data_9BMR
# 
_entry.id   9BMR 
# 
_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   9BMR         pdb_00009bmr 10.2210/pdb9bmr/pdb 
WWPDB D_1000283535 ?            ?                   
EMDB  EMD-44708    ?            ?                   
# 
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                        9BMR 
_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 phi dynein-1 in 5 mM ADP' 
_pdbx_database_related.db_id          EMD-44708 
_pdbx_database_related.content_type   'associated EM volume' 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              jack.zhang@yale.edu 
_pdbx_contact_author.name_first         Jack 
_pdbx_contact_author.name_last          Zhang 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-8617-2855 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Chai, P.'  1 0000-0001-9702-978X 
'Zhang, K.' 2 0000-0001-8617-2855 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Nat.Struct.Mol.Biol. 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1545-9985 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'The mechanochemical cycle of reactive full-length human dynein 1.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s41594-025-01543-3 
_citation.pdbx_database_id_PubMed   40263469 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Chai, P.'       1 0000-0001-9702-978X 
primary 'Yang, J.'       2 ?                   
primary 'Geohring, I.C.' 3 ?                   
primary 'Markus, S.M.'   4 0000-0002-3098-0236 
primary 'Wang, Y.'       5 0000-0002-8020-3937 
primary 'Zhang, K.'      6 0000-0001-8617-2855 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Cytoplasmic dynein 1 heavy chain 1' 533083.250 1 ? ? ? ? 
2 non-polymer syn "ADENOSINE-5'-DIPHOSPHATE"           427.201    3 ? ? ? ? 
3 non-polymer syn "ADENOSINE-5'-TRIPHOSPHATE"          507.181    1 ? ? ? ? 
4 non-polymer syn 'MAGNESIUM ION'                      24.305     2 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Cytoplasmic dynein heavy chain 1,Dynein heavy chain,cytosolic' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MSEPGGGGGEDGSAGLEVSAVQNVADVSVLQKHLRKLVPLLLEDGGEAPAALEAALEEKSALEQMRKFLSDPQVHTVLVE
RSTLKEDVGDEGEEEKEFISYNINIDIHYGVKSNSLAFIKRTPVIDADKPVSSQLRVLTLSEDSPYETLHSFISNAVAPF
FKSYIRESGKADRDGDKMAPSVEKKIAELEMGLLHLQQNIEIPEISLPIHPMITNVAKQCYERGEKPKVTDFGDKVEDPT
FLNQLQSGVNRWIREIQKVTKLDRDPASGTALQEISFWLNLERALYRIQEKRESPEVLLTLDILKHGKRFHATVSFDTDT
GLKQALETVNDYNPLMKDFPLNDLLSATELDKIRQALVAIFTHLRKIRNTKYPIQRALRLVEAISRDLSSQLLKVLGTRK
LMHVAYEEFEKVMVACFEVFQTWDDEYEKLQVLLRDIVKRKREENLKMVWRINPAHRKLQARLDQMRKFRRQHEQLRAVI
VRVLRPQVTAVAQQNQGEVPEPQDMKVAEVLFDAADANAIEEVNLAYENVKEVDGLDVSKEGTEAWEAAMKRYDERIDRV
ETRITARLRDQLGTAKNANEMFRIFSRFNALFVRPHIRGAIREYQTQLIQRVKDDIESLHDKFKVQYPQSQACKMSHVRD
LPPVSGSIIWAKQIDRQLTAYMKRVEDVLGKGWENHVEGQKLKQDGDSFRMKLNTQEIFDDWARKVQQRNLGVSGRIFTI
ESTRVRGRTGNVLKLKVNFLPEIITLSKEVRNLKWLGFRVPLAIVNKAHQANQLYPFAISLIESVRTYERTCEKVEERNT
ISLLVAGLKKEVQALIAEGIALVWESYKLDPYVQRLAETVFNFQEKVDDLLIIEEKIDLEVRSLETCMYDHKTFSEILNR
VQKAVDDLNLHSYSNLPIWVNKLDMEIERILGVRLQAGLRAWTQVLLGQAEDKAEVDMDTDAPQVSHKPGGEPKIKNVVH
ELRITNQVIYLNPPIEECRYKLYQEMFAWKMVVLSLPRIQSQRYQVGVHYELTEEEKFYRNALTRMPDGPVALEESYSAV
MGIVSEVEQYVKVWLQYQCLWDMQAENIYNRLGEDLNKWQALLVQIRKARGTFDNAETKKEFGPVVIDYGKVQSKVNLKY
DSWHKEVLSKFGQMLGSNMTEFHSQISKSRQELEQHSVDTASTSDAVTFITYVQSLKRKIKQFEKQVELYRNGQRLLEKQ
RFQFPPSWLYIDNIEGEWGAFNDIMRRKDSAIQQQVANLQMKIVQEDRAVESRTTDLLTDWEKTKPVTGNLRPEEALQAL
TIYEGKFGRLKDDREKCAKAKEALELTDTGLLSGSEERVQVALEELQDLKGVWSELSKVWEQIDQMKEQPWVSVQPRKLR
QNLDALLNQLKSFPARLRQYASYEFVQRLLKGYMKINMLVIELKSEALKDRHWKQLMKRLHVNWVVSELTLGQIWDVDLQ
KNEAIVKDVLLVAQGEMALEEFLKQIREVWNTYELDLVNYQNKCRLIRGWDDLFNKVKEHINSVSAMKLSPYYKVFEEDA
LSWEDKLNRIMALFDVWIDVQRRWVYLEGIFTGSADIKHLLPVETQRFQSISTEFLALMKKVSKSPLVMDVLNIQGVQRS
LERLADLLGKIQKALGEYLERERSSFPRFYFVGDEDLLEIIGNSKNVAKLQKHFKKMFAGVSSIILNEDNSVVLGISSRE
GEEVMFKTPVSITEHPKINEWLTLVEKEMRVTLAKLLAESVTEVEIFGKATSIDPNTYITWIDKYQAQLVVLSAQIAWSE
NVETALSSMGGGGDAAPLHSVLSNVEVTLNVLADSVLMEQPPLRRRKLEHLITELVHQRDVTRSLIKSKIDNAKSFEWLS
QMRFYFDPKQTDVLQQLSIQMANAKFNYGFEYLGVQDKLVQTPLTDRCYLTMTQALEARLGGSPFGPAGTGKTESVKALG
HQLGRFVLVFNCDETFDFQAMGRIFVGLCQVGAWGCFDEFNRLEERMLSAVSQQVQCIQEALREHSNPNYDKTSAPITCE
LLNKQVKVSPDMAIFITMNPGYAGRSNLPDNLKKLFRSLAMTKPDRQLIAQVMLYSQGFRTAEVLANKIVPFFKLCDEQL
SSQSHYDFGLRALKSVLVSAGNVKRERIQKIKREKEERGEAVDEGEIAENLPEQEILIQSVCETMVPKLVAEDIPLLFSL
LSDVFPGVQYHRGEMTALREELKKVCQEMYLTYGDGEEVGGMWVEKVLQLYQITQINHGLMMVGPSGSGKSMAWRVLLKA
LERLEGVEGVAHIIDPKAISKDHLYGTLDPNTREWTDGLFTHVLRKIIDSVRGELQKRQWIVFDGDVDPEWVENLNSVLD
DNKLLTLPNGERLSLPPNVRIMFEVQDLKYATLATVSRCGMVWFSEDVLSTDMIFNNFLARLRSIPLDEGEDEAQRRRKG
KEDEGEEAASPMLQIQRDAATIMQPYFTSNGLVTKALEHAFQLEHIMDLTRLRCLGSLFSMLHQACRNVAQYNANHPDFP
MQIEQLERYIQRYLVYAILWSLSGDSRLKMRAELGEYIRRITTVPLPTAPNIPIIDYEVSISGEWSPWQAKVPQIEVETH
KVAAPDVVVPTLDTVRHEALLYTWLAEHKPLVLCGPPGSGKTMTLFSALRALPDMEVVGLNFSSATTPELLLKTFDHYCE
YRRTPNGVVLAPVQLGKWLVLFCDEINLPDMDKYGTQRVISFIRQMVEHGGFYRTSDQTWVKLERIQFVGACNPPTDPGR
KPLSHRFLRHVPVVYVDYPGPASLTQIYGTFNRAMLRLIPSLRTYAEPLTAAMVEFYTMSQERFTQDTQPHYIYSPREMT
RWVRGIFEALRPLETLPVEGLIRIWAHEALRLFQDRLVEDEERRWTDENIDTVALKHFPNIDREKAMSRPILYSNWLSKD
YIPVDQEELRDYVKARLKVFYEEELDVPLVLFNEVLDHVLRIDRIFRQPQGHLLLIGVSGAGKTTLSRFVAWMNGLSVYQ
IKVHRKYTGEDFDEDLRTVLRRSGCKNEKIAFIMDESNVLDSGFLERMNTLLANGEVPGLFEGDEYATLMTQCKEGAQKE
GLMLDSHEELYKWFTSQVIRNLHVVFTMNPSSEGLKDRAATSPALFNRCVLNWFGDWSTEALYQVGKEFTSKMDLEKPNY
IVPDYMPVVYDKLPQPPSHREAIVNSCVFVHQTLHQANARLAKRGGRTMAITPRHYLDFINHYANLFHEKRSELEEQQMH
LNVGLRKIKETVDQVEELRRDLRIKSQELEVKNAAANDKLKKMVKDQQEAEKKKVMSQEIQEQLHKQQEVIADKQMSVKE
DLDKVEPAVIEAQNAVKSIKKQHLVEVRSMANPPAAVKLALESICLLLGESTTDWKQIRSIIMRENFIPTIVNFSAEEIS
DAIREKMKKNYMSNPSYNYEIVNRASLACGPMVKWAIAQLNYADMLKRVEPLRNELQKLEDDAKDNQQKANEVEQMIRDL
EASIARYKEEYAVLISEAQAIKADLAAVEAKVNRSTALLKSLSAERERWEKTSETFKNQMSTIAGDCLLSAAFIAYAGYF
DQQMRQNLFTTWSHHLQQANIQFRTDIARTEYLSNADERLRWQASSLPADDLCTENAIMLKRFNRYPLIIDPSGQATEFI
MNEYKDRKITRTSFLDDAFRKNLESALRFGNPLLVQDVESYDPVLNPVLNREVRRTGGRVLITLGDQDIDLSPSFVIFLS
TRDPTVEFPPDLCSRVTFVNFTVTRSSLQSQCLNEVLKAERPDVDEKRSDLLKLQGEFQLRLRQLEKSLLQALNEVKGRI
LDDDTIITTLENLKREAAEVTRKVEETDIVMQEVETVSQQYLPLSTACSSIYFTMESLKQIHFLYQYSLQFFLDIYHNVL
YENPNLKGVTDHTQRLSIITKDLFQVAFNRVARGMLHQDHITFAMLLARIKLKGTVGEPTYDAEFQHFLRGNEIVLSAGS
TPRIQGLTVEQAEAVVRLSCLPAFKDLIAKVQADEQFGIWLDSSSPEQTVPYLWSEETPATPIGQAIHRLLLIQAFRPDR
LLAMAHMFVSTNLGESFMSIMEQPLDLTHIVGTEVKPNTPVLMCSVPGYDASGHVEDLAAEQNTQITSIAIGSAEGFNQA
DKAINTAVKSGRWVMLKNVHLAPGWLMQLEKKLHSLQPHACFRLFLTMEINPKVPVNLLRAGRIFVFEPPPGVKANMLRT
FSSIPVSRICKSPNERARLYFLLAWFHAIIQERLRYAPLGWSKKYEFGESDLRSACDTVDTWLDDTAKGRQNISPDKIPW
SALKTLMAQSIYGGRVDNEFDQRLLNTFLERLFTTRSFDSEFKLACKVDGHKDIQMPDGIRREEFVQWVELLPDTQTPSW
LGLPNNAERVLLTTQGVDMISKMLKMQMLEDEDDLAYAETEKKTRTDSTSDGRPAWMRTLHTTASNWLHLIPQTLSHLKR
TVENIKDPLFRFFEREVKMGAKLLQDVRQDLADVVQVCEGKKKQTNYLRTLINELVKGILPRSWSHYTVPAGMTVIQWVS
DFSERIKQLQNISLAAASGGAKELKNIHVCLGGLFVPEAYITATRQYVAQANSWSLEELCLEVNVTTSQGATLDACSFGV
TGLKLQGATCNNNKLSLSNAISTALPLTQLRWVKQTNTEKKASVVTLPVYLNFTRADLIFTVDFEIATKEDPRSFYERGV
AVLCTE
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MSEPGGGGGEDGSAGLEVSAVQNVADVSVLQKHLRKLVPLLLEDGGEAPAALEAALEEKSALEQMRKFLSDPQVHTVLVE
RSTLKEDVGDEGEEEKEFISYNINIDIHYGVKSNSLAFIKRTPVIDADKPVSSQLRVLTLSEDSPYETLHSFISNAVAPF
FKSYIRESGKADRDGDKMAPSVEKKIAELEMGLLHLQQNIEIPEISLPIHPMITNVAKQCYERGEKPKVTDFGDKVEDPT
FLNQLQSGVNRWIREIQKVTKLDRDPASGTALQEISFWLNLERALYRIQEKRESPEVLLTLDILKHGKRFHATVSFDTDT
GLKQALETVNDYNPLMKDFPLNDLLSATELDKIRQALVAIFTHLRKIRNTKYPIQRALRLVEAISRDLSSQLLKVLGTRK
LMHVAYEEFEKVMVACFEVFQTWDDEYEKLQVLLRDIVKRKREENLKMVWRINPAHRKLQARLDQMRKFRRQHEQLRAVI
VRVLRPQVTAVAQQNQGEVPEPQDMKVAEVLFDAADANAIEEVNLAYENVKEVDGLDVSKEGTEAWEAAMKRYDERIDRV
ETRITARLRDQLGTAKNANEMFRIFSRFNALFVRPHIRGAIREYQTQLIQRVKDDIESLHDKFKVQYPQSQACKMSHVRD
LPPVSGSIIWAKQIDRQLTAYMKRVEDVLGKGWENHVEGQKLKQDGDSFRMKLNTQEIFDDWARKVQQRNLGVSGRIFTI
ESTRVRGRTGNVLKLKVNFLPEIITLSKEVRNLKWLGFRVPLAIVNKAHQANQLYPFAISLIESVRTYERTCEKVEERNT
ISLLVAGLKKEVQALIAEGIALVWESYKLDPYVQRLAETVFNFQEKVDDLLIIEEKIDLEVRSLETCMYDHKTFSEILNR
VQKAVDDLNLHSYSNLPIWVNKLDMEIERILGVRLQAGLRAWTQVLLGQAEDKAEVDMDTDAPQVSHKPGGEPKIKNVVH
ELRITNQVIYLNPPIEECRYKLYQEMFAWKMVVLSLPRIQSQRYQVGVHYELTEEEKFYRNALTRMPDGPVALEESYSAV
MGIVSEVEQYVKVWLQYQCLWDMQAENIYNRLGEDLNKWQALLVQIRKARGTFDNAETKKEFGPVVIDYGKVQSKVNLKY
DSWHKEVLSKFGQMLGSNMTEFHSQISKSRQELEQHSVDTASTSDAVTFITYVQSLKRKIKQFEKQVELYRNGQRLLEKQ
RFQFPPSWLYIDNIEGEWGAFNDIMRRKDSAIQQQVANLQMKIVQEDRAVESRTTDLLTDWEKTKPVTGNLRPEEALQAL
TIYEGKFGRLKDDREKCAKAKEALELTDTGLLSGSEERVQVALEELQDLKGVWSELSKVWEQIDQMKEQPWVSVQPRKLR
QNLDALLNQLKSFPARLRQYASYEFVQRLLKGYMKINMLVIELKSEALKDRHWKQLMKRLHVNWVVSELTLGQIWDVDLQ
KNEAIVKDVLLVAQGEMALEEFLKQIREVWNTYELDLVNYQNKCRLIRGWDDLFNKVKEHINSVSAMKLSPYYKVFEEDA
LSWEDKLNRIMALFDVWIDVQRRWVYLEGIFTGSADIKHLLPVETQRFQSISTEFLALMKKVSKSPLVMDVLNIQGVQRS
LERLADLLGKIQKALGEYLERERSSFPRFYFVGDEDLLEIIGNSKNVAKLQKHFKKMFAGVSSIILNEDNSVVLGISSRE
GEEVMFKTPVSITEHPKINEWLTLVEKEMRVTLAKLLAESVTEVEIFGKATSIDPNTYITWIDKYQAQLVVLSAQIAWSE
NVETALSSMGGGGDAAPLHSVLSNVEVTLNVLADSVLMEQPPLRRRKLEHLITELVHQRDVTRSLIKSKIDNAKSFEWLS
QMRFYFDPKQTDVLQQLSIQMANAKFNYGFEYLGVQDKLVQTPLTDRCYLTMTQALEARLGGSPFGPAGTGKTESVKALG
HQLGRFVLVFNCDETFDFQAMGRIFVGLCQVGAWGCFDEFNRLEERMLSAVSQQVQCIQEALREHSNPNYDKTSAPITCE
LLNKQVKVSPDMAIFITMNPGYAGRSNLPDNLKKLFRSLAMTKPDRQLIAQVMLYSQGFRTAEVLANKIVPFFKLCDEQL
SSQSHYDFGLRALKSVLVSAGNVKRERIQKIKREKEERGEAVDEGEIAENLPEQEILIQSVCETMVPKLVAEDIPLLFSL
LSDVFPGVQYHRGEMTALREELKKVCQEMYLTYGDGEEVGGMWVEKVLQLYQITQINHGLMMVGPSGSGKSMAWRVLLKA
LERLEGVEGVAHIIDPKAISKDHLYGTLDPNTREWTDGLFTHVLRKIIDSVRGELQKRQWIVFDGDVDPEWVENLNSVLD
DNKLLTLPNGERLSLPPNVRIMFEVQDLKYATLATVSRCGMVWFSEDVLSTDMIFNNFLARLRSIPLDEGEDEAQRRRKG
KEDEGEEAASPMLQIQRDAATIMQPYFTSNGLVTKALEHAFQLEHIMDLTRLRCLGSLFSMLHQACRNVAQYNANHPDFP
MQIEQLERYIQRYLVYAILWSLSGDSRLKMRAELGEYIRRITTVPLPTAPNIPIIDYEVSISGEWSPWQAKVPQIEVETH
KVAAPDVVVPTLDTVRHEALLYTWLAEHKPLVLCGPPGSGKTMTLFSALRALPDMEVVGLNFSSATTPELLLKTFDHYCE
YRRTPNGVVLAPVQLGKWLVLFCDEINLPDMDKYGTQRVISFIRQMVEHGGFYRTSDQTWVKLERIQFVGACNPPTDPGR
KPLSHRFLRHVPVVYVDYPGPASLTQIYGTFNRAMLRLIPSLRTYAEPLTAAMVEFYTMSQERFTQDTQPHYIYSPREMT
RWVRGIFEALRPLETLPVEGLIRIWAHEALRLFQDRLVEDEERRWTDENIDTVALKHFPNIDREKAMSRPILYSNWLSKD
YIPVDQEELRDYVKARLKVFYEEELDVPLVLFNEVLDHVLRIDRIFRQPQGHLLLIGVSGAGKTTLSRFVAWMNGLSVYQ
IKVHRKYTGEDFDEDLRTVLRRSGCKNEKIAFIMDESNVLDSGFLERMNTLLANGEVPGLFEGDEYATLMTQCKEGAQKE
GLMLDSHEELYKWFTSQVIRNLHVVFTMNPSSEGLKDRAATSPALFNRCVLNWFGDWSTEALYQVGKEFTSKMDLEKPNY
IVPDYMPVVYDKLPQPPSHREAIVNSCVFVHQTLHQANARLAKRGGRTMAITPRHYLDFINHYANLFHEKRSELEEQQMH
LNVGLRKIKETVDQVEELRRDLRIKSQELEVKNAAANDKLKKMVKDQQEAEKKKVMSQEIQEQLHKQQEVIADKQMSVKE
DLDKVEPAVIEAQNAVKSIKKQHLVEVRSMANPPAAVKLALESICLLLGESTTDWKQIRSIIMRENFIPTIVNFSAEEIS
DAIREKMKKNYMSNPSYNYEIVNRASLACGPMVKWAIAQLNYADMLKRVEPLRNELQKLEDDAKDNQQKANEVEQMIRDL
EASIARYKEEYAVLISEAQAIKADLAAVEAKVNRSTALLKSLSAERERWEKTSETFKNQMSTIAGDCLLSAAFIAYAGYF
DQQMRQNLFTTWSHHLQQANIQFRTDIARTEYLSNADERLRWQASSLPADDLCTENAIMLKRFNRYPLIIDPSGQATEFI
MNEYKDRKITRTSFLDDAFRKNLESALRFGNPLLVQDVESYDPVLNPVLNREVRRTGGRVLITLGDQDIDLSPSFVIFLS
TRDPTVEFPPDLCSRVTFVNFTVTRSSLQSQCLNEVLKAERPDVDEKRSDLLKLQGEFQLRLRQLEKSLLQALNEVKGRI
LDDDTIITTLENLKREAAEVTRKVEETDIVMQEVETVSQQYLPLSTACSSIYFTMESLKQIHFLYQYSLQFFLDIYHNVL
YENPNLKGVTDHTQRLSIITKDLFQVAFNRVARGMLHQDHITFAMLLARIKLKGTVGEPTYDAEFQHFLRGNEIVLSAGS
TPRIQGLTVEQAEAVVRLSCLPAFKDLIAKVQADEQFGIWLDSSSPEQTVPYLWSEETPATPIGQAIHRLLLIQAFRPDR
LLAMAHMFVSTNLGESFMSIMEQPLDLTHIVGTEVKPNTPVLMCSVPGYDASGHVEDLAAEQNTQITSIAIGSAEGFNQA
DKAINTAVKSGRWVMLKNVHLAPGWLMQLEKKLHSLQPHACFRLFLTMEINPKVPVNLLRAGRIFVFEPPPGVKANMLRT
FSSIPVSRICKSPNERARLYFLLAWFHAIIQERLRYAPLGWSKKYEFGESDLRSACDTVDTWLDDTAKGRQNISPDKIPW
SALKTLMAQSIYGGRVDNEFDQRLLNTFLERLFTTRSFDSEFKLACKVDGHKDIQMPDGIRREEFVQWVELLPDTQTPSW
LGLPNNAERVLLTTQGVDMISKMLKMQMLEDEDDLAYAETEKKTRTDSTSDGRPAWMRTLHTTASNWLHLIPQTLSHLKR
TVENIKDPLFRFFEREVKMGAKLLQDVRQDLADVVQVCEGKKKQTNYLRTLINELVKGILPRSWSHYTVPAGMTVIQWVS
DFSERIKQLQNISLAAASGGAKELKNIHVCLGGLFVPEAYITATRQYVAQANSWSLEELCLEVNVTTSQGATLDACSFGV
TGLKLQGATCNNNKLSLSNAISTALPLTQLRWVKQTNTEKKASVVTLPVYLNFTRADLIFTVDFEIATKEDPRSFYERGV
AVLCTE
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 "ADENOSINE-5'-DIPHOSPHATE"  ADP 
3 "ADENOSINE-5'-TRIPHOSPHATE" ATP 
4 'MAGNESIUM ION'             MG  
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1    MET n 
1 2    SER n 
1 3    GLU n 
1 4    PRO n 
1 5    GLY n 
1 6    GLY n 
1 7    GLY n 
1 8    GLY n 
1 9    GLY n 
1 10   GLU n 
1 11   ASP n 
1 12   GLY n 
1 13   SER n 
1 14   ALA n 
1 15   GLY n 
1 16   LEU n 
1 17   GLU n 
1 18   VAL n 
1 19   SER n 
1 20   ALA n 
1 21   VAL n 
1 22   GLN n 
1 23   ASN n 
1 24   VAL n 
1 25   ALA n 
1 26   ASP n 
1 27   VAL n 
1 28   SER n 
1 29   VAL n 
1 30   LEU n 
1 31   GLN n 
1 32   LYS n 
1 33   HIS n 
1 34   LEU n 
1 35   ARG n 
1 36   LYS n 
1 37   LEU n 
1 38   VAL n 
1 39   PRO n 
1 40   LEU n 
1 41   LEU n 
1 42   LEU n 
1 43   GLU n 
1 44   ASP n 
1 45   GLY n 
1 46   GLY n 
1 47   GLU n 
1 48   ALA n 
1 49   PRO n 
1 50   ALA n 
1 51   ALA n 
1 52   LEU n 
1 53   GLU n 
1 54   ALA n 
1 55   ALA n 
1 56   LEU n 
1 57   GLU n 
1 58   GLU n 
1 59   LYS n 
1 60   SER n 
1 61   ALA n 
1 62   LEU n 
1 63   GLU n 
1 64   GLN n 
1 65   MET n 
1 66   ARG n 
1 67   LYS n 
1 68   PHE n 
1 69   LEU n 
1 70   SER n 
1 71   ASP n 
1 72   PRO n 
1 73   GLN n 
1 74   VAL n 
1 75   HIS n 
1 76   THR n 
1 77   VAL n 
1 78   LEU n 
1 79   VAL n 
1 80   GLU n 
1 81   ARG n 
1 82   SER n 
1 83   THR n 
1 84   LEU n 
1 85   LYS n 
1 86   GLU n 
1 87   ASP n 
1 88   VAL n 
1 89   GLY n 
1 90   ASP n 
1 91   GLU n 
1 92   GLY n 
1 93   GLU n 
1 94   GLU n 
1 95   GLU n 
1 96   LYS n 
1 97   GLU n 
1 98   PHE n 
1 99   ILE n 
1 100  SER n 
1 101  TYR n 
1 102  ASN n 
1 103  ILE n 
1 104  ASN n 
1 105  ILE n 
1 106  ASP n 
1 107  ILE n 
1 108  HIS n 
1 109  TYR n 
1 110  GLY n 
1 111  VAL n 
1 112  LYS n 
1 113  SER n 
1 114  ASN n 
1 115  SER n 
1 116  LEU n 
1 117  ALA n 
1 118  PHE n 
1 119  ILE n 
1 120  LYS n 
1 121  ARG n 
1 122  THR n 
1 123  PRO n 
1 124  VAL n 
1 125  ILE n 
1 126  ASP n 
1 127  ALA n 
1 128  ASP n 
1 129  LYS n 
1 130  PRO n 
1 131  VAL n 
1 132  SER n 
1 133  SER n 
1 134  GLN n 
1 135  LEU n 
1 136  ARG n 
1 137  VAL n 
1 138  LEU n 
1 139  THR n 
1 140  LEU n 
1 141  SER n 
1 142  GLU n 
1 143  ASP n 
1 144  SER n 
1 145  PRO n 
1 146  TYR n 
1 147  GLU n 
1 148  THR n 
1 149  LEU n 
1 150  HIS n 
1 151  SER n 
1 152  PHE n 
1 153  ILE n 
1 154  SER n 
1 155  ASN n 
1 156  ALA n 
1 157  VAL n 
1 158  ALA n 
1 159  PRO n 
1 160  PHE n 
1 161  PHE n 
1 162  LYS n 
1 163  SER n 
1 164  TYR n 
1 165  ILE n 
1 166  ARG n 
1 167  GLU n 
1 168  SER n 
1 169  GLY n 
1 170  LYS n 
1 171  ALA n 
1 172  ASP n 
1 173  ARG n 
1 174  ASP n 
1 175  GLY n 
1 176  ASP n 
1 177  LYS n 
1 178  MET n 
1 179  ALA n 
1 180  PRO n 
1 181  SER n 
1 182  VAL n 
1 183  GLU n 
1 184  LYS n 
1 185  LYS n 
1 186  ILE n 
1 187  ALA n 
1 188  GLU n 
1 189  LEU n 
1 190  GLU n 
1 191  MET n 
1 192  GLY n 
1 193  LEU n 
1 194  LEU n 
1 195  HIS n 
1 196  LEU n 
1 197  GLN n 
1 198  GLN n 
1 199  ASN n 
1 200  ILE n 
1 201  GLU n 
1 202  ILE n 
1 203  PRO n 
1 204  GLU n 
1 205  ILE n 
1 206  SER n 
1 207  LEU n 
1 208  PRO n 
1 209  ILE n 
1 210  HIS n 
1 211  PRO n 
1 212  MET n 
1 213  ILE n 
1 214  THR n 
1 215  ASN n 
1 216  VAL n 
1 217  ALA n 
1 218  LYS n 
1 219  GLN n 
1 220  CYS n 
1 221  TYR n 
1 222  GLU n 
1 223  ARG n 
1 224  GLY n 
1 225  GLU n 
1 226  LYS n 
1 227  PRO n 
1 228  LYS n 
1 229  VAL n 
1 230  THR n 
1 231  ASP n 
1 232  PHE n 
1 233  GLY n 
1 234  ASP n 
1 235  LYS n 
1 236  VAL n 
1 237  GLU n 
1 238  ASP n 
1 239  PRO n 
1 240  THR n 
1 241  PHE n 
1 242  LEU n 
1 243  ASN n 
1 244  GLN n 
1 245  LEU n 
1 246  GLN n 
1 247  SER n 
1 248  GLY n 
1 249  VAL n 
1 250  ASN n 
1 251  ARG n 
1 252  TRP n 
1 253  ILE n 
1 254  ARG n 
1 255  GLU n 
1 256  ILE n 
1 257  GLN n 
1 258  LYS n 
1 259  VAL n 
1 260  THR n 
1 261  LYS n 
1 262  LEU n 
1 263  ASP n 
1 264  ARG n 
1 265  ASP n 
1 266  PRO n 
1 267  ALA n 
1 268  SER n 
1 269  GLY n 
1 270  THR n 
1 271  ALA n 
1 272  LEU n 
1 273  GLN n 
1 274  GLU n 
1 275  ILE n 
1 276  SER n 
1 277  PHE n 
1 278  TRP n 
1 279  LEU n 
1 280  ASN n 
1 281  LEU n 
1 282  GLU n 
1 283  ARG n 
1 284  ALA n 
1 285  LEU n 
1 286  TYR n 
1 287  ARG n 
1 288  ILE n 
1 289  GLN n 
1 290  GLU n 
1 291  LYS n 
1 292  ARG n 
1 293  GLU n 
1 294  SER n 
1 295  PRO n 
1 296  GLU n 
1 297  VAL n 
1 298  LEU n 
1 299  LEU n 
1 300  THR n 
1 301  LEU n 
1 302  ASP n 
1 303  ILE n 
1 304  LEU n 
1 305  LYS n 
1 306  HIS n 
1 307  GLY n 
1 308  LYS n 
1 309  ARG n 
1 310  PHE n 
1 311  HIS n 
1 312  ALA n 
1 313  THR n 
1 314  VAL n 
1 315  SER n 
1 316  PHE n 
1 317  ASP n 
1 318  THR n 
1 319  ASP n 
1 320  THR n 
1 321  GLY n 
1 322  LEU n 
1 323  LYS n 
1 324  GLN n 
1 325  ALA n 
1 326  LEU n 
1 327  GLU n 
1 328  THR n 
1 329  VAL n 
1 330  ASN n 
1 331  ASP n 
1 332  TYR n 
1 333  ASN n 
1 334  PRO n 
1 335  LEU n 
1 336  MET n 
1 337  LYS n 
1 338  ASP n 
1 339  PHE n 
1 340  PRO n 
1 341  LEU n 
1 342  ASN n 
1 343  ASP n 
1 344  LEU n 
1 345  LEU n 
1 346  SER n 
1 347  ALA n 
1 348  THR n 
1 349  GLU n 
1 350  LEU n 
1 351  ASP n 
1 352  LYS n 
1 353  ILE n 
1 354  ARG n 
1 355  GLN n 
1 356  ALA n 
1 357  LEU n 
1 358  VAL n 
1 359  ALA n 
1 360  ILE n 
1 361  PHE n 
1 362  THR n 
1 363  HIS n 
1 364  LEU n 
1 365  ARG n 
1 366  LYS n 
1 367  ILE n 
1 368  ARG n 
1 369  ASN n 
1 370  THR n 
1 371  LYS n 
1 372  TYR n 
1 373  PRO n 
1 374  ILE n 
1 375  GLN n 
1 376  ARG n 
1 377  ALA n 
1 378  LEU n 
1 379  ARG n 
1 380  LEU n 
1 381  VAL n 
1 382  GLU n 
1 383  ALA n 
1 384  ILE n 
1 385  SER n 
1 386  ARG n 
1 387  ASP n 
1 388  LEU n 
1 389  SER n 
1 390  SER n 
1 391  GLN n 
1 392  LEU n 
1 393  LEU n 
1 394  LYS n 
1 395  VAL n 
1 396  LEU n 
1 397  GLY n 
1 398  THR n 
1 399  ARG n 
1 400  LYS n 
1 401  LEU n 
1 402  MET n 
1 403  HIS n 
1 404  VAL n 
1 405  ALA n 
1 406  TYR n 
1 407  GLU n 
1 408  GLU n 
1 409  PHE n 
1 410  GLU n 
1 411  LYS n 
1 412  VAL n 
1 413  MET n 
1 414  VAL n 
1 415  ALA n 
1 416  CYS n 
1 417  PHE n 
1 418  GLU n 
1 419  VAL n 
1 420  PHE n 
1 421  GLN n 
1 422  THR n 
1 423  TRP n 
1 424  ASP n 
1 425  ASP n 
1 426  GLU n 
1 427  TYR n 
1 428  GLU n 
1 429  LYS n 
1 430  LEU n 
1 431  GLN n 
1 432  VAL n 
1 433  LEU n 
1 434  LEU n 
1 435  ARG n 
1 436  ASP n 
1 437  ILE n 
1 438  VAL n 
1 439  LYS n 
1 440  ARG n 
1 441  LYS n 
1 442  ARG n 
1 443  GLU n 
1 444  GLU n 
1 445  ASN n 
1 446  LEU n 
1 447  LYS n 
1 448  MET n 
1 449  VAL n 
1 450  TRP n 
1 451  ARG n 
1 452  ILE n 
1 453  ASN n 
1 454  PRO n 
1 455  ALA n 
1 456  HIS n 
1 457  ARG n 
1 458  LYS n 
1 459  LEU n 
1 460  GLN n 
1 461  ALA n 
1 462  ARG n 
1 463  LEU n 
1 464  ASP n 
1 465  GLN n 
1 466  MET n 
1 467  ARG n 
1 468  LYS n 
1 469  PHE n 
1 470  ARG n 
1 471  ARG n 
1 472  GLN n 
1 473  HIS n 
1 474  GLU n 
1 475  GLN n 
1 476  LEU n 
1 477  ARG n 
1 478  ALA n 
1 479  VAL n 
1 480  ILE n 
1 481  VAL n 
1 482  ARG n 
1 483  VAL n 
1 484  LEU n 
1 485  ARG n 
1 486  PRO n 
1 487  GLN n 
1 488  VAL n 
1 489  THR n 
1 490  ALA n 
1 491  VAL n 
1 492  ALA n 
1 493  GLN n 
1 494  GLN n 
1 495  ASN n 
1 496  GLN n 
1 497  GLY n 
1 498  GLU n 
1 499  VAL n 
1 500  PRO n 
1 501  GLU n 
1 502  PRO n 
1 503  GLN n 
1 504  ASP n 
1 505  MET n 
1 506  LYS n 
1 507  VAL n 
1 508  ALA n 
1 509  GLU n 
1 510  VAL n 
1 511  LEU n 
1 512  PHE n 
1 513  ASP n 
1 514  ALA n 
1 515  ALA n 
1 516  ASP n 
1 517  ALA n 
1 518  ASN n 
1 519  ALA n 
1 520  ILE n 
1 521  GLU n 
1 522  GLU n 
1 523  VAL n 
1 524  ASN n 
1 525  LEU n 
1 526  ALA n 
1 527  TYR n 
1 528  GLU n 
1 529  ASN n 
1 530  VAL n 
1 531  LYS n 
1 532  GLU n 
1 533  VAL n 
1 534  ASP n 
1 535  GLY n 
1 536  LEU n 
1 537  ASP n 
1 538  VAL n 
1 539  SER n 
1 540  LYS n 
1 541  GLU n 
1 542  GLY n 
1 543  THR n 
1 544  GLU n 
1 545  ALA n 
1 546  TRP n 
1 547  GLU n 
1 548  ALA n 
1 549  ALA n 
1 550  MET n 
1 551  LYS n 
1 552  ARG n 
1 553  TYR n 
1 554  ASP n 
1 555  GLU n 
1 556  ARG n 
1 557  ILE n 
1 558  ASP n 
1 559  ARG n 
1 560  VAL n 
1 561  GLU n 
1 562  THR n 
1 563  ARG n 
1 564  ILE n 
1 565  THR n 
1 566  ALA n 
1 567  ARG n 
1 568  LEU n 
1 569  ARG n 
1 570  ASP n 
1 571  GLN n 
1 572  LEU n 
1 573  GLY n 
1 574  THR n 
1 575  ALA n 
1 576  LYS n 
1 577  ASN n 
1 578  ALA n 
1 579  ASN n 
1 580  GLU n 
1 581  MET n 
1 582  PHE n 
1 583  ARG n 
1 584  ILE n 
1 585  PHE n 
1 586  SER n 
1 587  ARG n 
1 588  PHE n 
1 589  ASN n 
1 590  ALA n 
1 591  LEU n 
1 592  PHE n 
1 593  VAL n 
1 594  ARG n 
1 595  PRO n 
1 596  HIS n 
1 597  ILE n 
1 598  ARG n 
1 599  GLY n 
1 600  ALA n 
1 601  ILE n 
1 602  ARG n 
1 603  GLU n 
1 604  TYR n 
1 605  GLN n 
1 606  THR n 
1 607  GLN n 
1 608  LEU n 
1 609  ILE n 
1 610  GLN n 
1 611  ARG n 
1 612  VAL n 
1 613  LYS n 
1 614  ASP n 
1 615  ASP n 
1 616  ILE n 
1 617  GLU n 
1 618  SER n 
1 619  LEU n 
1 620  HIS n 
1 621  ASP n 
1 622  LYS n 
1 623  PHE n 
1 624  LYS n 
1 625  VAL n 
1 626  GLN n 
1 627  TYR n 
1 628  PRO n 
1 629  GLN n 
1 630  SER n 
1 631  GLN n 
1 632  ALA n 
1 633  CYS n 
1 634  LYS n 
1 635  MET n 
1 636  SER n 
1 637  HIS n 
1 638  VAL n 
1 639  ARG n 
1 640  ASP n 
1 641  LEU n 
1 642  PRO n 
1 643  PRO n 
1 644  VAL n 
1 645  SER n 
1 646  GLY n 
1 647  SER n 
1 648  ILE n 
1 649  ILE n 
1 650  TRP n 
1 651  ALA n 
1 652  LYS n 
1 653  GLN n 
1 654  ILE n 
1 655  ASP n 
1 656  ARG n 
1 657  GLN n 
1 658  LEU n 
1 659  THR n 
1 660  ALA n 
1 661  TYR n 
1 662  MET n 
1 663  LYS n 
1 664  ARG n 
1 665  VAL n 
1 666  GLU n 
1 667  ASP n 
1 668  VAL n 
1 669  LEU n 
1 670  GLY n 
1 671  LYS n 
1 672  GLY n 
1 673  TRP n 
1 674  GLU n 
1 675  ASN n 
1 676  HIS n 
1 677  VAL n 
1 678  GLU n 
1 679  GLY n 
1 680  GLN n 
1 681  LYS n 
1 682  LEU n 
1 683  LYS n 
1 684  GLN n 
1 685  ASP n 
1 686  GLY n 
1 687  ASP n 
1 688  SER n 
1 689  PHE n 
1 690  ARG n 
1 691  MET n 
1 692  LYS n 
1 693  LEU n 
1 694  ASN n 
1 695  THR n 
1 696  GLN n 
1 697  GLU n 
1 698  ILE n 
1 699  PHE n 
1 700  ASP n 
1 701  ASP n 
1 702  TRP n 
1 703  ALA n 
1 704  ARG n 
1 705  LYS n 
1 706  VAL n 
1 707  GLN n 
1 708  GLN n 
1 709  ARG n 
1 710  ASN n 
1 711  LEU n 
1 712  GLY n 
1 713  VAL n 
1 714  SER n 
1 715  GLY n 
1 716  ARG n 
1 717  ILE n 
1 718  PHE n 
1 719  THR n 
1 720  ILE n 
1 721  GLU n 
1 722  SER n 
1 723  THR n 
1 724  ARG n 
1 725  VAL n 
1 726  ARG n 
1 727  GLY n 
1 728  ARG n 
1 729  THR n 
1 730  GLY n 
1 731  ASN n 
1 732  VAL n 
1 733  LEU n 
1 734  LYS n 
1 735  LEU n 
1 736  LYS n 
1 737  VAL n 
1 738  ASN n 
1 739  PHE n 
1 740  LEU n 
1 741  PRO n 
1 742  GLU n 
1 743  ILE n 
1 744  ILE n 
1 745  THR n 
1 746  LEU n 
1 747  SER n 
1 748  LYS n 
1 749  GLU n 
1 750  VAL n 
1 751  ARG n 
1 752  ASN n 
1 753  LEU n 
1 754  LYS n 
1 755  TRP n 
1 756  LEU n 
1 757  GLY n 
1 758  PHE n 
1 759  ARG n 
1 760  VAL n 
1 761  PRO n 
1 762  LEU n 
1 763  ALA n 
1 764  ILE n 
1 765  VAL n 
1 766  ASN n 
1 767  LYS n 
1 768  ALA n 
1 769  HIS n 
1 770  GLN n 
1 771  ALA n 
1 772  ASN n 
1 773  GLN n 
1 774  LEU n 
1 775  TYR n 
1 776  PRO n 
1 777  PHE n 
1 778  ALA n 
1 779  ILE n 
1 780  SER n 
1 781  LEU n 
1 782  ILE n 
1 783  GLU n 
1 784  SER n 
1 785  VAL n 
1 786  ARG n 
1 787  THR n 
1 788  TYR n 
1 789  GLU n 
1 790  ARG n 
1 791  THR n 
1 792  CYS n 
1 793  GLU n 
1 794  LYS n 
1 795  VAL n 
1 796  GLU n 
1 797  GLU n 
1 798  ARG n 
1 799  ASN n 
1 800  THR n 
1 801  ILE n 
1 802  SER n 
1 803  LEU n 
1 804  LEU n 
1 805  VAL n 
1 806  ALA n 
1 807  GLY n 
1 808  LEU n 
1 809  LYS n 
1 810  LYS n 
1 811  GLU n 
1 812  VAL n 
1 813  GLN n 
1 814  ALA n 
1 815  LEU n 
1 816  ILE n 
1 817  ALA n 
1 818  GLU n 
1 819  GLY n 
1 820  ILE n 
1 821  ALA n 
1 822  LEU n 
1 823  VAL n 
1 824  TRP n 
1 825  GLU n 
1 826  SER n 
1 827  TYR n 
1 828  LYS n 
1 829  LEU n 
1 830  ASP n 
1 831  PRO n 
1 832  TYR n 
1 833  VAL n 
1 834  GLN n 
1 835  ARG n 
1 836  LEU n 
1 837  ALA n 
1 838  GLU n 
1 839  THR n 
1 840  VAL n 
1 841  PHE n 
1 842  ASN n 
1 843  PHE n 
1 844  GLN n 
1 845  GLU n 
1 846  LYS n 
1 847  VAL n 
1 848  ASP n 
1 849  ASP n 
1 850  LEU n 
1 851  LEU n 
1 852  ILE n 
1 853  ILE n 
1 854  GLU n 
1 855  GLU n 
1 856  LYS n 
1 857  ILE n 
1 858  ASP n 
1 859  LEU n 
1 860  GLU n 
1 861  VAL n 
1 862  ARG n 
1 863  SER n 
1 864  LEU n 
1 865  GLU n 
1 866  THR n 
1 867  CYS n 
1 868  MET n 
1 869  TYR n 
1 870  ASP n 
1 871  HIS n 
1 872  LYS n 
1 873  THR n 
1 874  PHE n 
1 875  SER n 
1 876  GLU n 
1 877  ILE n 
1 878  LEU n 
1 879  ASN n 
1 880  ARG n 
1 881  VAL n 
1 882  GLN n 
1 883  LYS n 
1 884  ALA n 
1 885  VAL n 
1 886  ASP n 
1 887  ASP n 
1 888  LEU n 
1 889  ASN n 
1 890  LEU n 
1 891  HIS n 
1 892  SER n 
1 893  TYR n 
1 894  SER n 
1 895  ASN n 
1 896  LEU n 
1 897  PRO n 
1 898  ILE n 
1 899  TRP n 
1 900  VAL n 
1 901  ASN n 
1 902  LYS n 
1 903  LEU n 
1 904  ASP n 
1 905  MET n 
1 906  GLU n 
1 907  ILE n 
1 908  GLU n 
1 909  ARG n 
1 910  ILE n 
1 911  LEU n 
1 912  GLY n 
1 913  VAL n 
1 914  ARG n 
1 915  LEU n 
1 916  GLN n 
1 917  ALA n 
1 918  GLY n 
1 919  LEU n 
1 920  ARG n 
1 921  ALA n 
1 922  TRP n 
1 923  THR n 
1 924  GLN n 
1 925  VAL n 
1 926  LEU n 
1 927  LEU n 
1 928  GLY n 
1 929  GLN n 
1 930  ALA n 
1 931  GLU n 
1 932  ASP n 
1 933  LYS n 
1 934  ALA n 
1 935  GLU n 
1 936  VAL n 
1 937  ASP n 
1 938  MET n 
1 939  ASP n 
1 940  THR n 
1 941  ASP n 
1 942  ALA n 
1 943  PRO n 
1 944  GLN n 
1 945  VAL n 
1 946  SER n 
1 947  HIS n 
1 948  LYS n 
1 949  PRO n 
1 950  GLY n 
1 951  GLY n 
1 952  GLU n 
1 953  PRO n 
1 954  LYS n 
1 955  ILE n 
1 956  LYS n 
1 957  ASN n 
1 958  VAL n 
1 959  VAL n 
1 960  HIS n 
1 961  GLU n 
1 962  LEU n 
1 963  ARG n 
1 964  ILE n 
1 965  THR n 
1 966  ASN n 
1 967  GLN n 
1 968  VAL n 
1 969  ILE n 
1 970  TYR n 
1 971  LEU n 
1 972  ASN n 
1 973  PRO n 
1 974  PRO n 
1 975  ILE n 
1 976  GLU n 
1 977  GLU n 
1 978  CYS n 
1 979  ARG n 
1 980  TYR n 
1 981  LYS n 
1 982  LEU n 
1 983  TYR n 
1 984  GLN n 
1 985  GLU n 
1 986  MET n 
1 987  PHE n 
1 988  ALA n 
1 989  TRP n 
1 990  LYS n 
1 991  MET n 
1 992  VAL n 
1 993  VAL n 
1 994  LEU n 
1 995  SER n 
1 996  LEU n 
1 997  PRO n 
1 998  ARG n 
1 999  ILE n 
1 1000 GLN n 
1 1001 SER n 
1 1002 GLN n 
1 1003 ARG n 
1 1004 TYR n 
1 1005 GLN n 
1 1006 VAL n 
1 1007 GLY n 
1 1008 VAL n 
1 1009 HIS n 
1 1010 TYR n 
1 1011 GLU n 
1 1012 LEU n 
1 1013 THR n 
1 1014 GLU n 
1 1015 GLU n 
1 1016 GLU n 
1 1017 LYS n 
1 1018 PHE n 
1 1019 TYR n 
1 1020 ARG n 
1 1021 ASN n 
1 1022 ALA n 
1 1023 LEU n 
1 1024 THR n 
1 1025 ARG n 
1 1026 MET n 
1 1027 PRO n 
1 1028 ASP n 
1 1029 GLY n 
1 1030 PRO n 
1 1031 VAL n 
1 1032 ALA n 
1 1033 LEU n 
1 1034 GLU n 
1 1035 GLU n 
1 1036 SER n 
1 1037 TYR n 
1 1038 SER n 
1 1039 ALA n 
1 1040 VAL n 
1 1041 MET n 
1 1042 GLY n 
1 1043 ILE n 
1 1044 VAL n 
1 1045 SER n 
1 1046 GLU n 
1 1047 VAL n 
1 1048 GLU n 
1 1049 GLN n 
1 1050 TYR n 
1 1051 VAL n 
1 1052 LYS n 
1 1053 VAL n 
1 1054 TRP n 
1 1055 LEU n 
1 1056 GLN n 
1 1057 TYR n 
1 1058 GLN n 
1 1059 CYS n 
1 1060 LEU n 
1 1061 TRP n 
1 1062 ASP n 
1 1063 MET n 
1 1064 GLN n 
1 1065 ALA n 
1 1066 GLU n 
1 1067 ASN n 
1 1068 ILE n 
1 1069 TYR n 
1 1070 ASN n 
1 1071 ARG n 
1 1072 LEU n 
1 1073 GLY n 
1 1074 GLU n 
1 1075 ASP n 
1 1076 LEU n 
1 1077 ASN n 
1 1078 LYS n 
1 1079 TRP n 
1 1080 GLN n 
1 1081 ALA n 
1 1082 LEU n 
1 1083 LEU n 
1 1084 VAL n 
1 1085 GLN n 
1 1086 ILE n 
1 1087 ARG n 
1 1088 LYS n 
1 1089 ALA n 
1 1090 ARG n 
1 1091 GLY n 
1 1092 THR n 
1 1093 PHE n 
1 1094 ASP n 
1 1095 ASN n 
1 1096 ALA n 
1 1097 GLU n 
1 1098 THR n 
1 1099 LYS n 
1 1100 LYS n 
1 1101 GLU n 
1 1102 PHE n 
1 1103 GLY n 
1 1104 PRO n 
1 1105 VAL n 
1 1106 VAL n 
1 1107 ILE n 
1 1108 ASP n 
1 1109 TYR n 
1 1110 GLY n 
1 1111 LYS n 
1 1112 VAL n 
1 1113 GLN n 
1 1114 SER n 
1 1115 LYS n 
1 1116 VAL n 
1 1117 ASN n 
1 1118 LEU n 
1 1119 LYS n 
1 1120 TYR n 
1 1121 ASP n 
1 1122 SER n 
1 1123 TRP n 
1 1124 HIS n 
1 1125 LYS n 
1 1126 GLU n 
1 1127 VAL n 
1 1128 LEU n 
1 1129 SER n 
1 1130 LYS n 
1 1131 PHE n 
1 1132 GLY n 
1 1133 GLN n 
1 1134 MET n 
1 1135 LEU n 
1 1136 GLY n 
1 1137 SER n 
1 1138 ASN n 
1 1139 MET n 
1 1140 THR n 
1 1141 GLU n 
1 1142 PHE n 
1 1143 HIS n 
1 1144 SER n 
1 1145 GLN n 
1 1146 ILE n 
1 1147 SER n 
1 1148 LYS n 
1 1149 SER n 
1 1150 ARG n 
1 1151 GLN n 
1 1152 GLU n 
1 1153 LEU n 
1 1154 GLU n 
1 1155 GLN n 
1 1156 HIS n 
1 1157 SER n 
1 1158 VAL n 
1 1159 ASP n 
1 1160 THR n 
1 1161 ALA n 
1 1162 SER n 
1 1163 THR n 
1 1164 SER n 
1 1165 ASP n 
1 1166 ALA n 
1 1167 VAL n 
1 1168 THR n 
1 1169 PHE n 
1 1170 ILE n 
1 1171 THR n 
1 1172 TYR n 
1 1173 VAL n 
1 1174 GLN n 
1 1175 SER n 
1 1176 LEU n 
1 1177 LYS n 
1 1178 ARG n 
1 1179 LYS n 
1 1180 ILE n 
1 1181 LYS n 
1 1182 GLN n 
1 1183 PHE n 
1 1184 GLU n 
1 1185 LYS n 
1 1186 GLN n 
1 1187 VAL n 
1 1188 GLU n 
1 1189 LEU n 
1 1190 TYR n 
1 1191 ARG n 
1 1192 ASN n 
1 1193 GLY n 
1 1194 GLN n 
1 1195 ARG n 
1 1196 LEU n 
1 1197 LEU n 
1 1198 GLU n 
1 1199 LYS n 
1 1200 GLN n 
1 1201 ARG n 
1 1202 PHE n 
1 1203 GLN n 
1 1204 PHE n 
1 1205 PRO n 
1 1206 PRO n 
1 1207 SER n 
1 1208 TRP n 
1 1209 LEU n 
1 1210 TYR n 
1 1211 ILE n 
1 1212 ASP n 
1 1213 ASN n 
1 1214 ILE n 
1 1215 GLU n 
1 1216 GLY n 
1 1217 GLU n 
1 1218 TRP n 
1 1219 GLY n 
1 1220 ALA n 
1 1221 PHE n 
1 1222 ASN n 
1 1223 ASP n 
1 1224 ILE n 
1 1225 MET n 
1 1226 ARG n 
1 1227 ARG n 
1 1228 LYS n 
1 1229 ASP n 
1 1230 SER n 
1 1231 ALA n 
1 1232 ILE n 
1 1233 GLN n 
1 1234 GLN n 
1 1235 GLN n 
1 1236 VAL n 
1 1237 ALA n 
1 1238 ASN n 
1 1239 LEU n 
1 1240 GLN n 
1 1241 MET n 
1 1242 LYS n 
1 1243 ILE n 
1 1244 VAL n 
1 1245 GLN n 
1 1246 GLU n 
1 1247 ASP n 
1 1248 ARG n 
1 1249 ALA n 
1 1250 VAL n 
1 1251 GLU n 
1 1252 SER n 
1 1253 ARG n 
1 1254 THR n 
1 1255 THR n 
1 1256 ASP n 
1 1257 LEU n 
1 1258 LEU n 
1 1259 THR n 
1 1260 ASP n 
1 1261 TRP n 
1 1262 GLU n 
1 1263 LYS n 
1 1264 THR n 
1 1265 LYS n 
1 1266 PRO n 
1 1267 VAL n 
1 1268 THR n 
1 1269 GLY n 
1 1270 ASN n 
1 1271 LEU n 
1 1272 ARG n 
1 1273 PRO n 
1 1274 GLU n 
1 1275 GLU n 
1 1276 ALA n 
1 1277 LEU n 
1 1278 GLN n 
1 1279 ALA n 
1 1280 LEU n 
1 1281 THR n 
1 1282 ILE n 
1 1283 TYR n 
1 1284 GLU n 
1 1285 GLY n 
1 1286 LYS n 
1 1287 PHE n 
1 1288 GLY n 
1 1289 ARG n 
1 1290 LEU n 
1 1291 LYS n 
1 1292 ASP n 
1 1293 ASP n 
1 1294 ARG n 
1 1295 GLU n 
1 1296 LYS n 
1 1297 CYS n 
1 1298 ALA n 
1 1299 LYS n 
1 1300 ALA n 
1 1301 LYS n 
1 1302 GLU n 
1 1303 ALA n 
1 1304 LEU n 
1 1305 GLU n 
1 1306 LEU n 
1 1307 THR n 
1 1308 ASP n 
1 1309 THR n 
1 1310 GLY n 
1 1311 LEU n 
1 1312 LEU n 
1 1313 SER n 
1 1314 GLY n 
1 1315 SER n 
1 1316 GLU n 
1 1317 GLU n 
1 1318 ARG n 
1 1319 VAL n 
1 1320 GLN n 
1 1321 VAL n 
1 1322 ALA n 
1 1323 LEU n 
1 1324 GLU n 
1 1325 GLU n 
1 1326 LEU n 
1 1327 GLN n 
1 1328 ASP n 
1 1329 LEU n 
1 1330 LYS n 
1 1331 GLY n 
1 1332 VAL n 
1 1333 TRP n 
1 1334 SER n 
1 1335 GLU n 
1 1336 LEU n 
1 1337 SER n 
1 1338 LYS n 
1 1339 VAL n 
1 1340 TRP n 
1 1341 GLU n 
1 1342 GLN n 
1 1343 ILE n 
1 1344 ASP n 
1 1345 GLN n 
1 1346 MET n 
1 1347 LYS n 
1 1348 GLU n 
1 1349 GLN n 
1 1350 PRO n 
1 1351 TRP n 
1 1352 VAL n 
1 1353 SER n 
1 1354 VAL n 
1 1355 GLN n 
1 1356 PRO n 
1 1357 ARG n 
1 1358 LYS n 
1 1359 LEU n 
1 1360 ARG n 
1 1361 GLN n 
1 1362 ASN n 
1 1363 LEU n 
1 1364 ASP n 
1 1365 ALA n 
1 1366 LEU n 
1 1367 LEU n 
1 1368 ASN n 
1 1369 GLN n 
1 1370 LEU n 
1 1371 LYS n 
1 1372 SER n 
1 1373 PHE n 
1 1374 PRO n 
1 1375 ALA n 
1 1376 ARG n 
1 1377 LEU n 
1 1378 ARG n 
1 1379 GLN n 
1 1380 TYR n 
1 1381 ALA n 
1 1382 SER n 
1 1383 TYR n 
1 1384 GLU n 
1 1385 PHE n 
1 1386 VAL n 
1 1387 GLN n 
1 1388 ARG n 
1 1389 LEU n 
1 1390 LEU n 
1 1391 LYS n 
1 1392 GLY n 
1 1393 TYR n 
1 1394 MET n 
1 1395 LYS n 
1 1396 ILE n 
1 1397 ASN n 
1 1398 MET n 
1 1399 LEU n 
1 1400 VAL n 
1 1401 ILE n 
1 1402 GLU n 
1 1403 LEU n 
1 1404 LYS n 
1 1405 SER n 
1 1406 GLU n 
1 1407 ALA n 
1 1408 LEU n 
1 1409 LYS n 
1 1410 ASP n 
1 1411 ARG n 
1 1412 HIS n 
1 1413 TRP n 
1 1414 LYS n 
1 1415 GLN n 
1 1416 LEU n 
1 1417 MET n 
1 1418 LYS n 
1 1419 ARG n 
1 1420 LEU n 
1 1421 HIS n 
1 1422 VAL n 
1 1423 ASN n 
1 1424 TRP n 
1 1425 VAL n 
1 1426 VAL n 
1 1427 SER n 
1 1428 GLU n 
1 1429 LEU n 
1 1430 THR n 
1 1431 LEU n 
1 1432 GLY n 
1 1433 GLN n 
1 1434 ILE n 
1 1435 TRP n 
1 1436 ASP n 
1 1437 VAL n 
1 1438 ASP n 
1 1439 LEU n 
1 1440 GLN n 
1 1441 LYS n 
1 1442 ASN n 
1 1443 GLU n 
1 1444 ALA n 
1 1445 ILE n 
1 1446 VAL n 
1 1447 LYS n 
1 1448 ASP n 
1 1449 VAL n 
1 1450 LEU n 
1 1451 LEU n 
1 1452 VAL n 
1 1453 ALA n 
1 1454 GLN n 
1 1455 GLY n 
1 1456 GLU n 
1 1457 MET n 
1 1458 ALA n 
1 1459 LEU n 
1 1460 GLU n 
1 1461 GLU n 
1 1462 PHE n 
1 1463 LEU n 
1 1464 LYS n 
1 1465 GLN n 
1 1466 ILE n 
1 1467 ARG n 
1 1468 GLU n 
1 1469 VAL n 
1 1470 TRP n 
1 1471 ASN n 
1 1472 THR n 
1 1473 TYR n 
1 1474 GLU n 
1 1475 LEU n 
1 1476 ASP n 
1 1477 LEU n 
1 1478 VAL n 
1 1479 ASN n 
1 1480 TYR n 
1 1481 GLN n 
1 1482 ASN n 
1 1483 LYS n 
1 1484 CYS n 
1 1485 ARG n 
1 1486 LEU n 
1 1487 ILE n 
1 1488 ARG n 
1 1489 GLY n 
1 1490 TRP n 
1 1491 ASP n 
1 1492 ASP n 
1 1493 LEU n 
1 1494 PHE n 
1 1495 ASN n 
1 1496 LYS n 
1 1497 VAL n 
1 1498 LYS n 
1 1499 GLU n 
1 1500 HIS n 
1 1501 ILE n 
1 1502 ASN n 
1 1503 SER n 
1 1504 VAL n 
1 1505 SER n 
1 1506 ALA n 
1 1507 MET n 
1 1508 LYS n 
1 1509 LEU n 
1 1510 SER n 
1 1511 PRO n 
1 1512 TYR n 
1 1513 TYR n 
1 1514 LYS n 
1 1515 VAL n 
1 1516 PHE n 
1 1517 GLU n 
1 1518 GLU n 
1 1519 ASP n 
1 1520 ALA n 
1 1521 LEU n 
1 1522 SER n 
1 1523 TRP n 
1 1524 GLU n 
1 1525 ASP n 
1 1526 LYS n 
1 1527 LEU n 
1 1528 ASN n 
1 1529 ARG n 
1 1530 ILE n 
1 1531 MET n 
1 1532 ALA n 
1 1533 LEU n 
1 1534 PHE n 
1 1535 ASP n 
1 1536 VAL n 
1 1537 TRP n 
1 1538 ILE n 
1 1539 ASP n 
1 1540 VAL n 
1 1541 GLN n 
1 1542 ARG n 
1 1543 ARG n 
1 1544 TRP n 
1 1545 VAL n 
1 1546 TYR n 
1 1547 LEU n 
1 1548 GLU n 
1 1549 GLY n 
1 1550 ILE n 
1 1551 PHE n 
1 1552 THR n 
1 1553 GLY n 
1 1554 SER n 
1 1555 ALA n 
1 1556 ASP n 
1 1557 ILE n 
1 1558 LYS n 
1 1559 HIS n 
1 1560 LEU n 
1 1561 LEU n 
1 1562 PRO n 
1 1563 VAL n 
1 1564 GLU n 
1 1565 THR n 
1 1566 GLN n 
1 1567 ARG n 
1 1568 PHE n 
1 1569 GLN n 
1 1570 SER n 
1 1571 ILE n 
1 1572 SER n 
1 1573 THR n 
1 1574 GLU n 
1 1575 PHE n 
1 1576 LEU n 
1 1577 ALA n 
1 1578 LEU n 
1 1579 MET n 
1 1580 LYS n 
1 1581 LYS n 
1 1582 VAL n 
1 1583 SER n 
1 1584 LYS n 
1 1585 SER n 
1 1586 PRO n 
1 1587 LEU n 
1 1588 VAL n 
1 1589 MET n 
1 1590 ASP n 
1 1591 VAL n 
1 1592 LEU n 
1 1593 ASN n 
1 1594 ILE n 
1 1595 GLN n 
1 1596 GLY n 
1 1597 VAL n 
1 1598 GLN n 
1 1599 ARG n 
1 1600 SER n 
1 1601 LEU n 
1 1602 GLU n 
1 1603 ARG n 
1 1604 LEU n 
1 1605 ALA n 
1 1606 ASP n 
1 1607 LEU n 
1 1608 LEU n 
1 1609 GLY n 
1 1610 LYS n 
1 1611 ILE n 
1 1612 GLN n 
1 1613 LYS n 
1 1614 ALA n 
1 1615 LEU n 
1 1616 GLY n 
1 1617 GLU n 
1 1618 TYR n 
1 1619 LEU n 
1 1620 GLU n 
1 1621 ARG n 
1 1622 GLU n 
1 1623 ARG n 
1 1624 SER n 
1 1625 SER n 
1 1626 PHE n 
1 1627 PRO n 
1 1628 ARG n 
1 1629 PHE n 
1 1630 TYR n 
1 1631 PHE n 
1 1632 VAL n 
1 1633 GLY n 
1 1634 ASP n 
1 1635 GLU n 
1 1636 ASP n 
1 1637 LEU n 
1 1638 LEU n 
1 1639 GLU n 
1 1640 ILE n 
1 1641 ILE n 
1 1642 GLY n 
1 1643 ASN n 
1 1644 SER n 
1 1645 LYS n 
1 1646 ASN n 
1 1647 VAL n 
1 1648 ALA n 
1 1649 LYS n 
1 1650 LEU n 
1 1651 GLN n 
1 1652 LYS n 
1 1653 HIS n 
1 1654 PHE n 
1 1655 LYS n 
1 1656 LYS n 
1 1657 MET n 
1 1658 PHE n 
1 1659 ALA n 
1 1660 GLY n 
1 1661 VAL n 
1 1662 SER n 
1 1663 SER n 
1 1664 ILE n 
1 1665 ILE n 
1 1666 LEU n 
1 1667 ASN n 
1 1668 GLU n 
1 1669 ASP n 
1 1670 ASN n 
1 1671 SER n 
1 1672 VAL n 
1 1673 VAL n 
1 1674 LEU n 
1 1675 GLY n 
1 1676 ILE n 
1 1677 SER n 
1 1678 SER n 
1 1679 ARG n 
1 1680 GLU n 
1 1681 GLY n 
1 1682 GLU n 
1 1683 GLU n 
1 1684 VAL n 
1 1685 MET n 
1 1686 PHE n 
1 1687 LYS n 
1 1688 THR n 
1 1689 PRO n 
1 1690 VAL n 
1 1691 SER n 
1 1692 ILE n 
1 1693 THR n 
1 1694 GLU n 
1 1695 HIS n 
1 1696 PRO n 
1 1697 LYS n 
1 1698 ILE n 
1 1699 ASN n 
1 1700 GLU n 
1 1701 TRP n 
1 1702 LEU n 
1 1703 THR n 
1 1704 LEU n 
1 1705 VAL n 
1 1706 GLU n 
1 1707 LYS n 
1 1708 GLU n 
1 1709 MET n 
1 1710 ARG n 
1 1711 VAL n 
1 1712 THR n 
1 1713 LEU n 
1 1714 ALA n 
1 1715 LYS n 
1 1716 LEU n 
1 1717 LEU n 
1 1718 ALA n 
1 1719 GLU n 
1 1720 SER n 
1 1721 VAL n 
1 1722 THR n 
1 1723 GLU n 
1 1724 VAL n 
1 1725 GLU n 
1 1726 ILE n 
1 1727 PHE n 
1 1728 GLY n 
1 1729 LYS n 
1 1730 ALA n 
1 1731 THR n 
1 1732 SER n 
1 1733 ILE n 
1 1734 ASP n 
1 1735 PRO n 
1 1736 ASN n 
1 1737 THR n 
1 1738 TYR n 
1 1739 ILE n 
1 1740 THR n 
1 1741 TRP n 
1 1742 ILE n 
1 1743 ASP n 
1 1744 LYS n 
1 1745 TYR n 
1 1746 GLN n 
1 1747 ALA n 
1 1748 GLN n 
1 1749 LEU n 
1 1750 VAL n 
1 1751 VAL n 
1 1752 LEU n 
1 1753 SER n 
1 1754 ALA n 
1 1755 GLN n 
1 1756 ILE n 
1 1757 ALA n 
1 1758 TRP n 
1 1759 SER n 
1 1760 GLU n 
1 1761 ASN n 
1 1762 VAL n 
1 1763 GLU n 
1 1764 THR n 
1 1765 ALA n 
1 1766 LEU n 
1 1767 SER n 
1 1768 SER n 
1 1769 MET n 
1 1770 GLY n 
1 1771 GLY n 
1 1772 GLY n 
1 1773 GLY n 
1 1774 ASP n 
1 1775 ALA n 
1 1776 ALA n 
1 1777 PRO n 
1 1778 LEU n 
1 1779 HIS n 
1 1780 SER n 
1 1781 VAL n 
1 1782 LEU n 
1 1783 SER n 
1 1784 ASN n 
1 1785 VAL n 
1 1786 GLU n 
1 1787 VAL n 
1 1788 THR n 
1 1789 LEU n 
1 1790 ASN n 
1 1791 VAL n 
1 1792 LEU n 
1 1793 ALA n 
1 1794 ASP n 
1 1795 SER n 
1 1796 VAL n 
1 1797 LEU n 
1 1798 MET n 
1 1799 GLU n 
1 1800 GLN n 
1 1801 PRO n 
1 1802 PRO n 
1 1803 LEU n 
1 1804 ARG n 
1 1805 ARG n 
1 1806 ARG n 
1 1807 LYS n 
1 1808 LEU n 
1 1809 GLU n 
1 1810 HIS n 
1 1811 LEU n 
1 1812 ILE n 
1 1813 THR n 
1 1814 GLU n 
1 1815 LEU n 
1 1816 VAL n 
1 1817 HIS n 
1 1818 GLN n 
1 1819 ARG n 
1 1820 ASP n 
1 1821 VAL n 
1 1822 THR n 
1 1823 ARG n 
1 1824 SER n 
1 1825 LEU n 
1 1826 ILE n 
1 1827 LYS n 
1 1828 SER n 
1 1829 LYS n 
1 1830 ILE n 
1 1831 ASP n 
1 1832 ASN n 
1 1833 ALA n 
1 1834 LYS n 
1 1835 SER n 
1 1836 PHE n 
1 1837 GLU n 
1 1838 TRP n 
1 1839 LEU n 
1 1840 SER n 
1 1841 GLN n 
1 1842 MET n 
1 1843 ARG n 
1 1844 PHE n 
1 1845 TYR n 
1 1846 PHE n 
1 1847 ASP n 
1 1848 PRO n 
1 1849 LYS n 
1 1850 GLN n 
1 1851 THR n 
1 1852 ASP n 
1 1853 VAL n 
1 1854 LEU n 
1 1855 GLN n 
1 1856 GLN n 
1 1857 LEU n 
1 1858 SER n 
1 1859 ILE n 
1 1860 GLN n 
1 1861 MET n 
1 1862 ALA n 
1 1863 ASN n 
1 1864 ALA n 
1 1865 LYS n 
1 1866 PHE n 
1 1867 ASN n 
1 1868 TYR n 
1 1869 GLY n 
1 1870 PHE n 
1 1871 GLU n 
1 1872 TYR n 
1 1873 LEU n 
1 1874 GLY n 
1 1875 VAL n 
1 1876 GLN n 
1 1877 ASP n 
1 1878 LYS n 
1 1879 LEU n 
1 1880 VAL n 
1 1881 GLN n 
1 1882 THR n 
1 1883 PRO n 
1 1884 LEU n 
1 1885 THR n 
1 1886 ASP n 
1 1887 ARG n 
1 1888 CYS n 
1 1889 TYR n 
1 1890 LEU n 
1 1891 THR n 
1 1892 MET n 
1 1893 THR n 
1 1894 GLN n 
1 1895 ALA n 
1 1896 LEU n 
1 1897 GLU n 
1 1898 ALA n 
1 1899 ARG n 
1 1900 LEU n 
1 1901 GLY n 
1 1902 GLY n 
1 1903 SER n 
1 1904 PRO n 
1 1905 PHE n 
1 1906 GLY n 
1 1907 PRO n 
1 1908 ALA n 
1 1909 GLY n 
1 1910 THR n 
1 1911 GLY n 
1 1912 LYS n 
1 1913 THR n 
1 1914 GLU n 
1 1915 SER n 
1 1916 VAL n 
1 1917 LYS n 
1 1918 ALA n 
1 1919 LEU n 
1 1920 GLY n 
1 1921 HIS n 
1 1922 GLN n 
1 1923 LEU n 
1 1924 GLY n 
1 1925 ARG n 
1 1926 PHE n 
1 1927 VAL n 
1 1928 LEU n 
1 1929 VAL n 
1 1930 PHE n 
1 1931 ASN n 
1 1932 CYS n 
1 1933 ASP n 
1 1934 GLU n 
1 1935 THR n 
1 1936 PHE n 
1 1937 ASP n 
1 1938 PHE n 
1 1939 GLN n 
1 1940 ALA n 
1 1941 MET n 
1 1942 GLY n 
1 1943 ARG n 
1 1944 ILE n 
1 1945 PHE n 
1 1946 VAL n 
1 1947 GLY n 
1 1948 LEU n 
1 1949 CYS n 
1 1950 GLN n 
1 1951 VAL n 
1 1952 GLY n 
1 1953 ALA n 
1 1954 TRP n 
1 1955 GLY n 
1 1956 CYS n 
1 1957 PHE n 
1 1958 ASP n 
1 1959 GLU n 
1 1960 PHE n 
1 1961 ASN n 
1 1962 ARG n 
1 1963 LEU n 
1 1964 GLU n 
1 1965 GLU n 
1 1966 ARG n 
1 1967 MET n 
1 1968 LEU n 
1 1969 SER n 
1 1970 ALA n 
1 1971 VAL n 
1 1972 SER n 
1 1973 GLN n 
1 1974 GLN n 
1 1975 VAL n 
1 1976 GLN n 
1 1977 CYS n 
1 1978 ILE n 
1 1979 GLN n 
1 1980 GLU n 
1 1981 ALA n 
1 1982 LEU n 
1 1983 ARG n 
1 1984 GLU n 
1 1985 HIS n 
1 1986 SER n 
1 1987 ASN n 
1 1988 PRO n 
1 1989 ASN n 
1 1990 TYR n 
1 1991 ASP n 
1 1992 LYS n 
1 1993 THR n 
1 1994 SER n 
1 1995 ALA n 
1 1996 PRO n 
1 1997 ILE n 
1 1998 THR n 
1 1999 CYS n 
1 2000 GLU n 
1 2001 LEU n 
1 2002 LEU n 
1 2003 ASN n 
1 2004 LYS n 
1 2005 GLN n 
1 2006 VAL n 
1 2007 LYS n 
1 2008 VAL n 
1 2009 SER n 
1 2010 PRO n 
1 2011 ASP n 
1 2012 MET n 
1 2013 ALA n 
1 2014 ILE n 
1 2015 PHE n 
1 2016 ILE n 
1 2017 THR n 
1 2018 MET n 
1 2019 ASN n 
1 2020 PRO n 
1 2021 GLY n 
1 2022 TYR n 
1 2023 ALA n 
1 2024 GLY n 
1 2025 ARG n 
1 2026 SER n 
1 2027 ASN n 
1 2028 LEU n 
1 2029 PRO n 
1 2030 ASP n 
1 2031 ASN n 
1 2032 LEU n 
1 2033 LYS n 
1 2034 LYS n 
1 2035 LEU n 
1 2036 PHE n 
1 2037 ARG n 
1 2038 SER n 
1 2039 LEU n 
1 2040 ALA n 
1 2041 MET n 
1 2042 THR n 
1 2043 LYS n 
1 2044 PRO n 
1 2045 ASP n 
1 2046 ARG n 
1 2047 GLN n 
1 2048 LEU n 
1 2049 ILE n 
1 2050 ALA n 
1 2051 GLN n 
1 2052 VAL n 
1 2053 MET n 
1 2054 LEU n 
1 2055 TYR n 
1 2056 SER n 
1 2057 GLN n 
1 2058 GLY n 
1 2059 PHE n 
1 2060 ARG n 
1 2061 THR n 
1 2062 ALA n 
1 2063 GLU n 
1 2064 VAL n 
1 2065 LEU n 
1 2066 ALA n 
1 2067 ASN n 
1 2068 LYS n 
1 2069 ILE n 
1 2070 VAL n 
1 2071 PRO n 
1 2072 PHE n 
1 2073 PHE n 
1 2074 LYS n 
1 2075 LEU n 
1 2076 CYS n 
1 2077 ASP n 
1 2078 GLU n 
1 2079 GLN n 
1 2080 LEU n 
1 2081 SER n 
1 2082 SER n 
1 2083 GLN n 
1 2084 SER n 
1 2085 HIS n 
1 2086 TYR n 
1 2087 ASP n 
1 2088 PHE n 
1 2089 GLY n 
1 2090 LEU n 
1 2091 ARG n 
1 2092 ALA n 
1 2093 LEU n 
1 2094 LYS n 
1 2095 SER n 
1 2096 VAL n 
1 2097 LEU n 
1 2098 VAL n 
1 2099 SER n 
1 2100 ALA n 
1 2101 GLY n 
1 2102 ASN n 
1 2103 VAL n 
1 2104 LYS n 
1 2105 ARG n 
1 2106 GLU n 
1 2107 ARG n 
1 2108 ILE n 
1 2109 GLN n 
1 2110 LYS n 
1 2111 ILE n 
1 2112 LYS n 
1 2113 ARG n 
1 2114 GLU n 
1 2115 LYS n 
1 2116 GLU n 
1 2117 GLU n 
1 2118 ARG n 
1 2119 GLY n 
1 2120 GLU n 
1 2121 ALA n 
1 2122 VAL n 
1 2123 ASP n 
1 2124 GLU n 
1 2125 GLY n 
1 2126 GLU n 
1 2127 ILE n 
1 2128 ALA n 
1 2129 GLU n 
1 2130 ASN n 
1 2131 LEU n 
1 2132 PRO n 
1 2133 GLU n 
1 2134 GLN n 
1 2135 GLU n 
1 2136 ILE n 
1 2137 LEU n 
1 2138 ILE n 
1 2139 GLN n 
1 2140 SER n 
1 2141 VAL n 
1 2142 CYS n 
1 2143 GLU n 
1 2144 THR n 
1 2145 MET n 
1 2146 VAL n 
1 2147 PRO n 
1 2148 LYS n 
1 2149 LEU n 
1 2150 VAL n 
1 2151 ALA n 
1 2152 GLU n 
1 2153 ASP n 
1 2154 ILE n 
1 2155 PRO n 
1 2156 LEU n 
1 2157 LEU n 
1 2158 PHE n 
1 2159 SER n 
1 2160 LEU n 
1 2161 LEU n 
1 2162 SER n 
1 2163 ASP n 
1 2164 VAL n 
1 2165 PHE n 
1 2166 PRO n 
1 2167 GLY n 
1 2168 VAL n 
1 2169 GLN n 
1 2170 TYR n 
1 2171 HIS n 
1 2172 ARG n 
1 2173 GLY n 
1 2174 GLU n 
1 2175 MET n 
1 2176 THR n 
1 2177 ALA n 
1 2178 LEU n 
1 2179 ARG n 
1 2180 GLU n 
1 2181 GLU n 
1 2182 LEU n 
1 2183 LYS n 
1 2184 LYS n 
1 2185 VAL n 
1 2186 CYS n 
1 2187 GLN n 
1 2188 GLU n 
1 2189 MET n 
1 2190 TYR n 
1 2191 LEU n 
1 2192 THR n 
1 2193 TYR n 
1 2194 GLY n 
1 2195 ASP n 
1 2196 GLY n 
1 2197 GLU n 
1 2198 GLU n 
1 2199 VAL n 
1 2200 GLY n 
1 2201 GLY n 
1 2202 MET n 
1 2203 TRP n 
1 2204 VAL n 
1 2205 GLU n 
1 2206 LYS n 
1 2207 VAL n 
1 2208 LEU n 
1 2209 GLN n 
1 2210 LEU n 
1 2211 TYR n 
1 2212 GLN n 
1 2213 ILE n 
1 2214 THR n 
1 2215 GLN n 
1 2216 ILE n 
1 2217 ASN n 
1 2218 HIS n 
1 2219 GLY n 
1 2220 LEU n 
1 2221 MET n 
1 2222 MET n 
1 2223 VAL n 
1 2224 GLY n 
1 2225 PRO n 
1 2226 SER n 
1 2227 GLY n 
1 2228 SER n 
1 2229 GLY n 
1 2230 LYS n 
1 2231 SER n 
1 2232 MET n 
1 2233 ALA n 
1 2234 TRP n 
1 2235 ARG n 
1 2236 VAL n 
1 2237 LEU n 
1 2238 LEU n 
1 2239 LYS n 
1 2240 ALA n 
1 2241 LEU n 
1 2242 GLU n 
1 2243 ARG n 
1 2244 LEU n 
1 2245 GLU n 
1 2246 GLY n 
1 2247 VAL n 
1 2248 GLU n 
1 2249 GLY n 
1 2250 VAL n 
1 2251 ALA n 
1 2252 HIS n 
1 2253 ILE n 
1 2254 ILE n 
1 2255 ASP n 
1 2256 PRO n 
1 2257 LYS n 
1 2258 ALA n 
1 2259 ILE n 
1 2260 SER n 
1 2261 LYS n 
1 2262 ASP n 
1 2263 HIS n 
1 2264 LEU n 
1 2265 TYR n 
1 2266 GLY n 
1 2267 THR n 
1 2268 LEU n 
1 2269 ASP n 
1 2270 PRO n 
1 2271 ASN n 
1 2272 THR n 
1 2273 ARG n 
1 2274 GLU n 
1 2275 TRP n 
1 2276 THR n 
1 2277 ASP n 
1 2278 GLY n 
1 2279 LEU n 
1 2280 PHE n 
1 2281 THR n 
1 2282 HIS n 
1 2283 VAL n 
1 2284 LEU n 
1 2285 ARG n 
1 2286 LYS n 
1 2287 ILE n 
1 2288 ILE n 
1 2289 ASP n 
1 2290 SER n 
1 2291 VAL n 
1 2292 ARG n 
1 2293 GLY n 
1 2294 GLU n 
1 2295 LEU n 
1 2296 GLN n 
1 2297 LYS n 
1 2298 ARG n 
1 2299 GLN n 
1 2300 TRP n 
1 2301 ILE n 
1 2302 VAL n 
1 2303 PHE n 
1 2304 ASP n 
1 2305 GLY n 
1 2306 ASP n 
1 2307 VAL n 
1 2308 ASP n 
1 2309 PRO n 
1 2310 GLU n 
1 2311 TRP n 
1 2312 VAL n 
1 2313 GLU n 
1 2314 ASN n 
1 2315 LEU n 
1 2316 ASN n 
1 2317 SER n 
1 2318 VAL n 
1 2319 LEU n 
1 2320 ASP n 
1 2321 ASP n 
1 2322 ASN n 
1 2323 LYS n 
1 2324 LEU n 
1 2325 LEU n 
1 2326 THR n 
1 2327 LEU n 
1 2328 PRO n 
1 2329 ASN n 
1 2330 GLY n 
1 2331 GLU n 
1 2332 ARG n 
1 2333 LEU n 
1 2334 SER n 
1 2335 LEU n 
1 2336 PRO n 
1 2337 PRO n 
1 2338 ASN n 
1 2339 VAL n 
1 2340 ARG n 
1 2341 ILE n 
1 2342 MET n 
1 2343 PHE n 
1 2344 GLU n 
1 2345 VAL n 
1 2346 GLN n 
1 2347 ASP n 
1 2348 LEU n 
1 2349 LYS n 
1 2350 TYR n 
1 2351 ALA n 
1 2352 THR n 
1 2353 LEU n 
1 2354 ALA n 
1 2355 THR n 
1 2356 VAL n 
1 2357 SER n 
1 2358 ARG n 
1 2359 CYS n 
1 2360 GLY n 
1 2361 MET n 
1 2362 VAL n 
1 2363 TRP n 
1 2364 PHE n 
1 2365 SER n 
1 2366 GLU n 
1 2367 ASP n 
1 2368 VAL n 
1 2369 LEU n 
1 2370 SER n 
1 2371 THR n 
1 2372 ASP n 
1 2373 MET n 
1 2374 ILE n 
1 2375 PHE n 
1 2376 ASN n 
1 2377 ASN n 
1 2378 PHE n 
1 2379 LEU n 
1 2380 ALA n 
1 2381 ARG n 
1 2382 LEU n 
1 2383 ARG n 
1 2384 SER n 
1 2385 ILE n 
1 2386 PRO n 
1 2387 LEU n 
1 2388 ASP n 
1 2389 GLU n 
1 2390 GLY n 
1 2391 GLU n 
1 2392 ASP n 
1 2393 GLU n 
1 2394 ALA n 
1 2395 GLN n 
1 2396 ARG n 
1 2397 ARG n 
1 2398 ARG n 
1 2399 LYS n 
1 2400 GLY n 
1 2401 LYS n 
1 2402 GLU n 
1 2403 ASP n 
1 2404 GLU n 
1 2405 GLY n 
1 2406 GLU n 
1 2407 GLU n 
1 2408 ALA n 
1 2409 ALA n 
1 2410 SER n 
1 2411 PRO n 
1 2412 MET n 
1 2413 LEU n 
1 2414 GLN n 
1 2415 ILE n 
1 2416 GLN n 
1 2417 ARG n 
1 2418 ASP n 
1 2419 ALA n 
1 2420 ALA n 
1 2421 THR n 
1 2422 ILE n 
1 2423 MET n 
1 2424 GLN n 
1 2425 PRO n 
1 2426 TYR n 
1 2427 PHE n 
1 2428 THR n 
1 2429 SER n 
1 2430 ASN n 
1 2431 GLY n 
1 2432 LEU n 
1 2433 VAL n 
1 2434 THR n 
1 2435 LYS n 
1 2436 ALA n 
1 2437 LEU n 
1 2438 GLU n 
1 2439 HIS n 
1 2440 ALA n 
1 2441 PHE n 
1 2442 GLN n 
1 2443 LEU n 
1 2444 GLU n 
1 2445 HIS n 
1 2446 ILE n 
1 2447 MET n 
1 2448 ASP n 
1 2449 LEU n 
1 2450 THR n 
1 2451 ARG n 
1 2452 LEU n 
1 2453 ARG n 
1 2454 CYS n 
1 2455 LEU n 
1 2456 GLY n 
1 2457 SER n 
1 2458 LEU n 
1 2459 PHE n 
1 2460 SER n 
1 2461 MET n 
1 2462 LEU n 
1 2463 HIS n 
1 2464 GLN n 
1 2465 ALA n 
1 2466 CYS n 
1 2467 ARG n 
1 2468 ASN n 
1 2469 VAL n 
1 2470 ALA n 
1 2471 GLN n 
1 2472 TYR n 
1 2473 ASN n 
1 2474 ALA n 
1 2475 ASN n 
1 2476 HIS n 
1 2477 PRO n 
1 2478 ASP n 
1 2479 PHE n 
1 2480 PRO n 
1 2481 MET n 
1 2482 GLN n 
1 2483 ILE n 
1 2484 GLU n 
1 2485 GLN n 
1 2486 LEU n 
1 2487 GLU n 
1 2488 ARG n 
1 2489 TYR n 
1 2490 ILE n 
1 2491 GLN n 
1 2492 ARG n 
1 2493 TYR n 
1 2494 LEU n 
1 2495 VAL n 
1 2496 TYR n 
1 2497 ALA n 
1 2498 ILE n 
1 2499 LEU n 
1 2500 TRP n 
1 2501 SER n 
1 2502 LEU n 
1 2503 SER n 
1 2504 GLY n 
1 2505 ASP n 
1 2506 SER n 
1 2507 ARG n 
1 2508 LEU n 
1 2509 LYS n 
1 2510 MET n 
1 2511 ARG n 
1 2512 ALA n 
1 2513 GLU n 
1 2514 LEU n 
1 2515 GLY n 
1 2516 GLU n 
1 2517 TYR n 
1 2518 ILE n 
1 2519 ARG n 
1 2520 ARG n 
1 2521 ILE n 
1 2522 THR n 
1 2523 THR n 
1 2524 VAL n 
1 2525 PRO n 
1 2526 LEU n 
1 2527 PRO n 
1 2528 THR n 
1 2529 ALA n 
1 2530 PRO n 
1 2531 ASN n 
1 2532 ILE n 
1 2533 PRO n 
1 2534 ILE n 
1 2535 ILE n 
1 2536 ASP n 
1 2537 TYR n 
1 2538 GLU n 
1 2539 VAL n 
1 2540 SER n 
1 2541 ILE n 
1 2542 SER n 
1 2543 GLY n 
1 2544 GLU n 
1 2545 TRP n 
1 2546 SER n 
1 2547 PRO n 
1 2548 TRP n 
1 2549 GLN n 
1 2550 ALA n 
1 2551 LYS n 
1 2552 VAL n 
1 2553 PRO n 
1 2554 GLN n 
1 2555 ILE n 
1 2556 GLU n 
1 2557 VAL n 
1 2558 GLU n 
1 2559 THR n 
1 2560 HIS n 
1 2561 LYS n 
1 2562 VAL n 
1 2563 ALA n 
1 2564 ALA n 
1 2565 PRO n 
1 2566 ASP n 
1 2567 VAL n 
1 2568 VAL n 
1 2569 VAL n 
1 2570 PRO n 
1 2571 THR n 
1 2572 LEU n 
1 2573 ASP n 
1 2574 THR n 
1 2575 VAL n 
1 2576 ARG n 
1 2577 HIS n 
1 2578 GLU n 
1 2579 ALA n 
1 2580 LEU n 
1 2581 LEU n 
1 2582 TYR n 
1 2583 THR n 
1 2584 TRP n 
1 2585 LEU n 
1 2586 ALA n 
1 2587 GLU n 
1 2588 HIS n 
1 2589 LYS n 
1 2590 PRO n 
1 2591 LEU n 
1 2592 VAL n 
1 2593 LEU n 
1 2594 CYS n 
1 2595 GLY n 
1 2596 PRO n 
1 2597 PRO n 
1 2598 GLY n 
1 2599 SER n 
1 2600 GLY n 
1 2601 LYS n 
1 2602 THR n 
1 2603 MET n 
1 2604 THR n 
1 2605 LEU n 
1 2606 PHE n 
1 2607 SER n 
1 2608 ALA n 
1 2609 LEU n 
1 2610 ARG n 
1 2611 ALA n 
1 2612 LEU n 
1 2613 PRO n 
1 2614 ASP n 
1 2615 MET n 
1 2616 GLU n 
1 2617 VAL n 
1 2618 VAL n 
1 2619 GLY n 
1 2620 LEU n 
1 2621 ASN n 
1 2622 PHE n 
1 2623 SER n 
1 2624 SER n 
1 2625 ALA n 
1 2626 THR n 
1 2627 THR n 
1 2628 PRO n 
1 2629 GLU n 
1 2630 LEU n 
1 2631 LEU n 
1 2632 LEU n 
1 2633 LYS n 
1 2634 THR n 
1 2635 PHE n 
1 2636 ASP n 
1 2637 HIS n 
1 2638 TYR n 
1 2639 CYS n 
1 2640 GLU n 
1 2641 TYR n 
1 2642 ARG n 
1 2643 ARG n 
1 2644 THR n 
1 2645 PRO n 
1 2646 ASN n 
1 2647 GLY n 
1 2648 VAL n 
1 2649 VAL n 
1 2650 LEU n 
1 2651 ALA n 
1 2652 PRO n 
1 2653 VAL n 
1 2654 GLN n 
1 2655 LEU n 
1 2656 GLY n 
1 2657 LYS n 
1 2658 TRP n 
1 2659 LEU n 
1 2660 VAL n 
1 2661 LEU n 
1 2662 PHE n 
1 2663 CYS n 
1 2664 ASP n 
1 2665 GLU n 
1 2666 ILE n 
1 2667 ASN n 
1 2668 LEU n 
1 2669 PRO n 
1 2670 ASP n 
1 2671 MET n 
1 2672 ASP n 
1 2673 LYS n 
1 2674 TYR n 
1 2675 GLY n 
1 2676 THR n 
1 2677 GLN n 
1 2678 ARG n 
1 2679 VAL n 
1 2680 ILE n 
1 2681 SER n 
1 2682 PHE n 
1 2683 ILE n 
1 2684 ARG n 
1 2685 GLN n 
1 2686 MET n 
1 2687 VAL n 
1 2688 GLU n 
1 2689 HIS n 
1 2690 GLY n 
1 2691 GLY n 
1 2692 PHE n 
1 2693 TYR n 
1 2694 ARG n 
1 2695 THR n 
1 2696 SER n 
1 2697 ASP n 
1 2698 GLN n 
1 2699 THR n 
1 2700 TRP n 
1 2701 VAL n 
1 2702 LYS n 
1 2703 LEU n 
1 2704 GLU n 
1 2705 ARG n 
1 2706 ILE n 
1 2707 GLN n 
1 2708 PHE n 
1 2709 VAL n 
1 2710 GLY n 
1 2711 ALA n 
1 2712 CYS n 
1 2713 ASN n 
1 2714 PRO n 
1 2715 PRO n 
1 2716 THR n 
1 2717 ASP n 
1 2718 PRO n 
1 2719 GLY n 
1 2720 ARG n 
1 2721 LYS n 
1 2722 PRO n 
1 2723 LEU n 
1 2724 SER n 
1 2725 HIS n 
1 2726 ARG n 
1 2727 PHE n 
1 2728 LEU n 
1 2729 ARG n 
1 2730 HIS n 
1 2731 VAL n 
1 2732 PRO n 
1 2733 VAL n 
1 2734 VAL n 
1 2735 TYR n 
1 2736 VAL n 
1 2737 ASP n 
1 2738 TYR n 
1 2739 PRO n 
1 2740 GLY n 
1 2741 PRO n 
1 2742 ALA n 
1 2743 SER n 
1 2744 LEU n 
1 2745 THR n 
1 2746 GLN n 
1 2747 ILE n 
1 2748 TYR n 
1 2749 GLY n 
1 2750 THR n 
1 2751 PHE n 
1 2752 ASN n 
1 2753 ARG n 
1 2754 ALA n 
1 2755 MET n 
1 2756 LEU n 
1 2757 ARG n 
1 2758 LEU n 
1 2759 ILE n 
1 2760 PRO n 
1 2761 SER n 
1 2762 LEU n 
1 2763 ARG n 
1 2764 THR n 
1 2765 TYR n 
1 2766 ALA n 
1 2767 GLU n 
1 2768 PRO n 
1 2769 LEU n 
1 2770 THR n 
1 2771 ALA n 
1 2772 ALA n 
1 2773 MET n 
1 2774 VAL n 
1 2775 GLU n 
1 2776 PHE n 
1 2777 TYR n 
1 2778 THR n 
1 2779 MET n 
1 2780 SER n 
1 2781 GLN n 
1 2782 GLU n 
1 2783 ARG n 
1 2784 PHE n 
1 2785 THR n 
1 2786 GLN n 
1 2787 ASP n 
1 2788 THR n 
1 2789 GLN n 
1 2790 PRO n 
1 2791 HIS n 
1 2792 TYR n 
1 2793 ILE n 
1 2794 TYR n 
1 2795 SER n 
1 2796 PRO n 
1 2797 ARG n 
1 2798 GLU n 
1 2799 MET n 
1 2800 THR n 
1 2801 ARG n 
1 2802 TRP n 
1 2803 VAL n 
1 2804 ARG n 
1 2805 GLY n 
1 2806 ILE n 
1 2807 PHE n 
1 2808 GLU n 
1 2809 ALA n 
1 2810 LEU n 
1 2811 ARG n 
1 2812 PRO n 
1 2813 LEU n 
1 2814 GLU n 
1 2815 THR n 
1 2816 LEU n 
1 2817 PRO n 
1 2818 VAL n 
1 2819 GLU n 
1 2820 GLY n 
1 2821 LEU n 
1 2822 ILE n 
1 2823 ARG n 
1 2824 ILE n 
1 2825 TRP n 
1 2826 ALA n 
1 2827 HIS n 
1 2828 GLU n 
1 2829 ALA n 
1 2830 LEU n 
1 2831 ARG n 
1 2832 LEU n 
1 2833 PHE n 
1 2834 GLN n 
1 2835 ASP n 
1 2836 ARG n 
1 2837 LEU n 
1 2838 VAL n 
1 2839 GLU n 
1 2840 ASP n 
1 2841 GLU n 
1 2842 GLU n 
1 2843 ARG n 
1 2844 ARG n 
1 2845 TRP n 
1 2846 THR n 
1 2847 ASP n 
1 2848 GLU n 
1 2849 ASN n 
1 2850 ILE n 
1 2851 ASP n 
1 2852 THR n 
1 2853 VAL n 
1 2854 ALA n 
1 2855 LEU n 
1 2856 LYS n 
1 2857 HIS n 
1 2858 PHE n 
1 2859 PRO n 
1 2860 ASN n 
1 2861 ILE n 
1 2862 ASP n 
1 2863 ARG n 
1 2864 GLU n 
1 2865 LYS n 
1 2866 ALA n 
1 2867 MET n 
1 2868 SER n 
1 2869 ARG n 
1 2870 PRO n 
1 2871 ILE n 
1 2872 LEU n 
1 2873 TYR n 
1 2874 SER n 
1 2875 ASN n 
1 2876 TRP n 
1 2877 LEU n 
1 2878 SER n 
1 2879 LYS n 
1 2880 ASP n 
1 2881 TYR n 
1 2882 ILE n 
1 2883 PRO n 
1 2884 VAL n 
1 2885 ASP n 
1 2886 GLN n 
1 2887 GLU n 
1 2888 GLU n 
1 2889 LEU n 
1 2890 ARG n 
1 2891 ASP n 
1 2892 TYR n 
1 2893 VAL n 
1 2894 LYS n 
1 2895 ALA n 
1 2896 ARG n 
1 2897 LEU n 
1 2898 LYS n 
1 2899 VAL n 
1 2900 PHE n 
1 2901 TYR n 
1 2902 GLU n 
1 2903 GLU n 
1 2904 GLU n 
1 2905 LEU n 
1 2906 ASP n 
1 2907 VAL n 
1 2908 PRO n 
1 2909 LEU n 
1 2910 VAL n 
1 2911 LEU n 
1 2912 PHE n 
1 2913 ASN n 
1 2914 GLU n 
1 2915 VAL n 
1 2916 LEU n 
1 2917 ASP n 
1 2918 HIS n 
1 2919 VAL n 
1 2920 LEU n 
1 2921 ARG n 
1 2922 ILE n 
1 2923 ASP n 
1 2924 ARG n 
1 2925 ILE n 
1 2926 PHE n 
1 2927 ARG n 
1 2928 GLN n 
1 2929 PRO n 
1 2930 GLN n 
1 2931 GLY n 
1 2932 HIS n 
1 2933 LEU n 
1 2934 LEU n 
1 2935 LEU n 
1 2936 ILE n 
1 2937 GLY n 
1 2938 VAL n 
1 2939 SER n 
1 2940 GLY n 
1 2941 ALA n 
1 2942 GLY n 
1 2943 LYS n 
1 2944 THR n 
1 2945 THR n 
1 2946 LEU n 
1 2947 SER n 
1 2948 ARG n 
1 2949 PHE n 
1 2950 VAL n 
1 2951 ALA n 
1 2952 TRP n 
1 2953 MET n 
1 2954 ASN n 
1 2955 GLY n 
1 2956 LEU n 
1 2957 SER n 
1 2958 VAL n 
1 2959 TYR n 
1 2960 GLN n 
1 2961 ILE n 
1 2962 LYS n 
1 2963 VAL n 
1 2964 HIS n 
1 2965 ARG n 
1 2966 LYS n 
1 2967 TYR n 
1 2968 THR n 
1 2969 GLY n 
1 2970 GLU n 
1 2971 ASP n 
1 2972 PHE n 
1 2973 ASP n 
1 2974 GLU n 
1 2975 ASP n 
1 2976 LEU n 
1 2977 ARG n 
1 2978 THR n 
1 2979 VAL n 
1 2980 LEU n 
1 2981 ARG n 
1 2982 ARG n 
1 2983 SER n 
1 2984 GLY n 
1 2985 CYS n 
1 2986 LYS n 
1 2987 ASN n 
1 2988 GLU n 
1 2989 LYS n 
1 2990 ILE n 
1 2991 ALA n 
1 2992 PHE n 
1 2993 ILE n 
1 2994 MET n 
1 2995 ASP n 
1 2996 GLU n 
1 2997 SER n 
1 2998 ASN n 
1 2999 VAL n 
1 3000 LEU n 
1 3001 ASP n 
1 3002 SER n 
1 3003 GLY n 
1 3004 PHE n 
1 3005 LEU n 
1 3006 GLU n 
1 3007 ARG n 
1 3008 MET n 
1 3009 ASN n 
1 3010 THR n 
1 3011 LEU n 
1 3012 LEU n 
1 3013 ALA n 
1 3014 ASN n 
1 3015 GLY n 
1 3016 GLU n 
1 3017 VAL n 
1 3018 PRO n 
1 3019 GLY n 
1 3020 LEU n 
1 3021 PHE n 
1 3022 GLU n 
1 3023 GLY n 
1 3024 ASP n 
1 3025 GLU n 
1 3026 TYR n 
1 3027 ALA n 
1 3028 THR n 
1 3029 LEU n 
1 3030 MET n 
1 3031 THR n 
1 3032 GLN n 
1 3033 CYS n 
1 3034 LYS n 
1 3035 GLU n 
1 3036 GLY n 
1 3037 ALA n 
1 3038 GLN n 
1 3039 LYS n 
1 3040 GLU n 
1 3041 GLY n 
1 3042 LEU n 
1 3043 MET n 
1 3044 LEU n 
1 3045 ASP n 
1 3046 SER n 
1 3047 HIS n 
1 3048 GLU n 
1 3049 GLU n 
1 3050 LEU n 
1 3051 TYR n 
1 3052 LYS n 
1 3053 TRP n 
1 3054 PHE n 
1 3055 THR n 
1 3056 SER n 
1 3057 GLN n 
1 3058 VAL n 
1 3059 ILE n 
1 3060 ARG n 
1 3061 ASN n 
1 3062 LEU n 
1 3063 HIS n 
1 3064 VAL n 
1 3065 VAL n 
1 3066 PHE n 
1 3067 THR n 
1 3068 MET n 
1 3069 ASN n 
1 3070 PRO n 
1 3071 SER n 
1 3072 SER n 
1 3073 GLU n 
1 3074 GLY n 
1 3075 LEU n 
1 3076 LYS n 
1 3077 ASP n 
1 3078 ARG n 
1 3079 ALA n 
1 3080 ALA n 
1 3081 THR n 
1 3082 SER n 
1 3083 PRO n 
1 3084 ALA n 
1 3085 LEU n 
1 3086 PHE n 
1 3087 ASN n 
1 3088 ARG n 
1 3089 CYS n 
1 3090 VAL n 
1 3091 LEU n 
1 3092 ASN n 
1 3093 TRP n 
1 3094 PHE n 
1 3095 GLY n 
1 3096 ASP n 
1 3097 TRP n 
1 3098 SER n 
1 3099 THR n 
1 3100 GLU n 
1 3101 ALA n 
1 3102 LEU n 
1 3103 TYR n 
1 3104 GLN n 
1 3105 VAL n 
1 3106 GLY n 
1 3107 LYS n 
1 3108 GLU n 
1 3109 PHE n 
1 3110 THR n 
1 3111 SER n 
1 3112 LYS n 
1 3113 MET n 
1 3114 ASP n 
1 3115 LEU n 
1 3116 GLU n 
1 3117 LYS n 
1 3118 PRO n 
1 3119 ASN n 
1 3120 TYR n 
1 3121 ILE n 
1 3122 VAL n 
1 3123 PRO n 
1 3124 ASP n 
1 3125 TYR n 
1 3126 MET n 
1 3127 PRO n 
1 3128 VAL n 
1 3129 VAL n 
1 3130 TYR n 
1 3131 ASP n 
1 3132 LYS n 
1 3133 LEU n 
1 3134 PRO n 
1 3135 GLN n 
1 3136 PRO n 
1 3137 PRO n 
1 3138 SER n 
1 3139 HIS n 
1 3140 ARG n 
1 3141 GLU n 
1 3142 ALA n 
1 3143 ILE n 
1 3144 VAL n 
1 3145 ASN n 
1 3146 SER n 
1 3147 CYS n 
1 3148 VAL n 
1 3149 PHE n 
1 3150 VAL n 
1 3151 HIS n 
1 3152 GLN n 
1 3153 THR n 
1 3154 LEU n 
1 3155 HIS n 
1 3156 GLN n 
1 3157 ALA n 
1 3158 ASN n 
1 3159 ALA n 
1 3160 ARG n 
1 3161 LEU n 
1 3162 ALA n 
1 3163 LYS n 
1 3164 ARG n 
1 3165 GLY n 
1 3166 GLY n 
1 3167 ARG n 
1 3168 THR n 
1 3169 MET n 
1 3170 ALA n 
1 3171 ILE n 
1 3172 THR n 
1 3173 PRO n 
1 3174 ARG n 
1 3175 HIS n 
1 3176 TYR n 
1 3177 LEU n 
1 3178 ASP n 
1 3179 PHE n 
1 3180 ILE n 
1 3181 ASN n 
1 3182 HIS n 
1 3183 TYR n 
1 3184 ALA n 
1 3185 ASN n 
1 3186 LEU n 
1 3187 PHE n 
1 3188 HIS n 
1 3189 GLU n 
1 3190 LYS n 
1 3191 ARG n 
1 3192 SER n 
1 3193 GLU n 
1 3194 LEU n 
1 3195 GLU n 
1 3196 GLU n 
1 3197 GLN n 
1 3198 GLN n 
1 3199 MET n 
1 3200 HIS n 
1 3201 LEU n 
1 3202 ASN n 
1 3203 VAL n 
1 3204 GLY n 
1 3205 LEU n 
1 3206 ARG n 
1 3207 LYS n 
1 3208 ILE n 
1 3209 LYS n 
1 3210 GLU n 
1 3211 THR n 
1 3212 VAL n 
1 3213 ASP n 
1 3214 GLN n 
1 3215 VAL n 
1 3216 GLU n 
1 3217 GLU n 
1 3218 LEU n 
1 3219 ARG n 
1 3220 ARG n 
1 3221 ASP n 
1 3222 LEU n 
1 3223 ARG n 
1 3224 ILE n 
1 3225 LYS n 
1 3226 SER n 
1 3227 GLN n 
1 3228 GLU n 
1 3229 LEU n 
1 3230 GLU n 
1 3231 VAL n 
1 3232 LYS n 
1 3233 ASN n 
1 3234 ALA n 
1 3235 ALA n 
1 3236 ALA n 
1 3237 ASN n 
1 3238 ASP n 
1 3239 LYS n 
1 3240 LEU n 
1 3241 LYS n 
1 3242 LYS n 
1 3243 MET n 
1 3244 VAL n 
1 3245 LYS n 
1 3246 ASP n 
1 3247 GLN n 
1 3248 GLN n 
1 3249 GLU n 
1 3250 ALA n 
1 3251 GLU n 
1 3252 LYS n 
1 3253 LYS n 
1 3254 LYS n 
1 3255 VAL n 
1 3256 MET n 
1 3257 SER n 
1 3258 GLN n 
1 3259 GLU n 
1 3260 ILE n 
1 3261 GLN n 
1 3262 GLU n 
1 3263 GLN n 
1 3264 LEU n 
1 3265 HIS n 
1 3266 LYS n 
1 3267 GLN n 
1 3268 GLN n 
1 3269 GLU n 
1 3270 VAL n 
1 3271 ILE n 
1 3272 ALA n 
1 3273 ASP n 
1 3274 LYS n 
1 3275 GLN n 
1 3276 MET n 
1 3277 SER n 
1 3278 VAL n 
1 3279 LYS n 
1 3280 GLU n 
1 3281 ASP n 
1 3282 LEU n 
1 3283 ASP n 
1 3284 LYS n 
1 3285 VAL n 
1 3286 GLU n 
1 3287 PRO n 
1 3288 ALA n 
1 3289 VAL n 
1 3290 ILE n 
1 3291 GLU n 
1 3292 ALA n 
1 3293 GLN n 
1 3294 ASN n 
1 3295 ALA n 
1 3296 VAL n 
1 3297 LYS n 
1 3298 SER n 
1 3299 ILE n 
1 3300 LYS n 
1 3301 LYS n 
1 3302 GLN n 
1 3303 HIS n 
1 3304 LEU n 
1 3305 VAL n 
1 3306 GLU n 
1 3307 VAL n 
1 3308 ARG n 
1 3309 SER n 
1 3310 MET n 
1 3311 ALA n 
1 3312 ASN n 
1 3313 PRO n 
1 3314 PRO n 
1 3315 ALA n 
1 3316 ALA n 
1 3317 VAL n 
1 3318 LYS n 
1 3319 LEU n 
1 3320 ALA n 
1 3321 LEU n 
1 3322 GLU n 
1 3323 SER n 
1 3324 ILE n 
1 3325 CYS n 
1 3326 LEU n 
1 3327 LEU n 
1 3328 LEU n 
1 3329 GLY n 
1 3330 GLU n 
1 3331 SER n 
1 3332 THR n 
1 3333 THR n 
1 3334 ASP n 
1 3335 TRP n 
1 3336 LYS n 
1 3337 GLN n 
1 3338 ILE n 
1 3339 ARG n 
1 3340 SER n 
1 3341 ILE n 
1 3342 ILE n 
1 3343 MET n 
1 3344 ARG n 
1 3345 GLU n 
1 3346 ASN n 
1 3347 PHE n 
1 3348 ILE n 
1 3349 PRO n 
1 3350 THR n 
1 3351 ILE n 
1 3352 VAL n 
1 3353 ASN n 
1 3354 PHE n 
1 3355 SER n 
1 3356 ALA n 
1 3357 GLU n 
1 3358 GLU n 
1 3359 ILE n 
1 3360 SER n 
1 3361 ASP n 
1 3362 ALA n 
1 3363 ILE n 
1 3364 ARG n 
1 3365 GLU n 
1 3366 LYS n 
1 3367 MET n 
1 3368 LYS n 
1 3369 LYS n 
1 3370 ASN n 
1 3371 TYR n 
1 3372 MET n 
1 3373 SER n 
1 3374 ASN n 
1 3375 PRO n 
1 3376 SER n 
1 3377 TYR n 
1 3378 ASN n 
1 3379 TYR n 
1 3380 GLU n 
1 3381 ILE n 
1 3382 VAL n 
1 3383 ASN n 
1 3384 ARG n 
1 3385 ALA n 
1 3386 SER n 
1 3387 LEU n 
1 3388 ALA n 
1 3389 CYS n 
1 3390 GLY n 
1 3391 PRO n 
1 3392 MET n 
1 3393 VAL n 
1 3394 LYS n 
1 3395 TRP n 
1 3396 ALA n 
1 3397 ILE n 
1 3398 ALA n 
1 3399 GLN n 
1 3400 LEU n 
1 3401 ASN n 
1 3402 TYR n 
1 3403 ALA n 
1 3404 ASP n 
1 3405 MET n 
1 3406 LEU n 
1 3407 LYS n 
1 3408 ARG n 
1 3409 VAL n 
1 3410 GLU n 
1 3411 PRO n 
1 3412 LEU n 
1 3413 ARG n 
1 3414 ASN n 
1 3415 GLU n 
1 3416 LEU n 
1 3417 GLN n 
1 3418 LYS n 
1 3419 LEU n 
1 3420 GLU n 
1 3421 ASP n 
1 3422 ASP n 
1 3423 ALA n 
1 3424 LYS n 
1 3425 ASP n 
1 3426 ASN n 
1 3427 GLN n 
1 3428 GLN n 
1 3429 LYS n 
1 3430 ALA n 
1 3431 ASN n 
1 3432 GLU n 
1 3433 VAL n 
1 3434 GLU n 
1 3435 GLN n 
1 3436 MET n 
1 3437 ILE n 
1 3438 ARG n 
1 3439 ASP n 
1 3440 LEU n 
1 3441 GLU n 
1 3442 ALA n 
1 3443 SER n 
1 3444 ILE n 
1 3445 ALA n 
1 3446 ARG n 
1 3447 TYR n 
1 3448 LYS n 
1 3449 GLU n 
1 3450 GLU n 
1 3451 TYR n 
1 3452 ALA n 
1 3453 VAL n 
1 3454 LEU n 
1 3455 ILE n 
1 3456 SER n 
1 3457 GLU n 
1 3458 ALA n 
1 3459 GLN n 
1 3460 ALA n 
1 3461 ILE n 
1 3462 LYS n 
1 3463 ALA n 
1 3464 ASP n 
1 3465 LEU n 
1 3466 ALA n 
1 3467 ALA n 
1 3468 VAL n 
1 3469 GLU n 
1 3470 ALA n 
1 3471 LYS n 
1 3472 VAL n 
1 3473 ASN n 
1 3474 ARG n 
1 3475 SER n 
1 3476 THR n 
1 3477 ALA n 
1 3478 LEU n 
1 3479 LEU n 
1 3480 LYS n 
1 3481 SER n 
1 3482 LEU n 
1 3483 SER n 
1 3484 ALA n 
1 3485 GLU n 
1 3486 ARG n 
1 3487 GLU n 
1 3488 ARG n 
1 3489 TRP n 
1 3490 GLU n 
1 3491 LYS n 
1 3492 THR n 
1 3493 SER n 
1 3494 GLU n 
1 3495 THR n 
1 3496 PHE n 
1 3497 LYS n 
1 3498 ASN n 
1 3499 GLN n 
1 3500 MET n 
1 3501 SER n 
1 3502 THR n 
1 3503 ILE n 
1 3504 ALA n 
1 3505 GLY n 
1 3506 ASP n 
1 3507 CYS n 
1 3508 LEU n 
1 3509 LEU n 
1 3510 SER n 
1 3511 ALA n 
1 3512 ALA n 
1 3513 PHE n 
1 3514 ILE n 
1 3515 ALA n 
1 3516 TYR n 
1 3517 ALA n 
1 3518 GLY n 
1 3519 TYR n 
1 3520 PHE n 
1 3521 ASP n 
1 3522 GLN n 
1 3523 GLN n 
1 3524 MET n 
1 3525 ARG n 
1 3526 GLN n 
1 3527 ASN n 
1 3528 LEU n 
1 3529 PHE n 
1 3530 THR n 
1 3531 THR n 
1 3532 TRP n 
1 3533 SER n 
1 3534 HIS n 
1 3535 HIS n 
1 3536 LEU n 
1 3537 GLN n 
1 3538 GLN n 
1 3539 ALA n 
1 3540 ASN n 
1 3541 ILE n 
1 3542 GLN n 
1 3543 PHE n 
1 3544 ARG n 
1 3545 THR n 
1 3546 ASP n 
1 3547 ILE n 
1 3548 ALA n 
1 3549 ARG n 
1 3550 THR n 
1 3551 GLU n 
1 3552 TYR n 
1 3553 LEU n 
1 3554 SER n 
1 3555 ASN n 
1 3556 ALA n 
1 3557 ASP n 
1 3558 GLU n 
1 3559 ARG n 
1 3560 LEU n 
1 3561 ARG n 
1 3562 TRP n 
1 3563 GLN n 
1 3564 ALA n 
1 3565 SER n 
1 3566 SER n 
1 3567 LEU n 
1 3568 PRO n 
1 3569 ALA n 
1 3570 ASP n 
1 3571 ASP n 
1 3572 LEU n 
1 3573 CYS n 
1 3574 THR n 
1 3575 GLU n 
1 3576 ASN n 
1 3577 ALA n 
1 3578 ILE n 
1 3579 MET n 
1 3580 LEU n 
1 3581 LYS n 
1 3582 ARG n 
1 3583 PHE n 
1 3584 ASN n 
1 3585 ARG n 
1 3586 TYR n 
1 3587 PRO n 
1 3588 LEU n 
1 3589 ILE n 
1 3590 ILE n 
1 3591 ASP n 
1 3592 PRO n 
1 3593 SER n 
1 3594 GLY n 
1 3595 GLN n 
1 3596 ALA n 
1 3597 THR n 
1 3598 GLU n 
1 3599 PHE n 
1 3600 ILE n 
1 3601 MET n 
1 3602 ASN n 
1 3603 GLU n 
1 3604 TYR n 
1 3605 LYS n 
1 3606 ASP n 
1 3607 ARG n 
1 3608 LYS n 
1 3609 ILE n 
1 3610 THR n 
1 3611 ARG n 
1 3612 THR n 
1 3613 SER n 
1 3614 PHE n 
1 3615 LEU n 
1 3616 ASP n 
1 3617 ASP n 
1 3618 ALA n 
1 3619 PHE n 
1 3620 ARG n 
1 3621 LYS n 
1 3622 ASN n 
