A CG    1 
ATOM   21675 C  CD    . ARG A 1 4400 ? 178.955 167.504 179.865 1.00 24.13 ? 4400 ARG A CD    1 
ATOM   21676 N  NE    . ARG A 1 4400 ? 177.936 168.355 179.266 1.00 26.44 ? 4400 ARG A NE    1 
ATOM   21677 C  CZ    . ARG A 1 4400 ? 178.034 169.672 179.146 1.00 20.20 ? 4400 ARG A CZ    1 
ATOM   21678 N  NH1   . ARG A 1 4400 ? 179.075 170.334 179.620 1.00 17.35 ? 4400 ARG A NH1   1 
ATOM   21679 N  NH2   . ARG A 1 4400 ? 177.059 170.343 178.541 1.00 22.58 ? 4400 ARG A NH2   1 
ATOM   21680 N  N     . THR A 1 4401 ? 175.846 163.572 177.125 1.00 29.37 ? 4401 THR A N     1 
ATOM   21681 C  CA    . THR A 1 4401 ? 175.385 162.967 175.885 1.00 29.66 ? 4401 THR A CA    1 
ATOM   21682 C  C     . THR A 1 4401 ? 174.551 164.004 175.146 1.00 33.39 ? 4401 THR A C     1 
ATOM   21683 O  O     . THR A 1 4401 ? 174.034 164.948 175.747 1.00 30.56 ? 4401 THR A O     1 
ATOM   21684 C  CB    . THR A 1 4401 ? 174.580 161.683 176.169 1.00 27.68 ? 4401 THR A CB    1 
ATOM   21685 O  OG1   . THR A 1 4401 ? 175.402 160.759 176.891 1.00 26.41 ? 4401 THR A OG1   1 
ATOM   21686 C  CG2   . THR A 1 4401 ? 174.129 161.004 174.884 1.00 26.51 ? 4401 THR A CG2   1 
ATOM   21687 N  N     . VAL A 1 4402 ? 174.440 163.834 173.824 1.00 34.21 ? 4402 VAL A N     1 
ATOM   21688 C  CA    . VAL A 1 4402 ? 173.713 164.803 173.006 1.00 30.32 ? 4402 VAL A CA    1 
ATOM   21689 C  C     . VAL A 1 4402 ? 172.268 164.933 173.475 1.00 27.92 ? 4402 VAL A C     1 
ATOM   21690 O  O     . VAL A 1 4402 ? 171.710 166.036 173.508 1.00 32.17 ? 4402 VAL A O     1 
ATOM   21691 C  CB    . VAL A 1 4402 ? 173.798 164.420 171.517 1.00 31.50 ? 4402 VAL A CB    1 
ATOM   21692 C  CG1   . VAL A 1 4402 ? 175.188 164.709 170.976 1.00 27.49 ? 4402 VAL A CG1   1 
ATOM   21693 C  CG2   . VAL A 1 4402 ? 173.444 162.952 171.318 1.00 29.85 ? 4402 VAL A CG2   1 
ATOM   21694 N  N     . GLU A 1 4403 ? 171.639 163.817 173.846 1.00 28.09 ? 4403 GLU A N     1 
ATOM   21695 C  CA    . GLU A 1 4403 ? 170.263 163.859 174.326 1.00 26.08 ? 4403 GLU A CA    1 
ATOM   21696 C  C     . GLU A 1 4403 ? 170.160 163.966 175.843 1.00 30.26 ? 4403 GLU A C     1 
ATOM   21697 O  O     . GLU A 1 4403 ? 169.057 164.184 176.358 1.00 29.64 ? 4403 GLU A O     1 
ATOM   21698 C  CB    . GLU A 1 4403 ? 169.488 162.633 173.824 1.00 25.39 ? 4403 GLU A CB    1 
ATOM   21699 C  CG    . GLU A 1 4403 ? 170.014 161.276 174.276 1.00 30.97 ? 4403 GLU A CG    1 
ATOM   21700 C  CD    . GLU A 1 4403 ? 169.455 160.837 175.615 1.00 36.19 ? 4403 GLU A CD    1 
ATOM   21701 O  OE1   . GLU A 1 4403 ? 168.409 161.376 176.032 1.00 39.88 ? 4403 GLU A OE1   1 
ATOM   21702 O  OE2   . GLU A 1 4403 ? 170.049 159.933 176.240 1.00 37.74 ? 4403 GLU A OE2   1 
ATOM   21703 N  N     . ASN A 1 4404 ? 171.273 163.825 176.567 1.00 26.20 ? 4404 ASN A N     1 
ATOM   21704 C  CA    . ASN A 1 4404 ? 171.266 164.086 178.003 1.00 25.37 ? 4404 ASN A CA    1 
ATOM   21705 C  C     . ASN A 1 4404 ? 171.289 165.577 178.310 1.00 28.19 ? 4404 ASN A C     1 
ATOM   21706 O  O     . ASN A 1 4404 ? 170.744 166.001 179.335 1.00 29.38 ? 4404 ASN A O     1 
ATOM   21707 C  CB    . ASN A 1 4404 ? 172.452 163.393 178.676 1.00 23.68 ? 4404 ASN A CB    1 
ATOM   21708 C  CG    . ASN A 1 4404 ? 172.268 161.892 178.782 1.00 28.48 ? 4404 ASN A CG    1 
ATOM   21709 O  OD1   . ASN A 1 4404 ? 171.825 161.242 177.837 1.00 35.06 ? 4404 ASN A OD1   1 
ATOM   21710 N  ND2   . ASN A 1 4404 ? 172.627 161.330 179.929 1.00 26.97 ? 4404 ASN A ND2   1 
ATOM   21711 N  N     . ILE A 1 4405 ? 171.916 166.381 177.448 1.00 25.72 ? 4405 ILE A N     1 
ATOM   21712 C  CA    . ILE A 1 4405 ? 171.969 167.822 177.675 1.00 24.20 ? 4405 ILE A CA    1 
ATOM   21713 C  C     . ILE A 1 4405 ? 170.573 168.426 177.599 1.00 25.44 ? 4405 ILE A C     1 
ATOM   21714 O  O     . ILE A 1 4405 ? 170.253 169.367 178.336 1.00 27.94 ? 4405 ILE A O     1 
ATOM   21715 C  CB    . ILE A 1 4405 ? 172.934 168.485 176.671 1.00 23.10 ? 4405 ILE A CB    1 
ATOM   21716 C  CG1   . ILE A 1 4405 ? 174.333 167.885 176.791 1.00 25.38 ? 4405 ILE A CG1   1 
ATOM   21717 C  CG2   . ILE A 1 4405 ? 173.017 169.972 176.913 1.00 27.63 ? 4405 ILE A CG2   1 
ATOM   21718 C  CD1   . ILE A 1 4405 ? 174.839 167.778 178.213 1.00 24.95 ? 4405 ILE A CD1   1 
ATOM   21719 N  N     . LYS A 1 4406 ? 169.720 167.893 176.724 1.00 26.27 ? 4406 LYS A N     1 
ATOM   21720 C  CA    . LYS A 1 4406 ? 168.348 168.365 176.599 1.00 22.49 ? 4406 LYS A CA    1 
ATOM   21721 C  C     . LYS A 1 4406 ? 167.471 167.989 177.787 1.00 24.15 ? 4406 LYS A C     1 
ATOM   21722 O  O     . LYS A 1 4406 ? 166.349 168.497 177.891 1.00 26.56 ? 4406 LYS A O     1 
ATOM   21723 C  CB    . LYS A 1 4406 ? 167.723 167.821 175.311 1.00 23.37 ? 4406 LYS A CB    1 
ATOM   21724 C  CG    . LYS A 1 4406 ? 168.522 168.132 174.056 1.00 33.05 ? 4406 LYS A CG    1 
ATOM   21725 C  CD    . LYS A 1 4406 ? 167.833 167.596 172.811 1.00 30.20 ? 4406 LYS A CD    1 
ATOM   21726 C  CE    . LYS A 1 4406 ? 167.591 166.099 172.912 1.00 31.27 ? 4406 LYS A CE    1 
ATOM   21727 N  NZ    . LYS A 1 4406 ? 166.971 165.552 171.675 1.00 27.23 ? 4406 LYS A NZ    1 
ATOM   21728 N  N     . ASP A 1 4407 ? 167.942 167.117 178.675 1.00 27.46 ? 4407 ASP A N     1 
ATOM   21729 C  CA    . ASP A 1 4407 ? 167.158 166.702 179.830 1.00 24.00 ? 4407 ASP A CA    1 
ATOM   21730 C  C     . ASP A 1 4407 ? 167.408 167.659 180.988 1.00 26.42 ? 4407 ASP A C     1 
ATOM   21731 O  O     . ASP A 1 4407 ? 168.549 167.753 181.460 1.00 27.58 ? 4407 ASP A O     1 
ATOM   21732 C  CB    . ASP A 1 4407 ? 167.518 165.281 180.236 1.00 25.61 ? 4407 ASP A CB    1 
ATOM   21733 C  CG    . ASP A 1 4407 ? 166.609 164.731 181.317 1.00 29.36 ? 4407 ASP A CG    1 
ATOM   21734 O  OD1   . ASP A 1 4407 ? 165.648 165.425 181.713 1.00 29.69 ? 4407 ASP A OD1   1 
ATOM   21735 O  OD2   . ASP A 1 4407 ? 166.852 163.592 181.768 1.00 36.18 ? 4407 ASP A OD2   1 
ATOM   21736 N  N     . PRO A 1 4408 ? 166.393 168.384 181.465 1.00 24.97 ? 4408 PRO A N     1 
ATOM   21737 C  CA    . PRO A 1 4408 ? 166.618 169.310 182.591 1.00 22.32 ? 4408 PRO A CA    1 
ATOM   21738 C  C     . PRO A 1 4408 ? 167.097 168.629 183.860 1.00 18.49 ? 4408 PRO A C     1 
ATOM   21739 O  O     . PRO A 1 4408 ? 167.893 169.213 184.607 1.00 20.64 ? 4408 PRO A O     1 
ATOM   21740 C  CB    . PRO A 1 4408 ? 165.240 169.960 182.785 1.00 22.83 ? 4408 PRO A CB    1 
ATOM   21741 C  CG    . PRO A 1 4408 ? 164.278 169.032 182.119 1.00 20.11 ? 4408 PRO A CG    1 
ATOM   21742 C  CD    . PRO A 1 4408 ? 165.014 168.461 180.960 1.00 19.62 ? 4408 PRO A CD    1 
ATOM   21743 N  N     . LEU A 1 4409 ? 166.623 167.412 184.136 1.00 21.67 ? 4409 LEU A N     1 
ATOM   21744 C  CA    . LEU A 1 4409 ? 167.059 166.703 185.334 1.00 20.99 ? 4409 LEU A CA    1 
ATOM   21745 C  C     . LEU A 1 4409 ? 168.550 166.400 185.277 1.00 25.71 ? 4409 LEU A C     1 
ATOM   21746 O  O     . LEU A 1 4409 ? 169.258 166.533 186.281 1.00 25.51 ? 4409 LEU A O     1 
ATOM   21747 C  CB    . LEU A 1 4409 ? 166.253 165.417 185.508 1.00 16.92 ? 4409 LEU A CB    1 
ATOM   21748 C  CG    . LEU A 1 4409 ? 165.054 165.494 186.454 1.00 21.62 ? 4409 LEU A CG    1 
ATOM   21749 C  CD1   . LEU A 1 4409 ? 164.351 164.152 186.533 1.00 19.31 ? 4409 LEU A CD1   1 
ATOM   21750 C  CD2   . LEU A 1 4409 ? 165.485 165.956 187.838 1.00 17.85 ? 4409 LEU A CD2   1 
ATOM   21751 N  N     . PHE A 1 4410 ? 169.041 165.994 184.104 1.00 23.76 ? 4410 PHE A N     1 
ATOM   21752 C  CA    . PHE A 1 4410 ? 170.468 165.744 183.942 1.00 21.16 ? 4410 PHE A CA    1 
ATOM   21753 C  C     . PHE A 1 4410 ? 171.273 167.021 184.149 1.00 22.82 ? 4410 PHE A C     1 
ATOM   21754 O  O     . PHE A 1 4410 ? 172.345 166.995 184.763 1.00 21.10 ? 4410 PHE A O     1 
ATOM   21755 C  CB    . PHE A 1 4410 ? 170.731 165.151 182.556 1.00 23.86 ? 4410 PHE A CB    1 
ATOM   21756 C  CG    . PHE A 1 4410 ? 172.124 164.619 182.372 1.00 27.60 ? 4410 PHE A CG    1 
ATOM   21757 C  CD1   . PHE A 1 4410 ? 172.424 163.305 182.688 1.00 22.37 ? 4410 PHE A CD1   1 
ATOM   21758 C  CD2   . PHE A 1 4410 ? 173.128 165.426 181.865 1.00 30.35 ? 4410 PHE A CD2   1 
ATOM   21759 C  CE1   . PHE A 1 4410 ? 173.700 162.811 182.512 1.00 20.28 ? 4410 PHE A CE1   1 
ATOM   21760 C  CE2   . PHE A 1 4410 ? 174.406 164.938 181.687 1.00 28.76 ? 4410 PHE A CE2   1 
ATOM   21761 C  CZ    . PHE A 1 4410 ? 174.692 163.628 182.008 1.00 27.49 ? 4410 PHE A CZ    1 
ATOM   21762 N  N     . ARG A 1 4411 ? 170.764 168.152 183.653 1.00 20.09 ? 4411 ARG A N     1 
ATOM   21763 C  CA    . ARG A 1 4411 ? 171.491 169.412 183.775 1.00 22.46 ? 4411 ARG A CA    1 
ATOM   21764 C  C     . ARG A 1 4411 ? 171.675 169.816 185.234 1.00 25.00 ? 4411 ARG A C     1 
ATOM   21765 O  O     . ARG A 1 4411 ? 172.760 170.256 185.631 1.00 31.58 ? 4411 ARG A O     1 
ATOM   21766 C  CB    . ARG A 1 4411 ? 170.769 170.511 182.999 1.00 20.37 ? 4411 ARG A CB    1 
ATOM   21767 C  CG    . ARG A 1 4411 ? 170.661 170.258 181.509 1.00 13.03 ? 4411 ARG A CG    1 
ATOM   21768 C  CD    . ARG A 1 4411 ? 170.137 171.486 180.788 1.00 22.46 ? 4411 ARG A CD    1 
ATOM   21769 N  NE    . ARG A 1 4411 ? 168.757 171.786 181.150 1.00 23.91 ? 4411 ARG A NE    1 
ATOM   21770 C  CZ    . ARG A 1 4411 ? 167.762 171.900 180.281 1.00 25.41 ? 4411 ARG A CZ    1 
ATOM   21771 N  NH1   . ARG A 1 4411 ? 167.959 171.755 178.982 1.00 20.77 ? 4411 ARG A NH1   1 
ATOM   21772 N  NH2   . ARG A 1 4411 ? 166.540 172.170 180.728 1.00 28.17 ? 4411 ARG A NH2   1 
ATOM   21773 N  N     . PHE A 1 4412 ? 170.627 169.677 186.049 1.00 26.40 ? 4412 PHE A N     1 
ATOM   21774 C  CA    . PHE A 1 4412 ? 170.767 169.965 187.473 1.00 26.93 ? 4412 PHE A CA    1 
ATOM   21775 C  C     . PHE A 1 4412 ? 171.629 168.915 188.164 1.00 24.08 ? 4412 PHE A C     1 
ATOM   21776 O  O     . PHE A 1 4412 ? 172.524 169.249 188.949 1.00 26.99 ? 4412 PHE A O     1 
ATOM   21777 C  CB    . PHE A 1 4412 ? 169.393 170.047 188.140 1.00 22.25 ? 4412 PHE A CB    1 
ATOM   21778 C  CG    . PHE A 1 4412 ? 169.429 169.779 189.616 1.00 19.53 ? 4412 PHE A CG    1 
ATOM   21779 C  CD1   . PHE A 1 4412 ? 169.857 170.754 190.497 1.00 21.28 ? 4412 PHE A CD1   1 
ATOM   21780 C  CD2   . PHE A 1 4412 ? 169.056 168.544 190.119 1.00 16.71 ? 4412 PHE A CD2   1 
ATOM   21781 C  CE1   . PHE A 1 4412 ? 169.903 170.510 191.852 1.00 20.48 ? 4412 PHE A CE1   1 
ATOM   21782 C  CE2   . PHE A 1 4412 ? 169.103 168.293 191.473 1.00 15.03 ? 4412 PHE A CE2   1 
ATOM   21783 C  CZ    . PHE A 1 4412 ? 169.528 169.276 192.340 1.00 18.23 ? 4412 PHE A CZ    1 
ATOM   21784 N  N     . PHE A 1 4413 ? 171.368 167.636 187.889 1.00 19.19 ? 4413 PHE A N     1 
ATOM   21785 C  CA    . PHE A 1 4413 ? 172.102 166.565 188.556 1.00 19.46 ? 4413 PHE A CA    1 
ATOM   21786 C  C     . PHE A 1 4413 ? 173.574 166.549 188.161 1.00 25.44 ? 4413 PHE A C     1 
ATOM   21787 O  O     . PHE A 1 4413 ? 174.421 166.139 188.963 1.00 28.29 ? 4413 PHE A O     1 
ATOM   21788 C  CB    . PHE A 1 4413 ? 171.452 165.217 188.253 1.00 17.70 ? 4413 PHE A CB    1 
ATOM   21789 C  CG    . PHE A 1 4413 ? 170.295 164.888 189.150 1.00 21.62 ? 4413 PHE A CG    1 
ATOM   21790 C  CD1   . PHE A 1 4413 ? 170.363 165.146 190.509 1.00 19.71 ? 4413 PHE A CD1   1 
ATOM   21791 C  CD2   . PHE A 1 4413 ? 169.140 164.322 188.636 1.00 21.25 ? 4413 PHE A CD2   1 
ATOM   21792 C  CE1   . PHE A 1 4413 ? 169.303 164.845 191.337 1.00 19.92 ? 4413 PHE A CE1   1 
ATOM   21793 C  CE2   . PHE A 1 4413 ? 168.078 164.015 189.461 1.00 22.93 ? 4413 PHE A CE2   1 
ATOM   21794 C  CZ    . PHE A 1 4413 ? 168.159 164.279 190.815 1.00 25.67 ? 4413 PHE A CZ    1 
ATOM   21795 N  N     . GLU A 1 4414 ? 173.899 166.976 186.940 1.00 23.80 ? 4414 GLU A N     1 
ATOM   21796 C  CA    . GLU A 1 4414 ? 175.300 167.058 186.541 1.00 25.15 ? 4414 GLU A CA    1 
ATOM   21797 C  C     . GLU A 1 4414 ? 176.045 168.094 187.372 1.00 24.47 ? 4414 GLU A C     1 
ATOM   21798 O  O     . GLU A 1 4414 ? 177.204 167.884 187.751 1.00 26.38 ? 4414 GLU A O     1 
ATOM   21799 C  CB    . GLU A 1 4414 ? 175.403 167.384 185.050 1.00 24.26 ? 4414 GLU A CB    1 
ATOM   21800 C  CG    . GLU A 1 4414 ? 176.816 167.598 184.555 1.00 23.04 ? 4414 GLU A CG    1 
ATOM   21801 C  CD    . GLU A 1 4414 ? 176.874 168.540 183.373 1.00 31.08 ? 4414 GLU A CD    1 
ATOM   21802 O  OE1   . GLU A 1 4414 ? 176.927 169.769 183.594 1.00 35.71 ? 4414 GLU A OE1   1 
ATOM   21803 O  OE2   . GLU A 1 4414 ? 176.858 168.054 182.224 1.00 32.07 ? 4414 GLU A OE2   1 
ATOM   21804 N  N     . ARG A 1 4415 ? 175.395 169.222 187.665 1.00 24.24 ? 4415 ARG A N     1 
ATOM   21805 C  CA    . ARG A 1 4415 ? 176.008 170.231 188.522 1.00 19.30 ? 4415 ARG A CA    1 
ATOM   21806 C  C     . ARG A 1 4415 ? 176.295 169.676 189.909 1.00 26.09 ? 4415 ARG A C     1 
ATOM   21807 O  O     . ARG A 1 4415 ? 177.353 169.947 190.486 1.00 29.78 ? 4415 ARG A O     1 
ATOM   21808 C  CB    . ARG A 1 4415 ? 175.103 171.455 188.625 1.00 20.53 ? 4415 ARG A CB    1 
ATOM   21809 C  CG    . ARG A 1 4415 ? 175.090 172.336 187.400 1.00 24.49 ? 4415 ARG A CG    1 
ATOM   21810 C  CD    . ARG A 1 4415 ? 174.432 173.658 187.720 1.00 18.55 ? 4415 ARG A CD    1 
ATOM   21811 N  NE    . ARG A 1 4415 ? 174.686 174.052 189.100 1.00 18.82 ? 4415 ARG A NE    1 
ATOM   21812 C  CZ    . ARG A 1 4415 ? 174.386 175.238 189.610 1.00 24.40 ? 4415 ARG A CZ    1 
ATOM   21813 N  NH1   . ARG A 1 4415 ? 173.834 176.188 188.874 1.00 16.60 ? 4415 ARG A NH1   1 
ATOM   21814 N  NH2   . ARG A 1 4415 ? 174.651 175.478 190.892 1.00 23.92 ? 4415 ARG A NH2   1 
ATOM   21815 N  N     . GLU A 1 4416 ? 175.361 168.895 190.458 1.00 26.05 ? 4416 GLU A N     1 
ATOM   21816 C  CA    . GLU A 1 4416 ? 175.510 168.388 191.819 1.00 25.82 ? 4416 GLU A CA    1 
ATOM   21817 C  C     . GLU A 1 4416 ? 176.750 167.514 191.953 1.00 25.89 ? 4416 GLU A C     1 
ATOM   21818 O  O     . GLU A 1 4416 ? 177.535 167.669 192.896 1.00 31.04 ? 4416 GLU A O     1 
ATOM   21819 C  CB    . GLU A 1 4416 ? 174.259 167.610 192.226 1.00 23.55 ? 4416 GLU A CB    1 
ATOM   21820 C  CG    . GLU A 1 4416 ? 173.076 168.486 192.595 1.00 23.44 ? 4416 GLU A CG    1 
ATOM   21821 C  CD    . GLU A 1 4416 ? 173.328 169.310 193.839 1.00 25.14 ? 4416 GLU A CD    1 
ATOM   21822 O  OE1   . GLU A 1 4416 ? 173.625 168.716 194.897 1.00 28.51 ? 4416 GLU A OE1   1 
ATOM   21823 O  OE2   . GLU A 1 4416 ? 173.223 170.553 193.763 1.00 24.97 ? 4416 GLU A OE2   1 
ATOM   21824 N  N     . VAL A 1 4417 ? 176.945 166.585 191.015 1.00 23.02 ? 4417 VAL A N     1 
ATOM   21825 C  CA    . VAL A 1 4417 ? 178.113 165.712 191.082 1.00 24.78 ? 4417 VAL A CA    1 
ATOM   21826 C  C     . VAL A 1 4417 ? 179.387 166.492 190.782 1.00 24.26 ? 4417 VAL A C     1 
ATOM   21827 O  O     . VAL A 1 4417 ? 180.420 166.282 191.426 1.00 25.34 ? 4417 VAL A O     1 
ATOM   21828 C  CB    . VAL A 1 4417 ? 177.940 164.511 190.135 1.00 23.95 ? 4417 VAL A CB    1 
ATOM   21829 C  CG1   . VAL A 1 4417 ? 179.196 163.662 190.120 1.00 22.52 ? 4417 VAL A CG1   1 
ATOM   21830 C  CG2   . VAL A 1 4417 ? 176.763 163.670 190.584 1.00 22.08 ? 4417 VAL A CG2   1 
ATOM   21831 N  N     . LYS A 1 4418 ? 179.337 167.404 189.808 1.00 26.88 ? 4418 LYS A N     1 
ATOM   21832 C  CA    . LYS A 1 4418 ? 180.535 168.149 189.432 1.00 25.72 ? 4418 LYS A CA    1 
ATOM   21833 C  C     . LYS A 1 4418 ? 181.064 168.970 190.602 1.00 26.98 ? 4418 LYS A C     1 
ATOM   21834 O  O     . LYS A 1 4418 ? 182.263 168.941 190.902 1.00 31.00 ? 4418 LYS A O     1 
ATOM   21835 C  CB    . LYS A 1 4418 ? 180.246 169.047 188.230 1.00 24.19 ? 4418 LYS A CB    1 
ATOM   21836 C  CG    . LYS A 1 4418 ? 181.444 169.230 187.310 1.00 26.43 ? 4418 LYS A CG    1 
ATOM   21837 C  CD    . LYS A 1 4418 ? 181.081 169.990 186.046 1.00 23.29 ? 4418 LYS A CD    1 
ATOM   21838 C  CE    . LYS A 1 4418 ? 179.905 169.354 185.328 1.00 23.74 ? 4418 LYS A CE    1 
ATOM   21839 N  NZ    . LYS A 1 4418 ? 179.493 170.150 184.138 1.00 21.88 ? 4418 LYS A NZ    1 
ATOM   21840 N  N     . MET A 1 4419 ? 180.182 169.700 191.287 1.00 30.32 ? 4419 MET A N     1 
ATOM   21841 C  CA    . MET A 1 4419 ? 180.622 170.421 192.476 1.00 31.08 ? 4419 MET A CA    1 
ATOM   21842 C  C     . MET A 1 4419 ? 180.816 169.470 193.650 1.00 23.68 ? 4419 MET A C     1 
ATOM   21843 O  O     . MET A 1 4419 ? 181.640 169.725 194.535 1.00 28.13 ? 4419 MET A O     1 
ATOM   21844 C  CB    . MET A 1 4419 ? 179.627 171.527 192.837 1.00 24.97 ? 4419 MET A CB    1 
ATOM   21845 C  CG    . MET A 1 4419 ? 178.253 171.042 193.252 1.00 27.96 ? 4419 MET A CG    1 
ATOM   21846 S  SD    . MET A 1 4419 ? 177.160 172.412 193.674 1.00 57.74 ? 4419 MET A SD    1 
ATOM   21847 C  CE    . MET A 1 4419 ? 177.869 172.933 195.234 1.00 20.82 ? 4419 MET A CE    1 
ATOM   21848 N  N     . GLY A 1 4420 ? 180.067 168.365 193.670 1.00 20.57 ? 4420 GLY A N     1 
ATOM   21849 C  CA    . GLY A 1 4420 ? 180.216 167.393 194.737 1.00 19.46 ? 4420 GLY A CA    1 
ATOM   21850 C  C     . GLY A 1 4420 ? 181.492 166.584 194.646 1.00 22.83 ? 4420 GLY A C     1 
ATOM   21851 O  O     . GLY A 1 4420 ? 182.105 166.271 195.670 1.00 26.25 ? 4420 GLY A O     1 
ATOM   21852 N  N     . ALA A 1 4421 ? 181.902 166.218 193.429 1.00 23.12 ? 4421 ALA A N     1 
ATOM   21853 C  CA    . ALA A 1 4421 ? 183.133 165.452 193.268 1.00 18.22 ? 4421 ALA A CA    1 
ATOM   21854 C  C     . ALA A 1 4421 ? 184.352 166.275 193.659 1.00 19.89 ? 4421 ALA A C     1 
ATOM   21855 O  O     . ALA A 1 4421 ? 185.279 165.758 194.291 1.00 20.90 ? 4421 ALA A O     1 
ATOM   21856 C  CB    . ALA A 1 4421 ? 183.258 164.953 191.830 1.00 21.42 ? 4421 ALA A CB    1 
ATOM   21857 N  N     . LYS A 1 4422 ? 184.370 167.559 193.287 1.00 20.47 ? 4422 LYS A N     1 
ATOM   21858 C  CA    . LYS A 1 4422 ? 185.495 168.418 193.636 1.00 17.21 ? 4422 LYS A CA    1 
ATOM   21859 C  C     . LYS A 1 4422 ? 185.622 168.574 195.147 1.00 23.10 ? 4422 LYS A C     1 
ATOM   21860 O  O     . LYS A 1 4422 ? 186.728 168.503 195.694 1.00 27.55 ? 4422 LYS A O     1 
ATOM   21861 C  CB    . LYS A 1 4422 ? 185.338 169.782 192.967 1.00 22.92 ? 4422 LYS A CB    1 
ATOM   21862 C  CG    . LYS A 1 4422 ? 186.347 170.822 193.424 1.00 22.02 ? 4422 LYS A CG    1 
ATOM   21863 C  CD    . LYS A 1 4422 ? 185.987 172.204 192.908 1.00 16.85 ? 4422 LYS A CD    1 
ATOM   21864 C  CE    . LYS A 1 4422 ? 186.949 173.258 193.430 1.00 25.56 ? 4422 LYS A CE    1 
ATOM   21865 N  NZ    . LYS A 1 4422 ? 186.591 174.623 192.955 1.00 25.40 ? 4422 LYS A NZ    1 
ATOM   21866 N  N     . LEU A 1 4423 ? 184.499 168.782 195.837 1.00 23.79 ? 4423 LEU A N     1 
ATOM   21867 C  CA    . LEU A 1 4423 ? 184.533 168.901 197.290 1.00 21.09 ? 4423 LEU A CA    1 
ATOM   21868 C  C     . LEU A 1 4423 ? 184.959 167.592 197.944 1.00 15.24 ? 4423 LEU A C     1 
ATOM   21869 O  O     . LEU A 1 4423 ? 185.678 167.599 198.950 1.00 18.04 ? 4423 LEU A O     1 
ATOM   21870 C  CB    . LEU A 1 4423 ? 183.167 169.349 197.809 1.00 21.69 ? 4423 LEU A CB    1 
ATOM   21871 C  CG    . LEU A 1 4423 ? 182.998 169.534 199.318 1.00 23.48 ? 4423 LEU A CG    1 
ATOM   21872 C  CD1   . LEU A 1 4423 ? 184.131 170.361 199.902 1.00 19.28 ? 4423 LEU A CD1   1 
ATOM   21873 C  CD2   . LEU A 1 4423 ? 181.654 170.175 199.617 1.00 21.38 ? 4423 LEU A CD2   1 
ATOM   21874 N  N     . LEU A 1 4424 ? 184.524 166.460 197.389 1.00 18.33 ? 4424 LEU A N     1 
ATOM   21875 C  CA    . LEU A 1 4424 ? 184.878 165.164 197.959 1.00 17.31 ? 4424 LEU A CA    1 
ATOM   21876 C  C     . LEU A 1 4424 ? 186.382 164.924 197.901 1.00 20.62 ? 4424 LEU A C     1 
ATOM   21877 O  O     . LEU A 1 4424 ? 186.986 164.462 198.875 1.00 22.84 ? 4424 LEU A O     1 
ATOM   21878 C  CB    . LEU A 1 4424 ? 184.124 164.053 197.230 1.00 16.98 ? 4424 LEU A CB    1 
ATOM   21879 C  CG    . LEU A 1 4424 ? 184.335 162.630 197.748 1.00 23.86 ? 4424 LEU A CG    1 
ATOM   21880 C  CD1   . LEU A 1 4424 ? 183.845 162.498 199.174 1.00 18.97 ? 4424 LEU A CD1   1 
ATOM   21881 C  CD2   . LEU A 1 4424 ? 183.632 161.635 196.845 1.00 21.24 ? 4424 LEU A CD2   1 
ATOM   21882 N  N     . GLN A 1 4425 ? 187.005 165.233 196.762 1.00 22.77 ? 4425 GLN A N     1 
ATOM   21883 C  CA    . GLN A 1 4425 ? 188.446 165.032 196.632 1.00 22.91 ? 4425 GLN A CA    1 
ATOM   21884 C  C     . GLN A 1 4425 ? 189.225 165.974 197.542 1.00 21.20 ? 4425 GLN A C     1 
ATOM   21885 O  O     . GLN A 1 4425 ? 190.237 165.577 198.133 1.00 15.50 ? 4425 GLN A O     1 
ATOM   21886 C  CB    . GLN A 1 4425 ? 188.870 165.213 195.175 1.00 18.35 ? 4425 GLN A CB    1 
ATOM   21887 C  CG    . GLN A 1 4425 ? 188.235 164.216 194.216 1.00 23.11 ? 4425 GLN A CG    1 
ATOM   21888 C  CD    . GLN A 1 4425 ? 188.298 164.669 192.771 1.00 30.52 ? 4425 GLN A CD    1 
ATOM   21889 O  OE1   . GLN A 1 4425 ? 187.271 164.821 192.110 1.00 31.23 ? 4425 GLN A OE1   1 
ATOM   21890 N  NE2   . GLN A 1 4425 ? 189.509 164.889 192.272 1.00 23.18 ? 4425 GLN A NE2   1 
ATOM   21891 N  N     . ASP A 1 4426 ? 188.777 167.227 197.662 1.00 18.58 ? 4426 ASP A N     1 
ATOM   21892 C  CA    . ASP A 1 4426 ? 189.504 168.197 198.476 1.00 17.24 ? 4426 ASP A CA    1 
ATOM   21893 C  C     . ASP A 1 4426 ? 189.507 167.801 199.948 1.00 19.35 ? 4426 ASP A C     1 
ATOM   21894 O  O     . ASP A 1 4426 ? 190.545 167.877 200.615 1.00 20.21 ? 4426 ASP A O     1 
ATOM   21895 C  CB    . ASP A 1 4426 ? 188.902 169.590 198.298 1.00 21.21 ? 4426 ASP A CB    1 
ATOM   21896 C  CG    . ASP A 1 4426 ? 189.011 170.093 196.875 1.00 29.39 ? 4426 ASP A CG    1 
ATOM   21897 O  OD1   . ASP A 1 4426 ? 189.605 169.383 196.037 1.00 26.67 ? 4426 ASP A OD1   1 
ATOM   21898 O  OD2   . ASP A 1 4426 ? 188.502 171.199 196.592 1.00 34.43 ? 4426 ASP A OD2   1 
ATOM   21899 N  N     . VAL A 1 4427 ? 188.356 167.374 200.472 1.00 16.47 ? 4427 VAL A N     1 
ATOM   21900 C  CA    . VAL A 1 4427 ? 188.279 167.002 201.881 1.00 18.14 ? 4427 VAL A CA    1 
ATOM   21901 C  C     . VAL A 1 4427 ? 189.117 165.761 202.156 1.00 17.35 ? 4427 VAL A C     1 
ATOM   21902 O  O     . VAL A 1 4427 ? 189.840 165.693 203.157 1.00 18.26 ? 4427 VAL A O     1 
ATOM   21903 C  CB    . VAL A 1 4427 ? 186.812 166.802 202.302 1.00 13.75 ? 4427 VAL A CB    1 
ATOM   21904 C  CG1   . VAL A 1 4427 ? 186.736 166.269 203.719 1.00 11.98 ? 4427 VAL A CG1   1 
ATOM   21905 C  CG2   . VAL A 1 4427 ? 186.045 168.107 202.180 1.00 17.52 ? 4427 VAL A CG2   1 
ATOM   21906 N  N     . ARG A 1 4428 ? 189.031 164.756 201.280 1.00 17.00 ? 4428 ARG A N     1 
ATOM   21907 C  CA    . ARG A 1 4428 ? 189.799 163.532 201.482 1.00 20.55 ? 4428 ARG A CA    1 
ATOM   21908 C  C     . ARG A 1 4428 ? 191.296 163.803 201.428 1.00 19.47 ? 4428 ARG A C     1 
ATOM   21909 O  O     . ARG A 1 4428 ? 192.063 163.259 202.233 1.00 21.55 ? 4428 ARG A O     1 
ATOM   21910 C  CB    . ARG A 1 4428 ? 189.400 162.485 200.441 1.00 21.02 ? 4428 ARG A CB    1 
ATOM   21911 C  CG    . ARG A 1 4428 ? 187.989 161.948 200.610 1.00 24.22 ? 4428 ARG A CG    1 
ATOM   21912 C  CD    . ARG A 1 4428 ? 187.759 160.705 199.763 1.00 23.13 ? 4428 ARG A CD    1 
ATOM   21913 N  NE    . ARG A 1 4428 ? 188.628 159.601 200.153 1.00 26.24 ? 4428 ARG A NE    1 
ATOM   21914 C  CZ    . ARG A 1 4428 ? 188.510 158.909 201.278 1.00 24.76 ? 4428 ARG A CZ    1 
ATOM   21915 N  NH1   . ARG A 1 4428 ? 187.542 159.157 202.146 1.00 25.85 ? 4428 ARG A NH1   1 
ATOM   21916 N  NH2   . ARG A 1 4428 ? 189.380 157.938 201.537 1.00 22.52 ? 4428 ARG A NH2   1 
ATOM   21917 N  N     . GLN A 1 4429 ? 191.735 164.636 200.481 1.00 18.13 ? 4429 GLN A N     1 
ATOM   21918 C  CA    . GLN A 1 4429 ? 193.153 164.969 200.391 1.00 21.46 ? 4429 GLN A CA    1 
ATOM   21919 C  C     . GLN A 1 4429 ? 193.623 165.731 201.624 1.00 18.74 ? 4429 GLN A C     1 
ATOM   21920 O  O     . GLN A 1 4429 ? 194.705 165.453 202.155 1.00 26.80 ? 4429 GLN A O     1 
ATOM   21921 C  CB    . GLN A 1 4429 ? 193.425 165.777 199.123 1.00 20.95 ? 4429 GLN A CB    1 
ATOM   21922 C  CG    . GLN A 1 4429 ? 194.887 165.817 198.690 1.00 22.12 ? 4429 GLN A CG    1 
ATOM   21923 C  CD    . GLN A 1 4429 ? 195.607 164.492 198.887 1.00 27.51 ? 4429 GLN A CD    1 
ATOM   21924 O  OE1   . GLN A 1 4429 ? 196.147 164.215 199.958 1.00 26.97 ? 4429 GLN A OE1   1 
ATOM   21925 N  NE2   . GLN A 1 4429 ? 195.615 163.666 197.848 1.00 29.86 ? 4429 GLN A NE2   1 
ATOM   21926 N  N     . ASP A 1 4430 ? 192.823 166.692 202.093 1.00 16.31 ? 4430 ASP A N     1 
ATOM   21927 C  CA    . ASP A 1 4430 ? 193.192 167.440 203.292 1.00 17.56 ? 4430 ASP A CA    1 
ATOM   21928 C  C     . ASP A 1 4430 ? 193.271 166.529 204.508 1.00 19.07 ? 4430 ASP A C     1 
ATOM   21929 O  O     . ASP A 1 4430 ? 194.197 166.641 205.319 1.00 21.61 ? 4430 ASP A O     1 
ATOM   21930 C  CB    . ASP A 1 4430 ? 192.192 168.570 203.538 1.00 17.46 ? 4430 ASP A CB    1 
ATOM   21931 C  CG    . ASP A 1 4430 ? 192.271 169.657 202.492 1.00 21.36 ? 4430 ASP A CG    1 
ATOM   21932 O  OD1   . ASP A 1 4430 ? 193.220 169.638 201.681 1.00 22.82 ? 4430 ASP A OD1   1 
ATOM   21933 O  OD2   . ASP A 1 4430 ? 191.381 170.533 202.480 1.00 29.05 ? 4430 ASP A OD2   1 
ATOM   21934 N  N     . LEU A 1 4431 ? 192.304 165.621 204.654 1.00 19.83 ? 4431 LEU A N     1 
ATOM   21935 C  CA    . LEU A 1 4431 ? 192.313 164.701 205.787 1.00 20.09 ? 4431 LEU A CA    1 
ATOM   21936 C  C     . LEU A 1 4431 ? 193.510 163.760 205.726 1.00 20.33 ? 4431 LEU A C     1 
ATOM   21937 O  O     . LEU A 1 4431 ? 194.119 163.456 206.758 1.00 25.60 ? 4431 LEU A O     1 
ATOM   21938 C  CB    . LEU A 1 4431 ? 191.006 163.914 205.830 1.00 21.05 ? 4431 LEU A CB    1 
ATOM   21939 C  CG    . LEU A 1 4431 ? 189.816 164.647 206.451 1.00 20.36 ? 4431 LEU A CG    1 
ATOM   21940 C  CD1   . LEU A 1 4431 ? 188.546 163.827 206.307 1.00 22.38 ? 4431 LEU A CD1   1 
ATOM   21941 C  CD2   . LEU A 1 4431 ? 190.089 164.970 207.911 1.00 15.33 ? 4431 LEU A CD2   1 
ATOM   21942 N  N     . ALA A 1 4432 ? 193.862 163.288 204.528 1.00 21.05 ? 4432 ALA A N     1 
ATOM   21943 C  CA    . ALA A 1 4432 ? 195.007 162.395 204.392 1.00 18.79 ? 4432 ALA A CA    1 
ATOM   21944 C  C     . ALA A 1 4432 ? 196.304 163.099 204.771 1.00 24.70 ? 4432 ALA A C     1 
ATOM   21945 O  O     . ALA A 1 4432 ? 197.187 162.497 205.391 1.00 27.55 ? 4432 ALA A O     1 
ATOM   21946 C  CB    . ALA A 1 4432 ? 195.085 161.851 202.967 1.00 16.39 ? 4432 ALA A CB    1 
ATOM   21947 N  N     . ASP A 1 4433 ? 196.439 164.374 204.397 1.00 23.14 ? 4433 ASP A N     1 
ATOM   21948 C  CA    . ASP A 1 4433 ? 197.625 165.134 204.778 1.00 18.52 ? 4433 ASP A CA    1 
ATOM   21949 C  C     . ASP A 1 4433 ? 197.705 165.311 206.290 1.00 21.44 ? 4433 ASP A C     1 
ATOM   21950 O  O     . ASP A 1 4433 ? 198.790 165.220 206.875 1.00 28.94 ? 4433 ASP A O     1 
ATOM   21951 C  CB    . ASP A 1 4433 ? 197.630 166.488 204.074 1.00 20.22 ? 4433 ASP A CB    1 
ATOM   21952 C  CG    . ASP A 1 4433 ? 197.902 166.370 202.587 1.00 32.53 ? 4433 ASP A CG    1 
ATOM   21953 O  OD1   . ASP A 1 4433 ? 198.168 165.243 202.119 1.00 35.10 ? 4433 ASP A OD1   1 
ATOM   21954 O  OD2   . ASP A 1 4433 ? 197.850 167.403 201.887 1.00 32.59 ? 4433 ASP A OD2   1 
ATOM   21955 N  N     . VAL A 1 4434 ? 196.564 165.562 206.941 1.00 19.33 ? 4434 VAL A N     1 
ATOM   21956 C  CA    . VAL A 1 4434 ? 196.555 165.725 208.393 1.00 20.26 ? 4434 VAL A CA    1 
ATOM   21957 C  C     . VAL A 1 4434 ? 197.003 164.440 209.078 1.00 25.14 ? 4434 VAL A C     1 
ATOM   21958 O  O     . VAL A 1 4434 ? 197.789 164.469 210.032 1.00 23.26 ? 4434 VAL A O     1 
ATOM   21959 C  CB    . VAL A 1 4434 ? 195.161 166.168 208.875 1.00 23.35 ? 4434 VAL A CB    1 
ATOM   21960 C  CG1   . VAL A 1 4434 ? 195.057 166.047 210.386 1.00 19.29 ? 4434 VAL A CG1   1 
ATOM   21961 C  CG2   . VAL A 1 4434 ? 194.882 167.594 208.440 1.00 15.36 ? 4434 VAL A CG2   1 
ATOM   21962 N  N     . VAL A 1 4435 ? 196.514 163.292 208.599 1.00 27.68 ? 4435 VAL A N     1 
ATOM   21963 C  CA    . VAL A 1 4435 ? 196.949 162.012 209.153 1.00 28.44 ? 4435 VAL A CA    1 
ATOM   21964 C  C     . VAL A 1 4435 ? 198.451 161.842 208.978 1.00 29.30 ? 4435 VAL A C     1 
ATOM   21965 O  O     . VAL A 1 4435 ? 199.160 161.443 209.909 1.00 32.45 ? 4435 VAL A O     1 
ATOM   21966 C  CB    . VAL A 1 4435 ? 196.176 160.853 208.497 1.00 20.83 ? 4435 VAL A CB    1 
ATOM   21967 C  CG1   . VAL A 1 4435 ? 196.708 159.518 208.988 1.00 25.05 ? 4435 VAL A CG1   1 
ATOM   21968 C  CG2   . VAL A 1 4435 ? 194.694 160.974 208.783 1.00 28.81 ? 4435 VAL A CG2   1 
ATOM   21969 N  N     . GLN A 1 4436 ? 198.958 162.148 207.784 1.00 27.43 ? 4436 GLN A N     1 
ATOM   21970 C  CA    . GLN A 1 4436 ? 200.386 162.000 207.531 1.00 27.05 ? 4436 GLN A CA    1 
ATOM   21971 C  C     . GLN A 1 4436 ? 201.196 162.992 208.359 1.00 25.69 ? 4436 GLN A C     1 
ATOM   21972 O  O     . GLN A 1 4436 ? 202.303 162.673 208.810 1.00 26.39 ? 4436 GLN A O     1 
ATOM   21973 C  CB    . GLN A 1 4436 ? 200.662 162.167 206.037 1.00 19.16 ? 4436 GLN A CB    1 
ATOM   21974 C  CG    . GLN A 1 4436 ? 202.123 162.115 205.658 1.00 31.18 ? 4436 GLN A CG    1 
ATOM   21975 C  CD    . GLN A 1 4436 ? 202.332 162.020 204.162 1.00 34.42 ? 4436 GLN A CD    1 
ATOM   21976 O  OE1   . GLN A 1 4436 ? 201.372 161.951 203.394 1.00 32.60 ? 4436 GLN A OE1   1 
ATOM   21977 N  NE2   . GLN A 1 4436 ? 203.590 162.015 203.738 1.00 29.25 ? 4436 GLN A NE2   1 
ATOM   21978 N  N     . VAL A 1 4437 ? 200.661 164.196 208.575 1.00 24.86 ? 4437 VAL A N     1 
ATOM   21979 C  CA    . VAL A 1 4437 ? 201.322 165.158 209.454 1.00 24.36 ? 4437 VAL A CA    1 
ATOM   21980 C  C     . VAL A 1 4437 ? 201.379 164.618 210.878 1.00 22.15 ? 4437 VAL A C     1 
ATOM   21981 O  O     . VAL A 1 4437 ? 202.421 164.665 211.540 1.00 25.70 ? 4437 VAL A O     1 
ATOM   21982 C  CB    . VAL A 1 4437 ? 200.605 166.519 209.397 1.00 20.31 ? 4437 VAL A CB    1 
ATOM   21983 C  CG1   . VAL A 1 4437 ? 200.954 167.359 210.618 1.00 14.96 ? 4437 VAL A CG1   1 
ATOM   21984 C  CG2   . VAL A 1 4437 ? 200.969 167.254 208.128 1.00 19.78 ? 4437 VAL A CG2   1 
ATOM   21985 N  N     . CYS A 1 4438 ? 200.257 164.081 211.363 1.00 26.23 ? 4438 CYS A N     1 
ATOM   21986 C  CA    . CYS A 1 4438 ? 200.194 163.551 212.718 1.00 27.38 ? 4438 CYS A CA    1 
ATOM   21987 C  C     . CYS A 1 4438 ? 200.978 162.256 212.882 1.00 27.34 ? 4438 CYS A C     1 
ATOM   21988 O  O     . CYS A 1 4438 ? 201.140 161.790 214.015 1.00 33.98 ? 4438 CYS A O     1 
ATOM   21989 C  CB    . CYS A 1 4438 ? 198.737 163.340 213.130 1.00 22.33 ? 4438 CYS A CB    1 
ATOM   21990 S  SG    . CYS A 1 4438 ? 197.774 164.867 213.210 1.00 55.20 ? 4438 CYS A SG    1 
ATOM   21991 N  N     . GLU A 1 4439 ? 201.448 161.659 211.793 1.00 25.73 ? 4439 GLU A N     1 
ATOM   21992 C  CA    . GLU A 1 4439 ? 202.392 160.554 211.859 1.00 22.07 ? 4439 GLU A CA    1 
ATOM   21993 C  C     . GLU A 1 4439 ? 203.830 161.010 211.663 1.00 27.41 ? 4439 GLU A C     1 
ATOM   21994 O  O     . GLU A 1 4439 ? 204.733 160.168 211.616 1.00 34.31 ? 4439 GLU A O     1 
ATOM   21995 C  CB    . GLU A 1 4439 ? 202.033 159.486 210.823 1.00 25.83 ? 4439 GLU A CB    1 
ATOM   21996 C  CG    . GLU A 1 4439 ? 200.922 158.552 211.267 1.00 25.76 ? 4439 GLU A CG    1 
ATOM   21997 C  CD    . GLU A 1 4439 ? 200.515 157.571 210.184 1.00 34.30 ? 4439 GLU A CD    1 
ATOM   21998 O  OE1   . GLU A 1 4439 ? 201.079 157.641 209.073 1.00 35.20 ? 4439 GLU A OE1   1 
ATOM   21999 O  OE2   . GLU A 1 4439 ? 199.629 156.729 210.446 1.00 37.10 ? 4439 GLU A OE2   1 
ATOM   22000 N  N     . GLY A 1 4440 ? 204.060 162.315 211.555 1.00 28.04 ? 4440 GLY A N     1 
ATOM   22001 C  CA    . GLY A 1 4440 ? 205.404 162.839 211.374 1.00 23.27 ? 4440 GLY A CA    1 
ATOM   22002 C  C     . GLY A 1 4440 ? 206.065 162.411 210.083 1.00 27.55 ? 4440 GLY A C     1 
ATOM   22003 O  O     . GLY A 1 4440 ? 207.251 162.059 210.084 1.00 32.90 ? 4440 GLY A O     1 
ATOM   22004 N  N     . LYS A 1 4441 ? 205.323 162.435 208.974 1.00 25.86 ? 4441 LYS A N     1 
ATOM   22005 C  CA    . LYS A 1 4441 ? 205.862 162.036 207.684 1.00 27.07 ? 4441 LYS A CA    1 
ATOM   22006 C  C     . LYS A 1 4441 ? 205.906 163.153 206.650 1.00 28.13 ? 4441 LYS A C     1 
ATOM   22007 O  O     . LYS A 1 4441 ? 206.691 163.052 205.702 1.00 35.52 ? 4441 LYS A O     1 
ATOM   22008 C  CB    . LYS A 1 4441 ? 205.064 160.856 207.105 1.00 28.48 ? 4441 LYS A CB    1 
ATOM   22009 C  CG    . LYS A 1 4441 ? 205.031 159.628 208.001 1.00 29.43 ? 4441 LYS A CG    1 
ATOM   22010 C  CD    . LYS A 1 4441 ? 204.178 158.529 207.389 1.00 31.79 ? 4441 LYS A CD    1 
ATOM   22011 C  CE    . LYS A 1 4441 ? 204.236 157.256 208.216 1.00 34.04 ? 4441 LYS A CE    1 
ATOM   22012 N  NZ    . LYS A 1 4441 ? 203.371 156.188 207.644 1.00 33.58 ? 4441 LYS A NZ    1 
ATOM   22013 N  N     . LYS A 1 4442 ? 205.100 164.201 206.794 1.00 26.04 ? 4442 LYS A N     1 
ATOM   22014 C  CA    . LYS A 1 4442 ? 205.199 165.377 205.944 1.00 24.97 ? 4442 LYS A CA    1 
ATOM   22015 C  C     . LYS A 1 4442 ? 205.177 166.628 206.810 1.00 21.64 ? 4442 LYS A C     1 
ATOM   22016 O  O     . LYS A 1 4442 ? 204.510 166.664 207.849 1.00 14.92 ? 4442 LYS A O     1 
ATOM   22017 C  CB    . LYS A 1 4442 ? 204.077 165.424 204.893 1.00 25.31 ? 4442 LYS A CB    1 
ATOM   22018 C  CG    . LYS A 1 4442 ? 202.685 165.650 205.444 1.00 25.72 ? 4442 LYS A CG    1 
ATOM   22019 C  CD    . LYS A 1 4442 ? 201.710 166.017 204.338 1.00 22.36 ? 4442 LYS A CD    1 
ATOM   22020 C  CE    . LYS A 1 4442 ? 202.173 167.249 203.583 1.00 23.50 ? 4442 LYS A CE    1 
ATOM   22021 N  NZ    . LYS A 1 4442 ? 201.198 167.670 202.541 1.00 25.39 ? 4442 LYS A NZ    1 
ATOM   22022 N  N     . LYS A 1 4443 ? 205.917 167.645 206.380 1.00 24.09 ? 4443 LYS A N     1 
ATOM   22023 C  CA    . LYS A 1 4443 ? 206.120 168.842 207.184 1.00 16.96 ? 4443 LYS A CA    1 
ATOM   22024 C  C     . LYS A 1 4443 ? 204.893 169.748 207.134 1.00 17.49 ? 4443 LYS A C     1 
ATOM   22025 O  O     . LYS A 1 4443 ? 204.196 169.838 206.121 1.00 24.73 ? 4443 LYS A O     1 
ATOM   22026 C  CB    . LYS A 1 4443 ? 207.375 169.578 206.702 1.00 14.84 ? 4443 LYS A CB    1 
ATOM   22027 C  CG    . LYS A 1 4443 ? 207.748 170.850 207.453 1.00 18.02 ? 4443 LYS A CG    1 
ATOM   22028 C  CD    . LYS A 1 4443 ? 207.169 172.085 206.782 1.00 20.76 ? 4443 LYS A CD    1 
ATOM   22029 C  CE    . LYS A 1 4443 ? 207.870 172.364 205.465 1.00 23.16 ? 4443 LYS A CE    1 
ATOM   22030 N  NZ    . LYS A 1 4443 ? 207.331 173.575 204.789 1.00 25.99 ? 4443 LYS A NZ    1 
ATOM   22031 N  N     . GLN A 1 4444 ? 204.637 170.428 208.251 1.00 16.49 ? 4444 GLN A N     1 
ATOM   22032 C  CA    . GLN A 1 4444 ? 203.452 171.267 208.375 1.00 18.93 ? 4444 GLN A CA    1 
ATOM   22033 C  C     . GLN A 1 4444 ? 203.612 172.560 207.584 1.00 17.39 ? 4444 GLN A C     1 
ATOM   22034 O  O     . GLN A 1 4444 ? 204.510 173.361 207.858 1.00 21.31 ? 4444 GLN A O     1 
ATOM   22035 C  CB    . GLN A 1 4444 ? 203.189 171.583 209.844 1.00 15.69 ? 4444 GLN A CB    1 
ATOM   22036 C  CG    . GLN A 1 4444 ? 201.727 171.573 210.239 1.00 18.72 ? 4444 GLN A CG    1 
ATOM   22037 C  CD    . GLN A 1 4444 ? 201.538 171.540 211.741 1.00 24.01 ? 4444 GLN A CD    1 
ATOM   22038 O  OE1   . GLN A 1 4444 ? 202.487 171.319 212.492 1.00 31.98 ? 4444 GLN A OE1   1 
ATOM   22039 N  NE2   . GLN A 1 4444 ? 200.310 171.773 212.190 1.00 22.00 ? 4444 GLN A NE2   1 
ATOM   22040 N  N     . THR A 1 4445 ? 202.723 172.776 206.618 1.00 17.33 ? 4445 THR A N     1 
ATOM   22041 C  CA    . THR A 1 4445 ? 202.711 173.988 205.817 1.00 11.95 ? 4445 THR A CA    1 
ATOM   22042 C  C     . THR A 1 4445 ? 201.748 175.004 206.429 1.00 10.51 ? 4445 THR A C     1 
ATOM   22043 O  O     . THR A 1 4445 ? 201.067 174.734 207.420 1.00 15.12 ? 4445 THR A O     1 
ATOM   22044 C  CB    . THR A 1 4445 ? 202.328 173.672 204.369 1.00 7.28  ? 4445 THR A CB    1 
ATOM   22045 O  OG1   . THR A 1 4445 ? 200.910 173.488 204.274 1.00 8.76  ? 4445 THR A OG1   1 
ATOM   22046 C  CG2   . THR A 1 4445 ? 203.028 172.409 203.902 1.00 8.15  ? 4445 THR A CG2   1 
ATOM   22047 N  N     . ASN A 1 4446 ? 201.697 176.195 205.826 1.00 9.03  ? 4446 ASN A N     1 
ATOM   22048 C  CA    . ASN A 1 4446 ? 200.787 177.229 206.310 1.00 11.36 ? 4446 ASN A CA    1 
ATOM   22049 C  C     . ASN A 1 4446 ? 199.334 176.790 206.191 1.00 9.68  ? 4446 ASN A C     1 
ATOM   22050 O  O     . ASN A 1 4446 ? 198.535 177.007 207.109 1.00 13.52 ? 4446 ASN A O     1 
ATOM   22051 C  CB    . ASN A 1 4446 ? 201.010 178.533 205.544 1.00 5.86  ? 4446 ASN A CB    1 
ATOM   22052 C  CG    . ASN A 1 4446 ? 202.257 179.260 205.988 1.00 6.29  ? 4446 ASN A CG    1 
ATOM   22053 O  OD1   . ASN A 1 4446 ? 202.668 179.159 207.142 1.00 15.85 ? 4446 ASN A OD1   1 
ATOM   22054 N  ND2   . ASN A 1 4446 ? 202.869 180.001 205.072 1.00 4.13  ? 4446 ASN A ND2   1 
ATOM   22055 N  N     . TYR A 1 4447 ? 198.971 176.176 205.062 1.00 6.19  ? 4447 TYR A N     1 
ATOM   22056 C  CA    . TYR A 1 4447 ? 197.608 175.686 204.894 1.00 11.89 ? 4447 TYR A CA    1 
ATOM   22057 C  C     . TYR A 1 4447 ? 197.282 174.608 205.918 1.00 15.74 ? 4447 TYR A C     1 
ATOM   22058 O  O     . TYR A 1 4447 ? 196.200 174.615 206.516 1.00 12.64 ? 4447 TYR A O     1 
ATOM   22059 C  CB    . TYR A 1 4447 ? 197.416 175.149 203.475 1.00 8.59  ? 4447 TYR A CB    1 
ATOM   22060 C  CG    . TYR A 1 4447 ? 196.068 174.509 203.244 1.00 13.80 ? 4447 TYR A CG    1 
ATOM   22061 C  CD1   . TYR A 1 4447 ? 194.939 175.288 203.028 1.00 16.80 ? 4447 TYR A CD1   1 
ATOM   22062 C  CD2   . TYR A 1 4447 ? 195.921 173.128 203.249 1.00 19.25 ? 4447 TYR A CD2   1 
ATOM   22063 C  CE1   . TYR A 1 4447 ? 193.703 174.709 202.819 1.00 21.81 ? 4447 TYR A CE1   1 
ATOM   22064 C  CE2   . TYR A 1 4447 ? 194.689 172.540 203.041 1.00 18.76 ? 4447 TYR A CE2   1 
ATOM   22065 C  CZ    . TYR A 1 4447 ? 193.583 173.336 202.826 1.00 24.34 ? 4447 TYR A CZ    1 
ATOM   22066 O  OH    . TYR A 1 4447 ? 192.353 172.758 202.620 1.00 28.56 ? 4447 TYR A OH    1 
ATOM   22067 N  N     . LEU A 1 4448 ? 198.209 173.675 206.135 1.00 15.21 ? 4448 LEU A N     1 
ATOM   22068 C  CA    . LEU A 1 4448 ? 197.982 172.615 207.109 1.00 10.50 ? 4448 LEU A CA    1 
ATOM   22069 C  C     . LEU A 1 4448 ? 197.908 173.171 208.526 1.00 15.54 ? 4448 LEU A C     1 
ATOM   22070 O  O     . LEU A 1 4448 ? 197.094 172.712 209.333 1.00 24.80 ? 4448 LEU A O     1 
ATOM   22071 C  CB    . LEU A 1 4448 ? 199.076 171.556 206.994 1.00 12.51 ? 4448 LEU A CB    1 
ATOM   22072 C  CG    . LEU A 1 4448 ? 198.988 170.689 205.736 1.00 14.75 ? 4448 LEU A CG    1 
ATOM   22073 C  CD1   . LEU A 1 4448 ? 200.159 169.731 205.655 1.00 15.48 ? 4448 LEU A CD1   1 
ATOM   22074 C  CD2   . LEU A 1 4448 ? 197.667 169.932 205.697 1.00 11.32 ? 4448 LEU A CD2   1 
ATOM   22075 N  N     . ARG A 1 4449 ? 198.743 174.165 208.843 1.00 12.94 ? 4449 ARG A N     1 
ATOM   22076 C  CA    . ARG A 1 4449 ? 198.666 174.797 210.156 1.00 12.28 ? 4449 ARG A CA    1 
ATOM   22077 C  C     . ARG A 1 4449 ? 197.303 175.441 210.374 1.00 15.07 ? 4449 ARG A C     1 
ATOM   22078 O  O     . ARG A 1 4449 ? 196.717 175.325 211.458 1.00 16.55 ? 4449 ARG A O     1 
ATOM   22079 C  CB    . ARG A 1 4449 ? 199.779 175.834 210.312 1.00 12.18 ? 4449 ARG A CB    1 
ATOM   22080 C  CG    . ARG A 1 4449 ? 201.150 175.246 210.596 1.00 16.60 ? 4449 ARG A CG    1 
ATOM   22081 C  CD    . ARG A 1 4449 ? 202.150 176.329 210.987 1.00 15.62 ? 4449 ARG A CD    1 
ATOM   22082 N  NE    . ARG A 1 4449 ? 202.908 176.826 209.844 1.00 12.12 ? 4449 ARG A NE    1 
ATOM   22083 C  CZ    . ARG A 1 4449 ? 203.865 176.151 209.221 1.00 15.76 ? 4449 ARG A CZ    1 
ATOM   22084 N  NH1   . ARG A 1 4449 ? 204.231 174.943 209.620 1.00 17.61 ? 4449 ARG A NH1   1 
ATOM   22085 N  NH2   . ARG A 1 4449 ? 204.471 176.702 208.174 1.00 10.53 ? 4449 ARG A NH2   1 
ATOM   22086 N  N     . THR A 1 4450 ? 196.782 176.128 209.355 1.00 14.59 ? 4450 THR A N     1 
ATOM   22087 C  CA    . THR A 1 4450 ? 195.456 176.728 209.464 1.00 14.08 ? 4450 THR A CA    1 
ATOM   22088 C  C     . THR A 1 4450 ? 194.375 175.661 209.595 1.00 20.65 ? 4450 THR A C     1 
ATOM   22089 O  O     . THR A 1 4450 ? 193.463 175.786 210.422 1.00 16.88 ? 4450 THR A O     1 
ATOM   22090 C  CB    . THR A 1 4450 ? 195.188 177.621 208.251 1.00 10.15 ? 4450 THR A CB    1 
ATOM   22091 O  OG1   . THR A 1 4450 ? 196.014 178.789 208.326 1.00 24.96 ? 4450 THR A OG1   1 
ATOM   22092 C  CG2   . THR A 1 4450 ? 193.730 178.042 208.199 1.00 9.91  ? 4450 THR A CG2   1 
ATOM   22093 N  N     . LEU A 1 4451 ? 194.465 174.600 208.791 1.00 15.40 ? 4451 LEU A N     1 
ATOM   22094 C  CA    . LEU A 1 4451 ? 193.469 173.536 208.851 1.00 14.44 ? 4451 LEU A CA    1 
ATOM   22095 C  C     . LEU A 1 4451 ? 193.535 172.784 210.174 1.00 19.78 ? 4451 LEU A C     1 
ATOM   22096 O  O     . LEU A 1 4451 ? 192.498 172.458 210.761 1.00 23.75 ? 4451 LEU A O     1 
ATOM   22097 C  CB    . LEU A 1 4451 ? 193.663 172.577 207.677 1.00 16.71 ? 4451 LEU A CB    1 
ATOM   22098 C  CG    . LEU A 1 4451 ? 192.801 171.315 207.636 1.00 12.68 ? 4451 LEU A CG    1 
ATOM   22099 C  CD1   . LEU A 1 4451 ? 191.364 171.656 207.307 1.00 18.11 ? 4451 LEU A CD1   1 
ATOM   22100 C  CD2   . LEU A 1 4451 ? 193.361 170.336 206.623 1.00 15.33 ? 4451 LEU A CD2   1 
ATOM   22101 N  N     . ILE A 1 4452 ? 194.746 172.505 210.657 1.00 20.80 ? 4452 ILE A N     1 
ATOM   22102 C  CA    . ILE A 1 4452 ? 194.896 171.747 211.894 1.00 18.34 ? 4452 ILE A CA    1 
ATOM   22103 C  C     . ILE A 1 4452 ? 194.374 172.547 213.082 1.00 15.50 ? 4452 ILE A C     1 
ATOM   22104 O  O     . ILE A 1 4452 ? 193.747 171.991 213.992 1.00 19.95 ? 4452 ILE A O     1 
ATOM   22105 C  CB    . ILE A 1 4452 ? 196.364 171.320 212.076 1.00 14.64 ? 4452 ILE A CB    1 
ATOM   22106 C  CG1   . ILE A 1 4452 ? 196.668 170.122 211.174 1.00 18.55 ? 4452 ILE A CG1   1 
ATOM   22107 C  CG2   . ILE A 1 4452 ? 196.669 171.002 213.529 1.00 15.50 ? 4452 ILE A CG2   1 
ATOM   22108 C  CD1   . ILE A 1 4452 ? 198.045 169.534 211.364 1.00 19.22 ? 4452 ILE A CD1   1 
ATOM   22109 N  N     . ASN A 1 4453 ? 194.606 173.862 213.089 1.00 17.66 ? 4453 ASN A N     1 
ATOM   22110 C  CA    . ASN A 1 4453 ? 194.092 174.693 214.173 1.00 20.57 ? 4453 ASN A CA    1 
ATOM   22111 C  C     . ASN A 1 4453 ? 192.570 174.654 214.229 1.00 19.22 ? 4453 ASN A C     1 
ATOM   22112 O  O     . ASN A 1 4453 ? 191.986 174.551 215.314 1.00 20.55 ? 4453 ASN A O     1 
ATOM   22113 C  CB    . ASN A 1 4453 ? 194.589 176.131 214.021 1.00 18.03 ? 4453 ASN A CB    1 
ATOM   22114 C  CG    . ASN A 1 4453 ? 195.947 176.348 214.663 1.00 31.16 ? 4453 ASN A CG    1 
ATOM   22115 O  OD1   . ASN A 1 4453 ? 196.888 176.808 214.014 1.00 31.11 ? 4453 ASN A OD1   1 
ATOM   22116 N  ND2   . ASN A 1 4453 ? 196.056 176.015 215.943 1.00 28.58 ? 4453 ASN A ND2   1 
ATOM   22117 N  N     . GLU A 1 4454 ? 191.910 174.732 213.070 1.00 17.84 ? 4454 GLU A N     1 
ATOM   22118 C  CA    . GLU A 1 4454 ? 190.451 174.652 213.043 1.00 14.82 ? 4454 GLU A CA    1 
ATOM   22119 C  C     . GLU A 1 4454 ? 189.960 173.302 213.548 1.00 15.89 ? 4454 GLU A C     1 
ATOM   22120 O  O     . GLU A 1 4454 ? 188.997 173.231 214.319 1.00 15.49 ? 4454 GLU A O     1 
ATOM   22121 C  CB    . GLU A 1 4454 ? 189.937 174.906 211.627 1.00 16.19 ? 4454 GLU A CB    1 
ATOM   22122 C  CG    . GLU A 1 4454 ? 189.993 176.353 211.183 1.00 16.90 ? 4454 GLU A CG    1 
ATOM   22123 C  CD    . GLU A 1 4454 ? 190.066 176.489 209.675 1.00 24.88 ? 4454 GLU A CD    1 
ATOM   22124 O  OE1   . GLU A 1 4454 ? 190.184 175.451 208.991 1.00 22.25 ? 4454 GLU A OE1   1 
ATOM   22125 O  OE2   . GLU A 1 4454 ? 190.003 177.631 209.173 1.00 28.50 ? 4454 GLU A OE2   1 
ATOM   22126 N  N     . LEU A 1 4455 ? 190.613 172.218 213.126 1.00 16.88 ? 4455 LEU A N     1 
ATOM   22127 C  CA    . LEU A 1 4455 ? 190.178 170.883 213.522 1.00 19.03 ? 4455 LEU A CA    1 
ATOM   22128 C  C     . LEU A 1 4455 ? 190.333 170.667 215.024 1.00 20.21 ? 4455 LEU A C     1 
ATOM   22129 O  O     . LEU A 1 4455 ? 189.498 170.001 215.647 1.00 25.01 ? 4455 LEU A O     1 
ATOM   22130 C  CB    . LEU A 1 4455 ? 190.959 169.829 212.741 1.00 19.87 ? 4455 LEU A CB    1 
ATOM   22131 C  CG    . LEU A 1 4455 ? 190.617 169.737 211.253 1.00 20.55 ? 4455 LEU A CG    1 
ATOM   22132 C  CD1   . LEU A 1 4455 ? 191.364 168.590 210.590 1.00 14.98 ? 4455 LEU A CD1   1 
ATOM   22133 C  CD2   . LEU A 1 4455 ? 189.115 169.591 211.060 1.00 13.86 ? 4455 LEU A CD2   1 
ATOM   22134 N  N     . VAL A 1 4456 ? 191.398 171.209 215.619 1.00 18.64 ? 4456 VAL A N     1 
ATOM   22135 C  CA    . VAL A 1 4456 ? 191.569 171.106 217.066 1.00 20.54 ? 4456 VAL A CA    1 
ATOM   22136 C  C     . VAL A 1 4456 ? 190.460 171.857 217.791 1.00 20.18 ? 4456 VAL A C     1 
ATOM   22137 O  O     . VAL A 1 4456 ? 189.896 171.363 218.773 1.00 24.08 ? 4456 VAL A O     1 
ATOM   22138 C  CB    . VAL A 1 4456 ? 192.965 171.611 217.481 1.00 19.85 ? 4456 VAL A CB    1 
ATOM   22139 C  CG1   . VAL A 1 4456 ? 193.094 171.620 218.991 1.00 19.11 ? 4456 VAL A CG1   1 
ATOM   22140 C  CG2   . VAL A 1 4456 ? 194.041 170.727 216.879 1.00 12.21 ? 4456 VAL A CG2   1 
ATOM   22141 N  N     . LYS A 1 4457 ? 190.124 173.056 217.316 1.00 17.89 ? 4457 LYS A N     1 
ATOM   22142 C  CA    . LYS A 1 4457 ? 189.064 173.843 217.933 1.00 22.14 ? 4457 LYS A CA    1 
ATOM   22143 C  C     . LYS A 1 4457 ? 187.668 173.363 217.560 1.00 24.56 ? 4457 LYS A C     1 
ATOM   22144 O  O     . LYS A 1 4457 ? 186.689 173.867 218.119 1.00 27.47 ? 4457 LYS A O     1 
ATOM   22145 C  CB    . LYS A 1 4457 ? 189.209 175.320 217.558 1.00 21.95 ? 4457 LYS A CB    1 
ATOM   22146 C  CG    . LYS A 1 4457 ? 190.514 175.955 218.012 1.00 22.16 ? 4457 LYS A CG    1 
ATOM   22147 C  CD    . LYS A 1 4457 ? 190.639 177.386 217.508 1.00 22.94 ? 4457 LYS A CD    1 
ATOM   22148 C  CE    . LYS A 1 4457 ? 190.628 177.449 215.990 1.00 25.72 ? 4457 LYS A CE    1 
ATOM   22149 N  NZ    . LYS A 1 4457 ? 190.709 178.852 215.495 1.00 31.93 ? 4457 LYS A NZ    1 
ATOM   22150 N  N     . GLY A 1 4458 ? 187.549 172.415 216.631 1.00 21.26 ? 4458 GLY A N     1 
ATOM   22151 C  CA    . GLY A 1 4458 ? 186.253 171.909 216.237 1.00 19.42 ? 4458 GLY A CA    1 
ATOM   22152 C  C     . GLY A 1 4458 ? 185.476 172.794 215.291 1.00 23.15 ? 4458 GLY A C     1 
ATOM   22153 O  O     . GLY A 1 4458 ? 184.300 172.515 215.033 1.00 24.28 ? 4458 GLY A O     1 
ATOM   22154 N  N     . ILE A 1 4459 ? 186.087 173.852 214.773 1.00 21.49 ? 4459 ILE A N     1 
ATOM   22155 C  CA    . ILE A 1 4459 ? 185.421 174.734 213.824 1.00 18.74 ? 4459 ILE A CA    1 
ATOM   22156 C  C     . ILE A 1 4459 ? 185.486 174.111 212.437 1.00 25.46 ? 4459 ILE A C     1 
ATOM   22157 O  O     . ILE A 1 4459 ? 186.510 173.545 212.038 1.00 23.48 ? 4459 ILE A O     1 
ATOM   22158 C  CB    . ILE A 1 4459 ? 186.064 176.132 213.843 1.00 18.32 ? 4459 ILE A CB    1 
ATOM   22159 C  CG1   . ILE A 1 4459 ? 185.984 176.735 215.246 1.00 25.37 ? 4459 ILE A CG1   1 
ATOM   22160 C  CG2   . ILE A 1 4459 ? 185.395 177.048 212.831 1.00 20.18 ? 4459 ILE A CG2   1 
ATOM   22161 C  CD1   . ILE A 1 4459 ? 186.671 178.077 215.372 1.00 22.57 ? 4459 ILE A CD1   1 
ATOM   22162 N  N     . LEU A 1 4460 ? 184.379 174.194 211.707 1.00 24.68 ? 4460 LEU A N     1 
ATOM   22163 C  CA    . LEU A 1 4460 ? 184.346 173.695 210.343 1.00 19.54 ? 4460 LEU A CA    1 
ATOM   22164 C  C     . LEU A 1 4460 ? 185.274 174.532 209.467 1.00 22.70 ? 4460 LEU A C     1 
ATOM   22165 O  O     . LEU A 1 4460 ? 185.161 175.765 209.456 1.00 25.99 ? 4460 LEU A O     1 
ATOM   22166 C  CB    . LEU A 1 4460 ? 182.920 173.740 209.798 1.00 23.28 ? 4460 LEU A CB    1 
ATOM   22167 C  CG    . LEU A 1 4460 ? 182.731 173.526 208.297 1.00 20.96 ? 4460 LEU A CG    1 
ATOM   22168 C  CD1   . LEU A 1 4460 ? 183.127 172.116 207.901 1.00 18.27 ? 4460 LEU A CD1   1 
ATOM   22169 C  CD2   . LEU A 1 4460 ? 181.295 173.816 207.898 1.00 18.75 ? 4460 LEU A CD2   1 
ATOM   22170 N  N     . PRO A 1 4461 ? 186.208 173.914 208.742 1.00 24.44 ? 4461 PRO A N     1 
ATOM   22171 C  CA    . PRO A 1 4461 ? 187.115 174.689 207.889 1.00 17.96 ? 4461 PRO A CA    1 
ATOM   22172 C  C     . PRO A 1 4461 ? 186.354 175.470 206.828 1.00 22.54 ? 4461 PRO A C     1 
ATOM   22173 O  O     . PRO A 1 4461 ? 185.370 174.989 206.263 1.00 30.20 ? 4461 PRO A O     1 
ATOM   22174 C  CB    . PRO A 1 4461 ? 188.009 173.616 207.263 1.00 17.52 ? 4461 PRO A CB    1 
ATOM   22175 C  CG    . PRO A 1 4461 ? 187.977 172.498 208.243 1.00 17.13 ? 4461 PRO A CG    1 
ATOM   22176 C  CD    . PRO A 1 4461 ? 186.581 172.491 208.786 1.00 19.58 ? 4461 PRO A CD    1 
ATOM   22177 N  N     . ARG A 1 4462 ? 186.825 176.690 206.560 1.00 25.89 ? 4462 ARG A N     1 
ATOM   22178 C  CA    . ARG A 1 4462 ? 186.174 177.522 205.555 1.00 22.11 ? 4462 ARG A CA    1 
ATOM   22179 C  C     . ARG A 1 4462 ? 186.394 176.979 204.150 1.00 23.36 ? 4462 ARG A C     1 
ATOM   22180 O  O     . ARG A 1 4462 ? 185.563 177.209 203.263 1.00 24.87 ? 4462 ARG A O     1 
ATOM   22181 C  CB    . ARG A 1 4462 ? 186.674 178.963 205.658 1.00 19.76 ? 4462 ARG A CB    1 
ATOM   22182 C  CG    . ARG A 1 4462 ? 186.364 179.655 206.983 1.00 27.11 ? 4462 ARG A CG    1 