1 3623 LEU n 
1 3624 GLU n 
1 3625 SER n 
1 3626 ALA n 
1 3627 LEU n 
1 3628 ARG n 
1 3629 PHE n 
1 3630 GLY n 
1 3631 ASN n 
1 3632 PRO n 
1 3633 LEU n 
1 3634 LEU n 
1 3635 VAL n 
1 3636 GLN n 
1 3637 ASP n 
1 3638 VAL n 
1 3639 GLU n 
1 3640 SER n 
1 3641 TYR n 
1 3642 ASP n 
1 3643 PRO n 
1 3644 VAL n 
1 3645 LEU n 
1 3646 ASN n 
1 3647 PRO n 
1 3648 VAL n 
1 3649 LEU n 
1 3650 ASN n 
1 3651 ARG n 
1 3652 GLU n 
1 3653 VAL n 
1 3654 ARG n 
1 3655 ARG n 
1 3656 THR n 
1 3657 GLY n 
1 3658 GLY n 
1 3659 ARG n 
1 3660 VAL n 
1 3661 LEU n 
1 3662 ILE n 
1 3663 THR n 
1 3664 LEU n 
1 3665 GLY n 
1 3666 ASP n 
1 3667 GLN n 
1 3668 ASP n 
1 3669 ILE n 
1 3670 ASP n 
1 3671 LEU n 
1 3672 SER n 
1 3673 PRO n 
1 3674 SER n 
1 3675 PHE n 
1 3676 VAL n 
1 3677 ILE n 
1 3678 PHE n 
1 3679 LEU n 
1 3680 SER n 
1 3681 THR n 
1 3682 ARG n 
1 3683 ASP n 
1 3684 PRO n 
1 3685 THR n 
1 3686 VAL n 
1 3687 GLU n 
1 3688 PHE n 
1 3689 PRO n 
1 3690 PRO n 
1 3691 ASP n 
1 3692 LEU n 
1 3693 CYS n 
1 3694 SER n 
1 3695 ARG n 
1 3696 VAL n 
1 3697 THR n 
1 3698 PHE n 
1 3699 VAL n 
1 3700 ASN n 
1 3701 PHE n 
1 3702 THR n 
1 3703 VAL n 
1 3704 THR n 
1 3705 ARG n 
1 3706 SER n 
1 3707 SER n 
1 3708 LEU n 
1 3709 GLN n 
1 3710 SER n 
1 3711 GLN n 
1 3712 CYS n 
1 3713 LEU n 
1 3714 ASN n 
1 3715 GLU n 
1 3716 VAL n 
1 3717 LEU n 
1 3718 LYS n 
1 3719 ALA n 
1 3720 GLU n 
1 3721 ARG n 
1 3722 PRO n 
1 3723 ASP n 
1 3724 VAL n 
1 3725 ASP n 
1 3726 GLU n 
1 3727 LYS n 
1 3728 ARG n 
1 3729 SER n 
1 3730 ASP n 
1 3731 LEU n 
1 3732 LEU n 
1 3733 LYS n 
1 3734 LEU n 
1 3735 GLN n 
1 3736 GLY n 
1 3737 GLU n 
1 3738 PHE n 
1 3739 GLN n 
1 3740 LEU n 
1 3741 ARG n 
1 3742 LEU n 
1 3743 ARG n 
1 3744 GLN n 
1 3745 LEU n 
1 3746 GLU n 
1 3747 LYS n 
1 3748 SER n 
1 3749 LEU n 
1 3750 LEU n 
1 3751 GLN n 
1 3752 ALA n 
1 3753 LEU n 
1 3754 ASN n 
1 3755 GLU n 
1 3756 VAL n 
1 3757 LYS n 
1 3758 GLY n 
1 3759 ARG n 
1 3760 ILE n 
1 3761 LEU n 
1 3762 ASP n 
1 3763 ASP n 
1 3764 ASP n 
1 3765 THR n 
1 3766 ILE n 
1 3767 ILE n 
1 3768 THR n 
1 3769 THR n 
1 3770 LEU n 
1 3771 GLU n 
1 3772 ASN n 
1 3773 LEU n 
1 3774 LYS n 
1 3775 ARG n 
1 3776 GLU n 
1 3777 ALA n 
1 3778 ALA n 
1 3779 GLU n 
1 3780 VAL n 
1 3781 THR n 
1 3782 ARG n 
1 3783 LYS n 
1 3784 VAL n 
1 3785 GLU n 
1 3786 GLU n 
1 3787 THR n 
1 3788 ASP n 
1 3789 ILE n 
1 3790 VAL n 
1 3791 MET n 
1 3792 GLN n 
1 3793 GLU n 
1 3794 VAL n 
1 3795 GLU n 
1 3796 THR n 
1 3797 VAL n 
1 3798 SER n 
1 3799 GLN n 
1 3800 GLN n 
1 3801 TYR n 
1 3802 LEU n 
1 3803 PRO n 
1 3804 LEU n 
1 3805 SER n 
1 3806 THR n 
1 3807 ALA n 
1 3808 CYS n 
1 3809 SER n 
1 3810 SER n 
1 3811 ILE n 
1 3812 TYR n 
1 3813 PHE n 
1 3814 THR n 
1 3815 MET n 
1 3816 GLU n 
1 3817 SER n 
1 3818 LEU n 
1 3819 LYS n 
1 3820 GLN n 
1 3821 ILE n 
1 3822 HIS n 
1 3823 PHE n 
1 3824 LEU n 
1 3825 TYR n 
1 3826 GLN n 
1 3827 TYR n 
1 3828 SER n 
1 3829 LEU n 
1 3830 GLN n 
1 3831 PHE n 
1 3832 PHE n 
1 3833 LEU n 
1 3834 ASP n 
1 3835 ILE n 
1 3836 TYR n 
1 3837 HIS n 
1 3838 ASN n 
1 3839 VAL n 
1 3840 LEU n 
1 3841 TYR n 
1 3842 GLU n 
1 3843 ASN n 
1 3844 PRO n 
1 3845 ASN n 
1 3846 LEU n 
1 3847 LYS n 
1 3848 GLY n 
1 3849 VAL n 
1 3850 THR n 
1 3851 ASP n 
1 3852 HIS n 
1 3853 THR n 
1 3854 GLN n 
1 3855 ARG n 
1 3856 LEU n 
1 3857 SER n 
1 3858 ILE n 
1 3859 ILE n 
1 3860 THR n 
1 3861 LYS n 
1 3862 ASP n 
1 3863 LEU n 
1 3864 PHE n 
1 3865 GLN n 
1 3866 VAL n 
1 3867 ALA n 
1 3868 PHE n 
1 3869 ASN n 
1 3870 ARG n 
1 3871 VAL n 
1 3872 ALA n 
1 3873 ARG n 
1 3874 GLY n 
1 3875 MET n 
1 3876 LEU n 
1 3877 HIS n 
1 3878 GLN n 
1 3879 ASP n 
1 3880 HIS n 
1 3881 ILE n 
1 3882 THR n 
1 3883 PHE n 
1 3884 ALA n 
1 3885 MET n 
1 3886 LEU n 
1 3887 LEU n 
1 3888 ALA n 
1 3889 ARG n 
1 3890 ILE n 
1 3891 LYS n 
1 3892 LEU n 
1 3893 LYS n 
1 3894 GLY n 
1 3895 THR n 
1 3896 VAL n 
1 3897 GLY n 
1 3898 GLU n 
1 3899 PRO n 
1 3900 THR n 
1 3901 TYR n 
1 3902 ASP n 
1 3903 ALA n 
1 3904 GLU n 
1 3905 PHE n 
1 3906 GLN n 
1 3907 HIS n 
1 3908 PHE n 
1 3909 LEU n 
1 3910 ARG n 
1 3911 GLY n 
1 3912 ASN n 
1 3913 GLU n 
1 3914 ILE n 
1 3915 VAL n 
1 3916 LEU n 
1 3917 SER n 
1 3918 ALA n 
1 3919 GLY n 
1 3920 SER n 
1 3921 THR n 
1 3922 PRO n 
1 3923 ARG n 
1 3924 ILE n 
1 3925 GLN n 
1 3926 GLY n 
1 3927 LEU n 
1 3928 THR n 
1 3929 VAL n 
1 3930 GLU n 
1 3931 GLN n 
1 3932 ALA n 
1 3933 GLU n 
1 3934 ALA n 
1 3935 VAL n 
1 3936 VAL n 
1 3937 ARG n 
1 3938 LEU n 
1 3939 SER n 
1 3940 CYS n 
1 3941 LEU n 
1 3942 PRO n 
1 3943 ALA n 
1 3944 PHE n 
1 3945 LYS n 
1 3946 ASP n 
1 3947 LEU n 
1 3948 ILE n 
1 3949 ALA n 
1 3950 LYS n 
1 3951 VAL n 
1 3952 GLN n 
1 3953 ALA n 
1 3954 ASP n 
1 3955 GLU n 
1 3956 GLN n 
1 3957 PHE n 
1 3958 GLY n 
1 3959 ILE n 
1 3960 TRP n 
1 3961 LEU n 
1 3962 ASP n 
1 3963 SER n 
1 3964 SER n 
1 3965 SER n 
1 3966 PRO n 
1 3967 GLU n 
1 3968 GLN n 
1 3969 THR n 
1 3970 VAL n 
1 3971 PRO n 
1 3972 TYR n 
1 3973 LEU n 
1 3974 TRP n 
1 3975 SER n 
1 3976 GLU n 
1 3977 GLU n 
1 3978 THR n 
1 3979 PRO n 
1 3980 ALA n 
1 3981 THR n 
1 3982 PRO n 
1 3983 ILE n 
1 3984 GLY n 
1 3985 GLN n 
1 3986 ALA n 
1 3987 ILE n 
1 3988 HIS n 
1 3989 ARG n 
1 3990 LEU n 
1 3991 LEU n 
1 3992 LEU n 
1 3993 ILE n 
1 3994 GLN n 
1 3995 ALA n 
1 3996 PHE n 
1 3997 ARG n 
1 3998 PRO n 
1 3999 ASP n 
1 4000 ARG n 
1 4001 LEU n 
1 4002 LEU n 
1 4003 ALA n 
1 4004 MET n 
1 4005 ALA n 
1 4006 HIS n 
1 4007 MET n 
1 4008 PHE n 
1 4009 VAL n 
1 4010 SER n 
1 4011 THR n 
1 4012 ASN n 
1 4013 LEU n 
1 4014 GLY n 
1 4015 GLU n 
1 4016 SER n 
1 4017 PHE n 
1 4018 MET n 
1 4019 SER n 
1 4020 ILE n 
1 4021 MET n 
1 4022 GLU n 
1 4023 GLN n 
1 4024 PRO n 
1 4025 LEU n 
1 4026 ASP n 
1 4027 LEU n 
1 4028 THR n 
1 4029 HIS n 
1 4030 ILE n 
1 4031 VAL n 
1 4032 GLY n 
1 4033 THR n 
1 4034 GLU n 
1 4035 VAL n 
1 4036 LYS n 
1 4037 PRO n 
1 4038 ASN n 
1 4039 THR n 
1 4040 PRO n 
1 4041 VAL n 
1 4042 LEU n 
1 4043 MET n 
1 4044 CYS n 
1 4045 SER n 
1 4046 VAL n 
1 4047 PRO n 
1 4048 GLY n 
1 4049 TYR n 
1 4050 ASP n 
1 4051 ALA n 
1 4052 SER n 
1 4053 GLY n 
1 4054 HIS n 
1 4055 VAL n 
1 4056 GLU n 
1 4057 ASP n 
1 4058 LEU n 
1 4059 ALA n 
1 4060 ALA n 
1 4061 GLU n 
1 4062 GLN n 
1 4063 ASN n 
1 4064 THR n 
1 4065 GLN n 
1 4066 ILE n 
1 4067 THR n 
1 4068 SER n 
1 4069 ILE n 
1 4070 ALA n 
1 4071 ILE n 
1 4072 GLY n 
1 4073 SER n 
1 4074 ALA n 
1 4075 GLU n 
1 4076 GLY n 
1 4077 PHE n 
1 4078 ASN n 
1 4079 GLN n 
1 4080 ALA n 
1 4081 ASP n 
1 4082 LYS n 
1 4083 ALA n 
1 4084 ILE n 
1 4085 ASN n 
1 4086 THR n 
1 4087 ALA n 
1 4088 VAL n 
1 4089 LYS n 
1 4090 SER n 
1 4091 GLY n 
1 4092 ARG n 
1 4093 TRP n 
1 4094 VAL n 
1 4095 MET n 
1 4096 LEU n 
1 4097 LYS n 
1 4098 ASN n 
1 4099 VAL n 
1 4100 HIS n 
1 4101 LEU n 
1 4102 ALA n 
1 4103 PRO n 
1 4104 GLY n 
1 4105 TRP n 
1 4106 LEU n 
1 4107 MET n 
1 4108 GLN n 
1 4109 LEU n 
1 4110 GLU n 
1 4111 LYS n 
1 4112 LYS n 
1 4113 LEU n 
1 4114 HIS n 
1 4115 SER n 
1 4116 LEU n 
1 4117 GLN n 
1 4118 PRO n 
1 4119 HIS n 
1 4120 ALA n 
1 4121 CYS n 
1 4122 PHE n 
1 4123 ARG n 
1 4124 LEU n 
1 4125 PHE n 
1 4126 LEU n 
1 4127 THR n 
1 4128 MET n 
1 4129 GLU n 
1 4130 ILE n 
1 4131 ASN n 
1 4132 PRO n 
1 4133 LYS n 
1 4134 VAL n 
1 4135 PRO n 
1 4136 VAL n 
1 4137 ASN n 
1 4138 LEU n 
1 4139 LEU n 
1 4140 ARG n 
1 4141 ALA n 
1 4142 GLY n 
1 4143 ARG n 
1 4144 ILE n 
1 4145 PHE n 
1 4146 VAL n 
1 4147 PHE n 
1 4148 GLU n 
1 4149 PRO n 
1 4150 PRO n 
1 4151 PRO n 
1 4152 GLY n 
1 4153 VAL n 
1 4154 LYS n 
1 4155 ALA n 
1 4156 ASN n 
1 4157 MET n 
1 4158 LEU n 
1 4159 ARG n 
1 4160 THR n 
1 4161 PHE n 
1 4162 SER n 
1 4163 SER n 
1 4164 ILE n 
1 4165 PRO n 
1 4166 VAL n 
1 4167 SER n 
1 4168 ARG n 
1 4169 ILE n 
1 4170 CYS n 
1 4171 LYS n 
1 4172 SER n 
1 4173 PRO n 
1 4174 ASN n 
1 4175 GLU n 
1 4176 ARG n 
1 4177 ALA n 
1 4178 ARG n 
1 4179 LEU n 
1 4180 TYR n 
1 4181 PHE n 
1 4182 LEU n 
1 4183 LEU n 
1 4184 ALA n 
1 4185 TRP n 
1 4186 PHE n 
1 4187 HIS n 
1 4188 ALA n 
1 4189 ILE n 
1 4190 ILE n 
1 4191 GLN n 
1 4192 GLU n 
1 4193 ARG n 
1 4194 LEU n 
1 4195 ARG n 
1 4196 TYR n 
1 4197 ALA n 
1 4198 PRO n 
1 4199 LEU n 
1 4200 GLY n 
1 4201 TRP n 
1 4202 SER n 
1 4203 LYS n 
1 4204 LYS n 
1 4205 TYR n 
1 4206 GLU n 
1 4207 PHE n 
1 4208 GLY n 
1 4209 GLU n 
1 4210 SER n 
1 4211 ASP n 
1 4212 LEU n 
1 4213 ARG n 
1 4214 SER n 
1 4215 ALA n 
1 4216 CYS n 
1 4217 ASP n 
1 4218 THR n 
1 4219 VAL n 
1 4220 ASP n 
1 4221 THR n 
1 4222 TRP n 
1 4223 LEU n 
1 4224 ASP n 
1 4225 ASP n 
1 4226 THR n 
1 4227 ALA n 
1 4228 LYS n 
1 4229 GLY n 
1 4230 ARG n 
1 4231 GLN n 
1 4232 ASN n 
1 4233 ILE n 
1 4234 SER n 
1 4235 PRO n 
1 4236 ASP n 
1 4237 LYS n 
1 4238 ILE n 
1 4239 PRO n 
1 4240 TRP n 
1 4241 SER n 
1 4242 ALA n 
1 4243 LEU n 
1 4244 LYS n 
1 4245 THR n 
1 4246 LEU n 
1 4247 MET n 
1 4248 ALA n 
1 4249 GLN n 
1 4250 SER n 
1 4251 ILE n 
1 4252 TYR n 
1 4253 GLY n 
1 4254 GLY n 
1 4255 ARG n 
1 4256 VAL n 
1 4257 ASP n 
1 4258 ASN n 
1 4259 GLU n 
1 4260 PHE n 
1 4261 ASP n 
1 4262 GLN n 
1 4263 ARG n 
1 4264 LEU n 
1 4265 LEU n 
1 4266 ASN n 
1 4267 THR n 
1 4268 PHE n 
1 4269 LEU n 
1 4270 GLU n 
1 4271 ARG n 
1 4272 LEU n 
1 4273 PHE n 
1 4274 THR n 
1 4275 THR n 
1 4276 ARG n 
1 4277 SER n 
1 4278 PHE n 
1 4279 ASP n 
1 4280 SER n 
1 4281 GLU n 
1 4282 PHE n 
1 4283 LYS n 
1 4284 LEU n 
1 4285 ALA n 
1 4286 CYS n 
1 4287 LYS n 
1 4288 VAL n 
1 4289 ASP n 
1 4290 GLY n 
1 4291 HIS n 
1 4292 LYS n 
1 4293 ASP n 
1 4294 ILE n 
1 4295 GLN n 
1 4296 MET n 
1 4297 PRO n 
1 4298 ASP n 
1 4299 GLY n 
1 4300 ILE n 
1 4301 ARG n 
1 4302 ARG n 
1 4303 GLU n 
1 4304 GLU n 
1 4305 PHE n 
1 4306 VAL n 
1 4307 GLN n 
1 4308 TRP n 
1 4309 VAL n 
1 4310 GLU n 
1 4311 LEU n 
1 4312 LEU n 
1 4313 PRO n 
1 4314 ASP n 
1 4315 THR n 
1 4316 GLN n 
1 4317 THR n 
1 4318 PRO n 
1 4319 SER n 
1 4320 TRP n 
1 4321 LEU n 
1 4322 GLY n 
1 4323 LEU n 
1 4324 PRO n 
1 4325 ASN n 
1 4326 ASN n 
1 4327 ALA n 
1 4328 GLU n 
1 4329 ARG n 
1 4330 VAL n 
1 4331 LEU n 
1 4332 LEU n 
1 4333 THR n 
1 4334 THR n 
1 4335 GLN n 
1 4336 GLY n 
1 4337 VAL n 
1 4338 ASP n 
1 4339 MET n 
1 4340 ILE n 
1 4341 SER n 
1 4342 LYS n 
1 4343 MET n 
1 4344 LEU n 
1 4345 LYS n 
1 4346 MET n 
1 4347 GLN n 
1 4348 MET n 
1 4349 LEU n 
1 4350 GLU n 
1 4351 ASP n 
1 4352 GLU n 
1 4353 ASP n 
1 4354 ASP n 
1 4355 LEU n 
1 4356 ALA n 
1 4357 TYR n 
1 4358 ALA n 
1 4359 GLU n 
1 4360 THR n 
1 4361 GLU n 
1 4362 LYS n 
1 4363 LYS n 
1 4364 THR n 
1 4365 ARG n 
1 4366 THR n 
1 4367 ASP n 
1 4368 SER n 
1 4369 THR n 
1 4370 SER n 
1 4371 ASP n 
1 4372 GLY n 
1 4373 ARG n 
1 4374 PRO n 
1 4375 ALA n 
1 4376 TRP n 
1 4377 MET n 
1 4378 ARG n 
1 4379 THR n 
1 4380 LEU n 
1 4381 HIS n 
1 4382 THR n 
1 4383 THR n 
1 4384 ALA n 
1 4385 SER n 
1 4386 ASN n 
1 4387 TRP n 
1 4388 LEU n 
1 4389 HIS n 
1 4390 LEU n 
1 4391 ILE n 
1 4392 PRO n 
1 4393 GLN n 
1 4394 THR n 
1 4395 LEU n 
1 4396 SER n 
1 4397 HIS n 
1 4398 LEU n 
1 4399 LYS n 
1 4400 ARG n 
1 4401 THR n 
1 4402 VAL n 
1 4403 GLU n 
1 4404 ASN n 
1 4405 ILE n 
1 4406 LYS n 
1 4407 ASP n 
1 4408 PRO n 
1 4409 LEU n 
1 4410 PHE n 
1 4411 ARG n 
1 4412 PHE n 
1 4413 PHE n 
1 4414 GLU n 
1 4415 ARG n 
1 4416 GLU n 
1 4417 VAL n 
1 4418 LYS n 
1 4419 MET n 
1 4420 GLY n 
1 4421 ALA n 
1 4422 LYS n 
1 4423 LEU n 
1 4424 LEU n 
1 4425 GLN n 
1 4426 ASP n 
1 4427 VAL n 
1 4428 ARG n 
1 4429 GLN n 
1 4430 ASP n 
1 4431 LEU n 
1 4432 ALA n 
1 4433 ASP n 
1 4434 VAL n 
1 4435 VAL n 
1 4436 GLN n 
1 4437 VAL n 
1 4438 CYS n 
1 4439 GLU n 
1 4440 GLY n 
1 4441 LYS n 
1 4442 LYS n 
1 4443 LYS n 
1 4444 GLN n 
1 4445 THR n 
1 4446 ASN n 
1 4447 TYR n 
1 4448 LEU n 
1 4449 ARG n 
1 4450 THR n 
1 4451 LEU n 
1 4452 ILE n 
1 4453 ASN n 
1 4454 GLU n 
1 4455 LEU n 
1 4456 VAL n 
1 4457 LYS n 
1 4458 GLY n 
1 4459 ILE n 
1 4460 LEU n 
1 4461 PRO n 
1 4462 ARG n 
1 4463 SER n 
1 4464 TRP n 
1 4465 SER n 
1 4466 HIS n 
1 4467 TYR n 
1 4468 THR n 
1 4469 VAL n 
1 4470 PRO n 
1 4471 ALA n 
1 4472 GLY n 
1 4473 MET n 
1 4474 THR n 
1 4475 VAL n 
1 4476 ILE n 
1 4477 GLN n 
1 4478 TRP n 
1 4479 VAL n 
1 4480 SER n 
1 4481 ASP n 
1 4482 PHE n 
1 4483 SER n 
1 4484 GLU n 
1 4485 ARG n 
1 4486 ILE n 
1 4487 LYS n 
1 4488 GLN n 
1 4489 LEU n 
1 4490 GLN n 
1 4491 ASN n 
1 4492 ILE n 
1 4493 SER n 
1 4494 LEU n 
1 4495 ALA n 
1 4496 ALA n 
1 4497 ALA n 
1 4498 SER n 
1 4499 GLY n 
1 4500 GLY n 
1 4501 ALA n 
1 4502 LYS n 
1 4503 GLU n 
1 4504 LEU n 
1 4505 LYS n 
1 4506 ASN n 
1 4507 ILE n 
1 4508 HIS n 
1 4509 VAL n 
1 4510 CYS n 
1 4511 LEU n 
1 4512 GLY n 
1 4513 GLY n 
1 4514 LEU n 
1 4515 PHE n 
1 4516 VAL n 
1 4517 PRO n 
1 4518 GLU n 
1 4519 ALA n 
1 4520 TYR n 
1 4521 ILE n 
1 4522 THR n 
1 4523 ALA n 
1 4524 THR n 
1 4525 ARG n 
1 4526 GLN n 
1 4527 TYR n 
1 4528 VAL n 
1 4529 ALA n 
1 4530 GLN n 
1 4531 ALA n 
1 4532 ASN n 
1 4533 SER n 
1 4534 TRP n 
1 4535 SER n 
1 4536 LEU n 
1 4537 GLU n 
1 4538 GLU n 
1 4539 LEU n 
1 4540 CYS n 
1 4541 LEU n 
1 4542 GLU n 
1 4543 VAL n 
1 4544 ASN n 
1 4545 VAL n 
1 4546 THR n 
1 4547 THR n 
1 4548 SER n 
1 4549 GLN n 
1 4550 GLY n 
1 4551 ALA n 
1 4552 THR n 
1 4553 LEU n 
1 4554 ASP n 
1 4555 ALA n 
1 4556 CYS n 
1 4557 SER n 
1 4558 PHE n 
1 4559 GLY n 
1 4560 VAL n 
1 4561 THR n 
1 4562 GLY n 
1 4563 LEU n 
1 4564 LYS n 
1 4565 LEU n 
1 4566 GLN n 
1 4567 GLY n 
1 4568 ALA n 
1 4569 THR n 
1 4570 CYS n 
1 4571 ASN n 
1 4572 ASN n 
1 4573 ASN n 
1 4574 LYS n 
1 4575 LEU n 
1 4576 SER n 
1 4577 LEU n 
1 4578 SER n 
1 4579 ASN n 
1 4580 ALA n 
1 4581 ILE n 
1 4582 SER n 
1 4583 THR n 
1 4584 ALA n 
1 4585 LEU n 
1 4586 PRO n 
1 4587 LEU n 
1 4588 THR n 
1 4589 GLN n 
1 4590 LEU n 
1 4591 ARG n 
1 4592 TRP n 
1 4593 VAL n 
1 4594 LYS n 
1 4595 GLN n 
1 4596 THR n 
1 4597 ASN n 
1 4598 THR n 
1 4599 GLU n 
1 4600 LYS n 
1 4601 LYS n 
1 4602 ALA n 
1 4603 SER n 
1 4604 VAL n 
1 4605 VAL n 
1 4606 THR n 
1 4607 LEU n 
1 4608 PRO n 
1 4609 VAL n 
1 4610 TYR n 
1 4611 LEU n 
1 4612 ASN n 
1 4613 PHE n 
1 4614 THR n 
1 4615 ARG n 
1 4616 ALA n 
1 4617 ASP n 
1 4618 LEU n 
1 4619 ILE n 
1 4620 PHE n 
1 4621 THR n 
1 4622 VAL n 
1 4623 ASP n 
1 4624 PHE n 
1 4625 GLU n 
1 4626 ILE n 
1 4627 ALA n 
1 4628 THR n 
1 4629 LYS n 
1 4630 GLU n 
1 4631 ASP n 
1 4632 PRO n 
1 4633 ARG n 
1 4634 SER n 
1 4635 PHE n 
1 4636 TYR n 
1 4637 GLU n 
1 4638 ARG n 
1 4639 GLY n 
1 4640 VAL n 
1 4641 ALA n 
1 4642 VAL n 
1 4643 LEU n 
1 4644 CYS n 
1 4645 THR n 
1 4646 GLU n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   4646 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'DYNC1H1, DHC1, DNCH1, DNCL, DNECL, DYHC, KIAA0325' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Spodoptera frugiperda' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     7108 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ADP non-polymer         n "ADENOSINE-5'-DIPHOSPHATE"  ? 'C10 H15 N5 O10 P2' 427.201 
ALA 'L-peptide linking' y ALANINE                     ? 'C3 H7 N O2'        89.093  
ARG 'L-peptide linking' y ARGININE                    ? 'C6 H15 N4 O2 1'    175.209 
ASN 'L-peptide linking' y ASPARAGINE                  ? 'C4 H8 N2 O3'       132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'             ? 'C4 H7 N O4'        133.103 
ATP non-polymer         . "ADENOSINE-5'-TRIPHOSPHATE" ? 'C10 H16 N5 O13 P3' 507.181 
CYS 'L-peptide linking' y CYSTEINE                    ? 'C3 H7 N O2 S'      121.158 
GLN 'L-peptide linking' y GLUTAMINE                   ? 'C5 H10 N2 O3'      146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'             ? 'C5 H9 N O4'        147.129 
GLY 'peptide linking'   y GLYCINE                     ? 'C2 H5 N O2'        75.067  
HIS 'L-peptide linking' y HISTIDINE                   ? 'C6 H10 N3 O2 1'    156.162 
ILE 'L-peptide linking' y ISOLEUCINE                  ? 'C6 H13 N O2'       131.173 
LEU 'L-peptide linking' y LEUCINE                     ? 'C6 H13 N O2'       131.173 
LYS 'L-peptide linking' y LYSINE                      ? 'C6 H15 N2 O2 1'    147.195 
MET 'L-peptide linking' y METHIONINE                  ? 'C5 H11 N O2 S'     149.211 
MG  non-polymer         . 'MAGNESIUM ION'             ? 'Mg 2'              24.305  
PHE 'L-peptide linking' y PHENYLALANINE               ? 'C9 H11 N O2'       165.189 
PRO 'L-peptide linking' y PROLINE                     ? 'C5 H9 N O2'        115.130 
SER 'L-peptide linking' y SERINE                      ? 'C3 H7 N O3'        105.093 
THR 'L-peptide linking' y THREONINE                   ? 'C4 H9 N O3'        119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                  ? 'C11 H12 N2 O2'     204.225 
TYR 'L-peptide linking' y TYROSINE                    ? 'C9 H11 N O3'       181.189 
VAL 'L-peptide linking' y VALINE                      ? 'C5 H11 N O2'       117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1    MET 1    1    ?    ?   ?   A . n 
A 1 2    SER 2    2    ?    ?   ?   A . n 
A 1 3    GLU 3    3    ?    ?   ?   A . n 
A 1 4    PRO 4    4    ?    ?   ?   A . n 
A 1 5    GLY 5    5    ?    ?   ?   A . n 
A 1 6    GLY 6    6    ?    ?   ?   A . n 
A 1 7    GLY 7    7    ?    ?   ?   A . n 
A 1 8    GLY 8    8    ?    ?   ?   A . n 
A 1 9    GLY 9    9    ?    ?   ?   A . n 
A 1 10   GLU 10   10   ?    ?   ?   A . n 
A 1 11   ASP 11   11   ?    ?   ?   A . n 
A 1 12   GLY 12   12   ?    ?   ?   A . n 
A 1 13   SER 13   13   ?    ?   ?   A . n 
A 1 14   ALA 14   14   ?    ?   ?   A . n 
A 1 15   GLY 15   15   ?    ?   ?   A . n 
A 1 16   LEU 16   16   ?    ?   ?   A . n 
A 1 17   GLU 17   17   ?    ?   ?   A . n 
A 1 18   VAL 18   18   ?    ?   ?   A . n 
A 1 19   SER 19   19   ?    ?   ?   A . n 
A 1 20   ALA 20   20   ?    ?   ?   A . n 
A 1 21   VAL 21   21   ?    ?   ?   A . n 
A 1 22   GLN 22   22   ?    ?   ?   A . n 
A 1 23   ASN 23   23   ?    ?   ?   A . n 
A 1 24   VAL 24   24   ?    ?   ?   A . n 
A 1 25   ALA 25   25   ?    ?   ?   A . n 
A 1 26   ASP 26   26   ?    ?   ?   A . n 
A 1 27   VAL 27   27   ?    ?   ?   A . n 
A 1 28   SER 28   28   ?    ?   ?   A . n 
A 1 29   VAL 29   29   ?    ?   ?   A . n 
A 1 30   LEU 30   30   ?    ?   ?   A . n 
A 1 31   GLN 31   31   ?    ?   ?   A . n 
A 1 32   LYS 32   32   ?    ?   ?   A . n 
A 1 33   HIS 33   33   ?    ?   ?   A . n 
A 1 34   LEU 34   34   ?    ?   ?   A . n 
A 1 35   ARG 35   35   ?    ?   ?   A . n 
A 1 36   LYS 36   36   ?    ?   ?   A . n 
A 1 37   LEU 37   37   ?    ?   ?   A . n 
A 1 38   VAL 38   38   ?    ?   ?   A . n 
A 1 39   PRO 39   39   ?    ?   ?   A . n 
A 1 40   LEU 40   40   ?    ?   ?   A . n 
A 1 41   LEU 41   41   ?    ?   ?   A . n 
A 1 42   LEU 42   42   ?    ?   ?   A . n 
A 1 43   GLU 43   43   ?    ?   ?   A . n 
A 1 44   ASP 44   44   ?    ?   ?   A . n 
A 1 45   GLY 45   45   ?    ?   ?   A . n 
A 1 46   GLY 46   46   ?    ?   ?   A . n 
A 1 47   GLU 47   47   ?    ?   ?   A . n 
A 1 48   ALA 48   48   ?    ?   ?   A . n 
A 1 49   PRO 49   49   ?    ?   ?   A . n 
A 1 50   ALA 50   50   ?    ?   ?   A . n 
A 1 51   ALA 51   51   ?    ?   ?   A . n 
A 1 52   LEU 52   52   ?    ?   ?   A . n 
A 1 53   GLU 53   53   ?    ?   ?   A . n 
A 1 54   ALA 54   54   ?    ?   ?   A . n 
A 1 55   ALA 55   55   ?    ?   ?   A . n 
A 1 56   LEU 56   56   ?    ?   ?   A . n 
A 1 57   GLU 57   57   ?    ?   ?   A . n 
A 1 58   GLU 58   58   ?    ?   ?   A . n 
A 1 59   LYS 59   59   ?    ?   ?   A . n 
A 1 60   SER 60   60   ?    ?   ?   A . n 
A 1 61   ALA 61   61   ?    ?   ?   A . n 
A 1 62   LEU 62   62   ?    ?   ?   A . n 
A 1 63   GLU 63   63   ?    ?   ?   A . n 
A 1 64   GLN 64   64   ?    ?   ?   A . n 
A 1 65   MET 65   65   ?    ?   ?   A . n 
A 1 66   ARG 66   66   ?    ?   ?   A . n 
A 1 67   LYS 67   67   ?    ?   ?   A . n 
A 1 68   PHE 68   68   ?    ?   ?   A . n 
A 1 69   LEU 69   69   ?    ?   ?   A . n 
A 1 70   SER 70   70   ?    ?   ?   A . n 
A 1 71   ASP 71   71   ?    ?   ?   A . n 
A 1 72   PRO 72   72   ?    ?   ?   A . n 
A 1 73   GLN 73   73   ?    ?   ?   A . n 
A 1 74   VAL 74   74   ?    ?   ?   A . n 
A 1 75   HIS 75   75   ?    ?   ?   A . n 
A 1 76   THR 76   76   ?    ?   ?   A . n 
A 1 77   VAL 77   77   ?    ?   ?   A . n 
A 1 78   LEU 78   78   ?    ?   ?   A . n 
A 1 79   VAL 79   79   ?    ?   ?   A . n 
A 1 80   GLU 80   80   ?    ?   ?   A . n 
A 1 81   ARG 81   81   ?    ?   ?   A . n 
A 1 82   SER 82   82   ?    ?   ?   A . n 
A 1 83   THR 83   83   ?    ?   ?   A . n 
A 1 84   LEU 84   84   ?    ?   ?   A . n 
A 1 85   LYS 85   85   ?    ?   ?   A . n 
A 1 86   GLU 86   86   ?    ?   ?   A . n 
A 1 87   ASP 87   87   ?    ?   ?   A . n 
A 1 88   VAL 88   88   ?    ?   ?   A . n 
A 1 89   GLY 89   89   ?    ?   ?   A . n 
A 1 90   ASP 90   90   ?    ?   ?   A . n 
A 1 91   GLU 91   91   ?    ?   ?   A . n 
A 1 92   GLY 92   92   ?    ?   ?   A . n 
A 1 93   GLU 93   93   ?    ?   ?   A . n 
A 1 94   GLU 94   94   ?    ?   ?   A . n 
A 1 95   GLU 95   95   ?    ?   ?   A . n 
A 1 96   LYS 96   96   ?    ?   ?   A . n 
A 1 97   GLU 97   97   ?    ?   ?   A . n 
A 1 98   PHE 98   98   ?    ?   ?   A . n 
A 1 99   ILE 99   99   ?    ?   ?   A . n 
A 1 100  SER 100  100  ?    ?   ?   A . n 
A 1 101  TYR 101  101  ?    ?   ?   A . n 
A 1 102  ASN 102  102  ?    ?   ?   A . n 
A 1 103  ILE 103  103  ?    ?   ?   A . n 
A 1 104  ASN 104  104  ?    ?   ?   A . n 
A 1 105  ILE 105  105  ?    ?   ?   A . n 
A 1 106  ASP 106  106  ?    ?   ?   A . n 
A 1 107  ILE 107  107  ?    ?   ?   A . n 
A 1 108  HIS 108  108  ?    ?   ?   A . n 
A 1 109  TYR 109  109  ?    ?   ?   A . n 
A 1 110  GLY 110  110  ?    ?   ?   A . n 
A 1 111  VAL 111  111  ?    ?   ?   A . n 
A 1 112  LYS 112  112  ?    ?   ?   A . n 
A 1 113  SER 113  113  ?    ?   ?   A . n 
A 1 114  ASN 114  114  ?    ?   ?   A . n 
A 1 115  SER 115  115  ?    ?   ?   A . n 
A 1 116  LEU 116  116  ?    ?   ?   A . n 
A 1 117  ALA 117  117  ?    ?   ?   A . n 
A 1 118  PHE 118  118  ?    ?   ?   A . n 
A 1 119  ILE 119  119  ?    ?   ?   A . n 
A 1 120  LYS 120  120  ?    ?   ?   A . n 
A 1 121  ARG 121  121  ?    ?   ?   A . n 
A 1 122  THR 122  122  ?    ?   ?   A . n 
A 1 123  PRO 123  123  ?    ?   ?   A . n 
A 1 124  VAL 124  124  ?    ?   ?   A . n 
A 1 125  ILE 125  125  ?    ?   ?   A . n 
A 1 126  ASP 126  126  ?    ?   ?   A . n 
A 1 127  ALA 127  127  ?    ?   ?   A . n 
A 1 128  ASP 128  128  ?    ?   ?   A . n 
A 1 129  LYS 129  129  ?    ?   ?   A . n 
A 1 130  PRO 130  130  ?    ?   ?   A . n 
A 1 131  VAL 131  131  ?    ?   ?   A . n 
A 1 132  SER 132  132  ?    ?   ?   A . n 
A 1 133  SER 133  133  ?    ?   ?   A . n 
A 1 134  GLN 134  134  ?    ?   ?   A . n 
A 1 135  LEU 135  135  ?    ?   ?   A . n 
A 1 136  ARG 136  136  ?    ?   ?   A . n 
A 1 137  VAL 137  137  ?    ?   ?   A . n 
A 1 138  LEU 138  138  ?    ?   ?   A . n 
A 1 139  THR 139  139  ?    ?   ?   A . n 
A 1 140  LEU 140  140  ?    ?   ?   A . n 
A 1 141  SER 141  141  ?    ?   ?   A . n 
A 1 142  GLU 142  142  ?    ?   ?   A . n 
A 1 143  ASP 143  143  ?    ?   ?   A . n 
A 1 144  SER 144  144  ?    ?   ?   A . n 
A 1 145  PRO 145  145  ?    ?   ?   A . n 
A 1 146  TYR 146  146  ?    ?   ?   A . n 
A 1 147  GLU 147  147  ?    ?   ?   A . n 
A 1 148  THR 148  148  ?    ?   ?   A . n 
A 1 149  LEU 149  149  ?    ?   ?   A . n 
A 1 150  HIS 150  150  ?    ?   ?   A . n 
A 1 151  SER 151  151  ?    ?   ?   A . n 
A 1 152  PHE 152  152  ?    ?   ?   A . n 
A 1 153  ILE 153  153  ?    ?   ?   A . n 
A 1 154  SER 154  154  ?    ?   ?   A . n 
A 1 155  ASN 155  155  ?    ?   ?   A . n 
A 1 156  ALA 156  156  ?    ?   ?   A . n 
A 1 157  VAL 157  157  ?    ?   ?   A . n 
A 1 158  ALA 158  158  ?    ?   ?   A . n 
A 1 159  PRO 159  159  ?    ?   ?   A . n 
A 1 160  PHE 160  160  ?    ?   ?   A . n 
A 1 161  PHE 161  161  ?    ?   ?   A . n 
A 1 162  LYS 162  162  ?    ?   ?   A . n 
A 1 163  SER 163  163  ?    ?   ?   A . n 
A 1 164  TYR 164  164  ?    ?   ?   A . n 
A 1 165  ILE 165  165  ?    ?   ?   A . n 
A 1 166  ARG 166  166  ?    ?   ?   A . n 
A 1 167  GLU 167  167  ?    ?   ?   A . n 
A 1 168  SER 168  168  ?    ?   ?   A . n 
A 1 169  GLY 169  169  ?    ?   ?   A . n 
A 1 170  LYS 170  170  ?    ?   ?   A . n 
A 1 171  ALA 171  171  ?    ?   ?   A . n 
A 1 172  ASP 172  172  ?    ?   ?   A . n 
A 1 173  ARG 173  173  ?    ?   ?   A . n 
A 1 174  ASP 174  174  ?    ?   ?   A . n 
A 1 175  GLY 175  175  ?    ?   ?   A . n 
A 1 176  ASP 176  176  ?    ?   ?   A . n 
A 1 177  LYS 177  177  ?    ?   ?   A . n 
A 1 178  MET 178  178  ?    ?   ?   A . n 
A 1 179  ALA 179  179  ?    ?   ?   A . n 
A 1 180  PRO 180  180  ?    ?   ?   A . n 
A 1 181  SER 181  181  ?    ?   ?   A . n 
A 1 182  VAL 182  182  ?    ?   ?   A . n 
A 1 183  GLU 183  183  ?    ?   ?   A . n 
A 1 184  LYS 184  184  ?    ?   ?   A . n 
A 1 185  LYS 185  185  ?    ?   ?   A . n 
A 1 186  ILE 186  186  ?    ?   ?   A . n 
A 1 187  ALA 187  187  ?    ?   ?   A . n 
A 1 188  GLU 188  188  ?    ?   ?   A . n 
A 1 189  LEU 189  189  ?    ?   ?   A . n 
A 1 190  GLU 190  190  ?    ?   ?   A . n 
A 1 191  MET 191  191  ?    ?   ?   A . n 
A 1 192  GLY 192  192  ?    ?   ?   A . n 
A 1 193  LEU 193  193  ?    ?   ?   A . n 
A 1 194  LEU 194  194  ?    ?   ?   A . n 
A 1 195  HIS 195  195  ?    ?   ?   A . n 
A 1 196  LEU 196  196  ?    ?   ?   A . n 
A 1 197  GLN 197  197  ?    ?   ?   A . n 
A 1 198  GLN 198  198  ?    ?   ?   A . n 
A 1 199  ASN 199  199  ?    ?   ?   A . n 
A 1 200  ILE 200  200  ?    ?   ?   A . n 
A 1 201  GLU 201  201  ?    ?   ?   A . n 
A 1 202  ILE 202  202  ?    ?   ?   A . n 
A 1 203  PRO 203  203  ?    ?   ?   A . n 
A 1 204  GLU 204  204  ?    ?   ?   A . n 
A 1 205  ILE 205  205  ?    ?   ?   A . n 
A 1 206  SER 206  206  ?    ?   ?   A . n 
A 1 207  LEU 207  207  ?    ?   ?   A . n 
A 1 208  PRO 208  208  ?    ?   ?   A . n 
A 1 209  ILE 209  209  ?    ?   ?   A . n 
A 1 210  HIS 210  210  ?    ?   ?   A . n 
A 1 211  PRO 211  211  ?    ?   ?   A . n 
A 1 212  MET 212  212  ?    ?   ?   A . n 
A 1 213  ILE 213  213  ?    ?   ?   A . n 
A 1 214  THR 214  214  ?    ?   ?   A . n 
A 1 215  ASN 215  215  ?    ?   ?   A . n 
A 1 216  VAL 216  216  ?    ?   ?   A . n 
A 1 217  ALA 217  217  ?    ?   ?   A . n 
A 1 218  LYS 218  218  ?    ?   ?   A . n 
A 1 219  GLN 219  219  ?    ?   ?   A . n 
A 1 220  CYS 220  220  ?    ?   ?   A . n 
A 1 221  TYR 221  221  ?    ?   ?   A . n 
A 1 222  GLU 222  222  ?    ?   ?   A . n 
A 1 223  ARG 223  223  ?    ?   ?   A . n 
A 1 224  GLY 224  224  ?    ?   ?   A . n 
A 1 225  GLU 225  225  ?    ?   ?   A . n 
A 1 226  LYS 226  226  ?    ?   ?   A . n 
A 1 227  PRO 227  227  ?    ?   ?   A . n 
A 1 228  LYS 228  228  ?    ?   ?   A . n 
A 1 229  VAL 229  229  ?    ?   ?   A . n 
A 1 230  THR 230  230  ?    ?   ?   A . n 
A 1 231  ASP 231  231  ?    ?   ?   A . n 
A 1 232  PHE 232  232  ?    ?   ?   A . n 
A 1 233  GLY 233  233  ?    ?   ?   A . n 
A 1 234  ASP 234  234  ?    ?   ?   A . n 
A 1 235  LYS 235  235  ?    ?   ?   A . n 
A 1 236  VAL 236  236  ?    ?   ?   A . n 
A 1 237  GLU 237  237  ?    ?   ?   A . n 
A 1 238  ASP 238  238  ?    ?   ?   A . n 
A 1 239  PRO 239  239  ?    ?   ?   A . n 
A 1 240  THR 240  240  ?    ?   ?   A . n 
A 1 241  PHE 241  241  ?    ?   ?   A . n 
A 1 242  LEU 242  242  ?    ?   ?   A . n 
A 1 243  ASN 243  243  ?    ?   ?   A . n 
A 1 244  GLN 244  244  ?    ?   ?   A . n 
A 1 245  LEU 245  245  ?    ?   ?   A . n 
A 1 246  GLN 246  246  ?    ?   ?   A . n 
A 1 247  SER 247  247  ?    ?   ?   A . n 
A 1 248  GLY 248  248  ?    ?   ?   A . n 
A 1 249  VAL 249  249  ?    ?   ?   A . n 
A 1 250  ASN 250  250  ?    ?   ?   A . n 
A 1 251  ARG 251  251  ?    ?   ?   A . n 
A 1 252  TRP 252  252  ?    ?   ?   A . n 
A 1 253  ILE 253  253  ?    ?   ?   A . n 
A 1 254  ARG 254  254  ?    ?   ?   A . n 
A 1 255  GLU 255  255  ?    ?   ?   A . n 
A 1 256  ILE 256  256  ?    ?   ?   A . n 
A 1 257  GLN 257  257  ?    ?   ?   A . n 
A 1 258  LYS 258  258  ?    ?   ?   A . n 
A 1 259  VAL 259  259  ?    ?   ?   A . n 
A 1 260  THR 260  260  ?    ?   ?   A . n 
A 1 261  LYS 261  261  ?    ?   ?   A . n 
A 1 262  LEU 262  262  ?    ?   ?   A . n 
A 1 263  ASP 263  263  ?    ?   ?   A . n 
A 1 264  ARG 264  264  ?    ?   ?   A . n 
A 1 265  ASP 265  265  ?    ?   ?   A . n 
A 1 266  PRO 266  266  ?    ?   ?   A . n 
A 1 267  ALA 267  267  ?    ?   ?   A . n 
A 1 268  SER 268  268  ?    ?   ?   A . n 
A 1 269  GLY 269  269  ?    ?   ?   A . n 
A 1 270  THR 270  270  ?    ?   ?   A . n 
A 1 271  ALA 271  271  ?    ?   ?   A . n 
A 1 272  LEU 272  272  ?    ?   ?   A . n 
A 1 273  GLN 273  273  ?    ?   ?   A . n 
A 1 274  GLU 274  274  ?    ?   ?   A . n 
A 1 275  ILE 275  275  ?    ?   ?   A . n 
A 1 276  SER 276  276  ?    ?   ?   A . n 
A 1 277  PHE 277  277  ?    ?   ?   A . n 
A 1 278  TRP 278  278  ?    ?   ?   A . n 
A 1 279  LEU 279  279  ?    ?   ?   A . n 
A 1 280  ASN 280  280  ?    ?   ?   A . n 
A 1 281  LEU 281  281  ?    ?   ?   A . n 
A 1 282  GLU 282  282  ?    ?   ?   A . n 
A 1 283  ARG 283  283  ?    ?   ?   A . n 
A 1 284  ALA 284  284  ?    ?   ?   A . n 
A 1 285  LEU 285  285  ?    ?   ?   A . n 
A 1 286  TYR 286  286  ?    ?   ?   A . n 
A 1 287  ARG 287  287  ?    ?   ?   A . n 
A 1 288  ILE 288  288  ?    ?   ?   A . n 
A 1 289  GLN 289  289  ?    ?   ?   A . n 
A 1 290  GLU 290  290  ?    ?   ?   A . n 
A 1 291  LYS 291  291  ?    ?   ?   A . n 
A 1 292  ARG 292  292  ?    ?   ?   A . n 
A 1 293  GLU 293  293  ?    ?   ?   A . n 
A 1 294  SER 294  294  ?    ?   ?   A . n 
A 1 295  PRO 295  295  ?    ?   ?   A . n 
A 1 296  GLU 296  296  ?    ?   ?   A . n 
A 1 297  VAL 297  297  ?    ?   ?   A . n 
A 1 298  LEU 298  298  ?    ?   ?   A . n 
A 1 299  LEU 299  299  ?    ?   ?   A . n 
A 1 300  THR 300  300  ?    ?   ?   A . n 
A 1 301  LEU 301  301  ?    ?   ?   A . n 
A 1 302  ASP 302  302  ?    ?   ?   A . n 
A 1 303  ILE 303  303  ?    ?   ?   A . n 
A 1 304  LEU 304  304  ?    ?   ?   A . n 
A 1 305  LYS 305  305  ?    ?   ?   A . n 
A 1 306  HIS 306  306  ?    ?   ?   A . n 
A 1 307  GLY 307  307  ?    ?   ?   A . n 
A 1 308  LYS 308  308  ?    ?   ?   A . n 
A 1 309  ARG 309  309  ?    ?   ?   A . n 
A 1 310  PHE 310  310  ?    ?   ?   A . n 
A 1 311  HIS 311  311  ?    ?   ?   A . n 
A 1 312  ALA 312  312  ?    ?   ?   A . n 
A 1 313  THR 313  313  ?    ?   ?   A . n 
A 1 314  VAL 314  314  ?    ?   ?   A . n 
A 1 315  SER 315  315  ?    ?   ?   A . n 
A 1 316  PHE 316  316  ?    ?   ?   A . n 
A 1 317  ASP 317  317  ?    ?   ?   A . n 
A 1 318  THR 318  318  ?    ?   ?   A . n 
A 1 319  ASP 319  319  ?    ?   ?   A . n 
A 1 320  THR 320  320  ?    ?   ?   A . n 
A 1 321  GLY 321  321  ?    ?   ?   A . n 
A 1 322  LEU 322  322  ?    ?   ?   A . n 
A 1 323  LYS 323  323  ?    ?   ?   A . n 
A 1 324  GLN 324  324  ?    ?   ?   A . n 
A 1 325  ALA 325  325  ?    ?   ?   A . n 
A 1 326  LEU 326  326  ?    ?   ?   A . n 
A 1 327  GLU 327  327  ?    ?   ?   A . n 
A 1 328  THR 328  328  ?    ?   ?   A . n 
A 1 329  VAL 329  329  ?    ?   ?   A . n 
A 1 330  ASN 330  330  ?    ?   ?   A . n 
A 1 331  ASP 331  331  ?    ?   ?   A . n 
A 1 332  TYR 332  332  ?    ?   ?   A . n 
A 1 333  ASN 333  333  ?    ?   ?   A . n 
A 1 334  PRO 334  334  ?    ?   ?   A . n 
A 1 335  LEU 335  335  ?    ?   ?   A . n 
A 1 336  MET 336  336  ?    ?   ?   A . n 
A 1 337  LYS 337  337  ?    ?   ?   A . n 
A 1 338  ASP 338  338  ?    ?   ?   A . n 
A 1 339  PHE 339  339  ?    ?   ?   A . n 
A 1 340  PRO 340  340  ?    ?   ?   A . n 
A 1 341  LEU 341  341  ?    ?   ?   A . n 
A 1 342  ASN 342  342  ?    ?   ?   A . n 
A 1 343  ASP 343  343  ?    ?   ?   A . n 
A 1 344  LEU 344  344  ?    ?   ?   A . n 
A 1 345  LEU 345  345  ?    ?   ?   A . n 
A 1 346  SER 346  346  ?    ?   ?   A . n 
A 1 347  ALA 347  347  ?    ?   ?   A . n 
A 1 348  THR 348  348  ?    ?   ?   A . n 
A 1 349  GLU 349  349  ?    ?   ?   A . n 
A 1 350  LEU 350  350  ?    ?   ?   A . n 
A 1 351  ASP 351  351  ?    ?   ?   A . n 
A 1 352  LYS 352  352  ?    ?   ?   A . n 
A 1 353  ILE 353  353  ?    ?   ?   A . n 
A 1 354  ARG 354  354  ?    ?   ?   A . n 
A 1 355  GLN 355  355  ?    ?   ?   A . n 
A 1 356  ALA 356  356  ?    ?   ?   A . n 
A 1 357  LEU 357  357  ?    ?   ?   A . n 
A 1 358  VAL 358  358  ?    ?   ?   A . n 
A 1 359  ALA 359  359  ?    ?   ?   A . n 
A 1 360  ILE 360  360  ?    ?   ?   A . n 
A 1 361  PHE 361  361  ?    ?   ?   A . n 
A 1 362  THR 362  362  ?    ?   ?   A . n 
A 1 363  HIS 363  363  ?    ?   ?   A . n 
A 1 364  LEU 364  364  ?    ?   ?   A . n 
A 1 365  ARG 365  365  ?    ?   ?   A . n 
A 1 366  LYS 366  366  ?    ?   ?   A . n 
A 1 367  ILE 367  367  ?    ?   ?   A . n 
A 1 368  ARG 368  368  ?    ?   ?   A . n 
A 1 369  ASN 369  369  ?    ?   ?   A . n 
A 1 370  THR 370  370  ?    ?   ?   A . n 
A 1 371  LYS 371  371  ?    ?   ?   A . n 
A 1 372  TYR 372  372  ?    ?   ?   A . n 
A 1 373  PRO 373  373  ?    ?   ?   A . n 
A 1 374  ILE 374  374  ?    ?   ?   A . n 
A 1 375  GLN 375  375  ?    ?   ?   A . n 
A 1 376  ARG 376  376  ?    ?   ?   A . n 
A 1 377  ALA 377  377  ?    ?   ?   A . n 
A 1 378  LEU 378  378  ?    ?   ?   A . n 
A 1 379  ARG 379  379  ?    ?   ?   A . n 
A 1 380  LEU 380  380  ?    ?   ?   A . n 
A 1 381  VAL 381  381  ?    ?   ?   A . n 
A 1 382  GLU 382  382  ?    ?   ?   A . n 
A 1 383  ALA 383  383  ?    ?   ?   A . n 
A 1 384  ILE 384  384  ?    ?   ?   A . n 
A 1 385  SER 385  385  ?    ?   ?   A . n 
A 1 386  ARG 386  386  ?    ?   ?   A . n 
A 1 387  ASP 387  387  ?    ?   ?   A . n 
A 1 388  LEU 388  388  ?    ?   ?   A . n 
A 1 389  SER 389  389  ?    ?   ?   A . n 
A 1 390  SER 390  390  ?    ?   ?   A . n 
A 1 391  GLN 391  391  ?    ?   ?   A . n 
A 1 392  LEU 392  392  ?    ?   ?   A . n 
A 1 393  LEU 393  393  ?    ?   ?   A . n 
A 1 394  LYS 394  394  ?    ?   ?   A . n 
A 1 395  VAL 395  395  ?    ?   ?   A . n 
A 1 396  LEU 396  396  ?    ?   ?   A . n 
A 1 397  GLY 397  397  ?    ?   ?   A . n 
A 1 398  THR 398  398  ?    ?   ?   A . n 
A 1 399  ARG 399  399  ?    ?   ?   A . n 
A 1 400  LYS 400  400  ?    ?   ?   A . n 
A 1 401  LEU 401  401  ?    ?   ?   A . n 
A 1 402  MET 402  402  ?    ?   ?   A . n 
A 1 403  HIS 403  403  ?    ?   ?   A . n 
A 1 404  VAL 404  404  ?    ?   ?   A . n 
A 1 405  ALA 405  405  ?    ?   ?   A . n 
A 1 406  TYR 406  406  ?    ?   ?   A . n 
A 1 407  GLU 407  407  ?    ?   ?   A . n 
A 1 408  GLU 408  408  ?    ?   ?   A . n 
A 1 409  PHE 409  409  ?    ?   ?   A . n 
A 1 410  GLU 410  410  ?    ?   ?   A . n 
A 1 411  LYS 411  411  ?    ?   ?   A . n 
A 1 412  VAL 412  412  ?    ?   ?   A . n 
A 1 413  MET 413  413  ?    ?   ?   A . n 
A 1 414  VAL 414  414  ?    ?   ?   A . n 
A 1 415  ALA 415  415  ?    ?   ?   A . n 
A 1 416  CYS 416  416  ?    ?   ?   A . n 
A 1 417  PHE 417  417  ?    ?   ?   A . n 
A 1 418  GLU 418  418  ?    ?   ?   A . n 
A 1 419  VAL 419  419  ?    ?   ?   A . n 
A 1 420  PHE 420  420  ?    ?   ?   A . n 
A 1 421  GLN 421  421  ?    ?   ?   A . n 
A 1 422  THR 422  422  ?    ?   ?   A . n 
A 1 423  TRP 423  423  ?    ?   ?   A . n 
A 1 424  ASP 424  424  ?    ?   ?   A . n 
A 1 425  ASP 425  425  ?    ?   ?   A . n 
A 1 426  GLU 426  426  ?    ?   ?   A . n 
A 1 427  TYR 427  427  ?    ?   ?   A . n 
A 1 428  GLU 428  428  ?    ?   ?   A . n 
A 1 429  LYS 429  429  ?    ?   ?   A . n 
A 1 430  LEU 430  430  ?    ?   ?   A . n 
A 1 431  GLN 431  431  ?    ?   ?   A . n 
A 1 432  VAL 432  432  ?    ?   ?   A . n 
A 1 433  LEU 433  433  ?    ?   ?   A . n 
A 1 434  LEU 434  434  ?    ?   ?   A . n 
A 1 435  ARG 435  435  ?    ?   ?   A . n 
A 1 436  ASP 436  436  ?    ?   ?   A . n 
A 1 437  ILE 437  437  ?    ?   ?   A . n 
A 1 438  VAL 438  438  ?    ?   ?   A . n 
A 1 439  LYS 439  439  ?    ?   ?   A . n 
A 1 440  ARG 440  440  ?    ?   ?   A . n 
A 1 441  LYS 441  441  ?    ?   ?   A . n 
A 1 442  ARG 442  442  ?    ?   ?   A . n 
A 1 443  GLU 443  443  ?    ?   ?   A . n 
A 1 444  GLU 444  444  ?    ?   ?   A . n 
A 1 445  ASN 445  445  ?    ?   ?   A . n 
A 1 446  LEU 446  446  ?    ?   ?   A . n 
A 1 447  LYS 447  447  ?    ?   ?   A . n 
A 1 448  MET 448  448  ?    ?   ?   A . n 
A 1 449  VAL 449  449  ?    ?   ?   A . n 
A 1 450  TRP 450  450  ?    ?   ?   A . n 
A 1 451  ARG 451  451  ?    ?   ?   A . n 
A 1 452  ILE 452  452  ?    ?   ?   A . n 
A 1 453  ASN 453  453  ?    ?   ?   A . n 
A 1 454  PRO 454  454  ?    ?   ?   A . n 
A 1 455  ALA 455  455  ?    ?   ?   A . n 
A 1 456  HIS 456  456  ?    ?   ?   A . n 
A 1 457  ARG 457  457  ?    ?   ?   A . n 
A 1 458  LYS 458  458  ?    ?   ?   A . n 
A 1 459  LEU 459  459  ?    ?   ?   A . n 
A 1 460  GLN 460  460  ?    ?   ?   A . n 
A 1 461  ALA 461  461  ?    ?   ?   A . n 
A 1 462  ARG 462  462  ?    ?   ?   A . n 
A 1 463  LEU 463  463  ?    ?   ?   A . n 
A 1 464  ASP 464  464  ?    ?   ?   A . n 
A 1 465  GLN 465  465  ?    ?   ?   A . n 
A 1 466  MET 466  466  ?    ?   ?   A . n 
A 1 467  ARG 467  467  ?    ?   ?   A . n 
A 1 468  LYS 468  468  ?    ?   ?   A . n 
A 1 469  PHE 469  469  ?    ?   ?   A . n 
A 1 470  ARG 470  470  ?    ?   ?   A . n 
A 1 471  ARG 471  471  ?    ?   ?   A . n 
A 1 472  GLN 472  472  ?    ?   ?   A . n 
A 1 473  HIS 473  473  ?    ?   ?   A . n 
A 1 474  GLU 474  474  ?    ?   ?   A . n 
A 1 475  GLN 475  475  ?    ?   ?   A . n 
A 1 476  LEU 476  476  ?    ?   ?   A . n 
A 1 477  ARG 477  477  ?    ?   ?   A . n 
A 1 478  ALA 478  478  ?    ?   ?   A . n 
A 1 479  VAL 479  479  ?    ?   ?   A . n 
A 1 480  ILE 480  480  ?    ?   ?   A . n 
A 1 481  VAL 481  481  ?    ?   ?   A . n 
A 1 482  ARG 482  482  ?    ?   ?   A . n 
A 1 483  VAL 483  483  ?    ?   ?   A . n 
A 1 484  LEU 484  484  ?    ?   ?   A . n 
A 1 485  ARG 485  485  ?    ?   ?   A . n 
A 1 486  PRO 486  486  ?    ?   ?   A . n 
A 1 487  GLN 487  487  ?    ?   ?   A . n 
A 1 488  VAL 488  488  ?    ?   ?   A . n 
A 1 489  THR 489  489  ?    ?   ?   A . n 
A 1 490  ALA 490  490  ?    ?   ?   A . n 
A 1 491  VAL 491  491  ?    ?   ?   A . n 
A 1 492  ALA 492  492  ?    ?   ?   A . n 
A 1 493  GLN 493  493  ?    ?   ?   A . n 
A 1 494  GLN 494  494  ?    ?   ?   A . n 
A 1 495  ASN 495  495  ?    ?   ?   A . n 
A 1 496  GLN 496  496  ?    ?   ?   A . n 
A 1 497  GLY 497  497  ?    ?   ?   A . n 
A 1 498  GLU 498  498  ?    ?   ?   A . n 
A 1 499  VAL 499  499  ?    ?   ?   A . n 
A 1 500  PRO 500  500  ?    ?   ?   A . n 
A 1 501  GLU 501  501  ?    ?   ?   A . n 
A 1 502  PRO 502  502  ?    ?   ?   A . n 
A 1 503  GLN 503  503  ?    ?   ?   A . n 
A 1 504  ASP 504  504  ?    ?   ?   A . n 
A 1 505  MET 505  505  ?    ?   ?   A . n 
A 1 506  LYS 506  506  ?    ?   ?   A . n 
A 1 507  VAL 507  507  ?    ?   ?   A . n 
A 1 508  ALA 508  508  ?    ?   ?   A . n 
A 1 509  GLU 509  509  ?    ?   ?   A . n 
A 1 510  VAL 510  510  ?    ?   ?   A . n 
A 1 511  LEU 511  511  ?    ?   ?   A . n 
A 1 512  PHE 512  512  ?    ?   ?   A . n 
A 1 513  ASP 513  513  ?    ?   ?   A . n 
A 1 514  ALA 514  514  ?    ?   ?   A . n 
A 1 515  ALA 515  515  ?    ?   ?   A . n 
A 1 516  ASP 516  516  ?    ?   ?   A . n 
A 1 517  ALA 517  517  ?    ?   ?   A . n 
A 1 518  ASN 518  518  ?    ?   ?   A . n 
A 1 519  ALA 519  519  ?    ?   ?   A . n 
A 1 520  ILE 520  520  ?    ?   ?   A . n 
A 1 521  GLU 521  521  ?    ?   ?   A . n 
A 1 522  GLU 522  522  ?    ?   ?   A . n 
A 1 523  VAL 523  523  ?    ?   ?   A . n 
A 1 524  ASN 524  524  ?    ?   ?   A . n 
A 1 525  LEU 525  525  ?    ?   ?   A . n 
A 1 526  ALA 526  526  ?    ?   ?   A . n 
A 1 527  TYR 527  527  ?    ?   ?   A . n 
A 1 528  GLU 528  528  ?    ?   ?   A . n 
A 1 529  ASN 529  529  ?    ?   ?   A . n 
A 1 530  VAL 530  530  ?    ?   ?   A . n 
A 1 531  LYS 531  531  ?    ?   ?   A . n 
A 1 532  GLU 532  532  ?    ?   ?   A . n 
A 1 533  VAL 533  533  ?    ?   ?   A . n 
A 1 534  ASP 534  534  ?    ?   ?   A . n 
A 1 535  GLY 535  535  ?    ?   ?   A . n 
A 1 536  LEU 536  536  ?    ?   ?   A . n 
A 1 537  ASP 537  537  ?    ?   ?   A . n 
A 1 538  VAL 538  538  ?    ?   ?   A . n 
A 1 539  SER 539  539  ?    ?   ?   A . n 
A 1 540  LYS 540  540  ?    ?   ?   A . n 
A 1 541  GLU 541  541  ?    ?   ?   A . n 
A 1 542  GLY 542  542  ?    ?   ?   A . n 
A 1 543  THR 543  543  ?    ?   ?   A . n 
A 1 544  GLU 544  544  ?    ?   ?   A . n 
A 1 545  ALA 545  545  ?    ?   ?   A . n 
A 1 546  TRP 546  546  ?    ?   ?   A . n 
A 1 547  GLU 547  547  ?    ?   ?   A . n 
A 1 548  ALA 548  548  ?    ?   ?   A . n 
A 1 549  ALA 549  549  ?    ?   ?   A . n 
A 1 550  MET 550  550  ?    ?   ?   A . n 
A 1 551  LYS 551  551  ?    ?   ?   A . n 
A 1 552  ARG 552  552  ?    ?   ?   A . n 
A 1 553  TYR 553  553  ?    ?   ?   A . n 
A 1 554  ASP 554  554  ?    ?   ?   A . n 
A 1 555  GLU 555  555  ?    ?   ?   A . n 
A 1 556  ARG 556  556  ?    ?   ?   A . n 
A 1 557  ILE 557  557  ?    ?   ?   A . n 
A 1 558  ASP 558  558  ?    ?   ?   A . n 
A 1 559  ARG 559  559  ?    ?   ?   A . n 
A 1 560  VAL 560  560  ?    ?   ?   A . n 
A 1 561  GLU 561  561  ?    ?   ?   A . n 
A 1 562  THR 562  562  ?    ?   ?   A . n 
A 1 563  ARG 563  563  ?    ?   ?   A . n 
A 1 564  ILE 564  564  ?    ?   ?   A . n 
A 1 565  THR 565  565  ?    ?   ?   A . n 
A 1 566  ALA 566  566  ?    ?   ?   A . n 
A 1 567  ARG 567  567  ?    ?   ?   A . n 
A 1 568  LEU 568  568  ?    ?   ?   A . n 
A 1 569  ARG 569  569  ?    ?   ?   A . n 
A 1 570  ASP 570  570  ?    ?   ?   A . n 
A 1 571  GLN 571  571  ?    ?   ?   A . n 
A 1 572  LEU 572  572  ?    ?   ?   A . n 
A 1 573  GLY 573  573  ?    ?   ?   A . n 
A 1 574  THR 574  574  ?    ?   ?   A . n 
A 1 575  ALA 575  575  ?    ?   ?   A . n 
A 1 576  LYS 576  576  ?    ?   ?   A . n 
A 1 577  ASN 577  577  ?    ?   ?   A . n 
A 1 578  ALA 578  578  ?    ?   ?   A . n 
A 1 579  ASN 579  579  ?    ?   ?   A . n 
A 1 580  GLU 580  580  ?    ?   ?   A . n 
A 1 581  MET 581  581  ?    ?   ?   A . n 
A 1 582  PHE 582  582  ?    ?   ?   A . n 
A 1 583  ARG 583  583  ?    ?   ?   A . n 
A 1 584  ILE 584  584  ?    ?   ?   A . n 
A 1 585  PHE 585  585  ?    ?   ?   A . n 
A 1 586  SER 586  586  ?    ?   ?   A . n 
A 1 587  ARG 587  587  ?    ?   ?   A . n 
A 1 588  PHE 588  588  ?    ?   ?   A . n 
A 1 589  ASN 589  589  ?    ?   ?   A . n 
A 1 590  ALA 590  590  ?    ?   ?   A . n 
A 1 591  LEU 591  591  ?    ?   ?   A . n 
A 1 592  PHE 592  592  ?    ?   ?   A . n 
A 1 593  VAL 593  593  ?    ?   ?   A . n 
A 1 594  ARG 594  594  ?    ?   ?   A . n 
A 1 595  PRO 595  595  ?    ?   ?   A . n 
A 1 596  HIS 596  596  ?    ?   ?   A . n 
A 1 597  ILE 597  597  ?    ?   ?   A . n 
A 1 598  ARG 598  598  ?    ?   ?   A . n 
A 1 599  GLY 599  599  ?    ?   ?   A . n 
A 1 600  ALA 600  600  ?    ?   ?   A . n 
A 1 601  ILE 601  601  ?    ?   ?   A . n 
A 1 602  ARG 602  602  ?    ?   ?   A . n 
A 1 603  GLU 603  603  ?    ?   ?   A . n 
A 1 604  TYR 604  604  ?    ?   ?   A . n 
A 1 605  GLN 605  605  ?    ?   ?   A . n 
A 1 606  THR 606  606  ?    ?   ?   A . n 
A 1 607  GLN 607  607  ?    ?   ?   A . n 
A 1 608  LEU 608  608  ?    ?   ?   A . n 
A 1 609  ILE 609  609  ?    ?   ?   A . n 
A 1 610  GLN 610  610  ?    ?   ?   A . n 
A 1 611  ARG 611  611  ?    ?   ?   A . n 
A 1 612  VAL 612  612  ?    ?   ?   A . n 
A 1 613  LYS 613  613  ?    ?   ?   A . n 
A 1 614  ASP 614  614  ?    ?   ?   A . n 
A 1 615  ASP 615  615  ?    ?   ?   A . n 
A 1 616  ILE 616  616  ?    ?   ?   A . n 
A 1 617  GLU 617  617  ?    ?   ?   A . n 
A 1 618  SER 618  618  ?    ?   ?   A . n 
A 1 619  LEU 619  619  ?    ?   ?   A . n 
A 1 620  HIS 620  620  ?    ?   ?   A . n 
A 1 621  ASP 621  621  ?    ?   ?   A . n 
A 1 622  LYS 622  622  ?    ?   ?   A . n 
A 1 623  PHE 623  623  ?    ?   ?   A . n 
A 1 624  LYS 624  624  ?    ?   ?   A . n 
A 1 625  VAL 625  625  ?    ?   ?   A . n 
A 1 626  GLN 626  626  ?    ?   ?   A . n 
A 1 627  TYR 627  627  ?    ?   ?   A . n 
A 1 628  PRO 628  628  ?    ?   ?   A . n 
A 1 629  GLN 629  629  ?    ?   ?   A . n 
A 1 630  SER 630  630  ?    ?   ?   A . n 
A 1 631  GLN 631  631  ?    ?   ?   A . n 
A 1 632  ALA 632  632  ?    ?   ?   A . n 
A 1 633  CYS 633  633  ?    ?   ?   A . n 
A 1 634  LYS 634  634  ?    ?   ?   A . n 
A 1 635  MET 635  635  ?    ?   ?   A . n 
A 1 636  SER 636  636  ?    ?   ?   A . n 
A 1 637  HIS 637  637  ?    ?   ?   A . n 
A 1 638  VAL 638  638  ?    ?   ?   A . n 
A 1 639  ARG 639  639  ?    ?   ?   A . n 
A 1 640  ASP 640  640  ?    ?   ?   A . n 
A 1 641  LEU 641  641  ?    ?   ?   A . n 
A 1 642  PRO 642  642  ?    ?   ?   A . n 
A 1 643  PRO 643  643  ?    ?   ?   A . n 
A 1 644  VAL 644  644  ?    ?   ?   A . n 
A 1 645  SER 645  645  ?    ?   ?   A . n 
A 1 646  GLY 646  646  ?    ?   ?   A . n 
A 1 647  SER 647  647  ?    ?   ?   A . n 
A 1 648  ILE 648  648  ?    ?   ?   A . n 
A 1 649  ILE 649  649  ?    ?   ?   A . n 
A 1 650  TRP 650  650  ?    ?   ?   A . n 
A 1 651  ALA 651  651  ?    ?   ?   A . n 
A 1 652  LYS 652  652  ?    ?   ?   A . n 
A 1 653  GLN 653  653  ?    ?   ?   A . n 
A 1 654  ILE 654  654  ?    ?   ?   A . n 
A 1 655  ASP 655  655  ?    ?   ?   A . n 
A 1 656  ARG 656  656  ?    ?   ?   A . n 
A 1 657  GLN 657  657  ?    ?   ?   A . n 
A 1 658  LEU 658  658  ?    ?   ?   A . n 
A 1 659  THR 659  659  ?    ?   ?   A . n 
A 1 660  ALA 660  660  ?    ?   ?   A . n 
A 1 661  TYR 661  661  ?    ?   ?   A . n 
A 1 662  MET 662  662  ?    ?   ?   A . n 
A 1 663  LYS 663  663  ?    ?   ?   A . n 
A 1 664  ARG 664  664  ?    ?   ?   A . n 
A 1 665  VAL 665  665  ?    ?   ?   A . n 
A 1 666  GLU 666  666  ?    ?   ?   A . n 
A 1 667  ASP 667  667  ?    ?   ?   A . n 
A 1 668  VAL 668  668  ?    ?   ?   A . n 
A 1 669  LEU 669  669  ?    ?   ?   A . n 
A 1 670  GLY 670  670  ?    ?   ?   A . n 
A 1 671  LYS 671  671  ?    ?   ?   A . n 
A 1 672  GLY 672  672  ?    ?   ?   A . n 
A 1 673  TRP 673  673  ?    ?   ?   A . n 
A 1 674  GLU 674  674  ?    ?   ?   A . n 
A 1 675  ASN 675  675  ?    ?   ?   A . n 
A 1 676  HIS 676  676  ?    ?   ?   A . n 
A 1 677  VAL 677  677  ?    ?   ?   A . n 
A 1 678  GLU 678  678  ?    ?   ?   A . n 
A 1 679  GLY 679  679  ?    ?   ?   A . n 
A 1 680  GLN 680  680  ?    ?   ?   A . n 
A 1 681  LYS 681  681  ?    ?   ?   A . n 
A 1 682  LEU 682  682  ?    ?   ?   A . n 
A 1 683  LYS 683  683  ?    ?   ?   A . n 
A 1 684  GLN 684  684  ?    ?   ?   A . n 
A 1 685  ASP 685  685  ?    ?   ?   A . n 
A 1 686  GLY 686  686  ?    ?   ?   A . n 
A 1 687  ASP 687  687  ?    ?   ?   A . n 
A 1 688  SER 688  688  ?    ?   ?   A . n 
A 1 689  PHE 689  689  ?    ?   ?   A . n 
A 1 690  ARG 690  690  ?    ?   ?   A . n 
A 1 691  MET 691  691  ?    ?   ?   A . n 
A 1 692  LYS 692  692  ?    ?   ?   A . n 
A 1 693  LEU 693  693  ?    ?   ?   A . n 
A 1 694  ASN 694  694  ?    ?   ?   A . n 
A 1 695  THR 695  695  ?    ?   ?   A . n 
A 1 696  GLN 696  696  ?    ?   ?   A . n 
A 1 697  GLU 697  697  ?    ?   ?   A . n 
A 1 698  ILE 698  698  ?    ?   ?   A . n 
A 1 699  PHE 699  699  ?    ?   ?   A . n 
A 1 700  ASP 700  700  ?    ?   ?   A . n 
A 1 701  ASP 701  701  ?    ?   ?   A . n 
A 1 702  TRP 702  702  ?    ?   ?   A . n 
A 1 703  ALA 703  703  ?    ?   ?   A . n 
A 1 704  ARG 704  704  ?    ?   ?   A . n 
A 1 705  LYS 705  705  ?    ?   ?   A . n 
A 1 706  VAL 706  706  ?    ?   ?   A . n 
A 1 707  GLN 707  707  ?    ?   ?   A . n 
A 1 708  GLN 708  708  ?    ?   ?   A . n 
A 1 709  ARG 709  709  ?    ?   ?   A . n 
A 1 710  ASN 710  710  ?    ?   ?   A . n 
A 1 711  LEU 711  711  ?    ?   ?   A . n 
A 1 712  GLY 712  712  ?    ?   ?   A . n 
A 1 713  VAL 713  713  ?    ?   ?   A . n 
A 1 714  SER 714  714  ?    ?   ?   A . n 
A 1 715  GLY 715  715  ?    ?   ?   A . n 
A 1 716  ARG 716  716  ?    ?   ?   A . n 
A 1 717  ILE 717  717  ?    ?   ?   A . n 
A 1 718  PHE 718  718  ?    ?   ?   A . n 
A 1 719  THR 719  719  ?    ?   ?   A . n 
A 1 720  ILE 720  720  ?    ?   ?   A . n 
A 1 721  GLU 721  721  ?    ?   ?   A . n 
A 1 722  SER 722  722  ?    ?   ?   A . n 
A 1 723  THR 723  723  ?    ?   ?   A . n 
A 1 724  ARG 724  724  ?    ?   ?   A . n 
A 1 725  VAL 725  725  ?    ?   ?   A . n 
A 1 726  ARG 726  726  ?    ?   ?   A . n 
A 1 727  GLY 727  727  ?    ?   ?   A . n 
A 1 728  ARG 728  728  ?    ?   ?   A . n 
A 1 729  THR 729  729  ?    ?   ?   A . n 
A 1 730  GLY 730  730  ?    ?   ?   A . n 
A 1 731  ASN 731  731  ?    ?   ?   A . n 
A 1 732  VAL 732  732  ?    ?   ?   A . n 
A 1 733  LEU 733  733  ?    ?   ?   A . n 
A 1 734  LYS 734  734  ?    ?   ?   A . n 
A 1 735  LEU 735  735  ?    ?   ?   A . n 
A 1 736  LYS 736  736  ?    ?   ?   A . n 
A 1 737  VAL 737  737  ?    ?   ?   A . n 
A 1 738  ASN 738  738  ?    ?   ?   A . n 
A 1 739  PHE 739  739  ?    ?   ?   A . n 
A 1 740  LEU 740  740  ?    ?   ?   A . n 
A 1 741  PRO 741  741  ?    ?   ?   A . n 
A 1 742  GLU 742  742  ?    ?   ?   A . n 
A 1 743  ILE 743  743  ?    ?   ?   A . n 
A 1 744  ILE 744  744  ?    ?   ?   A . n 
A 1 745  THR 745  745  ?    ?   ?   A . n 
A 1 746  LEU 746  746  ?    ?   ?   A . n 
A 1 747  SER 747  747  ?    ?   ?   A . n 
A 1 748  LYS 748  748  ?    ?   ?   A . n 
A 1 749  GLU 749  749  ?    ?   ?   A . n 
A 1 750  VAL 750  750  ?    ?   ?   A . n 
A 1 751  ARG 751  751  ?    ?   ?   A . n 
A 1 752  ASN 752  752  ?    ?   ?   A . n 
A 1 753  LEU 753  753  ?    ?   ?   A . n 
A 1 754  LYS 754  754  ?    ?   ?   A . n 
A 1 755  TRP 755  755  ?    ?   ?   A . n 
A 1 756  LEU 756  756  ?    ?   ?   A . n 
A 1 757  GLY 757  757  ?    ?   ?   A . n 
A 1 758  PHE 758  758  ?    ?   ?   A . n 
A 1 759  ARG 759  759  ?    ?   ?   A . n 
A 1 760  VAL 760  760  ?    ?   ?   A . n 
A 1 761  PRO 761  761  ?    ?   ?   A . n 
A 1 762  LEU 762  762  ?    ?   ?   A . n 
A 1 763  ALA 763  763  ?    ?   ?   A . n 
A 1 764  ILE 764  764  ?    ?   ?   A . n 
A 1 765  VAL 765  765  ?    ?   ?   A . n 
A 1 766  ASN 766  766  ?    ?   ?   A . n 
A 1 767  LYS 767  767  ?    ?   ?   A . n 
A 1 768  ALA 768  768  ?    ?   ?   A . n 
A 1 769  HIS 769  769  ?    ?   ?   A . n 
A 1 770  GLN 770  770  ?    ?   ?   A . n 
A 1 771  ALA 771  771  ?    ?   ?   A . n 
A 1 772  ASN 772  772  ?    ?   ?   A . n 
A 1 773  GLN 773  773  ?    ?   ?   A . n 
A 1 774  LEU 774  774  ?    ?   ?   A . n 
A 1 775  TYR 775  775  ?    ?   ?   A . n 
A 1 776  PRO 776  776  ?    ?   ?   A . n 
A 1 777  PHE 777  777  ?    ?   ?   A . n 
A 1 778  ALA 778  778  ?    ?   ?   A . n 
A 1 779  ILE 779  779  ?    ?   ?   A . n 
A 1 780  SER 780  780  ?    ?   ?   A . n 
A 1 781  LEU 781  781  ?    ?   ?   A . n 
A 1 782  ILE 782  782  ?    ?   ?   A . n 
A 1 783  GLU 783  783  ?    ?   ?   A . n 
A 1 784  SER 784  784  ?    ?   ?   A . n 
A 1 785  VAL 785  785  ?    ?   ?   A . n 
A 1 786  ARG 786  786  ?    ?   ?   A . n 
A 1 787  THR 787  787  ?    ?   ?   A . n 
A 1 788  TYR 788  788  ?    ?   ?   A . n 
A 1 789  GLU 789  789  ?    ?   ?   A . n 
A 1 790  ARG 790  790  ?    ?   ?   A . n 
A 1 791  THR 791  791  ?    ?   ?   A . n 
A 1 792  CYS 792  792  ?    ?   ?   A . n 
A 1 793  GLU 793  793  ?    ?   ?   A . n 
A 1 794  LYS 794  794  ?    ?   ?   A . n 
A 1 795  VAL 795  795  ?    ?   ?   A . n 
A 1 796  GLU 796  796  ?    ?   ?   A . n 
A 1 797  GLU 797  797  ?    ?   ?   A . n 
A 1 798  ARG 798  798  ?    ?   ?   A . n 
A 1 799  ASN 799  799  ?    ?   ?   A . n 
A 1 800  THR 800  800  ?    ?   ?   A . n 
A 1 801  ILE 801  801  ?    ?   ?   A . n 
A 1 802  SER 802  802  ?    ?   ?   A . n 
A 1 803  LEU 803  803  ?    ?   ?   A . n 
A 1 804  LEU 804  804  ?    ?   ?   A . n 
A 1 805  VAL 805  805  ?    ?   ?   A . n 
A 1 806  ALA 806  806  ?    ?   ?   A . n 
A 1 807  GLY 807  807  ?    ?   ?   A . n 
A 1 808  LEU 808  808  ?    ?   ?   A . n 
A 1 809  LYS 809  809  ?    ?   ?   A . n 
A 1 810  LYS 810  810  ?    ?   ?   A . n 
A 1 811  GLU 811  811  ?    ?   ?   A . n 
A 1 812  VAL 812  812  ?    ?   ?   A . n 
A 1 813  GLN 813  813  ?    ?   ?   A . n 
A 1 814  ALA 814  814  ?    ?   ?   A . n 
A 1 815  LEU 815  815  ?    ?   ?   A . n 
A 1 816  ILE 816  816  ?    ?   ?   A . n 
A 1 817  ALA 817  817  ?    ?   ?   A . n 
A 1 818  GLU 818  818  ?    ?   ?   A . n 
A 1 819  GLY 819  819  ?    ?   ?   A . n 
A 1 820  ILE 820  820  ?    ?   ?   A . n 
A 1 821  ALA 821  821  ?    ?   ?   A . n 
A 1 822  LEU 822  822  ?    ?   ?   A . n 
A 1 823  VAL 823  823  ?    ?   ?   A . n 
A 1 824  TRP 824  824  ?    ?   ?   A . n 
A 1 825  GLU 825  825  ?    ?   ?   A . n 
A 1 826  SER 826  826  ?    ?   ?   A . n 
A 1 827  TYR 827  827  ?    ?   ?   A . n 
A 1 828  LYS 828  828  ?    ?   ?   A . n 
A 1 829  LEU 829  829  ?    ?   ?   A . n 
A 1 830  ASP 830  830  ?    ?   ?   A . n 
A 1 831  PRO 831  831  ?    ?   ?   A . n 
A 1 832  TYR 832  832  ?    ?   ?   A . n 
A 1 833  VAL 833  833  ?    ?   ?   A . n 
A 1 834  GLN 834  834  ?    ?   ?   A . n 
A 1 835  ARG 835  835  ?    ?   ?   A . n 
A 1 836  LEU 836  836  ?    ?   ?   A . n 
A 1 837  ALA 837  837  ?    ?   ?   A . n 
A 1 838  GLU 838  838  ?    ?   ?   A . n 
A 1 839  THR 839  839  ?    ?   ?   A . n 
A 1 840  VAL 840  840  ?    ?   ?   A . n 
A 1 841  PHE 841  841  ?    ?   ?   A . n 
A 1 842  ASN 842  842  ?    ?   ?   A . n 
A 1 843  PHE 843  843  ?    ?   ?   A . n 
A 1 844  GLN 844  844  ?    ?   ?   A . n 
A 1 845  GLU 845  845  ?    ?   ?   A . n 
A 1 846  LYS 846  846  ?    ?   ?   A . n 
A 1 847  VAL 847  847  ?    ?   ?   A . n 
A 1 848  ASP 848  848  ?    ?   ?   A . n 
A 1 849  ASP 849  849  ?    ?   ?   A . n 
A 1 850  LEU 850  850  ?    ?   ?   A . n 
A 1 851  LEU 851  851  ?    ?   ?   A . n 
A 1 852  ILE 852  852  ?    ?   ?   A . n 
A 1 853  ILE 853  853  ?    ?   ?   A . n 
A 1 854  GLU 854  854  ?    ?   ?   A . n 
A 1 855  GLU 855  855  ?    ?   ?   A . n 
A 1 856  LYS 856  856  ?    ?   ?   A . n 
A 1 857  ILE 857  857  ?    ?   ?   A . n 
A 1 858  ASP 858  858  ?    ?   ?   A . n 
A 1 859  LEU 859  859  ?    ?   ?   A . n 
A 1 860  GLU 860  860  ?    ?   ?   A . n 
A 1 861  VAL 861  861  ?    ?   ?   A . n 
A 1 862  ARG 862  862  ?    ?   ?   A . n 
A 1 863  SER 863  863  ?    ?   ?   A . n 
A 1 864  LEU 864  864  ?    ?   ?   A . n 
A 1 865  GLU 865  865  ?    ?   ?   A . n 
A 1 866  THR 866  866  ?    ?   ?   A . n 
A 1 867  CYS 867  867  ?    ?   ?   A . n 
A 1 868  MET 868  868  ?    ?   ?   A . n 
A 1 869  TYR 869  869  ?    ?   ?   A . n 
A 1 870  ASP 870  870  ?    ?   ?   A . n 
A 1 871  HIS 871  871  ?    ?   ?   A . n 
A 1 872  LYS 872  872  ?    ?   ?   A . n 
A 1 873  THR 873  873  ?    ?   ?   A . n 
A 1 874  PHE 874  874  ?    ?   ?   A . n 
A 1 875  SER 875  875  ?    ?   ?   A . n 
A 1 876  GLU 876  876  ?    ?   ?   A . n 
A 1 877  ILE 877  877  ?    ?   ?   A . n 
A 1 878  LEU 878  878  ?    ?   ?   A . n 
A 1 879  ASN 879  879  ?    ?   ?   A . n 
A 1 880  ARG 880  880  ?    ?   ?   A . n 
A 1 881  VAL 881  881  ?    ?   ?   A . n 
A 1 882  GLN 882  882  ?    ?   ?   A . n 
A 1 883  LYS 883  883  ?    ?   ?   A . n 
A 1 884  ALA 884  884  ?    ?   ?   A . n 
A 1 885  VAL 885  885  ?    ?   ?   A . n 
A 1 886  ASP 886  886  ?    ?   ?   A . n 
A 1 887  ASP 887  887  ?    ?   ?   A . n 
A 1 888  LEU 888  888  ?    ?   ?   A . n 
A 1 889  ASN 889  889  ?    ?   ?   A . n 
A 1 890  LEU 890  890  ?    ?   ?   A . n 
A 1 891  HIS 891  891  ?    ?   ?   A . n 
A 1 892  SER 892  892  ?    ?   ?   A . n 
A 1 893  TYR 893  893  ?    ?   ?   A . n 
A 1 894  SER 894  894  ?    ?   ?   A . n 
A 1 895  ASN 895  895  ?    ?   ?   A . n 
A 1 896  LEU 896  896  ?    ?   ?   A . n 
A 1 897  PRO 897  897  ?    ?   ?   A . n 
A 1 898  ILE 898  898  ?    ?   ?   A . n 
A 1 899  TRP 899  899  ?    ?   ?   A . n 
A 1 900  VAL 900  900  ?    ?   ?   A . n 
A 1 901  ASN 901  901  ?    ?   ?   A . n 
A 1 902  LYS 902  902  ?    ?   ?   A . n 
A 1 903  LEU 903  903  ?    ?   ?   A . n 
A 1 904  ASP 904  904  ?    ?   ?   A . n 
A 1 905  MET 905  905  ?    ?   ?   A . n 
A 1 906  GLU 906  906  ?    ?   ?   A . n 
A 1 907  ILE 907  907  ?    ?   ?   A . n 
A 1 908  GLU 908  908  ?    ?   ?   A . n 
A 1 909  ARG 909  909  ?    ?   ?   A . n 
A 1 910  ILE 910  910  ?    ?   ?   A . n 
A 1 911  LEU 911  911  ?    ?   ?   A . n 
A 1 912  GLY 912  912  ?    ?   ?   A . n 
A 1 913  VAL 913  913  ?    ?   ?   A . n 
A 1 914  ARG 914  914  ?    ?   ?   A . n 
A 1 915  LEU 915  915  ?    ?   ?   A . n 
A 1 916  GLN 916  916  ?    ?   ?   A . n 
A 1 917  ALA 917  917  ?    ?   ?   A . n 
A 1 918  GLY 918  918  ?    ?   ?   A . n 
A 1 919  LEU 919  919  ?    ?   ?   A . n 
A 1 920  ARG 920  920  ?    ?   ?   A . n 
A 1 921  ALA 921  921  ?    ?   ?   A . n 
A 1 922  TRP 922  922  ?    ?   ?   A . n 
A 1 923  THR 923  923  ?    ?   ?   A . n 
A 1 924  GLN 924  924  ?    ?   ?   A . n 
A 1 925  VAL 925  925  ?    ?   ?   A . n 
A 1 926  LEU 926  926  ?    ?   ?   A . n 
A 1 927  LEU 927  927  ?    ?   ?   A . n 
A 1 928  GLY 928  928  ?    ?   ?   A . n 
A 1 929  GLN 929  929  ?    ?   ?   A . n 
A 1 930  ALA 930  930  ?    ?   ?   A . n 
A 1 931  GLU 931  931  ?    ?   ?   A . n 
A 1 932  ASP 932  932  ?    ?   ?   A . n 
A 1 933  LYS 933  933  ?    ?   ?   A . n 
A 1 934  ALA 934  934  ?    ?   ?   A . n 
A 1 935  GLU 935  935  ?    ?   ?   A . n 
A 1 936  VAL 936  936  ?    ?   ?   A . n 
A 1 937  ASP 937  937  ?    ?   ?   A . n 
A 1 938  MET 938  938  ?    ?   ?   A . n 
A 1 939  ASP 939  939  ?    ?   ?   A . n 
A 1 940  THR 940  940  ?    ?   ?   A . n 
A 1 941  ASP 941  941  ?    ?   ?   A . n 
A 1 942  ALA 942  942  ?    ?   ?   A . n 
A 1 943  PRO 943  943  ?    ?   ?   A . n 
A 1 944  GLN 944  944  ?    ?   ?   A . n 
A 1 945  VAL 945  945  ?    ?   ?   A . n 
A 1 946  SER 946  946  ?    ?   ?   A . n 
A 1 947  HIS 947  947  ?    ?   ?   A . n 
A 1 948  LYS 948  948  ?    ?   ?   A . n 
A 1 949  PRO 949  949  ?    ?   ?   A . n 
A 1 950  GLY 950  950  ?    ?   ?   A . n 
A 1 951  GLY 951  951  ?    ?   ?   A . n 
A 1 952  GLU 952  952  ?    ?   ?   A . n 
A 1 953  PRO 953  953  ?    ?   ?   A . n 
A 1 954  LYS 954  954  ?    ?   ?   A . n 
A 1 955  ILE 955  955  ?    ?   ?   A . n 
A 1 956  LYS 956  956  ?    ?   ?   A . n 
A 1 957  ASN 957  957  ?    ?   ?   A . n 
A 1 958  VAL 958  958  ?    ?   ?   A . n 
A 1 959  VAL 959  959  ?    ?   ?   A . n 
A 1 960  HIS 960  960  ?    ?   ?   A . n 
A 1 961  GLU 961  961  ?    ?   ?   A . n 
A 1 962  LEU 962  962  ?    ?   ?   A . n 
A 1 963  ARG 963  963  ?    ?   ?   A . n 
A 1 964  ILE 964  964  ?    ?   ?   A . n 
A 1 965  THR 965  965  ?    ?   ?   A . n 
A 1 966  ASN 966  966  ?    ?   ?   A . n 
A 1 967  GLN 967  967  ?    ?   ?   A . n 
A 1 968  VAL 968  968  ?    ?   ?   A . n 
A 1 969  ILE 969  969  ?    ?   ?   A . n 
A 1 970  TYR 970  970  ?    ?   ?   A . n 
A 1 971  LEU 971  971  ?    ?   ?   A . n 
A 1 972  ASN 972  972  ?    ?   ?   A . n 
A 1 973  PRO 973  973  ?    ?   ?   A . n 
A 1 974  PRO 974  974  ?    ?   ?   A . n 
A 1 975  ILE 975  975  ?    ?   ?   A . n 
A 1 976  GLU 976  976  ?    ?   ?   A . n 
A 1 977  GLU 977  977  ?    ?   ?   A . n 
A 1 978  CYS 978  978  ?    ?   ?   A . n 
A 1 979  ARG 979  979  ?    ?   ?   A . n 
A 1 980  TYR 980  980  ?    ?   ?   A . n 
A 1 981  LYS 981  981  ?    ?   ?   A . n 
A 1 982  LEU 982  982  ?    ?   ?   A . n 
A 1 983  TYR 983  983  ?    ?   ?   A . n 
A 1 984  GLN 984  984  ?    ?   ?   A . n 
A 1 985  GLU 985  985  ?    ?   ?   A . n 
A 1 986  MET 986  986  ?    ?   ?   A . n 
A 1 987  PHE 987  987  ?    ?   ?   A . n 
A 1 988  ALA 988  988  ?    ?   ?   A . n 
A 1 989  TRP 989  989  ?    ?   ?   A . n 
A 1 990  LYS 990  990  ?    ?   ?   A . n 
A 1 991  MET 991  991  ?    ?   ?   A . n 
A 1 992  VAL 992  992  ?    ?   ?   A . n 
A 1 993  VAL 993  993  ?    ?   ?   A . n 
A 1 994  LEU 994  994  ?    ?   ?   A . n 
A 1 995  SER 995  995  ?    ?   ?   A . n 
A 1 996  LEU 996  996  ?    ?   ?   A . n 
A 1 997  PRO 997  997  ?    ?   ?   A . n 
A 1 998  ARG 998  998  ?    ?   ?   A . n 
A 1 999  ILE 999  999  ?    ?   ?   A . n 
A 1 1000 GLN 1000 1000 ?    ?   ?   A . n 
A 1 1001 SER 1001 1001 ?    ?   ?   A . n 
A 1 1002 GLN 1002 1002 ?    ?   ?   A . n 
A 1 1003 ARG 1003 1003 ?    ?   ?   A . n 
A 1 1004 TYR 1004 1004 ?    ?   ?   A . n 
A 1 1005 GLN 1005 1005 ?    ?   ?   A . n 
A 1 1006 VAL 1006 1006 ?    ?   ?   A . n 
A 1 1007 GLY 1007 1007 ?    ?   ?   A . n 
A 1 1008 VAL 1008 1008 ?    ?   ?   A . n 
A 1 1009 HIS 1009 1009 ?    ?   ?   A . n 
A 1 1010 TYR 1010 1010 ?    ?   ?   A . n 
A 1 1011 GLU 1011 1011 ?    ?   ?   A . n 
A 1 1012 LEU 1012 1012 ?    ?   ?   A . n 
A 1 1013 THR 1013 1013 ?    ?   ?   A . n 
A 1 1014 GLU 1014 1014 ?    ?   ?   A . n 
A 1 1015 GLU 1015 1015 ?    ?   ?   A . n 
A 1 1016 GLU 1016 1016 ?    ?   ?   A . n 
A 1 1017 LYS 1017 1017 ?    ?   ?   A . n 
A 1 1018 PHE 1018 1018 ?    ?   ?   A . n 
A 1 1019 TYR 1019 1019 ?    ?   ?   A . n 
A 1 1020 ARG 1020 1020 ?    ?   ?   A . n 
A 1 1021 ASN 1021 1021 ?    ?   ?   A . n 
A 1 1022 ALA 1022 1022 ?    ?   ?   A . n 
A 1 1023 LEU 1023 1023 ?    ?   ?   A . n 
A 1 1024 THR 1024 1024 ?    ?   ?   A . n 
A 1 1025 ARG 1025 1025 ?    ?   ?   A . n 
A 1 1026 MET 1026 1026 ?    ?   ?   A . n 
A 1 1027 PRO 1027 1027 ?    ?   ?   A . n 
A 1 1028 ASP 1028 1028 ?    ?   ?   A . n 
A 1 1029 GLY 1029 1029 ?    ?   ?   A . n 
A 1 1030 PRO 1030 1030 ?    ?   ?   A . n 
A 1 1031 VAL 1031 1031 ?    ?   ?   A . n 
A 1 1032 ALA 1032 1032 ?    ?   ?   A . n 
A 1 1033 LEU 1033 1033 ?    ?   ?   A . n 
A 1 1034 GLU 1034 1034 ?    ?   ?   A . n 
A 1 1035 GLU 1035 1035 ?    ?   ?   A . n 
A 1 1036 SER 1036 1036 ?    ?   ?   A . n 
A 1 1037 TYR 1037 1037 ?    ?   ?   A . n 
A 1 1038 SER 1038 1038 ?    ?   ?   A . n 
A 1 1039 ALA 1039 1039 ?    ?   ?   A . n 
A 1 1040 VAL 1040 1040 ?    ?   ?   A . n 
A 1 1041 MET 1041 1041 ?    ?   ?   A . n 
A 1 1042 GLY 1042 1042 ?    ?   ?   A . n 
A 1 1043 ILE 1043 1043 ?    ?   ?   A . n 
A 1 1044 VAL 1044 1044 ?    ?   ?   A . n 
A 1 1045 SER 1045 1045 ?    ?   ?   A . n 
A 1 1046 GLU 1046 1046 ?    ?   ?   A . n 
A 1 1047 VAL 1047 1047 ?    ?   ?   A . n 
A 1 1048 GLU 1048 1048 ?    ?   ?   A . n 
A 1 1049 GLN 1049 1049 ?    ?   ?   A . n 
A 1 1050 TYR 1050 1050 ?    ?   ?   A . n 
A 1 1051 VAL 1051 1051 ?    ?   ?   A . n 
A 1 1052 LYS 1052 1052 ?    ?   ?   A . n 
A 1 1053 VAL 1053 1053 ?    ?   ?   A . n 
A 1 1054 TRP 1054 1054 ?    ?   ?   A . n 
A 1 1055 LEU 1055 1055 ?    ?   ?   A . n 
A 1 1056 GLN 1056 1056 ?    ?   ?   A . n 
A 1 1057 TYR 1057 1057 ?    ?   ?   A . n 
A 1 1058 GLN 1058 1058 ?    ?   ?   A . n 
A 1 1059 CYS 1059 1059 ?    ?   ?   A . n 
A 1 1060 LEU 1060 1060 ?    ?   ?   A . n 
A 1 1061 TRP 1061 1061 ?    ?   ?   A . n 
A 1 1062 ASP 1062 1062 ?    ?   ?   A . n 
A 1 1063 MET 1063 1063 ?    ?   ?   A . n 
A 1 1064 GLN 1064 1064 ?    ?   ?   A . n 
A 1 1065 ALA 1065 1065 ?    ?   ?   A . n 
A 1 1066 GLU 1066 1066 ?    ?   ?   A . n 
A 1 1067 ASN 1067 1067 ?    ?   ?   A . n 
A 1 1068 ILE 1068 1068 ?    ?   ?   A . n 
A 1 1069 TYR 1069 1069 ?    ?   ?   A . n 
A 1 1070 ASN 1070 1070 ?    ?   ?   A . n 
A 1 1071 ARG 1071 1071 ?    ?   ?   A . n 
A 1 1072 LEU 1072 1072 ?    ?   ?   A . n 
A 1 1073 GLY 1073 1073 ?    ?   ?   A . n 
A 1 1074 GLU 1074 1074 ?    ?   ?   A . n 
A 1 1075 ASP 1075 1075 ?    ?   ?   A . n 
A 1 1076 LEU 1076 1076 ?    ?   ?   A . n 
A 1 1077 ASN 1077 1077 ?    ?   ?   A . n 
A 1 1078 LYS 1078 1078 ?    ?   ?   A . n 
A 1 1079 TRP 1079 1079 ?    ?   ?   A . n 
A 1 1080 GLN 1080 1080 ?    ?   ?   A . n 
A 1 1081 ALA 1081 1081 ?    ?   ?   A . n 
A 1 1082 LEU 1082 1082 ?    ?   ?   A . n 
A 1 1083 LEU 1083 1083 ?    ?   ?   A . n 
A 1 1084 VAL 1084 1084 ?    ?   ?   A . n 
A 1 1085 GLN 1085 1085 ?    ?   ?   A . n 
A 1 1086 ILE 1086 1086 ?    ?   ?   A . n 
A 1 1087 ARG 1087 1087 ?    ?   ?   A . n 
A 1 1088 LYS 1088 1088 ?    ?   ?   A . n 
A 1 1089 ALA 1089 1089 ?    ?   ?   A . n 
A 1 1090 ARG 1090 1090 ?    ?   ?   A . n 
A 1 1091 GLY 1091 1091 ?    ?   ?   A . n 
A 1 1092 THR 1092 1092 ?    ?   ?   A . n 
A 1 1093 PHE 1093 1093 ?    ?   ?   A . n 
A 1 1094 ASP 1094 1094 ?    ?   ?   A . n 
A 1 1095 ASN 1095 1095 ?    ?   ?   A . n 
A 1 1096 ALA 1096 1096 ?    ?   ?   A . n 
A 1 1097 GLU 1097 1097 ?    ?   ?   A . n 
A 1 1098 THR 1098 1098 ?    ?   ?   A . n 
A 1 1099 LYS 1099 1099 ?    ?   ?   A . n 
A 1 1100 LYS 1100 1100 ?    ?   ?   A . n 
A 1 1101 GLU 1101 1101 ?    ?   ?   A . n 
A 1 1102 PHE 1102 1102 ?    ?   ?   A . n 
A 1 1103 GLY 1103 1103 ?    ?   ?   A . n 
A 1 1104 PRO 1104 1104 ?    ?   ?   A . n 
A 1 1105 VAL 1105 1105 ?    ?   ?   A . n 
A 1 1106 VAL 1106 1106 ?    ?   ?   A . n 
A 1 1107 ILE 1107 1107 ?    ?   ?   A . n 
A 1 1108 ASP 1108 1108 ?    ?   ?   A . n 
A 1 1109 TYR 1109 1109 ?    ?   ?   A . n 
A 1 1110 GLY 1110 1110 ?    ?   ?   A . n 
A 1 1111 LYS 1111 1111 ?    ?   ?   A . n 
A 1 1112 VAL 1112 1112 ?    ?   ?   A . n 
A 1 1113 GLN 1113 1113 ?    ?   ?   A . n 
A 1 1114 SER 1114 1114 ?    ?   ?   A . n 
A 1 1115 LYS 1115 1115 ?    ?   ?   A . n 
A 1 1116 VAL 1116 1116 ?    ?   ?   A . n 
A 1 1117 ASN 1117 1117 ?    ?   ?   A . n 
A 1 1118 LEU 1118 1118 ?    ?   ?   A . n 
A 1 1119 LYS 1119 1119 ?    ?   ?   A . n 
A 1 1120 TYR 1120 1120 ?    ?   ?   A . n 
A 1 1121 ASP 1121 1121 ?    ?   ?   A . n 
A 1 1122 SER 1122 1122 ?    ?   ?   A . n 
A 1 1123 TRP 1123 1123 ?    ?   ?   A . n 
A 1 1124 HIS 1124 1124 ?    ?   ?   A . n 
A 1 1125 LYS 1125 1125 ?    ?   ?   A . n 
A 1 1126 GLU 1126 1126 ?    ?   ?   A . n 
A 1 1127 VAL 1127 1127 ?    ?   ?   A . n 
A 1 1128 LEU 1128 1128 ?    ?   ?   A . n 
A 1 1129 SER 1129 1129 ?    ?   ?   A . n 
A 1 1130 LYS 1130 1130 ?    ?   ?   A . n 
A 1 1131 PHE 1131 1131 ?    ?   ?   A . n 
A 1 1132 GLY 1132 1132 ?    ?   ?   A . n 
A 1 1133 GLN 1133 1133 ?    ?   ?   A . n 
A 1 1134 MET 1134 1134 ?    ?   ?   A . n 
A 1 1135 LEU 1135 1135 ?    ?   ?   A . n 
A 1 1136 GLY 1136 1136 ?    ?   ?   A . n 
A 1 1137 SER 1137 1137 ?    ?   ?   A . n 
A 1 1138 ASN 1138 1138 ?    ?   ?   A . n 
A 1 1139 MET 1139 1139 ?    ?   ?   A . n 
A 1 1140 THR 1140 1140 ?    ?   ?   A . n 
A 1 1141 GLU 1141 1141 ?    ?   ?   A . n 
A 1 1142 PHE 1142 1142 ?    ?   ?   A . n 
A 1 1143 HIS 1143 1143 ?    ?   ?   A . n 
A 1 1144 SER 1144 1144 ?    ?   ?   A . n 
A 1 1145 GLN 1145 1145 ?    ?   ?   A . n 
A 1 1146 ILE 1146 1146 ?    ?   ?   A . n 
A 1 1147 SER 1147 1147 ?    ?   ?   A . n 
A 1 1148 LYS 1148 1148 ?    ?   ?   A . n 
A 1 1149 SER 1149 1149 ?    ?   ?   A . n 
A 1 1150 ARG 1150 1150 ?    ?   ?   A . n 
A 1 1151 GLN 1151 1151 ?    ?   ?   A . n 
A 1 1152 GLU 1152 1152 ?    ?   ?   A . n 
A 1 1153 LEU 1153 1153 ?    ?   ?   A . n 
A 1 1154 GLU 1154 1154 ?    ?   ?   A . n 
A 1 1155 GLN 1155 1155 ?    ?   ?   A . n 
A 1 1156 HIS 1156 1156 ?    ?   ?   A . n 
A 1 1157 SER 1157 1157 ?    ?   ?   A . n 
A 1 1158 VAL 1158 1158 ?    ?   ?   A . n 
A 1 1159 ASP 1159 1159 ?    ?   ?   A . n 
A 1 1160 THR 1160 1160 ?    ?   ?   A . n 
A 1 1161 ALA 1161 1161 ?    ?   ?   A . n 
A 1 1162 SER 1162 1162 ?    ?   ?   A . n 
A 1 1163 THR 1163 1163 ?    ?   ?   A . n 
A 1 1164 SER 1164 1164 ?    ?   ?   A . n 
A 1 1165 ASP 1165 1165 ?    ?   ?   A . n 
A 1 1166 ALA 1166 1166 ?    ?   ?   A . n 
A 1 1167 VAL 1167 1167 ?    ?   ?   A . n 
A 1 1168 THR 1168 1168 ?    ?   ?   A . n 
A 1 1169 PHE 1169 1169 ?    ?   ?   A . n 
A 1 1170 ILE 1170 1170 ?    ?   ?   A . n 
A 1 1171 THR 1171 1171 ?    ?   ?   A . n 
A 1 1172 TYR 1172 1172 ?    ?   ?   A . n 
A 1 1173 VAL 1173 1173 ?    ?   ?   A . n 
A 1 1174 GLN 1174 1174 ?    ?   ?   A . n 
A 1 1175 SER 1175 1175 ?    ?   ?   A . n 
A 1 1176 LEU 1176 1176 ?    ?   ?   A . n 
A 1 1177 LYS 1177 1177 ?    ?   ?   A . n 
A 1 1178 ARG 1178 1178 ?    ?   ?   A . n 
A 1 1179 LYS 1179 1179 ?    ?   ?   A . n 
A 1 1180 ILE 1180 1180 ?    ?   ?   A . n 
A 1 1181 LYS 1181 1181 ?    ?   ?   A . n 
A 1 1182 GLN 1182 1182 ?    ?   ?   A . n 
A 1 1183 PHE 1183 1183 ?    ?   ?   A . n 
A 1 1184 GLU 1184 1184 ?    ?   ?   A . n 
A 1 1185 LYS 1185 1185 ?    ?   ?   A . n 
A 1 1186 GLN 1186 1186 ?    ?   ?   A . n 
A 1 1187 VAL 1187 1187 ?    ?   ?   A . n 
A 1 1188 GLU 1188 1188 ?    ?   ?   A . n 
A 1 1189 LEU 1189 1189 ?    ?   ?   A . n 
A 1 1190 TYR 1190 1190 ?    ?   ?   A . n 
A 1 1191 ARG 1191 1191 ?    ?   ?   A . n 
A 1 1192 ASN 1192 1192 ?    ?   ?   A . n 
A 1 1193 GLY 1193 1193 ?    ?   ?   A . n 
A 1 1194 GLN 1194 1194 ?    ?   ?   A . n 
A 1 1195 ARG 1195 1195 ?    ?   ?   A . n 
A 1 1196 LEU 1196 1196 ?    ?   ?   A . n 
A 1 1197 LEU 1197 1197 ?    ?   ?   A . n 
A 1 1198 GLU 1198 1198 ?    ?   ?   A . n 
A 1 1199 LYS 1199 1199 ?    ?   ?   A . n 
A 1 1200 GLN 1200 1200 ?    ?   ?   A . n 
A 1 1201 ARG 1201 1201 ?    ?   ?   A . n 
A 1 1202 PHE 1202 1202 ?    ?   ?   A . n 
A 1 1203 GLN 1203 1203 ?    ?   ?   A . n 
A 1 1204 PHE 1204 1204 ?    ?   ?   A . n 
A 1 1205 PRO 1205 1205 ?    ?   ?   A . n 
A 1 1206 PRO 1206 1206 ?    ?   ?   A . n 
A 1 1207 SER 1207 1207 ?    ?   ?   A . n 
A 1 1208 TRP 1208 1208 ?    ?   ?   A . n 
A 1 1209 LEU 1209 1209 ?    ?   ?   A . n 
A 1 1210 TYR 1210 1210 ?    ?   ?   A . n 
A 1 1211 ILE 1211 1211 ?    ?   ?   A . n 
A 1 1212 ASP 1212 1212 ?    ?   ?   A . n 
A 1 1213 ASN 1213 1213 ?    ?   ?   A . n 
A 1 1214 ILE 1214 1214 ?    ?   ?   A . n 
A 1 1215 GLU 1215 1215 ?    ?   ?   A . n 
A 1 1216 GLY 1216 1216 ?    ?   ?   A . n 
A 1 1217 GLU 1217 1217 ?    ?   ?   A . n 
A 1 1218 TRP 1218 1218 ?    ?   ?   A . n 
A 1 1219 GLY 1219 1219 ?    ?   ?   A . n 
A 1 1220 ALA 1220 1220 ?    ?   ?   A . n 
A 1 1221 PHE 1221 1221 ?    ?   ?   A . n 
A 1 1222 ASN 1222 1222 ?    ?   ?   A . n 
A 1 1223 ASP 1223 1223 ?    ?   ?   A . n 
A 1 1224 ILE 1224 1224 ?    ?   ?   A . n 
A 1 1225 MET 1225 1225 ?    ?   ?   A . n 
A 1 1226 ARG 1226 1226 ?    ?   ?   A . n 
A 1 1227 ARG 1227 1227 ?    ?   ?   A . n 
A 1 1228 LYS 1228 1228 ?    ?   ?   A . n 
A 1 1229 ASP 1229 1229 ?    ?   ?   A . n 
A 1 1230 SER 1230 1230 ?    ?   ?   A . n 
A 1 1231 ALA 1231 1231 ?    ?   ?   A . n 
A 1 1232 ILE 1232 1232 ?    ?   ?   A . n 
A 1 1233 GLN 1233 1233 ?    ?   ?   A . n 
A 1 1234 GLN 1234 1234 ?    ?   ?   A . n 
A 1 1235 GLN 1235 1235 ?    ?   ?   A . n 
A 1 1236 VAL 1236 1236 ?    ?   ?   A . n 
A 1 1237 ALA 1237 1237 ?    ?   ?   A . n 
A 1 1238 ASN 1238 1238 ?    ?   ?   A . n 
A 1 1239 LEU 1239 1239 ?    ?   ?   A . n 
A 1 1240 GLN 1240 1240 ?    ?   ?   A . n 
A 1 1241 MET 1241 1241 ?    ?   ?   A . n 
A 1 1242 LYS 1242 1242 ?    ?   ?   A . n 
A 1 1243 ILE 1243 1243 ?    ?   ?   A . n 
A 1 1244 VAL 1244 1244 ?    ?   ?   A . n 
A 1 1245 GLN 1245 1245 ?    ?   ?   A . n 
A 1 1246 GLU 1246 1246 ?    ?   ?   A . n 
A 1 1247 ASP 1247 1247 ?    ?   ?   A . n 
A 1 1248 ARG 1248 1248 ?    ?   ?   A . n 
A 1 1249 ALA 1249 1249 ?    ?   ?   A . n 
A 1 1250 VAL 1250 1250 ?    ?   ?   A . n 
A 1 1251 GLU 1251 1251 ?    ?   ?   A . n 
A 1 1252 SER 1252 1252 ?    ?   ?   A . n 
A 1 1253 ARG 1253 1253 ?    ?   ?   A . n 
A 1 1254 THR 1254 1254 ?    ?   ?   A . n 
A 1 1255 THR 1255 1255 ?    ?   ?   A . n 
A 1 1256 ASP 1256 1256 ?    ?   ?   A . n 
A 1 1257 LEU 1257 1257 ?    ?   ?   A . n 
A 1 1258 LEU 1258 1258 ?    ?   ?   A . n 
A 1 1259 THR 1259 1259 ?    ?   ?   A . n 
A 1 1260 ASP 1260 1260 ?    ?   ?   A . n 
A 1 1261 TRP 1261 1261 ?    ?   ?   A . n 
A 1 1262 GLU 1262 1262 ?    ?   ?   A . n 
A 1 1263 LYS 1263 1263 ?    ?   ?   A . n 
A 1 1264 THR 1264 1264 ?    ?   ?   A . n 
A 1 1265 LYS 1265 1265 ?    ?   ?   A . n 
A 1 1266 PRO 1266 1266 ?    ?   ?   A . n 
A 1 1267 VAL 1267 1267 ?    ?   ?   A . n 
A 1 1268 THR 1268 1268 ?    ?   ?   A . n 
A 1 1269 GLY 1269 1269 ?    ?   ?   A . n 
A 1 1270 ASN 1270 1270 ?    ?   ?   A . n 
A 1 1271 LEU 1271 1271 ?    ?   ?   A . n 
A 1 1272 ARG 1272 1272 ?    ?   ?   A . n 
A 1 1273 PRO 1273 1273 ?    ?   ?   A . n 
A 1 1274 GLU 1274 1274 ?    ?   ?   A . n 
A 1 1275 GLU 1275 1275 ?    ?   ?   A . n 
A 1 1276 ALA 1276 1276 ?    ?   ?   A . n 
A 1 1277 LEU 1277 1277 ?    ?   ?   A . n 
A 1 1278 GLN 1278 1278 ?    ?   ?   A . n 
A 1 1279 ALA 1279 1279 ?    ?   ?   A . n 
A 1 1280 LEU 1280 1280 ?    ?   ?   A . n 
A 1 1281 THR 1281 1281 ?    ?   ?   A . n 
A 1 1282 ILE 1282 1282 ?    ?   ?   A . n 
A 1 1283 TYR 1283 1283 ?    ?   ?   A . n 
A 1 1284 GLU 1284 1284 ?    ?   ?   A . n 
A 1 1285 GLY 1285 1285 ?    ?   ?   A . n 
A 1 1286 LYS 1286 1286 ?    ?   ?   A . n 
A 1 1287 PHE 1287 1287 ?    ?   ?   A . n 
A 1 1288 GLY 1288 1288 ?    ?   ?   A . n 
A 1 1289 ARG 1289 1289 ?    ?   ?   A . n 
A 1 1290 LEU 1290 1290 ?    ?   ?   A . n 
A 1 1291 LYS 1291 1291 ?    ?   ?   A . n 
A 1 1292 ASP 1292 1292 ?    ?   ?   A . n 
A 1 1293 ASP 1293 1293 ?    ?   ?   A . n 
A 1 1294 ARG 1294 1294 ?    ?   ?   A . n 
A 1 1295 GLU 1295 1295 ?    ?   ?   A . n 
A 1 1296 LYS 1296 1296 ?    ?   ?   A . n 
A 1 1297 CYS 1297 1297 ?    ?   ?   A . n 
A 1 1298 ALA 1298 1298 ?    ?   ?   A . n 
A 1 1299 LYS 1299 1299 ?    ?   ?   A . n 
A 1 1300 ALA 1300 1300 ?    ?   ?   A . n 
A 1 1301 LYS 1301 1301 ?    ?   ?   A . n 
A 1 1302 GLU 1302 1302 ?    ?   ?   A . n 
A 1 1303 ALA 1303 1303 ?    ?   ?   A . n 
A 1 1304 LEU 1304 1304 ?    ?   ?   A . n 
A 1 1305 GLU 1305 1305 ?    ?   ?   A . n 
A 1 1306 LEU 1306 1306 ?    ?   ?   A . n 
A 1 1307 THR 1307 1307 ?    ?   ?   A . n 
A 1 1308 ASP 1308 1308 ?    ?   ?   A . n 
A 1 1309 THR 1309 1309 ?    ?   ?   A . n 
A 1 1310 GLY 1310 1310 ?    ?   ?   A . n 
A 1 1311 LEU 1311 1311 ?    ?   ?   A . n 
A 1 1312 LEU 1312 1312 ?    ?   ?   A . n 
A 1 1313 SER 1313 1313 ?    ?   ?   A . n 
A 1 1314 GLY 1314 1314 ?    ?   ?   A . n 
A 1 1315 SER 1315 1315 ?    ?   ?   A . n 
A 1 1316 GLU 1316 1316 ?    ?   ?   A . n 
A 1 1317 GLU 1317 1317 ?    ?   ?   A . n 
A 1 1318 ARG 1318 1318 ?    ?   ?   A . n 
A 1 1319 VAL 1319 1319 ?    ?   ?   A . n 
A 1 1320 GLN 1320 1320 ?    ?   ?   A . n 
A 1 1321 VAL 1321 1321 ?    ?   ?   A . n 
A 1 1322 ALA 1322 1322 ?    ?   ?   A . n 
A 1 1323 LEU 1323 1323 ?    ?   ?   A . n 
A 1 1324 GLU 1324 1324 ?    ?   ?   A . n 
A 1 1325 GLU 1325 1325 ?    ?   ?   A . n 
A 1 1326 LEU 1326 1326 ?    ?   ?   A . n 
A 1 1327 GLN 1327 1327 ?    ?   ?   A . n 
A 1 1328 ASP 1328 1328 ?    ?   ?   A . n 
A 1 1329 LEU 1329 1329 ?    ?   ?   A . n 
A 1 1330 LYS 1330 1330 ?    ?   ?   A . n 
A 1 1331 GLY 1331 1331 ?    ?   ?   A . n 
A 1 1332 VAL 1332 1332 ?    ?   ?   A . n 
A 1 1333 TRP 1333 1333 ?    ?   ?   A . n 
A 1 1334 SER 1334 1334 ?    ?   ?   A . n 
A 1 1335 GLU 1335 1335 ?    ?   ?   A . n 
A 1 1336 LEU 1336 1336 ?    ?   ?   A . n 
A 1 1337 SER 1337 1337 ?    ?   ?   A . n 
A 1 1338 LYS 1338 1338 ?    ?   ?   A . n 
A 1 1339 VAL 1339 1339 ?    ?   ?   A . n 
A 1 1340 TRP 1340 1340 ?    ?   ?   A . n 
A 1 1341 GLU 1341 1341 ?    ?   ?   A . n 
A 1 1342 GLN 1342 1342 ?    ?   ?   A . n 
A 1 1343 ILE 1343 1343 ?    ?   ?   A . n 
A 1 1344 ASP 1344 1344 ?    ?   ?   A . n 
A 1 1345 GLN 1345 1345 ?    ?   ?   A . n 
A 1 1346 MET 1346 1346 ?    ?   ?   A . n 
A 1 1347 LYS 1347 1347 ?    ?   ?   A . n 
A 1 1348 GLU 1348 1348 ?    ?   ?   A . n 
A 1 1349 GLN 1349 1349 ?    ?   ?   A . n 
A 1 1350 PRO 1350 1350 ?    ?   ?   A . n 
A 1 1351 TRP 1351 1351 ?    ?   ?   A . n 
A 1 1352 VAL 1352 1352 ?    ?   ?   A . n 
A 1 1353 SER 1353 1353 ?    ?   ?   A . n 
A 1 1354 VAL 1354 1354 ?    ?   ?   A . n 
A 1 1355 GLN 1355 1355 ?    ?   ?   A . n 
A 1 1356 PRO 1356 1356 ?    ?   ?   A . n 
A 1 1357 ARG 1357 1357 ?    ?   ?   A . n 
A 1 1358 LYS 1358 1358 ?    ?   ?   A . n 
A 1 1359 LEU 1359 1359 ?    ?   ?   A . n 
A 1 1360 ARG 1360 1360 ?    ?   ?   A . n 
A 1 1361 GLN 1361 1361 ?    ?   ?   A . n 
A 1 1362 ASN 1362 1362 ?    ?   ?   A . n 
A 1 1363 LEU 1363 1363 ?    ?   ?   A . n 
A 1 1364 ASP 1364 1364 ?    ?   ?   A . n 
A 1 1365 ALA 1365 1365 ?    ?   ?   A . n 
A 1 1366 LEU 1366 1366 ?    ?   ?   A . n 
A 1 1367 LEU 1367 1367 ?    ?   ?   A . n 
A 1 1368 ASN 1368 1368 ?    ?   ?   A . n 
A 1 1369 GLN 1369 1369 ?    ?   ?   A . n 
A 1 1370 LEU 1370 1370 ?    ?   ?   A . n 
A 1 1371 LYS 1371 1371 ?    ?   ?   A . n 
A 1 1372 SER 1372 1372 ?    ?   ?   A . n 
A 1 1373 PHE 1373 1373 ?    ?   ?   A . n 
A 1 1374 PRO 1374 1374 ?    ?   ?   A . n 
A 1 1375 ALA 1375 1375 ?    ?   ?   A . n 
A 1 1376 ARG 1376 1376 ?    ?   ?   A . n 
A 1 1377 LEU 1377 1377 ?    ?   ?   A . n 
A 1 1378 ARG 1378 1378 ?    ?   ?   A . n 
A 1 1379 GLN 1379 1379 ?    ?   ?   A . n 
A 1 1380 TYR 1380 1380 ?    ?   ?   A . n 
A 1 1381 ALA 1381 1381 ?    ?   ?   A . n 
A 1 1382 SER 1382 1382 ?    ?   ?   A . n 
A 1 1383 TYR 1383 1383 ?    ?   ?   A . n 
A 1 1384 GLU 1384 1384 ?    ?   ?   A . n 
A 1 1385 PHE 1385 1385 ?    ?   ?   A . n 
A 1 1386 VAL 1386 1386 ?    ?   ?   A . n 
A 1 1387 GLN 1387 1387 ?    ?   ?   A . n 
A 1 1388 ARG 1388 1388 ?    ?   ?   A . n 
A 1 1389 LEU 1389 1389 ?    ?   ?   A . n 
A 1 1390 LEU 1390 1390 ?    ?   ?   A . n 
A 1 1391 LYS 1391 1391 ?    ?   ?   A . n 
A 1 1392 GLY 1392 1392 ?    ?   ?   A . n 
A 1 1393 TYR 1393 1393 ?    ?   ?   A . n 
A 1 1394 MET 1394 1394 ?    ?   ?   A . n 
A 1 1395 LYS 1395 1395 ?    ?   ?   A . n 
A 1 1396 ILE 1396 1396 ?    ?   ?   A . n 
A 1 1397 ASN 1397 1397 ?    ?   ?   A . n 
A 1 1398 MET 1398 1398 ?    ?   ?   A . n 
A 1 1399 LEU 1399 1399 ?    ?   ?   A . n 
A 1 1400 VAL 1400 1400 ?    ?   ?   A . n 
A 1 1401 ILE 1401 1401 ?    ?   ?   A . n 
A 1 1402 GLU 1402 1402 ?    ?   ?   A . n 
A 1 1403 LEU 1403 1403 ?    ?   ?   A . n 
A 1 1404 LYS 1404 1404 ?    ?   ?   A . n 
A 1 1405 SER 1405 1405 ?    ?   ?   A . n 
A 1 1406 GLU 1406 1406 ?    ?   ?   A . n 
A 1 1407 ALA 1407 1407 ?    ?   ?   A . n 
A 1 1408 LEU 1408 1408 ?    ?   ?   A . n 
A 1 1409 LYS 1409 1409 ?    ?   ?   A . n 
A 1 1410 ASP 1410 1410 ?    ?   ?   A . n 
A 1 1411 ARG 1411 1411 ?    ?   ?   A . n 
A 1 1412 HIS 1412 1412 ?    ?   ?   A . n 
A 1 1413 TRP 1413 1413 ?    ?   ?   A . n 
A 1 1414 LYS 1414 1414 ?    ?   ?   A . n 
A 1 1415 GLN 1415 1415 ?    ?   ?   A . n 
A 1 1416 LEU 1416 1416 ?    ?   ?   A . n 
A 1 1417 MET 1417 1417 ?    ?   ?   A . n 
A 1 1418 LYS 1418 1418 ?    ?   ?   A . n 
A 1 1419 ARG 1419 1419 ?    ?   ?   A . n 
A 1 1420 LEU 1420 1420 ?    ?   ?   A . n 
A 1 1421 HIS 1421 1421 ?    ?   ?   A . n 
A 1 1422 VAL 1422 1422 ?    ?   ?   A . n 
A 1 1423 ASN 1423 1423 ?    ?   ?   A . n 
A 1 1424 TRP 1424 1424 ?    ?   ?   A . n 
A 1 1425 VAL 1425 1425 ?    ?   ?   A . n 
A 1 1426 VAL 1426 1426 ?    ?   ?   A . n 
A 1 1427 SER 1427 1427 ?    ?   ?   A . n 
A 1 1428 GLU 1428 1428 ?    ?   ?   A . n 
A 1 1429 LEU 1429 1429 ?    ?   ?   A . n 
A 1 1430 THR 1430 1430 ?    ?   ?   A . n 
A 1 1431 LEU 1431 1431 ?    ?   ?   A . n 
A 1 1432 GLY 1432 1432 ?    ?   ?   A . n 
A 1 1433 GLN 1433 1433 ?    ?   ?   A . n 
A 1 1434 ILE 1434 1434 ?    ?   ?   A . n 
A 1 1435 TRP 1435 1435 ?    ?   ?   A . n 
A 1 1436 ASP 1436 1436 ?    ?   ?   A . n 
A 1 1437 VAL 1437 1437 ?    ?   ?   A . n 
A 1 1438 ASP 1438 1438 ?    ?   ?   A . n 
A 1 1439 LEU 1439 1439 ?    ?   ?   A . n 
A 1 1440 GLN 1440 1440 ?    ?   ?   A . n 
A 1 1441 LYS 1441 1441 ?    ?   ?   A . n 
A 1 1442 ASN 1442 1442 ?    ?   ?   A . n 
A 1 1443 GLU 1443 1443 ?    ?   ?   A . n 
A 1 1444 ALA 1444 1444 ?    ?   ?   A . n 
A 1 1445 ILE 1445 1445 ?    ?   ?   A . n 
A 1 1446 VAL 1446 1446 ?    ?   ?   A . n 
A 1 1447 LYS 1447 1447 ?    ?   ?   A . n 
A 1 1448 ASP 1448 1448 ?    ?   ?   A . n 
A 1 1449 VAL 1449 1449 ?    ?   ?   A . n 
A 1 1450 LEU 1450 1450 ?    ?   ?   A . n 
A 1 1451 LEU 1451 1451 ?    ?   ?   A . n 
A 1 1452 VAL 1452 1452 ?    ?   ?   A . n 
A 1 1453 ALA 1453 1453 ?    ?   ?   A . n 
A 1 1454 GLN 1454 1454 ?    ?   ?   A . n 
A 1 1455 GLY 1455 1455 ?    ?   ?   A . n 
A 1 1456 GLU 1456 1456 ?    ?   ?   A . n 
A 1 1457 MET 1457 1457 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                   9BMR 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_struct.entry_id                     9BMR 
_struct.title                        'State-1 of motor domain from full-length human phi dynein-1 in 5 mM ADP' 
_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        9BMR 
_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              9BMR 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 4646 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q14204 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  4646 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       4646 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'electron microscopy' 
_pdbx_struct_assembly_auth_evidence.details                'not applicable' 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0 
_pdbx_struct_oper_list.matrix[1][2]         0.0 
_pdbx_struct_oper_list.matrix[1][3]         0.0 
_pdbx_struct_oper_list.vector[1]            0.0 
_pdbx_struct_oper_list.matrix[2][1]         0.0 
_pdbx_struct_oper_list.matrix[2][2]         1.0 
_pdbx_struct_oper_list.matrix[2][3]         0.0 
_pdbx_struct_oper_list.vector[2]            0.0 
_pdbx_struct_oper_list.matrix[3][1]         0.0 
_pdbx_struct_oper_list.matrix[3][2]         0.0 
_pdbx_struct_oper_list.matrix[3][3]         1.0 
_pdbx_struct_oper_list.vector[3]            0.0 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1   AA1 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 ? ? ? ? ? ? ? 2.956 ? ? 
# 
_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_555 101.7 ? 
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 56.3  ? 
# 
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                   9BMR 
_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 ? ? -99.36  32.69   
2  1 ASN A 1670 ? ? 71.06   33.21   
3  1 ALA A 1862 ? ? 58.20   -121.50 
4  1 THR A 2061 ? ? -99.05  38.28   
5  1 ALA A 2121 ? ? -98.92  37.00   
6  1 ASN A 2130 ? ? -101.19 75.71   
7  1 PRO A 2796 ? ? -59.74  -9.18   
8  1 SER A 3640 ? ? -103.06 40.29   
9  1 PRO A 3643 ? ? -66.60  2.22    
10 1 ARG A 3910 ? ? 52.86   -98.38  
11 1 ASP A 3946 ? ? -95.56  53.22   
12 1 GLU A 3977 ? ? -95.08  -60.60  
13 1 CYS A 4170 ? ? -90.39  30.25   
14 1 ALA A 4197 ? ? -20.70  -67.81  
15 1 GLU A 4206 ? ? -95.70  59.31   
16 1 TYR A 4252 ? ? 75.10   -9.73   
17 1 ASP A 4298 ? ? -92.26  48.96   
18 1 ASP A 4314 ? ? -90.58  31.06   
19 1 CYS A 4556 ? ? -97.30  30.04   
20 1 ASN A 4597 ? ? 35.13   47.89   
21 1 GLU A 4599 ? ? 59.36   -162.53 
22 1 ALA A 4602 ? ? 65.30   -0.68   
23 1 THR A 4628 ? ? 52.04   -142.76 
# 
_pdbx_validate_planes.id              1 
_pdbx_validate_planes.PDB_model_num   1 
_pdbx_validate_planes.auth_comp_id    ARG 
_pdbx_validate_planes.auth_asym_id    A 
_pdbx_validate_planes.auth_seq_id     4195 
_pdbx_validate_planes.PDB_ins_code    ? 
_pdbx_validate_planes.label_alt_id    ? 
_pdbx_validate_planes.rmsd            0.119 
_pdbx_validate_planes.type            'SIDE CHAIN' 
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          9BMR 
_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                    9BMR 
_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                  2.6 
_em_3d_reconstruction.resolution_method           'FSC 0.143 CUT-OFF' 
_em_3d_reconstruction.magnification_calibration   ? 
_em_3d_reconstruction.nominal_pixel_size          ? 
_em_3d_reconstruction.actual_pixel_size           ? 
_em_3d_reconstruction.num_particles               174680 
_em_3d_reconstruction.euler_angles_details        ? 
_em_3d_reconstruction.num_class_averages          ? 
_em_3d_reconstruction.refinement_type             ? 
_em_3d_reconstruction.image_processing_id         1 
_em_3d_reconstruction.symmetry_type               POINT 
# 
_em_buffer.id            1 
_em_buffer.specimen_id   1 
_em_buffer.name          ? 
_em_buffer.details       '25 mM HEPES pH 7.2, 150 mM KCl, 1 mM MgCl2, 5 mM DTT, 5 mM ADP' 
_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 phi dynein-1 in 5mM ADP' 
_em_entity_assembly.details              ? 
_em_entity_assembly.synonym              ? 
_em_entity_assembly.oligomeric_details   ? 
_em_entity_assembly.entity_id_list       1 
# 
_em_imaging.entry_id                        9BMR 
_em_imaging.id                              1 
_em_imaging.astigmatism                     ? 
_em_imaging.electron_beam_tilt_params       ? 
_em_imaging.residual_tilt                   ? 
_em_imaging.microscope_model                'FEI TITAN KRIOS' 
_em_imaging.specimen_holder_type            ? 
_em_imaging.specimen_holder_model           'FEI TITAN KRIOS AUTOGRID HOLDER' 
_em_imaging.details                         ? 
_em_imaging.date                            ? 
_em_imaging.accelerating_voltage            300 
_em_imaging.illumination_mode               'FLOOD BEAM' 
_em_imaging.mode                            'BRIGHT FIELD' 
_em_imaging.nominal_cs                      2.7 
_em_imaging.nominal_defocus_min             1200 
_em_imaging.nominal_defocus_max             3000 
_em_imaging.calibrated_defocus_min          1200 
_em_imaging.calibrated_defocus_max          3000 
_em_imaging.tilt_angle_min                  ? 
_em_imaging.tilt_angle_max                  ? 
_em_imaging.nominal_magnification           105000 
_em_imaging.calibrated_magnification        105000 
_em_imaging.electron_source                 'FIELD EMISSION GUN' 
_em_imaging.citation_id                     ? 
_em_imaging.temperature                     ? 
_em_imaging.detector_distance               ? 
_em_imaging.recording_temperature_minimum   ? 
_em_imaging.recording_temperature_maximum   ? 
_em_imaging.alignment_procedure             ? 
_em_imaging.c2_aperture_diameter            50 
_em_imaging.specimen_id                     1 
_em_imaging.cryogen                         NITROGEN 
# 
_em_vitrification.entry_id              9BMR 
_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                9BMR 
_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           9BMR 
_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 phi dynein-1 in 5 mM ADP' 
# 
_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 EPU       ? 
MASKING                    ? 3  ? ? ? ?         ? 
'CTF CORRECTION'           ? 4  1 ? ? ?         ? 
'LAYERLINE INDEXING'       ? 5  ? ? ? ?         ? 
'DIFFRACTION INDEXING'     ? 6  ? ? ? ?         ? 
'MODEL FITTING'            ? 7  ? ? ? ?         ? 
'MODEL REFINEMENT'         ? 8  ? ? ? ?         ? 
OTHER                      ? 9  ? ? ? ?         ? 
'INITIAL EULER ASSIGNMENT' ? 10 1 ? ? ?         ? 
'FINAL EULER ASSIGNMENT'   ? 11 1 ? ? cryoSPARC 4 
CLASSIFICATION             ? 12 1 ? ? ?         ? 
RECONSTRUCTION             ? 13 1 ? ? cryoSPARC 4 
# 
_em_specimen.concentration           2 
_em_specimen.details                 ? 
_em_specimen.embedding_applied       NO 
_em_specimen.experiment_id           1 
_em_specimen.id                      1 
_em_specimen.shadowing_applied       NO 
_em_specimen.staining_applied        NO 
_em_specimen.vitrification_applied   YES 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)' 'United States' R35GM142959 1 
'National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)' 'United States' R35GM139483 2 
# 
_atom_sites.entry_id                    9BMR 
_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 ? 210.898 223.742 271.459 1.00 36.31 ? 1457 MET A N     1 
ATOM   2     C  CA    . MET A 1 1457 ? 210.147 222.555 271.062 1.00 36.14 ? 1457 MET A CA    1 
ATOM   3     C  C     . MET A 1 1457 ? 208.828 222.939 270.401 1.00 36.56 ? 1457 MET A C     1 
ATOM   4     O  O     . MET A 1 1457 ? 208.018 222.075 270.068 1.00 37.52 ? 1457 MET A O     1 
ATOM   5     C  CB    . MET A 1 1457 ? 209.887 221.656 272.271 1.00 34.60 ? 1457 MET A CB    1 
ATOM   6     C  CG    . MET A 1 1457 ? 208.847 222.204 273.234 1.00 36.04 ? 1457 MET A CG    1 
ATOM   7     S  SD    . MET A 1 1457 ? 209.423 223.673 274.105 1.00 62.27 ? 1457 MET A SD    1 
ATOM   8     C  CE    . MET A 1 1457 ? 210.691 222.969 275.156 1.00 40.38 ? 1457 MET A CE    1 
ATOM   9     N  N     . ALA A 1 1458 ? 208.620 224.244 270.213 1.00 31.23 ? 1458 ALA A N     1 
ATOM   10    C  CA    . ALA A 1 1458 ? 207.417 224.706 269.530 1.00 31.23 ? 1458 ALA A CA    1 
ATOM   11    C  C     . ALA A 1 1458 ? 207.361 224.197 268.098 1.00 35.75 ? 1458 ALA A C     1 
ATOM   12    O  O     . ALA A 1 1458 ? 206.273 223.908 267.583 1.00 38.19 ? 1458 ALA A O     1 
ATOM   13    C  CB    . ALA A 1 1458 ? 207.349 226.233 269.557 1.00 30.17 ? 1458 ALA A CB    1 
ATOM   14    N  N     . LEU A 1 1459 ? 208.516 224.087 267.438 1.00 36.57 ? 1459 LEU A N     1 
ATOM   15    C  CA    . LEU A 1 1459 ? 208.557 223.486 266.110 1.00 32.87 ? 1459 LEU A CA    1 
ATOM   16    C  C     . LEU A 1 1459 ? 208.124 222.026 266.156 1.00 32.47 ? 1459 LEU A C     1 
ATOM   17    O  O     . LEU A 1 1459 ? 207.401 221.558 265.269 1.00 34.96 ? 1459 LEU A O     1 
ATOM   18    C  CB    . LEU A 1 1459 ? 209.961 223.608 265.520 1.00 25.11 ? 1459 LEU A CB    1 
ATOM   19    C  CG    . LEU A 1 1459 ? 210.482 225.005 265.175 1.00 32.15 ? 1459 LEU A CG    1 
ATOM   20    C  CD1   . LEU A 1 1459 ? 211.147 225.658 266.377 1.00 34.96 ? 1459 LEU A CD1   1 
ATOM   21    C  CD2   . LEU A 1 1459 ? 211.445 224.929 264.005 1.00 30.79 ? 1459 LEU A CD2   1 
ATOM   22    N  N     . GLU A 1 1460 ? 208.558 221.291 267.184 1.00 26.08 ? 1460 GLU A N     1 
ATOM   23    C  CA    . GLU A 1 1460 ? 208.167 219.891 267.305 1.00 30.66 ? 1460 GLU A CA    1 
ATOM   24    C  C     . GLU A 1 1460 ? 206.658 219.754 267.472 1.00 36.05 ? 1460 GLU A C     1 
ATOM   25    O  O     . GLU A 1 1460 ? 206.055 218.796 266.976 1.00 36.11 ? 1460 GLU A O     1 
ATOM   26    C  CB    . GLU A 1 1460 ? 208.904 219.238 268.475 1.00 30.79 ? 1460 GLU A CB    1 
ATOM   27    C  CG    . GLU A 1 1460 ? 208.519 217.789 268.727 1.00 31.46 ? 1460 GLU A CG    1 
ATOM   28    C  CD    . GLU A 1 1460 ? 209.211 217.202 269.943 1.00 42.28 ? 1460 GLU A CD    1 
ATOM   29    O  OE1   . GLU A 1 1460 ? 209.000 217.723 271.060 1.00 41.21 ? 1460 GLU A OE1   1 
ATOM   30    O  OE2   . GLU A 1 1460 ? 209.968 216.223 269.782 1.00 37.94 ? 1460 GLU A OE2   1 
ATOM   31    N  N     . GLU A 1 1461 ? 206.031 220.705 268.171 1.00 32.87 ? 1461 GLU A N     1 
ATOM   32    C  CA    . GLU A 1 1461 ? 204.581 220.669 268.329 1.00 29.66 ? 1461 GLU A CA    1 
ATOM   33    C  C     . GLU A 1 1461 ? 203.873 220.820 266.989 1.00 32.21 ? 1461 GLU A C     1 
ATOM   34    O  O     . GLU A 1 1461 ? 202.879 220.133 266.724 1.00 33.07 ? 1461 GLU A O     1 
ATOM   35    C  CB    . GLU A 1 1461 ? 204.131 221.760 269.300 1.00 27.72 ? 1461 GLU A CB    1 
ATOM   36    C  CG    . GLU A 1 1461 ? 204.877 221.755 270.623 1.00 33.58 ? 1461 GLU A CG    1 
ATOM   37    C  CD    . GLU A 1 1461 ? 205.061 220.357 271.180 1.00 40.13 ? 1461 GLU A CD    1 
ATOM   38    O  OE1   . GLU A 1 1461 ? 204.045 219.696 271.480 1.00 38.93 ? 1461 GLU A OE1   1 
ATOM   39    O  OE2   . GLU A 1 1461 ? 206.222 219.920 271.319 1.00 43.02 ? 1461 GLU A OE2   1 
ATOM   40    N  N     . PHE A 1 1462 ? 204.368 221.713 266.130 1.00 30.68 ? 1462 PHE A N     1 
ATOM   41    C  CA    . PHE A 1 1462 ? 203.753 221.897 264.820 1.00 26.41 ? 1462 PHE A CA    1 
ATOM   42    C  C     . PHE A 1 1462 ? 203.845 220.627 263.987 1.00 29.82 ? 1462 PHE A C     1 
ATOM   43    O  O     . PHE A 1 1462 ? 202.872 220.237 263.329 1.00 30.78 ? 1462 PHE A O     1 
ATOM   44    C  CB    . PHE A 1 1462 ? 204.400 223.073 264.090 1.00 27.55 ? 1462 PHE A CB    1 
ATOM   45    C  CG    . PHE A 1 1462 ? 204.154 224.406 264.743 1.00 37.74 ? 1462 PHE A CG    1 
ATOM   46    C  CD1   . PHE A 1 1462 ? 203.131 224.563 265.665 1.00 34.98 ? 1462 PHE A CD1   1 
ATOM   47    C  CD2   . PHE A 1 1462 ? 204.945 225.499 264.436 1.00 33.74 ? 1462 PHE A CD2   1 
ATOM   48    C  CE1   . PHE A 1 1462 ? 202.904 225.785 266.267 1.00 36.34 ? 1462 PHE A CE1   1 
ATOM   49    C  CE2   . PHE A 1 1462 ? 204.723 226.725 265.035 1.00 35.25 ? 1462 PHE A CE2   1 
ATOM   50    C  CZ    . PHE A 1 1462 ? 203.701 226.869 265.952 1.00 36.89 ? 1462 PHE A CZ    1 
ATOM   51    N  N     . LEU A 1 1463 ? 205.001 219.961 264.004 1.00 28.25 ? 1463 LEU A N     1 
ATOM   52    C  CA    . LEU A 1 1463 ? 205.128 218.696 263.288 1.00 25.26 ? 1463 LEU A CA    1 
ATOM   53    C  C     . LEU A 1 1463 ? 204.185 217.644 263.855 1.00 27.82 ? 1463 LEU A C     1 
ATOM   54    O  O     . LEU A 1 1463 ? 203.577 216.876 263.101 1.00 31.14 ? 1463 LEU A O     1 
ATOM   55    C  CB    . LEU A 1 1463 ? 206.572 218.193 263.332 1.00 28.03 ? 1463 LEU A CB    1 
ATOM   56    C  CG    . LEU A 1 1463 ? 207.575 218.731 262.307 1.00 28.14 ? 1463 LEU A CG    1 
ATOM   57    C  CD1   . LEU A 1 1463 ? 207.166 218.331 260.895 1.00 26.85 ? 1463 LEU A CD1   1 
ATOM   58    C  CD2   . LEU A 1 1463 ? 207.763 220.233 262.409 1.00 27.00 ? 1463 LEU A CD2   1 
ATOM   59    N  N     . LYS A 1 1464 ? 204.055 217.589 265.184 1.00 28.08 ? 1464 LYS A N     1 
ATOM   60    C  CA    . LYS A 1 1464 ? 203.137 216.636 265.798 1.00 25.69 ? 1464 LYS A CA    1 
ATOM   61    C  C     . LYS A 1 1464 ? 201.692 216.951 265.427 1.00 27.93 ? 1464 LYS A C     1 
ATOM   62    O  O     . LYS A 1 1464 ? 200.904 216.041 265.148 1.00 31.40 ? 1464 LYS A O     1 
ATOM   63    C  CB    . LYS A 1 1464 ? 203.321 216.637 267.315 1.00 27.40 ? 1464 LYS A CB    1 
ATOM   64    C  CG    . LYS A 1 1464 ? 202.493 215.595 268.048 1.00 24.34 ? 1464 LYS A CG    1 
ATOM   65    C  CD    . LYS A 1 1464 ? 203.001 214.188 267.771 1.00 28.00 ? 1464 LYS A CD    1 
ATOM   66    C  CE    . LYS A 1 1464 ? 202.242 213.156 268.588 1.00 32.94 ? 1464 LYS A CE    1 
ATOM   67    N  NZ    . LYS A 1 1464 ? 202.698 211.766 268.302 1.00 35.89 ? 1464 LYS A NZ    1 
ATOM   68    N  N     . GLN A 1 1465 ? 201.326 218.235 265.424 1.00 27.27 ? 1465 GLN A N     1 
ATOM   69    C  CA    . GLN A 1 1465 ? 199.977 218.619 265.024 1.00 23.93 ? 1465 GLN A CA    1 
ATOM   70    C  C     . GLN A 1 1465 ? 199.723 218.294 263.557 1.00 28.94 ? 1465 GLN A C     1 
ATOM   71    O  O     . GLN A 1 1465 ? 198.649 217.797 263.202 1.00 31.08 ? 1465 GLN A O     1 
ATOM   72    C  CB    . GLN A 1 1465 ? 199.748 220.106 265.290 1.00 24.02 ? 1465 GLN A CB    1 
ATOM   73    C  CG    . GLN A 1 1465 ? 199.677 220.472 266.760 1.00 27.05 ? 1465 GLN A CG    1 
ATOM   74    C  CD    . GLN A 1 1465 ? 199.903 221.951 267.005 1.00 33.71 ? 1465 GLN A CD    1 
ATOM   75    O  OE1   . GLN A 1 1465 ? 200.799 222.338 267.757 1.00 35.17 ? 1465 GLN A OE1   1 
ATOM   76    N  NE2   . GLN A 1 1465 ? 199.089 222.787 266.370 1.00 35.58 ? 1465 GLN A NE2   1 
ATOM   77    N  N     . ILE A 1 1466 ? 200.700 218.573 262.690 1.00 26.70 ? 1466 ILE A N     1 
ATOM   78    C  CA    . ILE A 1 1466 ? 200.559 218.234 261.278 1.00 23.10 ? 1466 ILE A CA    1 
ATOM   79    C  C     . ILE A 1 1466 ? 200.449 216.726 261.104 1.00 22.25 ? 1466 ILE A C     1 
ATOM   80    O  O     . ILE A 1 1466 ? 199.616 216.231 260.333 1.00 23.76 ? 1466 ILE A O     1 
ATOM   81    C  CB    . ILE A 1 1466 ? 201.733 218.814 260.468 1.00 18.36 ? 1466 ILE A CB    1 
ATOM   82    C  CG1   . ILE A 1 1466 ? 201.675 220.342 260.472 1.00 22.46 ? 1466 ILE A CG1   1 
ATOM   83    C  CG2   . ILE A 1 1466 ? 201.704 218.295 259.042 1.00 20.44 ? 1466 ILE A CG2   1 
ATOM   84    C  CD1   . ILE A 1 1466 ? 202.684 221.001 259.564 1.00 24.28 ? 1466 ILE A CD1   1 
ATOM   85    N  N     . ARG A 1 1467 ? 201.280 215.971 261.825 1.00 21.83 ? 1467 ARG A N     1 
ATOM   86    C  CA    . ARG A 1 1467 ? 201.227 214.515 261.751 1.00 25.61 ? 1467 ARG A CA    1 
ATOM   87    C  C     . ARG A 1 1467 ? 199.892 213.978 262.250 1.00 27.28 ? 1467 ARG A C     1 
ATOM   88    O  O     . ARG A 1 1467 ? 199.333 213.053 261.651 1.00 29.24 ? 1467 ARG A O     1 
ATOM   89    C  CB    . ARG A 1 1467 ? 202.385 213.916 262.551 1.00 26.41 ? 1467 ARG A CB    1 
ATOM   90    C  CG    . ARG A 1 1467 ? 202.311 212.414 262.768 1.00 29.22 ? 1467 ARG A CG    1 
ATOM   91    C  CD    . ARG A 1 1467 ? 202.549 211.657 261.474 1.00 25.69 ? 1467 ARG A CD    1 
ATOM   92    N  NE    . ARG A 1 1467 ? 203.822 212.002 260.854 1.00 26.52 ? 1467 ARG A NE    1 
ATOM   93    C  CZ    . ARG A 1 1467 ? 205.015 211.685 261.340 1.00 29.41 ? 1467 ARG A CZ    1 
ATOM   94    N  NH1   . ARG A 1 1467 ? 205.145 210.975 262.449 1.00 30.53 ? 1467 ARG A NH1   1 
ATOM   95    N  NH2   . ARG A 1 1467 ? 206.105 212.081 260.690 1.00 31.35 ? 1467 ARG A NH2   1 
ATOM   96    N  N     . GLU A 1 1468 ? 199.360 214.549 263.333 1.00 25.01 ? 1468 GLU A N     1 
ATOM   97    C  CA    . GLU A 1 1468 ? 198.098 214.075 263.890 1.00 25.54 ? 1468 GLU A CA    1 
ATOM   98    C  C     . GLU A 1 1468 ? 196.902 214.426 263.014 1.00 29.12 ? 1468 GLU A C     1 
ATOM   99    O  O     . GLU A 1 1468 ? 195.937 213.654 262.955 1.00 29.86 ? 1468 GLU A O     1 
ATOM   100   C  CB    . GLU A 1 1468 ? 197.896 214.644 265.296 1.00 23.03 ? 1468 GLU A CB    1 
ATOM   101   C  CG    . GLU A 1 1468 ? 198.712 213.946 266.374 1.00 29.41 ? 1468 GLU A CG    1 
ATOM   102   C  CD    . GLU A 1 1468 ? 198.175 212.571 266.730 1.00 38.60 ? 1468 GLU A CD    1 
ATOM   103   O  OE1   . GLU A 1 1468 ? 197.093 212.198 266.230 1.00 40.72 ? 1468 GLU A OE1   1 
ATOM   104   O  OE2   . GLU A 1 1468 ? 198.840 211.858 267.512 1.00 35.18 ? 1468 GLU A OE2   1 
ATOM   105   N  N     . VAL A 1 1469 ? 196.934 215.576 262.339 1.00 25.64 ? 1469 VAL A N     1 
ATOM   106   C  CA    . VAL A 1 1469 ? 195.819 215.968 261.484 1.00 19.91 ? 1469 VAL A CA    1 
ATOM   107   C  C     . VAL A 1 1469 ? 195.661 214.993 260.324 1.00 22.49 ? 1469 VAL A C     1 
ATOM   108   O  O     . VAL A 1 1469 ? 194.545 214.578 259.991 1.00 27.60 ? 1469 VAL A O     1 
ATOM   109   C  CB    . VAL A 1 1469 ? 196.006 217.414 260.989 1.00 19.91 ? 1469 VAL A CB    1 
ATOM   110   C  CG1   . VAL A 1 1469 ? 195.130 217.688 259.775 1.00 23.60 ? 1469 VAL A CG1   1 
ATOM   111   C  CG2   . VAL A 1 1469 ? 195.687 218.394 262.100 1.00 19.91 ? 1469 VAL A CG2   1 
ATOM   112   N  N     . TRP A 1 1470 ? 196.767 214.599 259.703 1.00 20.71 ? 1470 TRP A N     1 
ATOM   113   C  CA    . TRP A 1 1470 ? 196.736 213.776 258.501 1.00 20.44 ? 1470 TRP A CA    1 
ATOM   114   C  C     . TRP A 1 1470 ? 196.730 212.281 258.789 1.00 25.51 ? 1470 TRP A C     1 
ATOM   115   O  O     . TRP A 1 1470 ? 196.628 211.486 257.848 1.00 30.06 ? 1470 TRP A O     1 
ATOM   116   C  CB    . TRP A 1 1470 ? 197.917 214.135 257.597 1.00 18.98 ? 1470 TRP A CB    1 
ATOM   117   C  CG    . TRP A 1 1470 ? 197.808 215.528 257.072 1.00 16.07 ? 1470 TRP A CG    1 
ATOM   118   C  CD1   . TRP A 1 1470 ? 198.603 216.589 257.383 1.00 17.35 ? 1470 TRP A CD1   1 
ATOM   119   C  CD2   . TRP A 1 1470 ? 196.828 216.016 256.152 1.00 16.33 ? 1470 TRP A CD2   1 
ATOM   120   N  NE1   . TRP A 1 1470 ? 198.183 217.710 256.708 1.00 19.10 ? 1470 TRP A NE1   1 
ATOM   121   C  CE2   . TRP A 1 1470 ? 197.093 217.383 255.944 1.00 17.33 ? 1470 TRP A CE2   1 
ATOM   122   C  CE3   . TRP A 1 1470 ? 195.753 215.428 255.480 1.00 15.28 ? 1470 TRP A CE3   1 
ATOM   123   C  CZ2   . TRP A 1 1470 ? 196.324 218.170 255.093 1.00 14.09 ? 1470 TRP A CZ2   1 
ATOM   124   C  CZ3   . TRP A 1 1470 ? 194.993 216.211 254.637 1.00 16.23 ? 1470 TRP A CZ3   1 
ATOM   125   C  CH2   . TRP A 1 1470 ? 195.281 217.567 254.450 1.00 12.50 ? 1470 TRP A CH2   1 
ATOM   126   N  N     . ASN A 1 1471 ? 196.836 211.876 260.049 1.00 28.35 ? 1471 ASN A N     1 
ATOM   127   C  CA    . ASN A 1 1471 ? 196.680 210.475 260.407 1.00 25.48 ? 1471 ASN A CA    1 
ATOM   128   C  C     . ASN A 1 1471 ? 195.225 210.083 260.622 1.00 27.41 ? 1471 ASN A C     1 
ATOM   129   O  O     . ASN A 1 1471 ? 194.934 208.891 260.763 1.00 30.88 ? 1471 ASN A O     1 
ATOM   130   C  CB    . ASN A 1 1471 ? 197.489 210.156 261.668 1.00 23.08 ? 1471 ASN A CB    1 
ATOM   131   C  CG    . ASN A 1 1471 ? 198.979 210.090 261.403 1.00 32.94 ? 1471 ASN A CG    1 
ATOM   132   O  OD1   . ASN A 1 1471 ? 199.429 210.293 260.276 1.00 32.58 ? 1471 ASN A OD1   1 
ATOM   133   N  ND2   . ASN A 1 1471 ? 199.754 209.805 262.444 1.00 31.67 ? 1471 ASN A ND2   1 
ATOM   134   N  N     . THR A 1 1472 ? 194.311 211.053 260.650 1.00 22.40 ? 1472 THR A N     1 
ATOM   135   C  CA    . THR A 1 1472 ? 192.898 210.790 260.893 1.00 24.54 ? 1472 THR A CA    1 
ATOM   136   C  C     . THR A 1 1472 ? 191.959 211.421 259.877 1.00 30.25 ? 1472 THR A C     1 
ATOM   137   O  O     . THR A 1 1472 ? 190.825 210.946 259.744 1.00 31.66 ? 1472 THR A O     1 
ATOM   138   C  CB    . THR A 1 1472 ? 192.489 211.283 262.289 1.00 28.01 ? 1472 THR A CB    1 
ATOM   139   O  OG1   . THR A 1 1472 ? 192.663 212.703 262.362 1.00 27.75 ? 1472 THR A OG1   1 
ATOM   140   C  CG2   . THR A 1 1472 ? 193.332 210.617 263.368 1.00 28.19 ? 1472 THR A CG2   1 
ATOM   141   N  N     . TYR A 1 1473 ? 192.381 212.462 259.163 1.00 25.03 ? 1473 TYR A N     1 
ATOM   142   C  CA    . TYR A 1 1473 ? 191.474 213.196 258.291 1.00 21.26 ? 1473 TYR A CA    1 
ATOM   143   C  C     . TYR A 1 1473 ? 191.112 212.335 257.086 1.00 27.43 ? 1473 TYR A C     1 
ATOM   144   O  O     . TYR A 1 1473 ? 191.989 211.932 256.315 1.00 23.70 ? 1473 TYR A O     1 
ATOM   145   C  CB    . TYR A 1 1473 ? 192.124 214.502 257.846 1.00 18.63 ? 1473 TYR A CB    1 
ATOM   146   C  CG    . TYR A 1 1473 ? 191.246 215.368 256.974 1.00 23.06 ? 1473 TYR A CG    1 
ATOM   147   C  CD1   . TYR A 1 1473 ? 190.206 216.107 257.524 1.00 30.47 ? 1473 TYR A CD1   1 
ATOM   148   C  CD2   . TYR A 1 1473 ? 191.443 215.434 255.606 1.00 21.08 ? 1473 TYR A CD2   1 
ATOM   149   C  CE1   . TYR A 1 1473 ? 189.399 216.903 256.732 1.00 26.11 ? 1473 TYR A CE1   1 
ATOM   150   C  CE2   . TYR A 1 1473 ? 190.639 216.221 254.809 1.00 22.07 ? 1473 TYR A CE2   1 
ATOM   151   C  CZ    . TYR A 1 1473 ? 189.622 216.955 255.374 1.00 26.74 ? 1473 TYR A CZ    1 
ATOM   152   O  OH    . TYR A 1 1473 ? 188.823 217.738 254.574 1.00 23.25 ? 1473 TYR A OH    1 
ATOM   153   N  N     . GLU A 1 1474 ? 189.823 212.056 256.923 1.00 21.77 ? 1474 GLU A N     1 
ATOM   154   C  CA    . GLU A 1 1474 ? 189.331 211.191 255.864 1.00 19.81 ? 1474 GLU A CA    1 
ATOM   155   C  C     . GLU A 1 1474 ? 188.561 212.005 254.834 1.00 24.32 ? 1474 GLU A C     1 
ATOM   156   O  O     . GLU A 1 1474 ? 187.886 212.981 255.176 1.00 28.49 ? 1474 GLU A O     1 
ATOM   157   C  CB    . GLU A 1 1474 ? 188.428 210.089 256.429 1.00 20.98 ? 1474 GLU A CB    1 
ATOM   158   C  CG    . GLU A 1 1474 ? 189.169 209.007 257.192 1.00 22.04 ? 1474 GLU A CG    1 
ATOM   159   C  CD    . GLU A 1 1474 ? 188.279 207.837 257.557 1.00 30.16 ? 1474 GLU A CD    1 
ATOM   160   O  OE1   . GLU A 1 1474 ? 187.066 207.899 257.270 1.00 31.43 ? 1474 GLU A OE1   1 
ATOM   161   O  OE2   . GLU A 1 1474 ? 188.792 206.853 258.129 1.00 33.85 ? 1474 GLU A OE2   1 
ATOM   162   N  N     . LEU A 1 1475 ? 188.672 211.600 253.571 1.00 21.43 ? 1475 LEU A N     1 
ATOM   163   C  CA    . LEU A 1 1475 ? 187.887 212.217 252.511 1.00 17.40 ? 1475 LEU A CA    1 
ATOM   164   C  C     . LEU A 1 1475 ? 186.402 212.030 252.790 1.00 22.30 ? 1475 LEU A C     1 
ATOM   165   O  O     . LEU A 1 1475 ? 185.907 210.899 252.833 1.00 22.47 ? 1475 LEU A O     1 
ATOM   166   C  CB    . LEU A 1 1475 ? 188.259 211.612 251.160 1.00 12.85 ? 1475 LEU A CB    1 
ATOM   167   C  CG    . LEU A 1 1475 ? 189.651 211.965 250.636 1.00 16.69 ? 1475 LEU A CG    1 
ATOM   168   C  CD1   . LEU A 1 1475 ? 189.979 211.157 249.395 1.00 12.76 ? 1475 LEU A CD1   1 
ATOM   169   C  CD2   . LEU A 1 1475 ? 189.751 213.455 250.353 1.00 12.07 ? 1475 LEU A CD2   1 
ATOM   170   N  N     . ASP A 1 1476 ? 185.698 213.141 252.985 1.00 19.94 ? 1476 ASP A N     1 
ATOM   171   C  CA    . ASP A 1 1476 ? 184.277 213.093 253.304 1.00 17.67 ? 1476 ASP A CA    1 
ATOM   172   C  C     . ASP A 1 1476 ? 183.500 212.611 252.084 1.00 24.36 ? 1476 ASP A C     1 
ATOM   173   O  O     . ASP A 1 1476 ? 183.460 213.291 251.054 1.00 27.76 ? 1476 ASP A O     1 
ATOM   174   C  CB    . ASP A 1 1476 ? 183.802 214.472 253.754 1.00 26.96 ? 1476 ASP A CB    1 
ATOM   175   C  CG    . ASP A 1 1476 ? 182.386 214.463 254.287 1.00 36.95 ? 1476 ASP A CG    1 
ATOM   176   O  OD1   . ASP A 1 1476 ? 181.780 213.375 254.378 1.00 37.99 ? 1476 ASP A OD1   1 
ATOM   177   O  OD2   . ASP A 1 1476 ? 181.888 215.551 254.641 1.00 35.38 ? 1476 ASP A OD2   1 
ATOM   178   N  N     . LEU A 1 1477 ? 182.885 211.439 252.200 1.00 24.71 ? 1477 LEU A N     1 
ATOM   179   C  CA    . LEU A 1 1477 ? 182.251 210.774 251.071 1.00 17.60 ? 1477 LEU A CA    1 
ATOM   180   C  C     . LEU A 1 1477 ? 180.740 210.948 251.121 1.00 22.82 ? 1477 LEU A C     1 
ATOM   181   O  O     . LEU A 1 1477 ? 180.142 210.989 252.201 1.00 30.25 ? 1477 LEU A O     1 
ATOM   182   C  CB    . LEU A 1 1477 ? 182.599 209.285 251.047 1.00 18.09 ? 1477 LEU A CB    1 
ATOM   183   C  CG    . LEU A 1 1477 ? 184.049 208.940 250.705 1.00 19.44 ? 1477 LEU A CG    1 
ATOM   184   C  CD1   . LEU A 1 1477 ? 184.222 207.440 250.565 1.00 21.81 ? 1477 LEU A CD1   1 
ATOM   185   C  CD2   . LEU A 1 1477 ? 184.497 209.656 249.447 1.00 11.65 ? 1477 LEU A CD2   1 
ATOM   186   N  N     . VAL A 1 1478 ? 180.134 211.061 249.941 1.00 26.98 ? 1478 VAL A N     1 
ATOM   187   C  CA    . VAL A 1 1478 ? 178.687 211.125 249.782 1.00 21.35 ? 1478 VAL A CA    1 
ATOM   188   C  C     . VAL A 1 1478 ? 178.274 210.214 248.636 1.00 18.19 ? 1478 VAL A C     1 
ATOM   189   O  O     . VAL A 1 1478 ? 178.919 210.188 247.582 1.00 19.05 ? 1478 VAL A O     1 
ATOM   190   C  CB    . VAL A 1 1478 ? 178.195 212.570 249.540 1.00 22.35 ? 1478 VAL A CB    1 
ATOM   191   C  CG1   . VAL A 1 1478 ? 178.740 213.125 248.235 1.00 16.40 ? 1478 VAL A CG1   1 
ATOM   192   C  CG2   . VAL A 1 1478 ? 176.675 212.593 249.504 1.00 20.91 ? 1478 VAL A CG2   1 
ATOM   193   N  N     . ASN A 1 1479 ? 177.209 209.449 248.852 1.00 18.76 ? 1479 ASN A N     1 
ATOM   194   C  CA    . ASN A 1 1479 ? 176.657 208.625 247.787 1.00 18.15 ? 1479 ASN A CA    1 
ATOM   195   C  C     . ASN A 1 1479 ? 176.026 209.503 246.714 1.00 21.20 ? 1479 ASN A C     1 
ATOM   196   O  O     . ASN A 1 1479 ? 175.368 210.503 247.014 1.00 20.85 ? 1479 ASN A O     1 
ATOM   197   C  CB    . ASN A 1 1479 ? 175.624 207.652 248.345 1.00 19.14 ? 1479 ASN A CB    1 
ATOM   198   C  CG    . ASN A 1 1479 ? 174.908 206.880 247.260 1.00 18.96 ? 1479 ASN A CG    1 
ATOM   199   O  OD1   . ASN A 1 1479 ? 175.537 206.189 246.459 1.00 22.84 ? 1479 ASN A OD1   1 
ATOM   200   N  ND2   . ASN A 1 1479 ? 173.587 206.994 247.226 1.00 20.72 ? 1479 ASN A ND2   1 
ATOM   201   N  N     . TYR A 1 1480 ? 176.229 209.124 245.455 1.00 17.89 ? 1480 TYR A N     1 
ATOM   202   C  CA    . TYR A 1 1480 ? 175.700 209.866 244.314 1.00 20.18 ? 1480 TYR A CA    1 
ATOM   203   C  C     . TYR A 1 1480 ? 174.869 208.903 243.470 1.00 20.59 ? 1480 TYR A C     1 
ATOM   204   O  O     . TYR A 1 1480 ? 175.414 208.145 242.662 1.00 19.26 ? 1480 TYR A O     1 
ATOM   205   C  CB    . TYR A 1 1480 ? 176.831 210.504 243.509 1.00 16.84 ? 1480 TYR A CB    1 
ATOM   206   C  CG    . TYR A 1 1480 ? 176.396 211.131 242.202 1.00 13.44 ? 1480 TYR A CG    1 
ATOM   207   C  CD1   . TYR A 1 1480 ? 175.827 212.397 242.175 1.00 16.30 ? 1480 TYR A CD1   1 
ATOM   208   C  CD2   . TYR A 1 1480 ? 176.570 210.468 240.995 1.00 13.40 ? 1480 TYR A CD2   1 
ATOM   209   C  CE1   . TYR A 1 1480 ? 175.430 212.981 240.986 1.00 14.28 ? 1480 TYR A CE1   1 
ATOM   210   C  CE2   . TYR A 1 1480 ? 176.176 211.043 239.799 1.00 15.34 ? 1480 TYR A CE2   1 
ATOM   211   C  CZ    . TYR A 1 1480 ? 175.608 212.299 239.803 1.00 16.43 ? 1480 TYR A CZ    1 
ATOM   212   O  OH    . TYR A 1 1480 ? 175.217 212.879 238.618 1.00 20.91 ? 1480 TYR A OH    1 
ATOM   213   N  N     . GLN A 1 1481 ? 173.550 208.931 243.675 1.00 18.23 ? 1481 GLN A N     1 
ATOM   214   C  CA    . GLN A 1 1481 ? 172.594 208.140 242.896 1.00 19.36 ? 1481 GLN A CA    1 
ATOM   215   C  C     . GLN A 1 1481 ? 172.902 206.644 242.942 1.00 19.60 ? 1481 GLN A C     1 
ATOM   216   O  O     . GLN A 1 1481 ? 172.698 205.932 241.956 1.00 26.47 ? 1481 GLN A O     1 
ATOM   217   C  CB    . GLN A 1 1481 ? 172.532 208.620 241.443 1.00 22.87 ? 1481 GLN A CB    1 
ATOM   218   C  CG    . GLN A 1 1481 ? 172.386 210.121 241.287 1.00 17.83 ? 1481 GLN A CG    1 
ATOM   219   C  CD    . GLN A 1 1481 ? 172.591 210.572 239.858 1.00 18.21 ? 1481 GLN A CD    1 
ATOM   220   O  OE1   . GLN A 1 1481 ? 172.860 209.762 238.975 1.00 23.08 ? 1481 GLN A OE1   1 
ATOM   221   N  NE2   . GLN A 1 1481 ? 172.463 211.873 239.622 1.00 24.98 ? 1481 GLN A NE2   1 
ATOM   222   N  N     . ASN A 1 1482 ? 173.393 206.163 244.086 1.00 15.25 ? 1482 ASN A N     1 
ATOM   223   C  CA    . ASN A 1 1482 ? 173.696 204.744 244.293 1.00 17.77 ? 1482 ASN A CA    1 
ATOM   224   C  C     . ASN A 1 1482 ? 174.675 204.210 243.251 1.00 19.71 ? 1482 ASN A C     1 
ATOM   225   O  O     . ASN A 1 1482 ? 174.618 203.037 242.875 1.00 25.71 ? 1482 ASN A O     1 
ATOM   226   C  CB    . ASN A 1 1482 ? 172.419 203.898 244.308 1.00 20.52 ? 1482 ASN A CB    1 
ATOM   227   C  CG    . ASN A 1 1482 ? 171.498 204.254 245.458 1.00 29.09 ? 1482 ASN A CG    1 
ATOM   228   O  OD1   . ASN A 1 1482 ? 171.843 205.063 246.320 1.00 24.92 ? 1482 ASN A OD1   1 
ATOM   229   N  ND2   . ASN A 1 1482 ? 170.316 203.650 245.477 1.00 27.57 ? 1482 ASN A ND2   1 
ATOM   230   N  N     . LYS A 1 1483 ? 175.582 205.063 242.780 1.00 18.97 ? 1483 LYS A N     1 
ATOM   231   C  CA    . LYS A 1 1483 ? 176.597 204.664 241.817 1.00 18.04 ? 1483 LYS A CA    1 
ATOM   232   C  C     . LYS A 1 1483 ? 178.010 204.692 242.378 1.00 25.05 ? 1483 LYS A C     1 
ATOM   233   O  O     . LYS A 1 1483 ? 178.821 203.840 242.010 1.00 24.52 ? 1483 LYS A O     1 
ATOM   234   C  CB    . LYS A 1 1483 ? 176.548 205.567 240.578 1.00 17.46 ? 1483 LYS A CB    1 
ATOM   235   C  CG    . LYS A 1 1483 ? 175.198 205.628 239.881 1.00 24.86 ? 1483 LYS A CG    1 
ATOM   236   C  CD    . LYS A 1 1483 ? 175.071 206.898 239.048 1.00 25.37 ? 1483 LYS A CD    1 
ATOM   237   C  CE    . LYS A 1 1483 ? 173.895 206.828 238.088 1.00 24.38 ? 1483 LYS A CE    1 
ATOM   238   N  NZ    . LYS A 1 1483 ? 174.206 206.017 236.879 1.00 22.19 ? 1483 LYS A NZ    1 
ATOM   239   N  N     . CYS A 1 1484 ? 178.320 205.637 243.253 1.00 19.73 ? 1484 CYS A N     1 
ATOM   240   C  CA    . CYS A 1 1484 ? 179.668 205.816 243.780 1.00 16.99 ? 1484 CYS A CA    1 
ATOM   241   C  C     . CYS A 1 1484 ? 179.569 206.676 245.035 1.00 20.13 ? 1484 CYS A C     1 
ATOM   242   O  O     . CYS A 1 1484 ? 178.470 206.966 245.523 1.00 21.43 ? 1484 CYS A O     1 
ATOM   243   C  CB    . CYS A 1 1484 ? 180.593 206.431 242.729 1.00 14.22 ? 1484 CYS A CB    1 
ATOM   244   S  SG    . CYS A 1 1484 ? 180.170 208.122 242.275 1.00 42.47 ? 1484 CYS A SG    1 
ATOM   245   N  N     . ARG A 1 1485 ? 180.721 207.083 245.562 1.00 21.25 ? 1485 ARG A N     1 
ATOM   246   C  CA    . ARG A 1 1485 ? 180.791 207.895 246.773 1.00 17.36 ? 1485 ARG A CA    1 
ATOM   247   C  C     . ARG A 1 1485 ? 181.693 209.093 246.508 1.00 20.94 ? 1485 ARG A C     1 
ATOM   248   O  O     . ARG A 1 1485 ? 182.902 209.026 246.746 1.00 35.19 ? 1485 ARG A O     1 
ATOM   249   C  CB    . ARG A 1 1485 ? 181.303 207.078 247.958 1.00 17.47 ? 1485 ARG A CB    1 
ATOM   250   C  CG    . ARG A 1 1485 ? 180.464 205.856 248.276 1.00 20.08 ? 1485 ARG A CG    1 
ATOM   251   C  CD    . ARG A 1 1485 ? 179.431 206.167 249.346 1.00 21.80 ? 1485 ARG A CD    1 
ATOM   252   N  NE    . ARG A 1 1485 ? 180.031 206.706 250.559 1.00 17.82 ? 1485 ARG A NE    1 
ATOM   253   C  CZ    . ARG A 1 1485 ? 180.765 206.003 251.414 1.00 24.37 ? 1485 ARG A CZ    1 
ATOM   254   N  NH1   . ARG A 1 1485 ? 181.001 204.714 251.228 1.00 28.82 ? 1485 ARG A NH1   1 
ATOM   255   N  NH2   . ARG A 1 1485 ? 181.269 206.607 252.485 1.00 21.81 ? 1485 ARG A NH2   1 
ATOM   256   N  N     . LEU A 1 1486 ? 181.100 210.189 246.043 1.00 16.90 ? 1486 LEU A N     1 
ATOM   257   C  CA    . LEU A 1 1486 ? 181.839 211.390 245.684 1.00 14.60 ? 1486 LEU A CA    1 
ATOM   258   C  C     . LEU A 1 1486 ? 182.464 212.032 246.922 1.00 12.77 ? 1486 LEU A C     1 
ATOM   259   O  O     . LEU A 1 1486 ? 182.233 211.616 248.058 1.00 17.09 ? 1486 LEU A O     1 
ATOM   260   C  CB    . LEU A 1 1486 ? 180.922 212.385 244.981 1.00 13.15 ? 1486 LEU A CB    1 
ATOM   261   C  CG    . LEU A 1 1486 ? 180.451 212.038 243.570 1.00 9.95  ? 1486 LEU A CG    1 
ATOM   262   C  CD1   . LEU A 1 1486 ? 179.910 213.274 242.891 1.00 10.93 ? 1486 LEU A CD1   1 
ATOM   263   C  CD2   . LEU A 1 1486 ? 181.561 211.414 242.748 1.00 11.64 ? 1486 LEU A CD2   1 
ATOM   264   N  N     . ILE A 1 1487 ? 183.260 213.072 246.688 1.00 11.25 ? 1487 ILE A N     1 
ATOM   265   C  CA    . ILE A 1 1487 ? 183.992 213.769 247.741 1.00 13.94 ? 1487 ILE A CA    1 
ATOM   266   C  C     . ILE A 1 1487 ? 183.466 215.193 247.854 1.00 11.65 ? 1487 ILE A C     1 
ATOM   267   O  O     . ILE A 1 1487 ? 183.522 215.963 246.887 1.00 18.06 ? 1487 ILE A O     1 
ATOM   268   C  CB    . ILE A 1 1487 ? 185.505 213.763 247.469 1.00 12.50 ? 1487 ILE A CB    1 
ATOM   269   C  CG1   . ILE A 1 1487 ? 186.064 212.350 247.616 1.00 12.93 ? 1487 ILE A CG1   1 
ATOM   270   C  CG2   . ILE A 1 1487 ? 186.229 214.741 248.380 1.00 10.71 ? 1487 ILE A CG2   1 
ATOM   271   C  CD1   . ILE A 1 1487 ? 187.479 212.211 247.154 1.00 11.49 ? 1487 ILE A CD1   1 
ATOM   272   N  N     . ARG A 1 1488 ? 182.960 215.546 249.034 1.00 12.34 ? 1488 ARG A N     1 
ATOM   273   C  CA    . ARG A 1 1488 ? 182.629 216.924 249.353 1.00 14.96 ? 1488 ARG A CA    1 
ATOM   274   C  C     . ARG A 1 1488 ? 183.777 217.556 250.139 1.00 16.31 ? 1488 ARG A C     1 
ATOM   275   O  O     . ARG A 1 1488 ? 184.865 216.987 250.267 1.00 15.51 ? 1488 ARG A O     1 
ATOM   276   C  CB    . ARG A 1 1488 ? 181.323 217.036 250.145 1.00 15.81 ? 1488 ARG A CB    1 
ATOM   277   C  CG    . ARG A 1 1488 ? 181.404 216.456 251.548 1.00 27.26 ? 1488 ARG A CG    1 
ATOM   278   C  CD    . ARG A 1 1488 ? 180.073 216.498 252.293 1.00 28.09 ? 1488 ARG A CD    1 
ATOM   279   N  NE    . ARG A 1 1488 ? 179.028 215.626 251.781 1.00 28.35 ? 1488 ARG A NE    1 
ATOM   280   C  CZ    . ARG A 1 1488 ? 177.777 215.652 252.222 1.00 33.21 ? 1488 ARG A CZ    1 
ATOM   281   N  NH1   . ARG A 1 1488 ? 177.395 216.490 253.172 1.00 30.49 ? 1488 ARG A NH1   1 
ATOM   282   N  NH2   . ARG A 1 1488 ? 176.887 214.817 251.699 1.00 33.14 ? 1488 ARG A NH2   1 
ATOM   283   N  N     . GLY A 1 1489 ? 183.530 218.745 250.682 1.00 14.90 ? 1489 GLY A N     1 
ATOM   284   C  CA    . GLY A 1 1489 ? 184.494 219.395 251.556 1.00 15.69 ? 1489 GLY A CA    1 
ATOM   285   C  C     . GLY A 1 1489 ? 185.763 219.842 250.870 1.00 14.63 ? 1489 GLY A C     1 
ATOM   286   O  O     . GLY A 1 1489 ? 186.840 219.773 251.470 1.00 18.63 ? 1489 GLY A O     1 
ATOM   287   N  N     . TRP A 1 1490 ? 185.663 220.311 249.627 1.00 11.14 ? 1490 TRP A N     1 
ATOM   288   C  CA    . TRP A 1 1490 ? 186.844 220.795 248.920 1.00 11.84 ? 1490 TRP A CA    1 
ATOM   289   C  C     . TRP A 1 1490 ? 187.430 222.030 249.587 1.00 19.18 ? 1490 TRP A C     1 
ATOM   290   O  O     . TRP A 1 1490 ? 188.654 222.191 249.645 1.00 18.71 ? 1490 TRP A O     1 
ATOM   291   C  CB    . TRP A 1 1490 ? 186.499 221.080 247.464 1.00 11.07 ? 1490 TRP A CB    1 
ATOM   292   C  CG    . TRP A 1 1490 ? 186.153 219.849 246.732 1.00 11.13 ? 1490 TRP A CG    1 
ATOM   293   C  CD1   . TRP A 1 1490 ? 184.911 219.410 246.387 1.00 9.47  ? 1490 TRP A CD1   1 
ATOM   294   C  CD2   . TRP A 1 1490 ? 187.072 218.861 246.283 1.00 14.35 ? 1490 TRP A CD2   1 
ATOM   295   N  NE1   . TRP A 1 1490 ? 185.008 218.210 245.724 1.00 6.58  ? 1490 TRP A NE1   1 
ATOM   296   C  CE2   . TRP A 1 1490 ? 186.327 217.852 245.652 1.00 7.68  ? 1490 TRP A CE2   1 
ATOM   297   C  CE3   . TRP A 1 1490 ? 188.463 218.737 246.345 1.00 11.85 ? 1490 TRP A CE3   1 
ATOM   298   C  CZ2   . TRP A 1 1490 ? 186.924 216.738 245.088 1.00 8.25  ? 1490 TRP A CZ2   1 
ATOM   299   C  CZ3   . TRP A 1 1490 ? 189.049 217.635 245.789 1.00 10.92 ? 1490 TRP A CZ3   1 
ATOM   300   C  CH2   . TRP A 1 1490 ? 188.285 216.651 245.168 1.00 6.49  ? 1490 TRP A CH2   1 
ATOM   301   N  N     . ASP A 1 1491 ? 186.573 222.924 250.083 1.00 15.33 ? 1491 ASP A N     1 
ATOM   302   C  CA    . ASP A 1 1491 ? 187.075 224.090 250.799 1.00 15.57 ? 1491 ASP A CA    1 
ATOM   303   C  C     . ASP A 1 1491 ? 187.826 223.673 252.058 1.00 18.30 ? 1491 ASP A C     1 
ATOM   304   O  O     . ASP A 1 1491 ? 188.893 224.219 252.359 1.00 19.96 ? 1491 ASP A O     1 
ATOM   305   C  CB    . ASP A 1 1491 ? 185.921 225.033 251.138 1.00 18.07 ? 1491 ASP A CB    1 
ATOM   306   C  CG    . ASP A 1 1491 ? 185.578 225.964 249.991 1.00 27.14 ? 1491 ASP A CG    1 
ATOM   307   O  OD1   . ASP A 1 1491 ? 186.465 226.729 249.558 1.00 31.16 ? 1491 ASP A OD1   1 
ATOM   308   O  OD2   . ASP A 1 1491 ? 184.422 225.930 249.521 1.00 31.37 ? 1491 ASP A OD2   1 
ATOM   309   N  N     . ASP A 1 1492 ? 187.291 222.700 252.799 1.00 18.80 ? 1492 ASP A N     1 
ATOM   310   C  CA    . ASP A 1 1492 ? 187.978 222.227 253.997 1.00 17.93 ? 1492 ASP A CA    1 
ATOM   311   C  C     . ASP A 1 1492 ? 189.309 221.572 253.651 1.00 20.36 ? 1492 ASP A C     1 
ATOM   312   O  O     . ASP A 1 1492 ? 190.313 221.791 254.338 1.00 21.47 ? 1492 ASP A O     1 
ATOM   313   C  CB    . ASP A 1 1492 ? 187.083 221.252 254.763 1.00 17.72 ? 1492 ASP A CB    1 
ATOM   314   C  CG    . ASP A 1 1492 ? 185.805 221.898 255.251 1.00 26.87 ? 1492 ASP A CG    1 
ATOM   315   O  OD1   . ASP A 1 1492 ? 185.890 222.878 256.019 1.00 28.56 ? 1492 ASP A OD1   1 
ATOM   316   O  OD2   . ASP A 1 1492 ? 184.715 221.425 254.871 1.00 32.01 ? 1492 ASP A OD2   1 
ATOM   317   N  N     . LEU A 1 1493 ? 189.334 220.759 252.593 1.00 21.33 ? 1493 LEU A N     1 
ATOM   318   C  CA    . LEU A 1 1493 ? 190.571 220.103 252.176 1.00 13.89 ? 1493 LEU A CA    1 
ATOM   319   C  C     . LEU A 1 1493 ? 191.623 221.115 251.742 1.00 14.54 ? 1493 LEU A C     1 
ATOM   320   O  O     . LEU A 1 1493 ? 192.789 221.028 252.142 1.00 18.27 ? 1493 LEU A O     1 
ATOM   321   C  CB    . LEU A 1 1493 ? 190.277 219.119 251.043 1.00 16.99 ? 1493 LEU A CB    1 
ATOM   322   C  CG    . LEU A 1 1493 ? 191.359 218.122 250.621 1.00 13.36 ? 1493 LEU A CG    1 
ATOM   323   C  CD1   . LEU A 1 1493 ? 191.658 217.114 251.702 1.00 16.59 ? 1493 LEU A CD1   1 
ATOM   324   C  CD2   . LEU A 1 1493 ? 190.934 217.421 249.345 1.00 11.50 ? 1493 LEU A CD2   1 
ATOM   325   N  N     . PHE A 1 1494 ? 191.228 222.088 250.920 1.00 16.05 ? 1494 PHE A N     1 
ATOM   326   C  CA    . PHE A 1 1494 ? 192.208 222.994 250.331 1.00 15.92 ? 1494 PHE A CA    1 
ATOM   327   C  C     . PHE A 1 1494 ? 192.758 223.975 251.359 1.00 19.11 ? 1494 PHE A C     1 
ATOM   328   O  O     . PHE A 1 1494 ? 193.968 224.222 251.398 1.00 18.39 ? 1494 PHE A O     1 
ATOM   329   C  CB    . PHE A 1 1494 ? 191.588 223.730 249.146 1.00 14.24 ? 1494 PHE A CB    1 
ATOM   330   C  CG    . PHE A 1 1494 ? 191.439 222.877 247.921 1.00 13.35 ? 1494 PHE A CG    1 
ATOM   331   C  CD1   . PHE A 1 1494 ? 192.332 221.851 247.668 1.00 15.80 ? 1494 PHE A CD1   1 
ATOM   332   C  CD2   . PHE A 1 1494 ? 190.405 223.092 247.030 1.00 15.51 ? 1494 PHE A CD2   1 
ATOM   333   C  CE1   . PHE A 1 1494 ? 192.201 221.058 246.547 1.00 9.72  ? 1494 PHE A CE1   1 
ATOM   334   C  CE2   . PHE A 1 1494 ? 190.269 222.301 245.905 1.00 16.67 ? 1494 PHE A CE2   1 
ATOM   335   C  CZ    . PHE A 1 1494 ? 191.169 221.286 245.664 1.00 11.99 ? 1494 PHE A CZ    1 
ATOM   336   N  N     . ASN A 1 1495 ? 191.889 224.550 252.194 1.00 17.86 ? 1495 ASN A N     1 
ATOM   337   C  CA    . ASN A 1 1495 ? 192.365 225.471 253.222 1.00 19.36 ? 1495 ASN A CA    1 
ATOM   338   C  C     . ASN A 1 1495 ? 193.240 224.758 254.244 1.00 15.26 ? 1495 ASN A C     1 
ATOM   339   O  O     . ASN A 1 1495 ? 194.246 225.313 254.700 1.00 17.04 ? 1495 ASN A O     1 
ATOM   340   C  CB    . ASN A 1 1495 ? 191.191 226.163 253.910 1.00 15.38 ? 1495 ASN A CB    1 
ATOM   341   C  CG    . ASN A 1 1495 ? 190.198 226.739 252.926 1.00 19.26 ? 1495 ASN A CG    1 
ATOM   342   O  OD1   . ASN A 1 1495 ? 190.549 227.072 251.795 1.00 26.86 ? 1495 ASN A OD1   1 
ATOM   343   N  ND2   . ASN A 1 1495 ? 188.947 226.862 253.351 1.00 21.14 ? 1495 ASN A ND2   1 
ATOM   344   N  N     . LYS A 1 1496 ? 192.874 223.531 254.622 1.00 17.34 ? 1496 LYS A N     1 
ATOM   345   C  CA    . LYS A 1 1496 ? 193.691 222.785 255.574 1.00 15.65 ? 1496 LYS A CA    1 
ATOM   346   C  C     . LYS A 1 1496 ? 195.084 222.527 255.015 1.00 18.71 ? 1496 LYS A C     1 
ATOM   347   O  O     . LYS A 1 1496 ? 196.083 222.699 255.721 1.00 21.95 ? 1496 LYS A O     1 
ATOM   348   C  CB    . LYS A 1 1496 ? 193.010 221.467 255.939 1.00 18.19 ? 1496 LYS A CB    1 
ATOM   349   C  CG    . LYS A 1 1496 ? 193.763 220.640 256.967 1.00 19.28 ? 1496 LYS A CG    1 
ATOM   350   C  CD    . LYS A 1 1496 ? 193.887 221.372 258.294 1.00 21.64 ? 1496 LYS A CD    1 
ATOM   351   C  CE    . LYS A 1 1496 ? 192.533 221.570 258.949 1.00 23.20 ? 1496 LYS A CE    1 
ATOM   352   N  NZ    . LYS A 1 1496 ? 191.944 220.279 259.395 1.00 23.95 ? 1496 LYS A NZ    1 
ATOM   353   N  N     . VAL A 1 1497 ? 195.170 222.125 253.745 1.00 20.93 ? 1497 VAL A N     1 
ATOM   354   C  CA    . VAL A 1 1497 ? 196.473 221.891 253.129 1.00 14.33 ? 1497 VAL A CA    1 
ATOM   355   C  C     . VAL A 1 1497 ? 197.262 223.192 253.043 1.00 13.41 ? 1497 VAL A C     1 
ATOM   356   O  O     . VAL A 1 1497 ? 198.452 223.234 253.373 1.00 14.73 ? 1497 VAL A O     1 
ATOM   357   C  CB    . VAL A 1 1497 ? 196.304 221.238 251.744 1.00 15.55 ? 1497 VAL A CB    1 
ATOM   358   C  CG1   . VAL A 1 1497 ? 197.606 221.286 250.971 1.00 13.01 ? 1497 VAL A CG1   1 
ATOM   359   C  CG2   . VAL A 1 1497 ? 195.830 219.808 251.887 1.00 15.54 ? 1497 VAL A CG2   1 
ATOM   360   N  N     . LYS A 1 1498 ? 196.609 224.278 252.615 1.00 13.88 ? 1498 LYS A N     1 
ATOM   361   C  CA    . LYS A 1 1498 ? 197.295 225.564 252.519 1.00 15.82 ? 1498 LYS A CA    1 
ATOM   362   C  C     . LYS A 1 1498 ? 197.803 226.022 253.880 1.00 15.72 ? 1498 LYS A C     1 
ATOM   363   O  O     . LYS A 1 1498 ? 198.909 226.562 253.987 1.00 16.61 ? 1498 LYS A O     1 
ATOM   364   C  CB    . LYS A 1 1498 ? 196.373 226.627 251.922 1.00 16.07 ? 1498 LYS A CB    1 
ATOM   365   C  CG    . LYS A 1 1498 ? 196.038 226.459 250.450 1.00 16.84 ? 1498 LYS A CG    1 
ATOM   366   C  CD    . LYS A 1 1498 ? 195.009 227.502 250.027 1.00 23.95 ? 1498 LYS A CD    1 
ATOM   367   C  CE    . LYS A 1 1498 ? 193.986 226.953 249.046 1.00 18.30 ? 1498 LYS A CE    1 
ATOM   368   N  NZ    . LYS A 1 1498 ? 194.547 225.909 248.154 1.00 22.93 ? 1498 LYS A NZ    1 
ATOM   369   N  N     . GLU A 1 1499 ? 197.005 225.816 254.930 1.00 16.65 ? 1499 GLU A N     1 
ATOM   370   C  CA    . GLU A 1 1499 ? 197.408 226.254 256.262 1.00 16.38 ? 1499 GLU A CA    1 
ATOM   371   C  C     . GLU A 1 1499 ? 198.678 225.547 256.719 1.00 20.77 ? 1499 GLU A C     1 
ATOM   372   O  O     . GLU A 1 1499 ? 199.590 226.188 257.255 1.00 27.50 ? 1499 GLU A O     1 
ATOM   373   C  CB    . GLU A 1 1499 ? 196.266 226.021 257.251 1.00 15.68 ? 1499 GLU A CB    1 
ATOM   374   C  CG    . GLU A 1 1499 ? 196.456 226.667 258.615 1.00 26.35 ? 1499 GLU A CG    1 
ATOM   375   C  CD    . GLU A 1 1499 ? 197.288 225.823 259.560 1.00 33.58 ? 1499 GLU A CD    1 
ATOM   376   O  OE1   . GLU A 1 1499 ? 197.268 224.583 259.419 1.00 32.69 ? 1499 GLU A OE1   1 
ATOM   377   O  OE2   . GLU A 1 1499 ? 197.955 226.400 260.442 1.00 39.69 ? 1499 GLU A OE2   1 
ATOM   378   N  N     . HIS A 1 1500 ? 198.763 224.232 256.511 1.00 17.29 ? 1500 HIS A N     1 
ATOM   379   C  CA    . HIS A 1 1500 ? 199.977 223.516 256.883 1.00 16.37 ? 1500 HIS A CA    1 
ATOM   380   C  C     . HIS A 1 1500 ? 201.145 223.876 255.973 1.00 19.42 ? 1500 HIS A C     1 
ATOM   381   O  O     . HIS A 1 1500 ? 202.293 223.911 256.430 1.00 18.13 ? 1500 HIS A O     1 
ATOM   382   C  CB    . HIS A 1 1500 ? 199.735 222.006 256.861 1.00 15.95 ? 1500 HIS A CB    1 
ATOM   383   C  CG    . HIS A 1 1500 ? 198.740 221.539 257.877 1.00 21.08 ? 1500 HIS A CG    1 
ATOM   384   N  ND1   . HIS A 1 1500 ? 199.034 221.449 259.219 1.00 24.39 ? 1500 HIS A ND1   1 
ATOM   385   C  CD2   . HIS A 1 1500 ? 197.463 221.110 257.745 1.00 22.83 ? 1500 HIS A CD2   1 
ATOM   386   C  CE1   . HIS A 1 1500 ? 197.980 221.000 259.873 1.00 26.63 ? 1500 HIS A CE1   1 
ATOM   387   N  NE2   . HIS A 1 1500 ? 197.012 220.785 259.001 1.00 23.87 ? 1500 HIS A NE2   1 
ATOM   388   N  N     . ILE A 1 1501 ? 200.878 224.137 254.691 1.00 22.01 ? 1501 ILE A N     1 
ATOM   389   C  CA    . ILE A 1 1501 ? 201.944 224.524 253.772 1.00 16.17 ? 1501 ILE A CA    1 
ATOM   390   C  C     . ILE A 1 1501 ? 202.550 225.857 254.194 1.00 21.88 ? 1501 ILE A C     1 
ATOM   391   O  O     . ILE A 1 1501 ? 203.775 226.031 254.183 1.00 25.84 ? 1501 ILE A O     1 
ATOM   392   C  CB    . ILE A 1 1501 ? 201.414 224.565 252.326 1.00 17.81 ? 1501 ILE A CB    1 
ATOM   393   C  CG1   . ILE A 1 1501 ? 201.190 223.145 251.805 1.00 17.75 ? 1501 ILE A CG1   1 
ATOM   394   C  CG2   . ILE A 1 1501 ? 202.378 225.306 251.412 1.00 15.45 ? 1501 ILE A CG2   1 
ATOM   395   C  CD1   . ILE A 1 1501 ? 200.727 223.081 250.370 1.00 13.37 ? 1501 ILE A CD1   1 
ATOM   396   N  N     . ASN A 1 1502 ? 201.705 226.818 254.574 1.00 23.37 ? 1502 ASN A N     1 
ATOM   397   C  CA    . ASN A 1 1502 ? 202.214 228.088 255.077 1.00 21.43 ? 1502 ASN A CA    1 
ATOM   398   C  C     . ASN A 1 1502 ? 202.993 227.900 256.373 1.00 24.02 ? 1502 ASN A C     1 