ATOM   22183 C  CD    . ARG A 1 4462 ? 184.864 179.736 207.266 1.00 28.89 ? 4462 ARG A CD    1 
ATOM   22184 N  NE    . ARG A 1 4462 ? 184.355 178.544 207.937 1.00 30.67 ? 4462 ARG A NE    1 
ATOM   22185 C  CZ    . ARG A 1 4462 ? 183.078 178.333 208.224 1.00 36.81 ? 4462 ARG A CZ    1 
ATOM   22186 N  NH1   . ARG A 1 4462 ? 182.143 179.215 207.913 1.00 37.98 ? 4462 ARG A NH1   1 
ATOM   22187 N  NH2   . ARG A 1 4462 ? 182.729 177.205 208.839 1.00 30.19 ? 4462 ARG A NH2   1 
ATOM   22188 N  N     . SER A 1 4463 ? 187.500 176.266 203.926 1.00 24.72 ? 4463 SER A N     1 
ATOM   22189 C  CA    . SER A 1 4463 ? 187.714 175.623 202.635 1.00 16.96 ? 4463 SER A CA    1 
ATOM   22190 C  C     . SER A 1 4463 ? 186.663 174.553 202.377 1.00 26.27 ? 4463 SER A C     1 
ATOM   22191 O  O     . SER A 1 4463 ? 186.160 174.422 201.254 1.00 24.33 ? 4463 SER A O     1 
ATOM   22192 C  CB    . SER A 1 4463 ? 189.117 175.020 202.576 1.00 20.23 ? 4463 SER A CB    1 
ATOM   22193 O  OG    . SER A 1 4463 ? 190.100 175.980 202.919 1.00 29.03 ? 4463 SER A OG    1 
ATOM   22194 N  N     . TRP A 1 4464 ? 186.319 173.779 203.410 1.00 21.98 ? 4464 TRP A N     1 
ATOM   22195 C  CA    . TRP A 1 4464 ? 185.325 172.724 203.259 1.00 17.61 ? 4464 TRP A CA    1 
ATOM   22196 C  C     . TRP A 1 4464 ? 183.934 173.291 203.006 1.00 17.43 ? 4464 TRP A C     1 
ATOM   22197 O  O     . TRP A 1 4464 ? 183.120 172.651 202.328 1.00 19.67 ? 4464 TRP A O     1 
ATOM   22198 C  CB    . TRP A 1 4464 ? 185.319 171.840 204.507 1.00 17.91 ? 4464 TRP A CB    1 
ATOM   22199 C  CG    . TRP A 1 4464 ? 186.548 170.993 204.652 1.00 20.06 ? 4464 TRP A CG    1 
ATOM   22200 C  CD1   . TRP A 1 4464 ? 187.691 171.074 203.914 1.00 19.42 ? 4464 TRP A CD1   1 
ATOM   22201 C  CD2   . TRP A 1 4464 ? 186.765 169.952 205.611 1.00 15.69 ? 4464 TRP A CD2   1 
ATOM   22202 N  NE1   . TRP A 1 4464 ? 188.600 170.142 204.344 1.00 20.47 ? 4464 TRP A NE1   1 
ATOM   22203 C  CE2   . TRP A 1 4464 ? 188.057 169.441 205.386 1.00 16.55 ? 4464 TRP A CE2   1 
ATOM   22204 C  CE3   . TRP A 1 4464 ? 185.989 169.399 206.634 1.00 16.14 ? 4464 TRP A CE3   1 
ATOM   22205 C  CZ2   . TRP A 1 4464 ? 188.593 168.405 206.147 1.00 20.37 ? 4464 TRP A CZ2   1 
ATOM   22206 C  CZ3   . TRP A 1 4464 ? 186.522 168.370 207.387 1.00 14.09 ? 4464 TRP A CZ3   1 
ATOM   22207 C  CH2   . TRP A 1 4464 ? 187.810 167.884 207.139 1.00 17.64 ? 4464 TRP A CH2   1 
ATOM   22208 N  N     . SER A 1 4465 ? 183.645 174.480 203.531 1.00 18.52 ? 4465 SER A N     1 
ATOM   22209 C  CA    . SER A 1 4465 ? 182.318 175.074 203.403 1.00 20.28 ? 4465 SER A CA    1 
ATOM   22210 C  C     . SER A 1 4465 ? 182.076 175.480 201.955 1.00 18.23 ? 4465 SER A C     1 
ATOM   22211 O  O     . SER A 1 4465 ? 182.577 176.510 201.496 1.00 28.53 ? 4465 SER A O     1 
ATOM   22212 C  CB    . SER A 1 4465 ? 182.186 176.273 204.336 1.00 21.60 ? 4465 SER A CB    1 
ATOM   22213 O  OG    . SER A 1 4465 ? 183.179 177.244 204.060 1.00 30.13 ? 4465 SER A OG    1 
ATOM   22214 N  N     . HIS A 1 4466 ? 181.303 174.670 201.236 1.00 19.65 ? 4466 HIS A N     1 
ATOM   22215 C  CA    . HIS A 1 4466 ? 180.965 174.942 199.846 1.00 23.47 ? 4466 HIS A CA    1 
ATOM   22216 C  C     . HIS A 1 4466 ? 179.474 174.909 199.560 1.00 22.35 ? 4466 HIS A C     1 
ATOM   22217 O  O     . HIS A 1 4466 ? 179.050 175.480 198.548 1.00 30.39 ? 4466 HIS A O     1 
ATOM   22218 C  CB    . HIS A 1 4466 ? 181.671 173.945 198.915 1.00 22.40 ? 4466 HIS A CB    1 
ATOM   22219 C  CG    . HIS A 1 4466 ? 183.134 174.210 198.749 1.00 25.26 ? 4466 HIS A CG    1 
ATOM   22220 N  ND1   . HIS A 1 4466 ? 184.026 173.240 198.346 1.00 28.78 ? 4466 HIS A ND1   1 
ATOM   22221 C  CD2   . HIS A 1 4466 ? 183.863 175.337 198.935 1.00 21.74 ? 4466 HIS A CD2   1 
ATOM   22222 C  CE1   . HIS A 1 4466 ? 185.240 173.757 198.290 1.00 29.84 ? 4466 HIS A CE1   1 
ATOM   22223 N  NE2   . HIS A 1 4466 ? 185.169 175.028 198.643 1.00 26.92 ? 4466 HIS A NE2   1 
ATOM   22224 N  N     . TYR A 1 4467 ? 178.671 174.264 200.399 1.00 18.59 ? 4467 TYR A N     1 
ATOM   22225 C  CA    . TYR A 1 4467 ? 177.222 174.305 200.301 1.00 19.64 ? 4467 TYR A CA    1 
ATOM   22226 C  C     . TYR A 1 4467 ? 176.653 174.949 201.556 1.00 21.05 ? 4467 TYR A C     1 
ATOM   22227 O  O     . TYR A 1 4467 ? 177.210 174.814 202.650 1.00 19.86 ? 4467 TYR A O     1 
ATOM   22228 C  CB    . TYR A 1 4467 ? 176.631 172.901 200.103 1.00 17.15 ? 4467 TYR A CB    1 
ATOM   22229 C  CG    . TYR A 1 4467 ? 177.068 171.883 201.132 1.00 14.10 ? 4467 TYR A CG    1 
ATOM   22230 C  CD1   . TYR A 1 4467 ? 176.372 171.721 202.320 1.00 18.05 ? 4467 TYR A CD1   1 
ATOM   22231 C  CD2   . TYR A 1 4467 ? 178.179 171.081 200.911 1.00 15.56 ? 4467 TYR A CD2   1 
ATOM   22232 C  CE1   . TYR A 1 4467 ? 176.769 170.787 203.257 1.00 15.86 ? 4467 TYR A CE1   1 
ATOM   22233 C  CE2   . TYR A 1 4467 ? 178.582 170.144 201.840 1.00 13.40 ? 4467 TYR A CE2   1 
ATOM   22234 C  CZ    . TYR A 1 4467 ? 177.875 170.004 203.013 1.00 15.32 ? 4467 TYR A CZ    1 
ATOM   22235 O  OH    . TYR A 1 4467 ? 178.274 169.074 203.945 1.00 17.35 ? 4467 TYR A OH    1 
ATOM   22236 N  N     . THR A 1 4468 ? 175.541 175.660 201.384 1.00 19.15 ? 4468 THR A N     1 
ATOM   22237 C  CA    . THR A 1 4468 ? 174.952 176.415 202.482 1.00 17.01 ? 4468 THR A CA    1 
ATOM   22238 C  C     . THR A 1 4468 ? 174.540 175.499 203.632 1.00 20.10 ? 4468 THR A C     1 
ATOM   22239 O  O     . THR A 1 4468 ? 173.968 174.424 203.424 1.00 21.61 ? 4468 THR A O     1 
ATOM   22240 C  CB    . THR A 1 4468 ? 173.762 177.233 201.968 1.00 18.64 ? 4468 THR A CB    1 
ATOM   22241 O  OG1   . THR A 1 4468 ? 173.276 178.097 203.005 1.00 33.53 ? 4468 THR A OG1   1 
ATOM   22242 C  CG2   . THR A 1 4468 ? 172.651 176.342 201.450 1.00 15.53 ? 4468 THR A CG2   1 
ATOM   22243 N  N     . VAL A 1 4469 ? 174.868 175.921 204.848 1.00 20.58 ? 4469 VAL A N     1 
ATOM   22244 C  CA    . VAL A 1 4469 ? 174.620 175.137 206.055 1.00 18.49 ? 4469 VAL A CA    1 
ATOM   22245 C  C     . VAL A 1 4469 ? 174.038 176.062 207.113 1.00 23.12 ? 4469 VAL A C     1 
ATOM   22246 O  O     . VAL A 1 4469 ? 174.235 177.287 207.061 1.00 24.71 ? 4469 VAL A O     1 
ATOM   22247 C  CB    . VAL A 1 4469 ? 175.912 174.454 206.567 1.00 16.32 ? 4469 VAL A CB    1 
ATOM   22248 C  CG1   . VAL A 1 4469 ? 176.364 173.378 205.605 1.00 21.34 ? 4469 VAL A CG1   1 
ATOM   22249 C  CG2   . VAL A 1 4469 ? 177.008 175.485 206.780 1.00 26.34 ? 4469 VAL A CG2   1 
ATOM   22250 N  N     . PRO A 1 4470 ? 173.303 175.515 208.083 1.00 23.62 ? 4470 PRO A N     1 
ATOM   22251 C  CA    . PRO A 1 4470 ? 172.803 176.357 209.173 1.00 18.08 ? 4470 PRO A CA    1 
ATOM   22252 C  C     . PRO A 1 4470 ? 173.951 176.958 209.968 1.00 22.77 ? 4470 PRO A C     1 
ATOM   22253 O  O     . PRO A 1 4470 ? 174.986 176.321 210.179 1.00 23.70 ? 4470 PRO A O     1 
ATOM   22254 C  CB    . PRO A 1 4470 ? 171.971 175.389 210.018 1.00 14.78 ? 4470 PRO A CB    1 
ATOM   22255 C  CG    . PRO A 1 4470 ? 172.559 174.059 209.745 1.00 12.74 ? 4470 PRO A CG    1 
ATOM   22256 C  CD    . PRO A 1 4470 ? 172.995 174.091 208.309 1.00 15.66 ? 4470 PRO A CD    1 
ATOM   22257 N  N     . ALA A 1 4471 ? 173.759 178.200 210.405 1.00 29.20 ? 4471 ALA A N     1 
ATOM   22258 C  CA    . ALA A 1 4471 ? 174.795 178.895 211.156 1.00 25.34 ? 4471 ALA A CA    1 
ATOM   22259 C  C     . ALA A 1 4471 ? 175.060 178.190 212.479 1.00 27.04 ? 4471 ALA A C     1 
ATOM   22260 O  O     . ALA A 1 4471 ? 174.140 177.709 213.143 1.00 26.99 ? 4471 ALA A O     1 
ATOM   22261 C  CB    . ALA A 1 4471 ? 174.384 180.347 211.400 1.00 23.16 ? 4471 ALA A CB    1 
ATOM   22262 N  N     . GLY A 1 4472 ? 176.334 178.129 212.859 1.00 23.71 ? 4472 GLY A N     1 
ATOM   22263 C  CA    . GLY A 1 4472 ? 176.726 177.478 214.091 1.00 22.98 ? 4472 GLY A CA    1 
ATOM   22264 C  C     . GLY A 1 4472 ? 176.901 175.979 214.010 1.00 28.43 ? 4472 GLY A C     1 
ATOM   22265 O  O     . GLY A 1 4472 ? 176.808 175.306 215.042 1.00 25.59 ? 4472 GLY A O     1 
ATOM   22266 N  N     . MET A 1 4473 ? 177.145 175.435 212.822 1.00 28.58 ? 4473 MET A N     1 
ATOM   22267 C  CA    . MET A 1 4473 ? 177.319 173.998 212.662 1.00 24.36 ? 4473 MET A CA    1 
ATOM   22268 C  C     . MET A 1 4473 ? 178.790 173.636 212.827 1.00 24.15 ? 4473 MET A C     1 
ATOM   22269 O  O     . MET A 1 4473 ? 179.659 174.228 212.180 1.00 28.03 ? 4473 MET A O     1 
ATOM   22270 C  CB    . MET A 1 4473 ? 176.802 173.560 211.292 1.00 20.30 ? 4473 MET A CB    1 
ATOM   22271 C  CG    . MET A 1 4473 ? 177.241 172.181 210.847 1.00 21.32 ? 4473 MET A CG    1 
ATOM   22272 S  SD    . MET A 1 4473 ? 176.505 171.753 209.260 1.00 38.00 ? 4473 MET A SD    1 
ATOM   22273 C  CE    . MET A 1 4473 ? 176.245 169.996 209.461 1.00 16.76 ? 4473 MET A CE    1 
ATOM   22274 N  N     . THR A 1 4474 ? 179.071 172.665 213.694 1.00 18.21 ? 4474 THR A N     1 
ATOM   22275 C  CA    . THR A 1 4474 ? 180.445 172.306 214.008 1.00 18.63 ? 4474 THR A CA    1 
ATOM   22276 C  C     . THR A 1 4474 ? 180.961 171.247 213.035 1.00 21.97 ? 4474 THR A C     1 
ATOM   22277 O  O     . THR A 1 4474 ? 180.219 170.692 212.222 1.00 27.81 ? 4474 THR A O     1 
ATOM   22278 C  CB    . THR A 1 4474 ? 180.562 171.829 215.456 1.00 24.79 ? 4474 THR A CB    1 
ATOM   22279 O  OG1   . THR A 1 4474 ? 181.944 171.649 215.790 1.00 35.34 ? 4474 THR A OG1   1 
ATOM   22280 C  CG2   . THR A 1 4474 ? 179.835 170.517 215.648 1.00 18.22 ? 4474 THR A CG2   1 
ATOM   22281 N  N     . VAL A 1 4475 ? 182.262 170.964 213.122 1.00 23.84 ? 4475 VAL A N     1 
ATOM   22282 C  CA    . VAL A 1 4475 ? 182.912 170.108 212.135 1.00 18.60 ? 4475 VAL A CA    1 
ATOM   22283 C  C     . VAL A 1 4475 ? 182.477 168.650 212.272 1.00 16.93 ? 4475 VAL A C     1 
ATOM   22284 O  O     . VAL A 1 4475 ? 182.430 167.922 211.273 1.00 17.34 ? 4475 VAL A O     1 
ATOM   22285 C  CB    . VAL A 1 4475 ? 184.444 170.258 212.227 1.00 20.36 ? 4475 VAL A CB    1 
ATOM   22286 C  CG1   . VAL A 1 4475 ? 184.982 169.645 213.510 1.00 18.97 ? 4475 VAL A CG1   1 
ATOM   22287 C  CG2   . VAL A 1 4475 ? 185.117 169.641 211.005 1.00 15.55 ? 4475 VAL A CG2   1 
ATOM   22288 N  N     . ILE A 1 4476 ? 182.160 168.193 213.486 1.00 19.13 ? 4476 ILE A N     1 
ATOM   22289 C  CA    . ILE A 1 4476 ? 181.772 166.794 213.655 1.00 15.96 ? 4476 ILE A CA    1 
ATOM   22290 C  C     . ILE A 1 4476 ? 180.423 166.520 212.998 1.00 22.47 ? 4476 ILE A C     1 
ATOM   22291 O  O     . ILE A 1 4476 ? 180.200 165.427 212.462 1.00 24.40 ? 4476 ILE A O     1 
ATOM   22292 C  CB    . ILE A 1 4476 ? 181.786 166.405 215.147 1.00 19.30 ? 4476 ILE A CB    1 
ATOM   22293 C  CG1   . ILE A 1 4476 ? 181.955 164.893 215.301 1.00 19.17 ? 4476 ILE A CG1   1 
ATOM   22294 C  CG2   . ILE A 1 4476 ? 180.531 166.878 215.866 1.00 21.25 ? 4476 ILE A CG2   1 
ATOM   22295 C  CD1   . ILE A 1 4476 ? 182.119 164.443 216.735 1.00 22.00 ? 4476 ILE A CD1   1 
ATOM   22296 N  N     . GLN A 1 4477 ? 179.508 167.494 213.014 1.00 15.63 ? 4477 GLN A N     1 
ATOM   22297 C  CA    . GLN A 1 4477 ? 178.224 167.309 212.347 1.00 18.35 ? 4477 GLN A CA    1 
ATOM   22298 C  C     . GLN A 1 4477 ? 178.367 167.427 210.837 1.00 19.81 ? 4477 GLN A C     1 
ATOM   22299 O  O     . GLN A 1 4477 ? 177.668 166.739 210.086 1.00 20.54 ? 4477 GLN A O     1 
ATOM   22300 C  CB    . GLN A 1 4477 ? 177.206 168.327 212.864 1.00 23.61 ? 4477 GLN A CB    1 
ATOM   22301 C  CG    . GLN A 1 4477 ? 177.242 168.540 214.363 1.00 16.86 ? 4477 GLN A CG    1 
ATOM   22302 C  CD    . GLN A 1 4477 ? 176.201 169.536 214.832 1.00 21.92 ? 4477 GLN A CD    1 
ATOM   22303 O  OE1   . GLN A 1 4477 ? 176.481 170.728 214.957 1.00 21.47 ? 4477 GLN A OE1   1 
ATOM   22304 N  NE2   . GLN A 1 4477 ? 174.994 169.052 215.094 1.00 25.41 ? 4477 GLN A NE2   1 
ATOM   22305 N  N     . TRP A 1 4478 ? 179.265 168.300 210.376 1.00 22.88 ? 4478 TRP A N     1 
ATOM   22306 C  CA    . TRP A 1 4478 ? 179.457 168.482 208.942 1.00 14.94 ? 4478 TRP A CA    1 
ATOM   22307 C  C     . TRP A 1 4478 ? 179.983 167.214 208.283 1.00 15.32 ? 4478 TRP A C     1 
ATOM   22308 O  O     . TRP A 1 4478 ? 179.555 166.861 207.178 1.00 15.79 ? 4478 TRP A O     1 
ATOM   22309 C  CB    . TRP A 1 4478 ? 180.404 169.653 208.686 1.00 11.41 ? 4478 TRP A CB    1 
ATOM   22310 C  CG    . TRP A 1 4478 ? 180.388 170.131 207.272 1.00 13.99 ? 4478 TRP A CG    1 
ATOM   22311 C  CD1   . TRP A 1 4478 ? 179.593 171.103 206.743 1.00 15.18 ? 4478 TRP A CD1   1 
ATOM   22312 C  CD2   . TRP A 1 4478 ? 181.212 169.659 206.202 1.00 12.92 ? 4478 TRP A CD2   1 
ATOM   22313 N  NE1   . TRP A 1 4478 ? 179.872 171.267 205.409 1.00 17.63 ? 4478 TRP A NE1   1 
ATOM   22314 C  CE2   . TRP A 1 4478 ? 180.863 170.391 205.052 1.00 15.12 ? 4478 TRP A CE2   1 
ATOM   22315 C  CE3   . TRP A 1 4478 ? 182.213 168.688 206.103 1.00 14.13 ? 4478 TRP A CE3   1 
ATOM   22316 C  CZ2   . TRP A 1 4478 ? 181.474 170.182 203.821 1.00 17.14 ? 4478 TRP A CZ2   1 
ATOM   22317 C  CZ3   . TRP A 1 4478 ? 182.819 168.483 204.881 1.00 18.49 ? 4478 TRP A CZ3   1 
ATOM   22318 C  CH2   . TRP A 1 4478 ? 182.449 169.226 203.756 1.00 17.44 ? 4478 TRP A CH2   1 
ATOM   22319 N  N     . VAL A 1 4479 ? 180.912 166.518 208.939 1.00 14.15 ? 4479 VAL A N     1 
ATOM   22320 C  CA    . VAL A 1 4479 ? 181.474 165.301 208.357 1.00 15.97 ? 4479 VAL A CA    1 
ATOM   22321 C  C     . VAL A 1 4479 ? 180.388 164.245 208.187 1.00 14.64 ? 4479 VAL A C     1 
ATOM   22322 O  O     . VAL A 1 4479 ? 180.291 163.588 207.144 1.00 22.32 ? 4479 VAL A O     1 
ATOM   22323 C  CB    . VAL A 1 4479 ? 182.642 164.780 209.215 1.00 18.36 ? 4479 VAL A CB    1 
ATOM   22324 C  CG1   . VAL A 1 4479 ? 183.037 163.382 208.779 1.00 18.05 ? 4479 VAL A CG1   1 
ATOM   22325 C  CG2   . VAL A 1 4479 ? 183.828 165.723 209.119 1.00 15.43 ? 4479 VAL A CG2   1 
ATOM   22326 N  N     . SER A 1 4480 ? 179.550 164.070 209.213 1.00 17.48 ? 4480 SER A N     1 
ATOM   22327 C  CA    . SER A 1 4480 ? 178.431 163.141 209.101 1.00 14.20 ? 4480 SER A CA    1 
ATOM   22328 C  C     . SER A 1 4480 ? 177.437 163.599 208.042 1.00 16.54 ? 4480 SER A C     1 
ATOM   22329 O  O     . SER A 1 4480 ? 176.938 162.787 207.254 1.00 23.34 ? 4480 SER A O     1 
ATOM   22330 C  CB    . SER A 1 4480 ? 177.741 162.989 210.455 1.00 17.40 ? 4480 SER A CB    1 
ATOM   22331 O  OG    . SER A 1 4480 ? 177.515 164.252 211.051 1.00 23.78 ? 4480 SER A OG    1 
ATOM   22332 N  N     . ASP A 1 4481 ? 177.134 164.898 208.010 1.00 15.28 ? 4481 ASP A N     1 
ATOM   22333 C  CA    . ASP A 1 4481 ? 176.238 165.423 206.986 1.00 16.12 ? 4481 ASP A CA    1 
ATOM   22334 C  C     . ASP A 1 4481 ? 176.844 165.279 205.594 1.00 18.51 ? 4481 ASP A C     1 
ATOM   22335 O  O     . ASP A 1 4481 ? 176.156 164.873 204.650 1.00 16.67 ? 4481 ASP A O     1 
ATOM   22336 C  CB    . ASP A 1 4481 ? 175.912 166.887 207.281 1.00 12.67 ? 4481 ASP A CB    1 
ATOM   22337 C  CG    . ASP A 1 4481 ? 174.648 167.358 206.587 1.00 20.37 ? 4481 ASP A CG    1 
ATOM   22338 O  OD1   . ASP A 1 4481 ? 174.235 166.726 205.592 1.00 25.80 ? 4481 ASP A OD1   1 
ATOM   22339 O  OD2   . ASP A 1 4481 ? 174.064 168.363 207.041 1.00 28.85 ? 4481 ASP A OD2   1 
ATOM   22340 N  N     . PHE A 1 4482 ? 178.132 165.599 205.451 1.00 17.10 ? 4482 PHE A N     1 
ATOM   22341 C  CA    . PHE A 1 4482 ? 178.779 165.501 204.148 1.00 14.74 ? 4482 PHE A CA    1 
ATOM   22342 C  C     . PHE A 1 4482 ? 178.826 164.063 203.654 1.00 17.67 ? 4482 PHE A C     1 
ATOM   22343 O  O     . PHE A 1 4482 ? 178.720 163.819 202.446 1.00 22.37 ? 4482 PHE A O     1 
ATOM   22344 C  CB    . PHE A 1 4482 ? 180.187 166.092 204.216 1.00 16.38 ? 4482 PHE A CB    1 
ATOM   22345 C  CG    . PHE A 1 4482 ? 180.965 165.958 202.943 1.00 14.82 ? 4482 PHE A CG    1 
ATOM   22346 C  CD1   . PHE A 1 4482 ? 180.625 166.703 201.828 1.00 14.99 ? 4482 PHE A CD1   1 
ATOM   22347 C  CD2   . PHE A 1 4482 ? 182.040 165.090 202.861 1.00 17.62 ? 4482 PHE A CD2   1 
ATOM   22348 C  CE1   . PHE A 1 4482 ? 181.338 166.583 200.654 1.00 17.09 ? 4482 PHE A CE1   1 
ATOM   22349 C  CE2   . PHE A 1 4482 ? 182.758 164.967 201.690 1.00 16.59 ? 4482 PHE A CE2   1 
ATOM   22350 C  CZ    . PHE A 1 4482 ? 182.407 165.713 200.586 1.00 17.90 ? 4482 PHE A CZ    1 
ATOM   22351 N  N     . SER A 1 4483 ? 178.986 163.102 204.564 1.00 16.81 ? 4483 SER A N     1 
ATOM   22352 C  CA    . SER A 1 4483 ? 179.023 161.702 204.159 1.00 18.64 ? 4483 SER A CA    1 
ATOM   22353 C  C     . SER A 1 4483 ? 177.685 161.255 203.579 1.00 19.56 ? 4483 SER A C     1 
ATOM   22354 O  O     . SER A 1 4483 ? 177.649 160.523 202.582 1.00 22.30 ? 4483 SER A O     1 
ATOM   22355 C  CB    . SER A 1 4483 ? 179.418 160.826 205.346 1.00 18.63 ? 4483 SER A CB    1 
ATOM   22356 O  OG    . SER A 1 4483 ? 179.432 159.456 204.985 1.00 32.12 ? 4483 SER A OG    1 
ATOM   22357 N  N     . GLU A 1 4484 ? 176.576 161.684 204.186 1.00 14.53 ? 4484 GLU A N     1 
ATOM   22358 C  CA    . GLU A 1 4484 ? 175.260 161.311 203.674 1.00 15.63 ? 4484 GLU A CA    1 
ATOM   22359 C  C     . GLU A 1 4484 ? 175.011 161.906 202.293 1.00 18.79 ? 4484 GLU A C     1 
ATOM   22360 O  O     . GLU A 1 4484 ? 174.439 161.243 201.420 1.00 17.93 ? 4484 GLU A O     1 
ATOM   22361 C  CB    . GLU A 1 4484 ? 174.168 161.754 204.650 1.00 17.46 ? 4484 GLU A CB    1 
ATOM   22362 C  CG    . GLU A 1 4484 ? 174.257 161.187 206.074 1.00 20.75 ? 4484 GLU A CG    1 
ATOM   22363 C  CD    . GLU A 1 4484 ? 174.787 159.759 206.173 1.00 27.22 ? 4484 GLU A CD    1 
ATOM   22364 O  OE1   . GLU A 1 4484 ? 174.520 158.927 205.279 1.00 26.67 ? 4484 GLU A OE1   1 
ATOM   22365 O  OE2   . GLU A 1 4484 ? 175.483 159.468 207.169 1.00 31.05 ? 4484 GLU A OE2   1 
ATOM   22366 N  N     . ARG A 1 4485 ? 175.423 163.158 202.081 1.00 20.08 ? 4485 ARG A N     1 
ATOM   22367 C  CA    . ARG A 1 4485 ? 175.206 163.801 200.790 1.00 16.59 ? 4485 ARG A CA    1 
ATOM   22368 C  C     . ARG A 1 4485 ? 175.958 163.081 199.678 1.00 19.26 ? 4485 ARG A C     1 
ATOM   22369 O  O     . ARG A 1 4485 ? 175.451 162.952 198.557 1.00 24.02 ? 4485 ARG A O     1 
ATOM   22370 C  CB    . ARG A 1 4485 ? 175.623 165.269 200.858 1.00 15.48 ? 4485 ARG A CB    1 
ATOM   22371 C  CG    . ARG A 1 4485 ? 174.866 166.080 201.895 1.00 13.39 ? 4485 ARG A CG    1 
ATOM   22372 C  CD    . ARG A 1 4485 ? 175.315 167.530 201.906 1.00 16.30 ? 4485 ARG A CD    1 
ATOM   22373 N  NE    . ARG A 1 4485 ? 174.533 168.328 202.841 1.00 16.38 ? 4485 ARG A NE    1 
ATOM   22374 C  CZ    . ARG A 1 4485 ? 173.790 169.372 202.500 1.00 15.93 ? 4485 ARG A CZ    1 
ATOM   22375 N  NH1   . ARG A 1 4485 ? 173.715 169.785 201.246 1.00 14.82 ? 4485 ARG A NH1   1 
ATOM   22376 N  NH2   . ARG A 1 4485 ? 173.108 170.017 203.441 1.00 22.55 ? 4485 ARG A NH2   1 
ATOM   22377 N  N     . ILE A 1 4486 ? 177.174 162.613 199.964 1.00 18.01 ? 4486 ILE A N     1 
ATOM   22378 C  CA    . ILE A 1 4486 ? 177.962 161.928 198.944 1.00 20.14 ? 4486 ILE A CA    1 
ATOM   22379 C  C     . ILE A 1 4486 ? 177.321 160.597 198.572 1.00 21.52 ? 4486 ILE A C     1 
ATOM   22380 O  O     . ILE A 1 4486 ? 177.325 160.201 197.400 1.00 25.75 ? 4486 ILE A O     1 
ATOM   22381 C  CB    . ILE A 1 4486 ? 179.417 161.751 199.418 1.00 19.31 ? 4486 ILE A CB    1 
ATOM   22382 C  CG1   . ILE A 1 4486 ? 180.076 163.115 199.642 1.00 17.51 ? 4486 ILE A CG1   1 
ATOM   22383 C  CG2   . ILE A 1 4486 ? 180.221 160.961 198.405 1.00 20.25 ? 4486 ILE A CG2   1 
ATOM   22384 C  CD1   . ILE A 1 4486 ? 180.017 164.027 198.445 1.00 13.03 ? 4486 ILE A CD1   1 
ATOM   22385 N  N     . LYS A 1 4487 ? 176.756 159.886 199.554 1.00 18.78 ? 4487 LYS A N     1 
ATOM   22386 C  CA    . LYS A 1 4487 ? 176.093 158.617 199.260 1.00 18.59 ? 4487 LYS A CA    1 
ATOM   22387 C  C     . LYS A 1 4487 ? 174.940 158.815 198.283 1.00 21.96 ? 4487 LYS A C     1 
ATOM   22388 O  O     . LYS A 1 4487 ? 174.790 158.057 197.319 1.00 23.93 ? 4487 LYS A O     1 
ATOM   22389 C  CB    . LYS A 1 4487 ? 175.590 157.963 200.548 1.00 18.27 ? 4487 LYS A CB    1 
ATOM   22390 C  CG    . LYS A 1 4487 ? 176.676 157.585 201.541 1.00 22.74 ? 4487 LYS A CG    1 
ATOM   22391 C  CD    . LYS A 1 4487 ? 176.070 157.245 202.893 1.00 20.30 ? 4487 LYS A CD    1 
ATOM   22392 C  CE    . LYS A 1 4487 ? 177.140 157.050 203.956 1.00 26.80 ? 4487 LYS A CE    1 
ATOM   22393 N  NZ    . LYS A 1 4487 ? 178.045 155.911 203.634 1.00 29.76 ? 4487 LYS A NZ    1 
ATOM   22394 N  N     . GLN A 1 4488 ? 174.116 159.840 198.515 1.00 19.81 ? 4488 GLN A N     1 
ATOM   22395 C  CA    . GLN A 1 4488 ? 173.045 160.149 197.576 1.00 17.14 ? 4488 GLN A CA    1 
ATOM   22396 C  C     . GLN A 1 4488 ? 173.603 160.532 196.213 1.00 21.34 ? 4488 GLN A C     1 
ATOM   22397 O  O     . GLN A 1 4488 ? 173.050 160.144 195.176 1.00 20.67 ? 4488 GLN A O     1 
ATOM   22398 C  CB    . GLN A 1 4488 ? 172.168 161.272 198.125 1.00 17.58 ? 4488 GLN A CB    1 
ATOM   22399 C  CG    . GLN A 1 4488 ? 171.125 161.745 197.129 1.00 19.14 ? 4488 GLN A CG    1 
ATOM   22400 C  CD    . GLN A 1 4488 ? 170.000 162.512 197.771 1.00 15.75 ? 4488 GLN A CD    1 
ATOM   22401 O  OE1   . GLN A 1 4488 ? 168.827 162.297 197.469 1.00 22.26 ? 4488 GLN A OE1   1 
ATOM   22402 N  NE2   . GLN A 1 4488 ? 170.351 163.411 198.677 1.00 14.10 ? 4488 GLN A NE2   1 
ATOM   22403 N  N     . LEU A 1 4489 ? 174.697 161.294 196.196 1.00 23.47 ? 4489 LEU A N     1 
ATOM   22404 C  CA    . LEU A 1 4489 ? 175.322 161.663 194.931 1.00 16.33 ? 4489 LEU A CA    1 
ATOM   22405 C  C     . LEU A 1 4489 ? 175.811 160.430 194.184 1.00 24.10 ? 4489 LEU A C     1 
ATOM   22406 O  O     . LEU A 1 4489 ? 175.709 160.359 192.953 1.00 28.31 ? 4489 LEU A O     1 
ATOM   22407 C  CB    . LEU A 1 4489 ? 176.471 162.636 195.186 1.00 16.34 ? 4489 LEU A CB    1 
ATOM   22408 C  CG    . LEU A 1 4489 ? 176.068 164.074 195.509 1.00 17.95 ? 4489 LEU A CG    1 
ATOM   22409 C  CD1   . LEU A 1 4489 ? 177.211 164.810 196.190 1.00 17.82 ? 4489 LEU A CD1   1 
ATOM   22410 C  CD2   . LEU A 1 4489 ? 175.624 164.812 194.256 1.00 17.65 ? 4489 LEU A CD2   1 
ATOM   22411 N  N     . GLN A 1 4490 ? 176.351 159.448 194.911 1.00 19.85 ? 4490 GLN A N     1 
ATOM   22412 C  CA    . GLN A 1 4490 ? 176.792 158.210 194.275 1.00 22.86 ? 4490 GLN A CA    1 
ATOM   22413 C  C     . GLN A 1 4490 ? 175.625 157.461 193.648 1.00 24.08 ? 4490 GLN A C     1 
ATOM   22414 O  O     . GLN A 1 4490 ? 175.733 156.958 192.524 1.00 25.45 ? 4490 GLN A O     1 
ATOM   22415 C  CB    . GLN A 1 4490 ? 177.503 157.320 195.293 1.00 24.69 ? 4490 GLN A CB    1 
ATOM   22416 C  CG    . GLN A 1 4490 ? 178.903 157.766 195.645 1.00 22.44 ? 4490 GLN A CG    1 
ATOM   22417 C  CD    . GLN A 1 4490 ? 179.499 156.942 196.762 1.00 27.24 ? 4490 GLN A CD    1 
ATOM   22418 O  OE1   . GLN A 1 4490 ? 178.818 156.120 197.373 1.00 25.67 ? 4490 GLN A OE1   1 
ATOM   22419 N  NE2   . GLN A 1 4490 ? 180.783 157.146 197.026 1.00 32.38 ? 4490 GLN A NE2   1 
ATOM   22420 N  N     . ASN A 1 4491 ? 174.499 157.372 194.362 1.00 20.90 ? 4491 ASN A N     1 
ATOM   22421 C  CA    . ASN A 1 4491 ? 173.350 156.641 193.838 1.00 20.71 ? 4491 ASN A CA    1 
ATOM   22422 C  C     . ASN A 1 4491 ? 172.796 157.307 192.587 1.00 18.92 ? 4491 ASN A C     1 
ATOM   22423 O  O     . ASN A 1 4491 ? 172.396 156.623 191.637 1.00 21.82 ? 4491 ASN A O     1 
ATOM   22424 C  CB    . ASN A 1 4491 ? 172.269 156.523 194.910 1.00 17.89 ? 4491 ASN A CB    1 
ATOM   22425 C  CG    . ASN A 1 4491 ? 172.792 155.927 196.201 1.00 21.50 ? 4491 ASN A CG    1 
ATOM   22426 O  OD1   . ASN A 1 4491 ? 173.954 155.533 196.291 1.00 21.49 ? 4491 ASN A OD1   1 
ATOM   22427 N  ND2   . ASN A 1 4491 ? 171.937 155.863 197.213 1.00 25.61 ? 4491 ASN A ND2   1 
ATOM   22428 N  N     . ILE A 1 4492 ? 172.762 158.640 192.571 1.00 23.97 ? 4492 ILE A N     1 
ATOM   22429 C  CA    . ILE A 1 4492 ? 172.272 159.365 191.401 1.00 19.27 ? 4492 ILE A CA    1 
ATOM   22430 C  C     . ILE A 1 4492 ? 173.157 159.085 190.193 1.00 24.09 ? 4492 ILE A C     1 
ATOM   22431 O  O     . ILE A 1 4492 ? 172.662 158.832 189.087 1.00 26.62 ? 4492 ILE A O     1 
ATOM   22432 C  CB    . ILE A 1 4492 ? 172.189 160.870 191.712 1.00 19.87 ? 4492 ILE A CB    1 
ATOM   22433 C  CG1   . ILE A 1 4492 ? 171.134 161.131 192.789 1.00 18.69 ? 4492 ILE A CG1   1 
ATOM   22434 C  CG2   . ILE A 1 4492 ? 171.865 161.659 190.459 1.00 19.08 ? 4492 ILE A CG2   1 
ATOM   22435 C  CD1   . ILE A 1 4492 ? 171.148 162.543 193.323 1.00 17.61 ? 4492 ILE A CD1   1 
ATOM   22436 N  N     . SER A 1 4493 ? 174.477 159.121 190.384 1.00 26.95 ? 4493 SER A N     1 
ATOM   22437 C  CA    . SER A 1 4493 ? 175.393 158.842 189.283 1.00 22.98 ? 4493 SER A CA    1 
ATOM   22438 C  C     . SER A 1 4493 ? 175.339 157.375 188.873 1.00 27.04 ? 4493 SER A C     1 
ATOM   22439 O  O     . SER A 1 4493 ? 175.499 157.049 187.691 1.00 29.96 ? 4493 SER A O     1 
ATOM   22440 C  CB    . SER A 1 4493 ? 176.816 159.242 189.668 1.00 26.29 ? 4493 SER A CB    1 
ATOM   22441 O  OG    . SER A 1 4493 ? 177.722 158.980 188.611 1.00 30.58 ? 4493 SER A OG    1 
ATOM   22442 N  N     . LEU A 1 4494 ? 175.129 156.475 189.837 1.00 25.87 ? 4494 LEU A N     1 
ATOM   22443 C  CA    . LEU A 1 4494 ? 175.022 155.055 189.512 1.00 23.39 ? 4494 LEU A CA    1 
ATOM   22444 C  C     . LEU A 1 4494 ? 173.817 154.784 188.620 1.00 29.62 ? 4494 LEU A C     1 
ATOM   22445 O  O     . LEU A 1 4494 ? 173.903 154.000 187.667 1.00 32.37 ? 4494 LEU A O     1 
ATOM   22446 C  CB    . LEU A 1 4494 ? 174.941 154.228 190.795 1.00 26.40 ? 4494 LEU A CB    1 
ATOM   22447 C  CG    . LEU A 1 4494 ? 174.734 152.721 190.642 1.00 24.92 ? 4494 LEU A CG    1 
ATOM   22448 C  CD1   . LEU A 1 4494 ? 175.773 152.122 189.702 1.00 28.38 ? 4494 LEU A CD1   1 
ATOM   22449 C  CD2   . LEU A 1 4494 ? 174.779 152.036 191.997 1.00 17.84 ? 4494 LEU A CD2   1 
ATOM   22450 N  N     . ALA A 1 4495 ? 172.681 155.418 188.918 1.00 26.59 ? 4495 ALA A N     1 
ATOM   22451 C  CA    . ALA A 1 4495 ? 171.506 155.262 188.071 1.00 25.76 ? 4495 ALA A CA    1 
ATOM   22452 C  C     . ALA A 1 4495 ? 171.758 155.805 186.670 1.00 28.11 ? 4495 ALA A C     1 
ATOM   22453 O  O     . ALA A 1 4495 ? 171.386 155.174 185.674 1.00 33.36 ? 4495 ALA A O     1 
ATOM   22454 C  CB    . ALA A 1 4495 ? 170.303 155.957 188.708 1.00 24.79 ? 4495 ALA A CB    1 
ATOM   22455 N  N     . ALA A 1 4496 ? 172.391 156.977 186.574 1.00 29.32 ? 4496 ALA A N     1 
ATOM   22456 C  CA    . ALA A 1 4496 ? 172.700 157.546 185.266 1.00 26.09 ? 4496 ALA A CA    1 
ATOM   22457 C  C     . ALA A 1 4496 ? 173.704 156.684 184.511 1.00 28.62 ? 4496 ALA A C     1 
ATOM   22458 O  O     . ALA A 1 4496 ? 173.575 156.490 183.297 1.00 28.96 ? 4496 ALA A O     1 
ATOM   22459 C  CB    . ALA A 1 4496 ? 173.225 158.972 185.423 1.00 24.03 ? 4496 ALA A CB    1 
ATOM   22460 N  N     . ALA A 1 4497 ? 174.716 156.166 185.209 1.00 27.58 ? 4497 ALA A N     1 
ATOM   22461 C  CA    . ALA A 1 4497 ? 175.694 155.298 184.561 1.00 28.87 ? 4497 ALA A CA    1 
ATOM   22462 C  C     . ALA A 1 4497 ? 175.067 153.970 184.152 1.00 28.97 ? 4497 ALA A C     1 
ATOM   22463 O  O     . ALA A 1 4497 ? 175.291 153.483 183.038 1.00 29.55 ? 4497 ALA A O     1 
ATOM   22464 C  CB    . ALA A 1 4497 ? 176.890 155.069 185.485 1.00 26.95 ? 4497 ALA A CB    1 
ATOM   22465 N  N     . SER A 1 4498 ? 174.278 153.371 185.040 1.00 27.46 ? 4498 SER A N     1 
ATOM   22466 C  CA    . SER A 1 4498 ? 173.628 152.088 184.790 1.00 28.61 ? 4498 SER A CA    1 
ATOM   22467 C  C     . SER A 1 4498 ? 172.125 152.326 184.679 1.00 29.30 ? 4498 SER A C     1 
ATOM   22468 O  O     . SER A 1 4498 ? 171.413 152.339 185.687 1.00 31.91 ? 4498 SER A O     1 
ATOM   22469 C  CB    . SER A 1 4498 ? 173.953 151.087 185.895 1.00 29.51 ? 4498 SER A CB    1 
ATOM   22470 O  OG    . SER A 1 4498 ? 175.353 150.911 186.027 1.00 37.99 ? 4498 SER A OG    1 
ATOM   22471 N  N     . GLY A 1 4499 ? 171.645 152.507 183.447 1.00 31.00 ? 4499 GLY A N     1 
ATOM   22472 C  CA    . GLY A 1 4499 ? 170.240 152.751 183.167 1.00 30.52 ? 4499 GLY A CA    1 
ATOM   22473 C  C     . GLY A 1 4499 ? 169.993 154.012 182.363 1.00 30.64 ? 4499 GLY A C     1 
ATOM   22474 O  O     . GLY A 1 4499 ? 169.008 154.083 181.619 1.00 35.96 ? 4499 GLY A O     1 
ATOM   22475 N  N     . GLY A 1 4500 ? 170.865 155.005 182.496 1.00 28.47 ? 4500 GLY A N     1 
ATOM   22476 C  CA    . GLY A 1 4500 ? 170.754 156.237 181.738 1.00 28.16 ? 4500 GLY A CA    1 
ATOM   22477 C  C     . GLY A 1 4500 ? 170.136 157.360 182.549 1.00 34.09 ? 4500 GLY A C     1 
ATOM   22478 O  O     . GLY A 1 4500 ? 169.730 157.200 183.705 1.00 34.61 ? 4500 GLY A O     1 
ATOM   22479 N  N     . ALA A 1 4501 ? 170.066 158.527 181.907 1.00 24.32 ? 4501 ALA A N     1 
ATOM   22480 C  CA    . ALA A 1 4501 ? 169.511 159.709 182.555 1.00 31.33 ? 4501 ALA A CA    1 
ATOM   22481 C  C     . ALA A 1 4501 ? 168.017 159.580 182.825 1.00 33.75 ? 4501 ALA A C     1 
ATOM   22482 O  O     . ALA A 1 4501 ? 167.474 160.361 183.612 1.00 33.80 ? 4501 ALA A O     1 
ATOM   22483 C  CB    . ALA A 1 4501 ? 169.780 160.953 181.707 1.00 28.41 ? 4501 ALA A CB    1 
ATOM   22484 N  N     . LYS A 1 4502 ? 167.340 158.621 182.188 1.00 30.22 ? 4502 LYS A N     1 
ATOM   22485 C  CA    . LYS A 1 4502 ? 165.923 158.409 182.452 1.00 27.42 ? 4502 LYS A CA    1 
ATOM   22486 C  C     . LYS A 1 4502 ? 165.670 157.883 183.858 1.00 31.94 ? 4502 LYS A C     1 
ATOM   22487 O  O     . LYS A 1 4502 ? 164.557 158.040 184.373 1.00 29.20 ? 4502 LYS A O     1 
ATOM   22488 C  CB    . LYS A 1 4502 ? 165.333 157.446 181.421 1.00 28.05 ? 4502 LYS A CB    1 
ATOM   22489 C  CG    . LYS A 1 4502 ? 165.944 156.056 181.448 1.00 28.69 ? 4502 LYS A CG    1 
ATOM   22490 C  CD    . LYS A 1 4502 ? 165.138 155.080 180.606 1.00 29.22 ? 4502 LYS A CD    1 
ATOM   22491 C  CE    . LYS A 1 4502 ? 165.679 153.666 180.730 1.00 29.77 ? 4502 LYS A CE    1 
ATOM   22492 N  NZ    . LYS A 1 4502 ? 164.876 152.693 179.939 1.00 26.26 ? 4502 LYS A NZ    1 
ATOM   22493 N  N     . GLU A 1 4503 ? 166.667 157.260 184.487 1.00 29.62 ? 4503 GLU A N     1 
ATOM   22494 C  CA    . GLU A 1 4503 ? 166.520 156.790 185.858 1.00 25.75 ? 4503 GLU A CA    1 
ATOM   22495 C  C     . GLU A 1 4503 ? 166.580 157.919 186.878 1.00 24.70 ? 4503 GLU A C     1 
ATOM   22496 O  O     . GLU A 1 4503 ? 166.288 157.682 188.054 1.00 28.42 ? 4503 GLU A O     1 
ATOM   22497 C  CB    . GLU A 1 4503 ? 167.596 155.748 186.175 1.00 25.84 ? 4503 GLU A CB    1 
ATOM   22498 C  CG    . GLU A 1 4503 ? 167.804 154.714 185.078 1.00 31.54 ? 4503 GLU A CG    1 
ATOM   22499 C  CD    . GLU A 1 4503 ? 166.697 153.678 185.025 1.00 35.91 ? 4503 GLU A CD    1 
ATOM   22500 O  OE1   . GLU A 1 4503 ? 165.836 153.673 185.931 1.00 32.05 ? 4503 GLU A OE1   1 
ATOM   22501 O  OE2   . GLU A 1 4503 ? 166.689 152.865 184.075 1.00 35.02 ? 4503 GLU A OE2   1 
ATOM   22502 N  N     . LEU A 1 4504 ? 166.959 159.129 186.460 1.00 18.52 ? 4504 LEU A N     1 
ATOM   22503 C  CA    . LEU A 1 4504 ? 166.966 160.270 187.369 1.00 24.14 ? 4504 LEU A CA    1 
ATOM   22504 C  C     . LEU A 1 4504 ? 165.568 160.630 187.848 1.00 25.12 ? 4504 LEU A C     1 
ATOM   22505 O  O     . LEU A 1 4504 ? 165.422 161.183 188.943 1.00 26.16 ? 4504 LEU A O     1 
ATOM   22506 C  CB    . LEU A 1 4504 ? 167.603 161.481 186.685 1.00 26.62 ? 4504 LEU A CB    1 
ATOM   22507 C  CG    . LEU A 1 4504 ? 169.066 161.350 186.254 1.00 26.78 ? 4504 LEU A CG    1 
ATOM   22508 C  CD1   . LEU A 1 4504 ? 169.537 162.629 185.579 1.00 26.85 ? 4504 LEU A CD1   1 
ATOM   22509 C  CD2   . LEU A 1 4504 ? 169.948 161.007 187.439 1.00 18.13 ? 4504 LEU A CD2   1 
ATOM   22510 N  N     . LYS A 1 4505 ? 164.541 160.331 187.051 1.00 26.12 ? 4505 LYS A N     1 
ATOM   22511 C  CA    . LYS A 1 4505 ? 163.173 160.689 187.408 1.00 23.24 ? 4505 LYS A CA    1 
ATOM   22512 C  C     . LYS A 1 4505 ? 162.589 159.759 188.465 1.00 23.64 ? 4505 LYS A C     1 
ATOM   22513 O  O     . LYS A 1 4505 ? 161.782 160.198 189.290 1.00 31.32 ? 4505 LYS A O     1 
ATOM   22514 C  CB    . LYS A 1 4505 ? 162.300 160.688 186.149 1.00 17.77 ? 4505 LYS A CB    1 
ATOM   22515 C  CG    . LYS A 1 4505 ? 160.846 161.074 186.362 1.00 19.89 ? 4505 LYS A CG    1 
ATOM   22516 C  CD    . LYS A 1 4505 ? 159.949 159.855 186.468 1.00 21.33 ? 4505 LYS A CD    1 
ATOM   22517 C  CE    . LYS A 1 4505 ? 158.681 160.173 187.229 1.00 23.09 ? 4505 LYS A CE    1 
ATOM   22518 N  NZ    . LYS A 1 4505 ? 157.892 158.945 187.517 1.00 29.22 ? 4505 LYS A NZ    1 
ATOM   22519 N  N     . ASN A 1 4506 ? 162.976 158.488 188.460 1.00 21.08 ? 4506 ASN A N     1 
ATOM   22520 C  CA    . ASN A 1 4506 ? 162.342 157.483 189.302 1.00 25.98 ? 4506 ASN A CA    1 
ATOM   22521 C  C     . ASN A 1 4506 ? 162.992 157.385 190.681 1.00 22.50 ? 4506 ASN A C     1 
ATOM   22522 O  O     . ASN A 1 4506 ? 162.421 156.762 191.581 1.00 20.54 ? 4506 ASN A O     1 
ATOM   22523 C  CB    . ASN A 1 4506 ? 162.388 156.124 188.583 1.00 21.35 ? 4506 ASN A CB    1 
ATOM   22524 C  CG    . ASN A 1 4506 ? 161.491 155.073 189.221 1.00 29.07 ? 4506 ASN A CG    1 
ATOM   22525 O  OD1   . ASN A 1 4506 ? 160.808 155.325 190.212 1.00 35.45 ? 4506 ASN A OD1   1 
ATOM   22526 N  ND2   . ASN A 1 4506 ? 161.494 153.878 188.643 1.00 30.04 ? 4506 ASN A ND2   1 
ATOM   22527 N  N     . ILE A 1 4507 ? 164.150 158.003 190.880 1.00 22.25 ? 4507 ILE A N     1 
ATOM   22528 C  CA    . ILE A 1 4507 ? 164.873 157.903 192.142 1.00 20.56 ? 4507 ILE A CA    1 
ATOM   22529 C  C     . ILE A 1 4507 ? 164.316 158.916 193.135 1.00 23.65 ? 4507 ILE A C     1 
ATOM   22530 O  O     . ILE A 1 4507 ? 164.047 160.071 192.782 1.00 21.94 ? 4507 ILE A O     1 
ATOM   22531 C  CB    . ILE A 1 4507 ? 166.387 158.091 191.931 1.00 17.66 ? 4507 ILE A CB    1 
ATOM   22532 C  CG1   . ILE A 1 4507 ? 167.157 157.680 193.189 1.00 19.98 ? 4507 ILE A CG1   1 
ATOM   22533 C  CG2   . ILE A 1 4507 ? 166.729 159.517 191.517 1.00 12.50 ? 4507 ILE A CG2   1 
ATOM   22534 C  CD1   . ILE A 1 4507 ? 167.061 156.208 193.510 1.00 19.38 ? 4507 ILE A CD1   1 
ATOM   22535 N  N     . HIS A 1 4508 ? 164.110 158.471 194.372 1.00 21.06 ? 4508 HIS A N     1 
ATOM   22536 C  CA    . HIS A 1 4508 ? 163.683 159.373 195.432 1.00 18.41 ? 4508 HIS A CA    1 
ATOM   22537 C  C     . HIS A 1 4508 ? 164.855 160.227 195.898 1.00 22.74 ? 4508 HIS A C     1 
ATOM   22538 O  O     . HIS A 1 4508 ? 165.996 159.762 195.965 1.00 24.23 ? 4508 HIS A O     1 
ATOM   22539 C  CB    . HIS A 1 4508 ? 163.103 158.584 196.604 1.00 18.13 ? 4508 HIS A CB    1 
ATOM   22540 C  CG    . HIS A 1 4508 ? 161.917 157.749 196.240 1.00 16.76 ? 4508 HIS A CG    1 
ATOM   22541 N  ND1   . HIS A 1 4508 ? 161.497 156.680 197.002 1.00 20.07 ? 4508 HIS A ND1   1 
ATOM   22542 C  CD2   . HIS A 1 4508 ? 161.063 157.823 195.193 1.00 16.55 ? 4508 HIS A CD2   1 
ATOM   22543 C  CE1   . HIS A 1 4508 ? 160.432 156.134 196.442 1.00 21.30 ? 4508 HIS A CE1   1 
ATOM   22544 N  NE2   . HIS A 1 4508 ? 160.148 156.809 195.343 1.00 23.53 ? 4508 HIS A NE2   1 
ATOM   22545 N  N     . VAL A 1 4509 ? 164.567 161.483 196.228 1.00 19.46 ? 4509 VAL A N     1 
ATOM   22546 C  CA    . VAL A 1 4509 ? 165.594 162.479 196.499 1.00 17.72 ? 4509 VAL A CA    1 
ATOM   22547 C  C     . VAL A 1 4509 ? 165.375 163.056 197.890 1.00 19.72 ? 4509 VAL A C     1 
ATOM   22548 O  O     . VAL A 1 4509 ? 164.255 163.441 198.241 1.00 24.29 ? 4509 VAL A O     1 
ATOM   22549 C  CB    . VAL A 1 4509 ? 165.586 163.596 195.438 1.00 19.99 ? 4509 VAL A CB    1 
ATOM   22550 C  CG1   . VAL A 1 4509 ? 166.249 164.846 195.974 1.00 14.26 ? 4509 VAL A CG1   1 
ATOM   22551 C  CG2   . VAL A 1 4509 ? 166.274 163.124 194.166 1.00 23.83 ? 4509 VAL A CG2   1 
ATOM   22552 N  N     . CYS A 1 4510 ? 166.444 163.107 198.681 1.00 15.83 ? 4510 CYS A N     1 
ATOM   22553 C  CA    . CYS A 1 4510 ? 166.461 163.848 199.936 1.00 13.31 ? 4510 CYS A CA    1 
ATOM   22554 C  C     . CYS A 1 4510 ? 166.851 165.288 199.625 1.00 14.34 ? 4510 CYS A C     1 
ATOM   22555 O  O     . CYS A 1 4510 ? 168.011 165.570 199.308 1.00 15.71 ? 4510 CYS A O     1 
ATOM   22556 C  CB    . CYS A 1 4510 ? 167.430 163.212 200.928 1.00 14.28 ? 4510 CYS A CB    1 
ATOM   22557 S  SG    . CYS A 1 4510 ? 167.485 164.012 202.544 1.00 34.97 ? 4510 CYS A SG    1 
ATOM   22558 N  N     . LEU A 1 4511 ? 165.878 166.200 199.709 1.00 16.60 ? 4511 LEU A N     1 
ATOM   22559 C  CA    . LEU A 1 4511 ? 166.134 167.592 199.351 1.00 12.03 ? 4511 LEU A CA    1 
ATOM   22560 C  C     . LEU A 1 4511 ? 167.181 168.227 200.254 1.00 11.26 ? 4511 LEU A C     1 
ATOM   22561 O  O     . LEU A 1 4511 ? 167.918 169.117 199.816 1.00 15.16 ? 4511 LEU A O     1 
ATOM   22562 C  CB    . LEU A 1 4511 ? 164.837 168.396 199.401 1.00 12.13 ? 4511 LEU A CB    1 
ATOM   22563 C  CG    . LEU A 1 4511 ? 164.061 168.484 198.090 1.00 10.91 ? 4511 LEU A CG    1 
ATOM   22564 C  CD1   . LEU A 1 4511 ? 162.792 169.290 198.282 1.00 9.65  ? 4511 LEU A CD1   1 
ATOM   22565 C  CD2   . LEU A 1 4511 ? 164.927 169.085 196.996 1.00 16.64 ? 4511 LEU A CD2   1 
ATOM   22566 N  N     . GLY A 1 4512 ? 167.258 167.795 201.513 1.00 14.87 ? 4512 GLY A N     1 
ATOM   22567 C  CA    . GLY A 1 4512 ? 168.282 168.322 202.398 1.00 12.25 ? 4512 GLY A CA    1 
ATOM   22568 C  C     . GLY A 1 4512 ? 169.684 167.995 201.925 1.00 12.60 ? 4512 GLY A C     1 
ATOM   22569 O  O     . GLY A 1 4512 ? 170.591 168.825 202.016 1.00 17.05 ? 4512 GLY A O     1 
ATOM   22570 N  N     . GLY A 1 4513 ? 169.879 166.779 201.407 1.00 14.70 ? 4513 GLY A N     1 
ATOM   22571 C  CA    . GLY A 1 4513 ? 171.194 166.376 200.942 1.00 12.14 ? 4513 GLY A CA    1 
ATOM   22572 C  C     . GLY A 1 4513 ? 171.679 167.151 199.734 1.00 15.77 ? 4513 GLY A C     1 
ATOM   22573 O  O     . GLY A 1 4513 ? 172.883 167.378 199.584 1.00 18.53 ? 4513 GLY A O     1 
ATOM   22574 N  N     . LEU A 1 4514 ? 170.764 167.559 198.856 1.00 14.07 ? 4514 LEU A N     1 
ATOM   22575 C  CA    . LEU A 1 4514 ? 171.157 168.261 197.643 1.00 15.98 ? 4514 LEU A CA    1 
ATOM   22576 C  C     . LEU A 1 4514 ? 171.820 169.592 197.973 1.00 15.95 ? 4514 LEU A C     1 
ATOM   22577 O  O     . LEU A 1 4514 ? 171.436 170.282 198.920 1.00 18.27 ? 4514 LEU A O     1 
ATOM   22578 C  CB    . LEU A 1 4514 ? 169.948 168.495 196.740 1.00 17.77 ? 4514 LEU A CB    1 
ATOM   22579 C  CG    . LEU A 1 4514 ? 169.286 167.259 196.137 1.00 19.48 ? 4514 LEU A CG    1 
ATOM   22580 C  CD1   . LEU A 1 4514 ? 168.181 167.687 195.198 1.00 15.55 ? 4514 LEU A CD1   1 
ATOM   22581 C  CD2   . LEU A 1 4514 ? 170.310 166.398 195.418 1.00 17.66 ? 4514 LEU A CD2   1 
ATOM   22582 N  N     . PHE A 1 4515 ? 172.827 169.947 197.174 1.00 16.05 ? 4515 PHE A N     1 
ATOM   22583 C  CA    . PHE A 1 4515 ? 173.562 171.182 197.419 1.00 17.99 ? 4515 PHE A CA    1 
ATOM   22584 C  C     . PHE A 1 4515 ? 172.723 172.403 197.060 1.00 19.67 ? 4515 PHE A C     1 
ATOM   22585 O  O     . PHE A 1 4515 ? 172.811 173.441 197.726 1.00 20.22 ? 4515 PHE A O     1 
ATOM   22586 C  CB    . PHE A 1 4515 ? 174.869 171.170 196.627 1.00 20.05 ? 4515 PHE A CB    1 
ATOM   22587 C  CG    . PHE A 1 4515 ? 175.867 170.168 197.130 1.00 20.66 ? 4515 PHE A CG    1 
ATOM   22588 C  CD1   . PHE A 1 4515 ? 175.856 169.764 198.455 1.00 20.29 ? 4515 PHE A CD1   1 
ATOM   22589 C  CD2   . PHE A 1 4515 ? 176.810 169.624 196.278 1.00 20.57 ? 4515 PHE A CD2   1 
ATOM   22590 C  CE1   . PHE A 1 4515 ? 176.767 168.836 198.917 1.00 19.58 ? 4515 PHE A CE1   1 
ATOM   22591 C  CE2   . PHE A 1 4515 ? 177.725 168.700 196.738 1.00 22.44 ? 4515 PHE A CE2   1 
ATOM   22592 C  CZ    . PHE A 1 4515 ? 177.706 168.306 198.060 1.00 21.87 ? 4515 PHE A CZ    1 
ATOM   22593 N  N     . VAL A 1 4516 ? 171.912 172.300 196.012 1.00 20.18 ? 4516 VAL A N     1 
ATOM   22594 C  CA    . VAL A 1 4516 ? 170.997 173.369 195.611 1.00 19.24 ? 4516 VAL A CA    1 
ATOM   22595 C  C     . VAL A 1 4516 ? 169.594 172.784 195.494 1.00 19.24 ? 4516 VAL A C     1 
ATOM   22596 O  O     . VAL A 1 4516 ? 169.153 172.452 194.386 1.00 20.14 ? 4516 VAL A O     1 
ATOM   22597 C  CB    . VAL A 1 4516 ? 171.434 174.027 194.292 1.00 20.41 ? 4516 VAL A CB    1 
ATOM   22598 C  CG1   . VAL A 1 4516 ? 170.671 175.321 194.073 1.00 22.88 ? 4516 VAL A CG1   1 
ATOM   22599 C  CG2   . VAL A 1 4516 ? 172.933 174.286 194.285 1.00 19.55 ? 4516 VAL A CG2   1 
ATOM   22600 N  N     . PRO A 1 4517 ? 168.870 172.626 196.604 1.00 19.78 ? 4517 PRO A N     1 
ATOM   22601 C  CA    . PRO A 1 4517 ? 167.520 172.041 196.521 1.00 17.84 ? 4517 PRO A CA    1 
ATOM   22602 C  C     . PRO A 1 4517 ? 166.540 172.862 195.699 1.00 18.55 ? 4517 PRO A C     1 
ATOM   22603 O  O     . PRO A 1 4517 ? 165.608 172.291 195.119 1.00 18.05 ? 4517 PRO A O     1 
ATOM   22604 C  CB    . PRO A 1 4517 ? 167.091 171.950 197.991 1.00 11.67 ? 4517 PRO A CB    1 
ATOM   22605 C  CG    . PRO A 1 4517 ? 167.935 172.953 198.697 1.00 16.12 ? 4517 PRO A CG    1 
ATOM   22606 C  CD    . PRO A 1 4517 ? 169.247 172.959 197.987 1.00 13.77 ? 4517 PRO A CD    1 
ATOM   22607 N  N     . GLU A 1 4518 ? 166.711 174.186 195.633 1.00 15.65 ? 4518 GLU A N     1 
ATOM   22608 C  CA    . GLU A 1 4518 ? 165.796 175.007 194.846 1.00 17.71 ? 4518 GLU A CA    1 
ATOM   22609 C  C     . GLU A 1 4518 ? 165.885 174.667 193.364 1.00 20.39 ? 4518 GLU A C     1 
ATOM   22610 O  O     . GLU A 1 4518 ? 164.869 174.640 192.661 1.00 20.18 ? 4518 GLU A O     1 
ATOM   22611 C  CB    . GLU A 1 4518 ? 166.087 176.491 195.069 1.00 19.06 ? 4518 GLU A CB    1 
ATOM   22612 C  CG    . GLU A 1 4518 ? 166.324 176.870 196.516 1.00 20.36 ? 4518 GLU A CG    1 
ATOM   22613 C  CD    . GLU A 1 4518 ? 167.798 176.952 196.858 1.00 24.95 ? 4518 GLU A CD    1 
ATOM   22614 O  OE1   . GLU A 1 4518 ? 168.527 175.977 196.581 1.00 26.35 ? 4518 GLU A OE1   1 
ATOM   22615 O  OE2   . GLU A 1 4518 ? 168.226 177.991 197.402 1.00 35.12 ? 4518 GLU A OE2   1 
ATOM   22616 N  N     . ALA A 1 4519 ? 167.100 174.409 192.871 1.00 21.26 ? 4519 ALA A N     1 
ATOM   22617 C  CA    . ALA A 1 4519 ? 167.280 174.085 191.461 1.00 16.64 ? 4519 ALA A CA    1 
ATOM   22618 C  C     . ALA A 1 4519 ? 166.604 172.771 191.091 1.00 15.73 ? 4519 ALA A C     1 
ATOM   22619 O  O     . ALA A 1 4519 ? 166.118 172.625 189.965 1.00 22.29 ? 4519 ALA A O     1 
ATOM   22620 C  CB    . ALA A 1 4519 ? 168.768 174.034 191.125 1.00 15.91 ? 4519 ALA A CB    1 
ATOM   22621 N  N     . TYR A 1 4520 ? 166.567 171.806 192.015 1.00 17.13 ? 4520 TYR A N     1 
ATOM   22622 C  CA    . TYR A 1 4520 ? 165.865 170.555 191.749 1.00 11.99 ? 4520 TYR A CA    1 
ATOM   22623 C  C     . TYR A 1 4520 ? 164.374 170.794 191.551 1.00 15.67 ? 4520 TYR A C     1 
ATOM   22624 O  O     . TYR A 1 4520 ? 163.747 170.171 190.687 1.00 20.06 ? 4520 TYR A O     1 
ATOM   22625 C  CB    . TYR A 1 4520 ? 166.103 169.567 192.890 1.00 13.23 ? 4520 TYR A CB    1 
ATOM   22626 C  CG    . TYR A 1 4520 ? 165.331 168.272 192.767 1.00 14.26 ? 4520 TYR A CG    1 
ATOM   22627 C  CD1   . TYR A 1 4520 ? 165.772 167.253 191.934 1.00 14.45 ? 4520 TYR A CD1   1 
ATOM   22628 C  CD2   . TYR A 1 4520 ? 164.168 168.063 193.498 1.00 14.07 ? 4520 TYR A CD2   1 
ATOM   22629 C  CE1   . TYR A 1 4520 ? 165.074 166.070 191.823 1.00 13.81 ? 4520 TYR A CE1   1 
ATOM   22630 C  CE2   . TYR A 1 4520 ? 163.465 166.882 193.393 1.00 14.74 ? 4520 TYR A CE2   1 
ATOM   22631 C  CZ    . TYR A 1 4520 ? 163.921 165.888 192.554 1.00 15.99 ? 4520 TYR A CZ    1 
ATOM   22632 O  OH    . TYR A 1 4520 ? 163.223 164.709 192.446 1.00 19.76 ? 4520 TYR A OH    1 
ATOM   22633 N  N     . ILE A 1 4521 ? 163.789 171.694 192.344 1.00 15.43 ? 4521 ILE A N     1 
ATOM   22634 C  CA    . ILE A 1 4521 ? 162.373 172.011 192.198 1.00 12.39 ? 4521 ILE A CA    1 
ATOM   22635 C  C     . ILE A 1 4521 ? 162.108 172.611 190.824 1.00 16.65 ? 4521 ILE A C     1 
ATOM   22636 O  O     . ILE A 1 4521 ? 161.129 172.261 190.153 1.00 20.54 ? 4521 ILE A O     1 
ATOM   22637 C  CB    . ILE A 1 4521 ? 161.919 172.954 193.329 1.00 16.10 ? 4521 ILE A CB    1 
ATOM   22638 C  CG1   . ILE A 1 4521 ? 162.044 172.255 194.683 1.00 16.17 ? 4521 ILE A CG1   1 
ATOM   22639 C  CG2   . ILE A 1 4521 ? 160.484 173.410 193.110 1.00 11.76 ? 4521 ILE A CG2   1 
ATOM   22640 C  CD1   . ILE A 1 4521 ? 161.270 170.972 194.780 1.00 13.69 ? 4521 ILE A CD1   1 
ATOM   22641 N  N     . THR A 1 4522 ? 162.979 173.523 190.383 1.00 18.05 ? 4522 THR A N     1 
ATOM   22642 C  CA    . THR A 1 4522 ? 162.845 174.110 189.054 1.00 17.61 ? 4522 THR A CA    1 
ATOM   22643 C  C     . THR A 1 4522 ? 163.040 173.066 187.960 1.00 21.15 ? 4522 THR A C     1 
ATOM   22644 O  O     . THR A 1 4522 ? 162.314 173.066 186.959 1.00 18.93 ? 4522 THR A O     1 
ATOM   22645 C  CB    . THR A 1 4522 ? 163.844 175.258 188.889 1.00 18.19 ? 4522 THR A CB    1 
ATOM   22646 O  OG1   . THR A 1 4522 ? 163.449 176.358 189.717 1.00 25.96 ? 4522 THR A OG1   1 
ATOM   22647 C  CG2   . THR A 1 4522 ? 163.908 175.721 187.440 1.00 23.71 ? 4522 THR A CG2   1 
ATOM   22648 N  N     . ALA A 1 4523 ? 164.008 172.164 188.137 1.00 19.72 ? 4523 ALA A N     1 
ATOM   22649 C  CA    . ALA A 1 4523 ? 164.272 171.150 187.121 1.00 17.16 ? 4523 ALA A CA    1 
ATOM   22650 C  C     . ALA A 1 4523 ? 163.072 170.235 186.921 1.00 19.34 ? 4523 ALA A C     1 
ATOM   22651 O  O     . ALA A 1 4523 ? 162.716 169.903 185.784 1.00 25.25 ? 4523 ALA A O     1 
ATOM   22652 C  CB    . ALA A 1 4523 ? 165.509 170.338 187.502 1.00 12.35 ? 4523 ALA A CB    1 
ATOM   22653 N  N     . THR A 1 4524 ? 162.434 169.813 188.016 1.00 24.43 ? 4524 THR A N     1 
ATOM   22654 C  CA    . THR A 1 4524 ? 161.241 168.980 187.903 1.00 19.41 ? 4524 THR A CA    1 
ATOM   22655 C  C     . THR A 1 4524 ? 160.103 169.737 187.231 1.00 17.23 ? 4524 THR A C     1 
ATOM   22656 O  O     . THR A 1 4524 ? 159.347 169.165 186.439 1.00 22.63 ? 4524 THR A O     1 
ATOM   22657 C  CB    . THR A 1 4524 ? 160.817 168.483 189.285 1.00 18.40 ? 4524 THR A CB    1 
ATOM   22658 O  OG1   . THR A 1 4524 ? 160.755 169.590 190.192 1.00 22.54 ? 4524 THR A OG1   1 
ATOM   22659 C  CG2   . THR A 1 4524 ? 161.812 167.462 189.807 1.00 16.21 ? 4524 THR A CG2   1 
ATOM   22660 N  N     . ARG A 1 4525 ? 159.960 171.025 187.547 1.00 16.47 ? 4525 ARG A N     1 
ATOM   22661 C  CA    . ARG A 1 4525 ? 158.975 171.854 186.861 1.00 16.10 ? 4525 ARG A CA    1 
ATOM   22662 C  C     . ARG A 1 4525 ? 159.299 171.973 185.377 1.00 20.33 ? 4525 ARG A C     1 
ATOM   22663 O  O     . ARG A 1 4525 ? 158.403 171.904 184.528 1.00 23.11 ? 4525 ARG A O     1 
ATOM   22664 C  CB    . ARG A 1 4525 ? 158.919 173.234 187.514 1.00 14.93 ? 4525 ARG A CB    1 
ATOM   22665 C  CG    . ARG A 1 4525 ? 157.805 174.131 187.017 1.00 15.43 ? 4525 ARG A CG    1 
ATOM   22666 C  CD    . ARG A 1 4525 ? 158.043 175.564 187.456 1.00 19.69 ? 4525 ARG A CD    1 
ATOM   22667 N  NE    . ARG A 1 4525 ? 156.805 176.325 187.567 1.00 23.66 ? 4525 ARG A NE    1 
ATOM   22668 C  CZ    . ARG A 1 4525 ? 156.406 176.942 188.671 1.00 25.99 ? 4525 ARG A CZ    1 
ATOM   22669 N  NH1   . ARG A 1 4525 ? 157.126 176.904 189.781 1.00 20.56 ? 4525 ARG A NH1   1 
ATOM   22670 N  NH2   . ARG A 1 4525 ? 155.259 177.613 188.660 1.00 24.49 ? 4525 ARG A NH2   1 
ATOM   22671 N  N     . GLN A 1 4526 ? 160.580 172.150 185.047 1.00 19.57 ? 4526 GLN A N     1 
ATOM   22672 C  CA    . GLN A 1 4526 ? 160.992 172.233 183.651 1.00 18.50 ? 4526 GLN A CA    1 
ATOM   22673 C  C     . GLN A 1 4526 ? 160.845 170.894 182.938 1.00 20.51 ? 4526 GLN A C     1 
ATOM   22674 O  O     . GLN A 1 4526 ? 160.579 170.861 181.732 1.00 29.62 ? 4526 GLN A O     1 
ATOM   22675 C  CB    . GLN A 1 4526 ? 162.432 172.742 183.573 1.00 21.22 ? 4526 GLN A CB    1 
ATOM   22676 C  CG    . GLN A 1 4526 ? 163.051 172.725 182.188 1.00 23.69 ? 4526 GLN A CG    1 
ATOM   22677 C  CD    . GLN A 1 4526 ? 162.293 173.578 181.198 1.00 23.81 ? 4526 GLN A CD    1 
ATOM   22678 O  OE1   . GLN A 1 4526 ? 162.164 174.788 181.373 1.00 19.53 ? 4526 GLN A OE1   1 
ATOM   22679 N  NE2   . GLN A 1 4526 ? 161.782 172.947 180.145 1.00 32.43 ? 4526 GLN A NE2   1 
ATOM   22680 N  N     . TYR A 1 4527 ? 161.012 169.785 183.663 1.00 16.66 ? 4527 TYR A N     1 
ATOM   22681 C  CA    . TYR A 1 4527 ? 160.889 168.465 183.052 1.00 21.26 ? 4527 TYR A CA    1 
ATOM   22682 C  C     . TYR A 1 4527 ? 159.465 168.207 182.574 1.00 21.46 ? 4527 TYR A C     1 
ATOM   22683 O  O     . TYR A 1 4527 ? 159.249 167.726 181.455 1.00 27.69 ? 4527 TYR A O     1 
ATOM   22684 C  CB    . TYR A 1 4527 ? 161.347 167.399 184.056 1.00 18.01 ? 4527 TYR A CB    1 
ATOM   22685 C  CG    . TYR A 1 4527 ? 161.134 165.946 183.663 1.00 20.61 ? 4527 TYR A CG    1 
ATOM   22686 C  CD1   . TYR A 1 4527 ? 159.873 165.360 183.700 1.00 17.57 ? 4527 TYR A CD1   1 
ATOM   22687 C  CD2   . TYR A 1 4527 ? 162.208 165.153 183.278 1.00 23.78 ? 4527 TYR A CD2   1 
ATOM   22688 C  CE1   . TYR A 1 4527 ? 159.689 164.037 183.351 1.00 22.46 ? 4527 TYR A CE1   1 
ATOM   22689 C  CE2   . TYR A 1 4527 ? 162.035 163.830 182.928 1.00 19.93 ? 4527 TYR A CE2   1 
ATOM   22690 C  CZ    . TYR A 1 4527 ? 160.774 163.277 182.967 1.00 24.12 ? 4527 TYR A CZ    1 
ATOM   22691 O  OH    . TYR A 1 4527 ? 160.597 161.959 182.618 1.00 32.10 ? 4527 TYR A OH    1 