ATOM   399   O  O     . ASN A 1 1502 ? 204.068 228.485 256.548 1.00 27.03 ? 1502 ASN A O     1 
ATOM   400   C  CB    . ASN A 1 1502 ? 201.063 229.074 255.285 1.00 18.68 ? 1502 ASN A CB    1 
ATOM   401   C  CG    . ASN A 1 1502 ? 200.240 229.278 254.032 1.00 24.55 ? 1502 ASN A CG    1 
ATOM   402   O  OD1   . ASN A 1 1502 ? 200.756 229.207 252.919 1.00 25.26 ? 1502 ASN A OD1   1 
ATOM   403   N  ND2   . ASN A 1 1502 ? 198.948 229.533 254.209 1.00 22.56 ? 1502 ASN A ND2   1 
ATOM   404   N  N     . SER A 1 1503 ? 202.469 227.083 257.292 1.00 19.19 ? 1503 SER A N     1 
ATOM   405   C  CA    . SER A 1 1503 ? 203.145 226.876 258.569 1.00 20.11 ? 1503 SER A CA    1 
ATOM   406   C  C     . SER A 1 1503 ? 204.505 226.218 258.374 1.00 26.76 ? 1503 SER A C     1 
ATOM   407   O  O     . SER A 1 1503 ? 205.482 226.586 259.038 1.00 33.17 ? 1503 SER A O     1 
ATOM   408   C  CB    . SER A 1 1503 ? 202.272 226.037 259.501 1.00 19.62 ? 1503 SER A CB    1 
ATOM   409   O  OG    . SER A 1 1503 ? 202.155 224.707 259.032 1.00 28.75 ? 1503 SER A OG    1 
ATOM   410   N  N     . VAL A 1 1504 ? 204.588 225.238 257.472 1.00 26.60 ? 1504 VAL A N     1 
ATOM   411   C  CA    . VAL A 1 1504 ? 205.876 224.627 257.156 1.00 26.03 ? 1504 VAL A CA    1 
ATOM   412   C  C     . VAL A 1 1504 ? 206.814 225.656 256.538 1.00 26.05 ? 1504 VAL A C     1 
ATOM   413   O  O     . VAL A 1 1504 ? 208.002 225.716 256.872 1.00 30.49 ? 1504 VAL A O     1 
ATOM   414   C  CB    . VAL A 1 1504 ? 205.679 223.409 256.233 1.00 22.86 ? 1504 VAL A CB    1 
ATOM   415   C  CG1   . VAL A 1 1504 ? 206.989 223.019 255.570 1.00 24.11 ? 1504 VAL A CG1   1 
ATOM   416   C  CG2   . VAL A 1 1504 ? 205.113 222.240 257.017 1.00 20.23 ? 1504 VAL A CG2   1 
ATOM   417   N  N     . SER A 1 1505 ? 206.299 226.478 255.622 1.00 24.67 ? 1505 SER A N     1 
ATOM   418   C  CA    . SER A 1 1505 ? 207.123 227.524 255.023 1.00 27.10 ? 1505 SER A CA    1 
ATOM   419   C  C     . SER A 1 1505 ? 207.540 228.560 256.060 1.00 26.74 ? 1505 SER A C     1 
ATOM   420   O  O     . SER A 1 1505 ? 208.696 228.999 256.086 1.00 32.01 ? 1505 SER A O     1 
ATOM   421   C  CB    . SER A 1 1505 ? 206.372 228.188 253.869 1.00 20.19 ? 1505 SER A CB    1 
ATOM   422   O  OG    . SER A 1 1505 ? 206.191 227.284 252.796 1.00 29.75 ? 1505 SER A OG    1 
ATOM   423   N  N     . ALA A 1 1506 ? 206.608 228.960 256.928 1.00 27.60 ? 1506 ALA A N     1 
ATOM   424   C  CA    . ALA A 1 1506 ? 206.909 229.976 257.931 1.00 27.27 ? 1506 ALA A CA    1 
ATOM   425   C  C     . ALA A 1 1506 ? 207.917 229.497 258.963 1.00 27.89 ? 1506 ALA A C     1 
ATOM   426   O  O     . ALA A 1 1506 ? 208.733 230.296 259.431 1.00 35.10 ? 1506 ALA A O     1 
ATOM   427   C  CB    . ALA A 1 1506 ? 205.626 230.422 258.635 1.00 24.23 ? 1506 ALA A CB    1 
ATOM   428   N  N     . MET A 1 1507 ? 207.879 228.214 259.326 1.00 27.58 ? 1507 MET A N     1 
ATOM   429   C  CA    . MET A 1 1507 ? 208.780 227.708 260.356 1.00 30.16 ? 1507 MET A CA    1 
ATOM   430   C  C     . MET A 1 1507 ? 210.212 227.582 259.851 1.00 33.07 ? 1507 MET A C     1 
ATOM   431   O  O     . MET A 1 1507 ? 211.130 227.375 260.650 1.00 34.13 ? 1507 MET A O     1 
ATOM   432   C  CB    . MET A 1 1507 ? 208.266 226.368 260.881 1.00 27.29 ? 1507 MET A CB    1 
ATOM   433   C  CG    . MET A 1 1507 ? 208.384 225.228 259.894 1.00 25.56 ? 1507 MET A CG    1 
ATOM   434   S  SD    . MET A 1 1507 ? 208.427 223.605 260.669 1.00 53.56 ? 1507 MET A SD    1 
ATOM   435   C  CE    . MET A 1 1507 ? 206.680 223.206 260.653 1.00 30.51 ? 1507 MET A CE    1 
ATOM   436   N  N     . LYS A 1 1508 ? 210.427 227.694 258.537 1.00 28.53 ? 1508 LYS A N     1 
ATOM   437   C  CA    . LYS A 1 1508 ? 211.795 227.740 258.026 1.00 28.50 ? 1508 LYS A CA    1 
ATOM   438   C  C     . LYS A 1 1508 ? 212.508 229.015 258.460 1.00 32.57 ? 1508 LYS A C     1 
ATOM   439   O  O     . LYS A 1 1508 ? 213.730 229.010 258.649 1.00 32.96 ? 1508 LYS A O     1 
ATOM   440   C  CB    . LYS A 1 1508 ? 211.805 227.619 256.503 1.00 29.08 ? 1508 LYS A CB    1 
ATOM   441   C  CG    . LYS A 1 1508 ? 211.011 226.445 255.965 1.00 30.77 ? 1508 LYS A CG    1 
ATOM   442   C  CD    . LYS A 1 1508 ? 210.883 226.509 254.453 1.00 28.69 ? 1508 LYS A CD    1 
ATOM   443   C  CE    . LYS A 1 1508 ? 209.992 225.395 253.930 1.00 31.74 ? 1508 LYS A CE    1 
ATOM   444   N  NZ    . LYS A 1 1508 ? 209.799 225.488 252.456 1.00 35.82 ? 1508 LYS A NZ    1 
ATOM   445   N  N     . LEU A 1 1509 ? 211.763 230.111 258.621 1.00 33.25 ? 1509 LEU A N     1 
ATOM   446   C  CA    . LEU A 1 1509 ? 212.364 231.366 259.061 1.00 34.76 ? 1509 LEU A CA    1 
ATOM   447   C  C     . LEU A 1 1509 ? 212.891 231.267 260.486 1.00 35.22 ? 1509 LEU A C     1 
ATOM   448   O  O     . LEU A 1 1509 ? 213.834 231.982 260.845 1.00 35.53 ? 1509 LEU A O     1 
ATOM   449   C  CB    . LEU A 1 1509 ? 211.345 232.499 258.953 1.00 27.17 ? 1509 LEU A CB    1 
ATOM   450   C  CG    . LEU A 1 1509 ? 210.540 232.570 257.654 1.00 34.56 ? 1509 LEU A CG    1 
ATOM   451   C  CD1   . LEU A 1 1509 ? 209.535 233.708 257.711 1.00 30.97 ? 1509 LEU A CD1   1 
ATOM   452   C  CD2   . LEU A 1 1509 ? 211.462 232.729 256.455 1.00 32.16 ? 1509 LEU A CD2   1 
ATOM   453   N  N     . SER A 1 1510 ? 212.298 230.408 261.304 1.00 33.88 ? 1510 SER A N     1 
ATOM   454   C  CA    . SER A 1 1510 ? 212.742 230.264 262.681 1.00 33.58 ? 1510 SER A CA    1 
ATOM   455   C  C     . SER A 1 1510 ? 214.163 229.710 262.717 1.00 36.02 ? 1510 SER A C     1 
ATOM   456   O  O     . SER A 1 1510 ? 214.504 228.817 261.930 1.00 35.85 ? 1510 SER A O     1 
ATOM   457   C  CB    . SER A 1 1510 ? 211.796 229.345 263.454 1.00 32.28 ? 1510 SER A CB    1 
ATOM   458   O  OG    . SER A 1 1510 ? 211.844 228.024 262.944 1.00 37.12 ? 1510 SER A OG    1 
ATOM   459   N  N     . PRO A 1 1511 ? 215.023 230.223 263.600 1.00 39.57 ? 1511 PRO A N     1 
ATOM   460   C  CA    . PRO A 1 1511 ? 216.402 229.712 263.659 1.00 33.73 ? 1511 PRO A CA    1 
ATOM   461   C  C     . PRO A 1 1511 ? 216.498 228.249 264.054 1.00 33.71 ? 1511 PRO A C     1 
ATOM   462   O  O     . PRO A 1 1511 ? 217.474 227.582 263.692 1.00 34.27 ? 1511 PRO A O     1 
ATOM   463   C  CB    . PRO A 1 1511 ? 217.066 230.625 264.698 1.00 33.68 ? 1511 PRO A CB    1 
ATOM   464   C  CG    . PRO A 1 1511 ? 215.937 231.114 265.542 1.00 35.73 ? 1511 PRO A CG    1 
ATOM   465   C  CD    . PRO A 1 1511 ? 214.781 231.277 264.600 1.00 35.16 ? 1511 PRO A CD    1 
ATOM   466   N  N     . TYR A 1 1512 ? 215.513 227.722 264.781 1.00 31.33 ? 1512 TYR A N     1 
ATOM   467   C  CA    . TYR A 1 1512 ? 215.540 226.339 265.244 1.00 31.89 ? 1512 TYR A CA    1 
ATOM   468   C  C     . TYR A 1 1512 ? 215.039 225.352 264.194 1.00 33.39 ? 1512 TYR A C     1 
ATOM   469   O  O     . TYR A 1 1512 ? 214.675 224.222 264.542 1.00 34.01 ? 1512 TYR A O     1 
ATOM   470   C  CB    . TYR A 1 1512 ? 214.720 226.196 266.527 1.00 33.09 ? 1512 TYR A CB    1 
ATOM   471   C  CG    . TYR A 1 1512 ? 215.058 227.216 267.594 1.00 32.65 ? 1512 TYR A CG    1 
ATOM   472   C  CD1   . TYR A 1 1512 ? 216.370 227.628 267.802 1.00 37.51 ? 1512 TYR A CD1   1 
ATOM   473   C  CD2   . TYR A 1 1512 ? 214.065 227.768 268.392 1.00 33.98 ? 1512 TYR A CD2   1 
ATOM   474   C  CE1   . TYR A 1 1512 ? 216.680 228.558 268.773 1.00 36.98 ? 1512 TYR A CE1   1 
ATOM   475   C  CE2   . TYR A 1 1512 ? 214.366 228.699 269.367 1.00 34.76 ? 1512 TYR A CE2   1 
ATOM   476   C  CZ    . TYR A 1 1512 ? 215.675 229.090 269.553 1.00 37.63 ? 1512 TYR A CZ    1 
ATOM   477   O  OH    . TYR A 1 1512 ? 215.979 230.018 270.523 1.00 41.90 ? 1512 TYR A OH    1 
ATOM   478   N  N     . TYR A 1 1513 ? 215.016 225.756 262.924 1.00 33.29 ? 1513 TYR A N     1 
ATOM   479   C  CA    . TYR A 1 1513 ? 214.502 224.911 261.856 1.00 28.07 ? 1513 TYR A CA    1 
ATOM   480   C  C     . TYR A 1 1513 ? 215.488 223.829 261.430 1.00 32.72 ? 1513 TYR A C     1 
ATOM   481   O  O     . TYR A 1 1513 ? 215.084 222.868 260.766 1.00 36.18 ? 1513 TYR A O     1 
ATOM   482   C  CB    . TYR A 1 1513 ? 214.123 225.787 260.657 1.00 27.16 ? 1513 TYR A CB    1 
ATOM   483   C  CG    . TYR A 1 1513 ? 213.650 225.033 259.434 1.00 31.72 ? 1513 TYR A CG    1 
ATOM   484   C  CD1   . TYR A 1 1513 ? 212.354 224.540 259.360 1.00 31.47 ? 1513 TYR A CD1   1 
ATOM   485   C  CD2   . TYR A 1 1513 ? 214.495 224.825 258.352 1.00 28.99 ? 1513 TYR A CD2   1 
ATOM   486   C  CE1   . TYR A 1 1513 ? 211.915 223.854 258.245 1.00 32.58 ? 1513 TYR A CE1   1 
ATOM   487   C  CE2   . TYR A 1 1513 ? 214.065 224.140 257.233 1.00 33.34 ? 1513 TYR A CE2   1 
ATOM   488   C  CZ    . TYR A 1 1513 ? 212.776 223.656 257.184 1.00 36.05 ? 1513 TYR A CZ    1 
ATOM   489   O  OH    . TYR A 1 1513 ? 212.344 222.975 256.073 1.00 36.12 ? 1513 TYR A OH    1 
ATOM   490   N  N     . LYS A 1 1514 ? 216.762 223.950 261.813 1.00 33.24 ? 1514 LYS A N     1 
ATOM   491   C  CA    . LYS A 1 1514 ? 217.775 223.011 261.338 1.00 30.67 ? 1514 LYS A CA    1 
ATOM   492   C  C     . LYS A 1 1514 ? 217.541 221.604 261.879 1.00 31.38 ? 1514 LYS A C     1 
ATOM   493   O  O     . LYS A 1 1514 ? 217.741 220.619 261.160 1.00 31.15 ? 1514 LYS A O     1 
ATOM   494   C  CB    . LYS A 1 1514 ? 219.168 223.508 261.721 1.00 26.75 ? 1514 LYS A CB    1 
ATOM   495   C  CG    . LYS A 1 1514 ? 220.303 222.668 261.157 1.00 29.41 ? 1514 LYS A CG    1 
ATOM   496   C  CD    . LYS A 1 1514 ? 220.178 222.509 259.649 1.00 32.02 ? 1514 LYS A CD    1 
ATOM   497   C  CE    . LYS A 1 1514 ? 221.267 221.602 259.100 1.00 33.10 ? 1514 LYS A CE    1 
ATOM   498   N  NZ    . LYS A 1 1514 ? 221.156 221.426 257.625 1.00 29.50 ? 1514 LYS A NZ    1 
ATOM   499   N  N     . VAL A 1 1515 ? 217.127 221.488 263.142 1.00 28.70 ? 1515 VAL A N     1 
ATOM   500   C  CA    . VAL A 1 1515 ? 216.982 220.169 263.754 1.00 29.08 ? 1515 VAL A CA    1 
ATOM   501   C  C     . VAL A 1 1515 ? 215.842 219.393 263.103 1.00 32.56 ? 1515 VAL A C     1 
ATOM   502   O  O     . VAL A 1 1515 ? 215.923 218.171 262.935 1.00 30.88 ? 1515 VAL A O     1 
ATOM   503   C  CB    . VAL A 1 1515 ? 216.790 220.304 265.277 1.00 30.50 ? 1515 VAL A CB    1 
ATOM   504   C  CG1   . VAL A 1 1515 ? 215.562 221.148 265.601 1.00 28.55 ? 1515 VAL A CG1   1 
ATOM   505   C  CG2   . VAL A 1 1515 ? 216.693 218.934 265.929 1.00 27.41 ? 1515 VAL A CG2   1 
ATOM   506   N  N     . PHE A 1 1516 ? 214.770 220.086 262.718 1.00 31.47 ? 1516 PHE A N     1 
ATOM   507   C  CA    . PHE A 1 1516 ? 213.596 219.456 262.128 1.00 26.65 ? 1516 PHE A CA    1 
ATOM   508   C  C     . PHE A 1 1516 ? 213.486 219.727 260.632 1.00 30.22 ? 1516 PHE A C     1 
ATOM   509   O  O     . PHE A 1 1516 ? 212.390 219.641 260.068 1.00 29.82 ? 1516 PHE A O     1 
ATOM   510   C  CB    . PHE A 1 1516 ? 212.332 219.929 262.844 1.00 28.61 ? 1516 PHE A CB    1 
ATOM   511   C  CG    . PHE A 1 1516 ? 212.371 219.740 264.332 1.00 29.63 ? 1516 PHE A CG    1 
ATOM   512   C  CD1   . PHE A 1 1516 ? 212.834 218.555 264.879 1.00 27.99 ? 1516 PHE A CD1   1 
ATOM   513   C  CD2   . PHE A 1 1516 ? 211.950 220.748 265.183 1.00 28.11 ? 1516 PHE A CD2   1 
ATOM   514   C  CE1   . PHE A 1 1516 ? 212.872 218.379 266.250 1.00 31.24 ? 1516 PHE A CE1   1 
ATOM   515   C  CE2   . PHE A 1 1516 ? 211.986 220.578 266.552 1.00 30.37 ? 1516 PHE A CE2   1 
ATOM   516   C  CZ    . PHE A 1 1516 ? 212.448 219.391 267.087 1.00 33.57 ? 1516 PHE A CZ    1 
ATOM   517   N  N     . GLU A 1 1517 ? 214.603 220.056 259.980 1.00 33.74 ? 1517 GLU A N     1 
ATOM   518   C  CA    . GLU A 1 1517 ? 214.561 220.423 258.568 1.00 30.12 ? 1517 GLU A CA    1 
ATOM   519   C  C     . GLU A 1 1517 ? 214.103 219.257 257.702 1.00 22.85 ? 1517 GLU A C     1 
ATOM   520   O  O     . GLU A 1 1517 ? 213.244 219.419 256.829 1.00 27.06 ? 1517 GLU A O     1 
ATOM   521   C  CB    . GLU A 1 1517 ? 215.935 220.920 258.117 1.00 30.75 ? 1517 GLU A CB    1 
ATOM   522   C  CG    . GLU A 1 1517 ? 216.024 221.249 256.637 1.00 36.80 ? 1517 GLU A CG    1 
ATOM   523   C  CD    . GLU A 1 1517 ? 217.324 221.933 256.271 1.00 42.87 ? 1517 GLU A CD    1 
ATOM   524   O  OE1   . GLU A 1 1517 ? 218.398 221.349 256.532 1.00 40.14 ? 1517 GLU A OE1   1 
ATOM   525   O  OE2   . GLU A 1 1517 ? 217.274 223.052 255.718 1.00 41.55 ? 1517 GLU A OE2   1 
ATOM   526   N  N     . GLU A 1 1518 ? 214.664 218.067 257.932 1.00 25.47 ? 1518 GLU A N     1 
ATOM   527   C  CA    . GLU A 1 1518 ? 214.327 216.922 257.091 1.00 28.74 ? 1518 GLU A CA    1 
ATOM   528   C  C     . GLU A 1 1518 ? 212.863 216.529 257.247 1.00 27.18 ? 1518 GLU A C     1 
ATOM   529   O  O     . GLU A 1 1518 ? 212.180 216.244 256.255 1.00 27.18 ? 1518 GLU A O     1 
ATOM   530   C  CB    . GLU A 1 1518 ? 215.239 215.741 257.420 1.00 21.77 ? 1518 GLU A CB    1 
ATOM   531   C  CG    . GLU A 1 1518 ? 214.976 214.502 256.577 1.00 26.03 ? 1518 GLU A CG    1 
ATOM   532   C  CD    . GLU A 1 1518 ? 215.620 213.256 257.151 1.00 37.53 ? 1518 GLU A CD    1 
ATOM   533   O  OE1   . GLU A 1 1518 ? 215.304 212.897 258.304 1.00 33.74 ? 1518 GLU A OE1   1 
ATOM   534   O  OE2   . GLU A 1 1518 ? 216.446 212.635 256.449 1.00 41.61 ? 1518 GLU A OE2   1 
ATOM   535   N  N     . ASP A 1 1519 ? 212.363 216.506 258.483 1.00 28.61 ? 1519 ASP A N     1 
ATOM   536   C  CA    . ASP A 1 1519 ? 210.969 216.138 258.709 1.00 23.74 ? 1519 ASP A CA    1 
ATOM   537   C  C     . ASP A 1 1519 ? 210.020 217.172 258.113 1.00 24.84 ? 1519 ASP A C     1 
ATOM   538   O  O     . ASP A 1 1519 ? 208.992 216.814 257.528 1.00 26.92 ? 1519 ASP A O     1 
ATOM   539   C  CB    . ASP A 1 1519 ? 210.716 215.957 260.204 1.00 19.53 ? 1519 ASP A CB    1 
ATOM   540   C  CG    . ASP A 1 1519 ? 209.443 215.185 260.490 1.00 33.87 ? 1519 ASP A CG    1 
ATOM   541   O  OD1   . ASP A 1 1519 ? 209.219 214.143 259.840 1.00 35.01 ? 1519 ASP A OD1   1 
ATOM   542   O  OD2   . ASP A 1 1519 ? 208.676 215.607 261.380 1.00 35.81 ? 1519 ASP A OD2   1 
ATOM   543   N  N     . ALA A 1 1520 ? 210.345 218.458 258.257 1.00 24.82 ? 1520 ALA A N     1 
ATOM   544   C  CA    . ALA A 1 1520 ? 209.525 219.497 257.643 1.00 21.70 ? 1520 ALA A CA    1 
ATOM   545   C  C     . ALA A 1 1520 ? 209.562 219.408 256.121 1.00 22.71 ? 1520 ALA A C     1 
ATOM   546   O  O     . ALA A 1 1520 ? 208.533 219.575 255.460 1.00 24.86 ? 1520 ALA A O     1 
ATOM   547   C  CB    . ALA A 1 1520 ? 209.984 220.876 258.114 1.00 18.51 ? 1520 ALA A CB    1 
ATOM   548   N  N     . LEU A 1 1521 ? 210.741 219.150 255.549 1.00 24.74 ? 1521 LEU A N     1 
ATOM   549   C  CA    . LEU A 1 1521 ? 210.840 218.998 254.101 1.00 21.46 ? 1521 LEU A CA    1 
ATOM   550   C  C     . LEU A 1 1521 ? 210.077 217.775 253.613 1.00 20.52 ? 1521 LEU A C     1 
ATOM   551   O  O     . LEU A 1 1521 ? 209.542 217.783 252.500 1.00 22.09 ? 1521 LEU A O     1 
ATOM   552   C  CB    . LEU A 1 1521 ? 212.304 218.911 253.674 1.00 22.69 ? 1521 LEU A CB    1 
ATOM   553   C  CG    . LEU A 1 1521 ? 213.096 220.217 253.687 1.00 23.11 ? 1521 LEU A CG    1 
ATOM   554   C  CD1   . LEU A 1 1521 ? 214.535 219.968 253.272 1.00 21.57 ? 1521 LEU A CD1   1 
ATOM   555   C  CD2   . LEU A 1 1521 ? 212.442 221.248 252.784 1.00 20.95 ? 1521 LEU A CD2   1 
ATOM   556   N  N     . SER A 1 1522 ? 210.027 216.717 254.424 1.00 17.37 ? 1522 SER A N     1 
ATOM   557   C  CA    . SER A 1 1522 ? 209.203 215.565 254.079 1.00 20.82 ? 1522 SER A CA    1 
ATOM   558   C  C     . SER A 1 1522 ? 207.729 215.946 254.024 1.00 19.94 ? 1522 SER A C     1 
ATOM   559   O  O     . SER A 1 1522 ? 206.999 215.506 253.130 1.00 18.55 ? 1522 SER A O     1 
ATOM   560   C  CB    . SER A 1 1522 ? 209.430 214.438 255.085 1.00 21.00 ? 1522 SER A CB    1 
ATOM   561   O  OG    . SER A 1 1522 ? 208.556 214.564 256.193 1.00 25.19 ? 1522 SER A OG    1 
ATOM   562   N  N     . TRP A 1 1523 ? 207.276 216.766 254.975 1.00 17.48 ? 1523 TRP A N     1 
ATOM   563   C  CA    . TRP A 1 1523 ? 205.878 217.177 254.988 1.00 18.82 ? 1523 TRP A CA    1 
ATOM   564   C  C     . TRP A 1 1523 ? 205.572 218.171 253.877 1.00 20.59 ? 1523 TRP A C     1 
ATOM   565   O  O     . TRP A 1 1523 ? 204.463 218.162 253.332 1.00 23.36 ? 1523 TRP A O     1 
ATOM   566   C  CB    . TRP A 1 1523 ? 205.514 217.760 256.352 1.00 15.19 ? 1523 TRP A CB    1 
ATOM   567   C  CG    . TRP A 1 1523 ? 205.124 216.705 257.324 1.00 21.84 ? 1523 TRP A CG    1 
ATOM   568   C  CD1   . TRP A 1 1523 ? 205.872 216.225 258.357 1.00 23.91 ? 1523 TRP A CD1   1 
ATOM   569   C  CD2   . TRP A 1 1523 ? 203.899 215.967 257.337 1.00 24.20 ? 1523 TRP A CD2   1 
ATOM   570   N  NE1   . TRP A 1 1523 ? 205.184 215.243 259.022 1.00 27.31 ? 1523 TRP A NE1   1 
ATOM   571   C  CE2   . TRP A 1 1523 ? 203.968 215.065 258.416 1.00 24.98 ? 1523 TRP A CE2   1 
ATOM   572   C  CE3   . TRP A 1 1523 ? 202.747 215.986 256.545 1.00 18.74 ? 1523 TRP A CE3   1 
ATOM   573   C  CZ2   . TRP A 1 1523 ? 202.931 214.191 258.723 1.00 22.52 ? 1523 TRP A CZ2   1 
ATOM   574   C  CZ3   . TRP A 1 1523 ? 201.719 215.119 256.852 1.00 18.94 ? 1523 TRP A CZ3   1 
ATOM   575   C  CH2   . TRP A 1 1523 ? 201.818 214.234 257.932 1.00 20.00 ? 1523 TRP A CH2   1 
ATOM   576   N  N     . GLU A 1 1524 ? 206.534 219.027 253.525 1.00 18.31 ? 1524 GLU A N     1 
ATOM   577   C  CA    . GLU A 1 1524 ? 206.338 219.931 252.397 1.00 15.60 ? 1524 GLU A CA    1 
ATOM   578   C  C     . GLU A 1 1524 ? 206.106 219.148 251.111 1.00 13.24 ? 1524 GLU A C     1 
ATOM   579   O  O     . GLU A 1 1524 ? 205.256 219.519 250.294 1.00 14.44 ? 1524 GLU A O     1 
ATOM   580   C  CB    . GLU A 1 1524 ? 207.545 220.858 252.251 1.00 19.96 ? 1524 GLU A CB    1 
ATOM   581   C  CG    . GLU A 1 1524 ? 207.527 221.711 250.993 1.00 21.81 ? 1524 GLU A CG    1 
ATOM   582   C  CD    . GLU A 1 1524 ? 208.883 222.306 250.675 1.00 28.07 ? 1524 GLU A CD    1 
ATOM   583   O  OE1   . GLU A 1 1524 ? 209.507 221.873 249.684 1.00 25.76 ? 1524 GLU A OE1   1 
ATOM   584   O  OE2   . GLU A 1 1524 ? 209.326 223.208 251.418 1.00 25.71 ? 1524 GLU A OE2   1 
ATOM   585   N  N     . ASP A 1 1525 ? 206.854 218.061 250.915 1.00 17.36 ? 1525 ASP A N     1 
ATOM   586   C  CA    . ASP A 1 1525 ? 206.636 217.211 249.753 1.00 14.17 ? 1525 ASP A CA    1 
ATOM   587   C  C     . ASP A 1 1525 ? 205.261 216.552 249.793 1.00 16.55 ? 1525 ASP A C     1 
ATOM   588   O  O     . ASP A 1 1525 ? 204.551 216.522 248.782 1.00 16.46 ? 1525 ASP A O     1 
ATOM   589   C  CB    . ASP A 1 1525 ? 207.735 216.155 249.667 1.00 16.01 ? 1525 ASP A CB    1 
ATOM   590   C  CG    . ASP A 1 1525 ? 207.647 215.326 248.407 1.00 24.99 ? 1525 ASP A CG    1 
ATOM   591   O  OD1   . ASP A 1 1525 ? 207.999 215.847 247.325 1.00 28.25 ? 1525 ASP A OD1   1 
ATOM   592   O  OD2   . ASP A 1 1525 ? 207.233 214.153 248.494 1.00 26.79 ? 1525 ASP A OD2   1 
ATOM   593   N  N     . LYS A 1 1526 ? 204.870 216.017 250.951 1.00 15.25 ? 1526 LYS A N     1 
ATOM   594   C  CA    . LYS A 1 1526 ? 203.578 215.344 251.055 1.00 11.45 ? 1526 LYS A CA    1 
ATOM   595   C  C     . LYS A 1 1526 ? 202.426 216.322 250.871 1.00 14.18 ? 1526 LYS A C     1 
ATOM   596   O  O     . LYS A 1 1526 ? 201.472 216.040 250.136 1.00 18.24 ? 1526 LYS A O     1 
ATOM   597   C  CB    . LYS A 1 1526 ? 203.465 214.620 252.400 1.00 14.52 ? 1526 LYS A CB    1 
ATOM   598   C  CG    . LYS A 1 1526 ? 204.421 213.453 252.554 1.00 15.76 ? 1526 LYS A CG    1 
ATOM   599   C  CD    . LYS A 1 1526 ? 204.159 212.672 253.829 1.00 14.10 ? 1526 LYS A CD    1 
ATOM   600   C  CE    . LYS A 1 1526 ? 204.635 213.431 255.052 1.00 21.22 ? 1526 LYS A CE    1 
ATOM   601   N  NZ    . LYS A 1 1526 ? 204.487 212.634 256.300 1.00 25.79 ? 1526 LYS A NZ    1 
ATOM   602   N  N     . LEU A 1 1527 ? 202.499 217.486 251.521 1.00 10.40 ? 1527 LEU A N     1 
ATOM   603   C  CA    . LEU A 1 1527 ? 201.432 218.472 251.384 1.00 10.88 ? 1527 LEU A CA    1 
ATOM   604   C  C     . LEU A 1 1527 ? 201.337 218.986 249.954 1.00 12.44 ? 1527 LEU A C     1 
ATOM   605   O  O     . LEU A 1 1527 ? 200.235 219.213 249.441 1.00 12.50 ? 1527 LEU A O     1 
ATOM   606   C  CB    . LEU A 1 1527 ? 201.655 219.628 252.356 1.00 13.84 ? 1527 LEU A CB    1 
ATOM   607   C  CG    . LEU A 1 1527 ? 201.506 219.318 253.846 1.00 11.76 ? 1527 LEU A CG    1 
ATOM   608   C  CD1   . LEU A 1 1527 ? 202.314 220.304 254.677 1.00 17.59 ? 1527 LEU A CD1   1 
ATOM   609   C  CD2   . LEU A 1 1527 ? 200.047 219.335 254.258 1.00 14.74 ? 1527 LEU A CD2   1 
ATOM   610   N  N     . ASN A 1 1528 ? 202.481 219.183 249.297 1.00 14.13 ? 1528 ASN A N     1 
ATOM   611   C  CA    . ASN A 1 1528 ? 202.465 219.599 247.898 1.00 9.47  ? 1528 ASN A CA    1 
ATOM   612   C  C     . ASN A 1 1528 ? 201.861 218.524 247.005 1.00 10.44 ? 1528 ASN A C     1 
ATOM   613   O  O     . ASN A 1 1528 ? 201.178 218.846 246.025 1.00 10.79 ? 1528 ASN A O     1 
ATOM   614   C  CB    . ASN A 1 1528 ? 203.877 219.941 247.434 1.00 11.99 ? 1528 ASN A CB    1 
ATOM   615   C  CG    . ASN A 1 1528 ? 204.280 221.353 247.792 1.00 10.33 ? 1528 ASN A CG    1 
ATOM   616   O  OD1   . ASN A 1 1528 ? 203.465 222.272 247.759 1.00 17.74 ? 1528 ASN A OD1   1 
ATOM   617   N  ND2   . ASN A 1 1528 ? 205.548 221.535 248.137 1.00 12.43 ? 1528 ASN A ND2   1 
ATOM   618   N  N     . ARG A 1 1529 ? 202.106 217.252 247.322 1.00 10.26 ? 1529 ARG A N     1 
ATOM   619   C  CA    . ARG A 1 1529 ? 201.526 216.165 246.540 1.00 8.91  ? 1529 ARG A CA    1 
ATOM   620   C  C     . ARG A 1 1529 ? 200.020 216.072 246.753 1.00 9.16  ? 1529 ARG A C     1 
ATOM   621   O  O     . ARG A 1 1529 ? 199.278 215.741 245.822 1.00 12.26 ? 1529 ARG A O     1 
ATOM   622   C  CB    . ARG A 1 1529 ? 202.211 214.846 246.897 1.00 10.19 ? 1529 ARG A CB    1 
ATOM   623   C  CG    . ARG A 1 1529 ? 203.543 214.651 246.201 1.00 10.35 ? 1529 ARG A CG    1 
ATOM   624   C  CD    . ARG A 1 1529 ? 204.400 213.601 246.886 1.00 12.03 ? 1529 ARG A CD    1 
ATOM   625   N  NE    . ARG A 1 1529 ? 203.679 212.354 247.109 1.00 14.92 ? 1529 ARG A NE    1 
ATOM   626   C  CZ    . ARG A 1 1529 ? 203.601 211.732 248.277 1.00 16.49 ? 1529 ARG A CZ    1 
ATOM   627   N  NH1   . ARG A 1 1529 ? 204.190 212.218 249.358 1.00 13.39 ? 1529 ARG A NH1   1 
ATOM   628   N  NH2   . ARG A 1 1529 ? 202.919 210.595 248.363 1.00 19.26 ? 1529 ARG A NH2   1 
ATOM   629   N  N     . ILE A 1 1530 ? 199.553 216.358 247.970 1.00 10.81 ? 1530 ILE A N     1 
ATOM   630   C  CA    . ILE A 1 1530 ? 198.116 216.392 248.230 1.00 7.03  ? 1530 ILE A CA    1 
ATOM   631   C  C     . ILE A 1 1530 ? 197.455 217.496 247.415 1.00 10.18 ? 1530 ILE A C     1 
ATOM   632   O  O     . ILE A 1 1530 ? 196.370 217.308 246.852 1.00 16.30 ? 1530 ILE A O     1 
ATOM   633   C  CB    . ILE A 1 1530 ? 197.845 216.560 249.737 1.00 10.65 ? 1530 ILE A CB    1 
ATOM   634   C  CG1   . ILE A 1 1530 ? 198.444 215.396 250.525 1.00 13.21 ? 1530 ILE A CG1   1 
ATOM   635   C  CG2   . ILE A 1 1530 ? 196.353 216.662 250.007 1.00 10.42 ? 1530 ILE A CG2   1 
ATOM   636   C  CD1   . ILE A 1 1530 ? 198.241 215.502 252.019 1.00 12.56 ? 1530 ILE A CD1   1 
ATOM   637   N  N     . MET A 1 1531 ? 198.095 218.666 247.344 1.00 9.69  ? 1531 MET A N     1 
ATOM   638   C  CA    . MET A 1 1531 ? 197.556 219.756 246.537 1.00 7.52  ? 1531 MET A CA    1 
ATOM   639   C  C     . MET A 1 1531 ? 197.482 219.380 245.063 1.00 8.87  ? 1531 MET A C     1 
ATOM   640   O  O     . MET A 1 1531 ? 196.470 219.633 244.403 1.00 16.22 ? 1531 MET A O     1 
ATOM   641   C  CB    . MET A 1 1531 ? 198.403 221.016 246.720 1.00 7.85  ? 1531 MET A CB    1 
ATOM   642   C  CG    . MET A 1 1531 ? 197.779 222.273 246.133 1.00 12.99 ? 1531 MET A CG    1 
ATOM   643   S  SD    . MET A 1 1531 ? 196.224 222.755 246.901 1.00 28.89 ? 1531 MET A SD    1 
ATOM   644   C  CE    . MET A 1 1531 ? 196.826 223.588 248.363 1.00 14.22 ? 1531 MET A CE    1 
ATOM   645   N  N     . ALA A 1 1532 ? 198.542 218.767 244.532 1.00 8.14  ? 1532 ALA A N     1 
ATOM   646   C  CA    . ALA A 1 1532 ? 198.579 218.468 243.105 1.00 6.82  ? 1532 ALA A CA    1 
ATOM   647   C  C     . ALA A 1 1532 ? 197.569 217.396 242.720 1.00 9.18  ? 1532 ALA A C     1 
ATOM   648   O  O     . ALA A 1 1532 ? 197.118 217.361 241.569 1.00 17.27 ? 1532 ALA A O     1 
ATOM   649   C  CB    . ALA A 1 1532 ? 199.990 218.045 242.696 1.00 9.67  ? 1532 ALA A CB    1 
ATOM   650   N  N     . LEU A 1 1533 ? 197.198 216.522 243.655 1.00 5.75  ? 1533 LEU A N     1 
ATOM   651   C  CA    . LEU A 1 1533 ? 196.265 215.447 243.335 1.00 8.03  ? 1533 LEU A CA    1 
ATOM   652   C  C     . LEU A 1 1533 ? 194.821 215.930 243.354 1.00 9.11  ? 1533 LEU A C     1 
ATOM   653   O  O     . LEU A 1 1533 ? 194.098 215.788 242.362 1.00 11.78 ? 1533 LEU A O     1 
ATOM   654   C  CB    . LEU A 1 1533 ? 196.450 214.282 244.309 1.00 9.61  ? 1533 LEU A CB    1 
ATOM   655   C  CG    . LEU A 1 1533 ? 195.501 213.095 244.124 1.00 9.12  ? 1533 LEU A CG    1 
ATOM   656   C  CD1   . LEU A 1 1533 ? 195.758 212.388 242.802 1.00 5.85  ? 1533 LEU A CD1   1 
ATOM   657   C  CD2   . LEU A 1 1533 ? 195.624 212.124 245.285 1.00 8.62  ? 1533 LEU A CD2   1 
ATOM   658   N  N     . PHE A 1 1534 ? 194.386 216.508 244.472 1.00 8.39  ? 1534 PHE A N     1 
ATOM   659   C  CA    . PHE A 1 1534 ? 192.990 216.889 244.633 1.00 9.54  ? 1534 PHE A CA    1 
ATOM   660   C  C     . PHE A 1 1534 ? 192.632 218.174 243.905 1.00 9.22  ? 1534 PHE A C     1 
ATOM   661   O  O     . PHE A 1 1534 ? 191.442 218.476 243.773 1.00 12.56 ? 1534 PHE A O     1 
ATOM   662   C  CB    . PHE A 1 1534 ? 192.660 217.004 246.122 1.00 8.13  ? 1534 PHE A CB    1 
ATOM   663   C  CG    . PHE A 1 1534 ? 192.815 215.711 246.861 1.00 7.93  ? 1534 PHE A CG    1 
ATOM   664   C  CD1   . PHE A 1 1534 ? 192.099 214.592 246.473 1.00 11.05 ? 1534 PHE A CD1   1 
ATOM   665   C  CD2   . PHE A 1 1534 ? 193.693 215.603 247.922 1.00 8.42  ? 1534 PHE A CD2   1 
ATOM   666   C  CE1   . PHE A 1 1534 ? 192.243 213.394 247.140 1.00 11.27 ? 1534 PHE A CE1   1 
ATOM   667   C  CE2   . PHE A 1 1534 ? 193.843 214.407 248.593 1.00 13.97 ? 1534 PHE A CE2   1 
ATOM   668   C  CZ    . PHE A 1 1534 ? 193.116 213.300 248.202 1.00 17.38 ? 1534 PHE A CZ    1 
ATOM   669   N  N     . ASP A 1 1535 ? 193.619 218.936 243.427 1.00 8.05  ? 1535 ASP A N     1 
ATOM   670   C  CA    . ASP A 1 1535 ? 193.310 220.013 242.495 1.00 9.38  ? 1535 ASP A CA    1 
ATOM   671   C  C     . ASP A 1 1535 ? 192.935 219.462 241.126 1.00 6.65  ? 1535 ASP A C     1 
ATOM   672   O  O     . ASP A 1 1535 ? 192.243 220.135 240.354 1.00 10.19 ? 1535 ASP A O     1 
ATOM   673   C  CB    . ASP A 1 1535 ? 194.491 220.975 242.377 1.00 7.98  ? 1535 ASP A CB    1 
ATOM   674   C  CG    . ASP A 1 1535 ? 194.075 222.346 241.891 1.00 11.73 ? 1535 ASP A CG    1 
ATOM   675   O  OD1   . ASP A 1 1535 ? 193.340 223.037 242.626 1.00 6.79  ? 1535 ASP A OD1   1 
ATOM   676   O  OD2   . ASP A 1 1535 ? 194.482 222.734 240.776 1.00 13.46 ? 1535 ASP A OD2   1 
ATOM   677   N  N     . VAL A 1 1536 ? 193.382 218.248 240.807 1.00 5.67  ? 1536 VAL A N     1 
ATOM   678   C  CA    . VAL A 1 1536 ? 192.950 217.592 239.579 1.00 6.78  ? 1536 VAL A CA    1 
ATOM   679   C  C     . VAL A 1 1536 ? 191.706 216.751 239.833 1.00 7.45  ? 1536 VAL A C     1 
ATOM   680   O  O     . VAL A 1 1536 ? 190.801 216.694 238.994 1.00 10.14 ? 1536 VAL A O     1 
ATOM   681   C  CB    . VAL A 1 1536 ? 194.097 216.748 238.991 1.00 7.01  ? 1536 VAL A CB    1 
ATOM   682   C  CG1   . VAL A 1 1536 ? 193.651 216.058 237.712 1.00 8.32  ? 1536 VAL A CG1   1 
ATOM   683   C  CG2   . VAL A 1 1536 ? 195.319 217.610 238.733 1.00 6.12  ? 1536 VAL A CG2   1 
ATOM   684   N  N     . TRP A 1 1537 ? 191.635 216.102 240.999 1.00 7.24  ? 1537 TRP A N     1 
ATOM   685   C  CA    . TRP A 1 1537 ? 190.494 215.249 241.321 1.00 5.40  ? 1537 TRP A CA    1 
ATOM   686   C  C     . TRP A 1 1537 ? 189.192 216.037 241.272 1.00 6.91  ? 1537 TRP A C     1 
ATOM   687   O  O     . TRP A 1 1537 ? 188.171 215.536 240.786 1.00 8.14  ? 1537 TRP A O     1 
ATOM   688   C  CB    . TRP A 1 1537 ? 190.673 214.634 242.709 1.00 7.43  ? 1537 TRP A CB    1 
ATOM   689   C  CG    . TRP A 1 1537 ? 189.586 213.668 243.114 1.00 11.98 ? 1537 TRP A CG    1 
ATOM   690   C  CD1   . TRP A 1 1537 ? 188.549 213.922 243.950 1.00 25.31 ? 1537 TRP A CD1   1 
ATOM   691   C  CD2   . TRP A 1 1537 ? 189.514 212.269 242.817 1.00 9.70  ? 1537 TRP A CD2   1 
ATOM   692   N  NE1   . TRP A 1 1537 ? 187.783 212.802 244.122 1.00 24.62 ? 1537 TRP A NE1   1 
ATOM   693   C  CE2   . TRP A 1 1537 ? 188.366 211.766 243.448 1.00 22.14 ? 1537 TRP A CE2   1 
ATOM   694   C  CE3   . TRP A 1 1537 ? 190.294 211.401 242.059 1.00 27.35 ? 1537 TRP A CE3   1 
ATOM   695   C  CZ2   . TRP A 1 1537 ? 187.981 210.439 243.346 1.00 28.08 ? 1537 TRP A CZ2   1 
ATOM   696   C  CZ3   . TRP A 1 1537 ? 189.904 210.087 241.948 1.00 28.15 ? 1537 TRP A CZ3   1 
ATOM   697   C  CH2   . TRP A 1 1537 ? 188.760 209.615 242.589 1.00 24.73 ? 1537 TRP A CH2   1 
ATOM   698   N  N     . ILE A 1 1538 ? 189.208 217.273 241.781 1.00 5.87  ? 1538 ILE A N     1 
ATOM   699   C  CA    . ILE A 1 1538 ? 187.992 218.077 241.853 1.00 5.92  ? 1538 ILE A CA    1 
ATOM   700   C  C     . ILE A 1 1538 ? 187.459 218.379 240.458 1.00 6.79  ? 1538 ILE A C     1 
ATOM   701   O  O     . ILE A 1 1538 ? 186.247 218.326 240.215 1.00 5.50  ? 1538 ILE A O     1 
ATOM   702   C  CB    . ILE A 1 1538 ? 188.241 219.361 242.672 1.00 7.65  ? 1538 ILE A CB    1 
ATOM   703   C  CG1   . ILE A 1 1538 ? 186.939 220.147 242.840 1.00 5.36  ? 1538 ILE A CG1   1 
ATOM   704   C  CG2   . ILE A 1 1538 ? 189.330 220.224 242.042 1.00 4.85  ? 1538 ILE A CG2   1 
ATOM   705   C  CD1   . ILE A 1 1538 ? 187.063 221.354 243.730 1.00 4.01  ? 1538 ILE A CD1   1 
ATOM   706   N  N     . ASP A 1 1539 ? 188.350 218.700 239.517 1.00 6.54  ? 1539 ASP A N     1 
ATOM   707   C  CA    . ASP A 1 1539 ? 187.922 218.940 238.145 1.00 4.82  ? 1539 ASP A CA    1 
ATOM   708   C  C     . ASP A 1 1539 ? 187.482 217.656 237.456 1.00 5.02  ? 1539 ASP A C     1 
ATOM   709   O  O     . ASP A 1 1539 ? 186.579 217.690 236.613 1.00 9.97  ? 1539 ASP A O     1 
ATOM   710   C  CB    . ASP A 1 1539 ? 189.045 219.606 237.351 1.00 5.60  ? 1539 ASP A CB    1 
ATOM   711   C  CG    . ASP A 1 1539 ? 189.123 221.099 237.594 1.00 8.94  ? 1539 ASP A CG    1 
ATOM   712   O  OD1   . ASP A 1 1539 ? 188.075 221.717 237.864 1.00 10.86 ? 1539 ASP A OD1   1 
ATOM   713   O  OD2   . ASP A 1 1539 ? 190.237 221.658 237.509 1.00 20.78 ? 1539 ASP A OD2   1 
ATOM   714   N  N     . VAL A 1 1540 ? 188.102 216.526 237.796 1.00 3.82  ? 1540 VAL A N     1 
ATOM   715   C  CA    . VAL A 1 1540 ? 187.717 215.252 237.198 1.00 2.70  ? 1540 VAL A CA    1 
ATOM   716   C  C     . VAL A 1 1540 ? 186.347 214.817 237.702 1.00 2.14  ? 1540 VAL A C     1 
ATOM   717   O  O     . VAL A 1 1540 ? 185.491 214.380 236.926 1.00 1.22  ? 1540 VAL A O     1 
ATOM   718   C  CB    . VAL A 1 1540 ? 188.792 214.185 237.479 1.00 3.42  ? 1540 VAL A CB    1 
ATOM   719   C  CG1   . VAL A 1 1540 ? 188.281 212.795 237.138 1.00 2.60  ? 1540 VAL A CG1   1 
ATOM   720   C  CG2   . VAL A 1 1540 ? 190.053 214.497 236.696 1.00 4.07  ? 1540 VAL A CG2   1 
ATOM   721   N  N     . GLN A 1 1541 ? 186.118 214.931 239.013 1.00 2.90  ? 1541 GLN A N     1 
ATOM   722   C  CA    . GLN A 1 1541 ? 184.821 214.558 239.571 1.00 1.92  ? 1541 GLN A CA    1 
ATOM   723   C  C     . GLN A 1 1541 ? 183.714 215.464 239.047 1.00 2.22  ? 1541 GLN A C     1 
ATOM   724   O  O     . GLN A 1 1541 ? 182.616 214.995 238.734 1.00 2.48  ? 1541 GLN A O     1 
ATOM   725   C  CB    . GLN A 1 1541 ? 184.873 214.596 241.097 1.00 1.93  ? 1541 GLN A CB    1 
ATOM   726   C  CG    . GLN A 1 1541 ? 183.533 214.355 241.768 1.00 3.18  ? 1541 GLN A CG    1 
ATOM   727   C  CD    . GLN A 1 1541 ? 183.652 214.154 243.262 1.00 6.88  ? 1541 GLN A CD    1 
ATOM   728   O  OE1   . GLN A 1 1541 ? 184.227 213.171 243.723 1.00 17.40 ? 1541 GLN A OE1   1 
ATOM   729   N  NE2   . GLN A 1 1541 ? 183.105 215.087 244.028 1.00 8.89  ? 1541 GLN A NE2   1 
ATOM   730   N  N     . ARG A 1 1542 ? 183.986 216.765 238.945 1.00 3.46  ? 1542 ARG A N     1 
ATOM   731   C  CA    . ARG A 1 1542 ? 182.989 217.696 238.427 1.00 3.22  ? 1542 ARG A CA    1 
ATOM   732   C  C     . ARG A 1 1542 ? 182.609 217.357 236.992 1.00 2.96  ? 1542 ARG A C     1 
ATOM   733   O  O     . ARG A 1 1542 ? 181.426 217.330 236.640 1.00 3.24  ? 1542 ARG A O     1 
ATOM   734   C  CB    . ARG A 1 1542 ? 183.521 219.126 238.522 1.00 2.97  ? 1542 ARG A CB    1 
ATOM   735   C  CG    . ARG A 1 1542 ? 182.682 220.160 237.804 1.00 3.75  ? 1542 ARG A CG    1 
ATOM   736   C  CD    . ARG A 1 1542 ? 183.222 221.555 238.061 1.00 4.12  ? 1542 ARG A CD    1 
ATOM   737   N  NE    . ARG A 1 1542 ? 184.528 221.752 237.445 1.00 5.72  ? 1542 ARG A NE    1 
ATOM   738   C  CZ    . ARG A 1 1542 ? 184.728 221.930 236.147 1.00 13.20 ? 1542 ARG A CZ    1 
ATOM   739   N  NH1   . ARG A 1 1542 ? 183.720 221.978 235.292 1.00 13.10 ? 1542 ARG A NH1   1 
ATOM   740   N  NH2   . ARG A 1 1542 ? 185.972 222.068 235.696 1.00 11.49 ? 1542 ARG A NH2   1 
ATOM   741   N  N     . ARG A 1 1543 ? 183.606 217.084 236.149 1.00 3.00  ? 1543 ARG A N     1 
ATOM   742   C  CA    . ARG A 1 1543 ? 183.331 216.792 234.746 1.00 2.97  ? 1543 ARG A CA    1 
ATOM   743   C  C     . ARG A 1 1543 ? 182.639 215.448 234.583 1.00 2.81  ? 1543 ARG A C     1 
ATOM   744   O  O     . ARG A 1 1543 ? 181.764 215.295 233.720 1.00 8.39  ? 1543 ARG A O     1 
ATOM   745   C  CB    . ARG A 1 1543 ? 184.624 216.838 233.937 1.00 2.67  ? 1543 ARG A CB    1 
ATOM   746   C  CG    . ARG A 1 1543 ? 185.082 218.247 233.629 1.00 6.13  ? 1543 ARG A CG    1 
ATOM   747   C  CD    . ARG A 1 1543 ? 186.409 218.265 232.908 1.00 7.52  ? 1543 ARG A CD    1 
ATOM   748   N  NE    . ARG A 1 1543 ? 187.138 219.496 233.177 1.00 15.67 ? 1543 ARG A NE    1 
ATOM   749   C  CZ    . ARG A 1 1543 ? 187.296 220.478 232.300 1.00 17.21 ? 1543 ARG A CZ    1 
ATOM   750   N  NH1   . ARG A 1 1543 ? 186.786 220.404 231.082 1.00 15.55 ? 1543 ARG A NH1   1 
ATOM   751   N  NH2   . ARG A 1 1543 ? 187.983 221.559 232.654 1.00 18.32 ? 1543 ARG A NH2   1 
ATOM   752   N  N     . TRP A 1 1544 ? 183.011 214.461 235.400 1.00 1.86  ? 1544 TRP A N     1 
ATOM   753   C  CA    . TRP A 1 1544 ? 182.372 213.155 235.311 1.00 1.67  ? 1544 TRP A CA    1 
ATOM   754   C  C     . TRP A 1 1544 ? 180.903 213.216 235.707 1.00 3.10  ? 1544 TRP A C     1 
ATOM   755   O  O     . TRP A 1 1544 ? 180.093 212.450 235.176 1.00 4.05  ? 1544 TRP A O     1 
ATOM   756   C  CB    . TRP A 1 1544 ? 183.106 212.140 236.187 1.00 2.52  ? 1544 TRP A CB    1 
ATOM   757   C  CG    . TRP A 1 1544 ? 182.510 210.768 236.119 1.00 2.02  ? 1544 TRP A CG    1 
ATOM   758   C  CD1   . TRP A 1 1544 ? 182.794 209.797 235.208 1.00 3.76  ? 1544 TRP A CD1   1 
ATOM   759   C  CD2   . TRP A 1 1544 ? 181.509 210.225 236.986 1.00 1.86  ? 1544 TRP A CD2   1 
ATOM   760   N  NE1   . TRP A 1 1544 ? 182.042 208.677 235.457 1.00 3.38  ? 1544 TRP A NE1   1 
ATOM   761   C  CE2   . TRP A 1 1544 ? 181.243 208.914 236.544 1.00 2.57  ? 1544 TRP A CE2   1 
ATOM   762   C  CE3   . TRP A 1 1544 ? 180.814 210.716 238.094 1.00 2.25  ? 1544 TRP A CE3   1 
ATOM   763   C  CZ2   . TRP A 1 1544 ? 180.315 208.091 237.173 1.00 3.63  ? 1544 TRP A CZ2   1 
ATOM   764   C  CZ3   . TRP A 1 1544 ? 179.895 209.898 238.715 1.00 2.54  ? 1544 TRP A CZ3   1 
ATOM   765   C  CH2   . TRP A 1 1544 ? 179.652 208.600 238.253 1.00 4.28  ? 1544 TRP A CH2   1 
ATOM   766   N  N     . VAL A 1 1545 ? 180.539 214.110 236.627 1.00 2.59  ? 1545 VAL A N     1 
ATOM   767   C  CA    . VAL A 1 1545 ? 179.159 214.163 237.102 1.00 3.50  ? 1545 VAL A CA    1 
ATOM   768   C  C     . VAL A 1 1545 ? 178.211 214.545 235.970 1.00 4.76  ? 1545 VAL A C     1 
ATOM   769   O  O     . VAL A 1 1545 ? 177.189 213.885 235.746 1.00 5.89  ? 1545 VAL A O     1 
ATOM   770   C  CB    . VAL A 1 1545 ? 179.036 215.125 238.297 1.00 2.80  ? 1545 VAL A CB    1 
ATOM   771   C  CG1   . VAL A 1 1545 ? 177.590 215.532 238.506 1.00 4.63  ? 1545 VAL A CG1   1 
ATOM   772   C  CG2   . VAL A 1 1545 ? 179.576 214.466 239.546 1.00 2.88  ? 1545 VAL A CG2   1 
ATOM   773   N  N     . TYR A 1 1546 ? 178.530 215.611 235.233 1.00 3.17  ? 1546 TYR A N     1 
ATOM   774   C  CA    . TYR A 1 1546 ? 177.610 216.048 234.191 1.00 3.90  ? 1546 TYR A CA    1 
ATOM   775   C  C     . TYR A 1 1546 ? 177.782 215.274 232.888 1.00 4.74  ? 1546 TYR A C     1 
ATOM   776   O  O     . TYR A 1 1546 ? 176.828 215.189 232.110 1.00 5.21  ? 1546 TYR A O     1 
ATOM   777   C  CB    . TYR A 1 1546 ? 177.732 217.560 233.951 1.00 3.64  ? 1546 TYR A CB    1 
ATOM   778   C  CG    . TYR A 1 1546 ? 179.051 218.077 233.416 1.00 2.81  ? 1546 TYR A CG    1 
ATOM   779   C  CD1   . TYR A 1 1546 ? 179.438 217.843 232.101 1.00 3.36  ? 1546 TYR A CD1   1 
ATOM   780   C  CD2   . TYR A 1 1546 ? 179.891 218.842 234.214 1.00 3.14  ? 1546 TYR A CD2   1 
ATOM   781   C  CE1   . TYR A 1 1546 ? 180.628 218.324 231.612 1.00 3.57  ? 1546 TYR A CE1   1 
ATOM   782   C  CE2   . TYR A 1 1546 ? 181.085 219.330 233.729 1.00 3.71  ? 1546 TYR A CE2   1 
ATOM   783   C  CZ    . TYR A 1 1546 ? 181.450 219.069 232.427 1.00 5.57  ? 1546 TYR A CZ    1 
ATOM   784   O  OH    . TYR A 1 1546 ? 182.637 219.554 231.932 1.00 6.15  ? 1546 TYR A OH    1 
ATOM   785   N  N     . LEU A 1 1547 ? 178.961 214.707 232.631 1.00 3.39  ? 1547 LEU A N     1 
ATOM   786   C  CA    . LEU A 1 1547 ? 179.095 213.818 231.482 1.00 3.42  ? 1547 LEU A CA    1 
ATOM   787   C  C     . LEU A 1 1547 ? 178.358 212.506 231.716 1.00 3.45  ? 1547 LEU A C     1 
ATOM   788   O  O     . LEU A 1 1547 ? 177.755 211.953 230.791 1.00 5.90  ? 1547 LEU A O     1 
ATOM   789   C  CB    . LEU A 1 1547 ? 180.567 213.559 231.171 1.00 3.30  ? 1547 LEU A CB    1 
ATOM   790   C  CG    . LEU A 1 1547 ? 181.304 214.679 230.440 1.00 4.25  ? 1547 LEU A CG    1 
ATOM   791   C  CD1   . LEU A 1 1547 ? 182.769 214.328 230.264 1.00 3.46  ? 1547 LEU A CD1   1 
ATOM   792   C  CD2   . LEU A 1 1547 ? 180.647 214.962 229.099 1.00 3.50  ? 1547 LEU A CD2   1 
ATOM   793   N  N     . GLU A 1 1548 ? 178.392 211.996 232.948 1.00 3.86  ? 1548 GLU A N     1 
ATOM   794   C  CA    . GLU A 1 1548 ? 177.656 210.777 233.268 1.00 8.25  ? 1548 GLU A CA    1 
ATOM   795   C  C     . GLU A 1 1548 ? 176.155 211.002 233.143 1.00 8.23  ? 1548 GLU A C     1 
ATOM   796   O  O     . GLU A 1 1548 ? 175.422 210.111 232.702 1.00 15.14 ? 1548 GLU A O     1 
ATOM   797   C  CB    . GLU A 1 1548 ? 178.026 210.298 234.672 1.00 6.33  ? 1548 GLU A CB    1 
ATOM   798   C  CG    . GLU A 1 1548 ? 177.634 208.867 235.008 1.00 8.34  ? 1548 GLU A CG    1 
ATOM   799   C  CD    . GLU A 1 1548 ? 176.158 208.714 235.316 1.00 18.95 ? 1548 GLU A CD    1 
ATOM   800   O  OE1   . GLU A 1 1548 ? 175.629 209.519 236.111 1.00 20.52 ? 1548 GLU A OE1   1 
ATOM   801   O  OE2   . GLU A 1 1548 ? 175.533 207.784 234.768 1.00 19.04 ? 1548 GLU A OE2   1 
ATOM   802   N  N     . GLY A 1 1549 ? 175.678 212.187 233.527 1.00 5.09  ? 1549 GLY A N     1 
ATOM   803   C  CA    . GLY A 1 1549 ? 174.264 212.486 233.378 1.00 7.58  ? 1549 GLY A CA    1 
ATOM   804   C  C     . GLY A 1 1549 ? 173.821 212.526 231.927 1.00 9.60  ? 1549 GLY A C     1 
ATOM   805   O  O     . GLY A 1 1549 ? 172.729 212.067 231.589 1.00 18.95 ? 1549 GLY A O     1 
ATOM   806   N  N     . ILE A 1 1550 ? 174.659 213.085 231.054 1.00 7.75  ? 1550 ILE A N     1 
ATOM   807   C  CA    . ILE A 1 1550 ? 174.318 213.155 229.637 1.00 8.58  ? 1550 ILE A CA    1 
ATOM   808   C  C     . ILE A 1 1550 ? 174.366 211.774 228.994 1.00 9.62  ? 1550 ILE A C     1 
ATOM   809   O  O     . ILE A 1 1550 ? 173.478 211.406 228.217 1.00 16.79 ? 1550 ILE A O     1 
ATOM   810   C  CB    . ILE A 1 1550 ? 175.238 214.155 228.916 1.00 7.60  ? 1550 ILE A CB    1 
ATOM   811   C  CG1   . ILE A 1 1550 ? 175.011 215.560 229.472 1.00 6.54  ? 1550 ILE A CG1   1 
ATOM   812   C  CG2   . ILE A 1 1550 ? 174.999 214.122 227.419 1.00 12.98 ? 1550 ILE A CG2   1 
ATOM   813   C  CD1   . ILE A 1 1550 ? 176.030 216.569 229.030 1.00 5.28  ? 1550 ILE A CD1   1 
ATOM   814   N  N     . PHE A 1 1551 ? 175.390 210.984 229.308 1.00 13.36 ? 1551 PHE A N     1 
ATOM   815   C  CA    . PHE A 1 1551 ? 175.555 209.674 228.688 1.00 11.02 ? 1551 PHE A CA    1 
ATOM   816   C  C     . PHE A 1 1551 ? 174.713 208.594 229.352 1.00 12.72 ? 1551 PHE A C     1 
ATOM   817   O  O     . PHE A 1 1551 ? 174.879 207.413 229.026 1.00 18.87 ? 1551 PHE A O     1 
ATOM   818   C  CB    . PHE A 1 1551 ? 177.030 209.264 228.699 1.00 5.47  ? 1551 PHE A CB    1 
ATOM   819   C  CG    . PHE A 1 1551 ? 177.856 209.956 227.654 1.00 6.44  ? 1551 PHE A CG    1 
ATOM   820   C  CD1   . PHE A 1 1551 ? 177.736 209.613 226.319 1.00 6.07  ? 1551 PHE A CD1   1 
ATOM   821   C  CD2   . PHE A 1 1551 ? 178.761 210.940 228.009 1.00 6.46  ? 1551 PHE A CD2   1 
ATOM   822   C  CE1   . PHE A 1 1551 ? 178.493 210.246 225.355 1.00 6.45  ? 1551 PHE A CE1   1 
ATOM   823   C  CE2   . PHE A 1 1551 ? 179.523 211.577 227.051 1.00 4.85  ? 1551 PHE A CE2   1 
ATOM   824   C  CZ    . PHE A 1 1551 ? 179.389 211.229 225.722 1.00 8.68  ? 1551 PHE A CZ    1 
ATOM   825   N  N     . THR A 1 1552 ? 173.831 208.961 230.274 1.00 10.81 ? 1552 THR A N     1 
ATOM   826   C  CA    . THR A 1 1552 ? 172.888 208.036 230.887 1.00 13.88 ? 1552 THR A CA    1 
ATOM   827   C  C     . THR A 1 1552 ? 171.438 208.439 230.671 1.00 22.61 ? 1552 THR A C     1 
ATOM   828   O  O     . THR A 1 1552 ? 170.600 207.583 230.375 1.00 25.35 ? 1552 THR A O     1 
ATOM   829   C  CB    . THR A 1 1552 ? 173.169 207.915 232.396 1.00 16.46 ? 1552 THR A CB    1 
ATOM   830   O  OG1   . THR A 1 1552 ? 174.415 207.236 232.597 1.00 20.13 ? 1552 THR A OG1   1 
ATOM   831   C  CG2   . THR A 1 1552 ? 172.064 207.146 233.098 1.00 16.02 ? 1552 THR A CG2   1 
ATOM   832   N  N     . GLY A 1 1553 ? 171.123 209.726 230.785 1.00 17.83 ? 1553 GLY A N     1 
ATOM   833   C  CA    . GLY A 1 1553 ? 169.772 210.225 230.652 1.00 21.23 ? 1553 GLY A CA    1 
ATOM   834   C  C     . GLY A 1 1553 ? 169.302 210.502 229.241 1.00 22.63 ? 1553 GLY A C     1 
ATOM   835   O  O     . GLY A 1 1553 ? 168.164 210.948 229.064 1.00 23.45 ? 1553 GLY A O     1 
ATOM   836   N  N     . SER A 1 1554 ? 170.132 210.254 228.225 1.00 22.22 ? 1554 SER A N     1 
ATOM   837   C  CA    . SER A 1 1554 ? 169.752 210.494 226.830 1.00 25.16 ? 1554 SER A CA    1 
ATOM   838   C  C     . SER A 1 1554 ? 170.266 209.320 225.996 1.00 21.72 ? 1554 SER A C     1 
ATOM   839   O  O     . SER A 1 1554 ? 171.425 209.303 225.577 1.00 27.12 ? 1554 SER A O     1 
ATOM   840   C  CB    . SER A 1 1554 ? 170.296 211.824 226.324 1.00 28.25 ? 1554 SER A CB    1 
ATOM   841   O  OG    . SER A 1 1554 ? 171.713 211.828 226.311 1.00 26.49 ? 1554 SER A OG    1 
ATOM   842   N  N     . ALA A 1 1555 ? 169.388 208.345 225.755 1.00 24.61 ? 1555 ALA A N     1 
ATOM   843   C  CA    . ALA A 1 1555 ? 169.780 207.173 224.978 1.00 27.79 ? 1555 ALA A CA    1 
ATOM   844   C  C     . ALA A 1 1555 ? 170.031 207.519 223.517 1.00 29.02 ? 1555 ALA A C     1 
ATOM   845   O  O     . ALA A 1 1555 ? 170.665 206.741 222.795 1.00 31.36 ? 1555 ALA A O     1 
ATOM   846   C  CB    . ALA A 1 1555 ? 168.709 206.087 225.090 1.00 24.79 ? 1555 ALA A CB    1 
ATOM   847   N  N     . ASP A 1 1556 ? 169.545 208.676 223.064 1.00 23.59 ? 1556 ASP A N     1 
ATOM   848   C  CA    . ASP A 1 1556 ? 169.737 209.068 221.670 1.00 26.60 ? 1556 ASP A CA    1 
ATOM   849   C  C     . ASP A 1 1556 ? 171.198 209.374 221.369 1.00 29.03 ? 1556 ASP A C     1 
ATOM   850   O  O     . ASP A 1 1556 ? 171.645 209.236 220.223 1.00 30.48 ? 1556 ASP A O     1 
ATOM   851   C  CB    . ASP A 1 1556 ? 168.863 210.281 221.345 1.00 23.24 ? 1556 ASP A CB    1 
ATOM   852   C  CG    . ASP A 1 1556 ? 168.958 211.364 222.400 1.00 30.49 ? 1556 ASP A CG    1 
ATOM   853   O  OD1   . ASP A 1 1556 ? 168.586 211.097 223.560 1.00 33.07 ? 1556 ASP A OD1   1 
ATOM   854   O  OD2   . ASP A 1 1556 ? 169.405 212.481 222.066 1.00 30.35 ? 1556 ASP A OD2   1 
ATOM   855   N  N     . ILE A 1 1557 ? 171.957 209.803 222.379 1.00 21.40 ? 1557 ILE A N     1 
ATOM   856   C  CA    . ILE A 1 1557 ? 173.342 210.206 222.146 1.00 19.12 ? 1557 ILE A CA    1 
ATOM   857   C  C     . ILE A 1 1557 ? 174.207 208.994 221.821 1.00 20.58 ? 1557 ILE A C     1 
ATOM   858   O  O     . ILE A 1 1557 ? 175.235 209.111 221.142 1.00 20.94 ? 1557 ILE A O     1 
ATOM   859   C  CB    . ILE A 1 1557 ? 173.884 210.994 223.356 1.00 18.46 ? 1557 ILE A CB    1 
ATOM   860   C  CG1   . ILE A 1 1557 ? 175.063 211.873 222.938 1.00 17.15 ? 1557 ILE A CG1   1 
ATOM   861   C  CG2   . ILE A 1 1557 ? 174.310 210.060 224.477 1.00 16.78 ? 1557 ILE A CG2   1 
ATOM   862   C  CD1   . ILE A 1 1557 ? 175.595 212.744 224.051 1.00 11.64 ? 1557 ILE A CD1   1 
ATOM   863   N  N     . LYS A 1 1558 ? 173.804 207.812 222.294 1.00 19.87 ? 1558 LYS A N     1 
ATOM   864   C  CA    . LYS A 1 1558 ? 174.572 206.602 222.019 1.00 17.94 ? 1558 LYS A CA    1 
ATOM   865   C  C     . LYS A 1 1558 ? 174.598 206.300 220.526 1.00 21.88 ? 1558 LYS A C     1 
ATOM   866   O  O     . LYS A 1 1558 ? 175.631 205.903 219.976 1.00 22.64 ? 1558 LYS A O     1 
ATOM   867   C  CB    . LYS A 1 1558 ? 173.990 205.426 222.801 1.00 17.70 ? 1558 LYS A CB    1 
ATOM   868   C  CG    . LYS A 1 1558 ? 174.730 204.116 222.595 1.00 21.23 ? 1558 LYS A CG    1 
ATOM   869   C  CD    . LYS A 1 1558 ? 174.140 203.010 223.452 1.00 27.20 ? 1558 LYS A CD    1 
ATOM   870   C  CE    . LYS A 1 1558 ? 174.937 201.724 223.315 1.00 29.05 ? 1558 LYS A CE    1 
ATOM   871   N  NZ    . LYS A 1 1558 ? 176.360 201.908 223.713 1.00 29.64 ? 1558 LYS A NZ    1 
ATOM   872   N  N     . HIS A 1 1559 ? 173.461 206.480 219.852 1.00 25.89 ? 1559 HIS A N     1 
ATOM   873   C  CA    . HIS A 1 1559 ? 173.425 206.298 218.406 1.00 26.69 ? 1559 HIS A CA    1 
ATOM   874   C  C     . HIS A 1 1559 ? 174.069 207.474 217.684 1.00 22.90 ? 1559 HIS A C     1 
ATOM   875   O  O     . HIS A 1 1559 ? 174.761 207.288 216.676 1.00 27.09 ? 1559 HIS A O     1 
ATOM   876   C  CB    . HIS A 1 1559 ? 171.983 206.112 217.940 1.00 25.11 ? 1559 HIS A CB    1 
ATOM   877   C  CG    . HIS A 1 1559 ? 171.342 204.857 218.448 1.00 31.11 ? 1559 HIS A CG    1 
ATOM   878   N  ND1   . HIS A 1 1559 ? 170.674 204.798 219.652 1.00 32.94 ? 1559 HIS A ND1   1 
ATOM   879   C  CD2   . HIS A 1 1559 ? 171.272 203.614 217.919 1.00 31.60 ? 1559 HIS A CD2   1 
ATOM   880   C  CE1   . HIS A 1 1559 ? 170.217 203.573 219.841 1.00 32.83 ? 1559 HIS A CE1   1 
ATOM   881   N  NE2   . HIS A 1 1559 ? 170.567 202.835 218.802 1.00 30.53 ? 1559 HIS A NE2   1 
ATOM   882   N  N     . LEU A 1 1560 ? 173.847 208.692 218.182 1.00 20.32 ? 1560 LEU A N     1 
ATOM   883   C  CA    . LEU A 1 1560 ? 174.380 209.877 217.515 1.00 18.85 ? 1560 LEU A CA    1 
ATOM   884   C  C     . LEU A 1 1560 ? 175.904 209.886 217.539 1.00 21.92 ? 1560 LEU A C     1 
ATOM   885   O  O     . LEU A 1 1560 ? 176.549 210.204 216.534 1.00 23.19 ? 1560 LEU A O     1 
ATOM   886   C  CB    . LEU A 1 1560 ? 173.817 211.137 218.172 1.00 20.91 ? 1560 LEU A CB    1 
ATOM   887   C  CG    . LEU A 1 1560 ? 174.398 212.477 217.721 1.00 24.67 ? 1560 LEU A CG    1 
ATOM   888   C  CD1   . LEU A 1 1560 ? 174.199 212.678 216.227 1.00 23.84 ? 1560 LEU A CD1   1 
ATOM   889   C  CD2   . LEU A 1 1560 ? 173.774 213.622 218.505 1.00 20.75 ? 1560 LEU A CD2   1 
ATOM   890   N  N     . LEU A 1 1561 ? 176.498 209.541 218.680 1.00 20.82 ? 1561 LEU A N     1 
ATOM   891   C  CA    . LEU A 1 1561 ? 177.949 209.514 218.853 1.00 19.12 ? 1561 LEU A CA    1 
ATOM   892   C  C     . LEU A 1 1561 ? 178.365 208.189 219.477 1.00 20.73 ? 1561 LEU A C     1 
ATOM   893   O  O     . LEU A 1 1561 ? 178.665 208.116 220.674 1.00 20.36 ? 1561 LEU A O     1 
ATOM   894   C  CB    . LEU A 1 1561 ? 178.419 210.695 219.702 1.00 19.66 ? 1561 LEU A CB    1 
ATOM   895   C  CG    . LEU A 1 1561 ? 178.006 212.067 219.181 1.00 19.74 ? 1561 LEU A CG    1 
ATOM   896   C  CD1   . LEU A 1 1561 ? 178.393 213.159 220.157 1.00 20.94 ? 1561 LEU A CD1   1 
ATOM   897   C  CD2   . LEU A 1 1561 ? 178.672 212.296 217.834 1.00 21.58 ? 1561 LEU A CD2   1 
ATOM   898   N  N     . PRO A 1 1562 ? 178.381 207.110 218.688 1.00 21.62 ? 1562 PRO A N     1 
ATOM   899   C  CA    . PRO A 1 1562 ? 178.772 205.806 219.252 1.00 18.01 ? 1562 PRO A CA    1 
ATOM   900   C  C     . PRO A 1 1562 ? 180.201 205.771 219.767 1.00 18.40 ? 1562 PRO A C     1 
ATOM   901   O  O     . PRO A 1 1562 ? 180.465 205.163 220.812 1.00 15.29 ? 1562 PRO A O     1 
ATOM   902   C  CB    . PRO A 1 1562 ? 178.561 204.846 218.073 1.00 15.95 ? 1562 PRO A CB    1 
ATOM   903   C  CG    . PRO A 1 1562 ? 177.617 205.561 217.156 1.00 18.51 ? 1562 PRO A CG    1 
ATOM   904   C  CD    . PRO A 1 1562 ? 177.993 207.001 217.273 1.00 13.87 ? 1562 PRO A CD    1 
ATOM   905   N  N     . VAL A 1 1563 ? 181.135 206.412 219.060 1.00 19.08 ? 1563 VAL A N     1 
ATOM   906   C  CA    . VAL A 1 1563 ? 182.538 206.365 219.467 1.00 15.54 ? 1563 VAL A CA    1 
ATOM   907   C  C     . VAL A 1 1563 ? 182.722 207.062 220.807 1.00 18.31 ? 1563 VAL A C     1 
ATOM   908   O  O     . VAL A 1 1563 ? 183.344 206.521 221.730 1.00 21.23 ? 1563 VAL A O     1 
ATOM   909   C  CB    . VAL A 1 1563 ? 183.435 206.986 218.381 1.00 22.66 ? 1563 VAL A CB    1 
ATOM   910   C  CG1   . VAL A 1 1563 ? 184.877 207.034 218.851 1.00 20.90 ? 1563 VAL A CG1   1 
ATOM   911   C  CG2   . VAL A 1 1563 ? 183.320 206.201 217.087 1.00 17.92 ? 1563 VAL A CG2   1 
ATOM   912   N  N     . GLU A 1 1564 ? 182.170 208.269 220.940 1.00 18.15 ? 1564 GLU A N     1 
ATOM   913   C  CA    . GLU A 1 1564 ? 182.279 209.005 222.194 1.00 15.43 ? 1564 GLU A CA    1 
ATOM   914   C  C     . GLU A 1 1564 ? 181.584 208.267 223.330 1.00 14.94 ? 1564 GLU A C     1 
ATOM   915   O  O     . GLU A 1 1564 ? 182.085 208.233 224.460 1.00 18.90 ? 1564 GLU A O     1 
ATOM   916   C  CB    . GLU A 1 1564 ? 181.703 210.412 222.026 1.00 13.11 ? 1564 GLU A CB    1 
ATOM   917   C  CG    . GLU A 1 1564 ? 182.461 211.302 221.043 1.00 15.93 ? 1564 GLU A CG    1 
ATOM   918   C  CD    . GLU A 1 1564 ? 182.232 210.943 219.584 1.00 29.21 ? 1564 GLU A CD    1 
ATOM   919   O  OE1   . GLU A 1 1564 ? 181.475 209.990 219.305 1.00 32.26 ? 1564 GLU A OE1   1 
ATOM   920   O  OE2   . GLU A 1 1564 ? 182.811 211.622 218.710 1.00 32.54 ? 1564 GLU A OE2   1 
ATOM   921   N  N     . THR A 1 1565 ? 180.424 207.671 223.048 1.00 12.02 ? 1565 THR A N     1 
ATOM   922   C  CA    . THR A 1 1565 ? 179.685 206.965 224.090 1.00 11.39 ? 1565 THR A CA    1 
ATOM   923   C  C     . THR A 1 1565 ? 180.468 205.766 224.612 1.00 16.98 ? 1565 THR A C     1 
ATOM   924   O  O     . THR A 1 1565 ? 180.516 205.528 225.825 1.00 14.75 ? 1565 THR A O     1 
ATOM   925   C  CB    . THR A 1 1565 ? 178.322 206.527 223.558 1.00 11.29 ? 1565 THR A CB    1 
ATOM   926   O  OG1   . THR A 1 1565 ? 177.588 207.680 223.129 1.00 20.80 ? 1565 THR A OG1   1 
ATOM   927   C  CG2   . THR A 1 1565 ? 177.535 205.809 224.640 1.00 8.58  ? 1565 THR A CG2   1 
ATOM   928   N  N     . GLN A 1 1566 ? 181.087 204.996 223.715 1.00 17.17 ? 1566 GLN A N     1 
ATOM   929   C  CA    . GLN A 1 1566 ? 181.908 203.872 224.160 1.00 17.29 ? 1566 GLN A CA    1 
ATOM   930   C  C     . GLN A 1 1566 ? 183.181 204.355 224.843 1.00 16.96 ? 1566 GLN A C     1 
ATOM   931   O  O     . GLN A 1 1566 ? 183.614 203.773 225.845 1.00 14.73 ? 1566 GLN A O     1 
ATOM   932   C  CB    . GLN A 1 1566 ? 182.234 202.949 222.985 1.00 19.36 ? 1566 GLN A CB    1 
ATOM   933   C  CG    . GLN A 1 1566 ? 181.031 202.384 222.217 1.00 27.13 ? 1566 GLN A CG    1 
ATOM   934   C  CD    . GLN A 1 1566 ? 180.002 201.682 223.098 1.00 32.83 ? 1566 GLN A CD    1 
ATOM   935   O  OE1   . GLN A 1 1566 ? 179.347 202.297 223.940 1.00 29.53 ? 1566 GLN A OE1   1 
ATOM   936   N  NE2   . GLN A 1 1566 ? 179.863 200.374 222.905 1.00 25.49 ? 1566 GLN A NE2   1 
ATOM   937   N  N     . ARG A 1 1567 ? 183.797 205.417 224.319 1.00 18.56 ? 1567 ARG A N     1 
ATOM   938   C  CA    . ARG A 1 1567 ? 184.989 205.955 224.969 1.00 11.63 ? 1567 ARG A CA    1 
ATOM   939   C  C     . ARG A 1 1567 ? 184.674 206.454 226.370 1.00 14.70 ? 1567 ARG A C     1 
ATOM   940   O  O     . ARG A 1 1567 ? 185.452 206.231 227.302 1.00 17.82 ? 1567 ARG A O     1 
ATOM   941   C  CB    . ARG A 1 1567 ? 185.617 207.065 224.127 1.00 9.54  ? 1567 ARG A CB    1 
ATOM   942   C  CG    . ARG A 1 1567 ? 186.220 206.581 222.823 1.00 23.84 ? 1567 ARG A CG    1 
ATOM   943   C  CD    . ARG A 1 1567 ? 186.804 207.722 222.005 1.00 27.89 ? 1567 ARG A CD    1 
ATOM   944   N  NE    . ARG A 1 1567 ? 187.954 208.343 222.649 1.00 25.24 ? 1567 ARG A NE    1 
ATOM   945   C  CZ    . ARG A 1 1567 ? 188.546 209.449 222.219 1.00 32.08 ? 1567 ARG A CZ    1 
ATOM   946   N  NH1   . ARG A 1 1567 ? 188.132 210.075 221.129 1.00 27.40 ? 1567 ARG A NH1   1 
ATOM   947   N  NH2   . ARG A 1 1567 ? 189.584 209.935 222.892 1.00 34.02 ? 1567 ARG A NH2   1 
ATOM   948   N  N     . PHE A 1 1568 ? 183.529 207.117 226.549 1.00 14.72 ? 1568 PHE A N     1 
ATOM   949   C  CA    . PHE A 1 1568 ? 183.162 207.563 227.887 1.00 8.90  ? 1568 PHE A CA    1 
ATOM   950   C  C     . PHE A 1 1568 ? 182.899 206.391 228.819 1.00 9.03  ? 1568 PHE A C     1 
ATOM   951   O  O     . PHE A 1 1568 ? 183.174 206.486 230.019 1.00 10.37 ? 1568 PHE A O     1 
ATOM   952   C  CB    . PHE A 1 1568 ? 181.934 208.472 227.851 1.00 11.30 ? 1568 PHE A CB    1 
ATOM   953   C  CG    . PHE A 1 1568 ? 181.444 208.854 229.216 1.00 9.49  ? 1568 PHE A CG    1 
ATOM   954   C  CD1   . PHE A 1 1568 ? 182.101 209.828 229.951 1.00 5.71  ? 1568 PHE A CD1   1 
ATOM   955   C  CD2   . PHE A 1 1568 ? 180.355 208.216 229.783 1.00 4.59  ? 1568 PHE A CD2   1 
ATOM   956   C  CE1   . PHE A 1 1568 ? 181.666 210.170 231.214 1.00 3.49  ? 1568 PHE A CE1   1 
ATOM   957   C  CE2   . PHE A 1 1568 ? 179.921 208.555 231.044 1.00 5.01  ? 1568 PHE A CE2   1 
ATOM   958   C  CZ    . PHE A 1 1568 ? 180.578 209.532 231.760 1.00 4.22  ? 1568 PHE A CZ    1 
ATOM   959   N  N     . GLN A 1 1569 ? 182.359 205.292 228.293 1.00 16.62 ? 1569 GLN A N     1 
ATOM   960   C  CA    . GLN A 1 1569 ? 182.101 204.126 229.132 1.00 15.79 ? 1569 GLN A CA    1 
ATOM   961   C  C     . GLN A 1 1569 ? 183.397 203.565 229.705 1.00 16.35 ? 1569 GLN A C     1 
ATOM   962   O  O     . GLN A 1 1569 ? 183.451 203.178 230.877 1.00 16.30 ? 1569 GLN A O     1 
ATOM   963   C  CB    . GLN A 1 1569 ? 181.362 203.058 228.328 1.00 17.71 ? 1569 GLN A CB    1 
ATOM   964   C  CG    . GLN A 1 1569 ? 180.985 201.837 229.142 1.00 20.36 ? 1569 GLN A CG    1 
ATOM   965   C  CD    . GLN A 1 1569 ? 180.034 202.180 230.271 1.00 27.04 ? 1569 GLN A CD    1 
ATOM   966   O  OE1   . GLN A 1 1569 ? 180.429 202.236 231.434 1.00 27.79 ? 1569 GLN A OE1   1 
ATOM   967   N  NE2   . GLN A 1 1569 ? 178.771 202.405 229.932 1.00 27.03 ? 1569 GLN A NE2   1 
ATOM   968   N  N     . SER A 1 1570 ? 184.451 203.510 228.886 1.00 15.62 ? 1570 SER A N     1 
ATOM   969   C  CA    . SER A 1 1570 ? 185.738 203.002 229.351 1.00 14.84 ? 1570 SER A CA    1 
ATOM   970   C  C     . SER A 1 1570 ? 186.332 203.900 230.430 1.00 18.37 ? 1570 SER A C     1 
ATOM   971   O  O     . SER A 1 1570 ? 186.836 203.416 231.449 1.00 24.02 ? 1570 SER A O     1 
ATOM   972   C  CB    . SER A 1 1570 ? 186.700 202.874 228.168 1.00 18.73 ? 1570 SER A CB    1 
ATOM   973   O  OG    . SER A 1 1570 ? 186.102 202.157 227.100 1.00 21.35 ? 1570 SER A OG    1 
ATOM   974   N  N     . ILE A 1 1571 ? 186.284 205.216 230.220 1.00 16.59 ? 1571 ILE A N     1 
ATOM   975   C  CA    . ILE A 1 1571 ? 186.792 206.148 231.221 1.00 11.82 ? 1571 ILE A CA    1 
ATOM   976   C  C     . ILE A 1 1571 ? 185.911 206.137 232.462 1.00 14.38 ? 1571 ILE A C     1 
ATOM   977   O  O     . ILE A 1 1571 ? 186.409 206.224 233.591 1.00 15.63 ? 1571 ILE A O     1 
ATOM   978   C  CB    . ILE A 1 1571 ? 186.914 207.557 230.617 1.00 10.56 ? 1571 ILE A CB    1 
ATOM   979   C  CG1   . ILE A 1 1571 ? 187.445 207.461 229.189 1.00 14.81 ? 1571 ILE A CG1   1 
ATOM   980   C  CG2   . ILE A 1 1571 ? 187.803 208.435 231.467 1.00 13.00 ? 1571 ILE A CG2   1 
ATOM   981   C  CD1   . ILE A 1 1571 ? 187.690 208.780 228.543 1.00 15.44 ? 1571 ILE A CD1   1 
ATOM   982   N  N     . SER A 1 1572 ? 184.595 206.030 232.276 1.00 11.55 ? 1572 SER A N     1 
ATOM   983   C  CA    . SER A 1 1572 ? 183.692 205.955 233.419 1.00 10.47 ? 1572 SER A CA    1 
ATOM   984   C  C     . SER A 1 1572 ? 183.932 204.692 234.234 1.00 14.57 ? 1572 SER A C     1 
ATOM   985   O  O     . SER A 1 1572 ? 183.613 204.655 235.427 1.00 15.68 ? 1572 SER A O     1 
ATOM   986   C  CB    . SER A 1 1572 ? 182.241 206.018 232.943 1.00 9.59  ? 1572 SER A CB    1 
ATOM   987   O  OG    . SER A 1 1572 ? 181.339 206.063 234.030 1.00 16.28 ? 1572 SER A OG    1 
ATOM   988   N  N     . THR A 1 1573 ? 184.483 203.647 233.612 1.00 18.01 ? 1573 THR A N     1 
ATOM   989   C  CA    . THR A 1 1573 ? 184.807 202.435 234.358 1.00 16.69 ? 1573 THR A CA    1 
ATOM   990   C  C     . THR A 1 1573 ? 186.030 202.641 235.245 1.00 15.79 ? 1573 THR A C     1 
ATOM   991   O  O     . THR A 1 1573 ? 186.021 202.257 236.419 1.00 15.68 ? 1573 THR A O     1 
ATOM   992   C  CB    . THR A 1 1573 ? 185.031 201.268 233.397 1.00 16.79 ? 1573 THR A CB    1 
ATOM   993   O  OG1   . THR A 1 1573 ? 183.900 201.142 232.528 1.00 23.67 ? 1573 THR A OG1   1 
ATOM   994   C  CG2   . THR A 1 1573 ? 185.203 199.973 234.170 1.00 12.10 ? 1573 THR A CG2   1 
ATOM   995   N  N     . GLU A 1 1574 ? 187.086 203.254 234.704 1.00 15.04 ? 1574 GLU A N     1 
ATOM   996   C  CA    . GLU A 1 1574 ? 188.292 203.476 235.494 1.00 12.26 ? 1574 GLU A CA    1 
ATOM   997   C  C     . GLU A 1 1574 ? 188.038 204.476 236.615 1.00 16.44 ? 1574 GLU A C     1 
ATOM   998   O  O     . GLU A 1 1574 ? 188.615 204.362 237.702 1.00 17.63 ? 1574 GLU A O     1 
ATOM   999   C  CB    . GLU A 1 1574 ? 189.436 203.946 234.593 1.00 12.79 ? 1574 GLU A CB    1 
ATOM   1000  C  CG    . GLU A 1 1574 ? 190.698 204.388 235.334 1.00 14.67 ? 1574 GLU A CG    1 
ATOM   1001  C  CD    . GLU A 1 1574 ? 191.220 203.350 236.320 1.00 23.49 ? 1574 GLU A CD    1 
ATOM   1002  O  OE1   . GLU A 1 1574 ? 191.065 202.135 236.065 1.00 27.07 ? 1574 GLU A OE1   1 
ATOM   1003  O  OE2   . GLU A 1 1574 ? 191.789 203.751 237.357 1.00 19.21 ? 1574 GLU A OE2   1 
ATOM   1004  N  N     . PHE A 1 1575 ? 187.179 205.468 236.368 1.00 12.44 ? 1575 PHE A N     1 
ATOM   1005  C  CA    . PHE A 1 1575 ? 186.826 206.414 237.420 1.00 11.32 ? 1575 PHE A CA    1 
ATOM   1006  C  C     . PHE A 1 1575 ? 186.117 205.711 238.571 1.00 10.68 ? 1575 PHE A C     1 
ATOM   1007  O  O     . PHE A 1 1575 ? 186.488 205.880 239.737 1.00 8.84  ? 1575 PHE A O     1 
ATOM   1008  C  CB    . PHE A 1 1575 ? 185.955 207.537 236.852 1.00 11.44 ? 1575 PHE A CB    1 
ATOM   1009  C  CG    . PHE A 1 1575 ? 185.385 208.451 237.898 1.00 8.88  ? 1575 PHE A CG    1 
ATOM   1010  C  CD1   . PHE A 1 1575 ? 186.140 209.495 238.408 1.00 9.87  ? 1575 PHE A CD1   1 
ATOM   1011  C  CD2   . PHE A 1 1575 ? 184.096 208.273 238.369 1.00 7.40  ? 1575 PHE A CD2   1 
ATOM   1012  C  CE1   . PHE A 1 1575 ? 185.622 210.337 239.370 1.00 7.42  ? 1575 PHE A CE1   1 
ATOM   1013  C  CE2   . PHE A 1 1575 ? 183.575 209.111 239.330 1.00 6.80  ? 1575 PHE A CE2   1 
ATOM   1014  C  CZ    . PHE A 1 1575 ? 184.337 210.147 239.829 1.00 6.24  ? 1575 PHE A CZ    1 
ATOM   1015  N  N     . LEU A 1 1576 ? 185.103 204.899 238.257 1.00 17.90 ? 1576 LEU A N     1 
ATOM   1016  C  CA    . LEU A 1 1576 ? 184.366 204.188 239.298 1.00 15.98 ? 1576 LEU A CA    1 
ATOM   1017  C  C     . LEU A 1 1576 ? 185.248 203.193 240.041 1.00 14.28 ? 1576 LEU A C     1 
ATOM   1018  O  O     . LEU A 1 1576 ? 185.082 203.005 241.251 1.00 16.74 ? 1576 LEU A O     1 
ATOM   1019  C  CB    . LEU A 1 1576 ? 183.154 203.476 238.696 1.00 14.71 ? 1576 LEU A CB    1 
ATOM   1020  C  CG    . LEU A 1 1576 ? 181.993 204.353 238.222 1.00 16.38 ? 1576 LEU A CG    1 
ATOM   1021  C  CD1   . LEU A 1 1576 ? 180.894 203.508 237.602 1.00 20.16 ? 1576 LEU A CD1   1 
ATOM   1022  C  CD2   . LEU A 1 1576 ? 181.439 205.176 239.371 1.00 18.87 ? 1576 LEU A CD2   1 
ATOM   1023  N  N     . ALA A 1 1577 ? 186.177 202.539 239.340 1.00 12.99 ? 1577 ALA A N     1 
ATOM   1024  C  CA    . ALA A 1 1577 ? 187.102 201.632 240.010 1.00 15.29 ? 1577 ALA A CA    1 
ATOM   1025  C  C     . ALA A 1 1577 ? 187.964 202.378 241.021 1.00 16.86 ? 1577 ALA A C     1 
ATOM   1026  O  O     . ALA A 1 1577 ? 188.186 201.897 242.138 1.00 17.89 ? 1577 ALA A O     1 
ATOM   1027  C  CB    . ALA A 1 1577 ? 187.976 200.918 238.981 1.00 11.88 ? 1577 ALA A CB    1 
ATOM   1028  N  N     . LEU A 1 1578 ? 188.449 203.563 240.648 1.00 12.69 ? 1578 LEU A N     1 
ATOM   1029  C  CA    . LEU A 1 1578 ? 189.237 204.364 241.576 1.00 14.46 ? 1578 LEU A CA    1 
ATOM   1030  C  C     . LEU A 1 1578 ? 188.369 204.929 242.693 1.00 14.39 ? 1578 LEU A C     1 
ATOM   1031  O  O     . LEU A 1 1578 ? 188.852 205.154 243.808 1.00 15.57 ? 1578 LEU A O     1 
ATOM   1032  C  CB    . LEU A 1 1578 ? 189.956 205.472 240.810 1.00 12.35 ? 1578 LEU A CB    1 
ATOM   1033  C  CG    . LEU A 1 1578 ? 190.900 206.413 241.548 1.00 12.57 ? 1578 LEU A CG    1 
ATOM   1034  C  CD1   . LEU A 1 1578 ? 192.067 205.656 242.146 1.00 16.56 ? 1578 LEU A CD1   1 
ATOM   1035  C  CD2   . LEU A 1 1578 ? 191.407 207.424 240.553 1.00 13.40 ? 1578 LEU A CD2   1 
ATOM   1036  N  N     . MET A 1 1579 ? 187.082 205.160 242.417 1.00 15.47 ? 1579 MET A N     1 
ATOM   1037  C  CA    . MET A 1 1579 ? 186.158 205.579 243.467 1.00 11.02 ? 1579 MET A CA    1 
ATOM   1038  C  C     . MET A 1 1579 ? 185.985 204.500 244.526 1.00 13.54 ? 1579 MET A C     1 
ATOM   1039  O  O     . MET A 1 1579 ? 185.925 204.810 245.721 1.00 16.69 ? 1579 MET A O     1 
ATOM   1040  C  CB    . MET A 1 1579 ? 184.798 205.932 242.867 1.00 14.90 ? 1579 MET A CB    1 
ATOM   1041  C  CG    . MET A 1 1579 ? 184.809 207.134 241.954 1.00 16.72 ? 1579 MET A CG    1 
ATOM   1042  S  SD    . MET A 1 1579 ? 185.323 208.640 242.782 1.00 33.42 ? 1579 MET A SD    1 
ATOM   1043  C  CE    . MET A 1 1579 ? 183.922 208.905 243.855 1.00 29.41 ? 1579 MET A CE    1 
ATOM   1044  N  N     . LYS A 1 1580 ? 185.891 203.235 244.107 1.00 14.74 ? 1580 LYS A N     1 
ATOM   1045  C  CA    . LYS A 1 1580 ? 185.688 202.149 245.060 1.00 18.01 ? 1580 LYS A CA    1 
ATOM   1046  C  C     . LYS A 1 1580 ? 186.883 202.001 245.994 1.00 19.21 ? 1580 LYS A C     1 
ATOM   1047  O  O     . LYS A 1 1580 ? 186.717 201.699 247.181 1.00 22.13 ? 1580 LYS A O     1 
ATOM   1048  C  CB    . LYS A 1 1580 ? 185.416 200.843 244.311 1.00 18.13 ? 1580 LYS A CB    1 
ATOM   1049  C  CG    . LYS A 1 1580 ? 185.048 199.675 245.211 1.00 24.69 ? 1580 LYS A CG    1 