ATOM   22692 N  N     . VAL A 1 4528 ? 158.476 168.511 183.417 1.00 20.04 ? 4528 VAL A N     1 
ATOM   22693 C  CA    . VAL A 1 4528 ? 157.090 168.194 183.084 1.00 19.30 ? 4528 VAL A CA    1 
ATOM   22694 C  C     . VAL A 1 4528 ? 156.578 169.097 181.970 1.00 26.20 ? 4528 VAL A C     1 
ATOM   22695 O  O     . VAL A 1 4528 ? 155.894 168.637 181.048 1.00 32.58 ? 4528 VAL A O     1 
ATOM   22696 C  CB    . VAL A 1 4528 ? 156.210 168.282 184.344 1.00 22.96 ? 4528 VAL A CB    1 
ATOM   22697 C  CG1   . VAL A 1 4528 ? 154.767 167.945 184.011 1.00 17.16 ? 4528 VAL A CG1   1 
ATOM   22698 C  CG2   . VAL A 1 4528 ? 156.743 167.346 185.420 1.00 16.23 ? 4528 VAL A CG2   1 
ATOM   22699 N  N     . ALA A 1 4529 ? 156.901 170.391 182.029 1.00 23.43 ? 4529 ALA A N     1 
ATOM   22700 C  CA    . ALA A 1 4529 ? 156.452 171.309 180.986 1.00 25.26 ? 4529 ALA A CA    1 
ATOM   22701 C  C     . ALA A 1 4529 ? 157.070 170.974 179.636 1.00 30.87 ? 4529 ALA A C     1 
ATOM   22702 O  O     . ALA A 1 4529 ? 156.490 171.297 178.593 1.00 29.38 ? 4529 ALA A O     1 
ATOM   22703 C  CB    . ALA A 1 4529 ? 156.779 172.749 181.370 1.00 26.67 ? 4529 ALA A CB    1 
ATOM   22704 N  N     . GLN A 1 4530 ? 158.243 170.339 179.631 1.00 27.90 ? 4530 GLN A N     1 
ATOM   22705 C  CA    . GLN A 1 4530 ? 158.867 169.960 178.369 1.00 25.43 ? 4530 GLN A CA    1 
ATOM   22706 C  C     . GLN A 1 4530 ? 158.086 168.856 177.669 1.00 31.53 ? 4530 GLN A C     1 
ATOM   22707 O  O     . GLN A 1 4530 ? 157.842 168.934 176.458 1.00 38.68 ? 4530 GLN A O     1 
ATOM   22708 C  CB    . GLN A 1 4530 ? 160.309 169.526 178.614 1.00 26.02 ? 4530 GLN A CB    1 
ATOM   22709 C  CG    . GLN A 1 4530 ? 161.131 169.385 177.351 1.00 25.22 ? 4530 GLN A CG    1 
ATOM   22710 C  CD    . GLN A 1 4530 ? 162.619 169.460 177.621 1.00 33.52 ? 4530 GLN A CD    1 
ATOM   22711 O  OE1   . GLN A 1 4530 ? 163.043 169.660 178.757 1.00 32.23 ? 4530 GLN A OE1   1 
ATOM   22712 N  NE2   . GLN A 1 4530 ? 163.421 169.298 176.574 1.00 36.59 ? 4530 GLN A NE2   1 
ATOM   22713 N  N     . ALA A 1 4531 ? 157.678 167.824 178.411 1.00 26.43 ? 4531 ALA A N     1 
ATOM   22714 C  CA    . ALA A 1 4531 ? 156.952 166.715 177.799 1.00 26.53 ? 4531 ALA A CA    1 
ATOM   22715 C  C     . ALA A 1 4531 ? 155.592 167.161 177.280 1.00 30.50 ? 4531 ALA A C     1 
ATOM   22716 O  O     . ALA A 1 4531 ? 155.152 166.718 176.212 1.00 34.70 ? 4531 ALA A O     1 
ATOM   22717 C  CB    . ALA A 1 4531 ? 156.795 165.572 178.801 1.00 24.32 ? 4531 ALA A CB    1 
ATOM   22718 N  N     . ASN A 1 4532 ? 154.916 168.036 178.016 1.00 31.16 ? 4532 ASN A N     1 
ATOM   22719 C  CA    . ASN A 1 4532 ? 153.580 168.494 177.668 1.00 29.35 ? 4532 ASN A CA    1 
ATOM   22720 C  C     . ASN A 1 4532 ? 153.591 169.784 176.857 1.00 31.41 ? 4532 ASN A C     1 
ATOM   22721 O  O     . ASN A 1 4532 ? 152.520 170.335 176.583 1.00 31.78 ? 4532 ASN A O     1 
ATOM   22722 C  CB    . ASN A 1 4532 ? 152.752 168.681 178.940 1.00 29.36 ? 4532 ASN A CB    1 
ATOM   22723 C  CG    . ASN A 1 4532 ? 152.792 167.466 179.844 1.00 33.34 ? 4532 ASN A CG    1 
ATOM   22724 O  OD1   . ASN A 1 4532 ? 153.177 167.559 181.010 1.00 34.63 ? 4532 ASN A OD1   1 
ATOM   22725 N  ND2   . ASN A 1 4532 ? 152.407 166.314 179.307 1.00 34.20 ? 4532 ASN A ND2   1 
ATOM   22726 N  N     . SER A 1 4533 ? 154.775 170.271 176.475 1.00 29.98 ? 4533 SER A N     1 
ATOM   22727 C  CA    . SER A 1 4533 ? 154.922 171.477 175.659 1.00 28.51 ? 4533 SER A CA    1 
ATOM   22728 C  C     . SER A 1 4533 ? 154.251 172.686 176.311 1.00 29.42 ? 4533 SER A C     1 
ATOM   22729 O  O     . SER A 1 4533 ? 153.613 173.502 175.642 1.00 30.43 ? 4533 SER A O     1 
ATOM   22730 C  CB    . SER A 1 4533 ? 154.385 171.257 174.242 1.00 28.42 ? 4533 SER A CB    1 
ATOM   22731 O  OG    . SER A 1 4533 ? 154.641 172.382 173.420 1.00 29.99 ? 4533 SER A OG    1 
ATOM   22732 N  N     . TRP A 1 4534 ? 154.401 172.808 177.624 1.00 27.74 ? 4534 TRP A N     1 
ATOM   22733 C  CA    . TRP A 1 4534 ? 153.820 173.905 178.383 1.00 25.28 ? 4534 TRP A CA    1 
ATOM   22734 C  C     . TRP A 1 4534 ? 154.911 174.846 178.879 1.00 25.68 ? 4534 TRP A C     1 
ATOM   22735 O  O     . TRP A 1 4534 ? 156.109 174.591 178.730 1.00 27.45 ? 4534 TRP A O     1 
ATOM   22736 C  CB    . TRP A 1 4534 ? 152.999 173.379 179.565 1.00 25.98 ? 4534 TRP A CB    1 
ATOM   22737 C  CG    . TRP A 1 4534 ? 151.760 172.645 179.169 1.00 27.98 ? 4534 TRP A CG    1 
ATOM   22738 C  CD1   . TRP A 1 4534 ? 151.016 172.842 178.044 1.00 28.16 ? 4534 TRP A CD1   1 
ATOM   22739 C  CD2   . TRP A 1 4534 ? 151.106 171.606 179.906 1.00 27.46 ? 4534 TRP A CD2   1 
ATOM   22740 N  NE1   . TRP A 1 4534 ? 149.944 171.983 178.030 1.00 32.23 ? 4534 TRP A NE1   1 
ATOM   22741 C  CE2   . TRP A 1 4534 ? 149.976 171.216 179.163 1.00 27.30 ? 4534 TRP A CE2   1 
ATOM   22742 C  CE3   . TRP A 1 4534 ? 151.369 170.966 181.122 1.00 29.03 ? 4534 TRP A CE3   1 
ATOM   22743 C  CZ2   . TRP A 1 4534 ? 149.110 170.212 179.593 1.00 29.05 ? 4534 TRP A CZ2   1 
ATOM   22744 C  CZ3   . TRP A 1 4534 ? 150.509 169.970 181.546 1.00 30.05 ? 4534 TRP A CZ3   1 
ATOM   22745 C  CH2   . TRP A 1 4534 ? 149.393 169.603 180.785 1.00 29.73 ? 4534 TRP A CH2   1 
ATOM   22746 N  N     . SER A 1 4535 ? 154.471 175.954 179.465 1.00 25.76 ? 4535 SER A N     1 
ATOM   22747 C  CA    . SER A 1 4535 ? 155.366 176.912 180.093 1.00 27.37 ? 4535 SER A CA    1 
ATOM   22748 C  C     . SER A 1 4535 ? 155.472 176.631 181.586 1.00 31.07 ? 4535 SER A C     1 
ATOM   22749 O  O     . SER A 1 4535 ? 154.565 176.055 182.194 1.00 33.00 ? 4535 SER A O     1 
ATOM   22750 C  CB    . SER A 1 4535 ? 154.875 178.342 179.863 1.00 27.69 ? 4535 SER A CB    1 
ATOM   22751 O  OG    . SER A 1 4535 ? 155.638 179.270 180.613 1.00 32.65 ? 4535 SER A OG    1 
ATOM   22752 N  N     . LEU A 1 4536 ? 156.597 177.048 182.175 1.00 24.35 ? 4536 LEU A N     1 
ATOM   22753 C  CA    . LEU A 1 4536 ? 156.807 176.815 183.600 1.00 26.22 ? 4536 LEU A CA    1 
ATOM   22754 C  C     . LEU A 1 4536 ? 155.768 177.542 184.441 1.00 32.76 ? 4536 LEU A C     1 
ATOM   22755 O  O     . LEU A 1 4536 ? 155.353 177.033 185.489 1.00 32.26 ? 4536 LEU A O     1 
ATOM   22756 C  CB    . LEU A 1 4536 ? 158.215 177.246 184.012 1.00 26.07 ? 4536 LEU A CB    1 
ATOM   22757 C  CG    . LEU A 1 4536 ? 159.403 176.522 183.374 1.00 29.55 ? 4536 LEU A CG    1 
ATOM   22758 C  CD1   . LEU A 1 4536 ? 159.844 177.225 182.094 1.00 25.09 ? 4536 LEU A CD1   1 
ATOM   22759 C  CD2   . LEU A 1 4536 ? 160.556 176.402 184.353 1.00 22.50 ? 4536 LEU A CD2   1 
ATOM   22760 N  N     . GLU A 1 4537 ? 155.340 178.728 184.003 1.00 32.26 ? 4537 GLU A N     1 
ATOM   22761 C  CA    . GLU A 1 4537 ? 154.307 179.461 184.727 1.00 25.63 ? 4537 GLU A CA    1 
ATOM   22762 C  C     . GLU A 1 4537 ? 152.962 178.751 184.664 1.00 30.05 ? 4537 GLU A C     1 
ATOM   22763 O  O     . GLU A 1 4537 ? 152.097 178.989 185.516 1.00 36.34 ? 4537 GLU A O     1 
ATOM   22764 C  CB    . GLU A 1 4537 ? 154.180 180.880 184.173 1.00 27.43 ? 4537 GLU A CB    1 
ATOM   22765 C  CG    . GLU A 1 4537 ? 155.464 181.689 184.236 1.00 30.96 ? 4537 GLU A CG    1 
ATOM   22766 C  CD    . GLU A 1 4537 ? 155.323 183.053 183.591 1.00 35.51 ? 4537 GLU A CD    1 
ATOM   22767 O  OE1   . GLU A 1 4537 ? 154.458 183.836 184.036 1.00 31.75 ? 4537 GLU A OE1   1 
ATOM   22768 O  OE2   . GLU A 1 4537 ? 156.080 183.343 182.640 1.00 32.45 ? 4537 GLU A OE2   1 
ATOM   22769 N  N     . GLU A 1 4538 ? 152.763 177.884 183.673 1.00 25.04 ? 4538 GLU A N     1 
ATOM   22770 C  CA    . GLU A 1 4538 ? 151.494 177.185 183.517 1.00 31.00 ? 4538 GLU A CA    1 
ATOM   22771 C  C     . GLU A 1 4538 ? 151.399 175.925 184.365 1.00 27.28 ? 4538 GLU A C     1 
ATOM   22772 O  O     . GLU A 1 4538 ? 150.393 175.215 184.265 1.00 25.61 ? 4538 GLU A O     1 
ATOM   22773 C  CB    . GLU A 1 4538 ? 151.267 176.836 182.044 1.00 32.69 ? 4538 GLU A CB    1 
ATOM   22774 C  CG    . GLU A 1 4538 ? 151.406 178.017 181.100 1.00 32.88 ? 4538 GLU A CG    1 
ATOM   22775 C  CD    . GLU A 1 4538 ? 151.484 177.594 179.647 1.00 39.56 ? 4538 GLU A CD    1 
ATOM   22776 O  OE1   . GLU A 1 4538 ? 151.447 176.375 179.377 1.00 40.24 ? 4538 GLU A OE1   1 
ATOM   22777 O  OE2   . GLU A 1 4538 ? 151.580 178.482 178.773 1.00 39.94 ? 4538 GLU A OE2   1 
ATOM   22778 N  N     . LEU A 1 4539 ? 152.407 175.624 185.180 1.00 28.07 ? 4539 LEU A N     1 
ATOM   22779 C  CA    . LEU A 1 4539 ? 152.398 174.451 186.048 1.00 23.03 ? 4539 LEU A CA    1 
ATOM   22780 C  C     . LEU A 1 4539 ? 152.317 174.906 187.500 1.00 23.03 ? 4539 LEU A C     1 
ATOM   22781 O  O     . LEU A 1 4539 ? 153.143 175.703 187.956 1.00 27.78 ? 4539 LEU A O     1 
ATOM   22782 C  CB    . LEU A 1 4539 ? 153.639 173.593 185.827 1.00 18.40 ? 4539 LEU A CB    1 
ATOM   22783 C  CG    . LEU A 1 4539 ? 153.799 172.899 184.478 1.00 18.92 ? 4539 LEU A CG    1 
ATOM   22784 C  CD1   . LEU A 1 4539 ? 155.145 172.216 184.431 1.00 24.80 ? 4539 LEU A CD1   1 
ATOM   22785 C  CD2   . LEU A 1 4539 ? 152.682 171.897 184.257 1.00 20.09 ? 4539 LEU A CD2   1 
ATOM   22786 N  N     . CYS A 1 4540 ? 151.325 174.396 188.218 1.00 19.89 ? 4540 CYS A N     1 
ATOM   22787 C  CA    . CYS A 1 4540 ? 151.237 174.551 189.660 1.00 18.06 ? 4540 CYS A CA    1 
ATOM   22788 C  C     . CYS A 1 4540 ? 151.650 173.245 190.326 1.00 24.14 ? 4540 CYS A C     1 
ATOM   22789 O  O     . CYS A 1 4540 ? 151.453 172.159 189.776 1.00 24.14 ? 4540 CYS A O     1 
ATOM   22790 C  CB    . CYS A 1 4540 ? 149.822 174.943 190.089 1.00 17.90 ? 4540 CYS A CB    1 
ATOM   22791 S  SG    . CYS A 1 4540 ? 148.569 173.679 189.789 1.00 51.10 ? 4540 CYS A SG    1 
ATOM   22792 N  N     . LEU A 1 4541 ? 152.239 173.360 191.511 1.00 22.09 ? 4541 LEU A N     1 
ATOM   22793 C  CA    . LEU A 1 4541 ? 152.789 172.211 192.220 1.00 17.38 ? 4541 LEU A CA    1 
ATOM   22794 C  C     . LEU A 1 4541 ? 151.737 171.637 193.159 1.00 15.41 ? 4541 LEU A C     1 
ATOM   22795 O  O     . LEU A 1 4541 ? 151.298 172.314 194.094 1.00 25.07 ? 4541 LEU A O     1 
ATOM   22796 C  CB    . LEU A 1 4541 ? 154.046 172.601 192.997 1.00 15.60 ? 4541 LEU A CB    1 
ATOM   22797 C  CG    . LEU A 1 4541 ? 154.694 171.490 193.825 1.00 19.57 ? 4541 LEU A CG    1 
ATOM   22798 C  CD1   . LEU A 1 4541 ? 154.979 170.273 192.960 1.00 18.93 ? 4541 LEU A CD1   1 
ATOM   22799 C  CD2   . LEU A 1 4541 ? 155.969 171.990 194.483 1.00 16.38 ? 4541 LEU A CD2   1 
ATOM   22800 N  N     . GLU A 1 4542 ? 151.340 170.394 192.907 1.00 18.35 ? 4542 GLU A N     1 
ATOM   22801 C  CA    . GLU A 1 4542 ? 150.467 169.651 193.801 1.00 14.75 ? 4542 GLU A CA    1 
ATOM   22802 C  C     . GLU A 1 4542 ? 151.306 168.686 194.627 1.00 15.92 ? 4542 GLU A C     1 
ATOM   22803 O  O     . GLU A 1 4542 ? 152.216 168.035 194.106 1.00 20.55 ? 4542 GLU A O     1 
ATOM   22804 C  CB    . GLU A 1 4542 ? 149.395 168.885 193.023 1.00 16.44 ? 4542 GLU A CB    1 
ATOM   22805 C  CG    . GLU A 1 4542 ? 148.295 169.762 192.458 1.00 20.38 ? 4542 GLU A CG    1 
ATOM   22806 C  CD    . GLU A 1 4542 ? 147.716 170.711 193.490 1.00 33.42 ? 4542 GLU A CD    1 
ATOM   22807 O  OE1   . GLU A 1 4542 ? 147.958 171.930 193.380 1.00 29.95 ? 4542 GLU A OE1   1 
ATOM   22808 O  OE2   . GLU A 1 4542 ? 147.016 170.236 194.409 1.00 28.74 ? 4542 GLU A OE2   1 
ATOM   22809 N  N     . VAL A 1 4543 ? 151.001 168.604 195.918 1.00 15.95 ? 4543 VAL A N     1 
ATOM   22810 C  CA    . VAL A 1 4543 ? 151.805 167.855 196.873 1.00 11.77 ? 4543 VAL A CA    1 
ATOM   22811 C  C     . VAL A 1 4543 ? 150.970 166.707 197.421 1.00 11.45 ? 4543 VAL A C     1 
ATOM   22812 O  O     . VAL A 1 4543 ? 149.834 166.914 197.860 1.00 17.13 ? 4543 VAL A O     1 
ATOM   22813 C  CB    . VAL A 1 4543 ? 152.312 168.758 198.011 1.00 14.35 ? 4543 VAL A CB    1 
ATOM   22814 C  CG1   . VAL A 1 4543 ? 152.762 167.926 199.197 1.00 9.71  ? 4543 VAL A CG1   1 
ATOM   22815 C  CG2   . VAL A 1 4543 ? 153.443 169.644 197.514 1.00 12.60 ? 4543 VAL A CG2   1 
ATOM   22816 N  N     . ASN A 1 4544 ? 151.531 165.502 197.383 1.00 15.39 ? 4544 ASN A N     1 
ATOM   22817 C  CA    . ASN A 1 4544 ? 150.913 164.325 197.976 1.00 11.56 ? 4544 ASN A CA    1 
ATOM   22818 C  C     . ASN A 1 4544 ? 151.913 163.668 198.914 1.00 13.96 ? 4544 ASN A C     1 
ATOM   22819 O  O     . ASN A 1 4544 ? 153.073 163.459 198.542 1.00 17.00 ? 4544 ASN A O     1 
ATOM   22820 C  CB    . ASN A 1 4544 ? 150.453 163.333 196.904 1.00 17.05 ? 4544 ASN A CB    1 
ATOM   22821 C  CG    . ASN A 1 4544 ? 150.019 162.004 197.486 1.00 21.03 ? 4544 ASN A CG    1 
ATOM   22822 O  OD1   . ASN A 1 4544 ? 148.901 161.866 197.976 1.00 22.95 ? 4544 ASN A OD1   1 
ATOM   22823 N  ND2   . ASN A 1 4544 ? 150.904 161.017 197.435 1.00 22.46 ? 4544 ASN A ND2   1 
ATOM   22824 N  N     . VAL A 1 4545 ? 151.465 163.351 200.124 1.00 15.77 ? 4545 VAL A N     1 
ATOM   22825 C  CA    . VAL A 1 4545 ? 152.297 162.747 201.157 1.00 15.19 ? 4545 VAL A CA    1 
ATOM   22826 C  C     . VAL A 1 4545 ? 151.821 161.321 201.375 1.00 17.82 ? 4545 VAL A C     1 
ATOM   22827 O  O     . VAL A 1 4545 ? 150.628 161.085 201.600 1.00 24.83 ? 4545 VAL A O     1 
ATOM   22828 C  CB    . VAL A 1 4545 ? 152.244 163.557 202.465 1.00 18.98 ? 4545 VAL A CB    1 
ATOM   22829 C  CG1   . VAL A 1 4545 ? 152.868 162.768 203.605 1.00 23.25 ? 4545 VAL A CG1   1 
ATOM   22830 C  CG2   . VAL A 1 4545 ? 152.941 164.898 202.289 1.00 10.75 ? 4545 VAL A CG2   1 
ATOM   22831 N  N     . THR A 1 4546 ? 152.749 160.372 201.304 1.00 18.86 ? 4546 THR A N     1 
ATOM   22832 C  CA    . THR A 1 4546 ? 152.436 158.956 201.410 1.00 16.97 ? 4546 THR A CA    1 
ATOM   22833 C  C     . THR A 1 4546 ? 152.706 158.449 202.820 1.00 25.09 ? 4546 THR A C     1 
ATOM   22834 O  O     . THR A 1 4546 ? 153.580 158.955 203.529 1.00 28.31 ? 4546 THR A O     1 
ATOM   22835 C  CB    . THR A 1 4546 ? 153.255 158.139 200.410 1.00 22.04 ? 4546 THR A CB    1 
ATOM   22836 O  OG1   . THR A 1 4546 ? 154.563 157.904 200.945 1.00 30.80 ? 4546 THR A OG1   1 
ATOM   22837 C  CG2   . THR A 1 4546 ? 153.385 158.885 199.099 1.00 20.05 ? 4546 THR A CG2   1 
ATOM   22838 N  N     . THR A 1 4547 ? 151.938 157.432 203.219 1.00 26.80 ? 4547 THR A N     1 
ATOM   22839 C  CA    . THR A 1 4547 ? 152.151 156.806 204.519 1.00 29.66 ? 4547 THR A CA    1 
ATOM   22840 C  C     . THR A 1 4547 ? 153.512 156.126 204.585 1.00 32.00 ? 4547 THR A C     1 
ATOM   22841 O  O     . THR A 1 4547 ? 154.194 156.182 205.615 1.00 34.03 ? 4547 THR A O     1 
ATOM   22842 C  CB    . THR A 1 4547 ? 151.035 155.802 204.808 1.00 30.30 ? 4547 THR A CB    1 
ATOM   22843 O  OG1   . THR A 1 4547 ? 149.763 156.441 204.644 1.00 35.57 ? 4547 THR A OG1   1 
ATOM   22844 C  CG2   . THR A 1 4547 ? 151.148 155.271 206.230 1.00 25.31 ? 4547 THR A CG2   1 
ATOM   22845 N  N     . SER A 1 4548 ? 153.926 155.481 203.498 1.00 29.72 ? 4548 SER A N     1 
ATOM   22846 C  CA    . SER A 1 4548 ? 155.213 154.805 203.441 1.00 31.01 ? 4548 SER A CA    1 
ATOM   22847 C  C     . SER A 1 4548 ? 155.898 155.143 202.126 1.00 30.50 ? 4548 SER A C     1 
ATOM   22848 O  O     . SER A 1 4548 ? 155.253 155.498 201.136 1.00 28.30 ? 4548 SER A O     1 
ATOM   22849 C  CB    . SER A 1 4548 ? 155.064 153.284 203.584 1.00 29.17 ? 4548 SER A CB    1 
ATOM   22850 O  OG    . SER A 1 4548 ? 154.402 152.729 202.461 1.00 30.02 ? 4548 SER A OG    1 
ATOM   22851 N  N     . GLN A 1 4549 ? 157.223 155.025 202.129 1.00 33.72 ? 4549 GLN A N     1 
ATOM   22852 C  CA    . GLN A 1 4549 ? 158.006 155.264 200.928 1.00 28.35 ? 4549 GLN A CA    1 
ATOM   22853 C  C     . GLN A 1 4549 ? 157.849 154.099 199.953 1.00 29.41 ? 4549 GLN A C     1 
ATOM   22854 O  O     . GLN A 1 4549 ? 157.318 153.036 200.286 1.00 34.83 ? 4549 GLN A O     1 
ATOM   22855 C  CB    . GLN A 1 4549 ? 159.479 155.468 201.281 1.00 23.31 ? 4549 GLN A CB    1 
ATOM   22856 C  CG    . GLN A 1 4549 ? 159.757 156.701 202.129 1.00 24.15 ? 4549 GLN A CG    1 
ATOM   22857 C  CD    . GLN A 1 4549 ? 159.672 156.417 203.616 1.00 31.31 ? 4549 GLN A CD    1 
ATOM   22858 O  OE1   . GLN A 1 4549 ? 159.215 155.351 204.031 1.00 29.85 ? 4549 GLN A OE1   1 
ATOM   22859 N  NE2   . GLN A 1 4549 ? 160.120 157.368 204.427 1.00 28.23 ? 4549 GLN A NE2   1 
ATOM   22860 N  N     . GLY A 1 4550 ? 158.323 154.313 198.729 1.00 28.58 ? 4550 GLY A N     1 
ATOM   22861 C  CA    . GLY A 1 4550 ? 158.240 153.295 197.701 1.00 28.49 ? 4550 GLY A CA    1 
ATOM   22862 C  C     . GLY A 1 4550 ? 156.830 153.082 197.189 1.00 35.30 ? 4550 GLY A C     1 
ATOM   22863 O  O     . GLY A 1 4550 ? 156.267 151.993 197.330 1.00 34.41 ? 4550 GLY A O     1 
ATOM   22864 N  N     . ALA A 1 4551 ? 156.250 154.121 196.592 1.00 34.28 ? 4551 ALA A N     1 
ATOM   22865 C  CA    . ALA A 1 4551 ? 154.899 154.066 196.059 1.00 33.38 ? 4551 ALA A CA    1 
ATOM   22866 C  C     . ALA A 1 4551 ? 154.940 154.263 194.550 1.00 33.23 ? 4551 ALA A C     1 
ATOM   22867 O  O     . ALA A 1 4551 ? 155.990 154.557 193.969 1.00 36.21 ? 4551 ALA A O     1 
ATOM   22868 C  CB    . ALA A 1 4551 ? 153.994 155.123 196.706 1.00 28.51 ? 4551 ALA A CB    1 
ATOM   22869 N  N     . THR A 1 4552 ? 153.782 154.089 193.920 1.00 31.91 ? 4552 THR A N     1 
ATOM   22870 C  CA    . THR A 1 4552 ? 153.675 154.249 192.474 1.00 30.54 ? 4552 THR A CA    1 
ATOM   22871 C  C     . THR A 1 4552 ? 154.004 155.680 192.070 1.00 32.39 ? 4552 THR A C     1 
ATOM   22872 O  O     . THR A 1 4552 ? 153.360 156.630 192.524 1.00 35.55 ? 4552 THR A O     1 
ATOM   22873 C  CB    . THR A 1 4552 ? 152.266 153.877 192.009 1.00 32.53 ? 4552 THR A CB    1 
ATOM   22874 O  OG1   . THR A 1 4552 ? 151.311 154.746 192.628 1.00 37.30 ? 4552 THR A OG1   1 
ATOM   22875 C  CG2   . THR A 1 4552 ? 151.948 152.436 192.379 1.00 24.54 ? 4552 THR A CG2   1 
ATOM   22876 N  N     . LEU A 1 4553 ? 155.008 155.829 191.211 1.00 30.88 ? 4553 LEU A N     1 
ATOM   22877 C  CA    . LEU A 1 4553 ? 155.469 157.136 190.761 1.00 28.55 ? 4553 LEU A CA    1 
ATOM   22878 C  C     . LEU A 1 4553 ? 154.868 157.428 189.391 1.00 29.71 ? 4553 LEU A C     1 
ATOM   22879 O  O     . LEU A 1 4553 ? 155.191 156.756 188.405 1.00 34.38 ? 4553 LEU A O     1 
ATOM   22880 C  CB    . LEU A 1 4553 ? 156.994 157.189 190.720 1.00 27.28 ? 4553 LEU A CB    1 
ATOM   22881 C  CG    . LEU A 1 4553 ? 157.680 157.507 192.052 1.00 30.54 ? 4553 LEU A CG    1 
ATOM   22882 C  CD1   . LEU A 1 4553 ? 159.156 157.814 191.845 1.00 24.39 ? 4553 LEU A CD1   1 
ATOM   22883 C  CD2   . LEU A 1 4553 ? 156.979 158.661 192.750 1.00 17.43 ? 4553 LEU A CD2   1 
ATOM   22884 N  N     . ASP A 1 4554 ? 153.997 158.430 189.334 1.00 30.24 ? 4554 ASP A N     1 
ATOM   22885 C  CA    . ASP A 1 4554 ? 153.405 158.851 188.077 1.00 25.05 ? 4554 ASP A CA    1 
ATOM   22886 C  C     . ASP A 1 4554 ? 154.451 159.557 187.217 1.00 26.53 ? 4554 ASP A C     1 
ATOM   22887 O  O     . ASP A 1 4554 ? 155.518 159.958 187.691 1.00 30.40 ? 4554 ASP A O     1 
ATOM   22888 C  CB    . ASP A 1 4554 ? 152.208 159.768 188.338 1.00 26.61 ? 4554 ASP A CB    1 
ATOM   22889 C  CG    . ASP A 1 4554 ? 151.398 160.062 187.086 1.00 34.37 ? 4554 ASP A CG    1 
ATOM   22890 O  OD1   . ASP A 1 4554 ? 151.771 159.579 185.995 1.00 35.21 ? 4554 ASP A OD1   1 
ATOM   22891 O  OD2   . ASP A 1 4554 ? 150.381 160.778 187.195 1.00 40.28 ? 4554 ASP A OD2   1 
ATOM   22892 N  N     . ALA A 1 4555 ? 154.134 159.698 185.928 1.00 29.44 ? 4555 ALA A N     1 
ATOM   22893 C  CA    . ALA A 1 4555 ? 155.060 160.335 184.997 1.00 26.34 ? 4555 ALA A CA    1 
ATOM   22894 C  C     . ALA A 1 4555 ? 155.341 161.778 185.398 1.00 23.56 ? 4555 ALA A C     1 
ATOM   22895 O  O     . ALA A 1 4555 ? 156.480 162.249 185.309 1.00 27.89 ? 4555 ALA A O     1 
ATOM   22896 C  CB    . ALA A 1 4555 ? 154.503 160.268 183.576 1.00 21.27 ? 4555 ALA A CB    1 
ATOM   22897 N  N     . CYS A 1 4556 ? 154.309 162.498 185.842 1.00 24.44 ? 4556 CYS A N     1 
ATOM   22898 C  CA    . CYS A 1 4556 ? 154.442 163.890 186.256 1.00 23.18 ? 4556 CYS A CA    1 
ATOM   22899 C  C     . CYS A 1 4556 ? 154.593 164.046 187.765 1.00 24.83 ? 4556 CYS A C     1 
ATOM   22900 O  O     . CYS A 1 4556 ? 154.176 165.070 188.321 1.00 21.91 ? 4556 CYS A O     1 
ATOM   22901 C  CB    . CYS A 1 4556 ? 153.248 164.699 185.752 1.00 21.44 ? 4556 CYS A CB    1 
ATOM   22902 S  SG    . CYS A 1 4556 ? 151.640 164.093 186.320 1.00 53.93 ? 4556 CYS A SG    1 
ATOM   22903 N  N     . SER A 1 4557 ? 155.181 163.060 188.444 1.00 25.38 ? 4557 SER A N     1 
ATOM   22904 C  CA    . SER A 1 4557 ? 155.340 163.089 189.890 1.00 20.31 ? 4557 SER A CA    1 
ATOM   22905 C  C     . SER A 1 4557 ? 156.777 162.758 190.263 1.00 21.35 ? 4557 SER A C     1 
ATOM   22906 O  O     . SER A 1 4557 ? 157.473 162.037 189.543 1.00 29.57 ? 4557 SER A O     1 
ATOM   22907 C  CB    . SER A 1 4557 ? 154.384 162.109 190.575 1.00 21.26 ? 4557 SER A CB    1 
ATOM   22908 O  OG    . SER A 1 4557 ? 153.065 162.625 190.616 1.00 32.21 ? 4557 SER A OG    1 
ATOM   22909 N  N     . PHE A 1 4558 ? 157.219 163.295 191.398 1.00 15.87 ? 4558 PHE A N     1 
ATOM   22910 C  CA    . PHE A 1 4558 ? 158.578 163.085 191.876 1.00 16.60 ? 4558 PHE A CA    1 
ATOM   22911 C  C     . PHE A 1 4558 ? 158.556 162.811 193.372 1.00 14.00 ? 4558 PHE A C     1 
ATOM   22912 O  O     . PHE A 1 4558 ? 157.818 163.459 194.116 1.00 17.60 ? 4558 PHE A O     1 
ATOM   22913 C  CB    . PHE A 1 4558 ? 159.467 164.294 191.572 1.00 13.96 ? 4558 PHE A CB    1 
ATOM   22914 C  CG    . PHE A 1 4558 ? 159.606 164.587 190.110 1.00 17.18 ? 4558 PHE A CG    1 
ATOM   22915 C  CD1   . PHE A 1 4558 ? 160.580 163.960 189.355 1.00 18.68 ? 4558 PHE A CD1   1 
ATOM   22916 C  CD2   . PHE A 1 4558 ? 158.751 165.479 189.485 1.00 19.99 ? 4558 PHE A CD2   1 
ATOM   22917 C  CE1   . PHE A 1 4558 ? 160.705 164.224 188.008 1.00 15.17 ? 4558 PHE A CE1   1 
ATOM   22918 C  CE2   . PHE A 1 4558 ? 158.870 165.744 188.137 1.00 18.21 ? 4558 PHE A CE2   1 
ATOM   22919 C  CZ    . PHE A 1 4558 ? 159.849 165.117 187.399 1.00 17.36 ? 4558 PHE A CZ    1 
ATOM   22920 N  N     . GLY A 1 4559 ? 159.375 161.857 193.805 1.00 15.62 ? 4559 GLY A N     1 
ATOM   22921 C  CA    . GLY A 1 4559 ? 159.441 161.468 195.202 1.00 18.18 ? 4559 GLY A CA    1 
ATOM   22922 C  C     . GLY A 1 4559 ? 160.546 162.211 195.928 1.00 14.15 ? 4559 GLY A C     1 
ATOM   22923 O  O     . GLY A 1 4559 ? 161.686 162.268 195.460 1.00 21.94 ? 4559 GLY A O     1 
ATOM   22924 N  N     . VAL A 1 4560 ? 160.195 162.778 197.079 1.00 14.21 ? 4560 VAL A N     1 
ATOM   22925 C  CA    . VAL A 1 4560 ? 161.116 163.547 197.906 1.00 12.63 ? 4560 VAL A CA    1 
ATOM   22926 C  C     . VAL A 1 4560 ? 161.071 162.989 199.322 1.00 12.60 ? 4560 VAL A C     1 
ATOM   22927 O  O     . VAL A 1 4560 ? 159.987 162.746 199.863 1.00 18.76 ? 4560 VAL A O     1 
ATOM   22928 C  CB    . VAL A 1 4560 ? 160.774 165.050 197.897 1.00 12.20 ? 4560 VAL A CB    1 
ATOM   22929 C  CG1   . VAL A 1 4560 ? 161.626 165.804 198.902 1.00 13.68 ? 4560 VAL A CG1   1 
ATOM   22930 C  CG2   . VAL A 1 4560 ? 160.970 165.622 196.508 1.00 10.19 ? 4560 VAL A CG2   1 
ATOM   22931 N  N     . THR A 1 4561 ? 162.242 162.778 199.914 1.00 17.38 ? 4561 THR A N     1 
ATOM   22932 C  CA    . THR A 1 4561 ? 162.355 162.263 201.270 1.00 17.77 ? 4561 THR A CA    1 
ATOM   22933 C  C     . THR A 1 4561 ? 163.045 163.288 202.161 1.00 13.61 ? 4561 THR A C     1 
ATOM   22934 O  O     . THR A 1 4561 ? 163.792 164.150 201.692 1.00 16.45 ? 4561 THR A O     1 
ATOM   22935 C  CB    . THR A 1 4561 ? 163.133 160.940 201.308 1.00 15.79 ? 4561 THR A CB    1 
ATOM   22936 O  OG1   . THR A 1 4561 ? 164.537 161.206 201.215 1.00 21.03 ? 4561 THR A OG1   1 
ATOM   22937 C  CG2   . THR A 1 4561 ? 162.719 160.042 200.158 1.00 18.49 ? 4561 THR A CG2   1 
ATOM   22938 N  N     . GLY A 1 4562 ? 162.781 163.186 203.463 1.00 13.56 ? 4562 GLY A N     1 
ATOM   22939 C  CA    . GLY A 1 4562 ? 163.427 164.031 204.444 1.00 12.56 ? 4562 GLY A CA    1 
ATOM   22940 C  C     . GLY A 1 4562 ? 162.708 165.317 204.792 1.00 15.16 ? 4562 GLY A C     1 
ATOM   22941 O  O     . GLY A 1 4562 ? 163.215 166.078 205.625 1.00 14.64 ? 4562 GLY A O     1 
ATOM   22942 N  N     . LEU A 1 4563 ? 161.559 165.595 204.183 1.00 17.87 ? 4563 LEU A N     1 
ATOM   22943 C  CA    . LEU A 1 4563 ? 160.784 166.769 204.561 1.00 10.31 ? 4563 LEU A CA    1 
ATOM   22944 C  C     . LEU A 1 4563 ? 160.247 166.611 205.978 1.00 11.61 ? 4563 LEU A C     1 
ATOM   22945 O  O     . LEU A 1 4563 ? 159.732 165.553 206.350 1.00 13.14 ? 4563 LEU A O     1 
ATOM   22946 C  CB    . LEU A 1 4563 ? 159.631 166.989 203.584 1.00 9.35  ? 4563 LEU A CB    1 
ATOM   22947 C  CG    . LEU A 1 4563 ? 159.977 167.381 202.146 1.00 9.62  ? 4563 LEU A CG    1 
ATOM   22948 C  CD1   . LEU A 1 4563 ? 158.719 167.762 201.386 1.00 6.80  ? 4563 LEU A CD1   1 
ATOM   22949 C  CD2   . LEU A 1 4563 ? 160.988 168.513 202.117 1.00 8.59  ? 4563 LEU A CD2   1 
ATOM   22950 N  N     . LYS A 1 4564 ? 160.370 167.671 206.773 1.00 12.53 ? 4564 LYS A N     1 
ATOM   22951 C  CA    . LYS A 1 4564 ? 159.941 167.665 208.166 1.00 9.88  ? 4564 LYS A CA    1 
ATOM   22952 C  C     . LYS A 1 4564 ? 158.871 168.728 208.358 1.00 9.00  ? 4564 LYS A C     1 
ATOM   22953 O  O     . LYS A 1 4564 ? 159.105 169.908 208.078 1.00 10.28 ? 4564 LYS A O     1 
ATOM   22954 C  CB    . LYS A 1 4564 ? 161.123 167.915 209.106 1.00 8.97  ? 4564 LYS A CB    1 
ATOM   22955 C  CG    . LYS A 1 4564 ? 162.174 166.818 209.100 1.00 13.00 ? 4564 LYS A CG    1 
ATOM   22956 C  CD    . LYS A 1 4564 ? 161.603 165.502 209.595 1.00 15.46 ? 4564 LYS A CD    1 
ATOM   22957 C  CE    . LYS A 1 4564 ? 162.690 164.456 209.778 1.00 16.58 ? 4564 LYS A CE    1 
ATOM   22958 N  NZ    . LYS A 1 4564 ? 163.391 164.144 208.503 1.00 20.28 ? 4564 LYS A NZ    1 
ATOM   22959 N  N     . LEU A 1 4565 ? 157.704 168.312 208.840 1.00 7.44  ? 4565 LEU A N     1 
ATOM   22960 C  CA    . LEU A 1 4565 ? 156.598 169.230 209.075 1.00 4.32  ? 4565 LEU A CA    1 
ATOM   22961 C  C     . LEU A 1 4565 ? 156.714 169.818 210.477 1.00 6.65  ? 4565 LEU A C     1 
ATOM   22962 O  O     . LEU A 1 4565 ? 156.775 169.076 211.464 1.00 5.07  ? 4565 LEU A O     1 
ATOM   22963 C  CB    . LEU A 1 4565 ? 155.268 168.504 208.897 1.00 4.27  ? 4565 LEU A CB    1 
ATOM   22964 C  CG    . LEU A 1 4565 ? 153.985 169.314 209.085 1.00 5.89  ? 4565 LEU A CG    1 
ATOM   22965 C  CD1   . LEU A 1 4565 ? 153.989 170.557 208.215 1.00 3.37  ? 4565 LEU A CD1   1 
ATOM   22966 C  CD2   . LEU A 1 4565 ? 152.781 168.449 208.787 1.00 8.24  ? 4565 LEU A CD2   1 
ATOM   22967 N  N     . GLN A 1 4566 ? 156.741 171.144 210.568 1.00 4.90  ? 4566 GLN A N     1 
ATOM   22968 C  CA    . GLN A 1 4566 ? 156.920 171.842 211.835 1.00 6.22  ? 4566 GLN A CA    1 
ATOM   22969 C  C     . GLN A 1 4566 ? 155.578 172.379 212.316 1.00 7.51  ? 4566 GLN A C     1 
ATOM   22970 O  O     . GLN A 1 4566 ? 154.935 173.171 211.618 1.00 8.42  ? 4566 GLN A O     1 
ATOM   22971 C  CB    . GLN A 1 4566 ? 157.928 172.981 211.692 1.00 7.08  ? 4566 GLN A CB    1 
ATOM   22972 C  CG    . GLN A 1 4566 ? 159.186 172.620 210.928 1.00 5.82  ? 4566 GLN A CG    1 
ATOM   22973 C  CD    . GLN A 1 4566 ? 160.041 171.595 211.648 1.00 9.36  ? 4566 GLN A CD    1 
ATOM   22974 O  OE1   . GLN A 1 4566 ? 160.272 170.497 211.142 1.00 8.66  ? 4566 GLN A OE1   1 
ATOM   22975 N  NE2   . GLN A 1 4566 ? 160.525 171.953 212.830 1.00 9.85  ? 4566 GLN A NE2   1 
ATOM   22976 N  N     . GLY A 1 4567 ? 155.164 171.956 213.509 1.00 7.13  ? 4567 GLY A N     1 
ATOM   22977 C  CA    . GLY A 1 4567 ? 153.967 172.468 214.140 1.00 6.22  ? 4567 GLY A CA    1 
ATOM   22978 C  C     . GLY A 1 4567 ? 152.662 171.851 213.685 1.00 6.59  ? 4567 GLY A C     1 
ATOM   22979 O  O     . GLY A 1 4567 ? 151.599 172.319 214.109 1.00 7.97  ? 4567 GLY A O     1 
ATOM   22980 N  N     . ALA A 1 4568 ? 152.701 170.820 212.845 1.00 9.80  ? 4568 ALA A N     1 
ATOM   22981 C  CA    . ALA A 1 4568 ? 151.482 170.189 212.363 1.00 6.66  ? 4568 ALA A CA    1 
ATOM   22982 C  C     . ALA A 1 4568 ? 151.762 168.723 212.072 1.00 5.92  ? 4568 ALA A C     1 
ATOM   22983 O  O     . ALA A 1 4568 ? 152.911 168.277 212.059 1.00 10.06 ? 4568 ALA A O     1 
ATOM   22984 C  CB    . ALA A 1 4568 ? 150.940 170.896 211.117 1.00 7.60  ? 4568 ALA A CB    1 
ATOM   22985 N  N     . THR A 1 4569 ? 150.688 167.971 211.845 1.00 8.69  ? 4569 THR A N     1 
ATOM   22986 C  CA    . THR A 1 4569 ? 150.769 166.584 211.412 1.00 10.98 ? 4569 THR A CA    1 
ATOM   22987 C  C     . THR A 1 4569 ? 150.017 166.421 210.101 1.00 10.28 ? 4569 THR A C     1 
ATOM   22988 O  O     . THR A 1 4569 ? 148.991 167.070 209.877 1.00 14.68 ? 4569 THR A O     1 
ATOM   22989 C  CB    . THR A 1 4569 ? 150.189 165.626 212.460 1.00 11.64 ? 4569 THR A CB    1 
ATOM   22990 O  OG1   . THR A 1 4569 ? 148.905 166.100 212.886 1.00 14.40 ? 4569 THR A OG1   1 
ATOM   22991 C  CG2   . THR A 1 4569 ? 151.115 165.521 213.659 1.00 11.46 ? 4569 THR A CG2   1 
ATOM   22992 N  N     . CYS A 1 4570 ? 150.531 165.554 209.236 1.00 18.10 ? 4570 CYS A N     1 
ATOM   22993 C  CA    . CYS A 1 4570 ? 149.913 165.270 207.947 1.00 17.47 ? 4570 CYS A CA    1 
ATOM   22994 C  C     . CYS A 1 4570 ? 149.265 163.896 208.006 1.00 14.74 ? 4570 CYS A C     1 
ATOM   22995 O  O     . CYS A 1 4570 ? 149.936 162.901 208.298 1.00 20.60 ? 4570 CYS A O     1 
ATOM   22996 C  CB    . CYS A 1 4570 ? 150.941 165.334 206.819 1.00 10.54 ? 4570 CYS A CB    1 
ATOM   22997 S  SG    . CYS A 1 4570 ? 150.222 165.281 205.168 1.00 33.37 ? 4570 CYS A SG    1 
ATOM   22998 N  N     . ASN A 1 4571 ? 147.964 163.844 207.730 1.00 15.13 ? 4571 ASN A N     1 
ATOM   22999 C  CA    . ASN A 1 4571 ? 147.215 162.594 207.704 1.00 16.16 ? 4571 ASN A CA    1 
ATOM   23000 C  C     . ASN A 1 4571 ? 146.281 162.617 206.504 1.00 20.44 ? 4571 ASN A C     1 
ATOM   23001 O  O     . ASN A 1 4571 ? 145.348 163.424 206.459 1.00 18.84 ? 4571 ASN A O     1 
ATOM   23002 C  CB    . ASN A 1 4571 ? 146.428 162.393 209.000 1.00 14.45 ? 4571 ASN A CB    1 
ATOM   23003 C  CG    . ASN A 1 4571 ? 147.183 161.563 210.016 1.00 23.18 ? 4571 ASN A CG    1 
ATOM   23004 O  OD1   . ASN A 1 4571 ? 147.025 160.344 210.081 1.00 30.35 ? 4571 ASN A OD1   1 
ATOM   23005 N  ND2   . ASN A 1 4571 ? 148.015 162.220 210.817 1.00 20.96 ? 4571 ASN A ND2   1 
ATOM   23006 N  N     . ASN A 1 4572 ? 146.534 161.728 205.542 1.00 20.90 ? 4572 ASN A N     1 
ATOM   23007 C  CA    . ASN A 1 4572 ? 145.729 161.627 204.323 1.00 22.47 ? 4572 ASN A CA    1 
ATOM   23008 C  C     . ASN A 1 4572 ? 145.685 162.957 203.575 1.00 22.56 ? 4572 ASN A C     1 
ATOM   23009 O  O     . ASN A 1 4572 ? 144.633 163.385 203.097 1.00 23.75 ? 4572 ASN A O     1 
ATOM   23010 C  CB    . ASN A 1 4572 ? 144.315 161.132 204.634 1.00 21.79 ? 4572 ASN A CB    1 
ATOM   23011 C  CG    . ASN A 1 4572 ? 144.309 159.947 205.571 1.00 24.24 ? 4572 ASN A CG    1 
ATOM   23012 O  OD1   . ASN A 1 4572 ? 144.809 158.874 205.237 1.00 29.48 ? 4572 ASN A OD1   1 
ATOM   23013 N  ND2   . ASN A 1 4572 ? 143.748 160.137 206.760 1.00 27.18 ? 4572 ASN A ND2   1 
ATOM   23014 N  N     . ASN A 1 4573 ? 146.842 163.620 203.488 1.00 19.32 ? 4573 ASN A N     1 
ATOM   23015 C  CA    . ASN A 1 4573 ? 146.980 164.905 202.802 1.00 16.57 ? 4573 ASN A CA    1 
ATOM   23016 C  C     . ASN A 1 4573 ? 146.110 165.986 203.428 1.00 18.73 ? 4573 ASN A C     1 
ATOM   23017 O  O     . ASN A 1 4573 ? 145.664 166.910 202.744 1.00 25.65 ? 4573 ASN A O     1 
ATOM   23018 C  CB    . ASN A 1 4573 ? 146.670 164.777 201.310 1.00 18.33 ? 4573 ASN A CB    1 
ATOM   23019 C  CG    . ASN A 1 4573 ? 147.637 163.878 200.599 1.00 20.58 ? 4573 ASN A CG    1 
ATOM   23020 O  OD1   . ASN A 1 4573 ? 148.826 164.176 200.492 1.00 18.32 ? 4573 ASN A OD1   1 
ATOM   23021 N  ND2   . ASN A 1 4573 ? 147.133 162.765 200.101 1.00 25.21 ? 4573 ASN A ND2   1 
ATOM   23022 N  N     . LYS A 1 4574 ? 145.865 165.886 204.731 1.00 19.08 ? 4574 LYS A N     1 
ATOM   23023 C  CA    . LYS A 1 4574 ? 145.033 166.845 205.449 1.00 14.62 ? 4574 LYS A CA    1 
ATOM   23024 C  C     . LYS A 1 4574 ? 145.756 167.243 206.726 1.00 18.81 ? 4574 LYS A C     1 
ATOM   23025 O  O     . LYS A 1 4574 ? 145.830 166.457 207.674 1.00 19.25 ? 4574 LYS A O     1 
ATOM   23026 C  CB    . LYS A 1 4574 ? 143.653 166.261 205.747 1.00 16.00 ? 4574 LYS A CB    1 
ATOM   23027 C  CG    . LYS A 1 4574 ? 142.801 166.056 204.504 1.00 21.50 ? 4574 LYS A CG    1 
ATOM   23028 C  CD    . LYS A 1 4574 ? 141.467 165.407 204.832 1.00 24.77 ? 4574 LYS A CD    1 
ATOM   23029 C  CE    . LYS A 1 4574 ? 140.562 166.367 205.582 1.00 27.10 ? 4574 LYS A CE    1 
ATOM   23030 N  NZ    . LYS A 1 4574 ? 140.128 167.503 204.726 1.00 26.44 ? 4574 LYS A NZ    1 
ATOM   23031 N  N     . LEU A 1 4575 ? 146.289 168.463 206.745 1.00 21.05 ? 4575 LEU A N     1 
ATOM   23032 C  CA    . LEU A 1 4575 ? 147.054 168.941 207.884 1.00 10.94 ? 4575 LEU A CA    1 
ATOM   23033 C  C     . LEU A 1 4575 ? 146.141 169.278 209.052 1.00 13.84 ? 4575 LEU A C     1 
ATOM   23034 O  O     . LEU A 1 4575 ? 145.051 169.827 208.871 1.00 20.21 ? 4575 LEU A O     1 
ATOM   23035 C  CB    . LEU A 1 4575 ? 147.864 170.181 207.511 1.00 11.97 ? 4575 LEU A CB    1 
ATOM   23036 C  CG    . LEU A 1 4575 ? 148.974 170.054 206.476 1.00 10.15 ? 4575 LEU A CG    1 
ATOM   23037 C  CD1   . LEU A 1 4575 ? 149.720 171.366 206.390 1.00 7.09  ? 4575 LEU A CD1   1 
ATOM   23038 C  CD2   . LEU A 1 4575 ? 149.911 168.907 206.788 1.00 11.18 ? 4575 LEU A CD2   1 
ATOM   23039 N  N     . SER A 1 4576 ? 146.597 168.950 210.255 1.00 15.01 ? 4576 SER A N     1 
ATOM   23040 C  CA    . SER A 1 4576 ? 145.959 169.386 211.486 1.00 14.28 ? 4576 SER A CA    1 
ATOM   23041 C  C     . SER A 1 4576 ? 147.031 169.960 212.396 1.00 10.65 ? 4576 SER A C     1 
ATOM   23042 O  O     . SER A 1 4576 ? 148.182 169.518 212.363 1.00 11.95 ? 4576 SER A O     1 
ATOM   23043 C  CB    . SER A 1 4576 ? 145.224 168.238 212.189 1.00 16.88 ? 4576 SER A CB    1 
ATOM   23044 O  OG    . SER A 1 4576 ? 146.133 167.254 212.648 1.00 26.28 ? 4576 SER A OG    1 
ATOM   23045 N  N     . LEU A 1 4577 ? 146.655 170.954 213.195 1.00 13.11 ? 4577 LEU A N     1 
ATOM   23046 C  CA    . LEU A 1 4577 ? 147.616 171.577 214.094 1.00 8.77  ? 4577 LEU A CA    1 
ATOM   23047 C  C     . LEU A 1 4577 ? 148.072 170.585 215.152 1.00 10.51 ? 4577 LEU A C     1 
ATOM   23048 O  O     . LEU A 1 4577 ? 147.284 169.789 215.669 1.00 15.15 ? 4577 LEU A O     1 
ATOM   23049 C  CB    . LEU A 1 4577 ? 147.007 172.816 214.749 1.00 6.96  ? 4577 LEU A CB    1 
ATOM   23050 C  CG    . LEU A 1 4577 ? 146.958 174.052 213.847 1.00 8.60  ? 4577 LEU A CG    1 
ATOM   23051 C  CD1   . LEU A 1 4577 ? 146.222 175.195 214.522 1.00 11.12 ? 4577 LEU A CD1   1 
ATOM   23052 C  CD2   . LEU A 1 4577 ? 148.359 174.474 213.442 1.00 5.75  ? 4577 LEU A CD2   1 
ATOM   23053 N  N     . SER A 1 4578 ? 149.361 170.636 215.471 1.00 5.78  ? 4578 SER A N     1 
ATOM   23054 C  CA    . SER A 1 4578 ? 149.975 169.718 216.415 1.00 7.11  ? 4578 SER A CA    1 
ATOM   23055 C  C     . SER A 1 4578 ? 150.792 170.498 217.434 1.00 11.32 ? 4578 SER A C     1 
ATOM   23056 O  O     . SER A 1 4578 ? 151.318 171.575 217.138 1.00 14.81 ? 4578 SER A O     1 
ATOM   23057 C  CB    . SER A 1 4578 ? 150.872 168.700 215.699 1.00 13.38 ? 4578 SER A CB    1 
ATOM   23058 O  OG    . SER A 1 4578 ? 151.685 167.991 216.614 1.00 13.95 ? 4578 SER A OG    1 
ATOM   23059 N  N     . ASN A 1 4579 ? 150.893 169.945 218.637 1.00 11.65 ? 4579 ASN A N     1 
ATOM   23060 C  CA    . ASN A 1 4579 ? 151.727 170.518 219.681 1.00 9.22  ? 4579 ASN A CA    1 
ATOM   23061 C  C     . ASN A 1 4579 ? 153.140 169.953 219.679 1.00 9.84  ? 4579 ASN A C     1 
ATOM   23062 O  O     . ASN A 1 4579 ? 153.935 170.311 220.553 1.00 15.15 ? 4579 ASN A O     1 
ATOM   23063 C  CB    . ASN A 1 4579 ? 151.078 170.307 221.053 1.00 11.85 ? 4579 ASN A CB    1 
ATOM   23064 C  CG    . ASN A 1 4579 ? 149.872 171.203 221.266 1.00 19.62 ? 4579 ASN A CG    1 
ATOM   23065 O  OD1   . ASN A 1 4579 ? 148.771 170.728 221.544 1.00 21.00 ? 4579 ASN A OD1   1 
ATOM   23066 N  ND2   . ASN A 1 4579 ? 150.075 172.508 221.131 1.00 13.52 ? 4579 ASN A ND2   1 
ATOM   23067 N  N     . ALA A 1 4580 ? 153.467 169.085 218.726 1.00 11.25 ? 4580 ALA A N     1 
ATOM   23068 C  CA    . ALA A 1 4580 ? 154.819 168.572 218.584 1.00 6.96  ? 4580 ALA A CA    1 
ATOM   23069 C  C     . ALA A 1 4580 ? 155.666 169.526 217.747 1.00 10.00 ? 4580 ALA A C     1 
ATOM   23070 O  O     . ALA A 1 4580 ? 155.154 170.390 217.032 1.00 16.04 ? 4580 ALA A O     1 
ATOM   23071 C  CB    . ALA A 1 4580 ? 154.806 167.181 217.949 1.00 6.75  ? 4580 ALA A CB    1 
ATOM   23072 N  N     . ILE A 1 4581 ? 156.984 169.355 217.840 1.00 11.38 ? 4581 ILE A N     1 
ATOM   23073 C  CA    . ILE A 1 4581 ? 157.901 170.270 217.168 1.00 8.80  ? 4581 ILE A CA    1 
ATOM   23074 C  C     . ILE A 1 4581 ? 158.031 169.919 215.692 1.00 11.19 ? 4581 ILE A C     1 
ATOM   23075 O  O     . ILE A 1 4581 ? 157.694 170.723 214.816 1.00 11.87 ? 4581 ILE A O     1 
ATOM   23076 C  CB    . ILE A 1 4581 ? 159.271 170.265 217.870 1.00 11.75 ? 4581 ILE A CB    1 
ATOM   23077 C  CG1   . ILE A 1 4581 ? 159.119 170.680 219.334 1.00 14.40 ? 4581 ILE A CG1   1 
ATOM   23078 C  CG2   . ILE A 1 4581 ? 160.237 171.195 217.158 1.00 10.63 ? 4581 ILE A CG2   1 
ATOM   23079 C  CD1   . ILE A 1 4581 ? 158.565 172.068 219.518 1.00 10.54 ? 4581 ILE A CD1   1 
ATOM   23080 N  N     . SER A 1 4582 ? 158.518 168.720 215.391 1.00 12.00 ? 4582 SER A N     1 
ATOM   23081 C  CA    . SER A 1 4582 ? 158.739 168.288 214.020 1.00 9.36  ? 4582 SER A CA    1 
ATOM   23082 C  C     . SER A 1 4582 ? 158.064 166.946 213.800 1.00 10.88 ? 4582 SER A C     1 
ATOM   23083 O  O     . SER A 1 4582 ? 158.200 166.036 214.623 1.00 15.86 ? 4582 SER A O     1 
ATOM   23084 C  CB    . SER A 1 4582 ? 160.232 168.184 213.700 1.00 10.70 ? 4582 SER A CB    1 
ATOM   23085 O  OG    . SER A 1 4582 ? 160.863 169.446 213.786 1.00 18.73 ? 4582 SER A OG    1 
ATOM   23086 N  N     . THR A 1 4583 ? 157.335 166.831 212.695 1.00 8.75  ? 4583 THR A N     1 
ATOM   23087 C  CA    . THR A 1 4583 ? 156.717 165.581 212.277 1.00 8.18  ? 4583 THR A CA    1 
ATOM   23088 C  C     . THR A 1 4583 ? 157.343 165.165 210.955 1.00 13.32 ? 4583 THR A C     1 
ATOM   23089 O  O     . THR A 1 4583 ? 157.333 165.935 209.991 1.00 13.72 ? 4583 THR A O     1 
ATOM   23090 C  CB    . THR A 1 4583 ? 155.201 165.732 212.136 1.00 12.15 ? 4583 THR A CB    1 
ATOM   23091 O  OG1   . THR A 1 4583 ? 154.599 165.782 213.436 1.00 24.50 ? 4583 THR A OG1   1 
ATOM   23092 C  CG2   . THR A 1 4583 ? 154.619 164.561 211.362 1.00 10.56 ? 4583 THR A CG2   1 
ATOM   23093 N  N     . ALA A 1 4584 ? 157.885 163.952 210.912 1.00 20.92 ? 4584 ALA A N     1 
ATOM   23094 C  CA    . ALA A 1 4584 ? 158.535 163.472 209.702 1.00 14.98 ? 4584 ALA A CA    1 
ATOM   23095 C  C     . ALA A 1 4584 ? 157.498 163.114 208.645 1.00 17.43 ? 4584 ALA A C     1 
ATOM   23096 O  O     . ALA A 1 4584 ? 156.509 162.436 208.934 1.00 16.93 ? 4584 ALA A O     1 
ATOM   23097 C  CB    . ALA A 1 4584 ? 159.412 162.264 210.015 1.00 17.12 ? 4584 ALA A CB    1 
ATOM   23098 N  N     . LEU A 1 4585 ? 157.722 163.585 207.418 1.00 14.55 ? 4585 LEU A N     1 
ATOM   23099 C  CA    . LEU A 1 4585 ? 156.912 163.178 206.281 1.00 13.78 ? 4585 LEU A CA    1 
ATOM   23100 C  C     . LEU A 1 4585 ? 157.607 162.027 205.579 1.00 17.71 ? 4585 LEU A C     1 
ATOM   23101 O  O     . LEU A 1 4585 ? 158.734 162.207 205.092 1.00 24.08 ? 4585 LEU A O     1 
ATOM   23102 C  CB    . LEU A 1 4585 ? 156.706 164.340 205.315 1.00 13.87 ? 4585 LEU A CB    1 
ATOM   23103 C  CG    . LEU A 1 4585 ? 156.087 165.619 205.883 1.00 11.40 ? 4585 LEU A CG    1 
ATOM   23104 C  CD1   . LEU A 1 4585 ? 156.128 166.732 204.851 1.00 7.42  ? 4585 LEU A CD1   1 
ATOM   23105 C  CD2   . LEU A 1 4585 ? 154.665 165.371 206.344 1.00 12.79 ? 4585 LEU A CD2   1 
ATOM   23106 N  N     . PRO A 1 4586 ? 157.001 160.838 205.518 1.00 19.78 ? 4586 PRO A N     1 
ATOM   23107 C  CA    . PRO A 1 4586 ? 157.710 159.668 204.973 1.00 15.29 ? 4586 PRO A CA    1 
ATOM   23108 C  C     . PRO A 1 4586 ? 158.176 159.859 203.539 1.00 16.19 ? 4586 PRO A C     1 
ATOM   23109 O  O     . PRO A 1 4586 ? 159.372 159.757 203.250 1.00 24.00 ? 4586 PRO A O     1 
ATOM   23110 C  CB    . PRO A 1 4586 ? 156.665 158.550 205.072 1.00 20.11 ? 4586 PRO A CB    1 
ATOM   23111 C  CG    . PRO A 1 4586 ? 155.722 159.004 206.138 1.00 22.44 ? 4586 PRO A CG    1 
ATOM   23112 C  CD    . PRO A 1 4586 ? 155.662 160.493 206.021 1.00 15.93 ? 4586 PRO A CD    1 
ATOM   23113 N  N     . LEU A 1 4587 ? 157.242 160.141 202.637 1.00 19.06 ? 4587 LEU A N     1 
ATOM   23114 C  CA    . LEU A 1 4587 ? 157.570 160.342 201.231 1.00 13.47 ? 4587 LEU A CA    1 
ATOM   23115 C  C     . LEU A 1 4587 ? 156.578 161.328 200.640 1.00 17.18 ? 4587 LEU A C     1 
ATOM   23116 O  O     . LEU A 1 4587 ? 155.372 161.064 200.631 1.00 18.70 ? 4587 LEU A O     1 
ATOM   23117 C  CB    . LEU A 1 4587 ? 157.539 159.022 200.460 1.00 17.94 ? 4587 LEU A CB    1 
ATOM   23118 C  CG    . LEU A 1 4587 ? 157.875 159.107 198.972 1.00 16.23 ? 4587 LEU A CG    1 
ATOM   23119 C  CD1   . LEU A 1 4587 ? 159.375 159.126 198.757 1.00 15.41 ? 4587 LEU A CD1   1 
ATOM   23120 C  CD2   . LEU A 1 4587 ? 157.234 157.953 198.225 1.00 20.78 ? 4587 LEU A CD2   1 
ATOM   23121 N  N     . THR A 1 4588 ? 157.085 162.453 200.149 1.00 16.07 ? 4588 THR A N     1 
ATOM   23122 C  CA    . THR A 1 4588 ? 156.258 163.502 199.570 1.00 17.10 ? 4588 THR A CA    1 
ATOM   23123 C  C     . THR A 1 4588 ? 156.372 163.440 198.052 1.00 18.07 ? 4588 THR A C     1 
ATOM   23124 O  O     . THR A 1 4588 ? 157.478 163.524 197.505 1.00 15.74 ? 4588 THR A O     1 
ATOM   23125 C  CB    . THR A 1 4588 ? 156.687 164.875 200.089 1.00 15.52 ? 4588 THR A CB    1 
ATOM   23126 O  OG1   . THR A 1 4588 ? 156.548 164.912 201.514 1.00 21.06 ? 4588 THR A OG1   1 
ATOM   23127 C  CG2   . THR A 1 4588 ? 155.830 165.967 199.482 1.00 11.40 ? 4588 THR A CG2   1 
ATOM   23128 N  N     . GLN A 1 4589 ? 155.235 163.292 197.377 1.00 14.56 ? 4589 GLN A N     1 
ATOM   23129 C  CA    . GLN A 1 4589 ? 155.196 163.269 195.919 1.00 11.62 ? 4589 GLN A CA    1 
ATOM   23130 C  C     . GLN A 1 4589 ? 154.944 164.683 195.409 1.00 16.51 ? 4589 GLN A C     1 
ATOM   23131 O  O     . GLN A 1 4589 ? 153.883 165.261 195.659 1.00 27.24 ? 4589 GLN A O     1 
ATOM   23132 C  CB    . GLN A 1 4589 ? 154.126 162.309 195.406 1.00 14.39 ? 4589 GLN A CB    1 
ATOM   23133 C  CG    . GLN A 1 4589 ? 153.993 161.015 196.182 1.00 15.55 ? 4589 GLN A CG    1 
ATOM   23134 C  CD    . GLN A 1 4589 ? 153.519 159.876 195.304 1.00 19.79 ? 4589 GLN A CD    1 
ATOM   23135 O  OE1   . GLN A 1 4589 ? 153.128 160.086 194.157 1.00 28.18 ? 4589 GLN A OE1   1 
ATOM   23136 N  NE2   . GLN A 1 4589 ? 153.554 158.661 195.836 1.00 27.98 ? 4589 GLN A NE2   1 
ATOM   23137 N  N     . LEU A 1 4590 ? 155.919 165.233 194.694 1.00 11.66 ? 4590 LEU A N     1 
ATOM   23138 C  CA    . LEU A 1 4590 ? 155.783 166.542 194.069 1.00 11.93 ? 4590 LEU A CA    1 
ATOM   23139 C  C     . LEU A 1 4590 ? 155.289 166.339 192.643 1.00 18.63 ? 4590 LEU A C     1 
ATOM   23140 O  O     . LEU A 1 4590 ? 156.043 165.884 191.776 1.00 25.07 ? 4590 LEU A O     1 
ATOM   23141 C  CB    . LEU A 1 4590 ? 157.109 167.295 194.096 1.00 14.33 ? 4590 LEU A CB    1 
ATOM   23142 C  CG    . LEU A 1 4590 ? 157.732 167.458 195.482 1.00 14.93 ? 4590 LEU A CG    1 
ATOM   23143 C  CD1   . LEU A 1 4590 ? 158.920 168.391 195.416 1.00 16.82 ? 4590 LEU A CD1   1 
ATOM   23144 C  CD2   . LEU A 1 4590 ? 156.705 167.970 196.474 1.00 10.69 ? 4590 LEU A CD2   1 
ATOM   23145 N  N     . ARG A 1 4591 ? 154.028 166.674 192.399 1.00 19.65 ? 4591 ARG A N     1 
ATOM   23146 C  CA    . ARG A 1 4591 ? 153.388 166.448 191.112 1.00 18.99 ? 4591 ARG A CA    1 
ATOM   23147 C  C     . ARG A 1 4591 ? 153.117 167.784 190.436 1.00 21.36 ? 4591 ARG A C     1 
ATOM   23148 O  O     . ARG A 1 4591 ? 152.537 168.688 191.046 1.00 22.17 ? 4591 ARG A O     1 
ATOM   23149 C  CB    . ARG A 1 4591 ? 152.089 165.659 191.282 1.00 17.13 ? 4591 ARG A CB    1 
ATOM   23150 C  CG    . ARG A 1 4591 ? 151.112 165.809 190.135 1.00 20.00 ? 4591 ARG A CG    1 
ATOM   23151 C  CD    . ARG A 1 4591 ? 149.802 165.102 190.435 1.00 23.41 ? 4591 ARG A CD    1 
ATOM   23152 N  NE    . ARG A 1 4591 ? 149.748 163.773 189.840 1.00 28.04 ? 4591 ARG A NE    1 
ATOM   23153 C  CZ    . ARG A 1 4591 ? 149.775 162.642 190.531 1.00 33.32 ? 4591 ARG A CZ    1 
ATOM   23154 N  NH1   . ARG A 1 4591 ? 149.859 162.642 191.852 1.00 23.37 ? 4591 ARG A NH1   1 
ATOM   23155 N  NH2   . ARG A 1 4591 ? 149.718 161.483 189.882 1.00 28.54 ? 4591 ARG A NH2   1 
ATOM   23156 N  N     . TRP A 1 4592 ? 153.537 167.904 189.181 1.00 19.45 ? 4592 TRP A N     1 
ATOM   23157 C  CA    . TRP A 1 4592 ? 153.319 169.105 188.387 1.00 14.44 ? 4592 TRP A CA    1 
ATOM   23158 C  C     . TRP A 1 4592 ? 152.144 168.867 187.447 1.00 20.44 ? 4592 TRP A C     1 
ATOM   23159 O  O     . TRP A 1 4592 ? 152.151 167.908 186.668 1.00 23.02 ? 4592 TRP A O     1 
ATOM   23160 C  CB    . TRP A 1 4592 ? 154.580 169.470 187.605 1.00 17.84 ? 4592 TRP A CB    1 
ATOM   23161 C  CG    . TRP A 1 4592 ? 155.712 169.884 188.487 1.00 18.91 ? 4592 TRP A CG    1 
ATOM   23162 C  CD1   . TRP A 1 4592 ? 156.775 169.121 188.869 1.00 15.19 ? 4592 TRP A CD1   1 
ATOM   23163 C  CD2   . TRP A 1 4592 ? 155.886 171.159 189.116 1.00 18.91 ? 4592 TRP A CD2   1 
ATOM   23164 N  NE1   . TRP A 1 4592 ? 157.603 169.842 189.689 1.00 16.09 ? 4592 TRP A NE1   1 
ATOM   23165 C  CE2   . TRP A 1 4592 ? 157.081 171.097 189.859 1.00 18.66 ? 4592 TRP A CE2   1 
ATOM   23166 C  CE3   . TRP A 1 4592 ? 155.149 172.346 189.121 1.00 18.10 ? 4592 TRP A CE3   1 
ATOM   23167 C  CZ2   . TRP A 1 4592 ? 157.555 172.176 190.599 1.00 13.61 ? 4592 TRP A CZ2   1 
ATOM   23168 C  CZ3   . TRP A 1 4592 ? 155.622 173.415 189.854 1.00 19.08 ? 4592 TRP A CZ3   1 
ATOM   23169 C  CH2   . TRP A 1 4592 ? 156.813 173.324 190.582 1.00 15.01 ? 4592 TRP A CH2   1 
ATOM   23170 N  N     . VAL A 1 4593 ? 151.138 169.737 187.528 1.00 19.16 ? 4593 VAL A N     1 
ATOM   23171 C  CA    . VAL A 1 4593 ? 149.934 169.621 186.719 1.00 20.06 ? 4593 VAL A CA    1 
ATOM   23172 C  C     . VAL A 1 4593 ? 149.668 170.950 186.031 1.00 27.05 ? 4593 VAL A C     1 
ATOM   23173 O  O     . VAL A 1 4593 ? 150.173 172.000 186.434 1.00 25.52 ? 4593 VAL A O     1 
ATOM   23174 C  CB    . VAL A 1 4593 ? 148.700 169.198 187.546 1.00 21.79 ? 4593 VAL A CB    1 
ATOM   23175 C  CG1   . VAL A 1 4593 ? 148.951 167.881 188.249 1.00 19.52 ? 4593 VAL A CG1   1 
ATOM   23176 C  CG2   . VAL A 1 4593 ? 148.334 170.282 188.546 1.00 18.01 ? 4593 VAL A CG2   1 
ATOM   23177 N  N     . LYS A 1 4594 ? 148.861 170.888 184.974 1.00 28.68 ? 4594 LYS A N     1 
ATOM   23178 C  CA    . LYS A 1 4594 ? 148.457 172.097 184.271 1.00 28.06 ? 4594 LYS A CA    1 
ATOM   23179 C  C     . LYS A 1 4594 ? 147.649 172.991 185.203 1.00 27.38 ? 4594 LYS A C     1 
ATOM   23180 O  O     . LYS A 1 4594 ? 146.684 172.543 185.831 1.00 28.24 ? 4594 LYS A O     1 
ATOM   23181 C  CB    . LYS A 1 4594 ? 147.638 171.734 183.033 1.00 30.82 ? 4594 LYS A CB    1 
ATOM   23182 C  CG    . LYS A 1 4594 ? 147.399 172.887 182.073 1.00 30.02 ? 4594 LYS A CG    1 
ATOM   23183 C  CD    . LYS A 1 4594 ? 148.709 173.471 181.574 1.00 26.88 ? 4594 LYS A CD    1 
ATOM   23184 C  CE    . LYS A 1 4594 ? 148.482 174.788 180.851 1.00 34.15 ? 4594 LYS A CE    1 
ATOM   23185 N  NZ    . LYS A 1 4594 ? 147.962 175.838 181.769 1.00 34.24 ? 4594 LYS A NZ    1 
ATOM   23186 N  N     . GLN A 1 4595 ? 148.047 174.257 185.293 1.00 28.57 ? 4595 GLN A N     1 
ATOM   23187 C  CA    . GLN A 1 4595 ? 147.372 175.186 186.188 1.00 28.30 ? 4595 GLN A CA    1 
ATOM   23188 C  C     . GLN A 1 4595 ? 145.970 175.495 185.679 1.00 33.38 ? 4595 GLN A C     1 
ATOM   23189 O  O     . GLN A 1 4595 ? 145.751 175.674 184.478 1.00 37.47 ? 4595 GLN A O     1 
ATOM   23190 C  CB    . GLN A 1 4595 ? 148.181 176.475 186.325 1.00 26.64 ? 4595 GLN A CB    1 
ATOM   23191 C  CG    . GLN A 1 4595 ? 147.690 177.400 187.426 1.00 27.43 ? 4595 GLN A CG    1 
ATOM   23192 C  CD    . GLN A 1 4595 ? 148.536 178.650 187.559 1.00 36.84 ? 4595 GLN A CD    1 
ATOM   23193 O  OE1   . GLN A 1 4595 ? 149.495 178.846 186.813 1.00 38.25 ? 4595 GLN A OE1   1 
ATOM   23194 N  NE2   . GLN A 1 4595 ? 148.184 179.505 188.511 1.00 36.03 ? 4595 GLN A NE2   1 
ATOM   23195 N  N     . THR A 1 4596 ? 145.013 175.553 186.606 1.00 32.45 ? 4596 THR A N     1 
ATOM   23196 C  CA    . THR A 1 4596 ? 143.620 175.823 186.274 1.00 32.69 ? 4596 THR A CA    1 
ATOM   23197 C  C     . THR A 1 4596 ? 143.091 177.087 186.941 1.00 36.05 ? 4596 THR A C     1 
ATOM   23198 O  O     . THR A 1 4596 ? 141.878 177.321 186.909 1.00 39.19 ? 4596 THR A O     1 
ATOM   23199 C  CB    . THR A 1 4596 ? 142.740 174.630 186.657 1.00 33.41 ? 4596 THR A CB    1 