ATOM   1050  C  CD    . LYS A 1 1580 ? 184.786 198.414 244.404 1.00 24.94 ? 1580 LYS A CD    1 
ATOM   1051  C  CE    . LYS A 1 1580 ? 183.486 198.517 243.624 1.00 25.59 ? 1580 LYS A CE    1 
ATOM   1052  N  NZ    . LYS A 1 1580 ? 182.300 198.550 244.524 1.00 31.76 ? 1580 LYS A NZ    1 
ATOM   1053  N  N     . LYS A 1 1581 ? 188.096 202.206 245.475 1.00 17.42 ? 1581 LYS A N     1 
ATOM   1054  C  CA    . LYS A 1 1581 ? 189.279 202.177 246.331 1.00 15.33 ? 1581 LYS A CA    1 
ATOM   1055  C  C     . LYS A 1 1581 ? 189.224 203.277 247.384 1.00 17.11 ? 1581 LYS A C     1 
ATOM   1056  O  O     . LYS A 1 1581 ? 189.581 203.051 248.545 1.00 21.18 ? 1581 LYS A O     1 
ATOM   1057  C  CB    . LYS A 1 1581 ? 190.548 202.314 245.490 1.00 13.19 ? 1581 LYS A CB    1 
ATOM   1058  C  CG    . LYS A 1 1581 ? 190.962 201.047 244.769 1.00 14.77 ? 1581 LYS A CG    1 
ATOM   1059  C  CD    . LYS A 1 1581 ? 192.201 201.281 243.924 1.00 14.64 ? 1581 LYS A CD    1 
ATOM   1060  C  CE    . LYS A 1 1581 ? 191.859 201.988 242.627 1.00 15.90 ? 1581 LYS A CE    1 
ATOM   1061  N  NZ    . LYS A 1 1581 ? 192.398 201.265 241.442 1.00 18.54 ? 1581 LYS A NZ    1 
ATOM   1062  N  N     . VAL A 1 1582 ? 188.783 204.473 246.993 1.00 13.57 ? 1582 VAL A N     1 
ATOM   1063  C  CA    . VAL A 1 1582 ? 188.663 205.577 247.941 1.00 12.49 ? 1582 VAL A CA    1 
ATOM   1064  C  C     . VAL A 1 1582 ? 187.652 205.233 249.026 1.00 16.49 ? 1582 VAL A C     1 
ATOM   1065  O  O     . VAL A 1 1582 ? 187.827 205.594 250.197 1.00 19.46 ? 1582 VAL A O     1 
ATOM   1066  C  CB    . VAL A 1 1582 ? 188.291 206.876 247.202 1.00 13.56 ? 1582 VAL A CB    1 
ATOM   1067  C  CG1   . VAL A 1 1582 ? 188.041 208.008 248.189 1.00 8.75  ? 1582 VAL A CG1   1 
ATOM   1068  C  CG2   . VAL A 1 1582 ? 189.383 207.256 246.214 1.00 10.43 ? 1582 VAL A CG2   1 
ATOM   1069  N  N     . SER A 1 1583 ? 186.579 204.529 248.657 1.00 19.90 ? 1583 SER A N     1 
ATOM   1070  C  CA    . SER A 1 1583 ? 185.571 204.145 249.640 1.00 18.38 ? 1583 SER A CA    1 
ATOM   1071  C  C     . SER A 1 1583 ? 186.154 203.212 250.697 1.00 25.58 ? 1583 SER A C     1 
ATOM   1072  O  O     . SER A 1 1583 ? 185.838 203.339 251.887 1.00 30.74 ? 1583 SER A O     1 
ATOM   1073  C  CB    . SER A 1 1583 ? 184.381 203.492 248.941 1.00 22.32 ? 1583 SER A CB    1 
ATOM   1074  O  OG    . SER A 1 1583 ? 183.322 203.259 249.853 1.00 32.97 ? 1583 SER A OG    1 
ATOM   1075  N  N     . LYS A 1 1584 ? 186.994 202.263 250.282 1.00 16.72 ? 1584 LYS A N     1 
ATOM   1076  C  CA    . LYS A 1 1584 ? 187.609 201.347 251.239 1.00 20.25 ? 1584 LYS A CA    1 
ATOM   1077  C  C     . LYS A 1 1584 ? 188.534 202.089 252.197 1.00 26.24 ? 1584 LYS A C     1 
ATOM   1078  O  O     . LYS A 1 1584 ? 188.502 201.862 253.411 1.00 23.81 ? 1584 LYS A O     1 
ATOM   1079  C  CB    . LYS A 1 1584 ? 188.373 200.248 250.499 1.00 20.52 ? 1584 LYS A CB    1 
ATOM   1080  C  CG    . LYS A 1 1584 ? 187.573 199.548 249.422 1.00 22.30 ? 1584 LYS A CG    1 
ATOM   1081  C  CD    . LYS A 1 1584 ? 186.343 198.871 250.003 1.00 27.61 ? 1584 LYS A CD    1 
ATOM   1082  C  CE    . LYS A 1 1584 ? 185.557 198.142 248.929 1.00 28.44 ? 1584 LYS A CE    1 
ATOM   1083  N  NZ    . LYS A 1 1584 ? 186.394 197.134 248.222 1.00 29.68 ? 1584 LYS A NZ    1 
ATOM   1084  N  N     . SER A 1 1585 ? 189.362 202.990 251.666 1.00 21.71 ? 1585 SER A N     1 
ATOM   1085  C  CA    . SER A 1 1585 ? 190.332 203.748 252.455 1.00 20.62 ? 1585 SER A CA    1 
ATOM   1086  C  C     . SER A 1 1585 ? 190.107 205.233 252.205 1.00 19.91 ? 1585 SER A C     1 
ATOM   1087  O  O     . SER A 1 1585 ? 190.786 205.841 251.363 1.00 21.97 ? 1585 SER A O     1 
ATOM   1088  C  CB    . SER A 1 1585 ? 191.762 203.344 252.103 1.00 23.16 ? 1585 SER A CB    1 
ATOM   1089  O  OG    . SER A 1 1585 ? 192.067 203.678 250.759 1.00 33.13 ? 1585 SER A OG    1 
ATOM   1090  N  N     . PRO A 1 1586 ? 189.166 205.860 252.914 1.00 18.84 ? 1586 PRO A N     1 
ATOM   1091  C  CA    . PRO A 1 1586 ? 188.921 207.292 252.713 1.00 19.19 ? 1586 PRO A CA    1 
ATOM   1092  C  C     . PRO A 1 1586 ? 189.974 208.192 253.339 1.00 22.49 ? 1586 PRO A C     1 
ATOM   1093  O  O     . PRO A 1 1586 ? 189.883 209.416 253.181 1.00 21.51 ? 1586 PRO A O     1 
ATOM   1094  C  CB    . PRO A 1 1586 ? 187.551 207.503 253.366 1.00 18.31 ? 1586 PRO A CB    1 
ATOM   1095  C  CG    . PRO A 1 1586 ? 187.479 206.460 254.430 1.00 16.40 ? 1586 PRO A CG    1 
ATOM   1096  C  CD    . PRO A 1 1586 ? 188.376 205.312 254.030 1.00 19.16 ? 1586 PRO A CD    1 
ATOM   1097  N  N     . LEU A 1 1587 ? 190.955 207.628 254.040 1.00 22.55 ? 1587 LEU A N     1 
ATOM   1098  C  CA    . LEU A 1 1587 ? 192.043 208.423 254.589 1.00 19.54 ? 1587 LEU A CA    1 
ATOM   1099  C  C     . LEU A 1 1587 ? 192.847 209.054 253.458 1.00 16.41 ? 1587 LEU A C     1 
ATOM   1100  O  O     . LEU A 1 1587 ? 193.144 208.406 252.451 1.00 18.74 ? 1587 LEU A O     1 
ATOM   1101  C  CB    . LEU A 1 1587 ? 192.946 207.547 255.460 1.00 20.35 ? 1587 LEU A CB    1 
ATOM   1102  C  CG    . LEU A 1 1587 ? 194.101 208.230 256.192 1.00 19.85 ? 1587 LEU A CG    1 
ATOM   1103  C  CD1   . LEU A 1 1587 ? 193.562 209.241 257.190 1.00 25.31 ? 1587 LEU A CD1   1 
ATOM   1104  C  CD2   . LEU A 1 1587 ? 194.988 207.207 256.884 1.00 23.70 ? 1587 LEU A CD2   1 
ATOM   1105  N  N     . VAL A 1 1588 ? 193.199 210.329 253.631 1.00 16.51 ? 1588 VAL A N     1 
ATOM   1106  C  CA    . VAL A 1 1588 ? 193.858 211.074 252.560 1.00 17.19 ? 1588 VAL A CA    1 
ATOM   1107  C  C     . VAL A 1 1588 ? 195.215 210.465 252.232 1.00 17.11 ? 1588 VAL A C     1 
ATOM   1108  O  O     . VAL A 1 1588 ? 195.585 210.335 251.058 1.00 19.31 ? 1588 VAL A O     1 
ATOM   1109  C  CB    . VAL A 1 1588 ? 193.977 212.562 252.940 1.00 14.66 ? 1588 VAL A CB    1 
ATOM   1110  C  CG1   . VAL A 1 1588 ? 194.819 213.307 251.919 1.00 10.48 ? 1588 VAL A CG1   1 
ATOM   1111  C  CG2   . VAL A 1 1588 ? 192.599 213.187 253.054 1.00 17.54 ? 1588 VAL A CG2   1 
ATOM   1112  N  N     . MET A 1 1589 ? 195.978 210.080 253.256 1.00 21.59 ? 1589 MET A N     1 
ATOM   1113  C  CA    . MET A 1 1589 ? 197.300 209.506 253.020 1.00 18.42 ? 1589 MET A CA    1 
ATOM   1114  C  C     . MET A 1 1589 ? 197.206 208.199 252.240 1.00 19.30 ? 1589 MET A C     1 
ATOM   1115  O  O     . MET A 1 1589 ? 198.025 207.941 251.351 1.00 19.82 ? 1589 MET A O     1 
ATOM   1116  C  CB    . MET A 1 1589 ? 198.024 209.295 254.348 1.00 14.14 ? 1589 MET A CB    1 
ATOM   1117  C  CG    . MET A 1 1589 ? 198.540 210.579 254.982 1.00 19.41 ? 1589 MET A CG    1 
ATOM   1118  S  SD    . MET A 1 1589 ? 199.172 211.761 253.775 1.00 39.80 ? 1589 MET A SD    1 
ATOM   1119  C  CE    . MET A 1 1589 ? 200.813 211.112 253.486 1.00 20.09 ? 1589 MET A CE    1 
ATOM   1120  N  N     . ASP A 1 1590 ? 196.215 207.363 252.560 1.00 20.15 ? 1590 ASP A N     1 
ATOM   1121  C  CA    . ASP A 1 1590 ? 196.026 206.126 251.808 1.00 17.25 ? 1590 ASP A CA    1 
ATOM   1122  C  C     . ASP A 1 1590 ? 195.691 206.408 250.350 1.00 17.46 ? 1590 ASP A C     1 
ATOM   1123  O  O     . ASP A 1 1590 ? 196.196 205.733 249.445 1.00 21.31 ? 1590 ASP A O     1 
ATOM   1124  C  CB    . ASP A 1 1590 ? 194.933 205.279 252.456 1.00 20.10 ? 1590 ASP A CB    1 
ATOM   1125  C  CG    . ASP A 1 1590 ? 195.347 204.722 253.803 1.00 32.95 ? 1590 ASP A CG    1 
ATOM   1126  O  OD1   . ASP A 1 1590 ? 196.560 204.495 254.006 1.00 35.20 ? 1590 ASP A OD1   1 
ATOM   1127  O  OD2   . ASP A 1 1590 ? 194.463 204.510 254.658 1.00 38.73 ? 1590 ASP A OD2   1 
ATOM   1128  N  N     . VAL A 1 1591 ? 194.834 207.402 250.100 1.00 12.12 ? 1591 VAL A N     1 
ATOM   1129  C  CA    . VAL A 1 1591 ? 194.532 207.790 248.726 1.00 12.26 ? 1591 VAL A CA    1 
ATOM   1130  C  C     . VAL A 1 1591 ? 195.774 208.352 248.049 1.00 14.88 ? 1591 VAL A C     1 
ATOM   1131  O  O     . VAL A 1 1591 ? 196.049 208.060 246.878 1.00 20.39 ? 1591 VAL A O     1 
ATOM   1132  C  CB    . VAL A 1 1591 ? 193.364 208.796 248.698 1.00 13.93 ? 1591 VAL A CB    1 
ATOM   1133  C  CG1   . VAL A 1 1591 ? 193.083 209.244 247.275 1.00 9.37  ? 1591 VAL A CG1   1 
ATOM   1134  C  CG2   . VAL A 1 1591 ? 192.120 208.180 249.314 1.00 13.86 ? 1591 VAL A CG2   1 
ATOM   1135  N  N     . LEU A 1 1592 ? 196.549 209.162 248.774 1.00 14.12 ? 1592 LEU A N     1 
ATOM   1136  C  CA    . LEU A 1 1592 ? 197.760 209.748 248.212 1.00 16.61 ? 1592 LEU A CA    1 
ATOM   1137  C  C     . LEU A 1 1592 ? 198.805 208.697 247.859 1.00 13.96 ? 1592 LEU A C     1 
ATOM   1138  O  O     . LEU A 1 1592 ? 199.637 208.939 246.978 1.00 15.26 ? 1592 LEU A O     1 
ATOM   1139  C  CB    . LEU A 1 1592 ? 198.349 210.767 249.193 1.00 19.30 ? 1592 LEU A CB    1 
ATOM   1140  C  CG    . LEU A 1 1592 ? 199.605 211.527 248.763 1.00 16.60 ? 1592 LEU A CG    1 
ATOM   1141  C  CD1   . LEU A 1 1592 ? 199.280 212.518 247.657 1.00 10.13 ? 1592 LEU A CD1   1 
ATOM   1142  C  CD2   . LEU A 1 1592 ? 200.250 212.225 249.947 1.00 15.51 ? 1592 LEU A CD2   1 
ATOM   1143  N  N     . ASN A 1 1593 ? 198.777 207.539 248.514 1.00 18.56 ? 1593 ASN A N     1 
ATOM   1144  C  CA    . ASN A 1 1593 ? 199.736 206.471 248.268 1.00 17.46 ? 1593 ASN A CA    1 
ATOM   1145  C  C     . ASN A 1 1593 ? 199.250 205.448 247.247 1.00 18.78 ? 1593 ASN A C     1 
ATOM   1146  O  O     . ASN A 1 1593 ? 199.955 204.468 246.992 1.00 22.36 ? 1593 ASN A O     1 
ATOM   1147  C  CB    . ASN A 1 1593 ? 200.079 205.761 249.581 1.00 17.85 ? 1593 ASN A CB    1 
ATOM   1148  C  CG    . ASN A 1 1593 ? 200.728 206.687 250.591 1.00 26.08 ? 1593 ASN A CG    1 
ATOM   1149  O  OD1   . ASN A 1 1593 ? 200.958 207.863 250.315 1.00 23.67 ? 1593 ASN A OD1   1 
ATOM   1150  N  ND2   . ASN A 1 1593 ? 201.021 206.160 251.774 1.00 24.55 ? 1593 ASN A ND2   1 
ATOM   1151  N  N     . ILE A 1 1594 ? 198.066 205.646 246.662 1.00 19.26 ? 1594 ILE A N     1 
ATOM   1152  C  CA    . ILE A 1 1594 ? 197.600 204.744 245.616 1.00 17.05 ? 1594 ILE A CA    1 
ATOM   1153  C  C     . ILE A 1 1594 ? 198.531 204.848 244.420 1.00 16.27 ? 1594 ILE A C     1 
ATOM   1154  O  O     . ILE A 1 1594 ? 198.891 205.950 243.990 1.00 21.73 ? 1594 ILE A O     1 
ATOM   1155  C  CB    . ILE A 1 1594 ? 196.143 205.066 245.241 1.00 14.12 ? 1594 ILE A CB    1 
ATOM   1156  C  CG1   . ILE A 1 1594 ? 195.226 204.852 246.447 1.00 12.79 ? 1594 ILE A CG1   1 
ATOM   1157  C  CG2   . ILE A 1 1594 ? 195.691 204.215 244.067 1.00 11.99 ? 1594 ILE A CG2   1 
ATOM   1158  C  CD1   . ILE A 1 1594 ? 193.773 205.144 246.175 1.00 10.90 ? 1594 ILE A CD1   1 
ATOM   1159  N  N     . GLN A 1 1595 ? 198.933 203.696 243.885 1.00 18.61 ? 1595 GLN A N     1 
ATOM   1160  C  CA    . GLN A 1 1595 ? 199.961 203.663 242.854 1.00 19.11 ? 1595 GLN A CA    1 
ATOM   1161  C  C     . GLN A 1 1595 ? 199.504 204.396 241.600 1.00 14.90 ? 1595 GLN A C     1 
ATOM   1162  O  O     . GLN A 1 1595 ? 198.467 204.070 241.015 1.00 13.42 ? 1595 GLN A O     1 
ATOM   1163  C  CB    . GLN A 1 1595 ? 200.318 202.216 242.517 1.00 17.32 ? 1595 GLN A CB    1 
ATOM   1164  C  CG    . GLN A 1 1595 ? 201.430 202.074 241.495 1.00 17.62 ? 1595 GLN A CG    1 
ATOM   1165  C  CD    . GLN A 1 1595 ? 201.761 200.625 241.197 1.00 30.99 ? 1595 GLN A CD    1 
ATOM   1166  O  OE1   . GLN A 1 1595 ? 201.154 199.708 241.752 1.00 31.14 ? 1595 GLN A OE1   1 
ATOM   1167  N  NE2   . GLN A 1 1595 ? 202.732 200.408 240.317 1.00 28.97 ? 1595 GLN A NE2   1 
ATOM   1168  N  N     . GLY A 1 1596 ? 200.288 205.392 241.193 1.00 18.89 ? 1596 GLY A N     1 
ATOM   1169  C  CA    . GLY A 1 1596 ? 199.998 206.144 239.987 1.00 15.15 ? 1596 GLY A CA    1 
ATOM   1170  C  C     . GLY A 1 1596 ? 198.726 206.954 240.037 1.00 17.14 ? 1596 GLY A C     1 
ATOM   1171  O  O     . GLY A 1 1596 ? 198.172 207.282 238.986 1.00 20.06 ? 1596 GLY A O     1 
ATOM   1172  N  N     . VAL A 1 1597 ? 198.246 207.292 241.234 1.00 17.81 ? 1597 VAL A N     1 
ATOM   1173  C  CA    . VAL A 1 1597 ? 196.986 208.021 241.347 1.00 12.72 ? 1597 VAL A CA    1 
ATOM   1174  C  C     . VAL A 1 1597 ? 197.114 209.412 240.738 1.00 12.64 ? 1597 VAL A C     1 
ATOM   1175  O  O     . VAL A 1 1597 ? 196.163 209.937 240.148 1.00 18.03 ? 1597 VAL A O     1 
ATOM   1176  C  CB    . VAL A 1 1597 ? 196.514 208.062 242.815 1.00 13.98 ? 1597 VAL A CB    1 
ATOM   1177  C  CG1   . VAL A 1 1597 ? 197.320 209.057 243.635 1.00 14.34 ? 1597 VAL A CG1   1 
ATOM   1178  C  CG2   . VAL A 1 1597 ? 195.030 208.387 242.884 1.00 16.70 ? 1597 VAL A CG2   1 
ATOM   1179  N  N     . GLN A 1 1598 ? 198.291 210.031 240.862 1.00 9.79  ? 1598 GLN A N     1 
ATOM   1180  C  CA    . GLN A 1 1598 ? 198.517 211.330 240.240 1.00 7.98  ? 1598 GLN A CA    1 
ATOM   1181  C  C     . GLN A 1 1598 ? 198.416 211.236 238.724 1.00 11.44 ? 1598 GLN A C     1 
ATOM   1182  O  O     . GLN A 1 1598 ? 197.770 212.067 238.076 1.00 14.46 ? 1598 GLN A O     1 
ATOM   1183  C  CB    . GLN A 1 1598 ? 199.879 211.879 240.655 1.00 9.93  ? 1598 GLN A CB    1 
ATOM   1184  C  CG    . GLN A 1 1598 ? 200.127 213.310 240.220 1.00 7.23  ? 1598 GLN A CG    1 
ATOM   1185  C  CD    . GLN A 1 1598 ? 199.098 214.270 240.770 1.00 9.60  ? 1598 GLN A CD    1 
ATOM   1186  O  OE1   . GLN A 1 1598 ? 198.941 214.395 241.981 1.00 18.28 ? 1598 GLN A OE1   1 
ATOM   1187  N  NE2   . GLN A 1 1598 ? 198.402 214.968 239.882 1.00 4.80  ? 1598 GLN A NE2   1 
ATOM   1188  N  N     . ARG A 1 1599 ? 199.050 210.219 238.139 1.00 16.93 ? 1599 ARG A N     1 
ATOM   1189  C  CA    . ARG A 1 1599 ? 199.014 210.074 236.689 1.00 14.36 ? 1599 ARG A CA    1 
ATOM   1190  C  C     . ARG A 1 1599 ? 197.652 209.579 236.219 1.00 13.39 ? 1599 ARG A C     1 
ATOM   1191  O  O     . ARG A 1 1599 ? 197.236 209.883 235.095 1.00 14.43 ? 1599 ARG A O     1 
ATOM   1192  C  CB    . ARG A 1 1599 ? 200.141 209.138 236.239 1.00 11.98 ? 1599 ARG A CB    1 
ATOM   1193  C  CG    . ARG A 1 1599 ? 200.353 209.037 234.730 1.00 17.19 ? 1599 ARG A CG    1 
ATOM   1194  C  CD    . ARG A 1 1599 ? 199.528 207.923 234.106 1.00 20.86 ? 1599 ARG A CD    1 
ATOM   1195  N  NE    . ARG A 1 1599 ? 199.883 206.615 234.640 1.00 26.89 ? 1599 ARG A NE    1 
ATOM   1196  C  CZ    . ARG A 1 1599 ? 199.136 205.527 234.511 1.00 35.27 ? 1599 ARG A CZ    1 
ATOM   1197  N  NH1   . ARG A 1 1599 ? 197.962 205.565 233.901 1.00 25.34 ? 1599 ARG A NH1   1 
ATOM   1198  N  NH2   . ARG A 1 1599 ? 199.574 204.376 235.011 1.00 24.13 ? 1599 ARG A NH2   1 
ATOM   1199  N  N     . SER A 1 1600 ? 196.942 208.828 237.064 1.00 11.11 ? 1600 SER A N     1 
ATOM   1200  C  CA    . SER A 1 1600 ? 195.601 208.376 236.703 1.00 10.83 ? 1600 SER A CA    1 
ATOM   1201  C  C     . SER A 1 1600 ? 194.649 209.555 236.549 1.00 17.03 ? 1600 SER A C     1 
ATOM   1202  O  O     . SER A 1 1600 ? 193.886 209.630 235.579 1.00 15.75 ? 1600 SER A O     1 
ATOM   1203  C  CB    . SER A 1 1600 ? 195.077 207.397 237.753 1.00 9.55  ? 1600 SER A CB    1 
ATOM   1204  O  OG    . SER A 1 1600 ? 195.861 206.219 237.793 1.00 16.20 ? 1600 SER A OG    1 
ATOM   1205  N  N     . LEU A 1 1601 ? 194.685 210.495 237.497 1.00 9.31  ? 1601 LEU A N     1 
ATOM   1206  C  CA    . LEU A 1 1601 ? 193.835 211.675 237.393 1.00 8.10  ? 1601 LEU A CA    1 
ATOM   1207  C  C     . LEU A 1 1601 ? 194.251 212.564 236.233 1.00 10.65 ? 1601 LEU A C     1 
ATOM   1208  O  O     . LEU A 1 1601 ? 193.398 213.154 235.562 1.00 16.00 ? 1601 LEU A O     1 
ATOM   1209  C  CB    . LEU A 1 1601 ? 193.847 212.477 238.695 1.00 11.69 ? 1601 LEU A CB    1 
ATOM   1210  C  CG    . LEU A 1 1601 ? 192.842 212.019 239.744 1.00 6.55  ? 1601 LEU A CG    1 
ATOM   1211  C  CD1   . LEU A 1 1601 ? 191.469 212.213 239.129 1.00 9.73  ? 1601 LEU A CD1   1 
ATOM   1212  C  CD2   . LEU A 1 1601 ? 193.050 210.591 240.194 1.00 11.63 ? 1601 LEU A CD2   1 
ATOM   1213  N  N     . GLU A 1 1602 ? 195.556 212.683 235.992 1.00 11.33 ? 1602 GLU A N     1 
ATOM   1214  C  CA    . GLU A 1 1602 ? 196.018 213.490 234.870 1.00 12.01 ? 1602 GLU A CA    1 
ATOM   1215  C  C     . GLU A 1 1602 ? 195.487 212.938 233.555 1.00 9.43  ? 1602 GLU A C     1 
ATOM   1216  O  O     . GLU A 1 1602 ? 195.085 213.701 232.669 1.00 7.47  ? 1602 GLU A O     1 
ATOM   1217  C  CB    . GLU A 1 1602 ? 197.544 213.551 234.863 1.00 14.88 ? 1602 GLU A CB    1 
ATOM   1218  C  CG    . GLU A 1 1602 ? 198.127 214.437 233.775 1.00 19.14 ? 1602 GLU A CG    1 
ATOM   1219  C  CD    . GLU A 1 1602 ? 199.639 214.513 233.831 1.00 28.04 ? 1602 GLU A CD    1 
ATOM   1220  O  OE1   . GLU A 1 1602 ? 200.239 213.854 234.708 1.00 31.37 ? 1602 GLU A OE1   1 
ATOM   1221  O  OE2   . GLU A 1 1602 ? 200.229 215.236 233.001 1.00 26.19 ? 1602 GLU A OE2   1 
ATOM   1222  N  N     . ARG A 1 1603 ? 195.460 211.611 233.416 1.00 6.55  ? 1603 ARG A N     1 
ATOM   1223  C  CA    . ARG A 1 1603 ? 194.891 211.009 232.217 1.00 10.71 ? 1603 ARG A CA    1 
ATOM   1224  C  C     . ARG A 1 1603 ? 193.373 211.149 232.197 1.00 11.16 ? 1603 ARG A C     1 
ATOM   1225  O  O     . ARG A 1 1603 ? 192.781 211.398 231.141 1.00 12.27 ? 1603 ARG A O     1 
ATOM   1226  C  CB    . ARG A 1 1603 ? 195.292 209.537 232.122 1.00 11.13 ? 1603 ARG A CB    1 
ATOM   1227  C  CG    . ARG A 1 1603 ? 194.720 208.838 230.904 1.00 12.89 ? 1603 ARG A CG    1 
ATOM   1228  C  CD    . ARG A 1 1603 ? 195.340 207.474 230.693 1.00 14.15 ? 1603 ARG A CD    1 
ATOM   1229  N  NE    . ARG A 1 1603 ? 194.333 206.478 230.343 1.00 20.57 ? 1603 ARG A NE    1 
ATOM   1230  C  CZ    . ARG A 1 1603 ? 193.665 205.746 231.222 1.00 16.67 ? 1603 ARG A CZ    1 
ATOM   1231  N  NH1   . ARG A 1 1603 ? 193.858 205.877 232.524 1.00 13.24 ? 1603 ARG A NH1   1 
ATOM   1232  N  NH2   . ARG A 1 1603 ? 192.780 204.856 230.783 1.00 16.85 ? 1603 ARG A NH2   1 
ATOM   1233  N  N     . LEU A 1 1604 ? 192.727 210.993 233.357 1.00 8.80  ? 1604 LEU A N     1 
ATOM   1234  C  CA    . LEU A 1 1604 ? 191.278 211.151 233.425 1.00 8.05  ? 1604 LEU A CA    1 
ATOM   1235  C  C     . LEU A 1 1604 ? 190.861 212.566 233.048 1.00 7.46  ? 1604 LEU A C     1 
ATOM   1236  O  O     . LEU A 1 1604 ? 189.874 212.759 232.330 1.00 10.07 ? 1604 LEU A O     1 
ATOM   1237  C  CB    . LEU A 1 1604 ? 190.771 210.804 234.825 1.00 7.90  ? 1604 LEU A CB    1 
ATOM   1238  C  CG    . LEU A 1 1604 ? 190.742 209.331 235.241 1.00 6.14  ? 1604 LEU A CG    1 
ATOM   1239  C  CD1   . LEU A 1 1604 ? 190.181 209.178 236.642 1.00 6.44  ? 1604 LEU A CD1   1 
ATOM   1240  C  CD2   . LEU A 1 1604 ? 189.955 208.494 234.258 1.00 8.77  ? 1604 LEU A CD2   1 
ATOM   1241  N  N     . ALA A 1 1605 ? 191.598 213.569 233.527 1.00 7.02  ? 1605 ALA A N     1 
ATOM   1242  C  CA    . ALA A 1 1605 ? 191.274 214.953 233.193 1.00 4.96  ? 1605 ALA A CA    1 
ATOM   1243  C  C     . ALA A 1 1605 ? 191.405 215.205 231.696 1.00 9.01  ? 1605 ALA A C     1 
ATOM   1244  O  O     . ALA A 1 1605 ? 190.524 215.813 231.078 1.00 11.78 ? 1605 ALA A O     1 
ATOM   1245  C  CB    . ALA A 1 1605 ? 192.173 215.905 233.981 1.00 3.33  ? 1605 ALA A CB    1 
ATOM   1246  N  N     . ASP A 1 1606 ? 192.502 214.738 231.097 1.00 9.93  ? 1606 ASP A N     1 
ATOM   1247  C  CA    . ASP A 1 1606 ? 192.701 214.937 229.665 1.00 8.31  ? 1606 ASP A CA    1 
ATOM   1248  C  C     . ASP A 1 1606 ? 191.665 214.174 228.848 1.00 10.08 ? 1606 ASP A C     1 
ATOM   1249  O  O     . ASP A 1 1606 ? 191.104 214.710 227.886 1.00 8.68  ? 1606 ASP A O     1 
ATOM   1250  C  CB    . ASP A 1 1606 ? 194.115 214.513 229.272 1.00 14.13 ? 1606 ASP A CB    1 
ATOM   1251  C  CG    . ASP A 1 1606 ? 194.326 214.513 227.771 1.00 26.68 ? 1606 ASP A CG    1 
ATOM   1252  O  OD1   . ASP A 1 1606 ? 194.259 215.601 227.160 1.00 20.89 ? 1606 ASP A OD1   1 
ATOM   1253  O  OD2   . ASP A 1 1606 ? 194.552 213.425 227.202 1.00 27.39 ? 1606 ASP A OD2   1 
ATOM   1254  N  N     . LEU A 1 1607 ? 191.401 212.920 229.221 1.00 9.15  ? 1607 LEU A N     1 
ATOM   1255  C  CA    . LEU A 1 1607 ? 190.455 212.106 228.468 1.00 6.26  ? 1607 LEU A CA    1 
ATOM   1256  C  C     . LEU A 1 1607 ? 189.036 212.655 228.564 1.00 8.87  ? 1607 LEU A C     1 
ATOM   1257  O  O     . LEU A 1 1607 ? 188.308 212.685 227.566 1.00 14.20 ? 1607 LEU A O     1 
ATOM   1258  C  CB    . LEU A 1 1607 ? 190.507 210.662 228.958 1.00 9.42  ? 1607 LEU A CB    1 
ATOM   1259  C  CG    . LEU A 1 1607 ? 191.690 209.793 228.530 1.00 13.56 ? 1607 LEU A CG    1 
ATOM   1260  C  CD1   . LEU A 1 1607 ? 191.449 208.353 228.948 1.00 11.09 ? 1607 LEU A CD1   1 
ATOM   1261  C  CD2   . LEU A 1 1607 ? 191.930 209.892 227.030 1.00 7.28  ? 1607 LEU A CD2   1 
ATOM   1262  N  N     . LEU A 1 1608 ? 188.621 213.086 229.760 1.00 8.79  ? 1608 LEU A N     1 
ATOM   1263  C  CA    . LEU A 1 1608 ? 187.284 213.654 229.911 1.00 5.20  ? 1608 LEU A CA    1 
ATOM   1264  C  C     . LEU A 1 1608 ? 187.143 214.962 229.145 1.00 7.48  ? 1608 LEU A C     1 
ATOM   1265  O  O     . LEU A 1 1608 ? 186.049 215.290 228.673 1.00 10.05 ? 1608 LEU A O     1 
ATOM   1266  C  CB    . LEU A 1 1608 ? 186.965 213.869 231.390 1.00 4.50  ? 1608 LEU A CB    1 
ATOM   1267  C  CG    . LEU A 1 1608 ? 186.587 212.632 232.207 1.00 4.15  ? 1608 LEU A CG    1 
ATOM   1268  C  CD1   . LEU A 1 1608 ? 186.629 212.944 233.696 1.00 2.84  ? 1608 LEU A CD1   1 
ATOM   1269  C  CD2   . LEU A 1 1608 ? 185.223 212.101 231.805 1.00 2.23  ? 1608 LEU A CD2   1 
ATOM   1270  N  N     . GLY A 1 1609 ? 188.231 215.721 229.015 1.00 6.18  ? 1609 GLY A N     1 
ATOM   1271  C  CA    . GLY A 1 1609 ? 188.190 216.930 228.214 1.00 6.39  ? 1609 GLY A CA    1 
ATOM   1272  C  C     . GLY A 1 1609 ? 187.962 216.660 226.742 1.00 12.73 ? 1609 GLY A C     1 
ATOM   1273  O  O     . GLY A 1 1609 ? 187.275 217.430 226.066 1.00 14.08 ? 1609 GLY A O     1 
ATOM   1274  N  N     . LYS A 1 1610 ? 188.536 215.574 226.222 1.00 13.97 ? 1610 LYS A N     1 
ATOM   1275  C  CA    . LYS A 1 1610 ? 188.323 215.219 224.822 1.00 11.36 ? 1610 LYS A CA    1 
ATOM   1276  C  C     . LYS A 1 1610 ? 186.869 214.855 224.558 1.00 11.53 ? 1610 LYS A C     1 
ATOM   1277  O  O     . LYS A 1 1610 ? 186.304 215.239 223.528 1.00 17.33 ? 1610 LYS A O     1 
ATOM   1278  C  CB    . LYS A 1 1610 ? 189.248 214.069 224.427 1.00 12.18 ? 1610 LYS A CB    1 
ATOM   1279  C  CG    . LYS A 1 1610 ? 190.725 214.382 224.573 1.00 12.37 ? 1610 LYS A CG    1 
ATOM   1280  C  CD    . LYS A 1 1610 ? 191.149 215.471 223.604 1.00 21.43 ? 1610 LYS A CD    1 
ATOM   1281  C  CE    . LYS A 1 1610 ? 192.654 215.673 223.623 1.00 26.49 ? 1610 LYS A CE    1 
ATOM   1282  N  NZ    . LYS A 1 1610 ? 193.118 216.269 224.903 1.00 25.01 ? 1610 LYS A NZ    1 
ATOM   1283  N  N     . ILE A 1 1611 ? 186.248 214.109 225.475 1.00 10.18 ? 1611 ILE A N     1 
ATOM   1284  C  CA    . ILE A 1 1611 ? 184.827 213.796 225.347 1.00 10.40 ? 1611 ILE A CA    1 
ATOM   1285  C  C     . ILE A 1 1611 ? 183.999 215.071 225.379 1.00 9.35  ? 1611 ILE A C     1 
ATOM   1286  O  O     . ILE A 1 1611 ? 183.021 215.215 224.636 1.00 16.46 ? 1611 ILE A O     1 
ATOM   1287  C  CB    . ILE A 1 1611 ? 184.397 212.816 226.452 1.00 8.32  ? 1611 ILE A CB    1 
ATOM   1288  C  CG1   . ILE A 1 1611 ? 185.138 211.494 226.304 1.00 8.55  ? 1611 ILE A CG1   1 
ATOM   1289  C  CG2   . ILE A 1 1611 ? 182.896 212.601 226.431 1.00 6.36  ? 1611 ILE A CG2   1 
ATOM   1290  C  CD1   . ILE A 1 1611 ? 184.960 210.600 227.482 1.00 11.94 ? 1611 ILE A CD1   1 
ATOM   1291  N  N     . GLN A 1 1612 ? 184.374 216.012 226.245 1.00 10.68 ? 1612 GLN A N     1 
ATOM   1292  C  CA    . GLN A 1 1612 ? 183.655 217.277 226.336 1.00 9.77  ? 1612 GLN A CA    1 
ATOM   1293  C  C     . GLN A 1 1612 ? 183.695 218.038 225.015 1.00 11.40 ? 1612 GLN A C     1 
ATOM   1294  O  O     . GLN A 1 1612 ? 182.675 218.573 224.569 1.00 15.52 ? 1612 GLN A O     1 
ATOM   1295  C  CB    . GLN A 1 1612 ? 184.246 218.116 227.463 1.00 9.54  ? 1612 GLN A CB    1 
ATOM   1296  C  CG    . GLN A 1 1612 ? 183.536 219.416 227.718 1.00 8.53  ? 1612 GLN A CG    1 
ATOM   1297  C  CD    . GLN A 1 1612 ? 184.132 220.170 228.879 1.00 9.42  ? 1612 GLN A CD    1 
ATOM   1298  O  OE1   . GLN A 1 1612 ? 185.110 219.732 229.482 1.00 14.71 ? 1612 GLN A OE1   1 
ATOM   1299  N  NE2   . GLN A 1 1612 ? 183.554 221.317 229.195 1.00 14.91 ? 1612 GLN A NE2   1 
ATOM   1300  N  N     . LYS A 1 1613 ? 184.861 218.087 224.372 1.00 11.65 ? 1613 LYS A N     1 
ATOM   1301  C  CA    . LYS A 1 1613 ? 184.998 218.801 223.109 1.00 9.94  ? 1613 LYS A CA    1 
ATOM   1302  C  C     . LYS A 1 1613 ? 184.370 218.060 221.938 1.00 12.63 ? 1613 LYS A C     1 
ATOM   1303  O  O     . LYS A 1 1613 ? 184.239 218.643 220.857 1.00 16.66 ? 1613 LYS A O     1 
ATOM   1304  C  CB    . LYS A 1 1613 ? 186.477 219.066 222.816 1.00 13.07 ? 1613 LYS A CB    1 
ATOM   1305  C  CG    . LYS A 1 1613 ? 187.207 219.790 223.934 1.00 14.05 ? 1613 LYS A CG    1 
ATOM   1306  C  CD    . LYS A 1 1613 ? 186.923 221.281 223.920 1.00 16.40 ? 1613 LYS A CD    1 
ATOM   1307  C  CE    . LYS A 1 1613 ? 187.644 221.985 225.061 1.00 17.64 ? 1613 LYS A CE    1 
ATOM   1308  N  NZ    . LYS A 1 1613 ? 187.877 221.075 226.219 1.00 15.29 ? 1613 LYS A NZ    1 
ATOM   1309  N  N     . ALA A 1 1614 ? 183.986 216.800 222.123 1.00 12.94 ? 1614 ALA A N     1 
ATOM   1310  C  CA    . ALA A 1 1614 ? 183.374 216.003 221.071 1.00 10.97 ? 1614 ALA A CA    1 
ATOM   1311  C  C     . ALA A 1 1614 ? 181.853 216.016 221.119 1.00 12.36 ? 1614 ALA A C     1 
ATOM   1312  O  O     . ALA A 1 1614 ? 181.216 215.375 220.278 1.00 13.63 ? 1614 ALA A O     1 
ATOM   1313  C  CB    . ALA A 1 1614 ? 183.882 214.562 221.146 1.00 12.92 ? 1614 ALA A CB    1 
ATOM   1314  N  N     . LEU A 1 1615 ? 181.257 216.726 222.074 1.00 11.34 ? 1615 LEU A N     1 
ATOM   1315  C  CA    . LEU A 1 1615 ? 179.809 216.810 222.203 1.00 8.71  ? 1615 LEU A CA    1 
ATOM   1316  C  C     . LEU A 1 1615 ? 179.242 218.097 221.618 1.00 8.65  ? 1615 LEU A C     1 
ATOM   1317  O  O     . LEU A 1 1615 ? 178.081 218.424 221.879 1.00 9.68  ? 1615 LEU A O     1 
ATOM   1318  C  CB    . LEU A 1 1615 ? 179.402 216.686 223.673 1.00 9.02  ? 1615 LEU A CB    1 
ATOM   1319  C  CG    . LEU A 1 1615 ? 179.743 215.379 224.391 1.00 9.65  ? 1615 LEU A CG    1 
ATOM   1320  C  CD1   . LEU A 1 1615 ? 178.907 215.221 225.648 1.00 8.91  ? 1615 LEU A CD1   1 
ATOM   1321  C  CD2   . LEU A 1 1615 ? 179.550 214.187 223.470 1.00 11.47 ? 1615 LEU A CD2   1 
ATOM   1322  N  N     . GLY A 1 1616 ? 180.035 218.830 220.834 1.00 11.00 ? 1616 GLY A N     1 
ATOM   1323  C  CA    . GLY A 1 1616 ? 179.587 220.119 220.338 1.00 6.14  ? 1616 GLY A CA    1 
ATOM   1324  C  C     . GLY A 1 1616 ? 178.358 220.031 219.454 1.00 11.83 ? 1616 GLY A C     1 
ATOM   1325  O  O     . GLY A 1 1616 ? 177.429 220.830 219.588 1.00 13.80 ? 1616 GLY A O     1 
ATOM   1326  N  N     . GLU A 1 1617 ? 178.334 219.061 218.537 1.00 9.88  ? 1617 GLU A N     1 
ATOM   1327  C  CA    . GLU A 1 1617 ? 177.182 218.942 217.645 1.00 12.16 ? 1617 GLU A CA    1 
ATOM   1328  C  C     . GLU A 1 1617 ? 175.953 218.456 218.402 1.00 10.40 ? 1617 GLU A C     1 
ATOM   1329  O  O     . GLU A 1 1617 ? 174.824 218.813 218.054 1.00 12.97 ? 1617 GLU A O     1 
ATOM   1330  C  CB    . GLU A 1 1617 ? 177.510 218.020 216.469 1.00 11.19 ? 1617 GLU A CB    1 
ATOM   1331  C  CG    . GLU A 1 1617 ? 177.857 216.595 216.848 1.00 23.65 ? 1617 GLU A CG    1 
ATOM   1332  C  CD    . GLU A 1 1617 ? 176.628 215.721 216.994 1.00 28.80 ? 1617 GLU A CD    1 
ATOM   1333  O  OE1   . GLU A 1 1617 ? 175.564 216.091 216.455 1.00 22.01 ? 1617 GLU A OE1   1 
ATOM   1334  O  OE2   . GLU A 1 1617 ? 176.718 214.679 217.668 1.00 30.63 ? 1617 GLU A OE2   1 
ATOM   1335  N  N     . TYR A 1 1618 ? 176.153 217.630 219.432 1.00 8.73  ? 1618 TYR A N     1 
ATOM   1336  C  CA    . TYR A 1 1618 ? 175.034 217.220 220.272 1.00 11.14 ? 1618 TYR A CA    1 
ATOM   1337  C  C     . TYR A 1 1618 ? 174.458 218.410 221.029 1.00 9.37  ? 1618 TYR A C     1 
ATOM   1338  O  O     . TYR A 1 1618 ? 173.238 218.509 221.208 1.00 9.99  ? 1618 TYR A O     1 
ATOM   1339  C  CB    . TYR A 1 1618 ? 175.478 216.124 221.244 1.00 6.90  ? 1618 TYR A CB    1 
ATOM   1340  C  CG    . TYR A 1 1618 ? 174.463 215.799 222.315 1.00 7.05  ? 1618 TYR A CG    1 
ATOM   1341  C  CD1   . TYR A 1 1618 ? 173.413 214.929 222.059 1.00 9.53  ? 1618 TYR A CD1   1 
ATOM   1342  C  CD2   . TYR A 1 1618 ? 174.556 216.358 223.583 1.00 8.56  ? 1618 TYR A CD2   1 
ATOM   1343  C  CE1   . TYR A 1 1618 ? 172.482 214.625 223.030 1.00 11.98 ? 1618 TYR A CE1   1 
ATOM   1344  C  CE2   . TYR A 1 1618 ? 173.628 216.062 224.563 1.00 10.95 ? 1618 TYR A CE2   1 
ATOM   1345  C  CZ    . TYR A 1 1618 ? 172.593 215.195 224.280 1.00 17.69 ? 1618 TYR A CZ    1 
ATOM   1346  O  OH    . TYR A 1 1618 ? 171.666 214.895 225.253 1.00 20.47 ? 1618 TYR A OH    1 
ATOM   1347  N  N     . LEU A 1 1619 ? 175.321 219.320 221.483 1.00 7.26  ? 1619 LEU A N     1 
ATOM   1348  C  CA    . LEU A 1 1619 ? 174.854 220.506 222.190 1.00 5.39  ? 1619 LEU A CA    1 
ATOM   1349  C  C     . LEU A 1 1619 ? 174.073 221.432 221.263 1.00 8.59  ? 1619 LEU A C     1 
ATOM   1350  O  O     . LEU A 1 1619 ? 173.090 222.051 221.684 1.00 12.23 ? 1619 LEU A O     1 
ATOM   1351  C  CB    . LEU A 1 1619 ? 176.037 221.241 222.813 1.00 5.37  ? 1619 LEU A CB    1 
ATOM   1352  C  CG    . LEU A 1 1619 ? 176.694 220.523 223.990 1.00 5.41  ? 1619 LEU A CG    1 
ATOM   1353  C  CD1   . LEU A 1 1619 ? 177.862 221.329 224.518 1.00 7.85  ? 1619 LEU A CD1   1 
ATOM   1354  C  CD2   . LEU A 1 1619 ? 175.682 220.250 225.088 1.00 3.74  ? 1619 LEU A CD2   1 
ATOM   1355  N  N     . GLU A 1 1620 ? 174.501 221.545 220.003 1.00 10.66 ? 1620 GLU A N     1 
ATOM   1356  C  CA    . GLU A 1 1620 ? 173.769 222.374 219.052 1.00 8.20  ? 1620 GLU A CA    1 
ATOM   1357  C  C     . GLU A 1 1620 ? 172.378 221.820 218.778 1.00 9.37  ? 1620 GLU A C     1 
ATOM   1358  O  O     . GLU A 1 1620 ? 171.465 222.577 218.432 1.00 17.73 ? 1620 GLU A O     1 
ATOM   1359  C  CB    . GLU A 1 1620 ? 174.559 222.501 217.748 1.00 8.22  ? 1620 GLU A CB    1 
ATOM   1360  C  CG    . GLU A 1 1620 ? 175.590 223.620 217.755 1.00 11.08 ? 1620 GLU A CG    1 
ATOM   1361  C  CD    . GLU A 1 1620 ? 174.966 224.996 217.903 1.00 16.73 ? 1620 GLU A CD    1 
ATOM   1362  O  OE1   . GLU A 1 1620 ? 174.304 225.459 216.954 1.00 14.17 ? 1620 GLU A OE1   1 
ATOM   1363  O  OE2   . GLU A 1 1620 ? 175.138 225.612 218.974 1.00 13.99 ? 1620 GLU A OE2   1 
ATOM   1364  N  N     . ARG A 1 1621 ? 172.196 220.507 218.927 1.00 5.92  ? 1621 ARG A N     1 
ATOM   1365  C  CA    . ARG A 1 1621 ? 170.875 219.921 218.737 1.00 7.99  ? 1621 ARG A CA    1 
ATOM   1366  C  C     . ARG A 1 1621 ? 169.961 220.218 219.920 1.00 10.96 ? 1621 ARG A C     1 
ATOM   1367  O  O     . ARG A 1 1621 ? 168.759 220.447 219.740 1.00 12.07 ? 1621 ARG A O     1 
ATOM   1368  C  CB    . ARG A 1 1621 ? 170.997 218.416 218.518 1.00 10.86 ? 1621 ARG A CB    1 
ATOM   1369  C  CG    . ARG A 1 1621 ? 169.783 217.784 217.863 1.00 12.45 ? 1621 ARG A CG    1 
ATOM   1370  C  CD    . ARG A 1 1621 ? 170.035 216.321 217.552 1.00 17.54 ? 1621 ARG A CD    1 
ATOM   1371  N  NE    . ARG A 1 1621 ? 170.439 215.578 218.739 1.00 19.51 ? 1621 ARG A NE    1 
ATOM   1372  C  CZ    . ARG A 1 1621 ? 169.600 214.950 219.551 1.00 28.20 ? 1621 ARG A CZ    1 
ATOM   1373  N  NH1   . ARG A 1 1621 ? 168.295 214.951 219.331 1.00 29.75 ? 1621 ARG A NH1   1 
ATOM   1374  N  NH2   . ARG A 1 1621 ? 170.081 214.304 220.609 1.00 24.97 ? 1621 ARG A NH2   1 
ATOM   1375  N  N     . GLU A 1 1622 ? 170.507 220.216 221.136 1.00 9.42  ? 1622 GLU A N     1 
ATOM   1376  C  CA    . GLU A 1 1622 ? 169.701 220.504 222.314 1.00 7.94  ? 1622 GLU A CA    1 
ATOM   1377  C  C     . GLU A 1 1622 ? 169.327 221.976 222.409 1.00 7.08  ? 1622 GLU A C     1 
ATOM   1378  O  O     . GLU A 1 1622 ? 168.309 222.304 223.029 1.00 8.88  ? 1622 GLU A O     1 
ATOM   1379  C  CB    . GLU A 1 1622 ? 170.445 220.073 223.580 1.00 9.64  ? 1622 GLU A CB    1 
ATOM   1380  C  CG    . GLU A 1 1622 ? 170.931 218.636 223.554 1.00 12.86 ? 1622 GLU A CG    1 
ATOM   1381  C  CD    . GLU A 1 1622 ? 169.871 217.652 224.010 1.00 21.05 ? 1622 GLU A CD    1 
ATOM   1382  O  OE1   . GLU A 1 1622 ? 169.424 217.750 225.171 1.00 23.33 ? 1622 GLU A OE1   1 
ATOM   1383  O  OE2   . GLU A 1 1622 ? 169.488 216.778 223.206 1.00 24.10 ? 1622 GLU A OE2   1 
ATOM   1384  N  N     . ARG A 1 1623 ? 170.121 222.865 221.808 1.00 5.47  ? 1623 ARG A N     1 
ATOM   1385  C  CA    . ARG A 1 1623 ? 169.820 224.290 221.869 1.00 4.57  ? 1623 ARG A CA    1 
ATOM   1386  C  C     . ARG A 1 1623 ? 168.512 224.620 221.159 1.00 7.04  ? 1623 ARG A C     1 
ATOM   1387  O  O     . ARG A 1 1623 ? 167.844 225.595 221.517 1.00 13.77 ? 1623 ARG A O     1 
ATOM   1388  C  CB    . ARG A 1 1623 ? 170.975 225.095 221.273 1.00 2.81  ? 1623 ARG A CB    1 
ATOM   1389  C  CG    . ARG A 1 1623 ? 172.142 225.301 222.228 1.00 2.95  ? 1623 ARG A CG    1 
ATOM   1390  C  CD    . ARG A 1 1623 ? 173.171 226.248 221.645 1.00 2.76  ? 1623 ARG A CD    1 
ATOM   1391  N  NE    . ARG A 1 1623 ? 174.540 225.845 221.953 1.00 7.80  ? 1623 ARG A NE    1 
ATOM   1392  C  CZ    . ARG A 1 1623 ? 175.152 226.068 223.107 1.00 5.90  ? 1623 ARG A CZ    1 
ATOM   1393  N  NH1   . ARG A 1 1623 ? 174.546 226.697 224.100 1.00 8.75  ? 1623 ARG A NH1   1 
ATOM   1394  N  NH2   . ARG A 1 1623 ? 176.406 225.661 223.266 1.00 3.39  ? 1623 ARG A NH2   1 
ATOM   1395  N  N     . SER A 1 1624 ? 168.135 223.827 220.157 1.00 5.92  ? 1624 SER A N     1 
ATOM   1396  C  CA    . SER A 1 1624 ? 166.856 224.041 219.486 1.00 6.62  ? 1624 SER A CA    1 
ATOM   1397  C  C     . SER A 1 1624 ? 165.684 223.748 220.413 1.00 8.39  ? 1624 SER A C     1 
ATOM   1398  O  O     . SER A 1 1624 ? 164.678 224.466 220.399 1.00 15.32 ? 1624 SER A O     1 
ATOM   1399  C  CB    . SER A 1 1624 ? 166.777 223.174 218.231 1.00 8.80  ? 1624 SER A CB    1 
ATOM   1400  O  OG    . SER A 1 1624 ? 167.765 223.552 217.291 1.00 20.17 ? 1624 SER A OG    1 
ATOM   1401  N  N     . SER A 1 1625 ? 165.796 222.699 221.231 1.00 8.23  ? 1625 SER A N     1 
ATOM   1402  C  CA    . SER A 1 1625 ? 164.692 222.296 222.096 1.00 7.20  ? 1625 SER A CA    1 
ATOM   1403  C  C     . SER A 1 1625 ? 164.394 223.321 223.182 1.00 9.41  ? 1625 SER A C     1 
ATOM   1404  O  O     . SER A 1 1625 ? 163.284 223.325 223.727 1.00 16.02 ? 1625 SER A O     1 
ATOM   1405  C  CB    . SER A 1 1625 ? 165.001 220.936 222.725 1.00 9.74  ? 1625 SER A CB    1 
ATOM   1406  O  OG    . SER A 1 1625 ? 166.048 221.038 223.674 1.00 16.69 ? 1625 SER A OG    1 
ATOM   1407  N  N     . PHE A 1 1626 ? 165.355 224.181 223.516 1.00 9.20  ? 1626 PHE A N     1 
ATOM   1408  C  CA    . PHE A 1 1626 ? 165.141 225.291 224.443 1.00 4.97  ? 1626 PHE A CA    1 
ATOM   1409  C  C     . PHE A 1 1626 ? 166.022 226.438 223.973 1.00 3.67  ? 1626 PHE A C     1 
ATOM   1410  O  O     . PHE A 1 1626 ? 167.193 226.540 224.357 1.00 2.61  ? 1626 PHE A O     1 
ATOM   1411  C  CB    . PHE A 1 1626 ? 165.455 224.890 225.885 1.00 2.87  ? 1626 PHE A CB    1 
ATOM   1412  C  CG    . PHE A 1 1626 ? 165.041 225.911 226.905 1.00 3.00  ? 1626 PHE A CG    1 
ATOM   1413  C  CD1   . PHE A 1 1626 ? 163.703 226.134 227.179 1.00 3.14  ? 1626 PHE A CD1   1 
ATOM   1414  C  CD2   . PHE A 1 1626 ? 165.992 226.638 227.602 1.00 3.57  ? 1626 PHE A CD2   1 
ATOM   1415  C  CE1   . PHE A 1 1626 ? 163.320 227.071 228.120 1.00 3.05  ? 1626 PHE A CE1   1 
ATOM   1416  C  CE2   . PHE A 1 1626 ? 165.617 227.575 228.545 1.00 2.72  ? 1626 PHE A CE2   1 
ATOM   1417  C  CZ    . PHE A 1 1626 ? 164.278 227.791 228.805 1.00 3.35  ? 1626 PHE A CZ    1 
ATOM   1418  N  N     . PRO A 1 1627 ? 165.485 227.329 223.133 1.00 4.42  ? 1627 PRO A N     1 
ATOM   1419  C  CA    . PRO A 1 1627 ? 166.347 228.289 222.421 1.00 3.28  ? 1627 PRO A CA    1 
ATOM   1420  C  C     . PRO A 1 1627 ? 167.099 229.259 223.316 1.00 2.11  ? 1627 PRO A C     1 
ATOM   1421  O  O     . PRO A 1 1627 ? 168.062 229.877 222.846 1.00 1.91  ? 1627 PRO A O     1 
ATOM   1422  C  CB    . PRO A 1 1627 ? 165.364 229.022 221.496 1.00 2.11  ? 1627 PRO A CB    1 
ATOM   1423  C  CG    . PRO A 1 1627 ? 164.016 228.779 222.085 1.00 3.67  ? 1627 PRO A CG    1 
ATOM   1424  C  CD    . PRO A 1 1627 ? 164.080 227.425 222.704 1.00 4.99  ? 1627 PRO A CD    1 
ATOM   1425  N  N     . ARG A 1 1628 ? 166.707 229.422 224.580 1.00 1.19  ? 1628 ARG A N     1 
ATOM   1426  C  CA    . ARG A 1 1628 ? 167.521 230.233 225.475 1.00 1.83  ? 1628 ARG A CA    1 
ATOM   1427  C  C     . ARG A 1 1628 ? 168.875 229.596 225.766 1.00 2.27  ? 1628 ARG A C     1 
ATOM   1428  O  O     . ARG A 1 1628 ? 169.755 230.277 226.300 1.00 1.78  ? 1628 ARG A O     1 
ATOM   1429  C  CB    . ARG A 1 1628 ? 166.770 230.503 226.780 1.00 1.99  ? 1628 ARG A CB    1 
ATOM   1430  C  CG    . ARG A 1 1628 ? 165.464 231.251 226.580 1.00 1.40  ? 1628 ARG A CG    1 
ATOM   1431  C  CD    . ARG A 1 1628 ? 164.748 231.502 227.889 1.00 1.88  ? 1628 ARG A CD    1 
ATOM   1432  N  NE    . ARG A 1 1628 ? 163.493 232.217 227.690 1.00 3.61  ? 1628 ARG A NE    1 
ATOM   1433  C  CZ    . ARG A 1 1628 ? 163.285 233.482 228.026 1.00 1.60  ? 1628 ARG A CZ    1 
ATOM   1434  N  NH1   . ARG A 1 1628 ? 164.240 234.218 228.571 1.00 2.65  ? 1628 ARG A NH1   1 
ATOM   1435  N  NH2   . ARG A 1 1628 ? 162.092 234.023 227.810 1.00 1.60  ? 1628 ARG A NH2   1 
ATOM   1436  N  N     . PHE A 1 1629 ? 169.061 228.318 225.423 1.00 2.35  ? 1629 PHE A N     1 
ATOM   1437  C  CA    . PHE A 1 1629 ? 170.375 227.695 225.509 1.00 1.76  ? 1629 PHE A CA    1 
ATOM   1438  C  C     . PHE A 1 1629 ? 171.350 228.257 224.484 1.00 1.09  ? 1629 PHE A C     1 
ATOM   1439  O  O     . PHE A 1 1629 ? 172.561 228.070 224.633 1.00 2.27  ? 1629 PHE A O     1 
ATOM   1440  C  CB    . PHE A 1 1629 ? 170.262 226.182 225.324 1.00 1.42  ? 1629 PHE A CB    1 
ATOM   1441  C  CG    . PHE A 1 1629 ? 169.675 225.466 226.503 1.00 0.84  ? 1629 PHE A CG    1 
ATOM   1442  C  CD1   . PHE A 1 1629 ? 169.743 226.016 227.772 1.00 1.09  ? 1629 PHE A CD1   1 
ATOM   1443  C  CD2   . PHE A 1 1629 ? 169.059 224.238 226.343 1.00 0.76  ? 1629 PHE A CD2   1 
ATOM   1444  C  CE1   . PHE A 1 1629 ? 169.203 225.353 228.856 1.00 1.43  ? 1629 PHE A CE1   1 
ATOM   1445  C  CE2   . PHE A 1 1629 ? 168.518 223.575 227.420 1.00 0.61  ? 1629 PHE A CE2   1 
ATOM   1446  C  CZ    . PHE A 1 1629 ? 168.590 224.130 228.678 1.00 1.63  ? 1629 PHE A CZ    1 
ATOM   1447  N  N     . TYR A 1 1630 ? 170.851 228.936 223.447 1.00 1.36  ? 1630 TYR A N     1 
ATOM   1448  C  CA    . TYR A 1 1630 ? 171.731 229.539 222.453 1.00 1.38  ? 1630 TYR A CA    1 
ATOM   1449  C  C     . TYR A 1 1630 ? 172.615 230.622 223.053 1.00 0.91  ? 1630 TYR A C     1 
ATOM   1450  O  O     . TYR A 1 1630 ? 173.628 230.988 222.449 1.00 0.89  ? 1630 TYR A O     1 
ATOM   1451  C  CB    . TYR A 1 1630 ? 170.915 230.121 221.299 1.00 0.68  ? 1630 TYR A CB    1 
ATOM   1452  C  CG    . TYR A 1 1630 ? 170.535 229.115 220.239 1.00 2.80  ? 1630 TYR A CG    1 
ATOM   1453  C  CD1   . TYR A 1 1630 ? 171.461 228.685 219.298 1.00 2.97  ? 1630 TYR A CD1   1 
ATOM   1454  C  CD2   . TYR A 1 1630 ? 169.250 228.597 220.175 1.00 4.03  ? 1630 TYR A CD2   1 
ATOM   1455  C  CE1   . TYR A 1 1630 ? 171.117 227.764 218.328 1.00 2.41  ? 1630 TYR A CE1   1 
ATOM   1456  C  CE2   . TYR A 1 1630 ? 168.897 227.677 219.212 1.00 3.27  ? 1630 TYR A CE2   1 
ATOM   1457  C  CZ    . TYR A 1 1630 ? 169.834 227.263 218.291 1.00 3.33  ? 1630 TYR A CZ    1 
ATOM   1458  O  OH    . TYR A 1 1630 ? 169.483 226.347 217.329 1.00 11.13 ? 1630 TYR A OH    1 
ATOM   1459  N  N     . PHE A 1 1631 ? 172.253 231.141 224.222 1.00 1.56  ? 1631 PHE A N     1 
ATOM   1460  C  CA    . PHE A 1 1631 ? 173.015 232.178 224.897 1.00 1.47  ? 1631 PHE A CA    1 
ATOM   1461  C  C     . PHE A 1 1631 ? 173.845 231.620 226.046 1.00 1.52  ? 1631 PHE A C     1 
ATOM   1462  O  O     . PHE A 1 1631 ? 174.244 232.369 226.941 1.00 5.97  ? 1631 PHE A O     1 
ATOM   1463  C  CB    . PHE A 1 1631 ? 172.068 233.273 225.381 1.00 2.03  ? 1631 PHE A CB    1 
ATOM   1464  C  CG    . PHE A 1 1631 ? 171.156 233.784 224.305 1.00 1.20  ? 1631 PHE A CG    1 
ATOM   1465  C  CD1   . PHE A 1 1631 ? 171.666 234.175 223.077 1.00 0.82  ? 1631 PHE A CD1   1 
ATOM   1466  C  CD2   . PHE A 1 1631 ? 169.789 233.844 224.506 1.00 1.70  ? 1631 PHE A CD2   1 
ATOM   1467  C  CE1   . PHE A 1 1631 ? 170.832 234.634 222.078 1.00 0.65  ? 1631 PHE A CE1   1 
ATOM   1468  C  CE2   . PHE A 1 1631 ? 168.947 234.301 223.511 1.00 1.45  ? 1631 PHE A CE2   1 
ATOM   1469  C  CZ    . PHE A 1 1631 ? 169.469 234.696 222.295 1.00 1.09  ? 1631 PHE A CZ    1 
ATOM   1470  N  N     . VAL A 1 1632 ? 174.113 230.319 226.026 1.00 1.98  ? 1632 VAL A N     1 
ATOM   1471  C  CA    . VAL A 1 1632 ? 174.898 229.634 227.044 1.00 2.31  ? 1632 VAL A CA    1 
ATOM   1472  C  C     . VAL A 1 1632 ? 176.078 228.959 226.361 1.00 1.71  ? 1632 VAL A C     1 
ATOM   1473  O  O     . VAL A 1 1632 ? 175.934 228.387 225.277 1.00 1.90  ? 1632 VAL A O     1 
ATOM   1474  C  CB    . VAL A 1 1632 ? 174.047 228.601 227.813 1.00 1.65  ? 1632 VAL A CB    1 
ATOM   1475  C  CG1   . VAL A 1 1632 ? 174.850 227.965 228.921 1.00 1.02  ? 1632 VAL A CG1   1 
ATOM   1476  C  CG2   . VAL A 1 1632 ? 172.794 229.250 228.370 1.00 1.59  ? 1632 VAL A CG2   1 
ATOM   1477  N  N     . GLY A 1 1633 ? 177.246 229.035 226.993 1.00 3.57  ? 1633 GLY A N     1 
ATOM   1478  C  CA    . GLY A 1 1633 ? 178.413 228.367 226.458 1.00 5.45  ? 1633 GLY A CA    1 
ATOM   1479  C  C     . GLY A 1 1633 ? 178.285 226.858 226.507 1.00 2.30  ? 1633 GLY A C     1 
ATOM   1480  O  O     . GLY A 1 1633 ? 177.423 226.294 227.183 1.00 1.39  ? 1633 GLY A O     1 
ATOM   1481  N  N     . ASP A 1 1634 ? 179.170 226.192 225.764 1.00 3.65  ? 1634 ASP A N     1 
ATOM   1482  C  CA    . ASP A 1 1634 ? 179.101 224.739 225.643 1.00 3.37  ? 1634 ASP A CA    1 
ATOM   1483  C  C     . ASP A 1 1634 ? 179.311 224.054 226.990 1.00 4.69  ? 1634 ASP A C     1 
ATOM   1484  O  O     . ASP A 1 1634 ? 178.573 223.132 227.348 1.00 3.87  ? 1634 ASP A O     1 
ATOM   1485  C  CB    . ASP A 1 1634 ? 180.129 224.247 224.625 1.00 3.64  ? 1634 ASP A CB    1 
ATOM   1486  C  CG    . ASP A 1 1634 ? 179.629 224.352 223.202 1.00 11.18 ? 1634 ASP A CG    1 
ATOM   1487  O  OD1   . ASP A 1 1634 ? 178.421 224.145 222.985 1.00 15.70 ? 1634 ASP A OD1   1 
ATOM   1488  O  OD2   . ASP A 1 1634 ? 180.444 224.640 222.300 1.00 18.07 ? 1634 ASP A OD2   1 
ATOM   1489  N  N     . GLU A 1 1635 ? 180.316 224.495 227.750 1.00 3.18  ? 1635 GLU A N     1 
ATOM   1490  C  CA    . GLU A 1 1635 ? 180.602 223.855 229.031 1.00 5.96  ? 1635 GLU A CA    1 
ATOM   1491  C  C     . GLU A 1 1635 ? 179.470 224.072 230.025 1.00 5.22  ? 1635 GLU A C     1 
ATOM   1492  O  O     . GLU A 1 1635 ? 179.081 223.146 230.745 1.00 7.73  ? 1635 GLU A O     1 
ATOM   1493  C  CB    . GLU A 1 1635 ? 181.924 224.368 229.600 1.00 14.55 ? 1635 GLU A CB    1 
ATOM   1494  C  CG    . GLU A 1 1635 ? 182.336 223.689 230.897 1.00 13.84 ? 1635 GLU A CG    1 
ATOM   1495  C  CD    . GLU A 1 1635 ? 183.674 224.176 231.415 1.00 25.41 ? 1635 GLU A CD    1 
ATOM   1496  O  OE1   . GLU A 1 1635 ? 184.277 225.064 230.775 1.00 32.31 ? 1635 GLU A OE1   1 
ATOM   1497  O  OE2   . GLU A 1 1635 ? 184.131 223.658 232.456 1.00 25.20 ? 1635 GLU A OE2   1 
ATOM   1498  N  N     . ASP A 1 1636 ? 178.929 225.289 230.077 1.00 5.40  ? 1636 ASP A N     1 
ATOM   1499  C  CA    . ASP A 1 1636 ? 177.813 225.558 230.976 1.00 5.52  ? 1636 ASP A CA    1 
ATOM   1500  C  C     . ASP A 1 1636 ? 176.574 224.774 230.566 1.00 3.14  ? 1636 ASP A C     1 
ATOM   1501  O  O     . ASP A 1 1636 ? 175.802 224.330 231.425 1.00 2.07  ? 1636 ASP A O     1 
ATOM   1502  C  CB    . ASP A 1 1636 ? 177.516 227.057 231.009 1.00 5.73  ? 1636 ASP A CB    1 
ATOM   1503  C  CG    . ASP A 1 1636 ? 178.610 227.853 231.683 1.00 13.75 ? 1636 ASP A CG    1 
ATOM   1504  O  OD1   . ASP A 1 1636 ? 179.288 227.303 232.576 1.00 18.09 ? 1636 ASP A OD1   1 
ATOM   1505  O  OD2   . ASP A 1 1636 ? 178.783 229.035 231.328 1.00 17.31 ? 1636 ASP A OD2   1 
ATOM   1506  N  N     . LEU A 1 1637 ? 176.360 224.607 229.259 1.00 2.06  ? 1637 LEU A N     1 
ATOM   1507  C  CA    . LEU A 1 1637 ? 175.222 223.825 228.788 1.00 1.98  ? 1637 LEU A CA    1 
ATOM   1508  C  C     . LEU A 1 1637 ? 175.347 222.362 229.196 1.00 2.75  ? 1637 LEU A C     1 
ATOM   1509  O  O     . LEU A 1 1637 ? 174.358 221.735 229.587 1.00 1.70  ? 1637 LEU A O     1 
ATOM   1510  C  CB    . LEU A 1 1637 ? 175.086 223.954 227.270 1.00 4.17  ? 1637 LEU A CB    1 
ATOM   1511  C  CG    . LEU A 1 1637 ? 173.877 223.257 226.639 1.00 1.77  ? 1637 LEU A CG    1 
ATOM   1512  C  CD1   . LEU A 1 1637 ? 172.591 223.658 227.340 1.00 0.61  ? 1637 LEU A CD1   1 
ATOM   1513  C  CD2   . LEU A 1 1637 ? 173.798 223.553 225.152 1.00 1.72  ? 1637 LEU A CD2   1 
ATOM   1514  N  N     . LEU A 1 1638 ? 176.557 221.801 229.110 1.00 4.51  ? 1638 LEU A N     1 
ATOM   1515  C  CA    . LEU A 1 1638 ? 176.772 220.431 229.571 1.00 2.73  ? 1638 LEU A CA    1 
ATOM   1516  C  C     . LEU A 1 1638 ? 176.477 220.303 231.058 1.00 2.75  ? 1638 LEU A C     1 
ATOM   1517  O  O     . LEU A 1 1638 ? 175.912 219.299 231.504 1.00 5.09  ? 1638 LEU A O     1 
ATOM   1518  C  CB    . LEU A 1 1638 ? 178.203 219.988 229.275 1.00 3.36  ? 1638 LEU A CB    1 
ATOM   1519  C  CG    . LEU A 1 1638 ? 178.635 219.905 227.812 1.00 4.20  ? 1638 LEU A CG    1 
ATOM   1520  C  CD1   . LEU A 1 1638 ? 180.097 220.268 227.688 1.00 4.72  ? 1638 LEU A CD1   1 
ATOM   1521  C  CD2   . LEU A 1 1638 ? 178.380 218.528 227.242 1.00 4.11  ? 1638 LEU A CD2   1 
ATOM   1522  N  N     . GLU A 1 1639 ? 176.860 221.312 231.843 1.00 2.13  ? 1639 GLU A N     1 
ATOM   1523  C  CA    . GLU A 1 1639 ? 176.515 221.316 233.259 1.00 3.25  ? 1639 GLU A CA    1 
ATOM   1524  C  C     . GLU A 1 1639 ? 175.005 221.366 233.455 1.00 4.68  ? 1639 GLU A C     1 
ATOM   1525  O  O     . GLU A 1 1639 ? 174.466 220.697 234.342 1.00 11.54 ? 1639 GLU A O     1 
ATOM   1526  C  CB    . GLU A 1 1639 ? 177.193 222.494 233.958 1.00 4.78  ? 1639 GLU A CB    1 
ATOM   1527  C  CG    . GLU A 1 1639 ? 176.962 222.547 235.457 1.00 12.64 ? 1639 GLU A CG    1 
ATOM   1528  C  CD    . GLU A 1 1639 ? 177.690 223.698 236.120 1.00 19.57 ? 1639 GLU A CD    1 
ATOM   1529  O  OE1   . GLU A 1 1639 ? 178.362 224.470 235.404 1.00 18.20 ? 1639 GLU A OE1   1 
ATOM   1530  O  OE2   . GLU A 1 1639 ? 177.585 223.835 237.355 1.00 18.93 ? 1639 GLU A OE2   1 
ATOM   1531  N  N     . ILE A 1 1640 ? 174.303 222.152 232.632 1.00 3.72  ? 1640 ILE A N     1 
ATOM   1532  C  CA    . ILE A 1 1640 ? 172.848 222.232 232.729 1.00 3.65  ? 1640 ILE A CA    1 
ATOM   1533  C  C     . ILE A 1 1640 ? 172.207 220.903 232.349 1.00 3.97  ? 1640 ILE A C     1 
ATOM   1534  O  O     . ILE A 1 1640 ? 171.344 220.386 233.067 1.00 5.97  ? 1640 ILE A O     1 
ATOM   1535  C  CB    . ILE A 1 1640 ? 172.318 223.388 231.861 1.00 5.39  ? 1640 ILE A CB    1 
ATOM   1536  C  CG1   . ILE A 1 1640 ? 172.763 224.738 232.428 1.00 2.93  ? 1640 ILE A CG1   1 
ATOM   1537  C  CG2   . ILE A 1 1640 ? 170.803 223.307 231.701 1.00 1.90  ? 1640 ILE A CG2   1 
ATOM   1538  C  CD1   . ILE A 1 1640 ? 172.790 225.855 231.407 1.00 1.08  ? 1640 ILE A CD1   1 
ATOM   1539  N  N     . ILE A 1 1641 ? 172.616 220.330 231.216 1.00 3.51  ? 1641 ILE A N     1 
ATOM   1540  C  CA    . ILE A 1 1641 ? 172.008 219.086 230.749 1.00 2.54  ? 1641 ILE A CA    1 
ATOM   1541  C  C     . ILE A 1 1641 ? 172.374 217.932 231.676 1.00 5.13  ? 1641 ILE A C     1 
ATOM   1542  O  O     . ILE A 1 1641 ? 171.513 217.141 232.080 1.00 3.33  ? 1641 ILE A O     1 
ATOM   1543  C  CB    . ILE A 1 1641 ? 172.428 218.792 229.297 1.00 4.04  ? 1641 ILE A CB    1 
ATOM   1544  C  CG1   . ILE A 1 1641 ? 172.080 219.964 228.377 1.00 3.74  ? 1641 ILE A CG1   1 
ATOM   1545  C  CG2   . ILE A 1 1641 ? 171.780 217.508 228.801 1.00 4.88  ? 1641 ILE A CG2   1 
ATOM   1546  C  CD1   . ILE A 1 1641 ? 170.633 220.358 228.400 1.00 4.94  ? 1641 ILE A CD1   1 
ATOM   1547  N  N     . GLY A 1 1642 ? 173.656 217.821 232.026 1.00 7.67  ? 1642 GLY A N     1 
ATOM   1548  C  CA    . GLY A 1 1642 ? 174.114 216.679 232.794 1.00 3.62  ? 1642 GLY A CA    1 
ATOM   1549  C  C     . GLY A 1 1642 ? 173.650 216.680 234.236 1.00 7.85  ? 1642 GLY A C     1 
ATOM   1550  O  O     . GLY A 1 1642 ? 173.509 215.614 234.843 1.00 12.58 ? 1642 GLY A O     1 
ATOM   1551  N  N     . ASN A 1 1643 ? 173.410 217.858 234.805 1.00 6.65  ? 1643 ASN A N     1 
ATOM   1552  C  CA    . ASN A 1 1643 ? 172.946 217.981 236.184 1.00 9.79  ? 1643 ASN A CA    1 
ATOM   1553  C  C     . ASN A 1 1643 ? 171.445 218.200 236.257 1.00 10.55 ? 1643 ASN A C     1 
ATOM   1554  O  O     . ASN A 1 1643 ? 170.950 218.872 237.165 1.00 13.27 ? 1643 ASN A O     1 
ATOM   1555  C  CB    . ASN A 1 1643 ? 173.687 219.110 236.894 1.00 12.12 ? 1643 ASN A CB    1 
ATOM   1556  C  CG    . ASN A 1 1643 ? 175.051 218.685 237.391 1.00 10.98 ? 1643 ASN A CG    1 
ATOM   1557  O  OD1   . ASN A 1 1643 ? 176.078 219.153 236.901 1.00 12.44 ? 1643 ASN A OD1   1 
ATOM   1558  N  ND2   . ASN A 1 1643 ? 175.069 217.796 238.375 1.00 18.29 ? 1643 ASN A ND2   1 
ATOM   1559  N  N     . SER A 1 1644 ? 170.694 217.622 235.316 1.00 14.82 ? 1644 SER A N     1 
ATOM   1560  C  CA    . SER A 1 1644 ? 169.253 217.840 235.266 1.00 12.05 ? 1644 SER A CA    1 
ATOM   1561  C  C     . SER A 1 1644 ? 168.544 217.324 236.511 1.00 16.26 ? 1644 SER A C     1 
ATOM   1562  O  O     . SER A 1 1644 ? 167.411 217.739 236.780 1.00 21.91 ? 1644 SER A O     1 
ATOM   1563  C  CB    . SER A 1 1644 ? 168.669 217.187 234.014 1.00 12.01 ? 1644 SER A CB    1 
ATOM   1564  O  OG    . SER A 1 1644 ? 168.634 215.776 234.142 1.00 19.22 ? 1644 SER A OG    1 
ATOM   1565  N  N     . LYS A 1 1645 ? 169.176 216.432 237.273 1.00 14.40 ? 1645 LYS A N     1 
ATOM   1566  C  CA    . LYS A 1 1645 ? 168.614 215.970 238.537 1.00 14.27 ? 1645 LYS A CA    1 
ATOM   1567  C  C     . LYS A 1 1645 ? 169.087 216.812 239.718 1.00 22.83 ? 1645 LYS A C     1 
ATOM   1568  O  O     . LYS A 1 1645 ? 168.328 217.025 240.670 1.00 29.58 ? 1645 LYS A O     1 
ATOM   1569  C  CB    . LYS A 1 1645 ? 168.969 214.501 238.764 1.00 19.21 ? 1645 LYS A CB    1 
ATOM   1570  C  CG    . LYS A 1 1645 ? 168.443 213.566 237.685 1.00 20.33 ? 1645 LYS A CG    1 
ATOM   1571  C  CD    . LYS A 1 1645 ? 169.063 212.184 237.790 1.00 17.79 ? 1645 LYS A CD    1 
ATOM   1572  C  CE    . LYS A 1 1645 ? 168.925 211.623 239.195 1.00 25.61 ? 1645 LYS A CE    1 
ATOM   1573  N  NZ    . LYS A 1 1645 ? 169.464 210.238 239.299 1.00 29.00 ? 1645 LYS A NZ    1 
ATOM   1574  N  N     . ASN A 1 1646 ? 170.327 217.299 239.677 1.00 19.73 ? 1646 ASN A N     1 
ATOM   1575  C  CA    . ASN A 1 1646 ? 170.864 218.172 240.721 1.00 15.10 ? 1646 ASN A CA    1 
ATOM   1576  C  C     . ASN A 1 1646 ? 170.497 219.607 240.366 1.00 17.60 ? 1646 ASN A C     1 
ATOM   1577  O  O     . ASN A 1 1646 ? 171.269 220.336 239.743 1.00 20.75 ? 1646 ASN A O     1 
ATOM   1578  C  CB    . ASN A 1 1646 ? 172.371 217.990 240.854 1.00 21.20 ? 1646 ASN A CB    1 
ATOM   1579  C  CG    . ASN A 1 1646 ? 172.763 216.550 241.113 1.00 27.11 ? 1646 ASN A CG    1 
ATOM   1580  O  OD1   . ASN A 1 1646 ? 173.382 215.900 240.269 1.00 25.19 ? 1646 ASN A OD1   1 
ATOM   1581  N  ND2   . ASN A 1 1646 ? 172.404 216.040 242.287 1.00 26.94 ? 1646 ASN A ND2   1 
ATOM   1582  N  N     . VAL A 1 1647 ? 169.295 220.017 240.777 1.00 19.86 ? 1647 VAL A N     1 
ATOM   1583  C  CA    . VAL A 1 1647 ? 168.768 221.321 240.388 1.00 13.13 ? 1647 VAL A CA    1 
ATOM   1584  C  C     . VAL A 1 1647 ? 169.529 222.462 241.054 1.00 13.07 ? 1647 VAL A C     1 
ATOM   1585  O  O     . VAL A 1 1647 ? 169.592 223.571 240.509 1.00 15.31 ? 1647 VAL A O     1 
ATOM   1586  C  CB    . VAL A 1 1647 ? 167.266 221.393 240.706 1.00 11.75 ? 1647 VAL A CB    1 
ATOM   1587  C  CG1   . VAL A 1 1647 ? 166.492 220.437 239.816 1.00 12.19 ? 1647 VAL A CG1   1 
ATOM   1588  C  CG2   . VAL A 1 1647 ? 167.040 221.048 242.161 1.00 15.93 ? 1647 VAL A CG2   1 
ATOM   1589  N  N     . ALA A 1 1648 ? 170.104 222.228 242.237 1.00 11.60 ? 1648 ALA A N     1 
ATOM   1590  C  CA    . ALA A 1 1648 ? 170.808 223.299 242.937 1.00 12.94 ? 1648 ALA A CA    1 
ATOM   1591  C  C     . ALA A 1 1648 ? 171.984 223.827 242.127 1.00 16.00 ? 1648 ALA A C     1 
ATOM   1592  O  O     . ALA A 1 1648 ? 172.361 224.996 242.268 1.00 19.00 ? 1648 ALA A O     1 
ATOM   1593  C  CB    . ALA A 1 1648 ? 171.282 222.814 244.306 1.00 13.52 ? 1648 ALA A CB    1 
ATOM   1594  N  N     . LYS A 1 1649 ? 172.575 222.990 241.276 1.00 13.41 ? 1649 LYS A N     1 
ATOM   1595  C  CA    . LYS A 1 1649 ? 173.664 223.428 240.415 1.00 13.88 ? 1649 LYS A CA    1 
ATOM   1596  C  C     . LYS A 1 1649 ? 173.182 224.228 239.212 1.00 10.71 ? 1649 LYS A C     1 
ATOM   1597  O  O     . LYS A 1 1649 ? 174.007 224.839 238.524 1.00 11.86 ? 1649 LYS A O     1 
ATOM   1598  C  CB    . LYS A 1 1649 ? 174.473 222.217 239.947 1.00 13.62 ? 1649 LYS A CB    1 
ATOM   1599  C  CG    . LYS A 1 1649 ? 175.172 221.489 241.079 1.00 14.38 ? 1649 LYS A CG    1 
ATOM   1600  C  CD    . LYS A 1 1649 ? 175.808 220.197 240.611 1.00 16.17 ? 1649 LYS A CD    1 
ATOM   1601  C  CE    . LYS A 1 1649 ? 176.066 219.272 241.785 1.00 25.68 ? 1649 LYS A CE    1 
ATOM   1602  N  NZ    . LYS A 1 1649 ? 174.878 219.187 242.680 1.00 27.12 ? 1649 LYS A NZ    1 
ATOM   1603  N  N     . LEU A 1 1650 ? 171.878 224.246 238.951 1.00 10.51 ? 1650 LEU A N     1 
ATOM   1604  C  CA    . LEU A 1 1650 ? 171.311 224.999 237.843 1.00 6.58  ? 1650 LEU A CA    1 
ATOM   1605  C  C     . LEU A 1 1650 ? 171.133 226.474 238.153 1.00 8.48  ? 1650 LEU A C     1 
ATOM   1606  O  O     . LEU A 1 1650 ? 170.923 227.263 237.226 1.00 8.19  ? 1650 LEU A O     1 
ATOM   1607  C  CB    . LEU A 1 1650 ? 169.952 224.414 237.436 1.00 6.59  ? 1650 LEU A CB    1 
ATOM   1608  C  CG    . LEU A 1 1650 ? 169.912 223.211 236.496 1.00 7.91  ? 1650 LEU A CG    1 
ATOM   1609  C  CD1   . LEU A 1 1650 ? 170.489 223.617 235.164 1.00 6.09  ? 1650 LEU A CD1   1 
ATOM   1610  C  CD2   . LEU A 1 1650 ? 170.663 222.022 237.056 1.00 14.10 ? 1650 LEU A CD2   1 
ATOM   1611  N  N     . GLN A 1 1651 ? 171.228 226.865 239.426 1.00 7.64  ? 1651 GLN A N     1 
ATOM   1612  C  CA    . GLN A 1 1651 ? 170.848 228.216 239.820 1.00 6.14  ? 1651 GLN A CA    1 
ATOM   1613  C  C     . GLN A 1 1651 ? 171.759 229.263 239.189 1.00 6.91  ? 1651 GLN A C     1 
ATOM   1614  O  O     . GLN A 1 1651 ? 171.290 230.322 238.761 1.00 10.76 ? 1651 GLN A O     1 
ATOM   1615  C  CB    . GLN A 1 1651 ? 170.863 228.335 241.345 1.00 7.16  ? 1651 GLN A CB    1 
ATOM   1616  C  CG    . GLN A 1 1651 ? 169.868 227.425 242.069 1.00 6.59  ? 1651 GLN A CG    1 
ATOM   1617  C  CD    . GLN A 1 1651 ? 168.416 227.851 241.914 1.00 5.74  ? 1651 GLN A CD    1 
ATOM   1618  O  OE1   . GLN A 1 1651 ? 168.079 228.665 241.059 1.00 13.69 ? 1651 GLN A OE1   1 
ATOM   1619  N  NE2   . GLN A 1 1651 ? 167.550 227.300 242.752 1.00 5.31  ? 1651 GLN A NE2   1 
ATOM   1620  N  N     . LYS A 1 1652 ? 173.060 228.978 239.108 1.00 6.78  ? 1652 LYS A N     1 
ATOM   1621  C  CA    . LYS A 1 1652 ? 174.015 229.960 238.607 1.00 7.13  ? 1652 LYS A CA    1 
ATOM   1622  C  C     . LYS A 1 1652 ? 173.851 230.257 237.122 1.00 5.35  ? 1652 LYS A C     1 
ATOM   1623  O  O     . LYS A 1 1652 ? 174.433 231.234 236.641 1.00 6.97  ? 1652 LYS A O     1 
ATOM   1624  C  CB    . LYS A 1 1652 ? 175.447 229.486 238.866 1.00 6.19  ? 1652 LYS A CB    1 
ATOM   1625  C  CG    . LYS A 1 1652 ? 175.830 228.226 238.109 1.00 8.77  ? 1652 LYS A CG    1 
ATOM   1626  C  CD    . LYS A 1 1652 ? 177.267 227.820 238.383 1.00 11.74 ? 1652 LYS A CD    1 
ATOM   1627  C  CE    . LYS A 1 1652 ? 177.432 227.244 239.775 1.00 20.05 ? 1652 LYS A CE    1 
ATOM   1628  N  NZ    . LYS A 1 1652 ? 178.811 226.727 239.993 1.00 18.11 ? 1652 LYS A NZ    1 
ATOM   1629  N  N     . HIS A 1 1653 ? 173.089 229.451 236.385 1.00 5.13  ? 1653 HIS A N     1 
ATOM   1630  C  CA    . HIS A 1 1653 ? 172.983 229.608 234.940 1.00 4.34  ? 1653 HIS A CA    1 
ATOM   1631  C  C     . HIS A 1 1653 ? 171.738 230.360 234.491 1.00 3.56  ? 1653 HIS A C     1 
ATOM   1632  O  O     . HIS A 1 1653 ? 171.636 230.694 233.306 1.00 3.80  ? 1653 HIS A O     1 
ATOM   1633  C  CB    . HIS A 1 1653 ? 173.009 228.238 234.256 1.00 4.91  ? 1653 HIS A CB    1 
ATOM   1634  C  CG    . HIS A 1 1653 ? 174.218 227.421 234.586 1.00 4.92  ? 1653 HIS A CG    1 
ATOM   1635  N  ND1   . HIS A 1 1653 ? 175.487 227.777 234.186 1.00 6.02  ? 1653 HIS A ND1   1 
ATOM   1636  C  CD2   . HIS A 1 1653 ? 174.351 226.264 235.273 1.00 5.71  ? 1653 HIS A CD2   1 
ATOM   1637  C  CE1   . HIS A 1 1653 ? 176.350 226.875 234.614 1.00 5.35  ? 1653 HIS A CE1   1 
ATOM   1638  N  NE2   . HIS A 1 1653 ? 175.687 225.945 235.277 1.00 8.73  ? 1653 HIS A NE2   1 
ATOM   1639  N  N     . PHE A 1 1654 ? 170.797 230.640 235.396 1.00 4.04  ? 1654 PHE A N     1 
ATOM   1640  C  CA    . PHE A 1 1654 ? 169.550 231.275 234.981 1.00 2.77  ? 1654 PHE A CA    1 
ATOM   1641  C  C     . PHE A 1 1654 ? 169.759 232.717 234.539 1.00 3.66  ? 1654 PHE A C     1 
ATOM   1642  O  O     . PHE A 1 1654 ? 169.012 233.211 233.687 1.00 8.33  ? 1654 PHE A O     1 
ATOM   1643  C  CB    . PHE A 1 1654 ? 168.519 231.207 236.106 1.00 3.46  ? 1654 PHE A CB    1 
ATOM   1644  C  CG    . PHE A 1 1654 ? 167.956 229.834 236.326 1.00 3.61  ? 1654 PHE A CG    1 
ATOM   1645  C  CD1   . PHE A 1 1654 ? 167.057 229.289 235.425 1.00 3.00  ? 1654 PHE A CD1   1 
ATOM   1646  C  CD2   . PHE A 1 1654 ? 168.326 229.087 237.430 1.00 4.30  ? 1654 PHE A CD2   1 
ATOM   1647  C  CE1   . PHE A 1 1654 ? 166.539 228.026 235.622 1.00 2.45  ? 1654 PHE A CE1   1 
ATOM   1648  C  CE2   . PHE A 1 1654 ? 167.809 227.822 237.632 1.00 3.39  ? 1654 PHE A CE2   1 
ATOM   1649  C  CZ    . PHE A 1 1654 ? 166.916 227.291 236.726 1.00 2.44  ? 1654 PHE A CZ    1 
ATOM   1650  N  N     . LYS A 1 1655 ? 170.758 233.410 235.095 1.00 3.52  ? 1655 LYS A N     1 
ATOM   1651  C  CA    . LYS A 1 1655 ? 171.004 234.788 234.689 1.00 2.95  ? 1655 LYS A CA    1 
ATOM   1652  C  C     . LYS A 1 1655 ? 171.439 234.888 233.234 1.00 2.52  ? 1655 LYS A C     1 
ATOM   1653  O  O     . LYS A 1 1655 ? 171.315 235.959 232.632 1.00 5.09  ? 1655 LYS A O     1 
ATOM   1654  C  CB    . LYS A 1 1655 ? 172.059 235.441 235.587 1.00 3.81  ? 1655 LYS A CB    1 
ATOM   1655  C  CG    . LYS A 1 1655 ? 173.444 234.822 235.484 1.00 8.87  ? 1655 LYS A CG    1 
ATOM   1656  C  CD    . LYS A 1 1655 ? 174.446 235.536 236.383 1.00 5.37  ? 1655 LYS A CD    1 
ATOM   1657  C  CE    . LYS A 1 1655 ? 174.217 235.213 237.845 1.00 11.01 ? 1655 LYS A CE    1 
ATOM   1658  N  NZ    . LYS A 1 1655 ? 175.272 235.803 238.715 1.00 18.02 ? 1655 LYS A NZ    1 
ATOM   1659  N  N     . LYS A 1 1656 ? 171.951 233.802 232.661 1.00 3.17  ? 1656 LYS A N     1 
ATOM   1660  C  CA    . LYS A 1 1656 ? 172.361 233.796 231.265 1.00 4.11  ? 1656 LYS A CA    1 
ATOM   1661  C  C     . LYS A 1 1656 ? 171.201 233.543 230.312 1.00 4.18  ? 1656 LYS A C     1 
ATOM   1662  O  O     . LYS A 1 1656 ? 171.248 233.994 229.162 1.00 9.50  ? 1656 LYS A O     1 
ATOM   1663  C  CB    . LYS A 1 1656 ? 173.446 232.739 231.043 1.00 5.14  ? 1656 LYS A CB    1 
ATOM   1664  C  CG    . LYS A 1 1656 ? 174.463 232.672 232.163 1.00 4.47  ? 1656 LYS A CG    1 
ATOM   1665  C  CD    . LYS A 1 1656 ? 175.424 231.512 231.986 1.00 4.07  ? 1656 LYS A CD    1 
ATOM   1666  C  CE    . LYS A 1 1656 ? 176.173 231.239 233.276 1.00 7.82  ? 1656 LYS A CE    1 
ATOM   1667  N  NZ    . LYS A 1 1656 ? 177.097 230.088 233.158 1.00 10.03 ? 1656 LYS A NZ    1 
ATOM   1668  N  N     . MET A 1 1657 ? 170.162 232.841 230.761 1.00 2.62  ? 1657 MET A N     1 
ATOM   1669  C  CA    . MET A 1 1657 ? 169.032 232.498 229.910 1.00 2.57  ? 1657 MET A CA    1 
ATOM   1670  C  C     . MET A 1 1657 ? 167.841 233.429 230.079 1.00 1.89  ? 1657 MET A C     1 
ATOM   1671  O  O     . MET A 1 1657 ? 166.906 233.360 229.276 1.00 2.24  ? 1657 MET A O     1 
ATOM   1672  C  CB    . MET A 1 1657 ? 168.576 231.059 230.184 1.00 3.82  ? 1657 MET A CB    1 
ATOM   1673  C  CG    . MET A 1 1657 ? 169.659 230.012 230.030 1.00 2.17  ? 1657 MET A CG    1 
ATOM   1674  S  SD    . MET A 1 1657 ? 169.104 228.383 230.556 1.00 12.66 ? 1657 MET A SD    1 
ATOM   1675  C  CE    . MET A 1 1657 ? 169.264 228.517 232.333 1.00 3.20  ? 1657 MET A CE    1 
ATOM   1676  N  N     . PHE A 1 1658 ? 167.844 234.291 231.090 1.00 2.95  ? 1658 PHE A N     1 
ATOM   1677  C  CA    . PHE A 1 1658 ? 166.695 235.127 231.393 1.00 2.74  ? 1658 PHE A CA    1 
ATOM   1678  C  C     . PHE A 1 1658 ? 167.149 236.556 231.657 1.00 4.08  ? 1658 PHE A C     1 
ATOM   1679  O  O     . PHE A 1 1658 ? 168.295 236.808 232.035 1.00 4.20  ? 1658 PHE A O     1 
ATOM   1680  C  CB    . PHE A 1 1658 ? 165.916 234.591 232.599 1.00 1.06  ? 1658 PHE A CB    1 
ATOM   1681  C  CG    . PHE A 1 1658 ? 165.156 233.327 232.321 1.00 1.49  ? 1658 PHE A CG    1 
ATOM   1682  C  CD1   . PHE A 1 1658 ? 165.772 232.091 232.434 1.00 2.11  ? 1658 PHE A CD1   1 
ATOM   1683  C  CD2   . PHE A 1 1658 ? 163.822 233.372 231.953 1.00 1.88  ? 1658 PHE A CD2   1 
ATOM   1684  C  CE1   . PHE A 1 1658 ? 165.074 230.926 232.182 1.00 2.12  ? 1658 PHE A CE1   1 
ATOM   1685  C  CE2   . PHE A 1 1658 ? 163.118 232.210 231.700 1.00 1.85  ? 1658 PHE A CE2   1 
ATOM   1686  C  CZ    . PHE A 1 1658 ? 163.745 230.984 231.814 1.00 2.21  ? 1658 PHE A CZ    1 
ATOM   1687  N  N     . ALA A 1 1659 ? 166.225 237.494 231.444 1.00 2.81  ? 1659 ALA A N     1 
ATOM   1688  C  CA    . ALA A 1 1659 ? 166.528 238.903 231.669 1.00 2.01  ? 1659 ALA A CA    1 
ATOM   1689  C  C     . ALA A 1 1659 ? 166.683 239.207 233.154 1.00 3.28  ? 1659 ALA A C     1 
ATOM   1690  O  O     . ALA A 1 1659 ? 167.640 239.872 233.563 1.00 8.38  ? 1659 ALA A O     1 
ATOM   1691  C  CB    . ALA A 1 1659 ? 165.436 239.778 231.054 1.00 1.97  ? 1659 ALA A CB    1 
ATOM   1692  N  N     . GLY A 1 1660 ? 165.755 238.725 233.976 1.00 1.99  ? 1660 GLY A N     1 
ATOM   1693  C  CA    . GLY A 1 1660 ? 165.767 239.058 235.385 1.00 2.02  ? 1660 GLY A CA    1 
ATOM   1694  C  C     . GLY A 1 1660 ? 165.537 237.893 236.324 1.00 2.48  ? 1660 GLY A C     1 
ATOM   1695  O  O     . GLY A 1 1660 ? 165.305 238.095 237.519 1.00 4.22  ? 1660 GLY A O     1 
ATOM   1696  N  N     . VAL A 1 1661 ? 165.596 236.670 235.809 1.00 2.50  ? 1661 VAL A N     1 
ATOM   1697  C  CA    . VAL A 1 1661 ? 165.468 235.478 236.637 1.00 2.39  ? 1661 VAL A CA    1 
ATOM   1698  C  C     . VAL A 1 1661 ? 166.871 235.046 237.045 1.00 4.28  ? 1661 VAL A C     1 
ATOM   1699  O  O     . VAL A 1 1661 ? 167.649 234.569 236.217 1.00 7.25  ? 1661 VAL A O     1 