ATOM   23200 O  OG1   . THR A 1 4596 ? 142.812 174.415 188.072 1.00 40.32 ? 4596 THR A OG1   1 
ATOM   23201 C  CG2   . THR A 1 4596 ? 143.200 173.373 185.934 1.00 32.84 ? 4596 THR A CG2   1 
ATOM   23202 N  N     . ASN A 1 4597 ? 143.967 177.871 187.581 1.00 30.67 ? 4597 ASN A N     1 
ATOM   23203 C  CA    . ASN A 1 4597 ? 143.698 179.181 188.179 1.00 34.04 ? 4597 ASN A CA    1 
ATOM   23204 C  C     . ASN A 1 4597 ? 142.306 179.313 188.794 1.00 36.49 ? 4597 ASN A C     1 
ATOM   23205 O  O     . ASN A 1 4597 ? 141.610 180.308 188.570 1.00 37.77 ? 4597 ASN A O     1 
ATOM   23206 C  CB    . ASN A 1 4597 ? 143.969 180.305 187.159 1.00 31.16 ? 4597 ASN A CB    1 
ATOM   23207 C  CG    . ASN A 1 4597 ? 143.051 180.275 185.936 1.00 37.75 ? 4597 ASN A CG    1 
ATOM   23208 O  OD1   . ASN A 1 4597 ? 141.971 179.690 185.946 1.00 34.84 ? 4597 ASN A OD1   1 
ATOM   23209 N  ND2   . ASN A 1 4597 ? 143.498 180.920 184.866 1.00 36.24 ? 4597 ASN A ND2   1 
ATOM   23210 N  N     . THR A 1 4598 ? 141.905 178.325 189.597 1.00 37.81 ? 4598 THR A N     1 
ATOM   23211 C  CA    . THR A 1 4598 ? 140.624 178.341 190.287 1.00 33.88 ? 4598 THR A CA    1 
ATOM   23212 C  C     . THR A 1 4598 ? 140.734 178.882 191.709 1.00 36.87 ? 4598 THR A C     1 
ATOM   23213 O  O     . THR A 1 4598 ? 139.904 178.542 192.559 1.00 38.88 ? 4598 THR A O     1 
ATOM   23214 C  CB    . THR A 1 4598 ? 140.011 176.940 190.307 1.00 36.69 ? 4598 THR A CB    1 
ATOM   23215 O  OG1   . THR A 1 4598 ? 140.999 175.988 190.719 1.00 43.12 ? 4598 THR A OG1   1 
ATOM   23216 C  CG2   . THR A 1 4598 ? 139.489 176.563 188.927 1.00 29.89 ? 4598 THR A CG2   1 
ATOM   23217 N  N     . GLU A 1 4599 ? 141.752 179.704 191.981 1.00 37.50 ? 4599 GLU A N     1 
ATOM   23218 C  CA    . GLU A 1 4599 ? 141.969 180.303 193.296 1.00 31.28 ? 4599 GLU A CA    1 
ATOM   23219 C  C     . GLU A 1 4599 ? 142.149 179.238 194.370 1.00 32.71 ? 4599 GLU A C     1 
ATOM   23220 O  O     . GLU A 1 4599 ? 142.430 178.075 194.062 1.00 37.17 ? 4599 GLU A O     1 
ATOM   23221 C  CB    . GLU A 1 4599 ? 140.816 181.242 193.662 1.00 31.67 ? 4599 GLU A CB    1 
ATOM   23222 C  CG    . GLU A 1 4599 ? 140.573 182.352 192.654 1.00 33.90 ? 4599 GLU A CG    1 
ATOM   23223 C  CD    . GLU A 1 4599 ? 139.376 183.210 193.014 1.00 36.90 ? 4599 GLU A CD    1 
ATOM   23224 O  OE1   . GLU A 1 4599 ? 139.391 183.830 194.097 1.00 32.49 ? 4599 GLU A OE1   1 
ATOM   23225 O  OE2   . GLU A 1 4599 ? 138.420 183.263 192.213 1.00 39.54 ? 4599 GLU A OE2   1 
ATOM   23226 N  N     . LYS A 1 4600 ? 141.996 179.627 195.633 1.00 31.13 ? 4600 LYS A N     1 
ATOM   23227 C  CA    . LYS A 1 4600 ? 142.135 178.697 196.746 1.00 31.55 ? 4600 LYS A CA    1 
ATOM   23228 C  C     . LYS A 1 4600 ? 140.816 177.955 196.955 1.00 33.64 ? 4600 LYS A C     1 
ATOM   23229 O  O     . LYS A 1 4600 ? 139.890 178.036 196.142 1.00 35.78 ? 4600 LYS A O     1 
ATOM   23230 C  CB    . LYS A 1 4600 ? 142.589 179.441 197.999 1.00 32.07 ? 4600 LYS A CB    1 
ATOM   23231 C  CG    . LYS A 1 4600 ? 143.959 180.090 197.868 1.00 36.70 ? 4600 LYS A CG    1 
ATOM   23232 C  CD    . LYS A 1 4600 ? 145.013 179.078 197.443 1.00 34.49 ? 4600 LYS A CD    1 
ATOM   23233 C  CE    . LYS A 1 4600 ? 146.381 179.727 197.312 1.00 33.84 ? 4600 LYS A CE    1 
ATOM   23234 N  NZ    . LYS A 1 4600 ? 147.441 178.736 196.975 1.00 35.92 ? 4600 LYS A NZ    1 
ATOM   23235 N  N     . LYS A 1 4601 ? 140.714 177.214 198.060 1.00 32.22 ? 4601 LYS A N     1 
ATOM   23236 C  CA    . LYS A 1 4601 ? 139.531 176.412 198.345 1.00 34.14 ? 4601 LYS A CA    1 
ATOM   23237 C  C     . LYS A 1 4601 ? 138.950 176.705 199.726 1.00 34.65 ? 4601 LYS A C     1 
ATOM   23238 O  O     . LYS A 1 4601 ? 138.139 175.915 200.223 1.00 32.18 ? 4601 LYS A O     1 
ATOM   23239 C  CB    . LYS A 1 4601 ? 139.860 174.919 198.217 1.00 31.59 ? 4601 LYS A CB    1 
ATOM   23240 C  CG    . LYS A 1 4601 ? 138.669 174.026 197.892 1.00 29.57 ? 4601 LYS A CG    1 
ATOM   23241 C  CD    . LYS A 1 4601 ? 139.049 172.556 197.955 1.00 37.25 ? 4601 LYS A CD    1 
ATOM   23242 C  CE    . LYS A 1 4601 ? 140.239 172.253 197.059 1.00 34.73 ? 4601 LYS A CE    1 
ATOM   23243 N  NZ    . LYS A 1 4601 ? 140.605 170.810 197.092 1.00 31.96 ? 4601 LYS A NZ    1 
ATOM   23244 N  N     . ALA A 1 4602 ? 139.353 177.807 200.361 1.00 31.54 ? 4602 ALA A N     1 
ATOM   23245 C  CA    . ALA A 1 4602 ? 138.925 178.241 201.689 1.00 25.43 ? 4602 ALA A CA    1 
ATOM   23246 C  C     . ALA A 1 4602 ? 139.373 177.286 202.788 1.00 31.00 ? 4602 ALA A C     1 
ATOM   23247 O  O     . ALA A 1 4602 ? 139.087 177.539 203.965 1.00 29.28 ? 4602 ALA A O     1 
ATOM   23248 C  CB    . ALA A 1 4602 ? 137.404 178.439 201.787 1.00 26.55 ? 4602 ALA A CB    1 
ATOM   23249 N  N     . SER A 1 4603 ? 140.063 176.198 202.448 1.00 26.59 ? 4603 SER A N     1 
ATOM   23250 C  CA    . SER A 1 4603 ? 140.634 175.279 203.423 1.00 18.98 ? 4603 SER A CA    1 
ATOM   23251 C  C     . SER A 1 4603 ? 142.056 174.889 203.040 1.00 20.19 ? 4603 SER A C     1 
ATOM   23252 O  O     . SER A 1 4603 ? 142.513 173.799 203.395 1.00 25.99 ? 4603 SER A O     1 
ATOM   23253 C  CB    . SER A 1 4603 ? 139.763 174.030 203.571 1.00 22.81 ? 4603 SER A CB    1 
ATOM   23254 O  OG    . SER A 1 4603 ? 139.397 173.513 202.303 1.00 27.68 ? 4603 SER A OG    1 
ATOM   23255 N  N     . VAL A 1 4604 ? 142.761 175.757 202.320 1.00 18.35 ? 4604 VAL A N     1 
ATOM   23256 C  CA    . VAL A 1 4604 ? 144.093 175.473 201.803 1.00 17.93 ? 4604 VAL A CA    1 
ATOM   23257 C  C     . VAL A 1 4604 ? 145.065 176.482 202.395 1.00 17.02 ? 4604 VAL A C     1 
ATOM   23258 O  O     . VAL A 1 4604 ? 144.801 177.689 202.379 1.00 17.67 ? 4604 VAL A O     1 
ATOM   23259 C  CB    . VAL A 1 4604 ? 144.124 175.521 200.264 1.00 16.90 ? 4604 VAL A CB    1 
ATOM   23260 C  CG1   . VAL A 1 4604 ? 145.559 175.541 199.755 1.00 13.76 ? 4604 VAL A CG1   1 
ATOM   23261 C  CG2   . VAL A 1 4604 ? 143.366 174.341 199.688 1.00 18.14 ? 4604 VAL A CG2   1 
ATOM   23262 N  N     . VAL A 1 4605 ? 146.179 175.984 202.926 1.00 12.51 ? 4605 VAL A N     1 
ATOM   23263 C  CA    . VAL A 1 4605 ? 147.251 176.821 203.449 1.00 9.39  ? 4605 VAL A CA    1 
ATOM   23264 C  C     . VAL A 1 4605 ? 148.489 176.601 202.594 1.00 9.59  ? 4605 VAL A C     1 
ATOM   23265 O  O     . VAL A 1 4605 ? 148.804 175.465 202.222 1.00 9.06  ? 4605 VAL A O     1 
ATOM   23266 C  CB    . VAL A 1 4605 ? 147.540 176.529 204.936 1.00 8.62  ? 4605 VAL A CB    1 
ATOM   23267 C  CG1   . VAL A 1 4605 ? 146.324 176.832 205.774 1.00 11.67 ? 4605 VAL A CG1   1 
ATOM   23268 C  CG2   . VAL A 1 4605 ? 147.971 175.083 205.146 1.00 14.72 ? 4605 VAL A CG2   1 
ATOM   23269 N  N     . THR A 1 4606 ? 149.165 177.693 202.249 1.00 13.08 ? 4606 THR A N     1 
ATOM   23270 C  CA    . THR A 1 4606 ? 150.444 177.623 201.559 1.00 6.77  ? 4606 THR A CA    1 
ATOM   23271 C  C     . THR A 1 4606 ? 151.555 177.638 202.601 1.00 6.76  ? 4606 THR A C     1 
ATOM   23272 O  O     . THR A 1 4606 ? 151.706 178.616 203.340 1.00 10.65 ? 4606 THR A O     1 
ATOM   23273 C  CB    . THR A 1 4606 ? 150.608 178.780 200.574 1.00 9.27  ? 4606 THR A CB    1 
ATOM   23274 O  OG1   . THR A 1 4606 ? 149.599 178.693 199.562 1.00 16.76 ? 4606 THR A OG1   1 
ATOM   23275 C  CG2   . THR A 1 4606 ? 151.975 178.728 199.920 1.00 7.71  ? 4606 THR A CG2   1 
ATOM   23276 N  N     . LEU A 1 4607 ? 152.318 176.557 202.666 1.00 9.22  ? 4607 LEU A N     1 
ATOM   23277 C  CA    . LEU A 1 4607 ? 153.357 176.421 203.667 1.00 7.03  ? 4607 LEU A CA    1 
ATOM   23278 C  C     . LEU A 1 4607 ? 154.718 176.684 203.055 1.00 4.26  ? 4607 LEU A C     1 
ATOM   23279 O  O     . LEU A 1 4607 ? 155.056 176.079 202.029 1.00 6.16  ? 4607 LEU A O     1 
ATOM   23280 C  CB    . LEU A 1 4607 ? 153.334 175.023 204.287 1.00 4.25  ? 4607 LEU A CB    1 
ATOM   23281 C  CG    . LEU A 1 4607 ? 152.187 174.705 205.245 1.00 6.41  ? 4607 LEU A CG    1 
ATOM   23282 C  CD1   . LEU A 1 4607 ? 152.528 173.467 206.047 1.00 4.95  ? 4607 LEU A CD1   1 
ATOM   23283 C  CD2   . LEU A 1 4607 ? 151.888 175.883 206.158 1.00 6.08  ? 4607 LEU A CD2   1 
ATOM   23284 N  N     . PRO A 1 4608 ? 155.515 177.577 203.631 1.00 4.59  ? 4608 PRO A N     1 
ATOM   23285 C  CA    . PRO A 1 4608 ? 156.901 177.712 203.180 1.00 6.39  ? 4608 PRO A CA    1 
ATOM   23286 C  C     . PRO A 1 4608 ? 157.684 176.444 203.471 1.00 6.97  ? 4608 PRO A C     1 
ATOM   23287 O  O     . PRO A 1 4608 ? 157.454 175.768 204.477 1.00 7.08  ? 4608 PRO A O     1 
ATOM   23288 C  CB    . PRO A 1 4608 ? 157.426 178.897 203.994 1.00 3.87  ? 4608 PRO A CB    1 
ATOM   23289 C  CG    . PRO A 1 4608 ? 156.591 178.897 205.224 1.00 2.92  ? 4608 PRO A CG    1 
ATOM   23290 C  CD    . PRO A 1 4608 ? 155.233 178.404 204.817 1.00 4.59  ? 4608 PRO A CD    1 
ATOM   23291 N  N     . VAL A 1 4609 ? 158.609 176.119 202.576 1.00 3.29  ? 4609 VAL A N     1 
ATOM   23292 C  CA    . VAL A 1 4609 ? 159.533 175.008 202.764 1.00 4.56  ? 4609 VAL A CA    1 
ATOM   23293 C  C     . VAL A 1 4609 ? 160.930 175.599 202.865 1.00 5.39  ? 4609 VAL A C     1 
ATOM   23294 O  O     . VAL A 1 4609 ? 161.500 176.036 201.858 1.00 8.17  ? 4609 VAL A O     1 
ATOM   23295 C  CB    . VAL A 1 4609 ? 159.448 173.977 201.632 1.00 5.29  ? 4609 VAL A CB    1 
ATOM   23296 C  CG1   . VAL A 1 4609 ? 160.362 172.801 201.926 1.00 3.95  ? 4609 VAL A CG1   1 
ATOM   23297 C  CG2   . VAL A 1 4609 ? 158.021 173.505 201.461 1.00 4.96  ? 4609 VAL A CG2   1 
ATOM   23298 N  N     . TYR A 1 4610 ? 161.478 175.617 204.072 1.00 6.69  ? 4610 TYR A N     1 
ATOM   23299 C  CA    . TYR A 1 4610 ? 162.812 176.144 204.298 1.00 5.04  ? 4610 TYR A CA    1 
ATOM   23300 C  C     . TYR A 1 4610 ? 163.838 175.019 204.275 1.00 7.45  ? 4610 TYR A C     1 
ATOM   23301 O  O     . TYR A 1 4610 ? 163.511 173.840 204.419 1.00 14.69 ? 4610 TYR A O     1 
ATOM   23302 C  CB    . TYR A 1 4610 ? 162.880 176.897 205.628 1.00 4.84  ? 4610 TYR A CB    1 
ATOM   23303 C  CG    . TYR A 1 4610 ? 161.982 178.108 205.685 1.00 3.57  ? 4610 TYR A CG    1 
ATOM   23304 C  CD1   . TYR A 1 4610 ? 162.334 179.283 205.037 1.00 6.04  ? 4610 TYR A CD1   1 
ATOM   23305 C  CD2   . TYR A 1 4610 ? 160.786 178.078 206.385 1.00 3.53  ? 4610 TYR A CD2   1 
ATOM   23306 C  CE1   . TYR A 1 4610 ? 161.519 180.394 205.086 1.00 4.82  ? 4610 TYR A CE1   1 
ATOM   23307 C  CE2   . TYR A 1 4610 ? 159.964 179.184 206.441 1.00 3.67  ? 4610 TYR A CE2   1 
ATOM   23308 C  CZ    . TYR A 1 4610 ? 160.336 180.339 205.788 1.00 4.39  ? 4610 TYR A CZ    1 
ATOM   23309 O  OH    . TYR A 1 4610 ? 159.522 181.444 205.838 1.00 7.07  ? 4610 TYR A OH    1 
ATOM   23310 N  N     . LEU A 1 4611 ? 165.099 175.404 204.081 1.00 7.82  ? 4611 LEU A N     1 
ATOM   23311 C  CA    . LEU A 1 4611 ? 166.162 174.411 203.983 1.00 9.32  ? 4611 LEU A CA    1 
ATOM   23312 C  C     . LEU A 1 4611 ? 166.444 173.760 205.331 1.00 11.20 ? 4611 LEU A C     1 
ATOM   23313 O  O     . LEU A 1 4611 ? 166.548 172.532 205.428 1.00 19.29 ? 4611 LEU A O     1 
ATOM   23314 C  CB    . LEU A 1 4611 ? 167.424 175.054 203.417 1.00 7.70  ? 4611 LEU A CB    1 
ATOM   23315 C  CG    . LEU A 1 4611 ? 168.612 174.106 203.280 1.00 13.19 ? 4611 LEU A CG    1 
ATOM   23316 C  CD1   . LEU A 1 4611 ? 168.282 172.958 202.340 1.00 14.37 ? 4611 LEU A CD1   1 
ATOM   23317 C  CD2   . LEU A 1 4611 ? 169.815 174.867 202.791 1.00 11.60 ? 4611 LEU A CD2   1 
ATOM   23318 N  N     . ASN A 1 4612 ? 166.566 174.562 206.386 1.00 11.19 ? 4612 ASN A N     1 
ATOM   23319 C  CA    . ASN A 1 4612 ? 166.880 174.042 207.711 1.00 9.27  ? 4612 ASN A CA    1 
ATOM   23320 C  C     . ASN A 1 4612 ? 166.101 174.841 208.750 1.00 8.97  ? 4612 ASN A C     1 
ATOM   23321 O  O     . ASN A 1 4612 ? 165.278 175.700 208.418 1.00 9.84  ? 4612 ASN A O     1 
ATOM   23322 C  CB    . ASN A 1 4612 ? 168.394 174.070 207.963 1.00 7.81  ? 4612 ASN A CB    1 
ATOM   23323 C  CG    . ASN A 1 4612 ? 169.013 175.413 207.661 1.00 9.00  ? 4612 ASN A CG    1 
ATOM   23324 O  OD1   . ASN A 1 4612 ? 168.771 176.391 208.363 1.00 12.39 ? 4612 ASN A OD1   1 
ATOM   23325 N  ND2   . ASN A 1 4612 ? 169.821 175.468 206.611 1.00 13.45 ? 4612 ASN A ND2   1 
ATOM   23326 N  N     . PHE A 1 4613 ? 166.375 174.549 210.024 1.00 8.93  ? 4613 PHE A N     1 
ATOM   23327 C  CA    . PHE A 1 4613 ? 165.612 175.116 211.131 1.00 4.57  ? 4613 PHE A CA    1 
ATOM   23328 C  C     . PHE A 1 4613 ? 165.767 176.626 211.245 1.00 5.90  ? 4613 PHE A C     1 
ATOM   23329 O  O     . PHE A 1 4613 ? 164.900 177.276 211.837 1.00 10.61 ? 4613 PHE A O     1 
ATOM   23330 C  CB    . PHE A 1 4613 ? 166.030 174.446 212.441 1.00 6.63  ? 4613 PHE A CB    1 
ATOM   23331 C  CG    . PHE A 1 4613 ? 167.436 174.761 212.865 1.00 6.79  ? 4613 PHE A CG    1 
ATOM   23332 C  CD1   . PHE A 1 4613 ? 167.706 175.845 213.685 1.00 8.41  ? 4613 PHE A CD1   1 
ATOM   23333 C  CD2   . PHE A 1 4613 ? 168.495 173.982 212.427 1.00 10.36 ? 4613 PHE A CD2   1 
ATOM   23334 C  CE1   . PHE A 1 4613 ? 168.997 176.140 214.066 1.00 11.88 ? 4613 PHE A CE1   1 
ATOM   23335 C  CE2   . PHE A 1 4613 ? 169.790 174.272 212.807 1.00 14.86 ? 4613 PHE A CE2   1 
ATOM   23336 C  CZ    . PHE A 1 4613 ? 170.041 175.352 213.626 1.00 19.45 ? 4613 PHE A CZ    1 
ATOM   23337 N  N     . THR A 1 4614 ? 166.845 177.199 210.709 1.00 7.49  ? 4614 THR A N     1 
ATOM   23338 C  CA    . THR A 1 4614 ? 167.032 178.643 210.797 1.00 7.76  ? 4614 THR A CA    1 
ATOM   23339 C  C     . THR A 1 4614 ? 166.025 179.413 209.952 1.00 8.68  ? 4614 THR A C     1 
ATOM   23340 O  O     . THR A 1 4614 ? 165.817 180.605 210.200 1.00 15.91 ? 4614 THR A O     1 
ATOM   23341 C  CB    . THR A 1 4614 ? 168.455 179.023 210.383 1.00 6.86  ? 4614 THR A CB    1 
ATOM   23342 O  OG1   . THR A 1 4614 ? 168.588 178.926 208.960 1.00 12.78 ? 4614 THR A OG1   1 
ATOM   23343 C  CG2   . THR A 1 4614 ? 169.465 178.109 211.051 1.00 7.31  ? 4614 THR A CG2   1 
ATOM   23344 N  N     . ARG A 1 4615 ? 165.410 178.762 208.963 1.00 6.47  ? 4615 ARG A N     1 
ATOM   23345 C  CA    . ARG A 1 4615 ? 164.400 179.372 208.096 1.00 5.65  ? 4615 ARG A CA    1 
ATOM   23346 C  C     . ARG A 1 4615 ? 164.941 180.596 207.365 1.00 5.06  ? 4615 ARG A C     1 
ATOM   23347 O  O     . ARG A 1 4615 ? 164.189 181.511 207.023 1.00 11.06 ? 4615 ARG A O     1 
ATOM   23348 C  CB    . ARG A 1 4615 ? 163.135 179.734 208.880 1.00 4.70  ? 4615 ARG A CB    1 
ATOM   23349 C  CG    . ARG A 1 4615 ? 162.462 178.541 209.529 1.00 3.04  ? 4615 ARG A CG    1 
ATOM   23350 C  CD    . ARG A 1 4615 ? 161.077 178.876 210.045 1.00 3.67  ? 4615 ARG A CD    1 
ATOM   23351 N  NE    . ARG A 1 4615 ? 160.491 177.740 210.744 1.00 6.51  ? 4615 ARG A NE    1 
ATOM   23352 C  CZ    . ARG A 1 4615 ? 159.249 177.697 211.206 1.00 2.20  ? 4615 ARG A CZ    1 
ATOM   23353 N  NH1   . ARG A 1 4615 ? 158.415 178.710 211.043 1.00 2.18  ? 4615 ARG A NH1   1 
ATOM   23354 N  NH2   . ARG A 1 4615 ? 158.832 176.606 211.840 1.00 2.41  ? 4615 ARG A NH2   1 
ATOM   23355 N  N     . ALA A 1 4616 ? 166.247 180.623 207.116 1.00 6.95  ? 4616 ALA A N     1 
ATOM   23356 C  CA    . ALA A 1 4616 ? 166.874 181.739 206.426 1.00 5.92  ? 4616 ALA A CA    1 
ATOM   23357 C  C     . ALA A 1 4616 ? 166.829 181.608 204.911 1.00 8.80  ? 4616 ALA A C     1 
ATOM   23358 O  O     . ALA A 1 4616 ? 167.124 182.585 204.214 1.00 17.80 ? 4616 ALA A O     1 
ATOM   23359 C  CB    . ALA A 1 4616 ? 168.329 181.888 206.878 1.00 6.21  ? 4616 ALA A CB    1 
ATOM   23360 N  N     . ASP A 1 4617 ? 166.466 180.441 204.386 1.00 11.57 ? 4617 ASP A N     1 
ATOM   23361 C  CA    . ASP A 1 4617 ? 166.506 180.185 202.947 1.00 14.13 ? 4617 ASP A CA    1 
ATOM   23362 C  C     . ASP A 1 4617 ? 165.229 179.465 202.541 1.00 9.23  ? 4617 ASP A C     1 
ATOM   23363 O  O     . ASP A 1 4617 ? 164.993 178.330 202.965 1.00 10.43 ? 4617 ASP A O     1 
ATOM   23364 C  CB    . ASP A 1 4617 ? 167.738 179.362 202.571 1.00 10.27 ? 4617 ASP A CB    1 
ATOM   23365 C  CG    . ASP A 1 4617 ? 169.030 179.998 203.041 1.00 20.40 ? 4617 ASP A CG    1 
ATOM   23366 O  OD1   . ASP A 1 4617 ? 169.630 179.484 204.007 1.00 19.30 ? 4617 ASP A OD1   1 
ATOM   23367 O  OD2   . ASP A 1 4617 ? 169.443 181.014 202.444 1.00 24.06 ? 4617 ASP A OD2   1 
ATOM   23368 N  N     . LEU A 1 4618 ? 164.416 180.117 201.717 1.00 9.04  ? 4618 LEU A N     1 
ATOM   23369 C  CA    . LEU A 1 4618 ? 163.213 179.493 201.185 1.00 8.23  ? 4618 LEU A CA    1 
ATOM   23370 C  C     . LEU A 1 4618 ? 163.560 178.667 199.954 1.00 9.92  ? 4618 LEU A C     1 
ATOM   23371 O  O     . LEU A 1 4618 ? 164.289 179.129 199.071 1.00 17.40 ? 4618 LEU A O     1 
ATOM   23372 C  CB    . LEU A 1 4618 ? 162.170 180.552 200.838 1.00 8.25  ? 4618 LEU A CB    1 
ATOM   23373 C  CG    . LEU A 1 4618 ? 160.822 180.014 200.356 1.00 10.31 ? 4618 LEU A CG    1 
ATOM   23374 C  CD1   . LEU A 1 4618 ? 160.085 179.325 201.493 1.00 7.67  ? 4618 LEU A CD1   1 
ATOM   23375 C  CD2   . LEU A 1 4618 ? 159.978 181.124 199.755 1.00 8.65  ? 4618 LEU A CD2   1 
ATOM   23376 N  N     . ILE A 1 4619 ? 163.043 177.442 199.900 1.00 5.06  ? 4619 ILE A N     1 
ATOM   23377 C  CA    . ILE A 1 4619 ? 163.290 176.551 198.773 1.00 10.03 ? 4619 ILE A CA    1 
ATOM   23378 C  C     . ILE A 1 4619 ? 162.122 176.639 197.799 1.00 8.79  ? 4619 ILE A C     1 
ATOM   23379 O  O     . ILE A 1 4619 ? 162.298 177.000 196.631 1.00 10.18 ? 4619 ILE A O     1 
ATOM   23380 C  CB    . ILE A 1 4619 ? 163.512 175.102 199.241 1.00 10.71 ? 4619 ILE A CB    1 
ATOM   23381 C  CG1   . ILE A 1 4619 ? 164.580 175.049 200.335 1.00 13.17 ? 4619 ILE A CG1   1 
ATOM   23382 C  CG2   . ILE A 1 4619 ? 163.909 174.220 198.070 1.00 7.71  ? 4619 ILE A CG2   1 
ATOM   23383 C  CD1   . ILE A 1 4619 ? 165.886 175.705 199.949 1.00 10.83 ? 4619 ILE A CD1   1 
ATOM   23384 N  N     . PHE A 1 4620 ? 160.925 176.309 198.275 1.00 5.65  ? 4620 PHE A N     1 
ATOM   23385 C  CA    . PHE A 1 4620 ? 159.718 176.380 197.462 1.00 5.56  ? 4620 PHE A CA    1 
ATOM   23386 C  C     . PHE A 1 4620 ? 158.517 176.417 198.398 1.00 8.29  ? 4620 PHE A C     1 
ATOM   23387 O  O     . PHE A 1 4620 ? 158.659 176.493 199.621 1.00 9.00  ? 4620 PHE A O     1 
ATOM   23388 C  CB    . PHE A 1 4620 ? 159.646 175.216 196.466 1.00 6.10  ? 4620 PHE A CB    1 
ATOM   23389 C  CG    . PHE A 1 4620 ? 159.483 173.864 197.103 1.00 5.75  ? 4620 PHE A CG    1 
ATOM   23390 C  CD1   . PHE A 1 4620 ? 160.544 173.251 197.748 1.00 8.75  ? 4620 PHE A CD1   1 
ATOM   23391 C  CD2   . PHE A 1 4620 ? 158.279 173.189 197.026 1.00 5.93  ? 4620 PHE A CD2   1 
ATOM   23392 C  CE1   . PHE A 1 4620 ? 160.400 172.004 198.323 1.00 5.65  ? 4620 PHE A CE1   1 
ATOM   23393 C  CE2   . PHE A 1 4620 ? 158.132 171.939 197.594 1.00 6.25  ? 4620 PHE A CE2   1 
ATOM   23394 C  CZ    . PHE A 1 4620 ? 159.192 171.347 198.246 1.00 7.27  ? 4620 PHE A CZ    1 
ATOM   23395 N  N     . THR A 1 4621 ? 157.326 176.377 197.811 1.00 8.00  ? 4621 THR A N     1 
ATOM   23396 C  CA    . THR A 1 4621 ? 156.080 176.464 198.557 1.00 6.28  ? 4621 THR A CA    1 
ATOM   23397 C  C     . THR A 1 4621 ? 155.210 175.256 198.247 1.00 11.07 ? 4621 THR A C     1 
ATOM   23398 O  O     . THR A 1 4621 ? 155.170 174.781 197.108 1.00 12.46 ? 4621 THR A O     1 
ATOM   23399 C  CB    . THR A 1 4621 ? 155.313 177.748 198.218 1.00 10.78 ? 4621 THR A CB    1 
ATOM   23400 O  OG1   . THR A 1 4621 ? 154.969 177.748 196.828 1.00 12.85 ? 4621 THR A OG1   1 
ATOM   23401 C  CG2   . THR A 1 4621 ? 156.164 178.968 198.516 1.00 9.14  ? 4621 THR A CG2   1 
ATOM   23402 N  N     . VAL A 1 4622 ? 154.516 174.765 199.266 1.00 8.43  ? 4622 VAL A N     1 
ATOM   23403 C  CA    . VAL A 1 4622 ? 153.578 173.662 199.122 1.00 8.71  ? 4622 VAL A CA    1 
ATOM   23404 C  C     . VAL A 1 4622 ? 152.193 174.138 199.530 1.00 10.39 ? 4622 VAL A C     1 
ATOM   23405 O  O     . VAL A 1 4622 ? 152.037 175.061 200.335 1.00 12.41 ? 4622 VAL A O     1 
ATOM   23406 C  CB    . VAL A 1 4622 ? 153.997 172.431 199.954 1.00 10.82 ? 4622 VAL A CB    1 
ATOM   23407 C  CG1   . VAL A 1 4622 ? 155.390 172.001 199.588 1.00 11.19 ? 4622 VAL A CG1   1 
ATOM   23408 C  CG2   . VAL A 1 4622 ? 153.942 172.759 201.433 1.00 8.56  ? 4622 VAL A CG2   1 
ATOM   23409 N  N     . ASP A 1 4623 ? 151.179 173.499 198.953 1.00 12.39 ? 4623 ASP A N     1 
ATOM   23410 C  CA    . ASP A 1 4623 ? 149.786 173.763 199.281 1.00 12.00 ? 4623 ASP A CA    1 
ATOM   23411 C  C     . ASP A 1 4623 ? 149.195 172.508 199.901 1.00 9.89  ? 4623 ASP A C     1 
ATOM   23412 O  O     . ASP A 1 4623 ? 149.284 171.422 199.316 1.00 13.09 ? 4623 ASP A O     1 
ATOM   23413 C  CB    . ASP A 1 4623 ? 148.991 174.178 198.042 1.00 10.73 ? 4623 ASP A CB    1 
ATOM   23414 C  CG    . ASP A 1 4623 ? 149.394 175.535 197.520 1.00 18.88 ? 4623 ASP A CG    1 
ATOM   23415 O  OD1   . ASP A 1 4623 ? 149.831 176.379 198.330 1.00 23.12 ? 4623 ASP A OD1   1 
ATOM   23416 O  OD2   . ASP A 1 4623 ? 149.274 175.764 196.297 1.00 30.85 ? 4623 ASP A OD2   1 
ATOM   23417 N  N     . PHE A 1 4624 ? 148.606 172.654 201.080 1.00 11.18 ? 4624 PHE A N     1 
ATOM   23418 C  CA    . PHE A 1 4624 ? 147.929 171.566 201.760 1.00 10.18 ? 4624 PHE A CA    1 
ATOM   23419 C  C     . PHE A 1 4624 ? 146.496 171.967 202.068 1.00 12.82 ? 4624 PHE A C     1 
ATOM   23420 O  O     . PHE A 1 4624 ? 146.168 173.149 202.177 1.00 16.82 ? 4624 PHE A O     1 
ATOM   23421 C  CB    . PHE A 1 4624 ? 148.634 171.184 203.063 1.00 8.49  ? 4624 PHE A CB    1 
ATOM   23422 C  CG    . PHE A 1 4624 ? 149.859 170.346 202.874 1.00 7.40  ? 4624 PHE A CG    1 
ATOM   23423 C  CD1   . PHE A 1 4624 ? 149.753 168.978 202.695 1.00 10.16 ? 4624 PHE A CD1   1 
ATOM   23424 C  CD2   . PHE A 1 4624 ? 151.118 170.916 202.907 1.00 8.89  ? 4624 PHE A CD2   1 
ATOM   23425 C  CE1   . PHE A 1 4624 ? 150.880 168.198 202.533 1.00 14.90 ? 4624 PHE A CE1   1 
ATOM   23426 C  CE2   . PHE A 1 4624 ? 152.247 170.138 202.747 1.00 10.90 ? 4624 PHE A CE2   1 
ATOM   23427 C  CZ    . PHE A 1 4624 ? 152.127 168.780 202.559 1.00 12.80 ? 4624 PHE A CZ    1 
ATOM   23428 N  N     . GLU A 1 4625 ? 145.637 170.960 202.236 1.00 12.06 ? 4625 GLU A N     1 
ATOM   23429 C  CA    . GLU A 1 4625 ? 144.237 171.244 202.642 1.00 14.26 ? 4625 GLU A CA    1 
ATOM   23430 C  C     . GLU A 1 4625 ? 144.126 170.992 204.153 1.00 17.02 ? 4625 GLU A C     1 
ATOM   23431 O  O     . GLU A 1 4625 ? 144.514 169.890 204.598 1.00 20.05 ? 4625 GLU A O     1 
ATOM   23432 C  CB    . GLU A 1 4625 ? 143.244 170.363 201.889 1.00 14.96 ? 4625 GLU A CB    1 
ATOM   23433 C  CG    . GLU A 1 4625 ? 141.820 170.489 202.418 1.00 17.06 ? 4625 GLU A CG    1 
ATOM   23434 C  CD    . GLU A 1 4625 ? 140.875 169.407 201.929 1.00 28.49 ? 4625 GLU A CD    1 
ATOM   23435 O  OE1   . GLU A 1 4625 ? 141.326 168.537 201.154 1.00 32.56 ? 4625 GLU A OE1   1 
ATOM   23436 O  OE2   . GLU A 1 4625 ? 139.692 169.433 202.323 1.00 28.61 ? 4625 GLU A OE2   1 
ATOM   23437 N  N     . ILE A 1 4626 ? 143.631 171.976 204.902 1.00 13.85 ? 4626 ILE A N     1 
ATOM   23438 C  CA    . ILE A 1 4626 ? 143.472 171.822 206.379 1.00 17.32 ? 4626 ILE A CA    1 
ATOM   23439 C  C     . ILE A 1 4626 ? 142.229 170.959 206.652 1.00 19.37 ? 4626 ILE A C     1 
ATOM   23440 O  O     . ILE A 1 4626 ? 141.439 170.749 205.708 1.00 22.00 ? 4626 ILE A O     1 
ATOM   23441 C  CB    . ILE A 1 4626 ? 143.379 173.198 207.060 1.00 18.34 ? 4626 ILE A CB    1 
ATOM   23442 C  CG1   . ILE A 1 4626 ? 142.150 173.971 206.593 1.00 17.33 ? 4626 ILE A CG1   1 
ATOM   23443 C  CG2   . ILE A 1 4626 ? 144.664 173.997 206.842 1.00 15.57 ? 4626 ILE A CG2   1 
ATOM   23444 C  CD1   . ILE A 1 4626 ? 142.200 175.455 206.902 1.00 21.74 ? 4626 ILE A CD1   1 
ATOM   23445 N  N     . ALA A 1 4627 ? 142.066 170.492 207.893 1.00 21.36 ? 4627 ALA A N     1 
ATOM   23446 C  CA    . ALA A 1 4627 ? 140.924 169.612 208.233 1.00 25.35 ? 4627 ALA A CA    1 
ATOM   23447 C  C     . ALA A 1 4627 ? 140.069 170.249 209.329 1.00 28.12 ? 4627 ALA A C     1 
ATOM   23448 O  O     . ALA A 1 4627 ? 140.469 171.307 209.864 1.00 31.56 ? 4627 ALA A O     1 
ATOM   23449 C  CB    . ALA A 1 4627 ? 141.438 168.255 208.659 1.00 21.46 ? 4627 ALA A CB    1 
ATOM   23450 N  N     . THR A 1 4628 ? 138.918 169.642 209.637 1.00 29.19 ? 4628 THR A N     1 
ATOM   23451 C  CA    . THR A 1 4628 ? 138.040 170.140 210.722 1.00 35.08 ? 4628 THR A CA    1 
ATOM   23452 C  C     . THR A 1 4628 ? 137.757 171.615 210.525 1.00 31.16 ? 4628 THR A C     1 
ATOM   23453 O  O     . THR A 1 4628 ? 137.600 172.039 209.360 1.00 31.25 ? 4628 THR A O     1 