ATOM   1700  C  CB    . VAL A 1 1661 ? 164.730 234.350 235.908 1.00 1.58  ? 1661 VAL A CB    1 
ATOM   1701  C  CG1   . VAL A 1 1661 ? 164.732 233.089 236.752 1.00 1.99  ? 1661 VAL A CG1   1 
ATOM   1702  C  CG2   . VAL A 1 1661 ? 163.314 234.773 235.563 1.00 1.37  ? 1661 VAL A CG2   1 
ATOM   1703  N  N     . SER A 1 1662 ? 167.197 235.222 238.322 1.00 4.88  ? 1662 SER A N     1 
ATOM   1704  C  CA    . SER A 1 1662 ? 168.491 234.795 238.831 1.00 5.43  ? 1662 SER A CA    1 
ATOM   1705  C  C     . SER A 1 1662 ? 168.440 233.410 239.461 1.00 4.98  ? 1662 SER A C     1 
ATOM   1706  O  O     . SER A 1 1662 ? 169.448 232.697 239.452 1.00 8.38  ? 1662 SER A O     1 
ATOM   1707  C  CB    . SER A 1 1662 ? 169.018 235.810 239.849 1.00 6.89  ? 1662 SER A CB    1 
ATOM   1708  O  OG    . SER A 1 1662 ? 170.264 235.403 240.379 1.00 17.85 ? 1662 SER A OG    1 
ATOM   1709  N  N     . SER A 1 1663 ? 167.290 233.015 239.996 1.00 4.24  ? 1663 SER A N     1 
ATOM   1710  C  CA    . SER A 1 1663 ? 167.135 231.703 240.605 1.00 3.36  ? 1663 SER A CA    1 
ATOM   1711  C  C     . SER A 1 1663 ? 165.661 231.329 240.593 1.00 5.02  ? 1663 SER A C     1 
ATOM   1712  O  O     . SER A 1 1663 ? 164.789 232.174 240.377 1.00 6.35  ? 1663 SER A O     1 
ATOM   1713  C  CB    . SER A 1 1663 ? 167.688 231.672 242.035 1.00 3.86  ? 1663 SER A CB    1 
ATOM   1714  O  OG    . SER A 1 1663 ? 166.920 232.487 242.902 1.00 6.12  ? 1663 SER A OG    1 
ATOM   1715  N  N     . ILE A 1 1664 ? 165.399 230.050 240.829 1.00 4.27  ? 1664 ILE A N     1 
ATOM   1716  C  CA    . ILE A 1 1664 ? 164.044 229.523 240.922 1.00 4.20  ? 1664 ILE A CA    1 
ATOM   1717  C  C     . ILE A 1 1664 ? 163.795 229.062 242.351 1.00 5.29  ? 1664 ILE A C     1 
ATOM   1718  O  O     . ILE A 1 1664 ? 164.723 228.672 243.069 1.00 8.38  ? 1664 ILE A O     1 
ATOM   1719  C  CB    . ILE A 1 1664 ? 163.811 228.372 239.919 1.00 5.62  ? 1664 ILE A CB    1 
ATOM   1720  C  CG1   . ILE A 1 1664 ? 164.841 227.262 240.132 1.00 6.31  ? 1664 ILE A CG1   1 
ATOM   1721  C  CG2   . ILE A 1 1664 ? 163.863 228.884 238.492 1.00 3.25  ? 1664 ILE A CG2   1 
ATOM   1722  C  CD1   . ILE A 1 1664 ? 164.629 226.059 239.252 1.00 3.56  ? 1664 ILE A CD1   1 
ATOM   1723  N  N     . ILE A 1 1665 ? 162.533 229.122 242.769 1.00 7.10  ? 1665 ILE A N     1 
ATOM   1724  C  CA    . ILE A 1 1665 ? 162.115 228.659 244.088 1.00 6.47  ? 1665 ILE A CA    1 
ATOM   1725  C  C     . ILE A 1 1665 ? 161.622 227.225 243.965 1.00 8.59  ? 1665 ILE A C     1 
ATOM   1726  O  O     . ILE A 1 1665 ? 160.819 226.906 243.079 1.00 10.07 ? 1665 ILE A O     1 
ATOM   1727  C  CB    . ILE A 1 1665 ? 161.031 229.563 244.703 1.00 5.59  ? 1665 ILE A CB    1 
ATOM   1728  C  CG1   . ILE A 1 1665 ? 161.570 230.968 244.968 1.00 6.45  ? 1665 ILE A CG1   1 
ATOM   1729  C  CG2   . ILE A 1 1665 ? 160.495 228.963 245.990 1.00 9.06  ? 1665 ILE A CG2   1 
ATOM   1730  C  CD1   . ILE A 1 1665 ? 161.402 231.914 243.833 1.00 6.63  ? 1665 ILE A CD1   1 
ATOM   1731  N  N     . LEU A 1 1666 ? 162.097 226.367 244.861 1.00 7.17  ? 1666 LEU A N     1 
ATOM   1732  C  CA    . LEU A 1 1666 ? 161.810 224.945 244.831 1.00 8.27  ? 1666 LEU A CA    1 
ATOM   1733  C  C     . LEU A 1 1666 ? 161.260 224.517 246.183 1.00 14.85 ? 1666 LEU A C     1 
ATOM   1734  O  O     . LEU A 1 1666 ? 161.532 225.141 247.211 1.00 22.13 ? 1666 LEU A O     1 
ATOM   1735  C  CB    . LEU A 1 1666 ? 163.076 224.152 244.493 1.00 11.27 ? 1666 LEU A CB    1 
ATOM   1736  C  CG    . LEU A 1 1666 ? 163.610 224.404 243.085 1.00 9.42  ? 1666 LEU A CG    1 
ATOM   1737  C  CD1   . LEU A 1 1666 ? 164.943 223.737 242.895 1.00 8.96  ? 1666 LEU A CD1   1 
ATOM   1738  C  CD2   . LEU A 1 1666 ? 162.617 223.871 242.073 1.00 10.33 ? 1666 LEU A CD2   1 
ATOM   1739  N  N     . ASN A 1 1667 ? 160.480 223.442 246.173 1.00 16.81 ? 1667 ASN A N     1 
ATOM   1740  C  CA    . ASN A 1 1667 ? 159.963 222.873 247.410 1.00 15.35 ? 1667 ASN A CA    1 
ATOM   1741  C  C     . ASN A 1 1667 ? 161.098 222.154 248.138 1.00 19.91 ? 1667 ASN A C     1 
ATOM   1742  O  O     . ASN A 1 1667 ? 162.259 222.177 247.719 1.00 26.20 ? 1667 ASN A O     1 
ATOM   1743  C  CB    . ASN A 1 1667 ? 158.782 221.948 247.127 1.00 9.73  ? 1667 ASN A CB    1 
ATOM   1744  C  CG    . ASN A 1 1667 ? 159.069 220.948 246.025 1.00 17.40 ? 1667 ASN A CG    1 
ATOM   1745  O  OD1   . ASN A 1 1667 ? 160.204 220.816 245.566 1.00 22.22 ? 1667 ASN A OD1   1 
ATOM   1746  N  ND2   . ASN A 1 1667 ? 158.041 220.222 245.608 1.00 14.38 ? 1667 ASN A ND2   1 
ATOM   1747  N  N     . GLU A 1 1668 ? 160.768 221.501 249.255 1.00 23.05 ? 1668 GLU A N     1 
ATOM   1748  C  CA    . GLU A 1 1668 ? 161.792 220.792 250.017 1.00 19.99 ? 1668 GLU A CA    1 
ATOM   1749  C  C     . GLU A 1 1668 ? 162.360 219.615 249.236 1.00 21.47 ? 1668 GLU A C     1 
ATOM   1750  O  O     . GLU A 1 1668 ? 163.528 219.257 249.418 1.00 25.89 ? 1668 GLU A O     1 
ATOM   1751  C  CB    . GLU A 1 1668 ? 161.218 220.325 251.360 1.00 24.72 ? 1668 GLU A CB    1 
ATOM   1752  C  CG    . GLU A 1 1668 ? 160.532 218.956 251.349 1.00 28.33 ? 1668 GLU A CG    1 
ATOM   1753  C  CD    . GLU A 1 1668 ? 159.263 218.910 250.509 1.00 31.91 ? 1668 GLU A CD    1 
ATOM   1754  O  OE1   . GLU A 1 1668 ? 158.821 219.965 250.008 1.00 26.16 ? 1668 GLU A OE1   1 
ATOM   1755  O  OE2   . GLU A 1 1668 ? 158.706 217.803 250.346 1.00 35.99 ? 1668 GLU A OE2   1 
ATOM   1756  N  N     . ASP A 1 1669 ? 161.556 219.008 248.362 1.00 21.81 ? 1669 ASP A N     1 
ATOM   1757  C  CA    . ASP A 1 1669 ? 162.018 217.862 247.588 1.00 19.95 ? 1669 ASP A CA    1 
ATOM   1758  C  C     . ASP A 1 1669 ? 162.913 218.318 246.439 1.00 19.83 ? 1669 ASP A C     1 
ATOM   1759  O  O     . ASP A 1 1669 ? 163.839 217.596 246.055 1.00 26.01 ? 1669 ASP A O     1 
ATOM   1760  C  CB    . ASP A 1 1669 ? 160.778 217.075 247.119 1.00 20.16 ? 1669 ASP A CB    1 
ATOM   1761  C  CG    . ASP A 1 1669 ? 161.071 215.947 246.118 1.00 27.55 ? 1669 ASP A CG    1 
ATOM   1762  O  OD1   . ASP A 1 1669 ? 160.178 215.084 245.992 1.00 34.17 ? 1669 ASP A OD1   1 
ATOM   1763  O  OD2   . ASP A 1 1669 ? 162.130 215.871 245.468 1.00 32.20 ? 1669 ASP A OD2   1 
ATOM   1764  N  N     . ASN A 1 1670 ? 162.704 219.547 245.946 1.00 21.18 ? 1670 ASN A N     1 
ATOM   1765  C  CA    . ASN A 1 1670 ? 163.307 220.061 244.712 1.00 18.64 ? 1670 ASN A CA    1 
ATOM   1766  C  C     . ASN A 1 1670 ? 162.706 219.394 243.480 1.00 18.00 ? 1670 ASN A C     1 
ATOM   1767  O  O     . ASN A 1 1670 ? 163.388 219.195 242.473 1.00 19.58 ? 1670 ASN A O     1 
ATOM   1768  C  CB    . ASN A 1 1670 ? 164.836 219.921 244.697 1.00 13.76 ? 1670 ASN A CB    1 
ATOM   1769  C  CG    . ASN A 1 1670 ? 165.509 220.737 245.779 1.00 21.67 ? 1670 ASN A CG    1 
ATOM   1770  O  OD1   . ASN A 1 1670 ? 165.461 221.968 245.767 1.00 23.09 ? 1670 ASN A OD1   1 
ATOM   1771  N  ND2   . ASN A 1 1670 ? 166.146 220.057 246.722 1.00 27.55 ? 1670 ASN A ND2   1 
ATOM   1772  N  N     . SER A 1 1671 ? 161.420 219.053 243.556 1.00 20.74 ? 1671 SER A N     1 
ATOM   1773  C  CA    . SER A 1 1671 ? 160.703 218.408 242.468 1.00 14.74 ? 1671 SER A CA    1 
ATOM   1774  C  C     . SER A 1 1671 ? 159.658 219.296 241.815 1.00 17.11 ? 1671 SER A C     1 
ATOM   1775  O  O     . SER A 1 1671 ? 159.175 218.957 240.731 1.00 17.35 ? 1671 SER A O     1 
ATOM   1776  C  CB    . SER A 1 1671 ? 160.017 217.132 242.974 1.00 15.89 ? 1671 SER A CB    1 
ATOM   1777  O  OG    . SER A 1 1671 ? 159.190 217.413 244.087 1.00 19.81 ? 1671 SER A OG    1 
ATOM   1778  N  N     . VAL A 1 1672 ? 159.284 220.404 242.447 1.00 15.80 ? 1672 VAL A N     1 
ATOM   1779  C  CA    . VAL A 1 1672 ? 158.305 221.334 241.902 1.00 11.13 ? 1672 VAL A CA    1 
ATOM   1780  C  C     . VAL A 1 1672 ? 158.908 222.731 241.929 1.00 9.86  ? 1672 VAL A C     1 
ATOM   1781  O  O     . VAL A 1 1672 ? 159.423 223.166 242.967 1.00 12.59 ? 1672 VAL A O     1 
ATOM   1782  C  CB    . VAL A 1 1672 ? 156.979 221.299 242.686 1.00 9.95  ? 1672 VAL A CB    1 
ATOM   1783  C  CG1   . VAL A 1 1672 ? 155.995 222.288 242.102 1.00 9.26  ? 1672 VAL A CG1   1 
ATOM   1784  C  CG2   . VAL A 1 1672 ? 156.394 219.899 242.684 1.00 8.61  ? 1672 VAL A CG2   1 
ATOM   1785  N  N     . VAL A 1 1673 ? 158.852 223.425 240.798 1.00 11.99 ? 1673 VAL A N     1 
ATOM   1786  C  CA    . VAL A 1 1673 ? 159.312 224.806 240.708 1.00 8.34  ? 1673 VAL A CA    1 
ATOM   1787  C  C     . VAL A 1 1673 ? 158.165 225.698 241.169 1.00 5.34  ? 1673 VAL A C     1 
ATOM   1788  O  O     . VAL A 1 1673 ? 157.163 225.850 240.466 1.00 8.78  ? 1673 VAL A O     1 
ATOM   1789  C  CB    . VAL A 1 1673 ? 159.759 225.163 239.286 1.00 7.74  ? 1673 VAL A CB    1 
ATOM   1790  C  CG1   . VAL A 1 1673 ? 160.026 226.658 239.170 1.00 7.30  ? 1673 VAL A CG1   1 
ATOM   1791  C  CG2   . VAL A 1 1673 ? 160.986 224.364 238.898 1.00 3.99  ? 1673 VAL A CG2   1 
ATOM   1792  N  N     . LEU A 1 1674 ? 158.303 226.271 242.365 1.00 6.54  ? 1674 LEU A N     1 
ATOM   1793  C  CA    . LEU A 1 1674 ? 157.253 227.123 242.911 1.00 6.78  ? 1674 LEU A CA    1 
ATOM   1794  C  C     . LEU A 1 1674 ? 157.243 228.511 242.283 1.00 4.74  ? 1674 LEU A C     1 
ATOM   1795  O  O     . LEU A 1 1674 ? 156.172 229.110 242.140 1.00 5.57  ? 1674 LEU A O     1 
ATOM   1796  C  CB    . LEU A 1 1674 ? 157.405 227.235 244.429 1.00 9.83  ? 1674 LEU A CB    1 
ATOM   1797  C  CG    . LEU A 1 1674 ? 157.027 225.986 245.224 1.00 6.70  ? 1674 LEU A CG    1 
ATOM   1798  C  CD1   . LEU A 1 1674 ? 157.083 226.260 246.714 1.00 12.02 ? 1674 LEU A CD1   1 
ATOM   1799  C  CD2   . LEU A 1 1674 ? 155.650 225.488 244.818 1.00 7.10  ? 1674 LEU A CD2   1 
ATOM   1800  N  N     . GLY A 1 1675 ? 158.402 229.041 241.912 1.00 5.55  ? 1675 GLY A N     1 
ATOM   1801  C  CA    . GLY A 1 1675 ? 158.447 230.369 241.337 1.00 3.25  ? 1675 GLY A CA    1 
ATOM   1802  C  C     . GLY A 1 1675 ? 159.852 230.742 240.917 1.00 4.30  ? 1675 GLY A C     1 
ATOM   1803  O  O     . GLY A 1 1675 ? 160.746 229.898 240.848 1.00 6.22  ? 1675 GLY A O     1 
ATOM   1804  N  N     . ILE A 1 1676 ? 160.031 232.034 240.636 1.00 3.43  ? 1676 ILE A N     1 
ATOM   1805  C  CA    . ILE A 1 1676 ? 161.306 232.580 240.200 1.00 3.56  ? 1676 ILE A CA    1 
ATOM   1806  C  C     . ILE A 1 1676 ? 161.668 233.759 241.092 1.00 2.91  ? 1676 ILE A C     1 
ATOM   1807  O  O     . ILE A 1 1676 ? 160.813 234.374 241.731 1.00 4.45  ? 1676 ILE A O     1 
ATOM   1808  C  CB    . ILE A 1 1676 ? 161.281 233.021 238.720 1.00 6.21  ? 1676 ILE A CB    1 
ATOM   1809  C  CG1   . ILE A 1 1676 ? 160.117 233.984 238.474 1.00 1.92  ? 1676 ILE A CG1   1 
ATOM   1810  C  CG2   . ILE A 1 1676 ? 161.208 231.809 237.803 1.00 1.09  ? 1676 ILE A CG2   1 
ATOM   1811  C  CD1   . ILE A 1 1676 ? 159.952 234.394 237.037 1.00 2.17  ? 1676 ILE A CD1   1 
ATOM   1812  N  N     . SER A 1 1677 ? 162.962 234.061 241.136 1.00 3.02  ? 1677 SER A N     1 
ATOM   1813  C  CA    . SER A 1 1677 ? 163.479 235.144 241.959 1.00 3.54  ? 1677 SER A CA    1 
ATOM   1814  C  C     . SER A 1 1677 ? 164.515 235.932 241.170 1.00 5.00  ? 1677 SER A C     1 
ATOM   1815  O  O     . SER A 1 1677 ? 165.141 235.421 240.239 1.00 4.97  ? 1677 SER A O     1 
ATOM   1816  C  CB    . SER A 1 1677 ? 164.088 234.617 243.264 1.00 4.60  ? 1677 SER A CB    1 
ATOM   1817  O  OG    . SER A 1 1677 ? 164.768 235.642 243.964 1.00 13.24 ? 1677 SER A OG    1 
ATOM   1818  N  N     . SER A 1 1678 ? 164.686 237.192 241.555 1.00 3.57  ? 1678 SER A N     1 
ATOM   1819  C  CA    . SER A 1 1678 ? 165.665 238.075 240.941 1.00 5.40  ? 1678 SER A CA    1 
ATOM   1820  C  C     . SER A 1 1678 ? 166.948 238.105 241.765 1.00 7.52  ? 1678 SER A C     1 
ATOM   1821  O  O     . SER A 1 1678 ? 167.030 237.550 242.863 1.00 7.15  ? 1678 SER A O     1 
ATOM   1822  C  CB    . SER A 1 1678 ? 165.096 239.488 240.792 1.00 5.51  ? 1678 SER A CB    1 
ATOM   1823  O  OG    . SER A 1 1678 ? 164.635 239.983 242.035 1.00 6.12  ? 1678 SER A OG    1 
ATOM   1824  N  N     . ARG A 1 1679 ? 167.961 238.776 241.217 1.00 8.18  ? 1679 ARG A N     1 
ATOM   1825  C  CA    . ARG A 1 1679 ? 169.237 238.898 241.913 1.00 6.56  ? 1679 ARG A CA    1 
ATOM   1826  C  C     . ARG A 1 1679 ? 169.139 239.771 243.158 1.00 9.23  ? 1679 ARG A C     1 
ATOM   1827  O  O     . ARG A 1 1679 ? 170.000 239.669 244.037 1.00 18.41 ? 1679 ARG A O     1 
ATOM   1828  C  CB    . ARG A 1 1679 ? 170.300 239.454 240.966 1.00 7.69  ? 1679 ARG A CB    1 
ATOM   1829  C  CG    . ARG A 1 1679 ? 170.055 240.885 240.526 1.00 12.11 ? 1679 ARG A CG    1 
ATOM   1830  C  CD    . ARG A 1 1679 ? 171.207 241.403 239.689 1.00 12.89 ? 1679 ARG A CD    1 
ATOM   1831  N  NE    . ARG A 1 1679 ? 171.465 240.546 238.537 1.00 20.97 ? 1679 ARG A NE    1 
ATOM   1832  C  CZ    . ARG A 1 1679 ? 172.492 240.691 237.710 1.00 25.86 ? 1679 ARG A CZ    1 
ATOM   1833  N  NH1   . ARG A 1 1679 ? 173.386 241.649 237.880 1.00 26.34 ? 1679 ARG A NH1   1 
ATOM   1834  N  NH2   . ARG A 1 1679 ? 172.624 239.851 236.687 1.00 20.13 ? 1679 ARG A NH2   1 
ATOM   1835  N  N     . GLU A 1 1680 ? 168.115 240.617 243.256 1.00 12.32 ? 1680 GLU A N     1 
ATOM   1836  C  CA    . GLU A 1 1680 ? 167.906 241.461 244.424 1.00 8.69  ? 1680 GLU A CA    1 
ATOM   1837  C  C     . GLU A 1 1680 ? 166.984 240.831 245.458 1.00 8.82  ? 1680 GLU A C     1 
ATOM   1838  O  O     . GLU A 1 1680 ? 166.698 241.461 246.479 1.00 18.63 ? 1680 GLU A O     1 
ATOM   1839  C  CB    . GLU A 1 1680 ? 167.342 242.823 244.004 1.00 9.22  ? 1680 GLU A CB    1 
ATOM   1840  C  CG    . GLU A 1 1680 ? 168.282 243.656 243.156 1.00 10.77 ? 1680 GLU A CG    1 
ATOM   1841  C  CD    . GLU A 1 1680 ? 167.903 243.658 241.691 1.00 17.15 ? 1680 GLU A CD    1 
ATOM   1842  O  OE1   . GLU A 1 1680 ? 168.521 244.419 240.917 1.00 20.03 ? 1680 GLU A OE1   1 
ATOM   1843  O  OE2   . GLU A 1 1680 ? 166.981 242.903 241.316 1.00 12.15 ? 1680 GLU A OE2   1 
ATOM   1844  N  N     . GLY A 1 1681 ? 166.508 239.612 245.219 1.00 7.06  ? 1681 GLY A N     1 
ATOM   1845  C  CA    . GLY A 1 1681 ? 165.672 238.907 246.165 1.00 6.50  ? 1681 GLY A CA    1 
ATOM   1846  C  C     . GLY A 1 1681 ? 164.185 238.968 245.889 1.00 10.26 ? 1681 GLY A C     1 
ATOM   1847  O  O     . GLY A 1 1681 ? 163.424 238.258 246.557 1.00 9.67  ? 1681 GLY A O     1 
ATOM   1848  N  N     . GLU A 1 1682 ? 163.747 239.790 244.938 1.00 8.82  ? 1682 GLU A N     1 
ATOM   1849  C  CA    . GLU A 1 1682 ? 162.329 239.869 244.617 1.00 8.50  ? 1682 GLU A CA    1 
ATOM   1850  C  C     . GLU A 1 1682 ? 161.852 238.550 244.020 1.00 6.39  ? 1682 GLU A C     1 
ATOM   1851  O  O     . GLU A 1 1682 ? 162.490 237.997 243.119 1.00 7.54  ? 1682 GLU A O     1 
ATOM   1852  C  CB    . GLU A 1 1682 ? 162.062 241.020 243.653 1.00 7.58  ? 1682 GLU A CB    1 
ATOM   1853  C  CG    . GLU A 1 1682 ? 160.589 241.267 243.381 1.00 5.61  ? 1682 GLU A CG    1 
ATOM   1854  C  CD    . GLU A 1 1682 ? 160.360 242.263 242.264 1.00 4.66  ? 1682 GLU A CD    1 
ATOM   1855  O  OE1   . GLU A 1 1682 ? 160.637 241.924 241.097 1.00 4.11  ? 1682 GLU A OE1   1 
ATOM   1856  O  OE2   . GLU A 1 1682 ? 159.906 243.387 242.554 1.00 8.20  ? 1682 GLU A OE2   1 
ATOM   1857  N  N     . GLU A 1 1683 ? 160.723 238.052 244.516 1.00 6.17  ? 1683 GLU A N     1 
ATOM   1858  C  CA    . GLU A 1 1683 ? 160.218 236.737 244.157 1.00 4.16  ? 1683 GLU A CA    1 
ATOM   1859  C  C     . GLU A 1 1683 ? 158.898 236.855 243.412 1.00 5.73  ? 1683 GLU A C     1 
ATOM   1860  O  O     . GLU A 1 1683 ? 158.066 237.710 243.731 1.00 9.60  ? 1683 GLU A O     1 
ATOM   1861  C  CB    . GLU A 1 1683 ? 160.023 235.863 245.399 1.00 5.09  ? 1683 GLU A CB    1 
ATOM   1862  C  CG    . GLU A 1 1683 ? 161.308 235.464 246.096 1.00 14.87 ? 1683 GLU A CG    1 
ATOM   1863  C  CD    . GLU A 1 1683 ? 161.067 234.509 247.249 1.00 21.56 ? 1683 GLU A CD    1 
ATOM   1864  O  OE1   . GLU A 1 1683 ? 159.893 234.167 247.501 1.00 21.86 ? 1683 GLU A OE1   1 
ATOM   1865  O  OE2   . GLU A 1 1683 ? 162.049 234.101 247.901 1.00 27.32 ? 1683 GLU A OE2   1 
ATOM   1866  N  N     . VAL A 1 1684 ? 158.714 235.992 242.419 1.00 2.80  ? 1684 VAL A N     1 
ATOM   1867  C  CA    . VAL A 1 1684 ? 157.438 235.818 241.738 1.00 2.91  ? 1684 VAL A CA    1 
ATOM   1868  C  C     . VAL A 1 1684 ? 156.980 234.391 241.998 1.00 4.25  ? 1684 VAL A C     1 
ATOM   1869  O  O     . VAL A 1 1684 ? 157.674 233.436 241.630 1.00 9.51  ? 1684 VAL A O     1 
ATOM   1870  C  CB    . VAL A 1 1684 ? 157.546 236.090 240.229 1.00 2.59  ? 1684 VAL A CB    1 
ATOM   1871  C  CG1   . VAL A 1 1684 ? 156.171 236.028 239.586 1.00 1.81  ? 1684 VAL A CG1   1 
ATOM   1872  C  CG2   . VAL A 1 1684 ? 158.207 237.434 239.970 1.00 2.41  ? 1684 VAL A CG2   1 
ATOM   1873  N  N     . MET A 1 1685 ? 155.822 234.245 242.630 1.00 2.97  ? 1685 MET A N     1 
ATOM   1874  C  CA    . MET A 1 1685 ? 155.264 232.936 242.947 1.00 3.82  ? 1685 MET A CA    1 
ATOM   1875  C  C     . MET A 1 1685 ? 154.286 232.540 241.849 1.00 5.34  ? 1685 MET A C     1 
ATOM   1876  O  O     . MET A 1 1685 ? 153.318 233.260 241.587 1.00 9.08  ? 1685 MET A O     1 
ATOM   1877  C  CB    . MET A 1 1685 ? 154.571 232.949 244.308 1.00 3.63  ? 1685 MET A CB    1 
ATOM   1878  C  CG    . MET A 1 1685 ? 155.524 232.929 245.491 1.00 8.21  ? 1685 MET A CG    1 
ATOM   1879  S  SD    . MET A 1 1685 ? 156.867 231.739 245.304 1.00 22.81 ? 1685 MET A SD    1 
ATOM   1880  C  CE    . MET A 1 1685 ? 156.166 230.314 246.130 1.00 7.18  ? 1685 MET A CE    1 
ATOM   1881  N  N     . PHE A 1 1686 ? 154.539 231.397 241.217 1.00 4.96  ? 1686 PHE A N     1 
ATOM   1882  C  CA    . PHE A 1 1686 ? 153.689 230.938 240.129 1.00 3.93  ? 1686 PHE A CA    1 
ATOM   1883  C  C     . PHE A 1 1686 ? 152.288 230.629 240.636 1.00 8.39  ? 1686 PHE A C     1 
ATOM   1884  O  O     . PHE A 1 1686 ? 152.107 230.110 241.741 1.00 14.47 ? 1686 PHE A O     1 
ATOM   1885  C  CB    . PHE A 1 1686 ? 154.285 229.695 239.471 1.00 3.42  ? 1686 PHE A CB    1 
ATOM   1886  C  CG    . PHE A 1 1686 ? 155.576 229.945 238.750 1.00 4.52  ? 1686 PHE A CG    1 
ATOM   1887  C  CD1   . PHE A 1 1686 ? 155.909 231.217 238.314 1.00 4.43  ? 1686 PHE A CD1   1 
ATOM   1888  C  CD2   . PHE A 1 1686 ? 156.454 228.904 238.501 1.00 2.76  ? 1686 PHE A CD2   1 
ATOM   1889  C  CE1   . PHE A 1 1686 ? 157.098 231.445 237.649 1.00 4.14  ? 1686 PHE A CE1   1 
ATOM   1890  C  CE2   . PHE A 1 1686 ? 157.642 229.126 237.837 1.00 2.47  ? 1686 PHE A CE2   1 
ATOM   1891  C  CZ    . PHE A 1 1686 ? 157.963 230.400 237.410 1.00 4.09  ? 1686 PHE A CZ    1 
ATOM   1892  N  N     . LYS A 1 1687 ? 151.285 230.964 239.824 1.00 7.07  ? 1687 LYS A N     1 
ATOM   1893  C  CA    . LYS A 1 1687 ? 149.914 230.605 240.172 1.00 11.41 ? 1687 LYS A CA    1 
ATOM   1894  C  C     . LYS A 1 1687 ? 149.703 229.101 240.054 1.00 12.19 ? 1687 LYS A C     1 
ATOM   1895  O  O     . LYS A 1 1687 ? 149.038 228.493 240.900 1.00 17.53 ? 1687 LYS A O     1 
ATOM   1896  C  CB    . LYS A 1 1687 ? 148.929 231.367 239.286 1.00 8.00  ? 1687 LYS A CB    1 
ATOM   1897  C  CG    . LYS A 1 1687 ? 149.428 232.729 238.837 1.00 9.26  ? 1687 LYS A CG    1 
ATOM   1898  C  CD    . LYS A 1 1687 ? 149.511 233.711 239.999 1.00 11.37 ? 1687 LYS A CD    1 
ATOM   1899  C  CE    . LYS A 1 1687 ? 148.174 234.370 240.282 1.00 12.80 ? 1687 LYS A CE    1 
ATOM   1900  N  NZ    . LYS A 1 1687 ? 148.195 235.123 241.565 1.00 8.20  ? 1687 LYS A NZ    1 
ATOM   1901  N  N     . THR A 1 1688 ? 150.262 228.488 239.018 1.00 11.10 ? 1688 THR A N     1 
ATOM   1902  C  CA    . THR A 1 1688 ? 150.246 227.036 238.851 1.00 11.02 ? 1688 THR A CA    1 
ATOM   1903  C  C     . THR A 1 1688 ? 151.680 226.523 238.870 1.00 9.88  ? 1688 THR A C     1 
ATOM   1904  O  O     . THR A 1 1688 ? 152.422 226.734 237.892 1.00 9.15  ? 1688 THR A O     1 
ATOM   1905  C  CB    . THR A 1 1688 ? 149.553 226.642 237.547 1.00 16.59 ? 1688 THR A CB    1 
ATOM   1906  O  OG1   . THR A 1 1688 ? 148.179 227.046 237.596 1.00 19.54 ? 1688 THR A OG1   1 
ATOM   1907  C  CG2   . THR A 1 1688 ? 149.616 225.141 237.344 1.00 16.74 ? 1688 THR A CG2   1 
ATOM   1908  N  N     . PRO A 1 1689 ? 152.120 225.866 239.943 1.00 14.05 ? 1689 PRO A N     1 
ATOM   1909  C  CA    . PRO A 1 1689 ? 153.518 225.429 240.023 1.00 11.88 ? 1689 PRO A CA    1 
ATOM   1910  C  C     . PRO A 1 1689 ? 153.858 224.374 238.980 1.00 7.01  ? 1689 PRO A C     1 
ATOM   1911  O  O     . PRO A 1 1689 ? 153.002 223.613 238.525 1.00 11.53 ? 1689 PRO A O     1 
ATOM   1912  C  CB    . PRO A 1 1689 ? 153.631 224.862 241.444 1.00 9.42  ? 1689 PRO A CB    1 
ATOM   1913  C  CG    . PRO A 1 1689 ? 152.471 225.445 242.186 1.00 12.52 ? 1689 PRO A CG    1 
ATOM   1914  C  CD    . PRO A 1 1689 ? 151.380 225.571 241.179 1.00 9.22  ? 1689 PRO A CD    1 
ATOM   1915  N  N     . VAL A 1 1690 ? 155.134 224.340 238.608 1.00 7.67  ? 1690 VAL A N     1 
ATOM   1916  C  CA    . VAL A 1 1690 ? 155.645 223.442 237.576 1.00 6.68  ? 1690 VAL A CA    1 
ATOM   1917  C  C     . VAL A 1 1690 ? 156.292 222.243 238.257 1.00 9.94  ? 1690 VAL A C     1 
ATOM   1918  O  O     . VAL A 1 1690 ? 157.226 222.400 239.051 1.00 10.26 ? 1690 VAL A O     1 
ATOM   1919  C  CB    . VAL A 1 1690 ? 156.649 224.159 236.661 1.00 6.18  ? 1690 VAL A CB    1 
ATOM   1920  C  CG1   . VAL A 1 1690 ? 157.281 223.178 235.689 1.00 5.15  ? 1690 VAL A CG1   1 
ATOM   1921  C  CG2   . VAL A 1 1690 ? 155.977 225.293 235.923 1.00 5.13  ? 1690 VAL A CG2   1 
ATOM   1922  N  N     . SER A 1 1691 ? 155.811 221.046 237.932 1.00 11.19 ? 1691 SER A N     1 
ATOM   1923  C  CA    . SER A 1 1691 ? 156.332 219.819 238.520 1.00 11.66 ? 1691 SER A CA    1 
ATOM   1924  C  C     . SER A 1 1691 ? 157.432 219.244 237.637 1.00 16.01 ? 1691 SER A C     1 
ATOM   1925  O  O     . SER A 1 1691 ? 157.216 218.999 236.447 1.00 9.06  ? 1691 SER A O     1 
ATOM   1926  C  CB    . SER A 1 1691 ? 155.214 218.792 238.706 1.00 15.36 ? 1691 SER A CB    1 
ATOM   1927  O  OG    . SER A 1 1691 ? 155.739 217.488 238.853 1.00 15.76 ? 1691 SER A OG    1 
ATOM   1928  N  N     . ILE A 1 1692 ? 158.608 219.031 238.228 1.00 14.01 ? 1692 ILE A N     1 
ATOM   1929  C  CA    . ILE A 1 1692 ? 159.712 218.453 237.475 1.00 13.05 ? 1692 ILE A CA    1 
ATOM   1930  C  C     . ILE A 1 1692 ? 159.550 216.941 237.343 1.00 17.20 ? 1692 ILE A C     1 
ATOM   1931  O  O     . ILE A 1 1692 ? 159.996 216.352 236.354 1.00 17.10 ? 1692 ILE A O     1 
ATOM   1932  C  CB    . ILE A 1 1692 ? 161.055 218.833 238.124 1.00 13.74 ? 1692 ILE A CB    1 
ATOM   1933  C  CG1   . ILE A 1 1692 ? 161.224 220.352 238.134 1.00 7.60  ? 1692 ILE A CG1   1 
ATOM   1934  C  CG2   . ILE A 1 1692 ? 162.223 218.185 237.395 1.00 10.10 ? 1692 ILE A CG2   1 
ATOM   1935  C  CD1   . ILE A 1 1692 ? 162.583 220.817 238.602 1.00 5.35  ? 1692 ILE A CD1   1 
ATOM   1936  N  N     . THR A 1 1693 ? 158.900 216.290 238.312 1.00 15.39 ? 1693 THR A N     1 
ATOM   1937  C  CA    . THR A 1 1693 ? 158.703 214.846 238.223 1.00 13.73 ? 1693 THR A CA    1 
ATOM   1938  C  C     . THR A 1 1693 ? 157.830 214.475 237.032 1.00 11.95 ? 1693 THR A C     1 
ATOM   1939  O  O     . THR A 1 1693 ? 158.108 213.494 236.333 1.00 16.07 ? 1693 THR A O     1 
ATOM   1940  C  CB    . THR A 1 1693 ? 158.089 214.306 239.515 1.00 17.18 ? 1693 THR A CB    1 
ATOM   1941  O  OG1   . THR A 1 1693 ? 156.786 214.874 239.702 1.00 16.12 ? 1693 THR A OG1   1 
ATOM   1942  C  CG2   . THR A 1 1693 ? 158.967 214.639 240.703 1.00 13.25 ? 1693 THR A CG2   1 
ATOM   1943  N  N     . GLU A 1 1694 ? 156.767 215.243 236.787 1.00 11.52 ? 1694 GLU A N     1 
ATOM   1944  C  CA    . GLU A 1 1694 ? 155.847 214.896 235.707 1.00 12.18 ? 1694 GLU A CA    1 
ATOM   1945  C  C     . GLU A 1 1694 ? 156.405 215.299 234.349 1.00 12.27 ? 1694 GLU A C     1 
ATOM   1946  O  O     . GLU A 1 1694 ? 155.942 214.810 233.312 1.00 10.23 ? 1694 GLU A O     1 
ATOM   1947  C  CB    . GLU A 1 1694 ? 154.486 215.543 235.955 1.00 12.49 ? 1694 GLU A CB    1 
ATOM   1948  C  CG    . GLU A 1 1694 ? 153.763 214.978 237.168 1.00 19.66 ? 1694 GLU A CG    1 
ATOM   1949  C  CD    . GLU A 1 1694 ? 152.423 215.639 237.418 1.00 29.82 ? 1694 GLU A CD    1 
ATOM   1950  O  OE1   . GLU A 1 1694 ? 152.104 216.624 236.722 1.00 32.02 ? 1694 GLU A OE1   1 
ATOM   1951  O  OE2   . GLU A 1 1694 ? 151.687 215.168 238.311 1.00 24.67 ? 1694 GLU A OE2   1 
ATOM   1952  N  N     . HIS A 1 1695 ? 157.395 216.193 234.331 1.00 16.72 ? 1695 HIS A N     1 
ATOM   1953  C  CA    . HIS A 1 1695 ? 158.106 216.587 233.118 1.00 12.77 ? 1695 HIS A CA    1 
ATOM   1954  C  C     . HIS A 1 1695 ? 159.598 216.507 233.399 1.00 13.44 ? 1695 HIS A C     1 
ATOM   1955  O  O     . HIS A 1 1695 ? 160.253 217.538 233.616 1.00 12.95 ? 1695 HIS A O     1 
ATOM   1956  C  CB    . HIS A 1 1695 ? 157.704 217.995 232.675 1.00 10.70 ? 1695 HIS A CB    1 
ATOM   1957  C  CG    . HIS A 1 1695 ? 156.224 218.187 232.556 1.00 13.46 ? 1695 HIS A CG    1 
ATOM   1958  N  ND1   . HIS A 1 1695 ? 155.540 217.977 231.379 1.00 10.90 ? 1695 HIS A ND1   1 
ATOM   1959  C  CD2   . HIS A 1 1695 ? 155.297 218.566 233.468 1.00 9.56  ? 1695 HIS A CD2   1 
ATOM   1960  C  CE1   . HIS A 1 1695 ? 154.256 218.220 231.569 1.00 15.86 ? 1695 HIS A CE1   1 
ATOM   1961  N  NE2   . HIS A 1 1695 ? 154.082 218.578 232.828 1.00 12.73 ? 1695 HIS A NE2   1 
ATOM   1962  N  N     . PRO A 1 1696 ? 160.186 215.307 233.408 1.00 12.94 ? 1696 PRO A N     1 
ATOM   1963  C  CA    . PRO A 1 1696 ? 161.554 215.169 233.936 1.00 9.45  ? 1696 PRO A CA    1 
ATOM   1964  C  C     . PRO A 1 1696 ? 162.617 215.839 233.089 1.00 9.46  ? 1696 PRO A C     1 
ATOM   1965  O  O     . PRO A 1 1696 ? 163.564 216.410 233.639 1.00 13.72 ? 1696 PRO A O     1 
ATOM   1966  C  CB    . PRO A 1 1696 ? 161.748 213.646 233.989 1.00 10.79 ? 1696 PRO A CB    1 
ATOM   1967  C  CG    . PRO A 1 1696 ? 160.356 213.082 233.956 1.00 12.59 ? 1696 PRO A CG    1 
ATOM   1968  C  CD    . PRO A 1 1696 ? 159.608 214.002 233.057 1.00 8.76  ? 1696 PRO A CD    1 
ATOM   1969  N  N     . LYS A 1 1697 ? 162.496 215.783 231.767 1.00 10.52 ? 1697 LYS A N     1 
ATOM   1970  C  CA    . LYS A 1 1697 ? 163.592 216.209 230.909 1.00 13.29 ? 1697 LYS A CA    1 
ATOM   1971  C  C     . LYS A 1 1697 ? 163.758 217.726 230.966 1.00 13.84 ? 1697 LYS A C     1 
ATOM   1972  O  O     . LYS A 1 1697 ? 162.785 218.473 231.097 1.00 11.92 ? 1697 LYS A O     1 
ATOM   1973  C  CB    . LYS A 1 1697 ? 163.351 215.713 229.482 1.00 13.28 ? 1697 LYS A CB    1 
ATOM   1974  C  CG    . LYS A 1 1697 ? 164.451 216.032 228.493 1.00 16.58 ? 1697 LYS A CG    1 
ATOM   1975  C  CD    . LYS A 1 1697 ? 164.164 215.395 227.145 1.00 17.30 ? 1697 LYS A CD    1 
ATOM   1976  C  CE    . LYS A 1 1697 ? 165.181 215.827 226.102 1.00 24.02 ? 1697 LYS A CE    1 
ATOM   1977  N  NZ    . LYS A 1 1697 ? 166.543 215.316 226.420 1.00 17.60 ? 1697 LYS A NZ    1 
ATOM   1978  N  N     . ILE A 1 1698 ? 165.013 218.173 230.875 1.00 17.56 ? 1698 ILE A N     1 
ATOM   1979  C  CA    . ILE A 1 1698 ? 165.381 219.527 231.286 1.00 8.39  ? 1698 ILE A CA    1 
ATOM   1980  C  C     . ILE A 1 1698 ? 164.707 220.582 230.413 1.00 9.55  ? 1698 ILE A C     1 
ATOM   1981  O  O     . ILE A 1 1698 ? 164.313 221.648 230.900 1.00 13.27 ? 1698 ILE A O     1 
ATOM   1982  C  CB    . ILE A 1 1698 ? 166.916 219.677 231.291 1.00 10.26 ? 1698 ILE A CB    1 
ATOM   1983  C  CG1   . ILE A 1 1698 ? 167.348 220.965 231.993 1.00 8.99  ? 1698 ILE A CG1   1 
ATOM   1984  C  CG2   . ILE A 1 1698 ? 167.486 219.600 229.889 1.00 11.30 ? 1698 ILE A CG2   1 
ATOM   1985  C  CD1   . ILE A 1 1698 ? 167.051 220.989 233.456 1.00 8.11  ? 1698 ILE A CD1   1 
ATOM   1986  N  N     . ASN A 1 1699 ? 164.566 220.314 229.114 1.00 11.41 ? 1699 ASN A N     1 
ATOM   1987  C  CA    . ASN A 1 1699 ? 164.108 221.350 228.196 1.00 8.39  ? 1699 ASN A CA    1 
ATOM   1988  C  C     . ASN A 1 1699 ? 162.596 221.541 228.209 1.00 10.89 ? 1699 ASN A C     1 
ATOM   1989  O  O     . ASN A 1 1699 ? 162.113 222.555 227.696 1.00 11.81 ? 1699 ASN A O     1 
ATOM   1990  C  CB    . ASN A 1 1699 ? 164.582 221.041 226.778 1.00 7.91  ? 1699 ASN A CB    1 
ATOM   1991  C  CG    . ASN A 1 1699 ? 163.921 219.813 226.203 1.00 12.30 ? 1699 ASN A CG    1 
ATOM   1992  O  OD1   . ASN A 1 1699 ? 164.087 218.714 226.720 1.00 14.28 ? 1699 ASN A OD1   1 
ATOM   1993  N  ND2   . ASN A 1 1699 ? 163.149 219.994 225.141 1.00 14.25 ? 1699 ASN A ND2   1 
ATOM   1994  N  N     . GLU A 1 1700 ? 161.834 220.603 228.772 1.00 8.63  ? 1700 GLU A N     1 
ATOM   1995  C  CA    . GLU A 1 1700 ? 160.385 220.767 228.815 1.00 9.77  ? 1700 GLU A CA    1 
ATOM   1996  C  C     . GLU A 1 1700 ? 159.928 221.535 230.049 1.00 9.92  ? 1700 GLU A C     1 
ATOM   1997  O  O     . GLU A 1 1700 ? 159.109 222.453 229.938 1.00 10.12 ? 1700 GLU A O     1 
ATOM   1998  C  CB    . GLU A 1 1700 ? 159.688 219.409 228.728 1.00 11.17 ? 1700 GLU A CB    1 
ATOM   1999  C  CG    . GLU A 1 1700 ? 159.853 218.724 227.382 1.00 15.69 ? 1700 GLU A CG    1 
ATOM   2000  C  CD    . GLU A 1 1700 ? 161.160 217.995 227.259 1.00 23.15 ? 1700 GLU A CD    1 
ATOM   2001  O  OE1   . GLU A 1 1700 ? 161.906 217.980 228.254 1.00 28.64 ? 1700 GLU A OE1   1 
ATOM   2002  O  OE2   . GLU A 1 1700 ? 161.442 217.439 226.178 1.00 26.40 ? 1700 GLU A OE2   1 
ATOM   2003  N  N     . TRP A 1 1701 ? 160.430 221.182 231.236 1.00 7.25  ? 1701 TRP A N     1 
ATOM   2004  C  CA    . TRP A 1 1701 ? 160.017 221.939 232.411 1.00 5.26  ? 1701 TRP A CA    1 
ATOM   2005  C  C     . TRP A 1 1701 ? 160.635 223.331 232.431 1.00 3.97  ? 1701 TRP A C     1 
ATOM   2006  O  O     . TRP A 1 1701 ? 160.042 224.249 233.004 1.00 6.63  ? 1701 TRP A O     1 
ATOM   2007  C  CB    . TRP A 1 1701 ? 160.341 221.185 233.710 1.00 7.28  ? 1701 TRP A CB    1 
ATOM   2008  C  CG    . TRP A 1 1701 ? 161.790 221.113 234.100 1.00 6.91  ? 1701 TRP A CG    1 
ATOM   2009  C  CD1   . TRP A 1 1701 ? 162.657 220.090 233.854 1.00 7.51  ? 1701 TRP A CD1   1 
ATOM   2010  C  CD2   . TRP A 1 1701 ? 162.531 222.094 234.838 1.00 6.72  ? 1701 TRP A CD2   1 
ATOM   2011  N  NE1   . TRP A 1 1701 ? 163.893 220.380 234.381 1.00 7.04  ? 1701 TRP A NE1   1 
ATOM   2012  C  CE2   . TRP A 1 1701 ? 163.841 221.605 234.988 1.00 6.09  ? 1701 TRP A CE2   1 
ATOM   2013  C  CE3   . TRP A 1 1701 ? 162.214 223.344 235.378 1.00 4.11  ? 1701 TRP A CE3   1 
ATOM   2014  C  CZ2   . TRP A 1 1701 ? 164.832 222.320 235.658 1.00 4.26  ? 1701 TRP A CZ2   1 
ATOM   2015  C  CZ3   . TRP A 1 1701 ? 163.199 224.050 236.037 1.00 4.32  ? 1701 TRP A CZ3   1 
ATOM   2016  C  CH2   . TRP A 1 1701 ? 164.492 223.538 236.171 1.00 3.71  ? 1701 TRP A CH2   1 
ATOM   2017  N  N     . LEU A 1 1702 ? 161.803 223.510 231.810 1.00 5.02  ? 1702 LEU A N     1 
ATOM   2018  C  CA    . LEU A 1 1702 ? 162.337 224.855 231.619 1.00 4.58  ? 1702 LEU A CA    1 
ATOM   2019  C  C     . LEU A 1 1702 ? 161.425 225.679 230.721 1.00 5.00  ? 1702 LEU A C     1 
ATOM   2020  O  O     . LEU A 1 1702 ? 161.238 226.879 230.946 1.00 7.45  ? 1702 LEU A O     1 
ATOM   2021  C  CB    . LEU A 1 1702 ? 163.746 224.788 231.033 1.00 4.79  ? 1702 LEU A CB    1 
ATOM   2022  C  CG    . LEU A 1 1702 ? 164.908 224.824 232.026 1.00 3.57  ? 1702 LEU A CG    1 
ATOM   2023  C  CD1   . LEU A 1 1702 ? 166.233 224.817 231.286 1.00 5.48  ? 1702 LEU A CD1   1 
ATOM   2024  C  CD2   . LEU A 1 1702 ? 164.804 226.038 232.934 1.00 3.15  ? 1702 LEU A CD2   1 
ATOM   2025  N  N     . THR A 1 1703 ? 160.859 225.049 229.686 1.00 3.80  ? 1703 THR A N     1 
ATOM   2026  C  CA    . THR A 1 1703 ? 159.873 225.727 228.853 1.00 3.97  ? 1703 THR A CA    1 
ATOM   2027  C  C     . THR A 1 1703 ? 158.613 226.054 229.647 1.00 4.14  ? 1703 THR A C     1 
ATOM   2028  O  O     . THR A 1 1703 ? 158.048 227.145 229.508 1.00 7.10  ? 1703 THR A O     1 
ATOM   2029  C  CB    . THR A 1 1703 ? 159.534 224.867 227.634 1.00 4.17  ? 1703 THR A CB    1 
ATOM   2030  O  OG1   . THR A 1 1703 ? 160.718 224.647 226.859 1.00 9.79  ? 1703 THR A OG1   1 
ATOM   2031  C  CG2   . THR A 1 1703 ? 158.492 225.549 226.764 1.00 6.69  ? 1703 THR A CG2   1 
ATOM   2032  N  N     . LEU A 1 1704 ? 158.159 225.122 230.491 1.00 2.91  ? 1704 LEU A N     1 
ATOM   2033  C  CA    . LEU A 1 1704 ? 156.974 225.378 231.303 1.00 3.42  ? 1704 LEU A CA    1 
ATOM   2034  C  C     . LEU A 1 1704 ? 157.229 226.477 232.328 1.00 5.82  ? 1704 LEU A C     1 
ATOM   2035  O  O     . LEU A 1 1704 ? 156.324 227.254 232.649 1.00 6.12  ? 1704 LEU A O     1 
ATOM   2036  C  CB    . LEU A 1 1704 ? 156.516 224.094 231.994 1.00 4.76  ? 1704 LEU A CB    1 
ATOM   2037  C  CG    . LEU A 1 1704 ? 156.140 222.919 231.088 1.00 4.11  ? 1704 LEU A CG    1 
ATOM   2038  C  CD1   . LEU A 1 1704 ? 155.831 221.684 231.913 1.00 7.46  ? 1704 LEU A CD1   1 
ATOM   2039  C  CD2   . LEU A 1 1704 ? 154.963 223.279 230.204 1.00 2.99  ? 1704 LEU A CD2   1 
ATOM   2040  N  N     . VAL A 1 1705 ? 158.451 226.549 232.861 1.00 5.56  ? 1705 VAL A N     1 
ATOM   2041  C  CA    . VAL A 1 1705 ? 158.803 227.639 233.767 1.00 4.64  ? 1705 VAL A CA    1 
ATOM   2042  C  C     . VAL A 1 1705 ? 158.758 228.974 233.034 1.00 3.42  ? 1705 VAL A C     1 
ATOM   2043  O  O     . VAL A 1 1705 ? 158.264 229.976 233.566 1.00 7.52  ? 1705 VAL A O     1 
ATOM   2044  C  CB    . VAL A 1 1705 ? 160.182 227.381 234.407 1.00 3.74  ? 1705 VAL A CB    1 
ATOM   2045  C  CG1   . VAL A 1 1705 ? 160.733 228.650 235.037 1.00 1.16  ? 1705 VAL A CG1   1 
ATOM   2046  C  CG2   . VAL A 1 1705 ? 160.073 226.286 235.452 1.00 1.88  ? 1705 VAL A CG2   1 
ATOM   2047  N  N     . GLU A 1 1706 ? 159.266 229.008 231.801 1.00 2.47  ? 1706 GLU A N     1 
ATOM   2048  C  CA    . GLU A 1 1706 ? 159.245 230.238 231.018 1.00 3.41  ? 1706 GLU A CA    1 
ATOM   2049  C  C     . GLU A 1 1706 ? 157.815 230.674 230.714 1.00 4.75  ? 1706 GLU A C     1 
ATOM   2050  O  O     . GLU A 1 1706 ? 157.513 231.872 230.682 1.00 4.04  ? 1706 GLU A O     1 
ATOM   2051  C  CB    . GLU A 1 1706 ? 160.052 230.038 229.731 1.00 3.73  ? 1706 GLU A CB    1 
ATOM   2052  C  CG    . GLU A 1 1706 ? 159.855 231.099 228.661 1.00 5.18  ? 1706 GLU A CG    1 
ATOM   2053  C  CD    . GLU A 1 1706 ? 160.400 230.667 227.311 1.00 14.52 ? 1706 GLU A CD    1 
ATOM   2054  O  OE1   . GLU A 1 1706 ? 159.964 229.614 226.803 1.00 17.36 ? 1706 GLU A OE1   1 
ATOM   2055  O  OE2   . GLU A 1 1706 ? 161.263 231.378 226.758 1.00 16.00 ? 1706 GLU A OE2   1 
ATOM   2056  N  N     . LYS A 1 1707 ? 156.916 229.713 230.491 1.00 5.29  ? 1707 LYS A N     1 
ATOM   2057  C  CA    . LYS A 1 1707 ? 155.520 230.050 230.224 1.00 3.69  ? 1707 LYS A CA    1 
ATOM   2058  C  C     . LYS A 1 1707 ? 154.802 230.504 231.491 1.00 4.13  ? 1707 LYS A C     1 
ATOM   2059  O  O     . LYS A 1 1707 ? 154.054 231.487 231.472 1.00 6.31  ? 1707 LYS A O     1 
ATOM   2060  C  CB    . LYS A 1 1707 ? 154.800 228.860 229.590 1.00 4.20  ? 1707 LYS A CB    1 
ATOM   2061  C  CG    . LYS A 1 1707 ? 155.288 228.521 228.195 1.00 6.63  ? 1707 LYS A CG    1 
ATOM   2062  C  CD    . LYS A 1 1707 ? 154.499 227.370 227.598 1.00 9.60  ? 1707 LYS A CD    1 
ATOM   2063  C  CE    . LYS A 1 1707 ? 155.045 226.983 226.237 1.00 10.73 ? 1707 LYS A CE    1 
ATOM   2064  N  NZ    . LYS A 1 1707 ? 154.819 228.054 225.231 1.00 12.77 ? 1707 LYS A NZ    1 
ATOM   2065  N  N     . GLU A 1 1708 ? 155.007 229.795 232.606 1.00 3.68  ? 1708 GLU A N     1 
ATOM   2066  C  CA    . GLU A 1 1708 ? 154.370 230.198 233.858 1.00 4.79  ? 1708 GLU A CA    1 
ATOM   2067  C  C     . GLU A 1 1708 ? 154.865 231.555 234.332 1.00 3.58  ? 1708 GLU A C     1 
ATOM   2068  O  O     . GLU A 1 1708 ? 154.122 232.297 234.981 1.00 3.51  ? 1708 GLU A O     1 
ATOM   2069  C  CB    . GLU A 1 1708 ? 154.590 229.147 234.945 1.00 3.60  ? 1708 GLU A CB    1 
ATOM   2070  C  CG    . GLU A 1 1708 ? 153.902 227.833 234.684 1.00 13.04 ? 1708 GLU A CG    1 
ATOM   2071  C  CD    . GLU A 1 1708 ? 152.395 227.960 234.730 1.00 26.25 ? 1708 GLU A CD    1 
ATOM   2072  O  OE1   . GLU A 1 1708 ? 151.894 228.808 235.501 1.00 18.34 ? 1708 GLU A OE1   1 
ATOM   2073  O  OE2   . GLU A 1 1708 ? 151.707 227.213 234.000 1.00 28.61 ? 1708 GLU A OE2   1 
ATOM   2074  N  N     . MET A 1 1709 ? 156.116 231.899 234.026 1.00 2.54  ? 1709 MET A N     1 
ATOM   2075  C  CA    . MET A 1 1709 ? 156.601 233.235 234.356 1.00 1.95  ? 1709 MET A CA    1 
ATOM   2076  C  C     . MET A 1 1709 ? 155.772 234.295 233.641 1.00 2.61  ? 1709 MET A C     1 
ATOM   2077  O  O     . MET A 1 1709 ? 155.365 235.293 234.245 1.00 2.79  ? 1709 MET A O     1 
ATOM   2078  C  CB    . MET A 1 1709 ? 158.081 233.364 234.001 1.00 1.85  ? 1709 MET A CB    1 
ATOM   2079  C  CG    . MET A 1 1709 ? 158.525 234.779 233.670 1.00 1.75  ? 1709 MET A CG    1 
ATOM   2080  S  SD    . MET A 1 1709 ? 160.130 234.855 232.853 1.00 3.45  ? 1709 MET A SD    1 
ATOM   2081  C  CE    . MET A 1 1709 ? 159.655 234.645 231.139 1.00 1.55  ? 1709 MET A CE    1 
ATOM   2082  N  N     . ARG A 1 1710 ? 155.485 234.075 232.358 1.00 3.35  ? 1710 ARG A N     1 
ATOM   2083  C  CA    . ARG A 1 1710 ? 154.688 235.032 231.598 1.00 1.72  ? 1710 ARG A CA    1 
ATOM   2084  C  C     . ARG A 1 1710 ? 153.233 235.028 232.050 1.00 1.87  ? 1710 ARG A C     1 
ATOM   2085  O  O     . ARG A 1 1710 ? 152.603 236.085 232.160 1.00 4.08  ? 1710 ARG A O     1 
ATOM   2086  C  CB    . ARG A 1 1710 ? 154.798 234.729 230.105 1.00 1.88  ? 1710 ARG A CB    1 
ATOM   2087  C  CG    . ARG A 1 1710 ? 156.185 234.957 229.539 1.00 1.11  ? 1710 ARG A CG    1 
ATOM   2088  C  CD    . ARG A 1 1710 ? 156.212 234.772 228.037 1.00 1.20  ? 1710 ARG A CD    1 
ATOM   2089  N  NE    . ARG A 1 1710 ? 157.524 235.073 227.477 1.00 4.42  ? 1710 ARG A NE    1 
ATOM   2090  C  CZ    . ARG A 1 1710 ? 158.271 234.204 226.809 1.00 7.30  ? 1710 ARG A CZ    1 
ATOM   2091  N  NH1   . ARG A 1 1710 ? 157.873 232.957 226.612 1.00 6.39  ? 1710 ARG A NH1   1 
ATOM   2092  N  NH2   . ARG A 1 1710 ? 159.447 234.595 226.330 1.00 3.52  ? 1710 ARG A NH2   1 
ATOM   2093  N  N     . VAL A 1 1711 ? 152.681 233.844 232.321 1.00 3.63  ? 1711 VAL A N     1 
ATOM   2094  C  CA    . VAL A 1 1711 ? 151.274 233.748 232.703 1.00 2.29  ? 1711 VAL A CA    1 
ATOM   2095  C  C     . VAL A 1 1711 ? 151.052 234.324 234.097 1.00 2.31  ? 1711 VAL A C     1 
ATOM   2096  O  O     . VAL A 1 1711 ? 150.063 235.024 234.343 1.00 4.75  ? 1711 VAL A O     1 
ATOM   2097  C  CB    . VAL A 1 1711 ? 150.795 232.288 232.600 1.00 2.99  ? 1711 VAL A CB    1 
ATOM   2098  C  CG1   . VAL A 1 1711 ? 149.427 232.123 233.234 1.00 3.20  ? 1711 VAL A CG1   1 
ATOM   2099  C  CG2   . VAL A 1 1711 ? 150.758 231.855 231.145 1.00 1.83  ? 1711 VAL A CG2   1 
ATOM   2100  N  N     . THR A 1 1712 ? 151.961 234.038 235.031 1.00 2.83  ? 1712 THR A N     1 
ATOM   2101  C  CA    . THR A 1 1712 ? 151.815 234.547 236.391 1.00 3.27  ? 1712 THR A CA    1 
ATOM   2102  C  C     . THR A 1 1712 ? 151.898 236.068 236.422 1.00 2.44  ? 1712 THR A C     1 
ATOM   2103  O  O     . THR A 1 1712 ? 151.110 236.731 237.106 1.00 2.44  ? 1712 THR A O     1 
ATOM   2104  C  CB    . THR A 1 1712 ? 152.883 233.933 237.300 1.00 3.30  ? 1712 THR A CB    1 
ATOM   2105  O  OG1   . THR A 1 1712 ? 152.692 232.515 237.373 1.00 5.33  ? 1712 THR A OG1   1 
ATOM   2106  C  CG2   . THR A 1 1712 ? 152.813 234.525 238.695 1.00 2.63  ? 1712 THR A CG2   1 
ATOM   2107  N  N     . LEU A 1 1713 ? 152.852 236.637 235.684 1.00 2.34  ? 1713 LEU A N     1 
ATOM   2108  C  CA    . LEU A 1 1713 ? 153.002 238.087 235.642 1.00 1.26  ? 1713 LEU A CA    1 
ATOM   2109  C  C     . LEU A 1 1713 ? 151.773 238.760 235.043 1.00 1.71  ? 1713 LEU A C     1 
ATOM   2110  O  O     . LEU A 1 1713 ? 151.335 239.809 235.527 1.00 5.23  ? 1713 LEU A O     1 
ATOM   2111  C  CB    . LEU A 1 1713 ? 154.254 238.454 234.853 1.00 1.28  ? 1713 LEU A CB    1 
ATOM   2112  C  CG    . LEU A 1 1713 ? 155.574 238.139 235.554 1.00 0.97  ? 1713 LEU A CG    1 
ATOM   2113  C  CD1   . LEU A 1 1713 ? 156.741 238.525 234.675 1.00 0.74  ? 1713 LEU A CD1   1 
ATOM   2114  C  CD2   . LEU A 1 1713 ? 155.636 238.859 236.890 1.00 0.88  ? 1713 LEU A CD2   1 
ATOM   2115  N  N     . ALA A 1 1714 ? 151.210 238.180 233.981 1.00 1.78  ? 1714 ALA A N     1 
ATOM   2116  C  CA    . ALA A 1 1714 ? 149.993 238.734 233.397 1.00 1.71  ? 1714 ALA A CA    1 
ATOM   2117  C  C     . ALA A 1 1714 ? 148.818 238.631 234.364 1.00 1.43  ? 1714 ALA A C     1 
ATOM   2118  O  O     . ALA A 1 1714 ? 148.020 239.569 234.480 1.00 2.02  ? 1714 ALA A O     1 
ATOM   2119  C  CB    . ALA A 1 1714 ? 149.676 238.034 232.076 1.00 1.80  ? 1714 ALA A CB    1 
ATOM   2120  N  N     . LYS A 1 1715 ? 148.688 237.499 235.058 1.00 1.96  ? 1715 LYS A N     1 
ATOM   2121  C  CA    . LYS A 1 1715 ? 147.652 237.374 236.079 1.00 3.08  ? 1715 LYS A CA    1 
ATOM   2122  C  C     . LYS A 1 1715 ? 147.895 238.335 237.233 1.00 2.29  ? 1715 LYS A C     1 
ATOM   2123  O  O     . LYS A 1 1715 ? 146.949 238.928 237.764 1.00 4.28  ? 1715 LYS A O     1 
ATOM   2124  C  CB    . LYS A 1 1715 ? 147.582 235.934 236.585 1.00 4.50  ? 1715 LYS A CB    1 
ATOM   2125  C  CG    . LYS A 1 1715 ? 146.948 234.962 235.614 1.00 4.13  ? 1715 LYS A CG    1 
ATOM   2126  C  CD    . LYS A 1 1715 ? 146.335 233.781 236.349 1.00 8.28  ? 1715 LYS A CD    1 
ATOM   2127  C  CE    . LYS A 1 1715 ? 146.480 232.496 235.554 1.00 8.15  ? 1715 LYS A CE    1 
ATOM   2128  N  NZ    . LYS A 1 1715 ? 146.301 232.723 234.097 1.00 14.34 ? 1715 LYS A NZ    1 
ATOM   2129  N  N     . LEU A 1 1716 ? 149.156 238.498 237.638 1.00 2.24  ? 1716 LEU A N     1 
ATOM   2130  C  CA    . LEU A 1 1716 ? 149.479 239.448 238.698 1.00 2.40  ? 1716 LEU A CA    1 
ATOM   2131  C  C     . LEU A 1 1716 ? 149.244 240.883 238.254 1.00 2.99  ? 1716 LEU A C     1 
ATOM   2132  O  O     . LEU A 1 1716 ? 148.863 241.728 239.070 1.00 3.89  ? 1716 LEU A O     1 
ATOM   2133  C  CB    . LEU A 1 1716 ? 150.926 239.259 239.147 1.00 1.89  ? 1716 LEU A CB    1 
ATOM   2134  C  CG    . LEU A 1 1716 ? 151.204 238.163 240.175 1.00 1.79  ? 1716 LEU A CG    1 
ATOM   2135  C  CD1   . LEU A 1 1716 ? 152.696 237.965 240.341 1.00 2.16  ? 1716 LEU A CD1   1 
ATOM   2136  C  CD2   . LEU A 1 1716 ? 150.554 238.495 241.506 1.00 1.94  ? 1716 LEU A CD2   1 
ATOM   2137  N  N     . LEU A 1 1717 ? 149.475 241.181 236.971 1.00 2.51  ? 1717 LEU A N     1 
ATOM   2138  C  CA    . LEU A 1 1717 ? 149.197 242.517 236.460 1.00 2.06  ? 1717 LEU A CA    1 
ATOM   2139  C  C     . LEU A 1 1717 ? 147.712 242.844 236.554 1.00 3.72  ? 1717 LEU A C     1 
ATOM   2140  O  O     . LEU A 1 1717 ? 147.340 243.958 236.936 1.00 4.98  ? 1717 LEU A O     1 
ATOM   2141  C  CB    . LEU A 1 1717 ? 149.682 242.642 235.017 1.00 2.18  ? 1717 LEU A CB    1 
ATOM   2142  C  CG    . LEU A 1 1717 ? 149.426 243.992 234.339 1.00 2.54  ? 1717 LEU A CG    1 
ATOM   2143  C  CD1   . LEU A 1 1717 ? 150.197 245.107 235.032 1.00 0.99  ? 1717 LEU A CD1   1 
ATOM   2144  C  CD2   . LEU A 1 1717 ? 149.771 243.933 232.862 1.00 0.56  ? 1717 LEU A CD2   1 
ATOM   2145  N  N     . ALA A 1 1718 ? 146.850 241.881 236.222 1.00 3.21  ? 1718 ALA A N     1 
ATOM   2146  C  CA    . ALA A 1 1718 ? 145.412 242.124 236.274 1.00 4.07  ? 1718 ALA A CA    1 
ATOM   2147  C  C     . ALA A 1 1718 ? 144.956 242.436 237.693 1.00 9.25  ? 1718 ALA A C     1 
ATOM   2148  O  O     . ALA A 1 1718 ? 144.124 243.325 237.905 1.00 12.28 ? 1718 ALA A O     1 
ATOM   2149  C  CB    . ALA A 1 1718 ? 144.654 240.920 235.719 1.00 4.53  ? 1718 ALA A CB    1 
ATOM   2150  N  N     . GLU A 1 1719 ? 145.485 241.710 238.678 1.00 11.23 ? 1719 GLU A N     1 
ATOM   2151  C  CA    . GLU A 1 1719 ? 145.161 242.005 240.069 1.00 7.40  ? 1719 GLU A CA    1 
ATOM   2152  C  C     . GLU A 1 1719 ? 145.694 243.370 240.485 1.00 5.98  ? 1719 GLU A C     1 
ATOM   2153  O  O     . GLU A 1 1719 ? 145.023 244.111 241.213 1.00 10.63 ? 1719 GLU A O     1 
ATOM   2154  C  CB    . GLU A 1 1719 ? 145.714 240.907 240.977 1.00 7.58  ? 1719 GLU A CB    1 
ATOM   2155  C  CG    . GLU A 1 1719 ? 145.091 239.544 240.733 1.00 10.73 ? 1719 GLU A CG    1 
ATOM   2156  C  CD    . GLU A 1 1719 ? 146.073 238.407 240.932 1.00 15.34 ? 1719 GLU A CD    1 
ATOM   2157  O  OE1   . GLU A 1 1719 ? 147.270 238.685 241.144 1.00 12.12 ? 1719 GLU A OE1   1 
ATOM   2158  O  OE2   . GLU A 1 1719 ? 145.647 237.236 240.872 1.00 21.21 ? 1719 GLU A OE2   1 
ATOM   2159  N  N     . SER A 1 1720 ? 146.904 243.718 240.037 1.00 4.41  ? 1720 SER A N     1 
ATOM   2160  C  CA    . SER A 1 1720 ? 147.481 245.014 240.377 1.00 4.18  ? 1720 SER A CA    1 
ATOM   2161  C  C     . SER A 1 1720 ? 146.708 246.159 239.732 1.00 5.91  ? 1720 SER A C     1 
ATOM   2162  O  O     . SER A 1 1720 ? 146.499 247.200 240.362 1.00 6.55  ? 1720 SER A O     1 
ATOM   2163  C  CB    . SER A 1 1720 ? 148.951 245.054 239.961 1.00 3.80  ? 1720 SER A CB    1 
ATOM   2164  O  OG    . SER A 1 1720 ? 149.585 246.227 240.438 1.00 2.89  ? 1720 SER A OG    1 
ATOM   2165  N  N     . VAL A 1 1721 ? 146.287 245.990 238.475 1.00 8.31  ? 1721 VAL A N     1 
ATOM   2166  C  CA    . VAL A 1 1721 ? 145.521 247.035 237.798 1.00 6.90  ? 1721 VAL A CA    1 
ATOM   2167  C  C     . VAL A 1 1721 ? 144.212 247.302 238.531 1.00 8.77  ? 1721 VAL A C     1 
ATOM   2168  O  O     . VAL A 1 1721 ? 143.764 248.451 238.630 1.00 13.84 ? 1721 VAL A O     1 
ATOM   2169  C  CB    . VAL A 1 1721 ? 145.286 246.663 236.320 1.00 4.75  ? 1721 VAL A CB    1 
ATOM   2170  C  CG1   . VAL A 1 1721 ? 144.369 247.672 235.654 1.00 4.39  ? 1721 VAL A CG1   1 
ATOM   2171  C  CG2   . VAL A 1 1721 ? 146.604 246.623 235.574 1.00 3.22  ? 1721 VAL A CG2   1 
ATOM   2172  N  N     . THR A 1 1722 ? 143.584 246.253 239.064 1.00 9.65  ? 1722 THR A N     1 
ATOM   2173  C  CA    . THR A 1 1722 ? 142.336 246.433 239.797 1.00 9.57  ? 1722 THR A CA    1 
ATOM   2174  C  C     . THR A 1 1722 ? 142.531 247.325 241.015 1.00 12.77 ? 1722 THR A C     1 
ATOM   2175  O  O     . THR A 1 1722 ? 141.706 248.205 241.290 1.00 21.37 ? 1722 THR A O     1 
ATOM   2176  C  CB    . THR A 1 1722 ? 141.772 245.074 240.217 1.00 9.43  ? 1722 THR A CB    1 
ATOM   2177  O  OG1   . THR A 1 1722 ? 141.518 244.280 239.053 1.00 13.35 ? 1722 THR A OG1   1 
ATOM   2178  C  CG2   . THR A 1 1722 ? 140.479 245.249 240.991 1.00 11.12 ? 1722 THR A CG2   1 
ATOM   2179  N  N     . GLU A 1 1723 ? 143.621 247.116 241.757 1.00 14.69 ? 1723 GLU A N     1 
ATOM   2180  C  CA    . GLU A 1 1723 ? 143.853 247.894 242.970 1.00 10.67 ? 1723 GLU A CA    1 
ATOM   2181  C  C     . GLU A 1 1723 ? 144.316 249.312 242.656 1.00 13.66 ? 1723 GLU A C     1 
ATOM   2182  O  O     . GLU A 1 1723 ? 143.885 250.269 243.310 1.00 14.51 ? 1723 GLU A O     1 
ATOM   2183  C  CB    . GLU A 1 1723 ? 144.873 247.182 243.858 1.00 9.23  ? 1723 GLU A CB    1 
ATOM   2184  C  CG    . GLU A 1 1723 ? 144.459 245.782 244.271 1.00 11.53 ? 1723 GLU A CG    1 
ATOM   2185  C  CD    . GLU A 1 1723 ? 145.442 245.146 245.234 1.00 19.15 ? 1723 GLU A CD    1 
ATOM   2186  O  OE1   . GLU A 1 1723 ? 146.391 245.835 245.659 1.00 20.25 ? 1723 GLU A OE1   1 
ATOM   2187  O  OE2   . GLU A 1 1723 ? 145.265 243.954 245.562 1.00 22.31 ? 1723 GLU A OE2   1 
ATOM   2188  N  N     . VAL A 1 1724 ? 145.200 249.471 241.665 1.00 11.52 ? 1724 VAL A N     1 
ATOM   2189  C  CA    . VAL A 1 1724 ? 145.777 250.785 241.391 1.00 10.02 ? 1724 VAL A CA    1 
ATOM   2190  C  C     . VAL A 1 1724 ? 144.734 251.748 240.838 1.00 14.44 ? 1724 VAL A C     1 
ATOM   2191  O  O     . VAL A 1 1724 ? 144.902 252.969 240.956 1.00 17.05 ? 1724 VAL A O     1 
ATOM   2192  C  CB    . VAL A 1 1724 ? 146.979 250.660 240.432 1.00 7.76  ? 1724 VAL A CB    1 
ATOM   2193  C  CG1   . VAL A 1 1724 ? 146.534 250.196 239.059 1.00 8.94  ? 1724 VAL A CG1   1 
ATOM   2194  C  CG2   . VAL A 1 1724 ? 147.755 251.969 240.347 1.00 7.84  ? 1724 VAL A CG2   1 
ATOM   2195  N  N     . GLU A 1 1725 ? 143.651 251.235 240.245 1.00 15.45 ? 1725 GLU A N     1 
ATOM   2196  C  CA    . GLU A 1 1725 ? 142.602 252.111 239.734 1.00 15.42 ? 1725 GLU A CA    1 
ATOM   2197  C  C     . GLU A 1 1725 ? 141.936 252.905 240.849 1.00 19.09 ? 1725 GLU A C     1 
ATOM   2198  O  O     . GLU A 1 1725 ? 141.488 254.034 240.619 1.00 25.85 ? 1725 GLU A O     1 
ATOM   2199  C  CB    . GLU A 1 1725 ? 141.558 251.300 238.969 1.00 16.20 ? 1725 GLU A CB    1 
ATOM   2200  C  CG    . GLU A 1 1725 ? 141.998 250.874 237.581 1.00 16.10 ? 1725 GLU A CG    1 
ATOM   2201  C  CD    . GLU A 1 1725 ? 141.037 249.891 236.945 1.00 20.93 ? 1725 GLU A CD    1 
ATOM   2202  O  OE1   . GLU A 1 1725 ? 140.778 248.832 237.555 1.00 21.02 ? 1725 GLU A OE1   1 
ATOM   2203  O  OE2   . GLU A 1 1725 ? 140.549 250.174 235.832 1.00 25.87 ? 1725 GLU A OE2   1 
ATOM   2204  N  N     . ILE A 1 1726 ? 141.858 252.336 242.054 1.00 17.01 ? 1726 ILE A N     1 
ATOM   2205  C  CA    . ILE A 1 1726 ? 141.314 253.072 243.192 1.00 17.32 ? 1726 ILE A CA    1 
ATOM   2206  C  C     . ILE A 1 1726 ? 142.176 254.290 243.496 1.00 18.31 ? 1726 ILE A C     1 
ATOM   2207  O  O     . ILE A 1 1726 ? 141.664 255.382 243.765 1.00 23.06 ? 1726 ILE A O     1 
ATOM   2208  C  CB    . ILE A 1 1726 ? 141.190 252.149 244.418 1.00 14.34 ? 1726 ILE A CB    1 
ATOM   2209  C  CG1   . ILE A 1 1726 ? 140.565 250.807 244.020 1.00 15.25 ? 1726 ILE A CG1   1 
ATOM   2210  C  CG2   . ILE A 1 1726 ? 140.382 252.820 245.512 1.00 20.38 ? 1726 ILE A CG2   1 
ATOM   2211  C  CD1   . ILE A 1 1726 ? 139.200 250.924 243.389 1.00 17.83 ? 1726 ILE A CD1   1 
ATOM   2212  N  N     . PHE A 1 1727 ? 143.500 254.120 243.459 1.00 17.18 ? 1727 PHE A N     1 
ATOM   2213  C  CA    . PHE A 1 1727 ? 144.406 255.243 243.678 1.00 12.42 ? 1727 PHE A CA    1 
ATOM   2214  C  C     . PHE A 1 1727 ? 144.247 256.300 242.593 1.00 15.14 ? 1727 PHE A C     1 
ATOM   2215  O  O     . PHE A 1 1727 ? 144.287 257.503 242.878 1.00 20.89 ? 1727 PHE A O     1 
ATOM   2216  C  CB    . PHE A 1 1727 ? 145.848 254.743 243.735 1.00 9.29  ? 1727 PHE A CB    1 
ATOM   2217  C  CG    . PHE A 1 1727 ? 146.092 253.731 244.812 1.00 11.17 ? 1727 PHE A CG    1 
ATOM   2218  C  CD1   . PHE A 1 1727 ? 145.505 253.872 246.058 1.00 10.85 ? 1727 PHE A CD1   1 
ATOM   2219  C  CD2   . PHE A 1 1727 ? 146.896 252.628 244.574 1.00 10.28 ? 1727 PHE A CD2   1 
ATOM   2220  C  CE1   . PHE A 1 1727 ? 145.728 252.939 247.051 1.00 9.54  ? 1727 PHE A CE1   1 
ATOM   2221  C  CE2   . PHE A 1 1727 ? 147.122 251.694 245.563 1.00 6.55  ? 1727 PHE A CE2   1 
ATOM   2222  C  CZ    . PHE A 1 1727 ? 146.537 251.849 246.803 1.00 7.84  ? 1727 PHE A CZ    1 
ATOM   2223  N  N     . GLY A 1 1728 ? 144.081 255.872 241.344 1.00 17.30 ? 1728 GLY A N     1 
ATOM   2224  C  CA    . GLY A 1 1728 ? 143.826 256.816 240.276 1.00 14.30 ? 1728 GLY A CA    1 
ATOM   2225  C  C     . GLY A 1 1728 ? 142.487 257.508 240.442 1.00 17.64 ? 1728 GLY A C     1 
ATOM   2226  O  O     . GLY A 1 1728 ? 141.545 256.961 241.018 1.00 21.32 ? 1728 GLY A O     1 
ATOM   2227  N  N     . LYS A 1 1729 ? 142.415 258.732 239.920 1.00 21.43 ? 1729 LYS A N     1 
ATOM   2228  C  CA    . LYS A 1 1729 ? 141.259 259.629 240.050 1.00 28.16 ? 1729 LYS A CA    1 
ATOM   2229  C  C     . LYS A 1 1729 ? 140.653 259.566 241.453 1.00 31.58 ? 1729 LYS A C     1 
ATOM   2230  O  O     . LYS A 1 1729 ? 139.440 259.441 241.642 1.00 33.40 ? 1729 LYS A O     1 
ATOM   2231  C  CB    . LYS A 1 1729 ? 140.207 259.356 238.964 1.00 26.95 ? 1729 LYS A CB    1 
ATOM   2232  C  CG    . LYS A 1 1729 ? 139.624 257.948 238.905 1.00 26.27 ? 1729 LYS A CG    1 
ATOM   2233  C  CD    . LYS A 1 1729 ? 138.664 257.792 237.737 1.00 26.35 ? 1729 LYS A CD    1 
ATOM   2234  C  CE    . LYS A 1 1729 ? 139.325 258.179 236.423 1.00 21.55 ? 1729 LYS A CE    1 
ATOM   2235  N  NZ    . LYS A 1 1729 ? 138.411 257.988 235.263 1.00 28.31 ? 1729 LYS A NZ    1 
ATOM   2236  N  N     . ALA A 1 1730 ? 141.527 259.663 242.452 1.00 27.64 ? 1730 ALA A N     1 
ATOM   2237  C  CA    . ALA A 1 1730 ? 141.138 259.742 243.852 1.00 22.32 ? 1730 ALA A CA    1 
ATOM   2238  C  C     . ALA A 1 1730 ? 141.686 261.030 244.448 1.00 28.85 ? 1730 ALA A C     1 
ATOM   2239  O  O     . ALA A 1 1730 ? 142.830 261.410 244.178 1.00 28.80 ? 1730 ALA A O     1 
ATOM   2240  C  CB    . ALA A 1 1730 ? 141.647 258.536 244.642 1.00 21.40 ? 1730 ALA A CB    1 
ATOM   2241  N  N     . THR A 1 1731 ? 140.859 261.707 245.247 1.00 22.58 ? 1731 THR A N     1 
ATOM   2242  C  CA    . THR A 1 1731 ? 141.253 263.001 245.794 1.00 22.61 ? 1731 THR A CA    1 
ATOM   2243  C  C     . THR A 1 1731 ? 142.422 262.869 246.764 1.00 28.23 ? 1731 THR A C     1 
ATOM   2244  O  O     . THR A 1 1731 ? 143.358 263.675 246.728 1.00 31.87 ? 1731 THR A O     1 
ATOM   2245  C  CB    . THR A 1 1731 ? 140.060 263.665 246.484 1.00 26.53 ? 1731 THR A CB    1 
ATOM   2246  O  OG1   . THR A 1 1731 ? 139.613 262.842 247.569 1.00 34.17 ? 1731 THR A OG1   1 
ATOM   2247  C  CG2   . THR A 1 1731 ? 138.918 263.858 245.499 1.00 26.01 ? 1731 THR A CG2   1 
ATOM   2248  N  N     . SER A 1 1732 ? 142.389 261.867 247.638 1.00 22.50 ? 1732 SER A N     1 
ATOM   2249  C  CA    . SER A 1 1732 ? 143.414 261.688 248.655 1.00 21.66 ? 1732 SER A CA    1 
ATOM   2250  C  C     . SER A 1 1732 ? 143.842 260.232 248.709 1.00 18.44 ? 1732 SER A C     1 
ATOM   2251  O  O     . SER A 1 1732 ? 143.005 259.326 248.664 1.00 24.75 ? 1732 SER A O     1 
ATOM   2252  C  CB    . SER A 1 1732 ? 142.914 262.135 250.035 1.00 26.47 ? 1732 SER A CB    1 
ATOM   2253  O  OG    . SER A 1 1732 ? 141.792 261.370 250.439 1.00 28.51 ? 1732 SER A OG    1 
ATOM   2254  N  N     . ILE A 1 1733 ? 145.148 260.012 248.823 1.00 11.92 ? 1733 ILE A N     1 
ATOM   2255  C  CA    . ILE A 1 1733 ? 145.722 258.677 248.910 1.00 9.78  ? 1733 ILE A CA    1 
ATOM   2256  C  C     . ILE A 1 1733 ? 146.330 258.503 250.294 1.00 14.54 ? 1733 ILE A C     1 
ATOM   2257  O  O     . ILE A 1 1733 ? 147.175 259.302 250.715 1.00 21.41 ? 1733 ILE A O     1 
ATOM   2258  C  CB    . ILE A 1 1733 ? 146.770 258.436 247.815 1.00 11.45 ? 1733 ILE A CB    1 
ATOM   2259  C  CG1   . ILE A 1 1733 ? 146.120 258.543 246.436 1.00 15.99 ? 1733 ILE A CG1   1 
ATOM   2260  C  CG2   . ILE A 1 1733 ? 147.446 257.084 248.010 1.00 11.73 ? 1733 ILE A CG2   1 
ATOM   2261  C  CD1   . ILE A 1 1733 ? 147.015 258.116 245.315 1.00 6.96  ? 1733 ILE A CD1   1 
ATOM   2262  N  N     . ASP A 1 1734 ? 145.900 257.467 250.994 1.00 12.84 ? 1734 ASP A N     1 
ATOM   2263  C  CA    . ASP A 1 1734 ? 146.517 257.102 252.261 1.00 14.99 ? 1734 ASP A CA    1 
ATOM   2264  C  C     . ASP A 1 1734 ? 147.871 256.459 251.995 1.00 16.62 ? 1734 ASP A C     1 
ATOM   2265  O  O     . ASP A 1 1734 ? 147.941 255.481 251.239 1.00 11.68 ? 1734 ASP A O     1 
ATOM   2266  C  CB    . ASP A 1 1734 ? 145.613 256.147 253.032 1.00 14.86 ? 1734 ASP A CB    1 
ATOM   2267  C  CG    . ASP A 1 1734 ? 146.329 255.465 254.177 1.00 23.09 ? 1734 ASP A CG    1 
ATOM   2268  O  OD1   . ASP A 1 1734 ? 146.869 256.174 255.051 1.00 23.14 ? 1734 ASP A OD1   1 
ATOM   2269  O  OD2   . ASP A 1 1734 ? 146.357 254.218 254.200 1.00 23.56 ? 1734 ASP A OD2   1 
ATOM   2270  N  N     . PRO A 1 1735 ? 148.961 256.970 252.572 1.00 12.79 ? 1735 PRO A N     1 
ATOM   2271  C  CA    . PRO A 1 1735 ? 150.276 256.364 252.298 1.00 13.66 ? 1735 PRO A CA    1 
ATOM   2272  C  C     . PRO A 1 1735 ? 150.370 254.901 252.687 1.00 15.25 ? 1735 PRO A C     1 
ATOM   2273  O  O     . PRO A 1 1735 ? 151.025 254.123 251.983 1.00 12.35 ? 1735 PRO A O     1 
ATOM   2274  C  CB    . PRO A 1 1735 ? 151.236 257.240 253.118 1.00 15.58 ? 1735 PRO A CB    1 
ATOM   2275  C  CG    . PRO A 1 1735 ? 150.525 258.543 253.260 1.00 15.36 ? 1735 PRO A CG    1 
ATOM   2276  C  CD    . PRO A 1 1735 ? 149.073 258.191 253.385 1.00 15.16 ? 1735 PRO A CD    1 
ATOM   2277  N  N     . ASN A 1 1736 ? 149.726 254.496 253.785 1.00 15.85 ? 1736 ASN A N     1 
ATOM   2278  C  CA    . ASN A 1 1736 ? 149.831 253.110 254.233 1.00 15.86 ? 1736 ASN A CA    1 
ATOM   2279  C  C     . ASN A 1 1736 ? 149.240 252.147 253.212 1.00 14.77 ? 1736 ASN A C     1 
ATOM   2280  O  O     . ASN A 1 1736 ? 149.832 251.100 252.923 1.00 15.92 ? 1736 ASN A O     1 
ATOM   2281  C  CB    . ASN A 1 1736 ? 149.147 252.945 255.589 1.00 17.75 ? 1736 ASN A CB    1 
ATOM   2282  C  CG    . ASN A 1 1736 ? 149.691 253.896 256.635 1.00 21.48 ? 1736 ASN A CG    1 
ATOM   2283  O  OD1   . ASN A 1 1736 ? 150.902 253.988 256.835 1.00 16.05 ? 1736 ASN A OD1   1 
ATOM   2284  N  ND2   . ASN A 1 1736 ? 148.797 254.609 257.313 1.00 23.53 ? 1736 ASN A ND2   1 
ATOM   2285  N  N     . THR A 1 1737 ? 148.077 252.480 252.650 1.00 12.21 ? 1737 THR A N     1 
ATOM   2286  C  CA    . THR A 1 1737 ? 147.494 251.639 251.613 1.00 12.35 ? 1737 THR A CA    1 
ATOM   2287  C  C     . THR A 1 1737 ? 148.360 251.632 250.358 1.00 10.27 ? 1737 THR A C     1 
ATOM   2288  O  O     . THR A 1 1737 ? 148.583 250.575 249.754 1.00 13.14 ? 1737 THR A O     1 
ATOM   2289  C  CB    . THR A 1 1737 ? 146.077 252.114 251.286 1.00 12.11 ? 1737 THR A CB    1 
ATOM   2290  O  OG1   . THR A 1 1737 ? 145.279 252.091 252.474 1.00 19.77 ? 1737 THR A OG1   1 
ATOM   2291  C  CG2   . THR A 1 1737 ? 145.441 251.211 250.244 1.00 12.83 ? 1737 THR A CG2   1 
ATOM   2292  N  N     . TYR A 1 1738 ? 148.862 252.801 249.954 1.00 9.11  ? 1738 TYR A N     1 
ATOM   2293  C  CA    . TYR A 1 1738 ? 149.678 252.892 248.748 1.00 4.63  ? 1738 TYR A CA    1 
ATOM   2294  C  C     . TYR A 1 1738 ? 150.998 252.146 248.907 1.00 7.83  ? 1738 TYR A C     1 
ATOM   2295  O  O     . TYR A 1 1738 ? 151.443 251.458 247.981 1.00 8.58  ? 1738 TYR A O     1 
ATOM   2296  C  CB    . TYR A 1 1738 ? 149.922 254.359 248.399 1.00 7.86  ? 1738 TYR A CB    1 
ATOM   2297  C  CG    . TYR A 1 1738 ? 150.411 254.579 246.992 1.00 6.57  ? 1738 TYR A CG    1 
ATOM   2298  C  CD1   . TYR A 1 1738 ? 149.595 254.313 245.903 1.00 4.11  ? 1738 TYR A CD1   1 
ATOM   2299  C  CD2   . TYR A 1 1738 ? 151.689 255.060 246.750 1.00 4.93  ? 1738 TYR A CD2   1 
ATOM   2300  C  CE1   . TYR A 1 1738 ? 150.040 254.514 244.614 1.00 6.24  ? 1738 TYR A CE1   1 
ATOM   2301  C  CE2   . TYR A 1 1738 ? 152.142 255.265 245.465 1.00 4.22  ? 1738 TYR A CE2   1 
ATOM   2302  C  CZ    . TYR A 1 1738 ? 151.313 254.989 244.401 1.00 3.73  ? 1738 TYR A CZ    1 
ATOM   2303  O  OH    . TYR A 1 1738 ? 151.763 255.192 243.119 1.00 8.03  ? 1738 TYR A OH    1 
ATOM   2304  N  N     . ILE A 1 1739 ? 151.642 252.274 250.069 1.00 10.79 ? 1739 ILE A N     1 
ATOM   2305  C  CA    . ILE A 1 1739 ? 152.878 251.539 250.316 1.00 7.67  ? 1739 ILE A CA    1 
ATOM   2306  C  C     . ILE A 1 1739 ? 152.602 250.042 250.375 1.00 8.32  ? 1739 ILE A C     1 
ATOM   2307  O  O     . ILE A 1 1739 ? 153.421 249.227 249.931 1.00 10.64 ? 1739 ILE A O     1 
ATOM   2308  C  CB    . ILE A 1 1739 ? 153.555 252.056 251.600 1.00 9.38  ? 1739 ILE A CB    1 
ATOM   2309  C  CG1   . ILE A 1 1739 ? 154.048 253.490 251.403 1.00 10.41 ? 1739 ILE A CG1   1 
ATOM   2310  C  CG2   . ILE A 1 1739 ? 154.703 251.155 252.013 1.00 4.52  ? 1739 ILE A CG2   1 
ATOM   2311  C  CD1   . ILE A 1 1739 ? 155.233 253.610 250.472 1.00 10.71 ? 1739 ILE A CD1   1 
ATOM   2312  N  N     . THR A 1 1740 ? 151.444 249.656 250.912 1.00 8.94  ? 1740 THR A N     1 
ATOM   2313  C  CA    . THR A 1 1740 ? 151.066 248.248 250.932 1.00 7.45  ? 1740 THR A CA    1 
ATOM   2314  C  C     . THR A 1 1740 ? 150.946 247.689 249.519 1.00 7.87  ? 1740 THR A C     1 
ATOM   2315  O  O     . THR A 1 1740 ? 151.408 246.575 249.243 1.00 10.21 ? 1740 THR A O     1 
ATOM   2316  C  CB    . THR A 1 1740 ? 149.753 248.068 251.693 1.00 5.41  ? 1740 THR A CB    1 
ATOM   2317  O  OG1   . THR A 1 1740 ? 149.918 248.519 253.043 1.00 16.90 ? 1740 THR A OG1   1 
ATOM   2318  C  CG2   . THR A 1 1740 ? 149.330 246.609 251.705 1.00 6.76  ? 1740 THR A CG2   1 
ATOM   2319  N  N     . TRP A 1 1741 ? 150.337 248.452 248.608 1.00 4.95  ? 1741 TRP A N     1 
ATOM   2320  C  CA    . TRP A 1 1741 ? 150.192 247.988 247.232 1.00 3.49  ? 1741 TRP A CA    1 
ATOM   2321  C  C     . TRP A 1 1741 ? 151.542 247.914 246.523 1.00 4.02  ? 1741 TRP A C     1 
ATOM   2322  O  O     . TRP A 1 1741 ? 151.774 247.010 245.716 1.00 5.66  ? 1741 TRP A O     1 
ATOM   2323  C  CB    . TRP A 1 1741 ? 149.228 248.896 246.472 1.00 3.58  ? 1741 TRP A CB    1 
ATOM   2324  C  CG    . TRP A 1 1741 ? 149.313 248.741 244.984 1.00 3.16  ? 1741 TRP A CG    1 
ATOM   2325  C  CD1   . TRP A 1 1741 ? 148.682 247.805 244.223 1.00 3.11  ? 1741 TRP A CD1   1 
ATOM   2326  C  CD2   . TRP A 1 1741 ? 150.074 249.548 244.081 1.00 2.23  ? 1741 TRP A CD2   1 
ATOM   2327  N  NE1   . TRP A 1 1741 ? 149.005 247.975 242.901 1.00 2.57  ? 1741 TRP A NE1   1 
ATOM   2328  C  CE2   . TRP A 1 1741 ? 149.859 249.040 242.787 1.00 2.98  ? 1741 TRP A CE2   1 
ATOM   2329  C  CE3   . TRP A 1 1741 ? 150.917 250.651 244.239 1.00 1.89  ? 1741 TRP A CE3   1 
ATOM   2330  C  CZ2   . TRP A 1 1741 ? 150.455 249.595 241.658 1.00 3.79  ? 1741 TRP A CZ2   1 
ATOM   2331  C  CZ3   . TRP A 1 1741 ? 151.507 251.199 243.120 1.00 2.09  ? 1741 TRP A CZ3   1 
ATOM   2332  C  CH2   . TRP A 1 1741 ? 151.274 250.673 241.845 1.00 2.15  ? 1741 TRP A CH2   1 
ATOM   2333  N  N     . ILE A 1 1742 ? 152.441 248.859 246.808 1.00 3.62  ? 1742 ILE A N     1 
ATOM   2334  C  CA    . ILE A 1 1742 ? 153.774 248.821 246.213 1.00 5.15  ? 1742 ILE A CA    1 
ATOM   2335  C  C     . ILE A 1 1742 ? 154.527 247.577 246.666 1.00 7.02  ? 1742 ILE A C     1 
ATOM   2336  O  O     . ILE A 1 1742 ? 155.189 246.905 245.867 1.00 8.89  ? 1742 ILE A O     1 
ATOM   2337  C  CB    . ILE A 1 1742 ? 154.551 250.107 246.559 1.00 6.09  ? 1742 ILE A CB    1 
ATOM   2338  C  CG1   . ILE A 1 1742 ? 153.889 251.324 245.913 1.00 5.11  ? 1742 ILE A CG1   1 
ATOM   2339  C  CG2   . ILE A 1 1742 ? 156.001 249.994 246.123 1.00 2.42  ? 1742 ILE A CG2   1 
ATOM   2340  C  CD1   . ILE A 1 1742 ? 154.412 252.639 246.425 1.00 5.05  ? 1742 ILE A CD1   1 
ATOM   2341  N  N     . ASP A 1 1743 ? 154.433 247.250 247.956 1.00 7.45  ? 1743 ASP A N     1 
ATOM   2342  C  CA    . ASP A 1 1743 ? 155.168 246.110 248.493 1.00 7.90  ? 1743 ASP A CA    1 
ATOM   2343  C  C     . ASP A 1 1743 ? 154.612 244.783 247.991 1.00 8.85  ? 1743 ASP A C     1 
ATOM   2344  O  O     . ASP A 1 1743 ? 155.360 243.806 247.873 1.00 8.39  ? 1743 ASP A O     1 
ATOM   2345  C  CB    . ASP A 1 1743 ? 155.136 246.151 250.020 1.00 9.39  ? 1743 ASP A CB    1 
ATOM   2346  C  CG    . ASP A 1 1743 ? 156.256 246.980 250.601 1.00 9.58  ? 1743 ASP A CG    1 
ATOM   2347  O  OD1   . ASP A 1 1743 ? 157.240 247.236 249.878 1.00 16.11 ? 1743 ASP A OD1   1 
ATOM   2348  O  OD2   . ASP A 1 1743 ? 156.152 247.378 251.778 1.00 17.24 ? 1743 ASP A OD2   1 
ATOM   2349  N  N     . LYS A 1 1744 ? 153.312 244.727 247.696 1.00 4.92  ? 1744 LYS A N     1 
ATOM   2350  C  CA    . LYS A 1 1744 ? 152.682 243.462 247.336 1.00 4.39  ? 1744 LYS A CA    1 
ATOM   2351  C  C     . LYS A 1 1744 ? 153.079 242.995 245.939 1.00 4.59  ? 1744 LYS A C     1 
ATOM   2352  O  O     . LYS A 1 1744 ? 153.204 241.788 245.708 1.00 6.72  ? 1744 LYS A O     1 
ATOM   2353  C  CB    . LYS A 1 1744 ? 151.164 243.590 247.447 1.00 5.91  ? 1744 LYS A CB    1 
ATOM   2354  C  CG    . LYS A 1 1744 ? 150.385 242.352 247.024 1.00 6.08  ? 1744 LYS A CG    1 
ATOM   2355  C  CD    . LYS A 1 1744 ? 148.898 242.648 246.948 1.00 4.76  ? 1744 LYS A CD    1 
ATOM   2356  C  CE    . LYS A 1 1744 ? 148.067 241.467 247.411 1.00 11.22 ? 1744 LYS A CE    1 
ATOM   2357  N  NZ    . LYS A 1 1744 ? 147.578 240.645 246.271 1.00 17.50 ? 1744 LYS A NZ    1 
ATOM   2358  N  N     . TYR A 1 1745 ? 153.283 243.916 245.003 1.00 5.10  ? 1745 TYR A N     1 
ATOM   2359  C  CA    . TYR A 1 1745 ? 153.526 243.556 243.614 1.00 3.17  ? 1745 TYR A CA    1 
ATOM   2360  C  C     . TYR A 1 1745 ? 154.960 243.871 243.211 1.00 2.67  ? 1745 TYR A C     1 
ATOM   2361  O  O     . TYR A 1 1745 ? 155.666 244.634 243.875 1.00 6.02  ? 1745 TYR A O     1 
ATOM   2362  C  CB    . TYR A 1 1745 ? 152.540 244.274 242.687 1.00 1.41  ? 1745 TYR A CB    1 
ATOM   2363  C  CG    . TYR A 1 1745 ? 151.115 243.835 242.906 1.00 2.37  ? 1745 TYR A CG    1 
ATOM   2364  C  CD1   . TYR A 1 1745 ? 150.645 242.643 242.373 1.00 2.99  ? 1745 TYR A CD1   1 
ATOM   2365  C  CD2   . TYR A 1 1745 ? 150.244 244.602 243.663 1.00 3.44  ? 1745 TYR A CD2   1 
ATOM   2366  C  CE1   . TYR A 1 1745 ? 149.347 242.233 242.581 1.00 3.27  ? 1745 TYR A CE1   1 
ATOM   2367  C  CE2   . TYR A 1 1745 ? 148.944 244.202 243.874 1.00 4.37  ? 1745 TYR A CE2   1 
ATOM   2368  C  CZ    . TYR A 1 1745 ? 148.500 243.017 243.334 1.00 4.22  ? 1745 TYR A CZ    1 
ATOM   2369  O  OH    . TYR A 1 1745 ? 147.202 242.617 243.544 1.00 8.63  ? 1745 TYR A OH    1 
ATOM   2370  N  N     . GLN A 1 1746 ? 155.379 243.259 242.109 1.00 1.77  ? 1746 GLN A N     1 
ATOM   2371  C  CA    . GLN A 1 1746 ? 156.750 243.370 241.643 1.00 2.31  ? 1746 GLN A CA    1 
ATOM   2372  C  C     . GLN A 1 1746 ? 157.026 244.768 241.098 1.00 2.83  ? 1746 GLN A C     1 
ATOM   2373  O  O     . GLN A 1 1746 ? 156.116 245.512 240.729 1.00 9.22  ? 1746 GLN A O     1 
ATOM   2374  C  CB    . GLN A 1 1746 ? 157.036 242.312 240.578 1.00 2.86  ? 1746 GLN A CB    1 
ATOM   2375  C  CG    . GLN A 1 1746 ? 157.282 240.923 241.141 1.00 3.02  ? 1746 GLN A CG    1 
ATOM   2376  C  CD    . GLN A 1 1746 ? 156.006 240.218 241.564 1.00 2.72  ? 1746 GLN A CD    1 
ATOM   2377  O  OE1   . GLN A 1 1746 ? 154.903 240.716 241.342 1.00 3.36  ? 1746 GLN A OE1   1 
ATOM   2378  N  NE2   . GLN A 1 1746 ? 156.151 239.056 242.186 1.00 2.86  ? 1746 GLN A NE2   1 
ATOM   2379  N  N     . ALA A 1 1747 ? 158.313 245.118 241.050 1.00 2.13  ? 1747 ALA A N     1 
ATOM   2380  C  CA    . ALA A 1 1747 ? 158.701 246.462 240.637 1.00 2.42  ? 1747 ALA A CA    1 
ATOM   2381  C  C     . ALA A 1 1747 ? 158.251 246.761 239.212 1.00 2.30  ? 1747 ALA A C     1 
ATOM   2382  O  O     . ALA A 1 1747 ? 157.740 247.851 238.932 1.00 3.36  ? 1747 ALA A O     1 
ATOM   2383  C  CB    . ALA A 1 1747 ? 160.213 246.636 240.769 1.00 2.00  ? 1747 ALA A CB    1 
ATOM   2384  N  N     . GLN A 1 1748 ? 158.430 245.806 238.300 1.00 2.49  ? 1748 GLN A N     1 
ATOM   2385  C  CA    . GLN A 1 1748 ? 158.014 246.015 236.918 1.00 1.66  ? 1748 GLN A CA    1 
ATOM   2386  C  C     . GLN A 1 1748 ? 156.503 246.185 236.798 1.00 1.77  ? 1748 GLN A C     1 
ATOM   2387  O  O     . GLN A 1 1748 ? 156.037 247.001 235.994 1.00 1.58  ? 1748 GLN A O     1 
ATOM   2388  C  CB    . GLN A 1 1748 ? 158.513 244.862 236.048 1.00 1.32  ? 1748 GLN A CB    1 
ATOM   2389  C  CG    . GLN A 1 1748 ? 157.912 243.513 236.389 1.00 3.37  ? 1748 GLN A CG    1 
ATOM   2390  C  CD    . GLN A 1 1748 ? 158.476 242.394 235.548 1.00 4.22  ? 1748 GLN A CD    1 
ATOM   2391  O  OE1   . GLN A 1 1748 ? 159.290 242.619 234.658 1.00 2.39  ? 1748 GLN A OE1   1 
ATOM   2392  N  NE2   . GLN A 1 1748 ? 158.065 241.173 235.847 1.00 7.74  ? 1748 GLN A NE2   1 
ATOM   2393  N  N     . LEU A 1 1749 ? 155.725 245.435 237.579 1.00 2.51  ? 1749 LEU A N     1 
ATOM   2394  C  CA    . LEU A 1 1749 ? 154.274 245.538 237.506 1.00 2.00  ? 1749 LEU A CA    1 
ATOM   2395  C  C     . LEU A 1 1749 ? 153.749 246.793 238.189 1.00 2.42  ? 1749 LEU A C     1 
ATOM   2396  O  O     . LEU A 1 1749 ? 152.704 247.317 237.792 1.00 1.95  ? 1749 LEU A O     1 
ATOM   2397  C  CB    . LEU A 1 1749 ? 153.631 244.300 238.128 1.00 2.45  ? 1749 LEU A CB    1 
ATOM   2398  C  CG    . LEU A 1 1749 ? 153.888 242.974 237.416 1.00 3.73  ? 1749 LEU A CG    1 
ATOM   2399  C  CD1   . LEU A 1 1749 ? 152.922 241.925 237.918 1.00 2.90  ? 1749 LEU A CD1   1 
ATOM   2400  C  CD2   . LEU A 1 1749 ? 153.770 243.137 235.909 1.00 2.60  ? 1749 LEU A CD2   1 
ATOM   2401  N  N     . VAL A 1 1750 ? 154.451 247.278 239.214 1.00 2.19  ? 1750 VAL A N     1 
ATOM   2402  C  CA    . VAL A 1 1750 ? 154.019 248.483 239.918 1.00 2.05  ? 1750 VAL A CA    1 
ATOM   2403  C  C     . VAL A 1 1750 ? 154.087 249.692 238.993 1.00 1.28  ? 1750 VAL A C     1 
ATOM   2404  O  O     . VAL A 1 1750 ? 153.152 250.499 238.923 1.00 2.74  ? 1750 VAL A O     1 
ATOM   2405  C  CB    . VAL A 1 1750 ? 154.859 248.682 241.191 1.00 2.38  ? 1750 VAL A CB    1 
ATOM   2406  C  CG1   . VAL A 1 1750 ? 154.743 250.098 241.689 1.00 2.46  ? 1750 VAL A CG1   1 
ATOM   2407  C  CG2   . VAL A 1 1750 ? 154.412 247.715 242.270 1.00 1.81  ? 1750 VAL A CG2   1 
ATOM   2408  N  N     . VAL A 1 1751 ? 155.195 249.836 238.265 1.00 1.11  ? 1751 VAL A N     1 
ATOM   2409  C  CA    . VAL A 1 1751 ? 155.308 250.922 237.298 1.00 1.66  ? 1751 VAL A CA    1 
ATOM   2410  C  C     . VAL A 1 1751 ? 154.343 250.706 236.141 1.00 0.96  ? 1751 VAL A C     1 
ATOM   2411  O  O     . VAL A 1 1751 ? 153.716 251.652 235.653 1.00 1.65  ? 1751 VAL A O     1 
ATOM   2412  C  CB    . VAL A 1 1751 ? 156.764 251.057 236.817 1.00 1.74  ? 1751 VAL A CB    1 
ATOM   2413  C  CG1   . VAL A 1 1751 ? 156.853 252.011 235.636 1.00 2.06  ? 1751 VAL A CG1   1 
ATOM   2414  C  CG2   . VAL A 1 1751 ? 157.641 251.538 237.951 1.00 0.98  ? 1751 VAL A CG2   1 
ATOM   2415  N  N     . LEU A 1 1752 ? 154.198 249.457 235.696 1.00 1.04  ? 1752 LEU A N     1 
ATOM   2416  C  CA    . LEU A 1 1752 ? 153.258 249.148 234.625 1.00 0.76  ? 1752 LEU A CA    1 
ATOM   2417  C  C     . LEU A 1 1752 ? 151.826 249.470 235.034 1.00 0.79  ? 1752 LEU A C     1 
ATOM   2418  O  O     . LEU A 1 1752 ? 151.045 249.989 234.229 1.00 0.96  ? 1752 LEU A O     1 
ATOM   2419  C  CB    . LEU A 1 1752 ? 153.394 247.677 234.237 1.00 0.79  ? 1752 LEU A CB    1 
ATOM   2420  C  CG    . LEU A 1 1752 ? 152.937 247.240 232.849 1.00 0.52  ? 1752 LEU A CG    1 
ATOM   2421  C  CD1   . LEU A 1 1752 ? 153.629 248.055 231.772 1.00 0.34  ? 1752 LEU A CD1   1 
ATOM   2422  C  CD2   . LEU A 1 1752 ? 153.216 245.761 232.672 1.00 0.38  ? 1752 LEU A CD2   1 
ATOM   2423  N  N     . SER A 1 1753 ? 151.461 249.161 236.279 1.00 2.29  ? 1753 SER A N     1 
ATOM   2424  C  CA    . SER A 1 1753 ? 150.118 249.475 236.757 1.00 2.08  ? 1753 SER A CA    1 
ATOM   2425  C  C     . SER A 1 1753 ? 149.884 250.977 236.813 1.00 1.26  ? 1753 SER A C     1 
ATOM   2426  O  O     . SER A 1 1753 ? 148.789 251.455 236.493 1.00 0.99  ? 1753 SER A O     1 
ATOM   2427  C  CB    . SER A 1 1753 ? 149.890 248.842 238.128 1.00 1.23  ? 1753 SER A CB    1 
ATOM   2428  O  OG    . SER A 1 1753 ? 149.814 247.436 238.021 1.00 4.35  ? 1753 SER A OG    1 
ATOM   2429  N  N     . ALA A 1 1754 ? 150.896 251.741 237.230 1.00 1.21  ? 1754 ALA A N     1 
ATOM   2430  C  CA    . ALA A 1 1754 ? 150.759 253.192 237.271 1.00 1.45  ? 1754 ALA A CA    1 
ATOM   2431  C  C     . ALA A 1 1754 ? 150.574 253.770 235.874 1.00 1.20  ? 1754 ALA A C     1 
ATOM   2432  O  O     . ALA A 1 1754 ? 149.776 254.693 235.679 1.00 1.96  ? 1754 ALA A O     1 
ATOM   2433  C  CB    . ALA A 1 1754 ? 151.974 253.816 237.955 1.00 1.12  ? 1754 ALA A CB    1 
ATOM   2434  N  N     . GLN A 1 1755 ? 151.310 253.246 234.892 1.00 0.73  ? 1755 GLN A N     1 
ATOM   2435  C  CA    . GLN A 1 1755 ? 151.169 253.731 233.523 1.00 0.60  ? 1755 GLN A CA    1 
ATOM   2436  C  C     . GLN A 1 1755 ? 149.794 253.405 232.958 1.00 0.94  ? 1755 GLN A C     1 
ATOM   2437  O  O     . GLN A 1 1755 ? 149.198 254.223 232.248 1.00 8.31  ? 1755 GLN A O     1 
ATOM   2438  C  CB    . GLN A 1 1755 ? 152.270 253.141 232.642 1.00 0.57  ? 1755 GLN A CB    1 
ATOM   2439  C  CG    . GLN A 1 1755 ? 153.666 253.527 233.075 1.00 1.52  ? 1755 GLN A CG    1 
ATOM   2440  C  CD    . GLN A 1 1755 ? 154.746 252.882 232.234 1.00 0.85  ? 1755 GLN A CD    1 
ATOM   2441  O  OE1   . GLN A 1 1755 ? 154.822 251.661 232.131 1.00 0.88  ? 1755 GLN A OE1   1 
ATOM   2442  N  NE2   . GLN A 1 1755 ? 155.596 253.704 231.633 1.00 0.83  ? 1755 GLN A NE2   1 
ATOM   2443  N  N     . ILE A 1 1756 ? 149.274 252.213 233.260 1.00 0.68  ? 1756 ILE A N     1 
ATOM   2444  C  CA    . ILE A 1 1756 ? 147.950 251.826 232.777 1.00 0.74  ? 1756 ILE A CA    1 
ATOM   2445  C  C     . ILE A 1 1756 ? 146.883 252.745 233.355 1.00 1.46  ? 1756 ILE A C     1 
ATOM   2446  O  O     . ILE A 1 1756 ? 146.001 253.231 232.639 1.00 10.69 ? 1756 ILE A O     1 
ATOM   2447  C  CB    . ILE A 1 1756 ? 147.670 250.350 233.111 1.00 2.05  ? 1756 ILE A CB    1 
ATOM   2448  C  CG1   . ILE A 1 1756 ? 148.528 249.430 232.241 1.00 1.17  ? 1756 ILE A CG1   1 
ATOM   2449  C  CG2   . ILE A 1 1756 ? 146.196 250.027 232.933 1.00 1.00  ? 1756 ILE A CG2   1 
ATOM   2450  C  CD1   . ILE A 1 1756 ? 148.718 248.054 232.820 1.00 1.08  ? 1756 ILE A CD1   1 
ATOM   2451  N  N     . ALA A 1 1757 ? 146.949 252.998 234.665 1.00 1.41  ? 1757 ALA A N     1 
ATOM   2452  C  CA    . ALA A 1 1757 ? 145.943 253.834 235.308 1.00 1.19  ? 1757 ALA A CA    1 
ATOM   2453  C  C     . ALA A 1 1757 ? 145.974 255.258 234.766 1.00 2.71  ? 1757 ALA A C     1 
ATOM   2454  O  O     . ALA A 1 1757 ? 144.924 255.854 234.507 1.00 3.43  ? 1757 ALA A O     1 
ATOM   2455  C  CB    . ALA A 1 1757 ? 146.148 253.829 236.822 1.00 1.60  ? 1757 ALA A CB    1 
ATOM   2456  N  N     . TRP A 1 1758 ? 147.173 255.816 234.583 1.00 2.30  ? 1758 TRP A N     1 
ATOM   2457  C  CA    . TRP A 1 1758 ? 147.283 257.176 234.070 1.00 2.20  ? 1758 TRP A CA    1 
ATOM   2458  C  C     . TRP A 1 1758 ? 146.763 257.275 232.641 1.00 3.83  ? 1758 TRP A C     1 
ATOM   2459  O  O     . TRP A 1 1758 ? 146.082 258.246 232.290 1.00 6.83  ? 1758 TRP A O     1 
ATOM   2460  C  CB    . TRP A 1 1758 ? 148.732 257.648 234.151 1.00 2.35  ? 1758 TRP A CB    1 
ATOM   2461  C  CG    . TRP A 1 1758 ? 148.974 258.963 233.488 1.00 1.59  ? 1758 TRP A CG    1 
ATOM   2462  C  CD1   . TRP A 1 1758 ? 148.568 260.187 233.925 1.00 1.39  ? 1758 TRP A CD1   1 
ATOM   2463  C  CD2   . TRP A 1 1758 ? 149.676 259.186 232.262 1.00 1.18  ? 1758 TRP A CD2   1 
ATOM   2464  N  NE1   . TRP A 1 1758 ? 148.975 261.161 233.049 1.00 1.34  ? 1758 TRP A NE1   1 
ATOM   2465  C  CE2   . TRP A 1 1758 ? 149.658 260.572 232.018 1.00 0.93  ? 1758 TRP A CE2   1 
ATOM   2466  C  CE3   . TRP A 1 1758 ? 150.318 258.349 231.346 1.00 1.61  ? 1758 TRP A CE3   1 
ATOM   2467  C  CZ2   . TRP A 1 1758 ? 150.257 261.139 230.899 1.00 1.03  ? 1758 TRP A CZ2   1 
ATOM   2468  C  CZ3   . TRP A 1 1758 ? 150.912 258.914 230.238 1.00 4.21  ? 1758 TRP A CZ3   1 
ATOM   2469  C  CH2   . TRP A 1 1758 ? 150.878 260.294 230.022 1.00 1.53  ? 1758 TRP A CH2   1 
ATOM   2470  N  N     . SER A 1 1759 ? 147.073 256.283 231.804 1.00 2.90  ? 1759 SER A N     1 
ATOM   2471  C  CA    . SER A 1 1759 ? 146.605 256.308 230.420 1.00 2.08  ? 1759 SER A CA    1 
ATOM   2472  C  C     . SER A 1 1759 ? 145.084 256.279 230.350 1.00 3.65  ? 1759 SER A C     1 
ATOM   2473  O  O     . SER A 1 1759 ? 144.478 257.036 229.584 1.00 8.14  ? 1759 SER A O     1 
ATOM   2474  C  CB    . SER A 1 1759 ? 147.197 255.136 229.639 1.00 1.98  ? 1759 SER A CB    1 
ATOM   2475  O  OG    . SER A 1 1759 ? 148.524 255.405 229.231 1.00 2.60  ? 1759 SER A OG    1 
ATOM   2476  N  N     . GLU A 1 1760 ? 144.448 255.416 231.145 1.00 3.75  ? 1760 GLU A N     1 
ATOM   2477  C  CA    . GLU A 1 1760 ? 142.993 255.326 231.115 1.00 5.90  ? 1760 GLU A CA    1 
ATOM   2478  C  C     . GLU A 1 1760 ? 142.337 256.582 231.672 1.00 6.57  ? 1760 GLU A C     1 
ATOM   2479  O  O     . GLU A 1 1760 ? 141.241 256.949 231.234 1.00 11.28 ? 1760 GLU A O     1 
ATOM   2480  C  CB    . GLU A 1 1760 ? 142.526 254.086 231.880 1.00 12.09 ? 1760 GLU A CB    1 
ATOM   2481  C  CG    . GLU A 1 1760 ? 142.922 252.775 231.212 1.00 14.69 ? 1760 GLU A CG    1 
ATOM   2482  C  CD    . GLU A 1 1760 ? 142.467 251.554 231.990 1.00 22.63 ? 1760 GLU A CD    1 
ATOM   2483  O  OE1   . GLU A 1 1760 ? 141.951 251.715 233.114 1.00 27.85 ? 1760 GLU A OE1   1 
ATOM   2484  O  OE2   . GLU A 1 1760 ? 142.621 250.429 231.469 1.00 20.37 ? 1760 GLU A OE2   1 
ATOM   2485  N  N     . ASN A 1 1761 ? 142.979 257.248 232.634 1.00 4.52  ? 1761 ASN A N     1 
ATOM   2486  C  CA    . ASN A 1 1761 ? 142.453 258.516 233.131 1.00 6.68  ? 1761 ASN A CA    1 
ATOM   2487  C  C     . ASN A 1 1761 ? 142.489 259.592 232.053 1.00 7.45  ? 1761 ASN A C     1 
ATOM   2488  O  O     . ASN A 1 1761 ? 141.530 260.358 231.902 1.00 8.59  ? 1761 ASN A O     1 
ATOM   2489  C  CB    . ASN A 1 1761 ? 143.238 258.966 234.362 1.00 6.94  ? 1761 ASN A CB    1 
ATOM   2490  C  CG    . ASN A 1 1761 ? 142.950 258.114 235.579 1.00 7.72  ? 1761 ASN A CG    1 
ATOM   2491  O  OD1   . ASN A 1 1761 ? 142.207 257.138 235.505 1.00 8.66  ? 1761 ASN A OD1   1 
ATOM   2492  N  ND2   . ASN A 1 1761 ? 143.544 258.477 236.708 1.00 10.51 ? 1761 ASN A ND2   1 
ATOM   2493  N  N     . VAL A 1 1762 ? 143.586 259.669 231.297 1.00 4.60  ? 1762 VAL A N     1 
ATOM   2494  C  CA    . VAL A 1 1762 ? 143.683 260.654 230.223 1.00 4.41  ? 1762 VAL A CA    1 
ATOM   2495  C  C     . VAL A 1 1762 ? 142.679 260.334 229.121 1.00 9.61  ? 1762 VAL A C     1 
ATOM   2496  O  O     . VAL A 1 1762 ? 142.008 261.229 228.591 1.00 9.97  ? 1762 VAL A O     1 
ATOM   2497  C  CB    . VAL A 1 1762 ? 145.121 260.717 229.678 1.00 2.37  ? 1762 VAL A CB    1 
ATOM   2498  C  CG1   . VAL A 1 1762 ? 145.187 261.624 228.457 1.00 2.08  ? 1762 VAL A CG1   1 
ATOM   2499  C  CG2   . VAL A 1 1762 ? 146.078 261.192 230.758 1.00 1.73  ? 1762 VAL A CG2   1 
ATOM   2500  N  N     . GLU A 1 1763 ? 142.555 259.052 228.767 1.00 5.49  ? 1763 GLU A N     1 
ATOM   2501  C  CA    . GLU A 1 1763 ? 141.543 258.636 227.798 1.00 6.26  ? 1763 GLU A CA    1 
ATOM   2502  C  C     . GLU A 1 1763 ? 140.145 259.019 228.266 1.00 8.26  ? 1763 GLU A C     1 
ATOM   2503  O  O     . GLU A 1 1763 ? 139.315 259.478 227.473 1.00 7.29  ? 1763 GLU A O     1 
ATOM   2504  C  CB    . GLU A 1 1763 ? 141.625 257.129 227.557 1.00 5.57  ? 1763 GLU A CB    1 
ATOM   2505  C  CG    . GLU A 1 1763 ? 142.878 256.636 226.856 1.00 7.83  ? 1763 GLU A CG    1 
ATOM   2506  C  CD    . GLU A 1 1763 ? 142.961 257.095 225.416 1.00 8.32  ? 1763 GLU A CD    1 
ATOM   2507  O  OE1   . GLU A 1 1763 ? 141.901 257.249 224.779 1.00 13.81 ? 1763 GLU A OE1   1 
ATOM   2508  O  OE2   . GLU A 1 1763 ? 144.087 257.284 224.912 1.00 9.77  ? 1763 GLU A OE2   1 
ATOM   2509  N  N     . THR A 1 1764 ? 139.859 258.818 229.555 1.00 6.52  ? 1764 THR A N     1 
ATOM   2510  C  CA    . THR A 1 1764 ? 138.548 259.172 230.087 1.00 7.22  ? 1764 THR A CA    1 
ATOM   2511  C  C     . THR A 1 1764 ? 138.322 260.678 230.035 1.00 9.29  ? 1764 THR A C     1 
ATOM   2512  O  O     . THR A 1 1764 ? 137.238 261.144 229.665 1.00 12.82 ? 1764 THR A O     1 
ATOM   2513  C  CB    . THR A 1 1764 ? 138.408 258.655 231.518 1.00 10.22 ? 1764 THR A CB    1 
ATOM   2514  O  OG1   . THR A 1 1764 ? 138.745 257.264 231.559 1.00 16.82 ? 1764 THR A OG1   1 
ATOM   2515  C  CG2   . THR A 1 1764 ? 136.984 258.835 232.010 1.00 9.48  ? 1764 THR A CG2   1 
ATOM   2516  N  N     . ALA A 1 1765 ? 139.341 261.457 230.404 1.00 11.83 ? 1765 ALA A N     1 
ATOM   2517  C  CA    . ALA A 1 1765 ? 139.204 262.910 230.412 1.00 11.36 ? 1765 ALA A CA    1 
ATOM   2518  C  C     . ALA A 1 1765 ? 139.031 263.460 229.002 1.00 13.10 ? 1765 ALA A C     1 
ATOM   2519  O  O     . ALA A 1 1765 ? 138.164 264.305 228.754 1.00 20.54 ? 1765 ALA A O     1 
ATOM   2520  C  CB    . ALA A 1 1765 ? 140.415 263.545 231.093 1.00 11.00 ? 1765 ALA A CB    1 
ATOM   2521  N  N     . LEU A 1 1766 ? 139.849 262.985 228.059 1.00 9.85  ? 1766 LEU A N     1 
ATOM   2522  C  CA    . LEU A 1 1766 ? 139.761 263.478 226.689 1.00 12.00 ? 1766 LEU A CA    1 
ATOM   2523  C  C     . LEU A 1 1766 ? 138.426 263.110 226.052 1.00 14.04 ? 1766 LEU A C     1 
ATOM   2524  O  O     . LEU A 1 1766 ? 137.902 263.855 225.216 1.00 25.31 ? 1766 LEU A O     1 
ATOM   2525  C  CB    . LEU A 1 1766 ? 140.922 262.933 225.856 1.00 7.75  ? 1766 LEU A CB    1 
ATOM   2526  C  CG    . LEU A 1 1766 ? 142.327 263.395 226.249 1.00 9.42  ? 1766 LEU A CG    1 
ATOM   2527  C  CD1   . LEU A 1 1766 ? 143.372 262.798 225.322 1.00 4.86  ? 1766 LEU A CD1   1 
ATOM   2528  C  CD2   . LEU A 1 1766 ? 142.418 264.909 226.260 1.00 6.76  ? 1766 LEU A CD2   1 
ATOM   2529  N  N     . SER A 1 1767 ? 137.862 261.965 226.436 1.00 16.34 ? 1767 SER A N     1 
ATOM   2530  C  CA    . SER A 1 1767 ? 136.563 261.567 225.905 1.00 18.16 ? 1767 SER A CA    1 
ATOM   2531  C  C     . SER A 1 1767 ? 135.468 262.536 226.339 1.00 19.92 ? 1767 SER A C     1 
ATOM   2532  O  O     . SER A 1 1767 ? 134.561 262.848 225.560 1.00 31.60 ? 1767 SER A O     1 
ATOM   2533  C  CB    . SER A 1 1767 ? 136.232 260.144 226.347 1.00 12.28 ? 1767 SER A CB    1 
ATOM   2534  O  OG    . SER A 1 1767 ? 137.261 259.250 225.972 1.00 20.45 ? 1767 SER A OG    1 
ATOM   2535  N  N     . SER A 1 1768 ? 135.533 263.015 227.582 1.00 17.12 ? 1768 SER A N     1 
ATOM   2536  C  CA    . SER A 1 1768 ? 134.546 263.969 228.072 1.00 15.79 ? 1768 SER A CA    1 
ATOM   2537  C  C     . SER A 1 1768 ? 134.679 265.337 227.414 1.00 22.01 ? 1768 SER A C     1 
ATOM   2538  O  O     . SER A 1 1768 ? 133.703 266.093 227.387 1.00 32.39 ? 1768 SER A O     1 
ATOM   2539  C  CB    . SER A 1 1768 ? 134.666 264.109 229.590 1.00 16.95 ? 1768 SER A CB    1 
ATOM   2540  O  OG    . SER A 1 1768 ? 133.741 265.060 230.088 1.00 27.82 ? 1768 SER A OG    1 
ATOM   2541  N  N     . MET A 1 1769 ? 135.857 265.669 226.887 1.00 21.03 ? 1769 MET A N     1 
ATOM   2542  C  CA    . MET A 1 1769 ? 136.109 266.960 226.264 1.00 19.47 ? 1769 MET A CA    1 
ATOM   2543  C  C     . MET A 1 1769 ? 135.769 266.969 224.777 1.00 31.11 ? 1769 MET A C     1 
ATOM   2544  O  O     . MET A 1 1769 ? 136.294 267.811 224.036 1.00 27.33 ? 1769 MET A O     1 
ATOM   2545  C  CB    . MET A 1 1769 ? 137.569 267.362 226.471 1.00 16.99 ? 1769 MET A CB    1 
ATOM   2546  C  CG    . MET A 1 1769 ? 137.930 267.641 227.919 1.00 22.78 ? 1769 MET A CG    1 
ATOM   2547  S  SD    . MET A 1 1769 ? 139.670 268.034 228.168 1.00 29.22 ? 1769 MET A SD    1 
ATOM   2548  C  CE    . MET A 1 1769 ? 139.762 269.654 227.410 1.00 19.12 ? 1769 MET A CE    1 
ATOM   2549  N  N     . GLY A 1 1770 ? 134.904 266.056 224.330 1.00 29.81 ? 1770 GLY A N     1 
ATOM   2550  C  CA    . GLY A 1 1770 ? 134.604 265.957 222.911 1.00 28.22 ? 1770 GLY A CA    1 
ATOM   2551  C  C     . GLY A 1 1770 ? 133.960 267.211 222.349 1.00 30.97 ? 1770 GLY A C     1 
ATOM   2552  O  O     . GLY A 1 1770 ? 134.164 267.556 221.183 1.00 34.45 ? 1770 GLY A O     1 
ATOM   2553  N  N     . GLY A 1 1771 ? 133.173 267.909 223.170 1.00 26.85 ? 1771 GLY A N     1 
ATOM   2554  C  CA    . GLY A 1 1771 ? 132.515 269.118 222.709 1.00 29.71 ? 1771 GLY A CA    1 
ATOM   2555  C  C     . GLY A 1 1771 ? 133.444 270.299 222.534 1.00 33.83 ? 1771 GLY A C     1 
ATOM   2556  O  O     . GLY A 1 1771 ? 133.037 271.315 221.961 1.00 34.74 ? 1771 GLY A O     1 
ATOM   2557  N  N     . GLY A 1 1772 ? 134.682 270.190 223.010 1.00 31.66 ? 1772 GLY A N     1 
ATOM   2558  C  CA    . GLY A 1 1772 ? 135.639 271.271 222.880 1.00 26.99 ? 1772 GLY A CA    1 
ATOM   2559  C  C     . GLY A 1 1772 ? 135.505 272.313 223.971 1.00 29.59 ? 1772 GLY A C     1 
ATOM   2560  O  O     . GLY A 1 1772 ? 136.431 272.521 224.760 1.00 28.45 ? 1772 GLY A O     1 
ATOM   2561  N  N     . GLY A 1 1773 ? 134.348 272.975 224.024 1.00 28.66 ? 1773 GLY A N     1 
ATOM   2562  C  CA    . GLY A 1 1773 ? 134.111 273.984 225.042 1.00 29.05 ? 1773 GLY A CA    1 
ATOM   2563  C  C     . GLY A 1 1773 ? 133.774 273.412 226.402 1.00 32.40 ? 1773 GLY A C     1 
ATOM   2564  O  O     . GLY A 1 1773 ? 133.618 274.175 227.363 1.00 34.91 ? 1773 GLY A O     1 
ATOM   2565  N  N     . ASP A 1 1774 ? 133.648 272.091 226.508 1.00 32.76 ? 1774 ASP A N     1 
ATOM   2566  C  CA    . ASP A 1 1774 ? 133.361 271.464 227.790 1.00 31.61 ? 1774 ASP A CA    1 
ATOM   2567  C  C     . ASP A 1 1774 ? 134.518 271.681 228.756 1.00 32.34 ? 1774 ASP A C     1 
ATOM   2568  O  O     . ASP A 1 1774 ? 135.669 271.853 228.349 1.00 34.35 ? 1774 ASP A O     1 
ATOM   2569  C  CB    . ASP A 1 1774 ? 133.105 269.967 227.607 1.00 28.77 ? 1774 ASP A CB    1 
ATOM   2570  C  CG    . ASP A 1 1774 ? 131.814 269.680 226.867 1.00 32.36 ? 1774 ASP A CG    1 
ATOM   2571  O  OD1   . ASP A 1 1774 ? 130.876 270.497 226.970 1.00 31.94 ? 1774 ASP A OD1   1 
ATOM   2572  O  OD2   . ASP A 1 1774 ? 131.739 268.639 226.182 1.00 33.75 ? 1774 ASP A OD2   1 
ATOM   2573  N  N     . ALA A 1 1775 ? 134.198 271.681 230.049 1.00 35.06 ? 1775 ALA A N     1 
ATOM   2574  C  CA    . ALA A 1 1775 ? 135.226 271.837 231.066 1.00 31.24 ? 1775 ALA A CA    1 
ATOM   2575  C  C     . ALA A 1 1775 ? 136.252 270.717 230.953 1.00 29.71 ? 1775 ALA A C     1 
ATOM   2576  O  O     . ALA A 1 1775 ? 135.946 269.605 230.516 1.00 28.77 ? 1775 ALA A O     1 
ATOM   2577  C  CB    . ALA A 1 1775 ? 134.602 271.843 232.462 1.00 18.84 ? 1775 ALA A CB    1 
ATOM   2578  N  N     . ALA A 1 1776 ? 137.487 271.024 231.347 1.00 25.64 ? 1776 ALA A N     1 
ATOM   2579  C  CA    . ALA A 1 1776 ? 138.585 270.079 231.202 1.00 22.88 ? 1776 ALA A CA    1 
ATOM   2580  C  C     . ALA A 1 1776 ? 138.750 269.280 232.489 1.00 24.85 ? 1776 ALA A C     1 
ATOM   2581  O  O     . ALA A 1 1776 ? 139.142 269.856 233.515 1.00 17.50 ? 1776 ALA A O     1 
ATOM   2582  C  CB    . ALA A 1 1776 ? 139.876 270.809 230.863 1.00 10.48 ? 1776 ALA A CB    1 
ATOM   2583  N  N     . PRO A 1 1777 ? 138.465 267.975 232.490 1.00 25.88 ? 1777 PRO A N     1 
ATOM   2584  C  CA    . PRO A 1 1777 ? 138.844 267.130 233.627 1.00 22.25 ? 1777 PRO A CA    1 
ATOM   2585  C  C     . PRO A 1 1777 ? 140.276 266.631 233.562 1.00 17.80 ? 1777 PRO A C     1 
ATOM   2586  O  O     . PRO A 1 1777 ? 140.660 265.793 234.386 1.00 19.08 ? 1777 PRO A O     1 
ATOM   2587  C  CB    . PRO A 1 1777 ? 137.849 265.961 233.537 1.00 21.51 ? 1777 PRO A CB    1 
ATOM   2588  C  CG    . PRO A 1 1777 ? 137.346 265.958 232.128 1.00 21.51 ? 1777 PRO A CG    1 
ATOM   2589  C  CD    . PRO A 1 1777 ? 137.794 267.209 231.429 1.00 24.16 ? 1777 PRO A CD    1 
ATOM   2590  N  N     . LEU A 1 1778 ? 141.066 267.108 232.596 1.00 14.87 ? 1778 LEU A N     1 
ATOM   2591  C  CA    . LEU A 1 1778 ? 142.489 266.790 232.568 1.00 10.55 ? 1778 LEU A CA    1 
ATOM   2592  C  C     . LEU A 1 1778 ? 143.200 267.320 233.802 1.00 12.93 ? 1778 LEU A C     1 
ATOM   2593  O  O     . LEU A 1 1778 ? 144.207 266.746 234.234 1.00 14.00 ? 1778 LEU A O     1 
ATOM   2594  C  CB    . LEU A 1 1778 ? 143.136 267.366 231.310 1.00 11.85 ? 1778 LEU A CB    1 
ATOM   2595  C  CG    . LEU A 1 1778 ? 143.370 266.445 230.118 1.00 10.67 ? 1778 LEU A CG    1 
ATOM   2596  C  CD1   . LEU A 1 1778 ? 144.153 267.191 229.053 1.00 11.41 ? 1778 LEU A CD1   1 
ATOM   2597  C  CD2   . LEU A 1 1778 ? 144.105 265.189 230.545 1.00 7.15  ? 1778 LEU A CD2   1 
ATOM   2598  N  N     . HIS A 1 1779 ? 142.699 268.416 234.374 1.00 11.80 ? 1779 HIS A N     1 
ATOM   2599  C  CA    . HIS A 1 1779 ? 143.300 268.962 235.584 1.00 10.52 ? 1779 HIS A CA    1 
ATOM   2600  C  C     . HIS A 1 1779 ? 143.200 267.973 236.737 1.00 9.40  ? 1779 HIS A C     1 
ATOM   2601  O  O     . HIS A 1 1779 ? 144.103 267.896 237.579 1.00 8.86  ? 1779 HIS A O     1 
ATOM   2602  C  CB    . HIS A 1 1779 ? 142.635 270.290 235.942 1.00 15.84 ? 1779 HIS A CB    1 
ATOM   2603  C  CG    . HIS A 1 1779 ? 143.074 271.434 235.083 1.00 18.31 ? 1779 HIS A CG    1 
ATOM   2604  N  ND1   . HIS A 1 1779 ? 142.331 271.894 234.018 1.00 15.35 ? 1779 HIS A ND1   1 
ATOM   2605  C  CD2   . HIS A 1 1779 ? 144.187 272.206 235.125 1.00 17.66 ? 1779 HIS A CD2   1 
ATOM   2606  C  CE1   . HIS A 1 1779 ? 142.963 272.900 233.443 1.00 15.02 ? 1779 HIS A CE1   1 
ATOM   2607  N  NE2   . HIS A 1 1779 ? 144.091 273.111 234.096 1.00 19.76 ? 1779 HIS A NE2   1 
ATOM   2608  N  N     . SER A 1 1780 ? 142.108 267.208 236.793 1.00 11.95 ? 1780 SER A N     1 
ATOM   2609  C  CA    . SER A 1 1780 ? 141.992 266.157 237.799 1.00 12.29 ? 1780 SER A CA    1 
ATOM   2610  C  C     . SER A 1 1780 ? 143.025 265.059 237.574 1.00 9.91  ? 1780 SER A C     1 
ATOM   2611  O  O     . SER A 1 1780 ? 143.575 264.510 238.536 1.00 12.35 ? 1780 SER A O     1 
ATOM   2612  C  CB    . SER A 1 1780 ? 140.579 265.579 237.794 1.00 8.27  ? 1780 SER A CB    1 
ATOM   2613  O  OG    . SER A 1 1780 ? 139.633 266.562 238.174 1.00 15.65 ? 1780 SER A OG    1 
ATOM   2614  N  N     . VAL A 1 1781 ? 143.293 264.716 236.312 1.00 7.48  ? 1781 VAL A N     1 
ATOM   2615  C  CA    . VAL A 1 1781 ? 144.349 263.753 236.013 1.00 7.66  ? 1781 VAL A CA    1 
ATOM   2616  C  C     . VAL A 1 1781 ? 145.689 264.279 236.504 1.00 8.76  ? 1781 VAL A C     1 
ATOM   2617  O  O     . VAL A 1 1781 ? 146.470 263.552 237.131 1.00 12.45 ? 1781 VAL A O     1 
ATOM   2618  C  CB    . VAL A 1 1781 ? 144.383 263.436 234.507 1.00 8.46  ? 1781 VAL A CB    1 
ATOM   2619  C  CG1   . VAL A 1 1781 ? 145.634 262.641 234.155 1.00 4.93  ? 1781 VAL A CG1   1 
ATOM   2620  C  CG2   . VAL A 1 1781 ? 143.134 262.679 234.096 1.00 7.96  ? 1781 VAL A CG2   1 
ATOM   2621  N  N     . LEU A 1 1782 ? 145.974 265.554 236.235 1.00 8.39  ? 1782 LEU A N     1 
ATOM   2622  C  CA    . LEU A 1 1782 ? 147.157 266.186 236.803 1.00 5.07  ? 1782 LEU A CA    1 
ATOM   2623  C  C     . LEU A 1 1782 ? 147.080 266.219 238.324 1.00 8.81  ? 1782 LEU A C     1 
ATOM   2624  O  O     . LEU A 1 1782 ? 148.079 265.971 239.008 1.00 10.99 ? 1782 LEU A O     1 
ATOM   2625  C  CB    . LEU A 1 1782 ? 147.317 267.597 236.239 1.00 4.39  ? 1782 LEU A CB    1 
ATOM   2626  C  CG    . LEU A 1 1782 ? 148.545 268.391 236.680 1.00 8.75  ? 1782 LEU A CG    1 
ATOM   2627  C  CD1   . LEU A 1 1782 ? 149.826 267.650 236.329 1.00 4.29  ? 1782 LEU A CD1   1 
ATOM   2628  C  CD2   . LEU A 1 1782 ? 148.533 269.775 236.057 1.00 5.19  ? 1782 LEU A CD2   1 
ATOM   2629  N  N     . SER A 1 1783 ? 145.895 266.510 238.868 1.00 7.84  ? 1783 SER A N     1 
ATOM   2630  C  CA    . SER A 1 1783 ? 145.729 266.570 240.316 1.00 7.18  ? 1783 SER A CA    1 
ATOM   2631  C  C     . SER A 1 1783 ? 146.051 265.232 240.969 1.00 10.83 ? 1783 SER A C     1 
ATOM   2632  O  O     . SER A 1 1783 ? 146.716 265.186 242.011 1.00 11.93 ? 1783 SER A O     1 
ATOM   2633  C  CB    . SER A 1 1783 ? 144.303 267.002 240.660 1.00 10.93 ? 1783 SER A CB    1 
ATOM   2634  O  OG    . SER A 1 1783 ? 144.099 267.033 242.061 1.00 19.10 ? 1783 SER A OG    1 
ATOM   2635  N  N     . ASN A 1 1784 ? 145.579 264.132 240.378 1.00 12.67 ? 1784 ASN A N     1 
ATOM   2636  C  CA    . ASN A 1 1784 ? 145.874 262.814 240.929 1.00 8.07  ? 1784 ASN A CA    1 
ATOM   2637  C  C     . ASN A 1 1784 ? 147.367 262.522 240.889 1.00 6.67  ? 1784 ASN A C     1 
ATOM   2638  O  O     . ASN A 1 1784 ? 147.920 261.944 241.831 1.00 10.41 ? 1784 ASN A O     1 
ATOM   2639  C  CB    . ASN A 1 1784 ? 145.096 261.741 240.168 1.00 12.41 ? 1784 ASN A CB    1 
ATOM   2640  C  CG    . ASN A 1 1784 ? 145.236 260.368 240.793 1.00 16.13 ? 1784 ASN A CG    1 
ATOM   2641  O  OD1   . ASN A 1 1784 ? 145.867 259.477 240.226 1.00 16.09 ? 1784 ASN A OD1   1 
ATOM   2642  N  ND2   . ASN A 1 1784 ? 144.642 260.187 241.965 1.00 12.25 ? 1784 ASN A ND2   1 
ATOM   2643  N  N     . VAL A 1 1785 ? 148.035 262.907 239.800 1.00 8.78  ? 1785 VAL A N     1 
ATOM   2644  C  CA    . VAL A 1 1785 ? 149.476 262.694 239.695 1.00 7.52  ? 1785 VAL A CA    1 
ATOM   2645  C  C     . VAL A 1 1785 ? 150.221 263.535 240.728 1.00 9.17  ? 1785 VAL A C     1 
ATOM   2646  O  O     . VAL A 1 1785 ? 151.182 263.066 241.347 1.00 8.48  ? 1785 VAL A O     1 
ATOM   2647  C  CB    . VAL A 1 1785 ? 149.954 262.988 238.262 1.00 4.90  ? 1785 VAL A CB    1 
ATOM   2648  C  CG1   . VAL A 1 1785 ? 151.466 262.919 238.178 1.00 3.63  ? 1785 VAL A CG1   1 
ATOM   2649  C  CG2   . VAL A 1 1785 ? 149.324 262.006 237.288 1.00 3.89  ? 1785 VAL A CG2   1 
ATOM   2650  N  N     . GLU A 1 1786 ? 149.792 264.784 240.934 1.00 8.69  ? 1786 GLU A N     1 
ATOM   2651  C  CA    . GLU A 1 1786 ? 150.414 265.625 241.953 1.00 10.00 ? 1786 GLU A CA    1 
ATOM   2652  C  C     . GLU A 1 1786 ? 150.283 265.002 243.336 1.00 9.42  ? 1786 GLU A C     1 
ATOM   2653  O  O     . GLU A 1 1786 ? 151.254 264.951 244.101 1.00 10.04 ? 1786 GLU A O     1 
ATOM   2654  C  CB    . GLU A 1 1786 ? 149.789 267.021 241.946 1.00 12.51 ? 1786 GLU A CB    1 
ATOM   2655  C  CG    . GLU A 1 1786 ? 149.957 267.798 240.661 1.00 12.34 ? 1786 GLU A CG    1 
ATOM   2656  C  CD    . GLU A 1 1786 ? 151.346 268.366 240.515 1.00 17.86 ? 1786 GLU A CD    1 
ATOM   2657  O  OE1   . GLU A 1 1786 ? 151.653 269.377 241.184 1.00 24.63 ? 1786 GLU A OE1   1 
ATOM   2658  O  OE2   . GLU A 1 1786 ? 152.136 267.800 239.737 1.00 19.94 ? 1786 GLU A OE2   1 
ATOM   2659  N  N     . VAL A 1 1787 ? 149.086 264.522 243.676 1.00 8.09  ? 1787 VAL A N     1 
ATOM   2660  C  CA    . VAL A 1 1787 ? 148.858 263.951 244.999 1.00 8.56  ? 1787 VAL A CA    1 
ATOM   2661  C  C     . VAL A 1 1787 ? 149.687 262.685 245.179 1.00 7.69  ? 1787 VAL A C     1 
ATOM   2662  O  O     . VAL A 1 1787 ? 150.346 262.493 246.208 1.00 9.68  ? 1787 VAL A O     1 
ATOM   2663  C  CB    . VAL A 1 1787 ? 147.358 263.678 245.214 1.00 7.88  ? 1787 VAL A CB    1 
ATOM   2664  C  CG1   . VAL A 1 1787 ? 147.149 262.673 246.338 1.00 12.36 ? 1787 VAL A CG1   1 
ATOM   2665  C  CG2   . VAL A 1 1787 ? 146.619 264.972 245.499 1.00 10.99 ? 1787 VAL A CG2   1 
ATOM   2666  N  N     . THR A 1 1788 ? 149.678 261.809 244.173 1.00 5.68  ? 1788 THR A N     1 
ATOM   2667  C  CA    . THR A 1 1788 ? 150.412 260.554 244.275 1.00 6.05  ? 1788 THR A CA    1 
ATOM   2668  C  C     . THR A 1 1788 ? 151.911 260.808 244.354 1.00 6.37  ? 1788 THR A C     1 
ATOM   2669  O  O     . THR A 1 1788 ? 152.628 260.126 245.095 1.00 7.49  ? 1788 THR A O     1 
ATOM   2670  C  CB    . THR A 1 1788 ? 150.084 259.660 243.080 1.00 4.91  ? 1788 THR A CB    1 
ATOM   2671  O  OG1   . THR A 1 1788 ? 148.679 259.396 243.057 1.00 10.17 ? 1788 THR A OG1   1 
ATOM   2672  C  CG2   . THR A 1 1788 ? 150.800 258.331 243.210 1.00 5.16  ? 1788 THR A CG2   1 
ATOM   2673  N  N     . LEU A 1 1789 ? 152.401 261.794 243.601 1.00 7.87  ? 1789 LEU A N     1 
ATOM   2674  C  CA    . LEU A 1 1789 ? 153.829 262.086 243.591 1.00 5.42  ? 1789 LEU A CA    1 
ATOM   2675  C  C     . LEU A 1 1789 ? 154.277 262.686 244.919 1.00 6.15  ? 1789 LEU A C     1 
ATOM   2676  O  O     . LEU A 1 1789 ? 155.419 262.481 245.347 1.00 12.34 ? 1789 LEU A O     1 
ATOM   2677  C  CB    . LEU A 1 1789 ? 154.152 263.019 242.424 1.00 4.71  ? 1789 LEU A CB    1 
ATOM   2678  C  CG    . LEU A 1 1789 ? 155.601 263.416 242.157 1.00 10.58 ? 1789 LEU A CG    1 
ATOM   2679  C  CD1   . LEU A 1 1789 ? 156.417 262.183 241.814 1.00 3.22  ? 1789 LEU A CD1   1 
ATOM   2680  C  CD2   . LEU A 1 1789 ? 155.661 264.429 241.029 1.00 11.13 ? 1789 LEU A CD2   1 
ATOM   2681  N  N     . ASN A 1 1790 ? 153.394 263.435 245.587 1.00 8.19  ? 1790 ASN A N     1 
ATOM   2682  C  CA    . ASN A 1 1790 ? 153.727 263.973 246.904 1.00 6.82  ? 1790 ASN A CA    1 
ATOM   2683  C  C     . ASN A 1 1790 ? 153.898 262.861 247.932 1.00 9.00  ? 1790 ASN A C     1 
ATOM   2684  O  O     . ASN A 1 1790 ? 154.797 262.926 248.779 1.00 12.22 ? 1790 ASN A O     1 
ATOM   2685  C  CB    . ASN A 1 1790 ? 152.659 264.965 247.359 1.00 9.08  ? 1790 ASN A CB    1 
ATOM   2686  C  CG    . ASN A 1 1790 ? 152.729 266.282 246.609 1.00 15.43 ? 1790 ASN A CG    1 
ATOM   2687  O  OD1   . ASN A 1 1790 ? 153.813 266.773 246.297 1.00 15.45 ? 1790 ASN A OD1   1 
ATOM   2688  N  ND2   . ASN A 1 1790 ? 151.570 266.859 246.315 1.00 15.76 ? 1790 ASN A ND2   1 
ATOM   2689  N  N     . VAL A 1 1791 ? 153.040 261.840 247.881 1.00 7.09  ? 1791 VAL A N     1 
ATOM   2690  C  CA    . VAL A 1 1791 ? 153.187 260.698 248.780 1.00 7.92  ? 1791 VAL A CA    1 
ATOM   2691  C  C     . VAL A 1 1791 ? 154.482 259.952 248.484 1.00 9.05  ? 1791 VAL A C     1 
ATOM   2692  O  O     . VAL A 1 1791 ? 155.202 259.543 249.404 1.00 9.79  ? 1791 VAL A O     1 
ATOM   2693  C  CB    . VAL A 1 1791 ? 151.960 259.776 248.675 1.00 7.99  ? 1791 VAL A CB    1 
ATOM   2694  C  CG1   . VAL A 1 1791 ? 152.167 258.519 249.499 1.00 8.22  ? 1791 VAL A CG1   1 
ATOM   2695  C  CG2   . VAL A 1 1791 ? 150.712 260.506 249.127 1.00 9.48  ? 1791 VAL A CG2   1 
ATOM   2696  N  N     . LEU A 1 1792 ? 154.793 259.754 247.201 1.00 7.13  ? 1792 LEU A N     1 
ATOM   2697  C  CA    . LEU A 1 1792 ? 156.045 259.098 246.838 1.00 6.49  ? 1792 LEU A CA    1 
ATOM   2698  C  C     . LEU A 1 1792 ? 157.246 259.912 247.297 1.00 6.90  ? 1792 LEU A C     1 
ATOM   2699  O  O     . LEU A 1 1792 ? 158.220 259.357 247.819 1.00 6.51  ? 1792 LEU A O     1 
ATOM   2700  C  CB    . LEU A 1 1792 ? 156.097 258.874 245.328 1.00 5.35  ? 1792 LEU A CB    1 
ATOM   2701  C  CG    . LEU A 1 1792 ? 155.095 257.883 244.738 1.00 4.54  ? 1792 LEU A CG    1 
ATOM   2702  C  CD1   . LEU A 1 1792 ? 155.106 257.964 243.221 1.00 5.27  ? 1792 LEU A CD1   1 
ATOM   2703  C  CD2   . LEU A 1 1792 ? 155.405 256.477 245.201 1.00 3.55  ? 1792 LEU A CD2   1 
ATOM   2704  N  N     . ALA A 1 1793 ? 157.192 261.233 247.112 1.00 9.29  ? 1793 ALA A N     1 
ATOM   2705  C  CA    . ALA A 1 1793 ? 158.291 262.088 247.550 1.00 7.06  ? 1793 ALA A CA    1 
ATOM   2706  C  C     . ALA A 1 1793 ? 158.438 262.064 249.066 1.00 10.20 ? 1793 ALA A C     1 
ATOM   2707  O  O     . ALA A 1 1793 ? 159.557 262.084 249.588 1.00 13.31 ? 1793 ALA A O     1 
ATOM   2708  C  CB    . ALA A 1 1793 ? 158.075 263.516 247.052 1.00 8.94  ? 1793 ALA A CB    1 
ATOM   2709  N  N     . ASP A 1 1794 ? 157.316 262.031 249.790 1.00 10.20 ? 1794 ASP A N     1 
ATOM   2710  C  CA    . ASP A 1 1794 ? 157.380 261.941 251.245 1.00 9.32  ? 1794 ASP A CA    1 
ATOM   2711  C  C     . ASP A 1 1794 ? 157.975 260.612 251.695 1.00 11.24 ? 1794 ASP A C     1 
ATOM   2712  O  O     . ASP A 1 1794 ? 158.716 260.561 252.684 1.00 15.83 ? 1794 ASP A O     1 
ATOM   2713  C  CB    . ASP A 1 1794 ? 155.989 262.135 251.847 1.00 11.93 ? 1794 ASP A CB    1 
ATOM   2714  C  CG    . ASP A 1 1794 ? 155.652 263.594 252.074 1.00 27.37 ? 1794 ASP A CG    1 
ATOM   2715  O  OD1   . ASP A 1 1794 ? 156.506 264.455 251.775 1.00 27.98 ? 1794 ASP A OD1   1 
ATOM   2716  O  OD2   . ASP A 1 1794 ? 154.537 263.882 252.554 1.00 36.78 ? 1794 ASP A OD2   1 
ATOM   2717  N  N     . SER A 1 1795 ? 157.656 259.526 250.988 1.00 12.77 ? 1795 SER A N     1 
ATOM   2718  C  CA    . SER A 1 1795 ? 158.152 258.212 251.382 1.00 7.04  ? 1795 SER A CA    1 
ATOM   2719  C  C     . SER A 1 1795 ? 159.670 258.126 251.265 1.00 9.16  ? 1795 SER A C     1 
ATOM   2720  O  O     . SER A 1 1795 ? 160.331 257.522 252.119 1.00 13.57 ? 1795 SER A O     1 
ATOM   2721  C  CB    . SER A 1 1795 ? 157.485 257.125 250.540 1.00 6.40  ? 1795 SER A CB    1 
ATOM   2722  O  OG    . SER A 1 1795 ? 156.081 257.139 250.714 1.00 6.97  ? 1795 SER A OG    1 
ATOM   2723  N  N     . VAL A 1 1796 ? 160.243 258.721 250.214 1.00 6.87  ? 1796 VAL A N     1 
ATOM   2724  C  CA    . VAL A 1 1796 ? 161.690 258.650 250.016 1.00 8.42  ? 1796 VAL A CA    1 
ATOM   2725  C  C     . VAL A 1 1796 ? 162.449 259.659 250.861 1.00 11.49 ? 1796 VAL A C     1 
ATOM   2726  O  O     . VAL A 1 1796 ? 163.687 259.633 250.874 1.00 11.10 ? 1796 VAL A O     1 
ATOM   2727  C  CB    . VAL A 1 1796 ? 162.062 258.840 248.530 1.00 7.18  ? 1796 VAL A CB    1 
ATOM   2728  C  CG1   . VAL A 1 1796 ? 161.432 257.746 247.685 1.00 6.80  ? 1796 VAL A CG1   1 
ATOM   2729  C  CG2   . VAL A 1 1796 ? 161.646 260.211 248.040 1.00 7.10  ? 1796 VAL A CG2   1 
ATOM   2730  N  N     . LEU A 1 1797 ? 161.751 260.547 251.570 1.00 11.56 ? 1797 LEU A N     1 
ATOM   2731  C  CA    . LEU A 1 1797 ? 162.413 261.452 252.502 1.00 12.29 ? 1797 LEU A CA    1 
ATOM   2732  C  C     . LEU A 1 1797 ? 162.812 260.760 253.797 1.00 13.60 ? 1797 LEU A C     1 
ATOM   2733  O  O     . LEU A 1 1797 ? 163.565 261.339 254.587 1.00 19.65 ? 1797 LEU A O     1 
ATOM   2734  C  CB    . LEU A 1 1797 ? 161.509 262.646 252.815 1.00 10.82 ? 1797 LEU A CB    1 
ATOM   2735  C  CG    . LEU A 1 1797 ? 161.314 263.680 251.706 1.00 13.89 ? 1797 LEU A CG    1 
ATOM   2736  C  CD1   . LEU A 1 1797 ? 160.253 264.697 252.096 1.00 14.02 ? 1797 LEU A CD1   1 
ATOM   2737  C  CD2   . LEU A 1 1797 ? 162.620 264.371 251.378 1.00 10.60 ? 1797 LEU A CD2   1 
ATOM   2738  N  N     . MET A 1 1798 ? 162.329 259.547 254.027 1.00 9.56  ? 1798 MET A N     1 
ATOM   2739  C  CA    . MET A 1 1798 ? 162.616 258.768 255.221 1.00 13.28 ? 1798 MET A CA    1 
ATOM   2740  C  C     . MET A 1 1798 ? 163.210 257.420 254.819 1.00 17.10 ? 1798 MET A C     1 
ATOM   2741  O  O     . MET A 1 1798 ? 163.271 257.068 253.640 1.00 18.54 ? 1798 MET A O     1 
ATOM   2742  C  CB    . MET A 1 1798 ? 161.352 258.600 256.064 1.00 16.62 ? 1798 MET A CB    1 
ATOM   2743  C  CG    . MET A 1 1798 ? 160.264 257.781 255.394 1.00 15.56 ? 1798 MET A CG    1 
ATOM   2744  S  SD    . MET A 1 1798 ? 158.773 257.653 256.395 1.00 45.47 ? 1798 MET A SD    1 
ATOM   2745  C  CE    . MET A 1 1798 ? 157.728 256.670 255.323 1.00 19.16 ? 1798 MET A CE    1 
ATOM   2746  N  N     . GLU A 1 1799 ? 163.661 256.667 255.820 1.00 16.65 ? 1799 GLU A N     1 
ATOM   2747  C  CA    . GLU A 1 1799 ? 164.293 255.382 255.560 1.00 15.09 ? 1799 GLU A CA    1 
ATOM   2748  C  C     . GLU A 1 1799 ? 163.266 254.365 255.080 1.00 18.76 ? 1799 GLU A C     1 
ATOM   2749  O  O     . GLU A 1 1799 ? 162.138 254.313 255.578 1.00 17.67 ? 1799 GLU A O     1 
ATOM   2750  C  CB    . GLU A 1 1799 ? 164.995 254.870 256.818 1.00 17.27 ? 1799 GLU A CB    1 
ATOM   2751  C  CG    . GLU A 1 1799 ? 166.227 254.026 256.537 1.00 21.08 ? 1799 GLU A CG    1 
ATOM   2752  C  CD    . GLU A 1 1799 ? 166.691 253.252 257.754 1.00 31.32 ? 1799 GLU A CD    1 
ATOM   2753  O  OE1   . GLU A 1 1799 ? 166.033 253.348 258.809 1.00 33.21 ? 1799 GLU A OE1   1 
ATOM   2754  O  OE2   . GLU A 1 1799 ? 167.713 252.541 257.651 1.00 31.00 ? 1799 GLU A OE2   1 
ATOM   2755  N  N     . GLN A 1 1800 ? 163.660 253.564 254.100 1.00 18.46 ? 1800 GLN A N     1 
ATOM   2756  C  CA    . GLN A 1 1800 ? 162.801 252.559 253.497 1.00 13.34 ? 1800 GLN A CA    1 
ATOM   2757  C  C     . GLN A 1 1800 ? 163.609 251.294 253.263 1.00 9.35  ? 1800 GLN A C     1 
ATOM   2758  O  O     . GLN A 1 1800 ? 164.841 251.342 253.188 1.00 13.04 ? 1800 GLN A O     1 
ATOM   2759  C  CB    . GLN A 1 1800 ? 162.204 253.045 252.166 1.00 6.19  ? 1800 GLN A CB    1 
ATOM   2760  C  CG    . GLN A 1 1800 ? 161.360 254.305 252.262 1.00 7.26  ? 1800 GLN A CG    1 
ATOM   2761  C  CD    . GLN A 1 1800 ? 159.945 254.032 252.738 1.00 10.95 ? 1800 GLN A CD    1 
ATOM   2762  O  OE1   . GLN A 1 1800 ? 159.606 252.911 253.111 1.00 12.66 ? 1800 GLN A OE1   1 
ATOM   2763  N  NE2   . GLN A 1 1800 ? 159.111 255.063 252.725 1.00 8.50  ? 1800 GLN A NE2   1 
ATOM   2764  N  N     . PRO A 1 1801 ? 162.944 250.144 253.159 1.00 7.87  ? 1801 PRO A N     1 
ATOM   2765  C  CA    . PRO A 1 1801 ? 163.651 248.931 252.759 1.00 6.11  ? 1801 PRO A CA    1 
ATOM   2766  C  C     . PRO A 1 1801 ? 164.265 249.103 251.387 1.00 7.83  ? 1801 PRO A C     1 
ATOM   2767  O  O     . PRO A 1 1801 ? 163.723 249.825 250.528 1.00 9.68  ? 1801 PRO A O     1 
ATOM   2768  C  CB    . PRO A 1 1801 ? 162.547 247.867 252.753 1.00 8.23  ? 1801 PRO A CB    1 
ATOM   2769  C  CG    . PRO A 1 1801 ? 161.529 248.378 253.705 1.00 8.98  ? 1801 PRO A CG    1 
ATOM   2770  C  CD    . PRO A 1 1801 ? 161.558 249.870 253.575 1.00 8.36  ? 1801 PRO A CD    1 
ATOM   2771  N  N     . PRO A 1 1802 ? 165.415 248.468 251.134 1.00 9.92  ? 1802 PRO A N     1 
ATOM   2772  C  CA    . PRO A 1 1802 ? 166.117 248.703 249.858 1.00 7.14  ? 1802 PRO A CA    1 
ATOM   2773  C  C     . PRO A 1 1802 ? 165.297 248.361 248.627 1.00 7.93  ? 1802 PRO A C     1 
ATOM   2774  O  O     . PRO A 1 1802 ? 165.397 249.061 247.613 1.00 7.70  ? 1802 PRO A O     1 
ATOM   2775  C  CB    . PRO A 1 1802 ? 167.362 247.811 249.981 1.00 4.10  ? 1802 PRO A CB    1 
ATOM   2776  C  CG    . PRO A 1 1802 ? 167.542 247.612 251.449 1.00 7.22  ? 1802 PRO A CG    1 
ATOM   2777  C  CD    . PRO A 1 1802 ? 166.156 247.543 252.006 1.00 8.68  ? 1802 PRO A CD    1 
ATOM   2778  N  N     . LEU A 1 1803 ? 164.488 247.302 248.680 1.00 7.70  ? 1803 LEU A N     1 
ATOM   2779  C  CA    . LEU A 1 1803 ? 163.656 246.964 247.530 1.00 4.47  ? 1803 LEU A CA    1 
ATOM   2780  C  C     . LEU A 1 1803 ? 162.521 247.964 247.359 1.00 6.48  ? 1803 LEU A C     1 
ATOM   2781  O  O     . LEU A 1 1803 ? 162.230 248.394 246.237 1.00 6.66  ? 1803 LEU A O     1 
ATOM   2782  C  CB    . LEU A 1 1803 ? 163.106 245.547 247.673 1.00 5.03  ? 1803 LEU A CB    1 
ATOM   2783  C  CG    . LEU A 1 1803 ? 162.205 245.069 246.533 1.00 4.14  ? 1803 LEU A CG    1 
ATOM   2784  C  CD1   . LEU A 1 1803 ? 163.014 244.856 245.266 1.00 5.42  ? 1803 LEU A CD1   1 
ATOM   2785  C  CD2   . LEU A 1 1803 ? 161.462 243.801 246.920 1.00 5.94  ? 1803 LEU A CD2   1 
ATOM   2786  N  N     . ARG A 1 1804 ? 161.868 248.347 248.460 1.00 4.83  ? 1804 ARG A N     1 
ATOM   2787  C  CA    . ARG A 1 1804 ? 160.783 249.317 248.373 1.00 5.42  ? 1804 ARG A CA    1 
ATOM   2788  C  C     . ARG A 1 1804 ? 161.295 250.686 247.943 1.00 4.98  ? 1804 ARG A C     1 
ATOM   2789  O  O     . ARG A 1 1804 ? 160.641 251.378 247.153 1.00 5.51  ? 1804 ARG A O     1 
ATOM   2790  C  CB    . ARG A 1 1804 ? 160.053 249.416 249.710 1.00 6.50  ? 1804 ARG A CB    1 
ATOM   2791  C  CG    . ARG A 1 1804 ? 158.859 250.352 249.679 1.00 5.32  ? 1804 ARG A CG    1 
ATOM   2792  C  CD    . ARG A 1 1804 ? 158.457 250.787 251.070 1.00 8.25  ? 1804 ARG A CD    1 
ATOM   2793  N  NE    . ARG A 1 1804 ? 157.938 249.684 251.871 1.00 9.28  ? 1804 ARG A NE    1 
ATOM   2794  C  CZ    . ARG A 1 1804 ? 157.645 249.776 253.161 1.00 7.97  ? 1804 ARG A CZ    1 
ATOM   2795  N  NH1   . ARG A 1 1804 ? 157.837 250.899 253.833 1.00 10.18 ? 1804 ARG A NH1   1 
ATOM   2796  N  NH2   . ARG A 1 1804 ? 157.146 248.717 253.788 1.00 12.05 ? 1804 ARG A NH2   1 
ATOM   2797  N  N     . ARG A 1 1805 ? 162.464 251.089 248.447 1.00 4.98  ? 1805 ARG A N     1 
ATOM   2798  C  CA    . ARG A 1 1805 ? 163.019 252.388 248.081 1.00 3.59  ? 1805 ARG A CA    1 
ATOM   2799  C  C     . ARG A 1 1805 ? 163.269 252.478 246.583 1.00 5.69  ? 1805 ARG A C     1 
ATOM   2800  O  O     . ARG A 1 1805 ? 162.988 253.507 245.958 1.00 8.79  ? 1805 ARG A O     1 
ATOM   2801  C  CB    . ARG A 1 1805 ? 164.314 252.641 248.853 1.00 7.31  ? 1805 ARG A CB    1 
ATOM   2802  C  CG    . ARG A 1 1805 ? 164.915 254.012 248.606 1.00 6.51  ? 1805 ARG A CG    1 
ATOM   2803  C  CD    . ARG A 1 1805 ? 166.419 254.004 248.787 1.00 8.33  ? 1805 ARG A CD    1 
ATOM   2804  N  NE    . ARG A 1 1805 ? 167.107 253.466 247.621 1.00 15.89 ? 1805 ARG A NE    1 
ATOM   2805  C  CZ    . ARG A 1 1805 ? 168.030 252.516 247.666 1.00 15.22 ? 1805 ARG A CZ    1 
ATOM   2806  N  NH1   . ARG A 1 1805 ? 168.413 251.977 248.813 1.00 10.75 ? 1805 ARG A NH1   1 
ATOM   2807  N  NH2   . ARG A 1 1805 ? 168.588 252.098 246.535 1.00 13.50 ? 1805 ARG A NH2   1 
ATOM   2808  N  N     . ARG A 1 1806 ? 163.807 251.412 245.990 1.00 4.95  ? 1806 ARG A N     1 
ATOM   2809  C  CA    . ARG A 1 1806 ? 164.010 251.406 244.547 1.00 5.47  ? 1806 ARG A CA    1 
ATOM   2810  C  C     . ARG A 1 1806 ? 162.681 251.421 243.799 1.00 3.31  ? 1806 ARG A C     1 
ATOM   2811  O  O     . ARG A 1 1806 ? 162.545 252.148 242.811 1.00 3.38  ? 1806 ARG A O     1 
ATOM   2812  C  CB    . ARG A 1 1806 ? 164.875 250.210 244.151 1.00 7.90  ? 1806 ARG A CB    1 
ATOM   2813  C  CG    . ARG A 1 1806 ? 166.268 250.298 244.761 1.00 6.29  ? 1806 ARG A CG    1 
ATOM   2814  C  CD    . ARG A 1 1806 ? 167.199 249.179 244.342 1.00 8.28  ? 1806 ARG A CD    1 
ATOM   2815  N  NE    . ARG A 1 1806 ? 167.606 249.279 242.947 1.00 16.56 ? 1806 ARG A NE    1 
ATOM   2816  C  CZ    . ARG A 1 1806 ? 167.692 248.245 242.119 1.00 14.10 ? 1806 ARG A CZ    1 
ATOM   2817  N  NH1   . ARG A 1 1806 ? 167.427 247.014 242.522 1.00 14.28 ? 1806 ARG A NH1   1 
ATOM   2818  N  NH2   . ARG A 1 1806 ? 168.065 248.452 240.859 1.00 7.76  ? 1806 ARG A NH2   1 
ATOM   2819  N  N     . LYS A 1 1807 ? 161.685 250.669 244.275 1.00 4.25  ? 1807 LYS A N     1 
ATOM   2820  C  CA    . LYS A 1 1807 ? 160.351 250.744 243.684 1.00 2.22  ? 1807 LYS A CA    1 
ATOM   2821  C  C     . LYS A 1 1807 ? 159.804 252.163 243.733 1.00 2.45  ? 1807 LYS A C     1 
ATOM   2822  O  O     . LYS A 1 1807 ? 159.204 252.640 242.763 1.00 2.44  ? 1807 LYS A O     1 
ATOM   2823  C  CB    . LYS A 1 1807 ? 159.393 249.798 244.405 1.00 1.97  ? 1807 LYS A CB    1 
ATOM   2824  C  CG    . LYS A 1 1807 ? 159.519 248.338 244.044 1.00 1.23  ? 1807 LYS A CG    1 
ATOM   2825  C  CD    . LYS A 1 1807 ? 158.549 247.523 244.877 1.00 1.80  ? 1807 LYS A CD    1 
ATOM   2826  C  CE    . LYS A 1 1807 ? 158.546 246.065 244.482 1.00 3.79  ? 1807 LYS A CE    1 
ATOM   2827  N  NZ    . LYS A 1 1807 ? 157.702 245.265 245.409 1.00 4.51  ? 1807 LYS A NZ    1 
ATOM   2828  N  N     . LEU A 1 1808 ? 159.989 252.847 244.863 1.00 5.73  ? 1808 LEU A N     1 
ATOM   2829  C  CA    . LEU A 1 1808 ? 159.545 254.230 244.977 1.00 2.31  ? 1808 LEU A CA    1 
ATOM   2830  C  C     . LEU A 1 1808 ? 160.301 255.132 244.008 1.00 2.56  ? 1808 LEU A C     1 
ATOM   2831  O  O     . LEU A 1 1808 ? 159.727 256.073 243.451 1.00 3.25  ? 1808 LEU A O     1 
ATOM   2832  C  CB    . LEU A 1 1808 ? 159.717 254.715 246.415 1.00 3.41  ? 1808 LEU A CB    1 
ATOM   2833  C  CG    . LEU A 1 1808 ? 158.872 254.013 247.478 1.00 3.34  ? 1808 LEU A CG    1 
ATOM   2834  C  CD1   . LEU A 1 1808 ? 159.527 254.129 248.846 1.00 2.19  ? 1808 LEU A CD1   1 
ATOM   2835  C  CD2   . LEU A 1 1808 ? 157.466 254.577 247.508 1.00 6.37  ? 1808 LEU A CD2   1 
ATOM   2836  N  N     . GLU A 1 1809 ? 161.592 254.865 243.803 1.00 3.05  ? 1809 GLU A N     1 
ATOM   2837  C  CA    . GLU A 1 1809 ? 162.362 255.646 242.841 1.00 3.11  ? 1809 GLU A CA    1 
ATOM   2838  C  C     . GLU A 1 1809 ? 161.848 255.434 241.422 1.00 2.25  ? 1809 GLU A C     1 
ATOM   2839  O  O     . GLU A 1 1809 ? 161.827 256.371 240.618 1.00 1.92  ? 1809 GLU A O     1 
ATOM   2840  C  CB    . GLU A 1 1809 ? 163.846 255.290 242.937 1.00 3.01  ? 1809 GLU A CB    1 
ATOM   2841  C  CG    . GLU A 1 1809 ? 164.539 255.863 244.158 1.00 6.73  ? 1809 GLU A CG    1 
ATOM   2842  C  CD    . GLU A 1 1809 ? 165.818 255.127 244.507 1.00 18.94 ? 1809 GLU A CD    1 
ATOM   2843  O  OE1   . GLU A 1 1809 ? 166.115 254.103 243.860 1.00 18.24 ? 1809 GLU A OE1   1 
ATOM   2844  O  OE2   . GLU A 1 1809 ? 166.529 255.576 245.429 1.00 16.97 ? 1809 GLU A OE2   1 
ATOM   2845  N  N     . HIS A 1 1810 ? 161.442 254.205 241.092 1.00 5.35  ? 1810 HIS A N     1 
ATOM   2846  C  CA    . HIS A 1 1810 ? 160.897 253.950 239.762 1.00 2.59  ? 1810 HIS A CA    1 
ATOM   2847  C  C     . HIS A 1 1810 ? 159.568 254.671 239.568 1.00 2.16  ? 1810 HIS A C     1 
ATOM   2848  O  O     . HIS A 1 1810 ? 159.301 255.219 238.493 1.00 2.70  ? 1810 HIS A O     1 
ATOM   2849  C  CB    . HIS A 1 1810 ? 160.721 252.451 239.526 1.00 2.91  ? 1810 HIS A CB    1 
ATOM   2850  C  CG    . HIS A 1 1810 ? 162.003 251.679 239.519 1.00 5.44  ? 1810 HIS A CG    1 
ATOM   2851  N  ND1   . HIS A 1 1810 ? 162.889 251.718 238.467 1.00 13.33 ? 1810 HIS A ND1   1 
ATOM   2852  C  CD2   . HIS A 1 1810 ? 162.508 250.784 240.398 1.00 12.89 ? 1810 HIS A CD2   1 
ATOM   2853  C  CE1   . HIS A 1 1810 ? 163.915 250.927 238.726 1.00 10.44 ? 1810 HIS A CE1   1 
ATOM   2854  N  NE2   . HIS A 1 1810 ? 163.706 250.346 239.890 1.00 11.52 ? 1810 HIS A NE2   1 
ATOM   2855  N  N     . LEU A 1 1811 ? 158.721 254.674 240.600 1.00 1.60  ? 1811 LEU A N     1 
ATOM   2856  C  CA    . LEU A 1 1811 ? 157.421 255.326 240.493 1.00 1.25  ? 1811 LEU A CA    1 
ATOM   2857  C  C     . LEU A 1 1811 ? 157.560 256.836 240.367 1.00 1.62  ? 1811 LEU A C     1 
ATOM   2858  O  O     . LEU A 1 1811 ? 156.816 257.471 239.611 1.00 3.19  ? 1811 LEU A O     1 
ATOM   2859  C  CB    . LEU A 1 1811 ? 156.559 254.969 241.702 1.00 1.34  ? 1811 LEU A CB    1 
ATOM   2860  C  CG    . LEU A 1 1811 ? 155.802 253.644 241.626 1.00 2.56  ? 1811 LEU A CG    1 
ATOM   2861  C  CD1   . LEU A 1 1811 ? 155.070 253.400 242.926 1.00 4.83  ? 1811 LEU A CD1   1 
ATOM   2862  C  CD2   . LEU A 1 1811 ? 154.837 253.639 240.454 1.00 1.68  ? 1811 LEU A CD2   1 
ATOM   2863  N  N     . ILE A 1 1812 ? 158.500 257.429 241.106 1.00 1.41  ? 1812 ILE A N     1 
ATOM   2864  C  CA    . ILE A 1 1812 ? 158.724 258.868 241.009 1.00 1.11  ? 1812 ILE A CA    1 
ATOM   2865  C  C     . ILE A 1 1812 ? 159.152 259.241 239.595 1.00 1.11  ? 1812 ILE A C     1 
ATOM   2866  O  O     . ILE A 1 1812 ? 158.665 260.221 239.021 1.00 1.25  ? 1812 ILE A O     1 
ATOM   2867  C  CB    . ILE A 1 1812 ? 159.758 259.320 242.055 1.00 1.64  ? 1812 ILE A CB    1 
ATOM   2868  C  CG1   . ILE A 1 1812 ? 159.130 259.352 243.449 1.00 2.70  ? 1812 ILE A CG1   1 
ATOM   2869  C  CG2   . ILE A 1 1812 ? 160.327 260.684 241.700 1.00 1.58  ? 1812 ILE A CG2   1 
ATOM   2870  C  CD1   . ILE A 1 1812 ? 160.125 259.565 244.566 1.00 2.56  ? 1812 ILE A CD1   1 
ATOM   2871  N  N     . THR A 1 1813 ? 160.058 258.455 239.009 1.00 1.18  ? 1813 THR A N     1 
ATOM   2872  C  CA    . THR A 1 1813 ? 160.509 258.729 237.650 1.00 0.96  ? 1813 THR A CA    1 
ATOM   2873  C  C     . THR A 1 1813 ? 159.364 258.608 236.653 1.00 1.12  ? 1813 THR A C     1 
ATOM   2874  O  O     . THR A 1 1813 ? 159.237 259.431 235.739 1.00 1.56  ? 1813 THR A O     1 
ATOM   2875  C  CB    . THR A 1 1813 ? 161.652 257.782 237.282 1.00 1.66  ? 1813 THR A CB    1 
ATOM   2876  O  OG1   . THR A 1 1813 ? 162.661 257.834 238.297 1.00 6.45  ? 1813 THR A OG1   1 
ATOM   2877  C  CG2   . THR A 1 1813 ? 162.270 258.174 235.950 1.00 1.09  ? 1813 THR A CG2   1 
ATOM   2878  N  N     . GLU A 1 1814 ? 158.517 257.590 236.815 1.00 1.65  ? 1814 GLU A N     1 
ATOM   2879  C  CA    . GLU A 1 1814 ? 157.380 257.416 235.919 1.00 1.53  ? 1814 GLU A CA    1 
ATOM   2880  C  C     . GLU A 1 1814 ? 156.376 258.555 236.058 1.00 1.66  ? 1814 GLU A C     1 
ATOM   2881  O  O     . GLU A 1 1814 ? 155.856 259.054 235.054 1.00 1.24  ? 1814 GLU A O     1 
ATOM   2882  C  CB    . GLU A 1 1814 ? 156.701 256.073 236.191 1.00 1.92  ? 1814 GLU A CB    1 
ATOM   2883  C  CG    . GLU A 1 1814 ? 155.591 255.729 235.213 1.00 1.84  ? 1814 GLU A CG    1 
ATOM   2884  C  CD    . GLU A 1 1814 ? 155.948 256.072 233.778 1.00 9.63  ? 1814 GLU A CD    1 
ATOM   2885  O  OE1   . GLU A 1 1814 ? 156.987 255.582 233.288 1.00 5.65  ? 1814 GLU A OE1   1 
ATOM   2886  O  OE2   . GLU A 1 1814 ? 155.188 256.828 233.140 1.00 15.45 ? 1814 GLU A OE2   1 
ATOM   2887  N  N     . LEU A 1 1815 ? 156.088 258.977 237.290 1.00 1.27  ? 1815 LEU A N     1 
ATOM   2888  C  CA    . LEU A 1 1815 ? 155.058 259.989 237.496 1.00 1.05  ? 1815 LEU A CA    1 
ATOM   2889  C  C     . LEU A 1 1815 ? 155.535 261.385 237.121 1.00 0.86  ? 1815 LEU A C     1 
ATOM   2890  O  O     . LEU A 1 1815 ? 154.722 262.217 236.702 1.00 0.96  ? 1815 LEU A O     1 
ATOM   2891  C  CB    . LEU A 1 1815 ? 154.573 259.966 238.941 1.00 0.98  ? 1815 LEU A CB    1 
ATOM   2892  C  CG    . LEU A 1 1815 ? 153.311 259.137 239.179 1.00 2.21  ? 1815 LEU A CG    1 
ATOM   2893  C  CD1   . LEU A 1 1815 ? 153.496 257.668 238.809 1.00 2.11  ? 1815 LEU A CD1   1 
ATOM   2894  C  CD2   . LEU A 1 1815 ? 152.878 259.282 240.611 1.00 3.02  ? 1815 LEU A CD2   1 
ATOM   2895  N  N     . VAL A 1 1816 ? 156.830 261.670 237.269 1.00 1.00  ? 1816 VAL A N     1 
ATOM   2896  C  CA    . VAL A 1 1816 ? 157.354 262.955 236.817 1.00 1.99  ? 1816 VAL A CA    1 
ATOM   2897  C  C     . VAL A 1 1816 ? 157.128 263.114 235.321 1.00 2.34  ? 1816 VAL A C     1 
ATOM   2898  O  O     . VAL A 1 1816 ? 156.769 264.197 234.842 1.00 3.57  ? 1816 VAL A O     1 
ATOM   2899  C  CB    . VAL A 1 1816 ? 158.842 263.090 237.196 1.00 1.98  ? 1816 VAL A CB    1 
ATOM   2900  C  CG1   . VAL A 1 1816 ? 159.514 264.172 236.370 1.00 3.54  ? 1816 VAL A CG1   1 
ATOM   2901  C  CG2   . VAL A 1 1816 ? 158.976 263.408 238.673 1.00 1.02  ? 1816 VAL A CG2   1 
ATOM   2902  N  N     . HIS A 1 1817 ? 157.315 262.034 234.561 1.00 1.14  ? 1817 HIS A N     1 
ATOM   2903  C  CA    . HIS A 1 1817 ? 157.017 262.076 233.134 1.00 0.78  ? 1817 HIS A CA    1 
ATOM   2904  C  C     . HIS A 1 1817 ? 155.523 262.235 232.878 1.00 0.97  ? 1817 HIS A C     1 
ATOM   2905  O  O     . HIS A 1 1817 ? 155.118 263.009 232.005 1.00 2.93  ? 1817 HIS A O     1 
ATOM   2906  C  CB    . HIS A 1 1817 ? 157.557 260.822 232.450 1.00 0.95  ? 1817 HIS A CB    1 
ATOM   2907  C  CG    . HIS A 1 1817 ? 157.184 260.720 231.006 1.00 0.96  ? 1817 HIS A CG    1 
ATOM   2908  N  ND1   . HIS A 1 1817 ? 157.752 261.513 230.034 1.00 1.27  ? 1817 HIS A ND1   1 
ATOM   2909  C  CD2   . HIS A 1 1817 ? 156.313 259.904 230.366 1.00 0.96  ? 1817 HIS A CD2   1 
ATOM   2910  C  CE1   . HIS A 1 1817 ? 157.238 261.200 228.859 1.00 1.81  ? 1817 HIS A CE1   1 
ATOM   2911  N  NE2   . HIS A 1 1817 ? 156.365 260.225 229.031 1.00 2.28  ? 1817 HIS A NE2   1 
ATOM   2912  N  N     . GLN A 1 1818 ? 154.685 261.509 233.625 1.00 1.09  ? 1818 GLN A N     1 
ATOM   2913  C  CA    . GLN A 1 1818 ? 153.242 261.652 233.459 1.00 0.66  ? 1818 GLN A CA    1 
ATOM   2914  C  C     . GLN A 1 1818 ? 152.785 263.056 233.830 1.00 1.57  ? 1818 GLN A C     1 
ATOM   2915  O  O     . GLN A 1 1818 ? 151.883 263.612 233.193 1.00 3.24  ? 1818 GLN A O     1 
ATOM   2916  C  CB    . GLN A 1 1818 ? 152.500 260.611 234.301 1.00 0.67  ? 1818 GLN A CB    1 
ATOM   2917  C  CG    . GLN A 1 1818 ? 152.732 259.176 233.877 1.00 1.39  ? 1818 GLN A CG    1 
ATOM   2918  C  CD    . GLN A 1 1818 ? 152.089 258.184 234.825 1.00 2.55  ? 1818 GLN A CD    1 
ATOM   2919  O  OE1   . GLN A 1 1818 ? 151.524 258.567 235.848 1.00 2.65  ? 1818 GLN A OE1   1 
ATOM   2920  N  NE2   . GLN A 1 1818 ? 152.168 256.904 234.489 1.00 1.89  ? 1818 GLN A NE2   1 
ATOM   2921  N  N     . ARG A 1 1819 ? 153.393 263.641 234.863 1.00 1.29  ? 1819 ARG A N     1 
ATOM   2922  C  CA    . ARG A 1 1819 ? 153.098 265.025 235.211 1.00 1.67  ? 1819 ARG A CA    1 
ATOM   2923  C  C     . ARG A 1 1819 ? 153.470 265.972 234.076 1.00 2.38  ? 1819 ARG A C     1 
ATOM   2924  O  O     . ARG A 1 1819 ? 152.719 266.902 233.764 1.00 2.08  ? 1819 ARG A O     1 
ATOM   2925  C  CB    . ARG A 1 1819 ? 153.841 265.406 236.489 1.00 4.06  ? 1819 ARG A CB    1 
ATOM   2926  C  CG    . ARG A 1 1819 ? 153.603 266.828 236.948 1.00 2.42  ? 1819 ARG A CG    1 
ATOM   2927  C  CD    . ARG A 1 1819 ? 154.595 267.219 238.018 1.00 2.98  ? 1819 ARG A CD    1 
ATOM   2928  N  NE    . ARG A 1 1819 ? 155.976 267.076 237.574 1.00 4.61  ? 1819 ARG A NE    1 
ATOM   2929  C  CZ    . ARG A 1 1819 ? 157.027 267.170 238.377 1.00 5.88  ? 1819 ARG A CZ    1 
ATOM   2930  N  NH1   . ARG A 1 1819 ? 156.886 267.390 239.675 1.00 3.55  ? 1819 ARG A NH1   1 
ATOM   2931  N  NH2   . ARG A 1 1819 ? 158.247 267.039 237.868 1.00 10.95 ? 1819 ARG A NH2   1 
ATOM   2932  N  N     . ASP A 1 1820 ? 154.628 265.748 233.452 1.00 3.03  ? 1820 ASP A N     1 
ATOM   2933  C  CA    . ASP A 1 1820 ? 155.068 266.613 232.364 1.00 1.86  ? 1820 ASP A CA    1 
ATOM   2934  C  C     . ASP A 1 1820 ? 154.182 266.457 231.133 1.00 3.14  ? 1820 ASP A C     1 
ATOM   2935  O  O     . ASP A 1 1820 ? 153.853 267.447 230.470 1.00 6.39  ? 1820 ASP A O     1 
ATOM   2936  C  CB    . ASP A 1 1820 ? 156.526 266.315 232.020 1.00 2.84  ? 1820 ASP A CB    1 
ATOM   2937  C  CG    . ASP A 1 1820 ? 157.493 266.909 233.025 1.00 18.99 ? 1820 ASP A CG    1 
ATOM   2938  O  OD1   . ASP A 1 1820 ? 157.063 267.759 233.834 1.00 14.57 ? 1820 ASP A OD1   1 
ATOM   2939  O  OD2   . ASP A 1 1820 ? 158.681 266.525 233.011 1.00 18.58 ? 1820 ASP A OD2   1 
ATOM   2940  N  N     . VAL A 1 1821 ? 153.795 265.223 230.807 1.00 2.17  ? 1821 VAL A N     1 
ATOM   2941  C  CA    . VAL A 1 1821 ? 152.936 264.995 229.650 1.00 3.15  ? 1821 VAL A CA    1 
ATOM   2942  C  C     . VAL A 1 1821 ? 151.557 265.600 229.879 1.00 2.36  ? 1821 VAL A C     1 
ATOM   2943  O  O     . VAL A 1 1821 ? 150.987 266.235 228.982 1.00 3.78  ? 1821 VAL A O     1 
ATOM   2944  C  CB    . VAL A 1 1821 ? 152.853 263.491 229.335 1.00 1.38  ? 1821 VAL A CB    1 
ATOM   2945  C  CG1   . VAL A 1 1821 ? 151.785 263.224 228.291 1.00 0.98  ? 1821 VAL A CG1   1 
ATOM   2946  C  CG2   . VAL A 1 1821 ? 154.200 262.979 228.863 1.00 0.83  ? 1821 VAL A CG2   1 
ATOM   2947  N  N     . THR A 1 1822 ? 150.999 265.418 231.076 1.00 1.85  ? 1822 THR A N     1 
ATOM   2948  C  CA    . THR A 1 1822 ? 149.680 265.967 231.368 1.00 2.75  ? 1822 THR A CA    1 
ATOM   2949  C  C     . THR A 1 1822 ? 149.707 267.490 231.350 1.00 4.43  ? 1822 THR A C     1 
ATOM   2950  O  O     . THR A 1 1822 ? 148.765 268.129 230.866 1.00 5.29  ? 1822 THR A O     1 
ATOM   2951  C  CB    . THR A 1 1822 ? 149.181 265.448 232.716 1.00 3.48  ? 1822 THR A CB    1 
ATOM   2952  O  OG1   . THR A 1 1822 ? 149.107 264.020 232.677 1.00 2.37  ? 1822 THR A OG1   1 
ATOM   2953  C  CG2   . THR A 1 1822 ? 147.794 265.991 233.011 1.00 3.59  ? 1822 THR A CG2   1 
ATOM   2954  N  N     . ARG A 1 1823 ? 150.781 268.090 231.869 1.00 4.29  ? 1823 ARG A N     1 
ATOM   2955  C  CA    . ARG A 1 1823 ? 150.927 269.540 231.801 1.00 3.32  ? 1823 ARG A CA    1 
ATOM   2956  C  C     . ARG A 1 1823 ? 151.010 270.016 230.356 1.00 4.90  ? 1823 ARG A C     1 
ATOM   2957  O  O     . ARG A 1 1823 ? 150.415 271.039 229.997 1.00 7.16  ? 1823 ARG A O     1 
ATOM   2958  C  CB    . ARG A 1 1823 ? 152.165 269.982 232.579 1.00 2.35  ? 1823 ARG A CB    1 
ATOM   2959  C  CG    . ARG A 1 1823 ? 151.937 270.165 234.065 1.00 2.35  ? 1823 ARG A CG    1 
ATOM   2960  C  CD    . ARG A 1 1823 ? 153.258 270.284 234.801 1.00 3.10  ? 1823 ARG A CD    1 
ATOM   2961  N  NE    . ARG A 1 1823 ? 153.070 270.571 236.216 1.00 4.73  ? 1823 ARG A NE    1 
ATOM   2962  C  CZ    . ARG A 1 1823 ? 154.042 270.565 237.117 1.00 6.95  ? 1823 ARG A CZ    1 
ATOM   2963  N  NH1   . ARG A 1 1823 ? 155.291 270.283 236.784 1.00 8.96  ? 1823 ARG A NH1   1 
ATOM   2964  N  NH2   . ARG A 1 1823 ? 153.755 270.846 238.384 1.00 7.45  ? 1823 ARG A NH2   1 
ATOM   2965  N  N     . SER A 1 1824 ? 151.747 269.288 229.516 1.00 3.47  ? 1824 SER A N     1 
ATOM   2966  C  CA    . SER A 1 1824 ? 151.827 269.639 228.102 1.00 4.42  ? 1824 SER A CA    1 
ATOM   2967  C  C     . SER A 1 1824 ? 150.465 269.521 227.427 1.00 7.58  ? 1824 SER A C     1 
ATOM   2968  O  O     . SER A 1 1824 ? 150.110 270.349 226.582 1.00 11.73 ? 1824 SER A O     1 
ATOM   2969  C  CB    . SER A 1 1824 ? 152.855 268.752 227.402 1.00 3.23  ? 1824 SER A CB    1 
ATOM   2970  O  OG    . SER A 1 1824 ? 152.937 269.048 226.022 1.00 9.74  ? 1824 SER A OG    1 
ATOM   2971  N  N     . LEU A 1 1825 ? 149.690 268.495 227.787 1.00 5.86  ? 1825 LEU A N     1 
ATOM   2972  C  CA    . LEU A 1 1825 ? 148.357 268.334 227.218 1.00 5.48  ? 1825 LEU A CA    1 
ATOM   2973  C  C     . LEU A 1 1825 ? 147.438 269.481 227.624 1.00 7.49  ? 1825 LEU A C     1 
ATOM   2974  O  O     . LEU A 1 1825 ? 146.648 269.971 226.810 1.00 14.42 ? 1825 LEU A O     1 
ATOM   2975  C  CB    . LEU A 1 1825 ? 147.762 266.994 227.649 1.00 6.90  ? 1825 LEU A CB    1 
ATOM   2976  C  CG    . LEU A 1 1825 ? 148.398 265.724 227.079 1.00 5.73  ? 1825 LEU A CG    1 
ATOM   2977  C  CD1   . LEU A 1 1825 ? 147.638 264.495 227.539 1.00 4.53  ? 1825 LEU A CD1   1 
ATOM   2978  C  CD2   . LEU A 1 1825 ? 148.469 265.776 225.562 1.00 4.29  ? 1825 LEU A CD2   1 
ATOM   2979  N  N     . ILE A 1 1826 ? 147.517 269.915 228.883 1.00 6.93  ? 1826 ILE A N     1 
ATOM   2980  C  CA    . ILE A 1 1826 ? 146.678 271.016 229.344 1.00 8.93  ? 1826 ILE A CA    1 
ATOM   2981  C  C     . ILE A 1 1826 ? 147.108 272.327 228.697 1.00 10.05 ? 1826 ILE A C     1 
ATOM   2982  O  O     . ILE A 1 1826 ? 146.269 273.135 228.285 1.00 14.34 ? 1826 ILE A O     1 
ATOM   2983  C  CB    . ILE A 1 1826 ? 146.711 271.102 230.882 1.00 5.49  ? 1826 ILE A CB    1 
ATOM   2984  C  CG1   . ILE A 1 1826 ? 146.097 269.846 231.498 1.00 8.76  ? 1826 ILE A CG1   1 
ATOM   2985  C  CG2   . ILE A 1 1826 ? 145.981 272.345 231.363 1.00 6.70  ? 1826 ILE A CG2   1 
ATOM   2986  C  CD1   . ILE A 1 1826 ? 146.258 269.760 233.000 1.00 8.85  ? 1826 ILE A CD1   1 
ATOM   2987  N  N     . LYS A 1 1827 ? 148.419 272.557 228.595 1.00 9.27  ? 1827 LYS A N     1 
ATOM   2988  C  CA    . LYS A 1 1827 ? 148.913 273.802 228.015 1.00 11.25 ? 1827 LYS A CA    1 
ATOM   2989  C  C     . LYS A 1 1827 ? 148.551 273.918 226.541 1.00 13.65 ? 1827 LYS A C     1 
ATOM   2990  O  O     . LYS A 1 1827 ? 148.340 275.026 226.037 1.00 26.04 ? 1827 LYS A O     1 
ATOM   2991  C  CB    . LYS A 1 1827 ? 150.427 273.899 228.208 1.00 11.68 ? 1827 LYS A CB    1 
ATOM   2992  C  CG    . LYS A 1 1827 ? 151.058 275.175 227.682 1.00 15.20 ? 1827 LYS A CG    1 
ATOM   2993  C  CD    . LYS A 1 1827 ? 152.562 275.166 227.893 1.00 19.01 ? 1827 LYS A CD    1 
ATOM   2994  C  CE    . LYS A 1 1827 ? 153.173 276.527 227.611 1.00 24.37 ? 1827 LYS A CE    1 
ATOM   2995  N  NZ    . LYS A 1 1827 ? 152.616 277.581 228.502 1.00 26.27 ? 1827 LYS A NZ    1 
ATOM   2996  N  N     . SER A 1 1828 ? 148.460 272.793 225.839 1.00 9.67  ? 1828 SER A N     1 
ATOM   2997  C  CA    . SER A 1 1828 ? 148.142 272.781 224.419 1.00 9.97  ? 1828 SER A CA    1 
ATOM   2998  C  C     . SER A 1 1828 ? 146.649 272.678 224.144 1.00 12.33 ? 1828 SER A C     1 
ATOM   2999  O  O     . SER A 1 1828 ? 146.256 272.600 222.975 1.00 13.57 ? 1828 SER A O     1 
ATOM   3000  C  CB    . SER A 1 1828 ? 148.874 271.631 223.727 1.00 12.06 ? 1828 SER A CB    1 
ATOM   3001  O  OG    . SER A 1 1828 ? 150.257 271.907 223.614 1.00 17.76 ? 1828 SER A OG    1 