ATOM   23454 C  CB    . THR A 1 4628 ? 138.682 169.866 212.083 1.00 28.98 ? 4628 THR A CB    1 
ATOM   23455 O  OG1   . THR A 1 4628 ? 139.733 170.816 212.227 1.00 27.59 ? 4628 THR A OG1   1 
ATOM   23456 C  CG2   . THR A 1 4628 ? 139.236 168.456 212.190 1.00 26.52 ? 4628 THR A CG2   1 
ATOM   23457 N  N     . LYS A 1 4629 ? 137.690 172.372 211.624 1.00 26.01 ? 4629 LYS A N     1 
ATOM   23458 C  CA    . LYS A 1 4629 ? 137.383 173.823 211.546 1.00 34.15 ? 4629 LYS A CA    1 
ATOM   23459 C  C     . LYS A 1 4629 ? 138.681 174.624 211.728 1.00 33.34 ? 4629 LYS A C     1 
ATOM   23460 O  O     . LYS A 1 4629 ? 138.592 175.846 211.985 1.00 34.17 ? 4629 LYS A O     1 
ATOM   23461 C  CB    . LYS A 1 4629 ? 136.354 174.199 212.616 1.00 31.43 ? 4629 LYS A CB    1 
ATOM   23462 C  CG    . LYS A 1 4629 ? 136.797 173.921 214.046 1.00 31.81 ? 4629 LYS A CG    1 
ATOM   23463 C  CD    . LYS A 1 4629 ? 135.716 174.224 215.077 1.00 32.82 ? 4629 LYS A CD    1 
ATOM   23464 C  CE    . LYS A 1 4629 ? 134.480 173.413 214.852 1.00 35.60 ? 4629 LYS A CE    1 
ATOM   23465 N  NZ    . LYS A 1 4629 ? 133.446 173.715 215.845 1.00 37.30 ? 4629 LYS A NZ    1 
ATOM   23466 N  N     . GLU A 1 4630 ? 139.833 173.962 211.596 1.00 26.47 ? 4630 GLU A N     1 
ATOM   23467 C  CA    . GLU A 1 4630 ? 141.136 174.649 211.787 1.00 24.22 ? 4630 GLU A CA    1 
ATOM   23468 C  C     . GLU A 1 4630 ? 141.147 175.938 210.953 1.00 28.73 ? 4630 GLU A C     1 
ATOM   23469 O  O     . GLU A 1 4630 ? 140.961 175.846 209.721 1.00 22.35 ? 4630 GLU A O     1 
ATOM   23470 C  CB    . GLU A 1 4630 ? 142.295 173.739 211.383 1.00 20.53 ? 4630 GLU A CB    1 
ATOM   23471 C  CG    . GLU A 1 4630 ? 142.345 172.436 212.175 1.00 24.84 ? 4630 GLU A CG    1 
ATOM   23472 C  CD    . GLU A 1 4630 ? 142.392 172.637 213.678 1.00 34.20 ? 4630 GLU A CD    1 
ATOM   23473 O  OE1   . GLU A 1 4630 ? 143.360 173.259 214.164 1.00 33.74 ? 4630 GLU A OE1   1 
ATOM   23474 O  OE2   . GLU A 1 4630 ? 141.453 172.176 214.362 1.00 32.61 ? 4630 GLU A OE2   1 
ATOM   23475 N  N     . ASP A 1 4631 ? 141.358 177.088 211.599 1.00 25.11 ? 4631 ASP A N     1 
ATOM   23476 C  CA    . ASP A 1 4631 ? 141.449 178.378 210.863 1.00 17.54 ? 4631 ASP A CA    1 
ATOM   23477 C  C     . ASP A 1 4631 ? 142.801 178.434 210.148 1.00 14.75 ? 4631 ASP A C     1 
ATOM   23478 O  O     . ASP A 1 4631 ? 143.836 178.307 210.831 1.00 17.94 ? 4631 ASP A O     1 
ATOM   23479 C  CB    . ASP A 1 4631 ? 141.252 179.566 211.791 1.00 20.23 ? 4631 ASP A CB    1 
ATOM   23480 C  CG    . ASP A 1 4631 ? 141.380 180.941 211.149 1.00 24.07 ? 4631 ASP A CG    1 
ATOM   23481 O  OD1   . ASP A 1 4631 ? 141.600 181.003 209.921 1.00 20.85 ? 4631 ASP A OD1   1 
ATOM   23482 O  OD2   . ASP A 1 4631 ? 141.262 181.944 211.886 1.00 28.15 ? 4631 ASP A OD2   1 
ATOM   23483 N  N     . PRO A 1 4632 ? 142.853 178.618 208.813 1.00 13.90 ? 4632 PRO A N     1 
ATOM   23484 C  CA    . PRO A 1 4632 ? 144.136 178.759 208.107 1.00 15.16 ? 4632 PRO A CA    1 
ATOM   23485 C  C     . PRO A 1 4632 ? 145.002 179.869 208.672 1.00 13.88 ? 4632 PRO A C     1 
ATOM   23486 O  O     . PRO A 1 4632 ? 146.232 179.812 208.552 1.00 10.77 ? 4632 PRO A O     1 
ATOM   23487 C  CB    . PRO A 1 4632 ? 143.708 179.047 206.659 1.00 13.02 ? 4632 PRO A CB    1 
ATOM   23488 C  CG    . PRO A 1 4632 ? 142.277 179.480 206.752 1.00 15.98 ? 4632 PRO A CG    1 
ATOM   23489 C  CD    . PRO A 1 4632 ? 141.711 178.699 207.889 1.00 13.76 ? 4632 PRO A CD    1 
ATOM   23490 N  N     . ARG A 1 4633 ? 144.387 180.879 209.286 1.00 17.18 ? 4633 ARG A N     1 
ATOM   23491 C  CA    . ARG A 1 4633 ? 145.150 181.960 209.900 1.00 13.26 ? 4633 ARG A CA    1 
ATOM   23492 C  C     . ARG A 1 4633 ? 145.930 181.471 211.115 1.00 12.56 ? 4633 ARG A C     1 
ATOM   23493 O  O     . ARG A 1 4633 ? 147.003 182.002 211.426 1.00 13.93 ? 4633 ARG A O     1 
ATOM   23494 C  CB    . ARG A 1 4633 ? 144.202 183.100 210.269 1.00 10.69 ? 4633 ARG A CB    1 
ATOM   23495 C  CG    . ARG A 1 4633 ? 143.578 183.760 209.048 1.00 14.62 ? 4633 ARG A CG    1 
ATOM   23496 C  CD    . ARG A 1 4633 ? 142.815 185.022 209.398 1.00 17.20 ? 4633 ARG A CD    1 
ATOM   23497 N  NE    . ARG A 1 4633 ? 141.642 184.740 210.217 1.00 14.01 ? 4633 ARG A NE    1 
ATOM   23498 C  CZ    . ARG A 1 4633 ? 141.448 185.228 211.433 1.00 18.85 ? 4633 ARG A CZ    1 
ATOM   23499 N  NH1   . ARG A 1 4633 ? 142.333 186.024 212.006 1.00 24.29 ? 4633 ARG A NH1   1 
ATOM   23500 N  NH2   . ARG A 1 4633 ? 140.336 184.910 212.089 1.00 20.56 ? 4633 ARG A NH2   1 
ATOM   23501 N  N     . SER A 1 4634 ? 145.406 180.463 211.817 1.00 9.02  ? 4634 SER A N     1 
ATOM   23502 C  CA    . SER A 1 4634 ? 146.132 179.893 212.948 1.00 6.69  ? 4634 SER A CA    1 
ATOM   23503 C  C     . SER A 1 4634 ? 147.409 179.201 212.488 1.00 8.47  ? 4634 SER A C     1 
ATOM   23504 O  O     . SER A 1 4634 ? 148.425 179.223 213.193 1.00 11.92 ? 4634 SER A O     1 
ATOM   23505 C  CB    . SER A 1 4634 ? 145.240 178.919 213.717 1.00 8.98  ? 4634 SER A CB    1 
ATOM   23506 O  OG    . SER A 1 4634 ? 144.891 177.803 212.918 1.00 17.77 ? 4634 SER A OG    1 
ATOM   23507 N  N     . PHE A 1 4635 ? 147.371 178.571 211.312 1.00 9.62  ? 4635 PHE A N     1 
ATOM   23508 C  CA    . PHE A 1 4635 ? 148.585 178.004 210.736 1.00 5.68  ? 4635 PHE A CA    1 
ATOM   23509 C  C     . PHE A 1 4635 ? 149.625 179.085 210.479 1.00 5.97  ? 4635 PHE A C     1 
ATOM   23510 O  O     . PHE A 1 4635 ? 150.825 178.864 210.673 1.00 6.79  ? 4635 PHE A O     1 
ATOM   23511 C  CB    . PHE A 1 4635 ? 148.252 177.259 209.443 1.00 6.72  ? 4635 PHE A CB    1 
ATOM   23512 C  CG    . PHE A 1 4635 ? 147.644 175.908 209.663 1.00 7.99  ? 4635 PHE A CG    1 
ATOM   23513 C  CD1   . PHE A 1 4635 ? 146.284 175.772 209.876 1.00 8.66  ? 4635 PHE A CD1   1 
ATOM   23514 C  CD2   . PHE A 1 4635 ? 148.430 174.768 209.642 1.00 8.20  ? 4635 PHE A CD2   1 
ATOM   23515 C  CE1   . PHE A 1 4635 ? 145.723 174.528 210.080 1.00 10.29 ? 4635 PHE A CE1   1 
ATOM   23516 C  CE2   . PHE A 1 4635 ? 147.873 173.521 209.843 1.00 6.65  ? 4635 PHE A CE2   1 
ATOM   23517 C  CZ    . PHE A 1 4635 ? 146.518 173.401 210.061 1.00 9.72  ? 4635 PHE A CZ    1 
ATOM   23518 N  N     . TYR A 1 4636 ? 149.180 180.262 210.036 1.00 8.33  ? 4636 TYR A N     1 
ATOM   23519 C  CA    . TYR A 1 4636 ? 150.108 181.354 209.777 1.00 5.05  ? 4636 TYR A CA    1 
ATOM   23520 C  C     . TYR A 1 4636 ? 150.714 181.874 211.075 1.00 4.29  ? 4636 TYR A C     1 
ATOM   23521 O  O     . TYR A 1 4636 ? 151.910 182.178 211.132 1.00 5.61  ? 4636 TYR A O     1 
ATOM   23522 C  CB    . TYR A 1 4636 ? 149.389 182.482 209.039 1.00 7.58  ? 4636 TYR A CB    1 
ATOM   23523 C  CG    . TYR A 1 4636 ? 148.744 182.061 207.741 1.00 7.63  ? 4636 TYR A CG    1 
ATOM   23524 C  CD1   . TYR A 1 4636 ? 147.625 182.723 207.260 1.00 10.45 ? 4636 TYR A CD1   1 
ATOM   23525 C  CD2   . TYR A 1 4636 ? 149.229 180.983 207.016 1.00 6.54  ? 4636 TYR A CD2   1 
ATOM   23526 C  CE1   . TYR A 1 4636 ? 147.021 182.339 206.084 1.00 11.82 ? 4636 TYR A CE1   1 
ATOM   23527 C  CE2   . TYR A 1 4636 ? 148.626 180.589 205.842 1.00 8.92  ? 4636 TYR A CE2   1 
ATOM   23528 C  CZ    . TYR A 1 4636 ? 147.526 181.273 205.378 1.00 12.89 ? 4636 TYR A CZ    1 
ATOM   23529 O  OH    . TYR A 1 4636 ? 146.924 180.886 204.203 1.00 18.38 ? 4636 TYR A OH    1 
ATOM   23530 N  N     . GLU A 1 4637 ? 149.900 181.969 212.131 1.00 4.43  ? 4637 GLU A N     1 
ATOM   23531 C  CA    . GLU A 1 4637 ? 150.359 182.562 213.384 1.00 3.99  ? 4637 GLU A CA    1 
ATOM   23532 C  C     . GLU A 1 4637 ? 151.270 181.618 214.157 1.00 4.18  ? 4637 GLU A C     1 
ATOM   23533 O  O     . GLU A 1 4637 ? 152.166 182.068 214.879 1.00 11.67 ? 4637 GLU A O     1 
ATOM   23534 C  CB    . GLU A 1 4637 ? 149.158 182.965 214.238 1.00 5.25  ? 4637 GLU A CB    1 
ATOM   23535 C  CG    . GLU A 1 4637 ? 148.406 184.166 213.706 1.00 7.20  ? 4637 GLU A CG    1 
ATOM   23536 C  CD    . GLU A 1 4637 ? 147.425 184.725 214.708 1.00 18.45 ? 4637 GLU A CD    1 
ATOM   23537 O  OE1   . GLU A 1 4637 ? 147.317 184.156 215.813 1.00 12.78 ? 4637 GLU A OE1   1 
ATOM   23538 O  OE2   . GLU A 1 4637 ? 146.764 185.736 214.392 1.00 25.75 ? 4637 GLU A OE2   1 
ATOM   23539 N  N     . ARG A 1 4638 ? 151.056 180.313 214.029 1.00 4.99  ? 4638 ARG A N     1 
ATOM   23540 C  CA    . ARG A 1 4638 ? 151.874 179.351 214.754 1.00 3.94  ? 4638 ARG A CA    1 
ATOM   23541 C  C     . ARG A 1 4638 ? 153.188 179.049 214.046 1.00 5.79  ? 4638 ARG A C     1 
ATOM   23542 O  O     . ARG A 1 4638 ? 153.986 178.263 214.565 1.00 6.19  ? 4638 ARG A O     1 
ATOM   23543 C  CB    . ARG A 1 4638 ? 151.084 178.061 214.981 1.00 3.10  ? 4638 ARG A CB    1 
ATOM   23544 C  CG    . ARG A 1 4638 ? 149.928 178.234 215.954 1.00 3.14  ? 4638 ARG A CG    1 
ATOM   23545 C  CD    . ARG A 1 4638 ? 149.086 176.983 216.082 1.00 5.73  ? 4638 ARG A CD    1 
ATOM   23546 N  NE    . ARG A 1 4638 ? 149.874 175.820 216.470 1.00 7.94  ? 4638 ARG A NE    1 
ATOM   23547 C  CZ    . ARG A 1 4638 ? 149.671 175.117 217.576 1.00 5.80  ? 4638 ARG A CZ    1 
ATOM   23548 N  NH1   . ARG A 1 4638 ? 148.717 175.433 218.433 1.00 3.18  ? 4638 ARG A NH1   1 
ATOM   23549 N  NH2   . ARG A 1 4638 ? 150.450 174.068 217.828 1.00 12.31 ? 4638 ARG A NH2   1 
ATOM   23550 N  N     . GLY A 1 4639 ? 153.431 179.660 212.892 1.00 4.01  ? 4639 GLY A N     1 
ATOM   23551 C  CA    . GLY A 1 4639 ? 154.661 179.429 212.159 1.00 3.28  ? 4639 GLY A CA    1 
ATOM   23552 C  C     . GLY A 1 4639 ? 154.786 178.030 211.603 1.00 4.22  ? 4639 GLY A C     1 
ATOM   23553 O  O     . GLY A 1 4639 ? 155.877 177.448 211.639 1.00 9.33  ? 4639 GLY A O     1 
ATOM   23554 N  N     . VAL A 1 4640 ? 153.688 177.469 211.094 1.00 4.06  ? 4640 VAL A N     1 
ATOM   23555 C  CA    . VAL A 1 4640 ? 153.744 176.146 210.493 1.00 3.87  ? 4640 VAL A CA    1 
ATOM   23556 C  C     . VAL A 1 4640 ? 154.532 176.218 209.194 1.00 5.69  ? 4640 VAL A C     1 
ATOM   23557 O  O     . VAL A 1 4640 ? 154.279 177.070 208.333 1.00 8.65  ? 4640 VAL A O     1 
ATOM   23558 C  CB    . VAL A 1 4640 ? 152.325 175.603 210.263 1.00 3.94  ? 4640 VAL A CB    1 
ATOM   23559 C  CG1   . VAL A 1 4640 ? 152.381 174.215 209.653 1.00 5.48  ? 4640 VAL A CG1   1 
ATOM   23560 C  CG2   . VAL A 1 4640 ? 151.549 175.591 211.566 1.00 4.97  ? 4640 VAL A CG2   1 
ATOM   23561 N  N     . ALA A 1 4641 ? 155.499 175.319 209.050 1.00 8.24  ? 4641 ALA A N     1 
ATOM   23562 C  CA    . ALA A 1 4641 ? 156.393 175.324 207.901 1.00 3.48  ? 4641 ALA A CA    1 
ATOM   23563 C  C     . ALA A 1 4641 ? 156.919 173.911 207.690 1.00 5.87  ? 4641 ALA A C     1 
ATOM   23564 O  O     . ALA A 1 4641 ? 156.650 173.001 208.478 1.00 5.98  ? 4641 ALA A O     1 
ATOM   23565 C  CB    . ALA A 1 4641 ? 157.538 176.324 208.096 1.00 3.24  ? 4641 ALA A CB    1 
ATOM   23566 N  N     . VAL A 1 4642 ? 157.678 173.738 206.612 1.00 8.28  ? 4642 VAL A N     1 
ATOM   23567 C  CA    . VAL A 1 4642 ? 158.299 172.467 206.267 1.00 3.64  ? 4642 VAL A CA    1 
ATOM   23568 C  C     . VAL A 1 4642 ? 159.797 172.691 206.137 1.00 4.68  ? 4642 VAL A C     1 
ATOM   23569 O  O     . VAL A 1 4642 ? 160.235 173.681 205.541 1.00 5.31  ? 4642 VAL A O     1 
ATOM   23570 C  CB    . VAL A 1 4642 ? 157.713 171.882 204.963 1.00 5.64  ? 4642 VAL A CB    1 
ATOM   23571 C  CG1   . VAL A 1 4642 ? 158.463 170.625 204.548 1.00 4.76  ? 4642 VAL A CG1   1 
ATOM   23572 C  CG2   . VAL A 1 4642 ? 156.231 171.590 205.131 1.00 3.75  ? 4642 VAL A CG2   1 
ATOM   23573 N  N     . LEU A 1 4643 ? 160.583 171.786 206.710 1.00 7.50  ? 4643 LEU A N     1 
ATOM   23574 C  CA    . LEU A 1 4643 ? 162.035 171.851 206.642 1.00 5.09  ? 4643 LEU A CA    1 
ATOM   23575 C  C     . LEU A 1 4643 ? 162.564 170.753 205.731 1.00 7.81  ? 4643 LEU A C     1 
ATOM   23576 O  O     . LEU A 1 4643 ? 162.079 169.619 205.763 1.00 10.28 ? 4643 LEU A O     1 
ATOM   23577 C  CB    . LEU A 1 4643 ? 162.664 171.715 208.029 1.00 7.42  ? 4643 LEU A CB    1 
ATOM   23578 C  CG    . LEU A 1 4643 ? 162.253 172.728 209.097 1.00 4.86  ? 4643 LEU A CG    1 
ATOM   23579 C  CD1   . LEU A 1 4643 ? 163.098 172.542 210.346 1.00 4.60  ? 4643 LEU A CD1   1 
ATOM   23580 C  CD2   . LEU A 1 4643 ? 162.353 174.151 208.578 1.00 5.03  ? 4643 LEU A CD2   1 
ATOM   23581 N  N     . CYS A 1 4644 ? 163.561 171.100 204.916 1.00 10.70 ? 4644 CYS A N     1 
ATOM   23582 C  CA    . CYS A 1 4644 ? 164.172 170.108 204.036 1.00 11.80 ? 4644 CYS A CA    1 
ATOM   23583 C  C     . CYS A 1 4644 ? 165.056 169.140 204.812 1.00 8.77  ? 4644 CYS A C     1 
ATOM   23584 O  O     . CYS A 1 4644 ? 165.188 167.976 204.419 1.00 15.47 ? 4644 CYS A O     1 
ATOM   23585 C  CB    . CYS A 1 4644 ? 164.979 170.801 202.937 1.00 11.64 ? 4644 CYS A CB    1 
ATOM   23586 S  SG    . CYS A 1 4644 ? 163.978 171.632 201.686 1.00 38.35 ? 4644 CYS A SG    1 
ATOM   23587 N  N     . THR A 1 4645 ? 165.666 169.595 205.901 1.00 8.55  ? 4645 THR A N     1 
ATOM   23588 C  CA    . THR A 1 4645 ? 166.533 168.741 206.705 1.00 12.85 ? 4645 THR A CA    1 
ATOM   23589 C  C     . THR A 1 4645 ? 166.407 169.059 208.192 1.00 10.61 ? 4645 THR A C     1 
ATOM   23590 O  O     . THR A 1 4645 ? 165.548 169.837 208.600 1.00 13.35 ? 4645 THR A O     1 
ATOM   23591 C  CB    . THR A 1 4645 ? 168.008 168.881 206.289 1.00 22.72 ? 4645 THR A CB    1 
ATOM   23592 O  OG1   . THR A 1 4645 ? 168.786 167.862 206.928 1.00 31.56 ? 4645 THR A OG1   1 
ATOM   23593 C  CG2   . THR A 1 4645 ? 168.549 170.249 206.686 1.00 8.63  ? 4645 THR A CG2   1 
HETATM 23594 P  PB    . ADP B 2 .    ? 169.659 198.942 193.032 1.00 0.03  ? 4701 ADP A PB    1 
HETATM 23595 O  O1B   . ADP B 2 .    ? 171.006 198.289 192.885 1.00 0.73  ? 4701 ADP A O1B   1 
HETATM 23596 O  O2B   . ADP B 2 .    ? 168.713 198.159 193.901 1.00 1.20  ? 4701 ADP A O2B   1 
HETATM 23597 O  O3B   . ADP B 2 .    ? 169.753 200.392 193.426 1.00 0.36  ? 4701 ADP A O3B   1 
HETATM 23598 P  PA    . ADP B 2 .    ? 168.973 200.033 190.411 1.00 0.07  ? 4701 ADP A PA    1 
HETATM 23599 O  O1A   . ADP B 2 .    ? 168.110 201.158 190.874 1.00 0.10  ? 4701 ADP A O1A   1 
HETATM 23600 O  O2A   . ADP B 2 .    ? 170.371 200.337 189.991 1.00 11.38 ? 4701 ADP A O2A   1 
HETATM 23601 O  O3A   . ADP B 2 .    ? 169.010 198.927 191.564 1.00 0.72  ? 4701 ADP A O3A   1 
HETATM 23602 O  "O5'" . ADP B 2 .    ? 168.233 199.223 189.244 1.00 1.64  ? 4701 ADP A "O5'" 1 
HETATM 23603 C  "C5'" . ADP B 2 .    ? 168.894 198.057 188.692 1.00 0.68  ? 4701 ADP A "C5'" 1 
HETATM 23604 C  "C4'" . ADP B 2 .    ? 168.471 197.875 187.255 1.00 0.84  ? 4701 ADP A "C4'" 1 
HETATM 23605 O  "O4'" . ADP B 2 .    ? 167.068 197.504 187.219 1.00 2.06  ? 4701 ADP A "O4'" 1 
HETATM 23606 C  "C3'" . ADP B 2 .    ? 168.581 199.120 186.365 1.00 0.86  ? 4701 ADP A "C3'" 1 
HETATM 23607 O  "O3'" . ADP B 2 .    ? 168.873 198.756 185.022 1.00 9.72  ? 4701 ADP A "O3'" 1 
HETATM 23608 C  "C2'" . ADP B 2 .    ? 167.177 199.715 186.489 1.00 0.35  ? 4701 ADP A "C2'" 1 
HETATM 23609 O  "O2'" . ADP B 2 .    ? 166.838 200.609 185.451 1.00 1.76  ? 4701 ADP A "O2'" 1 
HETATM 23610 C  "C1'" . ADP B 2 .    ? 166.341 198.441 186.459 1.00 0.82  ? 4701 ADP A "C1'" 1 
HETATM 23611 N  N9    . ADP B 2 .    ? 165.023 198.598 187.059 1.00 0.92  ? 4701 ADP A N9    1 
HETATM 23612 C  C8    . ADP B 2 .    ? 164.713 198.492 188.391 1.00 0.23  ? 4701 ADP A C8    1 
HETATM 23613 N  N7    . ADP B 2 .    ? 163.445 198.686 188.647 1.00 0.11  ? 4701 ADP A N7    1 
HETATM 23614 C  C5    . ADP B 2 .    ? 162.878 198.933 187.406 1.00 0.16  ? 4701 ADP A C5    1 
HETATM 23615 C  C6    . ADP B 2 .    ? 161.557 199.212 187.008 1.00 0.17  ? 4701 ADP A C6    1 
HETATM 23616 N  N6    . ADP B 2 .    ? 160.532 199.293 187.850 1.00 0.22  ? 4701 ADP A N6    1 
HETATM 23617 N  N1    . ADP B 2 .    ? 161.331 199.408 185.688 1.00 0.27  ? 4701 ADP A N1    1 
HETATM 23618 C  C2    . ADP B 2 .    ? 162.367 199.326 184.843 1.00 0.30  ? 4701 ADP A C2    1 
HETATM 23619 N  N3    . ADP B 2 .    ? 163.646 199.072 185.102 1.00 0.25  ? 4701 ADP A N3    1 
HETATM 23620 C  C4    . ADP B 2 .    ? 163.841 198.881 186.417 1.00 0.29  ? 4701 ADP A C4    1 
HETATM 23621 P  PG    . ATP C 3 .    ? 197.540 188.301 182.390 1.00 0.00  ? 4702 ATP A PG    1 
HETATM 23622 O  O1G   . ATP C 3 .    ? 196.581 187.328 183.014 1.00 0.13  ? 4702 ATP A O1G   1 
HETATM 23623 O  O2G   . ATP C 3 .    ? 197.054 189.721 182.456 1.00 0.08  ? 4702 ATP A O2G   1 
HETATM 23624 O  O3G   . ATP C 3 .    ? 198.937 188.148 182.907 1.00 0.32  ? 4702 ATP A O3G   1 
HETATM 23625 P  PB    . ATP C 3 .    ? 196.528 187.861 179.647 1.00 0.00  ? 4702 ATP A PB    1 
HETATM 23626 O  O1B   . ATP C 3 .    ? 195.563 186.768 179.945 1.00 0.06  ? 4702 ATP A O1B   1 
HETATM 23627 O  O2B   . ATP C 3 .    ? 196.029 189.241 179.395 1.00 0.02  ? 4702 ATP A O2B   1 
HETATM 23628 O  O3B   . ATP C 3 .    ? 197.608 187.920 180.827 1.00 0.05  ? 4702 ATP A O3B   1 
HETATM 23629 P  PA    . ATP C 3 .    ? 198.273 188.180 177.300 1.00 0.00  ? 4702 ATP A PA    1 
HETATM 23630 O  O1A   . ATP C 3 .    ? 198.765 189.470 177.859 1.00 3.21  ? 4702 ATP A O1A   1 
HETATM 23631 O  O2A   . ATP C 3 .    ? 197.460 188.225 176.052 1.00 0.02  ? 4702 ATP A O2A   1 
HETATM 23632 O  O3A   . ATP C 3 .    ? 197.449 187.396 178.427 1.00 0.03  ? 4702 ATP A O3A   1 
HETATM 23633 O  "O5'" . ATP C 3 .    ? 199.520 187.195 177.103 1.00 5.30  ? 4702 ATP A "O5'" 1 
HETATM 23634 C  "C5'" . ATP C 3 .    ? 199.347 185.937 176.410 1.00 1.34  ? 4702 ATP A "C5'" 1 
HETATM 23635 C  "C4'" . ATP C 3 .    ? 200.699 185.423 175.987 1.00 0.91  ? 4702 ATP A "C4'" 1 
HETATM 23636 O  "O4'" . ATP C 3 .    ? 200.557 184.702 174.740 1.00 4.12  ? 4702 ATP A "O4'" 1 
HETATM 23637 C  "C3'" . ATP C 3 .    ? 201.740 186.490 175.649 1.00 1.62  ? 4702 ATP A "C3'" 1 
HETATM 23638 O  "O3'" . ATP C 3 .    ? 203.048 185.938 175.609 1.00 23.47 ? 4702 ATP A "O3'" 1 
HETATM 23639 C  "C2'" . ATP C 3 .    ? 201.275 186.909 174.253 1.00 1.27  ? 4702 ATP A "C2'" 1 
HETATM 23640 O  "O2'" . ATP C 3 .    ? 202.302 187.477 173.470 1.00 11.03 ? 4702 ATP A "O2'" 1 
HETATM 23641 C  "C1'" . ATP C 3 .    ? 200.785 185.585 173.665 1.00 1.12  ? 4702 ATP A "C1'" 1 
HETATM 23642 N  N9    . ATP C 3 .    ? 199.542 185.723 172.918 1.00 0.46  ? 4702 ATP A N9    1 
HETATM 23643 C  C8    . ATP C 3 .    ? 198.377 186.311 173.339 1.00 0.22  ? 4702 ATP A C8    1 
HETATM 23644 N  N7    . ATP C 3 .    ? 197.439 186.288 172.421 1.00 0.30  ? 4702 ATP A N7    1 
HETATM 23645 C  C5    . ATP C 3 .    ? 198.033 185.666 171.331 1.00 0.33  ? 4702 ATP A C5    1 
HETATM 23646 C  C6    . ATP C 3 .    ? 197.560 185.343 170.045 1.00 0.46  ? 4702 ATP A C6    1 
HETATM 23647 N  N6    . ATP C 3 .    ? 196.331 185.618 169.620 1.00 0.46  ? 4702 ATP A N6    1 
HETATM 23648 N  N1    . ATP C 3 .    ? 198.419 184.719 169.206 1.00 0.79  ? 4702 ATP A N1    1 
HETATM 23649 C  C2    . ATP C 3 .    ? 199.656 184.446 169.640 1.00 0.73  ? 4702 ATP A C2    1 
HETATM 23650 N  N3    . ATP C 3 .    ? 200.209 184.703 170.822 1.00 0.84  ? 4702 ATP A N3    1 
HETATM 23651 C  C4    . ATP C 3 .    ? 199.331 185.319 171.630 1.00 0.42  ? 4702 ATP A C4    1 
HETATM 23652 P  PB    . ADP D 2 .    ? 220.375 182.904 201.356 1.00 0.01  ? 4703 ADP A PB    1 
HETATM 23653 O  O1B   . ADP D 2 .    ? 220.475 183.919 200.254 1.00 1.10  ? 4703 ADP A O1B   1 
HETATM 23654 O  O2B   . ADP D 2 .    ? 219.649 183.423 202.564 1.00 1.80  ? 4703 ADP A O2B   1 
HETATM 23655 O  O3B   . ADP D 2 .    ? 219.841 181.580 200.876 1.00 0.24  ? 4703 ADP A O3B   1 
HETATM 23656 P  PA    . ADP D 2 .    ? 223.239 183.460 201.733 1.00 0.11  ? 4703 ADP A PA    1 
HETATM 23657 O  O1A   . ADP D 2 .    ? 223.720 183.423 200.322 1.00 0.29  ? 4703 ADP A O1A   1 
HETATM 23658 O  O2A   . ADP D 2 .    ? 223.015 184.793 202.364 1.00 3.75  ? 4703 ADP A O2A   1 
HETATM 23659 O  O3A   . ADP D 2 .    ? 221.885 182.611 201.833 1.00 1.85  ? 4703 ADP A O3A   1 
HETATM 23660 O  "O5'" . ADP D 2 .    ? 224.216 182.597 202.663 1.00 1.08  ? 4703 ADP A "O5'" 1 
HETATM 23661 C  "C5'" . ADP D 2 .    ? 224.487 181.217 202.324 1.00 1.21  ? 4703 ADP A "C5'" 1 
HETATM 23662 C  "C4'" . ADP D 2 .    ? 225.476 180.653 203.313 1.00 0.60  ? 4703 ADP A "C4'" 1 
HETATM 23663 O  "O4'" . ADP D 2 .    ? 225.938 179.365 202.832 1.00 0.64  ? 4703 ADP A "O4'" 1 
HETATM 23664 C  "C3'" . ADP D 2 .    ? 226.747 181.481 203.538 1.00 1.07  ? 4703 ADP A "C3'" 1 
HETATM 23665 O  "O3'" . ADP D 2 .    ? 227.211 181.336 204.874 1.00 9.37  ? 4703 ADP A "O3'" 1 
HETATM 23666 C  "C2'" . ADP D 2 .    ? 227.714 180.853 202.534 1.00 0.59  ? 4703 ADP A "C2'" 1 
HETATM 23667 O  "O2'" . ADP D 2 .    ? 229.071 181.081 202.846 1.00 3.64  ? 4703 ADP A "O2'" 1 
HETATM 23668 C  "C1'" . ADP D 2 .    ? 227.335 179.381 202.654 1.00 0.52  ? 4703 ADP A "C1'" 1 
HETATM 23669 N  N9    . ADP D 2 .    ? 227.642 178.605 201.459 1.00 0.46  ? 4703 ADP A N9    1 
HETATM 23670 C  C8    . ADP D 2 .    ? 226.830 177.665 200.878 1.00 0.38  ? 4703 ADP A C8    1 
HETATM 23671 N  N7    . ADP D 2 .    ? 227.353 177.115 199.812 1.00 0.90  ? 4703 ADP A N7    1 
HETATM 23672 C  C5    . ADP D 2 .    ? 228.593 177.722 199.684 1.00 0.43  ? 4703 ADP A C5    1 
HETATM 23673 C  C6    . ADP D 2 .    ? 229.628 177.564 198.744 1.00 0.30  ? 4703 ADP A C6    1 
HETATM 23674 N  N6    . ADP D 2 .    ? 229.574 176.716 197.722 1.00 0.58  ? 4703 ADP A N6    1 
HETATM 23675 N  N1    . ADP D 2 .    ? 230.737 178.322 198.904 1.00 0.51  ? 4703 ADP A N1    1 
HETATM 23676 C  C2    . ADP D 2 .    ? 230.784 179.174 199.937 1.00 0.57  ? 4703 ADP A C2    1 
HETATM 23677 N  N3    . ADP D 2 .    ? 229.874 179.406 200.878 1.00 0.35  ? 4703 ADP A N3    1 
HETATM 23678 C  C4    . ADP D 2 .    ? 228.787 178.641 200.697 1.00 0.31  ? 4703 ADP A C4    1 
HETATM 23679 P  PB    . ADP E 2 .    ? 216.516 194.449 231.315 1.00 0.44  ? 4704 ADP A PB    1 
HETATM 23680 O  O1B   . ADP E 2 .    ? 216.659 192.956 231.449 1.00 1.06  ? 4704 ADP A O1B   1 
HETATM 23681 O  O2B   . ADP E 2 .    ? 217.306 195.012 230.164 1.00 1.45  ? 4704 ADP A O2B   1 
HETATM 23682 O  O3B   . ADP E 2 .    ? 215.080 194.897 231.310 1.00 1.03  ? 4704 ADP A O3B   1 
HETATM 23683 P  PA    . ADP E 2 .    ? 218.121 196.335 232.902 1.00 0.14  ? 4704 ADP A PA    1 
HETATM 23684 O  O1A   . ADP E 2 .    ? 219.439 196.079 232.254 1.00 0.49  ? 4704 ADP A O1A   1 
HETATM 23685 O  O2A   . ADP E 2 .    ? 217.383 197.578 232.534 1.00 3.90  ? 4704 ADP A O2A   1 
HETATM 23686 O  O3A   . ADP E 2 .    ? 217.172 195.071 232.646 1.00 0.95  ? 4704 ADP A O3A   1 
HETATM 23687 O  "O5'" . ADP E 2 .    ? 218.287 196.268 234.494 1.00 1.57  ? 4704 ADP A "O5'" 1 
HETATM 23688 C  "C5'" . ADP E 2 .    ? 217.171 196.657 235.332 1.00 1.25  ? 4704 ADP A "C5'" 1 
HETATM 23689 C  "C4'" . ADP E 2 .    ? 217.634 196.725 236.765 1.00 1.41  ? 4704 ADP A "C4'" 1 
HETATM 23690 O  "O4'" . ADP E 2 .    ? 217.732 195.386 237.313 1.00 2.11  ? 4704 ADP A "O4'" 1 
HETATM 23691 C  "C3'" . ADP E 2 .    ? 219.028 197.314 236.995 1.00 1.91  ? 4704 ADP A "C3'" 1 
HETATM 23692 O  "O3'" . ADP E 2 .    ? 219.010 198.736 236.987 1.00 12.37 ? 4704 ADP A "O3'" 1 
HETATM 23693 C  "C2'" . ADP E 2 .    ? 219.367 196.741 238.372 1.00 2.55  ? 4704 ADP A "C2'" 1 
HETATM 23694 O  "O2'" . ADP E 2 .    ? 218.771 197.475 239.417 1.00 2.11  ? 4704 ADP A "O2'" 1 
HETATM 23695 C  "C1'" . ADP E 2 .    ? 218.762 195.342 238.278 1.00 0.76  ? 4704 ADP A "C1'" 1 
HETATM 23696 N  N9    . ADP E 2 .    ? 219.713 194.304 237.896 1.00 0.60  ? 4704 ADP A N9    1 
HETATM 23697 C  C8    . ADP E 2 .    ? 219.844 193.721 236.661 1.00 1.29  ? 4704 ADP A C8    1 
HETATM 23698 N  N7    . ADP E 2 .    ? 220.786 192.815 236.613 1.00 1.66  ? 4704 ADP A N7    1 
HETATM 23699 C  C5    . ADP E 2 .    ? 221.321 192.807 237.891 1.00 0.72  ? 4704 ADP A C5    1 
HETATM 23700 C  C6    . ADP E 2 .    ? 222.364 192.063 238.476 1.00 0.99  ? 4704 ADP A C6    1 
HETATM 23701 N  N6    . ADP E 2 .    ? 223.075 191.149 237.827 1.00 0.77  ? 4704 ADP A N6    1 
HETATM 23702 N  N1    . ADP E 2 .    ? 222.646 192.301 239.779 1.00 1.61  ? 4704 ADP A N1    1 
HETATM 23703 C  C2    . ADP E 2 .    ? 221.926 193.223 240.429 1.00 1.18  ? 4704 ADP A C2    1 
HETATM 23704 N  N3    . ADP E 2 .    ? 220.929 193.981 239.984 1.00 0.85  ? 4704 ADP A N3    1 
HETATM 23705 C  C4    . ADP E 2 .    ? 220.671 193.724 238.691 1.00 0.57  ? 4704 ADP A C4    1 
HETATM 23706 MG MG    . MG  F 4 .    ? 171.551 201.443 193.714 1.00 0.63  ? 4705 MG  A MG    1 
HETATM 23707 MG MG    . MG  G 4 .    ? 196.804 190.762 180.682 1.00 0.04  ? 4706 MG  A MG    1 
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