ATOM   3002  N  N     . LYS A 1 1829 ? 145.816 272.669 225.186 1.00 12.57 ? 1829 LYS A N     1 
ATOM   3003  C  CA    . LYS A 1 1829 ? 144.359 272.663 225.050 1.00 13.56 ? 1829 LYS A CA    1 
ATOM   3004  C  C     . LYS A 1 1829 ? 143.873 271.484 224.209 1.00 13.48 ? 1829 LYS A C     1 
ATOM   3005  O  O     . LYS A 1 1829 ? 143.022 271.631 223.331 1.00 18.40 ? 1829 LYS A O     1 
ATOM   3006  C  CB    . LYS A 1 1829 ? 143.859 273.988 224.469 1.00 17.20 ? 1829 LYS A CB    1 
ATOM   3007  C  CG    . LYS A 1 1829 ? 144.176 275.197 225.330 1.00 17.40 ? 1829 LYS A CG    1 
ATOM   3008  C  CD    . LYS A 1 1829 ? 143.510 275.093 226.691 1.00 22.57 ? 1829 LYS A CD    1 
ATOM   3009  C  CE    . LYS A 1 1829 ? 141.998 275.176 226.576 1.00 25.41 ? 1829 LYS A CE    1 
ATOM   3010  N  NZ    . LYS A 1 1829 ? 141.555 276.504 226.071 1.00 25.49 ? 1829 LYS A NZ    1 
ATOM   3011  N  N     . ILE A 1 1830 ? 144.413 270.298 224.486 1.00 14.28 ? 1830 ILE A N     1 
ATOM   3012  C  CA    . ILE A 1 1830 ? 143.982 269.097 223.782 1.00 14.28 ? 1830 ILE A CA    1 
ATOM   3013  C  C     . ILE A 1 1830 ? 142.668 268.608 224.373 1.00 15.88 ? 1830 ILE A C     1 
ATOM   3014  O  O     . ILE A 1 1830 ? 142.549 268.400 225.588 1.00 28.09 ? 1830 ILE A O     1 
ATOM   3015  C  CB    . ILE A 1 1830 ? 145.065 268.012 223.853 1.00 11.75 ? 1830 ILE A CB    1 
ATOM   3016  C  CG1   . ILE A 1 1830 ? 146.360 268.528 223.226 1.00 11.39 ? 1830 ILE A CG1   1 
ATOM   3017  C  CG2   . ILE A 1 1830 ? 144.596 266.741 223.170 1.00 12.46 ? 1830 ILE A CG2   1 
ATOM   3018  C  CD1   . ILE A 1 1830 ? 146.212 268.893 221.771 1.00 17.42 ? 1830 ILE A CD1   1 
ATOM   3019  N  N     . ASP A 1 1831 ? 141.670 268.418 223.509 1.00 14.65 ? 1831 ASP A N     1 
ATOM   3020  C  CA    . ASP A 1 1831 ? 140.339 268.012 223.937 1.00 14.17 ? 1831 ASP A CA    1 
ATOM   3021  C  C     . ASP A 1 1831 ? 139.850 266.757 223.224 1.00 17.66 ? 1831 ASP A C     1 
ATOM   3022  O  O     . ASP A 1 1831 ? 138.709 266.336 223.451 1.00 18.17 ? 1831 ASP A O     1 
ATOM   3023  C  CB    . ASP A 1 1831 ? 139.342 269.155 223.727 1.00 19.15 ? 1831 ASP A CB    1 
ATOM   3024  C  CG    . ASP A 1 1831 ? 139.380 269.709 222.315 1.00 24.02 ? 1831 ASP A CG    1 
ATOM   3025  O  OD1   . ASP A 1 1831 ? 140.132 269.169 221.478 1.00 27.24 ? 1831 ASP A OD1   1 
ATOM   3026  O  OD2   . ASP A 1 1831 ? 138.661 270.690 222.041 1.00 30.63 ? 1831 ASP A OD2   1 
ATOM   3027  N  N     . ASN A 1 1832 ? 140.673 266.151 222.376 1.00 11.71 ? 1832 ASN A N     1 
ATOM   3028  C  CA    . ASN A 1 1832 ? 140.286 264.977 221.611 1.00 10.36 ? 1832 ASN A CA    1 
ATOM   3029  C  C     . ASN A 1 1832 ? 141.305 263.870 221.836 1.00 11.76 ? 1832 ASN A C     1 
ATOM   3030  O  O     . ASN A 1 1832 ? 142.513 264.117 221.844 1.00 10.05 ? 1832 ASN A O     1 
ATOM   3031  C  CB    . ASN A 1 1832 ? 140.178 265.314 220.116 1.00 10.08 ? 1832 ASN A CB    1 
ATOM   3032  C  CG    . ASN A 1 1832 ? 140.046 264.084 219.246 1.00 16.86 ? 1832 ASN A CG    1 
ATOM   3033  O  OD1   . ASN A 1 1832 ? 139.427 263.094 219.634 1.00 21.15 ? 1832 ASN A OD1   1 
ATOM   3034  N  ND2   . ASN A 1 1832 ? 140.626 264.144 218.053 1.00 22.79 ? 1832 ASN A ND2   1 
ATOM   3035  N  N     . ALA A 1 1833 ? 140.806 262.646 222.024 1.00 10.49 ? 1833 ALA A N     1 
ATOM   3036  C  CA    . ALA A 1 1833 ? 141.688 261.502 222.225 1.00 5.75  ? 1833 ALA A CA    1 
ATOM   3037  C  C     . ALA A 1 1833 ? 142.449 261.130 220.961 1.00 8.77  ? 1833 ALA A C     1 
ATOM   3038  O  O     . ALA A 1 1833 ? 143.491 260.471 221.054 1.00 7.74  ? 1833 ALA A O     1 
ATOM   3039  C  CB    . ALA A 1 1833 ? 140.889 260.297 222.719 1.00 9.91  ? 1833 ALA A CB    1 
ATOM   3040  N  N     . LYS A 1 1834 ? 141.963 261.536 219.793 1.00 10.01 ? 1834 LYS A N     1 
ATOM   3041  C  CA    . LYS A 1 1834 ? 142.623 261.240 218.529 1.00 9.38  ? 1834 LYS A CA    1 
ATOM   3042  C  C     . LYS A 1 1834 ? 143.622 262.314 218.121 1.00 8.27  ? 1834 LYS A C     1 
ATOM   3043  O  O     . LYS A 1 1834 ? 144.201 262.218 217.036 1.00 9.56  ? 1834 LYS A O     1 
ATOM   3044  C  CB    . LYS A 1 1834 ? 141.584 261.050 217.424 1.00 12.02 ? 1834 LYS A CB    1 
ATOM   3045  C  CG    . LYS A 1 1834 ? 140.788 259.760 217.537 1.00 10.81 ? 1834 LYS A CG    1 
ATOM   3046  C  CD    . LYS A 1 1834 ? 141.698 258.548 217.536 1.00 14.12 ? 1834 LYS A CD    1 
ATOM   3047  C  CE    . LYS A 1 1834 ? 141.051 257.373 218.255 1.00 18.17 ? 1834 LYS A CE    1 
ATOM   3048  N  NZ    . LYS A 1 1834 ? 141.110 257.524 219.737 1.00 17.47 ? 1834 LYS A NZ    1 
ATOM   3049  N  N     . SER A 1 1835 ? 143.825 263.330 218.955 1.00 7.91  ? 1835 SER A N     1 
ATOM   3050  C  CA    . SER A 1 1835 ? 144.854 264.324 218.690 1.00 5.86  ? 1835 SER A CA    1 
ATOM   3051  C  C     . SER A 1 1835 ? 146.229 263.676 218.724 1.00 5.75  ? 1835 SER A C     1 
ATOM   3052  O  O     . SER A 1 1835 ? 146.494 262.785 219.536 1.00 9.82  ? 1835 SER A O     1 
ATOM   3053  C  CB    . SER A 1 1835 ? 144.780 265.452 219.716 1.00 8.25  ? 1835 SER A CB    1 
ATOM   3054  O  OG    . SER A 1 1835 ? 145.881 266.333 219.586 1.00 18.09 ? 1835 SER A OG    1 
ATOM   3055  N  N     . PHE A 1 1836 ? 147.112 264.124 217.829 1.00 5.33  ? 1836 PHE A N     1 
ATOM   3056  C  CA    . PHE A 1 1836 ? 148.417 263.490 217.720 1.00 3.41  ? 1836 PHE A CA    1 
ATOM   3057  C  C     . PHE A 1 1836 ? 149.301 263.746 218.930 1.00 2.95  ? 1836 PHE A C     1 
ATOM   3058  O  O     . PHE A 1 1836 ? 150.151 262.907 219.243 1.00 2.55  ? 1836 PHE A O     1 
ATOM   3059  C  CB    . PHE A 1 1836 ? 149.137 263.946 216.454 1.00 1.70  ? 1836 PHE A CB    1 
ATOM   3060  C  CG    . PHE A 1 1836 ? 150.342 263.123 216.131 1.00 1.26  ? 1836 PHE A CG    1 
ATOM   3061  C  CD1   . PHE A 1 1836 ? 150.206 261.810 215.713 1.00 1.37  ? 1836 PHE A CD1   1 
ATOM   3062  C  CD2   . PHE A 1 1836 ? 151.613 263.646 216.267 1.00 0.67  ? 1836 PHE A CD2   1 
ATOM   3063  C  CE1   . PHE A 1 1836 ? 151.312 261.043 215.425 1.00 1.25  ? 1836 PHE A CE1   1 
ATOM   3064  C  CE2   . PHE A 1 1836 ? 152.723 262.882 215.980 1.00 0.60  ? 1836 PHE A CE2   1 
ATOM   3065  C  CZ    . PHE A 1 1836 ? 152.574 261.583 215.558 1.00 0.80  ? 1836 PHE A CZ    1 
ATOM   3066  N  N     . GLU A 1 1837 ? 149.130 264.878 219.618 1.00 5.61  ? 1837 GLU A N     1 
ATOM   3067  C  CA    . GLU A 1 1837 ? 149.944 265.136 220.800 1.00 6.29  ? 1837 GLU A CA    1 
ATOM   3068  C  C     . GLU A 1 1837 ? 149.642 264.145 221.916 1.00 3.36  ? 1837 GLU A C     1 
ATOM   3069  O  O     . GLU A 1 1837 ? 150.460 263.968 222.824 1.00 6.01  ? 1837 GLU A O     1 
ATOM   3070  C  CB    . GLU A 1 1837 ? 149.749 266.574 221.277 1.00 7.14  ? 1837 GLU A CB    1 
ATOM   3071  C  CG    . GLU A 1 1837 ? 150.291 267.605 220.304 1.00 12.13 ? 1837 GLU A CG    1 
ATOM   3072  C  CD    . GLU A 1 1837 ? 150.079 269.025 220.775 1.00 27.37 ? 1837 GLU A CD    1 
ATOM   3073  O  OE1   . GLU A 1 1837 ? 149.397 269.213 221.802 1.00 30.75 ? 1837 GLU A OE1   1 
ATOM   3074  O  OE2   . GLU A 1 1837 ? 150.593 269.953 220.119 1.00 28.26 ? 1837 GLU A OE2   1 
ATOM   3075  N  N     . TRP A 1 1838 ? 148.482 263.492 221.868 1.00 3.13  ? 1838 TRP A N     1 
ATOM   3076  C  CA    . TRP A 1 1838 ? 148.211 262.366 222.753 1.00 2.07  ? 1838 TRP A CA    1 
ATOM   3077  C  C     . TRP A 1 1838 ? 148.611 261.036 222.124 1.00 2.34  ? 1838 TRP A C     1 
ATOM   3078  O  O     . TRP A 1 1838 ? 149.142 260.162 222.817 1.00 2.56  ? 1838 TRP A O     1 
ATOM   3079  C  CB    . TRP A 1 1838 ? 146.730 262.335 223.136 1.00 1.90  ? 1838 TRP A CB    1 
ATOM   3080  C  CG    . TRP A 1 1838 ? 146.341 261.149 223.977 1.00 1.51  ? 1838 TRP A CG    1 
ATOM   3081  C  CD1   . TRP A 1 1838 ? 145.318 260.280 223.738 1.00 1.58  ? 1838 TRP A CD1   1 
ATOM   3082  C  CD2   . TRP A 1 1838 ? 146.959 260.713 225.197 1.00 1.42  ? 1838 TRP A CD2   1 
ATOM   3083  N  NE1   . TRP A 1 1838 ? 145.265 259.329 224.722 1.00 1.49  ? 1838 TRP A NE1   1 
ATOM   3084  C  CE2   . TRP A 1 1838 ? 146.259 259.571 225.633 1.00 1.68  ? 1838 TRP A CE2   1 
ATOM   3085  C  CE3   . TRP A 1 1838 ? 148.036 261.173 225.962 1.00 1.04  ? 1838 TRP A CE3   1 
ATOM   3086  C  CZ2   . TRP A 1 1838 ? 146.602 258.882 226.794 1.00 1.44  ? 1838 TRP A CZ2   1 
ATOM   3087  C  CZ3   . TRP A 1 1838 ? 148.372 260.490 227.112 1.00 0.90  ? 1838 TRP A CZ3   1 
ATOM   3088  C  CH2   . TRP A 1 1838 ? 147.658 259.357 227.518 1.00 1.12  ? 1838 TRP A CH2   1 
ATOM   3089  N  N     . LEU A 1 1839 ? 148.370 260.867 220.823 1.00 2.11  ? 1839 LEU A N     1 
ATOM   3090  C  CA    . LEU A 1 1839 ? 148.738 259.621 220.157 1.00 1.06  ? 1839 LEU A CA    1 
ATOM   3091  C  C     . LEU A 1 1839 ? 150.249 259.433 220.123 1.00 0.79  ? 1839 LEU A C     1 
ATOM   3092  O  O     . LEU A 1 1839 ? 150.738 258.301 220.215 1.00 3.16  ? 1839 LEU A O     1 
ATOM   3093  C  CB    . LEU A 1 1839 ? 148.165 259.586 218.741 1.00 2.00  ? 1839 LEU A CB    1 
ATOM   3094  C  CG    . LEU A 1 1839 ? 146.645 259.520 218.604 1.00 1.91  ? 1839 LEU A CG    1 
ATOM   3095  C  CD1   . LEU A 1 1839 ? 146.253 259.573 217.141 1.00 1.91  ? 1839 LEU A CD1   1 
ATOM   3096  C  CD2   . LEU A 1 1839 ? 146.089 258.270 219.267 1.00 1.57  ? 1839 LEU A CD2   1 
ATOM   3097  N  N     . SER A 1 1840 ? 151.003 260.525 219.988 1.00 1.00  ? 1840 SER A N     1 
ATOM   3098  C  CA    . SER A 1 1840 ? 152.458 260.431 220.000 1.00 0.96  ? 1840 SER A CA    1 
ATOM   3099  C  C     . SER A 1 1840 ? 152.999 259.969 221.346 1.00 1.17  ? 1840 SER A C     1 
ATOM   3100  O  O     . SER A 1 1840 ? 154.112 259.439 221.403 1.00 1.77  ? 1840 SER A O     1 
ATOM   3101  C  CB    . SER A 1 1840 ? 153.074 261.778 219.622 1.00 0.95  ? 1840 SER A CB    1 
ATOM   3102  O  OG    . SER A 1 1840 ? 152.630 262.803 220.493 1.00 2.33  ? 1840 SER A OG    1 
ATOM   3103  N  N     . GLN A 1 1841 ? 152.244 260.163 222.425 1.00 0.92  ? 1841 GLN A N     1 
ATOM   3104  C  CA    . GLN A 1 1841 ? 152.641 259.649 223.726 1.00 0.82  ? 1841 GLN A CA    1 
ATOM   3105  C  C     . GLN A 1 1841 ? 152.513 258.131 223.768 1.00 0.65  ? 1841 GLN A C     1 
ATOM   3106  O  O     . GLN A 1 1841 ? 151.689 257.536 223.069 1.00 0.81  ? 1841 GLN A O     1 
ATOM   3107  C  CB    . GLN A 1 1841 ? 151.785 260.270 224.831 1.00 0.80  ? 1841 GLN A CB    1 
ATOM   3108  C  CG    . GLN A 1 1841 ? 151.805 261.783 224.866 1.00 1.09  ? 1841 GLN A CG    1 
ATOM   3109  C  CD    . GLN A 1 1841 ? 153.208 262.350 224.849 1.00 1.17  ? 1841 GLN A CD    1 
ATOM   3110  O  OE1   . GLN A 1 1841 ? 154.037 262.004 225.687 1.00 3.71  ? 1841 GLN A OE1   1 
ATOM   3111  N  NE2   . GLN A 1 1841 ? 153.479 263.227 223.896 1.00 2.23  ? 1841 GLN A NE2   1 
ATOM   3112  N  N     . MET A 1 1842 ? 153.341 257.504 224.597 1.00 0.53  ? 1842 MET A N     1 
ATOM   3113  C  CA    . MET A 1 1842 ? 153.251 256.067 224.816 1.00 0.39  ? 1842 MET A CA    1 
ATOM   3114  C  C     . MET A 1 1842 ? 152.080 255.777 225.746 1.00 0.25  ? 1842 MET A C     1 
ATOM   3115  O  O     . MET A 1 1842 ? 152.064 256.232 226.895 1.00 0.40  ? 1842 MET A O     1 
ATOM   3116  C  CB    . MET A 1 1842 ? 154.554 255.531 225.399 1.00 0.33  ? 1842 MET A CB    1 
ATOM   3117  C  CG    . MET A 1 1842 ? 154.544 254.035 225.645 1.00 0.44  ? 1842 MET A CG    1 
ATOM   3118  S  SD    . MET A 1 1842 ? 156.197 253.324 225.656 1.00 7.95  ? 1842 MET A SD    1 
ATOM   3119  C  CE    . MET A 1 1842 ? 156.478 253.089 223.908 1.00 0.14  ? 1842 MET A CE    1 
ATOM   3120  N  N     . ARG A 1 1843 ? 151.101 255.031 225.251 1.00 0.35  ? 1843 ARG A N     1 
ATOM   3121  C  CA    . ARG A 1 1843 ? 149.861 254.784 225.966 1.00 0.35  ? 1843 ARG A CA    1 
ATOM   3122  C  C     . ARG A 1 1843 ? 149.735 253.307 226.316 1.00 0.25  ? 1843 ARG A C     1 
ATOM   3123  O  O     . ARG A 1 1843 ? 150.387 252.444 225.723 1.00 0.45  ? 1843 ARG A O     1 
ATOM   3124  C  CB    . ARG A 1 1843 ? 148.660 255.251 225.138 1.00 0.90  ? 1843 ARG A CB    1 
ATOM   3125  C  CG    . ARG A 1 1843 ? 148.857 256.633 224.532 1.00 1.11  ? 1843 ARG A CG    1 
ATOM   3126  C  CD    . ARG A 1 1843 ? 147.636 257.111 223.769 1.00 3.31  ? 1843 ARG A CD    1 
ATOM   3127  N  NE    . ARG A 1 1843 ? 147.195 256.166 222.749 1.00 4.30  ? 1843 ARG A NE    1 
ATOM   3128  C  CZ    . ARG A 1 1843 ? 147.831 255.928 221.611 1.00 1.73  ? 1843 ARG A CZ    1 
ATOM   3129  N  NH1   . ARG A 1 1843 ? 148.947 256.563 221.295 1.00 0.53  ? 1843 ARG A NH1   1 
ATOM   3130  N  NH2   . ARG A 1 1843 ? 147.333 255.033 220.766 1.00 6.16  ? 1843 ARG A NH2   1 
ATOM   3131  N  N     . PHE A 1 1844 ? 148.897 253.028 227.311 1.00 0.60  ? 1844 PHE A N     1 
ATOM   3132  C  CA    . PHE A 1 1844 ? 148.766 251.694 227.887 1.00 0.54  ? 1844 PHE A CA    1 
ATOM   3133  C  C     . PHE A 1 1844 ? 147.289 251.386 228.073 1.00 0.65  ? 1844 PHE A C     1 
ATOM   3134  O  O     . PHE A 1 1844 ? 146.634 251.965 228.944 1.00 1.21  ? 1844 PHE A O     1 
ATOM   3135  C  CB    . PHE A 1 1844 ? 149.516 251.592 229.218 1.00 0.36  ? 1844 PHE A CB    1 
ATOM   3136  C  CG    . PHE A 1 1844 ? 150.966 251.963 229.123 1.00 0.21  ? 1844 PHE A CG    1 
ATOM   3137  C  CD1   . PHE A 1 1844 ? 151.364 253.291 229.172 1.00 0.33  ? 1844 PHE A CD1   1 
ATOM   3138  C  CD2   . PHE A 1 1844 ? 151.931 250.988 228.977 1.00 0.14  ? 1844 PHE A CD2   1 
ATOM   3139  C  CE1   . PHE A 1 1844 ? 152.696 253.631 229.075 1.00 0.34  ? 1844 PHE A CE1   1 
ATOM   3140  C  CE2   . PHE A 1 1844 ? 153.262 251.323 228.881 1.00 0.27  ? 1844 PHE A CE2   1 
ATOM   3141  C  CZ    . PHE A 1 1844 ? 153.646 252.646 228.933 1.00 0.23  ? 1844 PHE A CZ    1 
ATOM   3142  N  N     . TYR A 1 1845 ? 146.769 250.472 227.258 1.00 0.80  ? 1845 TYR A N     1 
ATOM   3143  C  CA    . TYR A 1 1845 ? 145.371 250.068 227.306 1.00 1.88  ? 1845 TYR A CA    1 
ATOM   3144  C  C     . TYR A 1 1845 ? 145.278 248.654 227.857 1.00 2.09  ? 1845 TYR A C     1 
ATOM   3145  O  O     . TYR A 1 1845 ? 145.993 247.756 227.402 1.00 1.20  ? 1845 TYR A O     1 
ATOM   3146  C  CB    . TYR A 1 1845 ? 144.730 250.146 225.920 1.00 1.27  ? 1845 TYR A CB    1 
ATOM   3147  C  CG    . TYR A 1 1845 ? 144.801 251.522 225.307 1.00 5.55  ? 1845 TYR A CG    1 
ATOM   3148  C  CD1   . TYR A 1 1845 ? 145.914 251.923 224.581 1.00 3.88  ? 1845 TYR A CD1   1 
ATOM   3149  C  CD2   . TYR A 1 1845 ? 143.759 252.425 225.463 1.00 5.52  ? 1845 TYR A CD2   1 
ATOM   3150  C  CE1   . TYR A 1 1845 ? 145.984 253.181 224.025 1.00 3.21  ? 1845 TYR A CE1   1 
ATOM   3151  C  CE2   . TYR A 1 1845 ? 143.821 253.684 224.910 1.00 4.27  ? 1845 TYR A CE2   1 
ATOM   3152  C  CZ    . TYR A 1 1845 ? 144.937 254.057 224.193 1.00 5.26  ? 1845 TYR A CZ    1 
ATOM   3153  O  OH    . TYR A 1 1845 ? 145.000 255.313 223.640 1.00 8.64  ? 1845 TYR A OH    1 
ATOM   3154  N  N     . PHE A 1 1846 ? 144.401 248.461 228.835 1.00 2.42  ? 1846 PHE A N     1 
ATOM   3155  C  CA    . PHE A 1 1846 ? 144.230 247.180 229.502 1.00 2.93  ? 1846 PHE A CA    1 
ATOM   3156  C  C     . PHE A 1 1846 ? 142.784 246.734 229.338 1.00 6.37  ? 1846 PHE A C     1 
ATOM   3157  O  O     . PHE A 1 1846 ? 141.859 247.465 229.704 1.00 11.03 ? 1846 PHE A O     1 
ATOM   3158  C  CB    . PHE A 1 1846 ? 144.610 247.287 230.980 1.00 5.37  ? 1846 PHE A CB    1 
ATOM   3159  C  CG    . PHE A 1 1846 ? 144.539 245.987 231.725 1.00 5.86  ? 1846 PHE A CG    1 
ATOM   3160  C  CD1   . PHE A 1 1846 ? 145.638 245.147 231.777 1.00 4.14  ? 1846 PHE A CD1   1 
ATOM   3161  C  CD2   . PHE A 1 1846 ? 143.385 245.614 232.389 1.00 7.15  ? 1846 PHE A CD2   1 
ATOM   3162  C  CE1   . PHE A 1 1846 ? 145.581 243.956 232.466 1.00 5.08  ? 1846 PHE A CE1   1 
ATOM   3163  C  CE2   . PHE A 1 1846 ? 143.323 244.424 233.081 1.00 9.00  ? 1846 PHE A CE2   1 
ATOM   3164  C  CZ    . PHE A 1 1846 ? 144.423 243.596 233.118 1.00 7.51  ? 1846 PHE A CZ    1 
ATOM   3165  N  N     . ASP A 1 1847 ? 142.591 245.537 228.789 1.00 10.09 ? 1847 ASP A N     1 
ATOM   3166  C  CA    . ASP A 1 1847 ? 141.257 244.971 228.616 1.00 11.44 ? 1847 ASP A CA    1 
ATOM   3167  C  C     . ASP A 1 1847 ? 141.100 243.786 229.557 1.00 15.94 ? 1847 ASP A C     1 
ATOM   3168  O  O     . ASP A 1 1847 ? 141.625 242.697 229.278 1.00 18.69 ? 1847 ASP A O     1 
ATOM   3169  C  CB    . ASP A 1 1847 ? 141.034 244.539 227.163 1.00 9.03  ? 1847 ASP A CB    1 
ATOM   3170  C  CG    . ASP A 1 1847 ? 139.643 243.975 226.924 1.00 19.23 ? 1847 ASP A CG    1 
ATOM   3171  O  OD1   . ASP A 1 1847 ? 138.789 244.057 227.831 1.00 20.38 ? 1847 ASP A OD1   1 
ATOM   3172  O  OD2   . ASP A 1 1847 ? 139.401 243.441 225.822 1.00 29.45 ? 1847 ASP A OD2   1 
ATOM   3173  N  N     . PRO A 1 1848 ? 140.400 243.942 230.683 1.00 15.62 ? 1848 PRO A N     1 
ATOM   3174  C  CA    . PRO A 1 1848 ? 140.178 242.794 231.573 1.00 16.66 ? 1848 PRO A CA    1 
ATOM   3175  C  C     . PRO A 1 1848 ? 139.305 241.710 230.963 1.00 18.44 ? 1848 PRO A C     1 
ATOM   3176  O  O     . PRO A 1 1848 ? 139.364 240.565 231.421 1.00 25.89 ? 1848 PRO A O     1 
ATOM   3177  C  CB    . PRO A 1 1848 ? 139.507 243.432 232.796 1.00 16.22 ? 1848 PRO A CB    1 
ATOM   3178  C  CG    . PRO A 1 1848 ? 138.799 244.618 232.229 1.00 12.56 ? 1848 PRO A CG    1 
ATOM   3179  C  CD    . PRO A 1 1848 ? 139.749 245.161 231.193 1.00 12.01 ? 1848 PRO A CD    1 
ATOM   3180  N  N     . LYS A 1 1849 ? 138.501 242.035 229.951 1.00 19.46 ? 1849 LYS A N     1 
ATOM   3181  C  CA    . LYS A 1 1849 ? 137.602 241.065 229.341 1.00 18.49 ? 1849 LYS A CA    1 
ATOM   3182  C  C     . LYS A 1 1849 ? 138.300 240.153 228.342 1.00 18.36 ? 1849 LYS A C     1 
ATOM   3183  O  O     . LYS A 1 1849 ? 137.687 239.181 227.887 1.00 22.58 ? 1849 LYS A O     1 
ATOM   3184  C  CB    . LYS A 1 1849 ? 136.444 241.790 228.649 1.00 23.29 ? 1849 LYS A CB    1 
ATOM   3185  C  CG    . LYS A 1 1849 ? 135.486 242.477 229.605 1.00 23.84 ? 1849 LYS A CG    1 
ATOM   3186  C  CD    . LYS A 1 1849 ? 134.404 243.237 228.855 1.00 28.39 ? 1849 LYS A CD    1 
ATOM   3187  C  CE    . LYS A 1 1849 ? 133.428 242.287 228.182 1.00 30.91 ? 1849 LYS A CE    1 
ATOM   3188  N  NZ    . LYS A 1 1849 ? 132.615 241.534 229.177 1.00 32.11 ? 1849 LYS A NZ    1 
ATOM   3189  N  N     . GLN A 1 1850 ? 139.551 240.442 227.991 1.00 19.23 ? 1850 GLN A N     1 
ATOM   3190  C  CA    . GLN A 1 1850 ? 140.277 239.619 227.034 1.00 16.59 ? 1850 GLN A CA    1 
ATOM   3191  C  C     . GLN A 1 1850 ? 140.513 238.227 227.611 1.00 18.17 ? 1850 GLN A C     1 
ATOM   3192  O  O     . GLN A 1 1850 ? 140.908 238.083 228.771 1.00 18.24 ? 1850 GLN A O     1 
ATOM   3193  C  CB    . GLN A 1 1850 ? 141.603 240.293 226.680 1.00 18.49 ? 1850 GLN A CB    1 
ATOM   3194  C  CG    . GLN A 1 1850 ? 142.586 239.431 225.917 1.00 15.20 ? 1850 GLN A CG    1 
ATOM   3195  C  CD    . GLN A 1 1850 ? 142.127 239.133 224.505 1.00 17.90 ? 1850 GLN A CD    1 
ATOM   3196  O  OE1   . GLN A 1 1850 ? 141.591 238.063 224.231 1.00 26.19 ? 1850 GLN A OE1   1 
ATOM   3197  N  NE2   . GLN A 1 1850 ? 142.327 240.087 223.603 1.00 15.40 ? 1850 GLN A NE2   1 
ATOM   3198  N  N     . THR A 1 1851 ? 140.258 237.200 226.796 1.00 21.34 ? 1851 THR A N     1 
ATOM   3199  C  CA    . THR A 1 1851 ? 140.359 235.826 227.283 1.00 16.84 ? 1851 THR A CA    1 
ATOM   3200  C  C     . THR A 1 1851 ? 141.809 235.424 227.530 1.00 21.27 ? 1851 THR A C     1 
ATOM   3201  O  O     . THR A 1 1851 ? 142.121 234.803 228.553 1.00 22.79 ? 1851 THR A O     1 
ATOM   3202  C  CB    . THR A 1 1851 ? 139.703 234.866 226.292 1.00 20.70 ? 1851 THR A CB    1 
ATOM   3203  O  OG1   . THR A 1 1851 ? 140.569 234.674 225.167 1.00 28.68 ? 1851 THR A OG1   1 
ATOM   3204  C  CG2   . THR A 1 1851 ? 138.375 235.429 225.808 1.00 19.70 ? 1851 THR A CG2   1 
ATOM   3205  N  N     . ASP A 1 1852 ? 142.705 235.761 226.608 1.00 21.01 ? 1852 ASP A N     1 
ATOM   3206  C  CA    . ASP A 1 1852 ? 144.119 235.438 226.761 1.00 14.10 ? 1852 ASP A CA    1 
ATOM   3207  C  C     . ASP A 1 1852 ? 144.769 236.469 227.678 1.00 16.09 ? 1852 ASP A C     1 
ATOM   3208  O  O     . ASP A 1 1852 ? 144.764 237.666 227.375 1.00 16.59 ? 1852 ASP A O     1 
ATOM   3209  C  CB    . ASP A 1 1852 ? 144.808 235.406 225.400 1.00 10.57 ? 1852 ASP A CB    1 
ATOM   3210  C  CG    . ASP A 1 1852 ? 146.256 234.947 225.482 1.00 20.30 ? 1852 ASP A CG    1 
ATOM   3211  O  OD1   . ASP A 1 1852 ? 146.711 234.567 226.582 1.00 23.53 ? 1852 ASP A OD1   1 
ATOM   3212  O  OD2   . ASP A 1 1852 ? 146.943 234.968 224.440 1.00 17.09 ? 1852 ASP A OD2   1 
ATOM   3213  N  N     . VAL A 1 1853 ? 145.326 236.004 228.797 1.00 11.92 ? 1853 VAL A N     1 
ATOM   3214  C  CA    . VAL A 1 1853 ? 145.931 236.922 229.760 1.00 9.66  ? 1853 VAL A CA    1 
ATOM   3215  C  C     . VAL A 1 1853 ? 147.151 237.609 229.166 1.00 9.24  ? 1853 VAL A C     1 
ATOM   3216  O  O     . VAL A 1 1853 ? 147.496 238.729 229.561 1.00 13.75 ? 1853 VAL A O     1 
ATOM   3217  C  CB    . VAL A 1 1853 ? 146.280 236.179 231.063 1.00 11.20 ? 1853 VAL A CB    1 
ATOM   3218  C  CG1   . VAL A 1 1853 ? 145.016 235.845 231.833 1.00 9.75  ? 1853 VAL A CG1   1 
ATOM   3219  C  CG2   . VAL A 1 1853 ? 147.082 234.920 230.768 1.00 10.33 ? 1853 VAL A CG2   1 
ATOM   3220  N  N     . LEU A 1 1854 ? 147.819 236.966 228.209 1.00 8.13  ? 1854 LEU A N     1 
ATOM   3221  C  CA    . LEU A 1 1854 ? 149.018 237.531 227.607 1.00 6.96  ? 1854 LEU A CA    1 
ATOM   3222  C  C     . LEU A 1 1854 ? 148.728 238.672 226.642 1.00 8.12  ? 1854 LEU A C     1 
ATOM   3223  O  O     . LEU A 1 1854 ? 149.667 239.344 226.209 1.00 9.37  ? 1854 LEU A O     1 
ATOM   3224  C  CB    . LEU A 1 1854 ? 149.803 236.437 226.882 1.00 7.19  ? 1854 LEU A CB    1 
ATOM   3225  C  CG    . LEU A 1 1854 ? 150.453 235.378 227.774 1.00 6.21  ? 1854 LEU A CG    1 
ATOM   3226  C  CD1   . LEU A 1 1854 ? 151.352 234.473 226.958 1.00 3.50  ? 1854 LEU A CD1   1 
ATOM   3227  C  CD2   . LEU A 1 1854 ? 151.230 236.031 228.909 1.00 3.04  ? 1854 LEU A CD2   1 
ATOM   3228  N  N     . GLN A 1 1855 ? 147.460 238.909 226.297 1.00 9.55  ? 1855 GLN A N     1 
ATOM   3229  C  CA    . GLN A 1 1855 ? 147.096 239.965 225.358 1.00 4.85  ? 1855 GLN A CA    1 
ATOM   3230  C  C     . GLN A 1 1855 ? 146.149 240.989 225.975 1.00 5.99  ? 1855 GLN A C     1 
ATOM   3231  O  O     . GLN A 1 1855 ? 145.518 241.760 225.246 1.00 9.99  ? 1855 GLN A O     1 
ATOM   3232  C  CB    . GLN A 1 1855 ? 146.477 239.368 224.094 1.00 6.81  ? 1855 GLN A CB    1 
ATOM   3233  C  CG    . GLN A 1 1855 ? 147.415 238.474 223.298 1.00 5.71  ? 1855 GLN A CG    1 
ATOM   3234  C  CD    . GLN A 1 1855 ? 148.654 239.205 222.818 1.00 11.73 ? 1855 GLN A CD    1 
ATOM   3235  O  OE1   . GLN A 1 1855 ? 148.578 240.344 222.360 1.00 17.39 ? 1855 GLN A OE1   1 
ATOM   3236  N  NE2   . GLN A 1 1855 ? 149.805 238.551 222.926 1.00 14.36 ? 1855 GLN A NE2   1 
ATOM   3237  N  N     . GLN A 1 1856 ? 146.037 241.018 227.305 1.00 4.79  ? 1856 GLN A N     1 
ATOM   3238  C  CA    . GLN A 1 1856 ? 145.169 242.003 227.943 1.00 5.53  ? 1856 GLN A CA    1 
ATOM   3239  C  C     . GLN A 1 1856 ? 145.778 243.399 227.915 1.00 4.47  ? 1856 GLN A C     1 
ATOM   3240  O  O     . GLN A 1 1856 ? 145.045 244.392 227.922 1.00 5.84  ? 1856 GLN A O     1 
ATOM   3241  C  CB    . GLN A 1 1856 ? 144.864 241.595 229.383 1.00 8.26  ? 1856 GLN A CB    1 
ATOM   3242  C  CG    . GLN A 1 1856 ? 144.318 240.189 229.534 1.00 9.33  ? 1856 GLN A CG    1 
ATOM   3243  C  CD    . GLN A 1 1856 ? 143.545 239.999 230.823 1.00 14.22 ? 1856 GLN A CD    1 
ATOM   3244  O  OE1   . GLN A 1 1856 ? 144.031 240.316 231.908 1.00 17.79 ? 1856 GLN A OE1   1 
ATOM   3245  N  NE2   . GLN A 1 1856 ? 142.331 239.475 230.711 1.00 20.48 ? 1856 GLN A NE2   1 
ATOM   3246  N  N     . LEU A 1 1857 ? 147.101 243.494 227.875 1.00 3.21  ? 1857 LEU A N     1 
ATOM   3247  C  CA    . LEU A 1 1857 ? 147.791 244.775 227.884 1.00 0.91  ? 1857 LEU A CA    1 
ATOM   3248  C  C     . LEU A 1 1857 ? 148.274 245.113 226.482 1.00 1.05  ? 1857 LEU A C     1 
ATOM   3249  O  O     . LEU A 1 1857 ? 148.968 244.314 225.847 1.00 1.47  ? 1857 LEU A O     1 
ATOM   3250  C  CB    . LEU A 1 1857 ? 148.971 244.753 228.856 1.00 0.87  ? 1857 LEU A CB    1 
ATOM   3251  C  CG    . LEU A 1 1857 ? 149.843 246.008 228.828 1.00 0.69  ? 1857 LEU A CG    1 
ATOM   3252  C  CD1   . LEU A 1 1857 ? 149.021 247.233 229.193 1.00 0.60  ? 1857 LEU A CD1   1 
ATOM   3253  C  CD2   . LEU A 1 1857 ? 151.029 245.856 229.757 1.00 0.59  ? 1857 LEU A CD2   1 
ATOM   3254  N  N     . SER A 1 1858 ? 147.904 246.297 226.007 1.00 1.37  ? 1858 SER A N     1 
ATOM   3255  C  CA    . SER A 1 1858 ? 148.347 246.808 224.719 1.00 0.76  ? 1858 SER A CA    1 
ATOM   3256  C  C     . SER A 1 1858 ? 149.071 248.129 224.934 1.00 0.58  ? 1858 SER A C     1 
ATOM   3257  O  O     . SER A 1 1858 ? 148.538 249.035 225.581 1.00 0.78  ? 1858 SER A O     1 
ATOM   3258  C  CB    . SER A 1 1858 ? 147.162 246.992 223.764 1.00 1.02  ? 1858 SER A CB    1 
ATOM   3259  O  OG    . SER A 1 1858 ? 147.595 247.442 222.493 1.00 7.58  ? 1858 SER A OG    1 
ATOM   3260  N  N     . ILE A 1 1859 ? 150.282 248.231 224.400 1.00 0.45  ? 1859 ILE A N     1 
ATOM   3261  C  CA    . ILE A 1 1859 ? 151.085 249.445 224.473 1.00 0.45  ? 1859 ILE A CA    1 
ATOM   3262  C  C     . ILE A 1 1859 ? 151.127 250.056 223.082 1.00 0.62  ? 1859 ILE A C     1 
ATOM   3263  O  O     . ILE A 1 1859 ? 151.576 249.413 222.126 1.00 0.94  ? 1859 ILE A O     1 
ATOM   3264  C  CB    . ILE A 1 1859 ? 152.498 249.165 225.002 1.00 0.29  ? 1859 ILE A CB    1 
ATOM   3265  C  CG1   . ILE A 1 1859 ? 152.428 248.557 226.404 1.00 0.31  ? 1859 ILE A CG1   1 
ATOM   3266  C  CG2   . ILE A 1 1859 ? 153.328 250.436 225.010 1.00 0.22  ? 1859 ILE A CG2   1 
ATOM   3267  C  CD1   . ILE A 1 1859 ? 153.567 247.624 226.719 1.00 0.14  ? 1859 ILE A CD1   1 
ATOM   3268  N  N     . GLN A 1 1860 ? 150.655 251.293 222.965 1.00 1.11  ? 1860 GLN A N     1 
ATOM   3269  C  CA    . GLN A 1 1860 ? 150.533 251.961 221.677 1.00 0.86  ? 1860 GLN A CA    1 
ATOM   3270  C  C     . GLN A 1 1860 ? 151.244 253.303 221.718 1.00 0.36  ? 1860 GLN A C     1 
ATOM   3271  O  O     . GLN A 1 1860 ? 151.060 254.080 222.658 1.00 0.36  ? 1860 GLN A O     1 
ATOM   3272  C  CB    . GLN A 1 1860 ? 149.064 252.149 221.294 1.00 1.95  ? 1860 GLN A CB    1 
ATOM   3273  C  CG    . GLN A 1 1860 ? 148.231 250.890 221.435 1.00 2.27  ? 1860 GLN A CG    1 
ATOM   3274  C  CD    . GLN A 1 1860 ? 146.786 251.104 221.049 1.00 3.40  ? 1860 GLN A CD    1 
ATOM   3275  O  OE1   . GLN A 1 1860 ? 146.396 252.199 220.652 1.00 9.91  ? 1860 GLN A OE1   1 
ATOM   3276  N  NE2   . GLN A 1 1860 ? 145.981 250.057 221.163 1.00 6.24  ? 1860 GLN A NE2   1 
ATOM   3277  N  N     . MET A 1 1861 ? 152.062 253.562 220.701 1.00 0.78  ? 1861 MET A N     1 
ATOM   3278  C  CA    . MET A 1 1861 ? 152.720 254.849 220.513 1.00 0.90  ? 1861 MET A CA    1 
ATOM   3279  C  C     . MET A 1 1861 ? 152.563 255.246 219.054 1.00 0.46  ? 1861 MET A C     1 
ATOM   3280  O  O     . MET A 1 1861 ? 153.069 254.552 218.166 1.00 0.46  ? 1861 MET A O     1 
ATOM   3281  C  CB    . MET A 1 1861 ? 154.199 254.783 220.905 1.00 0.70  ? 1861 MET A CB    1 
ATOM   3282  C  CG    . MET A 1 1861 ? 154.802 256.125 221.278 1.00 0.38  ? 1861 MET A CG    1 
ATOM   3283  S  SD    . MET A 1 1861 ? 156.548 256.020 221.701 1.00 4.29  ? 1861 MET A SD    1 
ATOM   3284  C  CE    . MET A 1 1861 ? 156.889 257.717 222.157 1.00 0.70  ? 1861 MET A CE    1 
ATOM   3285  N  N     . ALA A 1 1862 ? 151.861 256.356 218.812 1.00 1.52  ? 1862 ALA A N     1 
ATOM   3286  C  CA    . ALA A 1 1862 ? 151.454 256.795 217.470 1.00 0.93  ? 1862 ALA A CA    1 
ATOM   3287  C  C     . ALA A 1 1862 ? 150.620 255.675 216.861 1.00 1.39  ? 1862 ALA A C     1 
ATOM   3288  O  O     . ALA A 1 1862 ? 149.595 255.303 217.459 1.00 4.48  ? 1862 ALA A O     1 
ATOM   3289  C  CB    . ALA A 1 1862 ? 152.682 257.229 216.666 1.00 0.67  ? 1862 ALA A CB    1 
ATOM   3290  N  N     . ASN A 1 1863 ? 150.995 255.110 215.717 1.00 0.67  ? 1863 ASN A N     1 
ATOM   3291  C  CA    . ASN A 1 1863 ? 150.266 253.986 215.146 1.00 0.97  ? 1863 ASN A CA    1 
ATOM   3292  C  C     . ASN A 1 1863 ? 150.847 252.640 215.550 1.00 2.36  ? 1863 ASN A C     1 
ATOM   3293  O  O     . ASN A 1 1863 ? 150.236 251.607 215.260 1.00 5.67  ? 1863 ASN A O     1 
ATOM   3294  C  CB    . ASN A 1 1863 ? 150.238 254.086 213.615 1.00 1.16  ? 1863 ASN A CB    1 
ATOM   3295  C  CG    . ASN A 1 1863 ? 151.617 254.256 213.018 1.00 2.69  ? 1863 ASN A CG    1 
ATOM   3296  O  OD1   . ASN A 1 1863 ? 152.307 255.240 213.287 1.00 4.08  ? 1863 ASN A OD1   1 
ATOM   3297  N  ND2   . ASN A 1 1863 ? 152.030 253.292 212.207 1.00 2.59  ? 1863 ASN A ND2   1 
ATOM   3298  N  N     . ALA A 1 1864 ? 152.003 252.625 216.206 1.00 1.44  ? 1864 ALA A N     1 
ATOM   3299  C  CA    . ALA A 1 1864 ? 152.628 251.373 216.602 1.00 1.06  ? 1864 ALA A CA    1 
ATOM   3300  C  C     . ALA A 1 1864 ? 151.893 250.764 217.789 1.00 1.07  ? 1864 ALA A C     1 
ATOM   3301  O  O     . ALA A 1 1864 ? 151.620 251.445 218.779 1.00 2.13  ? 1864 ALA A O     1 
ATOM   3302  C  CB    . ALA A 1 1864 ? 154.098 251.601 216.946 1.00 0.52  ? 1864 ALA A CB    1 
ATOM   3303  N  N     . LYS A 1 1865 ? 151.568 249.480 217.681 1.00 1.18  ? 1865 LYS A N     1 
ATOM   3304  C  CA    . LYS A 1 1865 ? 150.937 248.728 218.755 1.00 1.21  ? 1865 LYS A CA    1 
ATOM   3305  C  C     . LYS A 1 1865 ? 151.810 247.536 219.111 1.00 0.48  ? 1865 LYS A C     1 
ATOM   3306  O  O     . LYS A 1 1865 ? 152.344 246.859 218.229 1.00 0.82  ? 1865 LYS A O     1 
ATOM   3307  C  CB    . LYS A 1 1865 ? 149.537 248.249 218.362 1.00 0.93  ? 1865 LYS A CB    1 
ATOM   3308  C  CG    . LYS A 1 1865 ? 148.548 249.367 218.162 1.00 2.91  ? 1865 LYS A CG    1 
ATOM   3309  C  CD    . LYS A 1 1865 ? 147.176 248.844 217.790 1.00 5.71  ? 1865 LYS A CD    1 
ATOM   3310  C  CE    . LYS A 1 1865 ? 146.190 249.991 217.686 1.00 11.88 ? 1865 LYS A CE    1 
ATOM   3311  N  NZ    . LYS A 1 1865 ? 146.531 250.881 216.543 1.00 7.30  ? 1865 LYS A NZ    1 
ATOM   3312  N  N     . PHE A 1 1866 ? 151.955 247.291 220.407 1.00 0.37  ? 1866 PHE A N     1 
ATOM   3313  C  CA    . PHE A 1 1866 ? 152.800 246.216 220.894 1.00 0.50  ? 1866 PHE A CA    1 
ATOM   3314  C  C     . PHE A 1 1866 ? 152.067 245.444 221.977 1.00 0.33  ? 1866 PHE A C     1 
ATOM   3315  O  O     . PHE A 1 1866 ? 151.270 246.005 222.733 1.00 0.58  ? 1866 PHE A O     1 
ATOM   3316  C  CB    . PHE A 1 1866 ? 154.125 246.747 221.455 1.00 0.29  ? 1866 PHE A CB    1 
ATOM   3317  C  CG    . PHE A 1 1866 ? 154.931 247.527 220.466 1.00 0.27  ? 1866 PHE A CG    1 
ATOM   3318  C  CD1   . PHE A 1 1866 ? 155.823 246.888 219.628 1.00 0.24  ? 1866 PHE A CD1   1 
ATOM   3319  C  CD2   . PHE A 1 1866 ? 154.797 248.901 220.376 1.00 0.10  ? 1866 PHE A CD2   1 
ATOM   3320  C  CE1   . PHE A 1 1866 ? 156.568 247.606 218.718 1.00 1.31  ? 1866 PHE A CE1   1 
ATOM   3321  C  CE2   . PHE A 1 1866 ? 155.535 249.622 219.470 1.00 0.11  ? 1866 PHE A CE2   1 
ATOM   3322  C  CZ    . PHE A 1 1866 ? 156.422 248.976 218.637 1.00 0.34  ? 1866 PHE A CZ    1 
ATOM   3323  N  N     . ASN A 1 1867 ? 152.340 244.149 222.035 1.00 0.43  ? 1867 ASN A N     1 
ATOM   3324  C  CA    . ASN A 1 1867 ? 151.969 243.343 223.182 1.00 0.64  ? 1867 ASN A CA    1 
ATOM   3325  C  C     . ASN A 1 1867 ? 153.095 243.383 224.206 1.00 0.40  ? 1867 ASN A C     1 
ATOM   3326  O  O     . ASN A 1 1867 ? 154.263 243.577 223.866 1.00 0.32  ? 1867 ASN A O     1 
ATOM   3327  C  CB    . ASN A 1 1867 ? 151.686 241.898 222.769 1.00 1.57  ? 1867 ASN A CB    1 
ATOM   3328  C  CG    . ASN A 1 1867 ? 152.948 241.142 222.397 1.00 5.27  ? 1867 ASN A CG    1 
ATOM   3329  O  OD1   . ASN A 1 1867 ? 153.666 241.527 221.476 1.00 6.31  ? 1867 ASN A OD1   1 
ATOM   3330  N  ND2   . ASN A 1 1867 ? 153.226 240.063 223.116 1.00 6.76  ? 1867 ASN A ND2   1 
ATOM   3331  N  N     . TYR A 1 1868 ? 152.730 243.209 225.470 1.00 0.40  ? 1868 TYR A N     1 
ATOM   3332  C  CA    . TYR A 1 1868 ? 153.721 243.118 226.530 1.00 0.24  ? 1868 TYR A CA    1 
ATOM   3333  C  C     . TYR A 1 1868 ? 154.289 241.704 226.571 1.00 0.53  ? 1868 TYR A C     1 
ATOM   3334  O  O     . TYR A 1 1868 ? 153.538 240.725 226.618 1.00 1.01  ? 1868 TYR A O     1 
ATOM   3335  C  CB    . TYR A 1 1868 ? 153.097 243.493 227.872 1.00 0.33  ? 1868 TYR A CB    1 
ATOM   3336  C  CG    . TYR A 1 1868 ? 154.097 243.850 228.946 1.00 0.44  ? 1868 TYR A CG    1 
ATOM   3337  C  CD1   . TYR A 1 1868 ? 154.816 245.038 228.890 1.00 0.19  ? 1868 TYR A CD1   1 
ATOM   3338  C  CD2   . TYR A 1 1868 ? 154.316 243.001 230.020 1.00 0.13  ? 1868 TYR A CD2   1 
ATOM   3339  C  CE1   . TYR A 1 1868 ? 155.728 245.363 229.874 1.00 0.16  ? 1868 TYR A CE1   1 
ATOM   3340  C  CE2   . TYR A 1 1868 ? 155.221 243.319 231.005 1.00 0.10  ? 1868 TYR A CE2   1 
ATOM   3341  C  CZ    . TYR A 1 1868 ? 155.926 244.498 230.930 1.00 0.17  ? 1868 TYR A CZ    1 
ATOM   3342  O  OH    . TYR A 1 1868 ? 156.828 244.811 231.918 1.00 1.26  ? 1868 TYR A OH    1 
ATOM   3343  N  N     . GLY A 1 1869 ? 155.619 241.598 226.536 1.00 0.15  ? 1869 GLY A N     1 
ATOM   3344  C  CA    . GLY A 1 1869 ? 156.246 240.289 226.483 1.00 0.62  ? 1869 GLY A CA    1 
ATOM   3345  C  C     . GLY A 1 1869 ? 156.142 239.510 227.777 1.00 0.81  ? 1869 GLY A C     1 
ATOM   3346  O  O     . GLY A 1 1869 ? 156.197 238.278 227.769 1.00 1.90  ? 1869 GLY A O     1 
ATOM   3347  N  N     . PHE A 1 1870 ? 155.984 240.213 228.900 1.00 0.51  ? 1870 PHE A N     1 
ATOM   3348  C  CA    . PHE A 1 1870 ? 155.881 239.607 230.229 1.00 0.63  ? 1870 PHE A CA    1 
ATOM   3349  C  C     . PHE A 1 1870 ? 157.116 238.782 230.577 1.00 0.84  ? 1870 PHE A C     1 
ATOM   3350  O  O     . PHE A 1 1870 ? 157.027 237.764 231.265 1.00 1.71  ? 1870 PHE A O     1 
ATOM   3351  C  CB    . PHE A 1 1870 ? 154.604 238.771 230.363 1.00 0.53  ? 1870 PHE A CB    1 
ATOM   3352  C  CG    . PHE A 1 1870 ? 153.367 239.601 230.527 1.00 0.73  ? 1870 PHE A CG    1 
ATOM   3353  C  CD1   . PHE A 1 1870 ? 153.135 240.296 231.701 1.00 0.46  ? 1870 PHE A CD1   1 
ATOM   3354  C  CD2   . PHE A 1 1870 ? 152.448 239.710 229.497 1.00 0.67  ? 1870 PHE A CD2   1 
ATOM   3355  C  CE1   . PHE A 1 1870 ? 152.008 241.072 231.851 1.00 0.52  ? 1870 PHE A CE1   1 
ATOM   3356  C  CE2   . PHE A 1 1870 ? 151.316 240.481 229.644 1.00 0.66  ? 1870 PHE A CE2   1 
ATOM   3357  C  CZ    . PHE A 1 1870 ? 151.096 241.164 230.824 1.00 0.77  ? 1870 PHE A CZ    1 
ATOM   3358  N  N     . GLU A 1 1871 ? 158.273 239.223 230.094 1.00 1.04  ? 1871 GLU A N     1 
ATOM   3359  C  CA    . GLU A 1 1871 ? 159.543 238.718 230.590 1.00 0.66  ? 1871 GLU A CA    1 
ATOM   3360  C  C     . GLU A 1 1871 ? 159.795 239.281 231.982 1.00 1.02  ? 1871 GLU A C     1 
ATOM   3361  O  O     . GLU A 1 1871 ? 159.644 240.484 232.207 1.00 4.28  ? 1871 GLU A O     1 
ATOM   3362  C  CB    . GLU A 1 1871 ? 160.674 239.118 229.643 1.00 0.47  ? 1871 GLU A CB    1 
ATOM   3363  C  CG    . GLU A 1 1871 ? 162.055 238.645 230.055 1.00 1.52  ? 1871 GLU A CG    1 
ATOM   3364  C  CD    . GLU A 1 1871 ? 162.326 237.203 229.671 1.00 2.34  ? 1871 GLU A CD    1 
ATOM   3365  O  OE1   . GLU A 1 1871 ? 161.430 236.552 229.094 1.00 4.13  ? 1871 GLU A OE1   1 
ATOM   3366  O  OE2   . GLU A 1 1871 ? 163.441 236.719 229.941 1.00 2.87  ? 1871 GLU A OE2   1 
ATOM   3367  N  N     . TYR A 1 1872 ? 160.168 238.418 232.922 1.00 1.29  ? 1872 TYR A N     1 
ATOM   3368  C  CA    . TYR A 1 1872 ? 160.502 238.888 234.261 1.00 0.95  ? 1872 TYR A CA    1 
ATOM   3369  C  C     . TYR A 1 1872 ? 161.794 239.689 234.187 1.00 1.52  ? 1872 TYR A C     1 
ATOM   3370  O  O     . TYR A 1 1872 ? 162.860 239.136 233.903 1.00 3.19  ? 1872 TYR A O     1 
ATOM   3371  C  CB    . TYR A 1 1872 ? 160.651 237.725 235.237 1.00 1.20  ? 1872 TYR A CB    1 
ATOM   3372  C  CG    . TYR A 1 1872 ? 160.926 238.195 236.647 1.00 1.56  ? 1872 TYR A CG    1 
ATOM   3373  C  CD1   . TYR A 1 1872 ? 160.246 239.284 237.175 1.00 2.45  ? 1872 TYR A CD1   1 
ATOM   3374  C  CD2   . TYR A 1 1872 ? 161.900 237.592 237.428 1.00 2.02  ? 1872 TYR A CD2   1 
ATOM   3375  C  CE1   . TYR A 1 1872 ? 160.497 239.733 238.452 1.00 2.24  ? 1872 TYR A CE1   1 
ATOM   3376  C  CE2   . TYR A 1 1872 ? 162.162 238.037 238.710 1.00 3.35  ? 1872 TYR A CE2   1 
ATOM   3377  C  CZ    . TYR A 1 1872 ? 161.457 239.111 239.215 1.00 2.82  ? 1872 TYR A CZ    1 
ATOM   3378  O  OH    . TYR A 1 1872 ? 161.710 239.562 240.487 1.00 4.17  ? 1872 TYR A OH    1 
ATOM   3379  N  N     . LEU A 1 1873 ? 161.704 240.993 234.430 1.00 1.74  ? 1873 LEU A N     1 
ATOM   3380  C  CA    . LEU A 1 1873 ? 162.867 241.861 234.357 1.00 2.52  ? 1873 LEU A CA    1 
ATOM   3381  C  C     . LEU A 1 1873 ? 163.551 242.067 235.699 1.00 2.77  ? 1873 LEU A C     1 
ATOM   3382  O  O     . LEU A 1 1873 ? 164.634 242.657 235.737 1.00 8.63  ? 1873 LEU A O     1 
ATOM   3383  C  CB    . LEU A 1 1873 ? 162.469 243.218 233.769 1.00 3.27  ? 1873 LEU A CB    1 
ATOM   3384  C  CG    . LEU A 1 1873 ? 161.761 243.143 232.417 1.00 1.26  ? 1873 LEU A CG    1 
ATOM   3385  C  CD1   . LEU A 1 1873 ? 161.267 244.507 231.999 1.00 0.97  ? 1873 LEU A CD1   1 
ATOM   3386  C  CD2   . LEU A 1 1873 ? 162.689 242.561 231.362 1.00 1.94  ? 1873 LEU A CD2   1 
ATOM   3387  N  N     . GLY A 1 1874 ? 162.966 241.579 236.790 1.00 2.90  ? 1874 GLY A N     1 
ATOM   3388  C  CA    . GLY A 1 1874 ? 163.529 241.865 238.095 1.00 2.79  ? 1874 GLY A CA    1 
ATOM   3389  C  C     . GLY A 1 1874 ? 163.407 243.337 238.424 1.00 2.52  ? 1874 GLY A C     1 
ATOM   3390  O  O     . GLY A 1 1874 ? 162.365 243.963 238.208 1.00 5.46  ? 1874 GLY A O     1 
ATOM   3391  N  N     . VAL A 1 1875 ? 164.483 243.905 238.960 1.00 3.75  ? 1875 VAL A N     1 
ATOM   3392  C  CA    . VAL A 1 1875 ? 164.503 245.328 239.273 1.00 4.60  ? 1875 VAL A CA    1 
ATOM   3393  C  C     . VAL A 1 1875 ? 165.584 246.001 238.441 1.00 6.45  ? 1875 VAL A C     1 
ATOM   3394  O  O     . VAL A 1 1875 ? 166.746 246.077 238.854 1.00 14.61 ? 1875 VAL A O     1 
ATOM   3395  C  CB    . VAL A 1 1875 ? 164.729 245.566 240.778 1.00 5.42  ? 1875 VAL A CB    1 
ATOM   3396  C  CG1   . VAL A 1 1875 ? 164.416 247.008 241.139 1.00 7.29  ? 1875 VAL A CG1   1 
ATOM   3397  C  CG2   . VAL A 1 1875 ? 163.889 244.609 241.606 1.00 3.87  ? 1875 VAL A CG2   1 
ATOM   3398  N  N     . GLN A 1 1876 ? 165.209 246.498 237.265 1.00 8.23  ? 1876 GLN A N     1 
ATOM   3399  C  CA    . GLN A 1 1876 ? 166.136 247.192 236.383 1.00 8.32  ? 1876 GLN A CA    1 
ATOM   3400  C  C     . GLN A 1 1876 ? 166.046 248.692 236.615 1.00 10.80 ? 1876 GLN A C     1 
ATOM   3401  O  O     . GLN A 1 1876 ? 164.953 249.260 236.619 1.00 16.32 ? 1876 GLN A O     1 
ATOM   3402  C  CB    . GLN A 1 1876 ? 165.834 246.886 234.915 1.00 11.71 ? 1876 GLN A CB    1 
ATOM   3403  C  CG    . GLN A 1 1876 ? 165.617 245.420 234.591 1.00 8.82  ? 1876 GLN A CG    1 
ATOM   3404  C  CD    . GLN A 1 1876 ? 166.883 244.726 234.128 1.00 15.16 ? 1876 GLN A CD    1 
ATOM   3405  O  OE1   . GLN A 1 1876 ? 167.946 245.339 234.042 1.00 15.84 ? 1876 GLN A OE1   1 
ATOM   3406  N  NE2   . GLN A 1 1876 ? 166.773 243.438 233.819 1.00 17.28 ? 1876 GLN A NE2   1 
ATOM   3407  N  N     . ASP A 1 1877 ? 167.202 249.326 236.800 1.00 15.75 ? 1877 ASP A N     1 
ATOM   3408  C  CA    . ASP A 1 1877 ? 167.241 250.775 236.961 1.00 11.76 ? 1877 ASP A CA    1 
ATOM   3409  C  C     . ASP A 1 1877 ? 166.642 251.454 235.736 1.00 9.17  ? 1877 ASP A C     1 
ATOM   3410  O  O     . ASP A 1 1877 ? 166.999 251.139 234.599 1.00 8.57  ? 1877 ASP A O     1 
ATOM   3411  C  CB    . ASP A 1 1877 ? 168.679 251.244 237.175 1.00 9.20  ? 1877 ASP A CB    1 
ATOM   3412  C  CG    . ASP A 1 1877 ? 169.199 250.920 238.561 1.00 19.38 ? 1877 ASP A CG    1 
ATOM   3413  O  OD1   . ASP A 1 1877 ? 168.480 251.181 239.548 1.00 23.13 ? 1877 ASP A OD1   1 
ATOM   3414  O  OD2   . ASP A 1 1877 ? 170.329 250.399 238.664 1.00 22.81 ? 1877 ASP A OD2   1 
ATOM   3415  N  N     . LYS A 1 1878 ? 165.729 252.390 235.973 1.00 10.44 ? 1878 LYS A N     1 
ATOM   3416  C  CA    . LYS A 1 1878 ? 165.031 253.060 234.887 1.00 7.91  ? 1878 LYS A CA    1 
ATOM   3417  C  C     . LYS A 1 1878 ? 165.698 254.375 234.519 1.00 6.68  ? 1878 LYS A C     1 
ATOM   3418  O  O     . LYS A 1 1878 ? 166.344 255.021 235.348 1.00 10.83 ? 1878 LYS A O     1 
ATOM   3419  C  CB    . LYS A 1 1878 ? 163.566 253.308 235.239 1.00 6.53  ? 1878 LYS A CB    1 
ATOM   3420  C  CG    . LYS A 1 1878 ? 162.747 252.045 235.355 1.00 11.96 ? 1878 LYS A CG    1 
ATOM   3421  C  CD    . LYS A 1 1878 ? 161.296 252.366 235.651 1.00 13.09 ? 1878 LYS A CD    1 
ATOM   3422  C  CE    . LYS A 1 1878 ? 160.488 251.104 235.845 1.00 10.49 ? 1878 LYS A CE    1 
ATOM   3423  N  NZ    . LYS A 1 1878 ? 160.369 250.328 234.588 1.00 13.13 ? 1878 LYS A NZ    1 
ATOM   3424  N  N     . LEU A 1 1879 ? 165.531 254.759 233.259 1.00 4.10  ? 1879 LEU A N     1 
ATOM   3425  C  CA    . LEU A 1 1879 ? 166.048 256.017 232.758 1.00 1.26  ? 1879 LEU A CA    1 
ATOM   3426  C  C     . LEU A 1 1879 ? 165.055 257.133 233.043 1.00 1.24  ? 1879 LEU A C     1 
ATOM   3427  O  O     . LEU A 1 1879 ? 163.844 256.910 233.121 1.00 1.93  ? 1879 LEU A O     1 
ATOM   3428  C  CB    . LEU A 1 1879 ? 166.299 255.923 231.253 1.00 0.53  ? 1879 LEU A CB    1 
ATOM   3429  C  CG    . LEU A 1 1879 ? 167.456 255.061 230.750 1.00 0.46  ? 1879 LEU A CG    1 
ATOM   3430  C  CD1   . LEU A 1 1879 ? 167.707 255.332 229.276 1.00 0.11  ? 1879 LEU A CD1   1 
ATOM   3431  C  CD2   . LEU A 1 1879 ? 168.718 255.276 231.567 1.00 0.51  ? 1879 LEU A CD2   1 
ATOM   3432  N  N     . VAL A 1 1880 ? 165.576 258.348 233.204 1.00 0.78  ? 1880 VAL A N     1 
ATOM   3433  C  CA    . VAL A 1 1880 ? 164.707 259.514 233.247 1.00 0.65  ? 1880 VAL A CA    1 
ATOM   3434  C  C     . VAL A 1 1880 ? 164.143 259.745 231.853 1.00 0.80  ? 1880 VAL A C     1 
ATOM   3435  O  O     . VAL A 1 1880 ? 164.888 259.811 230.869 1.00 0.93  ? 1880 VAL A O     1 
ATOM   3436  C  CB    . VAL A 1 1880 ? 165.468 260.745 233.761 1.00 0.94  ? 1880 VAL A CB    1 
ATOM   3437  C  CG1   . VAL A 1 1880 ? 164.607 261.996 233.623 1.00 0.37  ? 1880 VAL A CG1   1 
ATOM   3438  C  CG2   . VAL A 1 1880 ? 165.893 260.538 235.203 1.00 0.69  ? 1880 VAL A CG2   1 
ATOM   3439  N  N     . GLN A 1 1881 ? 162.824 259.853 231.763 1.00 1.33  ? 1881 GLN A N     1 
ATOM   3440  C  CA    . GLN A 1 1881 ? 162.143 259.887 230.473 1.00 2.16  ? 1881 GLN A CA    1 
ATOM   3441  C  C     . GLN A 1 1881 ? 162.212 261.314 229.936 1.00 1.63  ? 1881 GLN A C     1 
ATOM   3442  O  O     . GLN A 1 1881 ? 161.294 262.113 230.130 1.00 3.96  ? 1881 GLN A O     1 
ATOM   3443  C  CB    . GLN A 1 1881 ? 160.709 259.400 230.643 1.00 2.73  ? 1881 GLN A CB    1 
ATOM   3444  C  CG    . GLN A 1 1881 ? 159.889 259.272 229.378 1.00 2.55  ? 1881 GLN A CG    1 
ATOM   3445  C  CD    . GLN A 1 1881 ? 160.443 258.252 228.407 1.00 3.71  ? 1881 GLN A CD    1 
ATOM   3446  O  OE1   . GLN A 1 1881 ? 161.033 258.605 227.391 1.00 5.66  ? 1881 GLN A OE1   1 
ATOM   3447  N  NE2   . GLN A 1 1881 ? 160.258 256.977 228.720 1.00 7.50  ? 1881 GLN A NE2   1 
ATOM   3448  N  N     . THR A 1 1882 ? 163.319 261.642 229.266 1.00 1.92  ? 1882 THR A N     1 
ATOM   3449  C  CA    . THR A 1 1882 ? 163.638 262.962 228.743 1.00 0.95  ? 1882 THR A CA    1 
ATOM   3450  C  C     . THR A 1 1882 ? 163.071 263.154 227.343 1.00 1.21  ? 1882 THR A C     1 
ATOM   3451  O  O     . THR A 1 1882 ? 162.683 262.187 226.681 1.00 1.59  ? 1882 THR A O     1 
ATOM   3452  C  CB    . THR A 1 1882 ? 165.159 263.170 228.716 1.00 1.09  ? 1882 THR A CB    1 
ATOM   3453  O  OG1   . THR A 1 1882 ? 165.738 262.389 227.662 1.00 1.32  ? 1882 THR A OG1   1 
ATOM   3454  C  CG2   . THR A 1 1882 ? 165.777 262.773 230.039 1.00 0.70  ? 1882 THR A CG2   1 
ATOM   3455  N  N     . PRO A 1 1883 ? 162.989 264.402 226.865 1.00 3.02  ? 1883 PRO A N     1 
ATOM   3456  C  CA    . PRO A 1 1883 ? 162.552 264.627 225.476 1.00 1.11  ? 1883 PRO A CA    1 
ATOM   3457  C  C     . PRO A 1 1883 ? 163.380 263.888 224.435 1.00 1.13  ? 1883 PRO A C     1 
ATOM   3458  O  O     . PRO A 1 1883 ? 162.824 263.431 223.430 1.00 1.74  ? 1883 PRO A O     1 
ATOM   3459  C  CB    . PRO A 1 1883 ? 162.680 266.147 225.333 1.00 0.92  ? 1883 PRO A CB    1 
ATOM   3460  C  CG    . PRO A 1 1883 ? 162.376 266.644 226.695 1.00 1.97  ? 1883 PRO A CG    1 
ATOM   3461  C  CD    . PRO A 1 1883 ? 163.065 265.672 227.612 1.00 1.04  ? 1883 PRO A CD    1 
ATOM   3462  N  N     . LEU A 1 1884 ? 164.693 263.764 224.636 1.00 1.22  ? 1884 LEU A N     1 
ATOM   3463  C  CA    . LEU A 1 1884 ? 165.494 262.925 223.750 1.00 0.72  ? 1884 LEU A CA    1 
ATOM   3464  C  C     . LEU A 1 1884 ? 165.046 261.471 223.832 1.00 0.58  ? 1884 LEU A C     1 
ATOM   3465  O  O     . LEU A 1 1884 ? 164.946 260.781 222.812 1.00 0.79  ? 1884 LEU A O     1 
ATOM   3466  C  CB    . LEU A 1 1884 ? 166.979 263.049 224.095 1.00 1.16  ? 1884 LEU A CB    1 
ATOM   3467  C  CG    . LEU A 1 1884 ? 167.935 262.262 223.191 1.00 1.60  ? 1884 LEU A CG    1 
ATOM   3468  C  CD1   . LEU A 1 1884 ? 167.749 262.639 221.724 1.00 1.41  ? 1884 LEU A CD1   1 
ATOM   3469  C  CD2   . LEU A 1 1884 ? 169.382 262.447 223.618 1.00 0.57  ? 1884 LEU A CD2   1 
ATOM   3470  N  N     . THR A 1 1885 ? 164.761 260.995 225.045 1.00 1.33  ? 1885 THR A N     1 
ATOM   3471  C  CA    . THR A 1 1885 ? 164.295 259.624 225.210 1.00 1.11  ? 1885 THR A CA    1 
ATOM   3472  C  C     . THR A 1 1885 ? 162.900 259.453 224.615 1.00 0.91  ? 1885 THR A C     1 
ATOM   3473  O  O     . THR A 1 1885 ? 162.585 258.403 224.045 1.00 0.78  ? 1885 THR A O     1 
ATOM   3474  C  CB    . THR A 1 1885 ? 164.304 259.243 226.692 1.00 0.66  ? 1885 THR A CB    1 
ATOM   3475  O  OG1   . THR A 1 1885 ? 165.624 259.412 227.217 1.00 3.34  ? 1885 THR A OG1   1 
ATOM   3476  C  CG2   . THR A 1 1885 ? 163.927 257.783 226.862 1.00 0.60  ? 1885 THR A CG2   1 
ATOM   3477  N  N     . ASP A 1 1886 ? 162.055 260.480 224.735 1.00 0.82  ? 1886 ASP A N     1 
ATOM   3478  C  CA    . ASP A 1 1886 ? 160.746 260.452 224.090 1.00 0.62  ? 1886 ASP A CA    1 
ATOM   3479  C  C     . ASP A 1 1886 ? 160.889 260.349 222.578 1.00 0.37  ? 1886 ASP A C     1 
ATOM   3480  O  O     . ASP A 1 1886 ? 160.194 259.562 221.925 1.00 0.18  ? 1886 ASP A O     1 
ATOM   3481  C  CB    . ASP A 1 1886 ? 159.948 261.704 224.458 1.00 1.01  ? 1886 ASP A CB    1 
ATOM   3482  C  CG    . ASP A 1 1886 ? 159.243 261.581 225.789 1.00 3.60  ? 1886 ASP A CG    1 
ATOM   3483  O  OD1   . ASP A 1 1886 ? 159.773 260.896 226.682 1.00 6.31  ? 1886 ASP A OD1   1 
ATOM   3484  O  OD2   . ASP A 1 1886 ? 158.155 262.175 225.945 1.00 11.07 ? 1886 ASP A OD2   1 
ATOM   3485  N  N     . ARG A 1 1887 ? 161.792 261.146 222.008 1.00 0.35  ? 1887 ARG A N     1 
ATOM   3486  C  CA    . ARG A 1 1887 ? 162.046 261.074 220.576 1.00 0.14  ? 1887 ARG A CA    1 
ATOM   3487  C  C     . ARG A 1 1887 ? 162.630 259.720 220.193 1.00 0.15  ? 1887 ARG A C     1 
ATOM   3488  O  O     . ARG A 1 1887 ? 162.313 259.176 219.130 1.00 0.16  ? 1887 ARG A O     1 
ATOM   3489  C  CB    . ARG A 1 1887 ? 162.982 262.211 220.166 1.00 0.25  ? 1887 ARG A CB    1 
ATOM   3490  C  CG    . ARG A 1 1887 ? 163.215 262.346 218.680 1.00 0.44  ? 1887 ARG A CG    1 
ATOM   3491  C  CD    . ARG A 1 1887 ? 164.300 263.368 218.406 1.00 0.64  ? 1887 ARG A CD    1 
ATOM   3492  N  NE    . ARG A 1 1887 ? 164.560 263.520 216.980 1.00 1.91  ? 1887 ARG A NE    1 
ATOM   3493  C  CZ    . ARG A 1 1887 ? 164.495 264.670 216.325 1.00 1.02  ? 1887 ARG A CZ    1 
ATOM   3494  N  NH1   . ARG A 1 1887 ? 164.220 265.803 216.947 1.00 2.43  ? 1887 ARG A NH1   1 
ATOM   3495  N  NH2   . ARG A 1 1887 ? 164.718 264.684 215.015 1.00 1.21  ? 1887 ARG A NH2   1 
ATOM   3496  N  N     . CYS A 1 1888 ? 163.484 259.160 221.054 1.00 0.22  ? 1888 CYS A N     1 
ATOM   3497  C  CA    . CYS A 1 1888 ? 164.020 257.826 220.800 1.00 0.23  ? 1888 CYS A CA    1 
ATOM   3498  C  C     . CYS A 1 1888 ? 162.915 256.782 220.790 1.00 0.07  ? 1888 CYS A C     1 
ATOM   3499  O  O     . CYS A 1 1888 ? 162.887 255.904 219.920 1.00 0.06  ? 1888 CYS A O     1 
ATOM   3500  C  CB    . CYS A 1 1888 ? 165.087 257.481 221.841 1.00 0.24  ? 1888 CYS A CB    1 
ATOM   3501  S  SG    . CYS A 1 1888 ? 166.029 255.982 221.482 1.00 6.60  ? 1888 CYS A SG    1 
ATOM   3502  N  N     . TYR A 1 1889 ? 161.985 256.869 221.741 1.00 0.10  ? 1889 TYR A N     1 
ATOM   3503  C  CA    . TYR A 1 1889 ? 160.882 255.913 221.795 1.00 0.13  ? 1889 TYR A CA    1 
ATOM   3504  C  C     . TYR A 1 1889 ? 160.012 256.007 220.548 1.00 0.07  ? 1889 TYR A C     1 
ATOM   3505  O  O     . TYR A 1 1889 ? 159.613 254.987 219.977 1.00 0.04  ? 1889 TYR A O     1 
ATOM   3506  C  CB    . TYR A 1 1889 ? 160.045 256.155 223.051 1.00 0.12  ? 1889 TYR A CB    1 
ATOM   3507  C  CG    . TYR A 1 1889 ? 160.582 255.504 224.302 1.00 0.14  ? 1889 TYR A CG    1 
ATOM   3508  C  CD1   . TYR A 1 1889 ? 161.939 255.256 224.456 1.00 0.19  ? 1889 TYR A CD1   1 
ATOM   3509  C  CD2   . TYR A 1 1889 ? 159.729 255.152 225.340 1.00 0.42  ? 1889 TYR A CD2   1 
ATOM   3510  C  CE1   . TYR A 1 1889 ? 162.430 254.666 225.602 1.00 0.26  ? 1889 TYR A CE1   1 
ATOM   3511  C  CE2   . TYR A 1 1889 ? 160.212 254.562 226.490 1.00 0.69  ? 1889 TYR A CE2   1 
ATOM   3512  C  CZ    . TYR A 1 1889 ? 161.563 254.322 226.617 1.00 0.52  ? 1889 TYR A CZ    1 
ATOM   3513  O  OH    . TYR A 1 1889 ? 162.047 253.737 227.759 1.00 0.51  ? 1889 TYR A OH    1 
ATOM   3514  N  N     . LEU A 1 1890 ? 159.709 257.229 220.112 1.00 0.07  ? 1890 LEU A N     1 
ATOM   3515  C  CA    . LEU A 1 1890 ? 158.850 257.411 218.948 1.00 0.05  ? 1890 LEU A CA    1 
ATOM   3516  C  C     . LEU A 1 1890 ? 159.500 256.852 217.689 1.00 0.07  ? 1890 LEU A C     1 
ATOM   3517  O  O     . LEU A 1 1890 ? 158.855 256.157 216.896 1.00 0.07  ? 1890 LEU A O     1 
ATOM   3518  C  CB    . LEU A 1 1890 ? 158.519 258.890 218.777 1.00 0.14  ? 1890 LEU A CB    1 
ATOM   3519  C  CG    . LEU A 1 1890 ? 157.559 259.252 217.644 1.00 0.06  ? 1890 LEU A CG    1 
ATOM   3520  C  CD1   . LEU A 1 1890 ? 156.184 258.674 217.906 1.00 0.03  ? 1890 LEU A CD1   1 
ATOM   3521  C  CD2   . LEU A 1 1890 ? 157.495 260.760 217.467 1.00 0.09  ? 1890 LEU A CD2   1 
ATOM   3522  N  N     . THR A 1 1891 ? 160.788 257.135 217.496 1.00 0.06  ? 1891 THR A N     1 
ATOM   3523  C  CA    . THR A 1 1891 ? 161.471 256.708 216.280 1.00 0.05  ? 1891 THR A CA    1 
ATOM   3524  C  C     . THR A 1 1891 ? 161.631 255.192 216.238 1.00 0.04  ? 1891 THR A C     1 
ATOM   3525  O  O     . THR A 1 1891 ? 161.358 254.556 215.215 1.00 0.09  ? 1891 THR A O     1 
ATOM   3526  C  CB    . THR A 1 1891 ? 162.831 257.400 216.179 1.00 0.12  ? 1891 THR A CB    1 
ATOM   3527  O  OG1   . THR A 1 1891 ? 162.667 258.807 216.385 1.00 1.63  ? 1891 THR A OG1   1 
ATOM   3528  C  CG2   . THR A 1 1891 ? 163.453 257.165 214.814 1.00 0.11  ? 1891 THR A CG2   1 
ATOM   3529  N  N     . MET A 1 1892 ? 162.071 254.594 217.347 1.00 0.05  ? 1892 MET A N     1 
ATOM   3530  C  CA    . MET A 1 1892 ? 162.301 253.154 217.362 1.00 0.03  ? 1892 MET A CA    1 
ATOM   3531  C  C     . MET A 1 1892 ? 160.998 252.375 217.219 1.00 0.03  ? 1892 MET A C     1 
ATOM   3532  O  O     . MET A 1 1892 ? 160.958 251.351 216.528 1.00 0.02  ? 1892 MET A O     1 
ATOM   3533  C  CB    . MET A 1 1892 ? 163.042 252.746 218.635 1.00 0.03  ? 1892 MET A CB    1 
ATOM   3534  C  CG    . MET A 1 1892 ? 164.379 253.434 218.833 1.00 0.02  ? 1892 MET A CG    1 
ATOM   3535  S  SD    . MET A 1 1892 ? 165.586 253.064 217.552 1.00 2.09  ? 1892 MET A SD    1 
ATOM   3536  C  CE    . MET A 1 1892 ? 165.701 254.638 216.710 1.00 0.06  ? 1892 MET A CE    1 
ATOM   3537  N  N     . THR A 1 1893 ? 159.921 252.839 217.856 1.00 0.03  ? 1893 THR A N     1 
ATOM   3538  C  CA    . THR A 1 1893 ? 158.645 252.145 217.714 1.00 0.04  ? 1893 THR A CA    1 
ATOM   3539  C  C     . THR A 1 1893 ? 158.080 252.292 216.306 1.00 0.06  ? 1893 THR A C     1 
ATOM   3540  O  O     . THR A 1 1893 ? 157.356 251.407 215.841 1.00 0.10  ? 1893 THR A O     1 
ATOM   3541  C  CB    . THR A 1 1893 ? 157.633 252.644 218.749 1.00 0.05  ? 1893 THR A CB    1 
ATOM   3542  O  OG1   . THR A 1 1893 ? 157.512 254.070 218.671 1.00 0.13  ? 1893 THR A OG1   1 
ATOM   3543  C  CG2   . THR A 1 1893 ? 158.060 252.242 220.147 1.00 0.03  ? 1893 THR A CG2   1 
ATOM   3544  N  N     . GLN A 1 1894 ? 158.386 253.395 215.620 1.00 0.06  ? 1894 GLN A N     1 
ATOM   3545  C  CA    . GLN A 1 1894 ? 158.023 253.501 214.211 1.00 0.08  ? 1894 GLN A CA    1 
ATOM   3546  C  C     . GLN A 1 1894 ? 158.761 252.460 213.382 1.00 0.17  ? 1894 GLN A C     1 
ATOM   3547  O  O     . GLN A 1 1894 ? 158.179 251.850 212.478 1.00 0.37  ? 1894 GLN A O     1 
ATOM   3548  C  CB    . GLN A 1 1894 ? 158.309 254.909 213.687 1.00 0.26  ? 1894 GLN A CB    1 
ATOM   3549  C  CG    . GLN A 1 1894 ? 157.302 255.957 214.120 1.00 0.07  ? 1894 GLN A CG    1 
ATOM   3550  C  CD    . GLN A 1 1894 ? 155.930 255.734 213.522 1.00 0.23  ? 1894 GLN A CD    1 
ATOM   3551  O  OE1   . GLN A 1 1894 ? 155.765 255.728 212.303 1.00 4.51  ? 1894 GLN A OE1   1 
ATOM   3552  N  NE2   . GLN A 1 1894 ? 154.935 255.546 214.378 1.00 0.34  ? 1894 GLN A NE2   1 
ATOM   3553  N  N     . ALA A 1 1895 ? 160.045 252.244 213.677 1.00 0.18  ? 1895 ALA A N     1 
ATOM   3554  C  CA    . ALA A 1 1895 ? 160.804 251.205 212.989 1.00 0.11  ? 1895 ALA A CA    1 
ATOM   3555  C  C     . ALA A 1 1895 ? 160.255 249.820 213.301 1.00 0.15  ? 1895 ALA A C     1 
ATOM   3556  O  O     . ALA A 1 1895 ? 160.203 248.955 212.418 1.00 0.28  ? 1895 ALA A O     1 
ATOM   3557  C  CB    . ALA A 1 1895 ? 162.280 251.297 213.368 1.00 0.08  ? 1895 ALA A CB    1 
ATOM   3558  N  N     . LEU A 1 1896 ? 159.852 249.587 214.551 1.00 0.11  ? 1896 LEU A N     1 
ATOM   3559  C  CA    . LEU A 1 1896 ? 159.298 248.291 214.924 1.00 0.14  ? 1896 LEU A CA    1 
ATOM   3560  C  C     . LEU A 1 1896 ? 157.985 248.019 214.202 1.00 0.78  ? 1896 LEU A C     1 
ATOM   3561  O  O     . LEU A 1 1896 ? 157.734 246.890 213.767 1.00 2.98  ? 1896 LEU A O     1 
ATOM   3562  C  CB    . LEU A 1 1896 ? 159.108 248.220 216.437 1.00 0.19  ? 1896 LEU A CB    1 
ATOM   3563  C  CG    . LEU A 1 1896 ? 160.376 248.262 217.291 1.00 0.13  ? 1896 LEU A CG    1 
ATOM   3564  C  CD1   . LEU A 1 1896 ? 160.030 248.387 218.763 1.00 0.14  ? 1896 LEU A CD1   1 
ATOM   3565  C  CD2   . LEU A 1 1896 ? 161.232 247.040 217.043 1.00 0.07  ? 1896 LEU A CD2   1 
ATOM   3566  N  N     . GLU A 1 1897 ? 157.129 249.034 214.075 1.00 0.34  ? 1897 GLU A N     1 
ATOM   3567  C  CA    . GLU A 1 1897 ? 155.891 248.860 213.324 1.00 0.67  ? 1897 GLU A CA    1 
ATOM   3568  C  C     . GLU A 1 1897 ? 156.163 248.611 211.847 1.00 1.18  ? 1897 GLU A C     1 
ATOM   3569  O  O     . GLU A 1 1897 ? 155.459 247.820 211.211 1.00 2.16  ? 1897 GLU A O     1 
ATOM   3570  C  CB    . GLU A 1 1897 ? 154.983 250.079 213.503 1.00 0.88  ? 1897 GLU A CB    1 
ATOM   3571  C  CG    . GLU A 1 1897 ? 153.513 249.807 213.200 1.00 1.08  ? 1897 GLU A CG    1 
ATOM   3572  C  CD    . GLU A 1 1897 ? 152.850 248.870 214.200 1.00 6.36  ? 1897 GLU A CD    1 
ATOM   3573  O  OE1   . GLU A 1 1897 ? 153.509 248.442 215.171 1.00 9.21  ? 1897 GLU A OE1   1 
ATOM   3574  O  OE2   . GLU A 1 1897 ? 151.657 248.556 214.010 1.00 11.59 ? 1897 GLU A OE2   1 
ATOM   3575  N  N     . ALA A 1 1898 ? 157.173 249.269 211.286 1.00 0.64  ? 1898 ALA A N     1 
ATOM   3576  C  CA    . ALA A 1 1898 ? 157.585 249.038 209.910 1.00 0.48  ? 1898 ALA A CA    1 
ATOM   3577  C  C     . ALA A 1 1898 ? 158.416 247.773 209.752 1.00 0.89  ? 1898 ALA A C     1 
ATOM   3578  O  O     . ALA A 1 1898 ? 158.905 247.505 208.650 1.00 1.04  ? 1898 ALA A O     1 
ATOM   3579  C  CB    . ALA A 1 1898 ? 158.371 250.243 209.385 1.00 0.35  ? 1898 ALA A CB    1 
ATOM   3580  N  N     . ARG A 1 1899 ? 158.582 247.005 210.830 1.00 0.97  ? 1899 ARG A N     1 
ATOM   3581  C  CA    . ARG A 1 1899 ? 159.401 245.793 210.831 1.00 1.08  ? 1899 ARG A CA    1 
ATOM   3582  C  C     . ARG A 1 1899 ? 160.827 246.101 210.384 1.00 0.81  ? 1899 ARG A C     1 
ATOM   3583  O  O     . ARG A 1 1899 ? 161.453 245.332 209.655 1.00 1.93  ? 1899 ARG A O     1 
ATOM   3584  C  CB    . ARG A 1 1899 ? 158.778 244.684 209.975 1.00 2.01  ? 1899 ARG A CB    1 
ATOM   3585  C  CG    . ARG A 1 1899 ? 157.702 243.856 210.678 1.00 3.90  ? 1899 ARG A CG    1 
ATOM   3586  C  CD    . ARG A 1 1899 ? 156.557 244.705 211.207 1.00 4.57  ? 1899 ARG A CD    1 
ATOM   3587  N  NE    . ARG A 1 1899 ? 155.788 244.025 212.241 1.00 12.14 ? 1899 ARG A NE    1 
ATOM   3588  C  CZ    . ARG A 1 1899 ? 154.734 244.548 212.853 1.00 10.75 ? 1899 ARG A CZ    1 
ATOM   3589  N  NH1   . ARG A 1 1899 ? 154.294 245.759 212.562 1.00 5.98  ? 1899 ARG A NH1   1 
ATOM   3590  N  NH2   . ARG A 1 1899 ? 154.106 243.835 213.786 1.00 12.71 ? 1899 ARG A NH2   1 
ATOM   3591  N  N     . LEU A 1 1900 ? 161.335 247.245 210.821 1.00 0.86  ? 1900 LEU A N     1 
ATOM   3592  C  CA    . LEU A 1 1900 ? 162.698 247.669 210.565 1.00 0.17  ? 1900 LEU A CA    1 
ATOM   3593  C  C     . LEU A 1 1900 ? 163.480 247.688 211.868 1.00 0.15  ? 1900 LEU A C     1 
ATOM   3594  O  O     . LEU A 1 1900 ? 162.911 247.677 212.962 1.00 0.19  ? 1900 LEU A O     1 
ATOM   3595  C  CB    . LEU A 1 1900 ? 162.731 249.059 209.916 1.00 0.48  ? 1900 LEU A CB    1 
ATOM   3596  C  CG    . LEU A 1 1900 ? 162.262 249.161 208.464 1.00 1.57  ? 1900 LEU A CG    1 
ATOM   3597  C  CD1   . LEU A 1 1900 ? 162.162 250.617 208.037 1.00 1.01  ? 1900 LEU A CD1   1 
ATOM   3598  C  CD2   . LEU A 1 1900 ? 163.195 248.393 207.544 1.00 0.46  ? 1900 LEU A CD2   1 
ATOM   3599  N  N     . GLY A 1 1901 ? 164.798 247.705 211.740 1.00 0.12  ? 1901 GLY A N     1 
ATOM   3600  C  CA    . GLY A 1 1901 ? 165.640 247.832 212.903 1.00 0.05  ? 1901 GLY A CA    1 
ATOM   3601  C  C     . GLY A 1 1901 ? 165.814 249.272 213.336 1.00 0.06  ? 1901 GLY A C     1 
ATOM   3602  O  O     . GLY A 1 1901 ? 165.622 250.215 212.570 1.00 0.12  ? 1901 GLY A O     1 
ATOM   3603  N  N     . GLY A 1 1902 ? 166.177 249.442 214.601 1.00 0.03  ? 1902 GLY A N     1 
ATOM   3604  C  CA    . GLY A 1 1902 ? 166.498 250.749 215.145 1.00 0.03  ? 1902 GLY A CA    1 
ATOM   3605  C  C     . GLY A 1 1902 ? 168.000 250.973 215.127 1.00 0.02  ? 1902 GLY A C     1 
ATOM   3606  O  O     . GLY A 1 1902 ? 168.776 250.073 215.443 1.00 0.03  ? 1902 GLY A O     1 
ATOM   3607  N  N     . SER A 1 1903 ? 168.399 252.181 214.743 1.00 0.04  ? 1903 SER A N     1 
ATOM   3608  C  CA    . SER A 1 1903 ? 169.812 252.549 214.641 1.00 0.03  ? 1903 SER A CA    1 
ATOM   3609  C  C     . SER A 1 1903 ? 170.066 253.894 215.312 1.00 0.06  ? 1903 SER A C     1 
ATOM   3610  O  O     . SER A 1 1903 ? 170.299 254.903 214.638 1.00 0.09  ? 1903 SER A O     1 
ATOM   3611  C  CB    . SER A 1 1903 ? 170.259 252.577 213.181 1.00 0.05  ? 1903 SER A CB    1 
ATOM   3612  O  OG    . SER A 1 1903 ? 171.627 252.926 213.079 1.00 5.69  ? 1903 SER A OG    1 
ATOM   3613  N  N     . PRO A 1 1904 ? 170.039 253.946 216.643 1.00 0.06  ? 1904 PRO A N     1 
ATOM   3614  C  CA    . PRO A 1 1904 ? 170.477 255.167 217.334 1.00 0.05  ? 1904 PRO A CA    1 
ATOM   3615  C  C     . PRO A 1 1904 ? 171.971 255.381 217.140 1.00 0.06  ? 1904 PRO A C     1 
ATOM   3616  O  O     . PRO A 1 1904 ? 172.774 254.468 217.340 1.00 0.31  ? 1904 PRO A O     1 
ATOM   3617  C  CB    . PRO A 1 1904 ? 170.127 254.893 218.803 1.00 0.05  ? 1904 PRO A CB    1 
ATOM   3618  C  CG    . PRO A 1 1904 ? 169.164 253.747 218.768 1.00 0.05  ? 1904 PRO A CG    1 
ATOM   3619  C  CD    . PRO A 1 1904 ? 169.577 252.926 217.598 1.00 0.05  ? 1904 PRO A CD    1 
ATOM   3620  N  N     . PHE A 1 1905 ? 172.341 256.595 216.741 1.00 0.06  ? 1905 PHE A N     1 
ATOM   3621  C  CA    . PHE A 1 1905 ? 173.730 256.935 216.476 1.00 0.11  ? 1905 PHE A CA    1 
ATOM   3622  C  C     . PHE A 1 1905 ? 174.074 258.260 217.140 1.00 0.07  ? 1905 PHE A C     1 
ATOM   3623  O  O     . PHE A 1 1905 ? 173.222 259.139 217.286 1.00 0.14  ? 1905 PHE A O     1 
ATOM   3624  C  CB    . PHE A 1 1905 ? 174.016 257.012 214.966 1.00 0.17  ? 1905 PHE A CB    1 
ATOM   3625  C  CG    . PHE A 1 1905 ? 173.316 258.142 214.270 1.00 0.08  ? 1905 PHE A CG    1 
ATOM   3626  C  CD1   . PHE A 1 1905 ? 172.037 257.975 213.769 1.00 0.08  ? 1905 PHE A CD1   1 
ATOM   3627  C  CD2   . PHE A 1 1905 ? 173.941 259.365 214.103 1.00 0.09  ? 1905 PHE A CD2   1 
ATOM   3628  C  CE1   . PHE A 1 1905 ? 171.394 259.009 213.126 1.00 0.15  ? 1905 PHE A CE1   1 
ATOM   3629  C  CE2   . PHE A 1 1905 ? 173.300 260.400 213.461 1.00 0.19  ? 1905 PHE A CE2   1 
ATOM   3630  C  CZ    . PHE A 1 1905 ? 172.025 260.222 212.971 1.00 0.38  ? 1905 PHE A CZ    1 
ATOM   3631  N  N     . GLY A 1 1906 ? 175.335 258.393 217.534 1.00 0.10  ? 1906 GLY A N     1 
ATOM   3632  C  CA    . GLY A 1 1906 ? 175.819 259.603 218.149 1.00 0.35  ? 1906 GLY A CA    1 
ATOM   3633  C  C     . GLY A 1 1906 ? 177.136 259.393 218.863 1.00 0.74  ? 1906 GLY A C     1 
ATOM   3634  O  O     . GLY A 1 1906 ? 177.721 258.307 218.835 1.00 0.86  ? 1906 GLY A O     1 
ATOM   3635  N  N     . PRO A 1 1907 ? 177.674 260.440 219.532 1.00 2.28  ? 1907 PRO A N     1 
ATOM   3636  C  CA    . PRO A 1 1907 ? 178.908 260.298 220.291 1.00 1.36  ? 1907 PRO A CA    1 
ATOM   3637  C  C     . PRO A 1 1907 ? 178.699 259.442 221.530 1.00 1.94  ? 1907 PRO A C     1 
ATOM   3638  O  O     . PRO A 1 1907 ? 177.548 259.089 221.844 1.00 2.30  ? 1907 PRO A O     1 
ATOM   3639  C  CB    . PRO A 1 1907 ? 179.265 261.748 220.632 1.00 1.18  ? 1907 PRO A CB    1 
ATOM   3640  C  CG    . PRO A 1 1907 ? 177.924 262.434 220.725 1.00 1.62  ? 1907 PRO A CG    1 
ATOM   3641  C  CD    . PRO A 1 1907 ? 177.120 261.794 219.610 1.00 1.12  ? 1907 PRO A CD    1 
ATOM   3642  N  N     . ALA A 1 1908 ? 179.785 259.125 222.235 1.00 2.83  ? 1908 ALA A N     1 
ATOM   3643  C  CA    . ALA A 1 1908 ? 179.700 258.231 223.414 1.00 2.35  ? 1908 ALA A CA    1 
ATOM   3644  C  C     . ALA A 1 1908 ? 179.015 258.921 224.597 1.00 1.69  ? 1908 ALA A C     1 
ATOM   3645  O  O     . ALA A 1 1908 ? 179.160 260.150 224.752 1.00 4.60  ? 1908 ALA A O     1 
ATOM   3646  C  CB    . ALA A 1 1908 ? 181.089 257.766 223.788 1.00 3.80  ? 1908 ALA A CB    1 
ATOM   3647  N  N     . GLY A 1 1909 ? 178.294 258.147 225.408 1.00 0.67  ? 1909 GLY A N     1 
ATOM   3648  C  CA    . GLY A 1 1909 ? 177.666 258.692 226.625 1.00 0.90  ? 1909 GLY A CA    1 
ATOM   3649  C  C     . GLY A 1 1909 ? 176.445 259.536 226.329 1.00 0.99  ? 1909 GLY A C     1 
ATOM   3650  O  O     . GLY A 1 1909 ? 176.236 260.530 227.047 1.00 1.51  ? 1909 GLY A O     1 
ATOM   3651  N  N     . THR A 1 1910 ? 175.654 259.163 225.326 1.00 1.20  ? 1910 THR A N     1 
ATOM   3652  C  CA    . THR A 1 1910 ? 174.429 259.912 225.089 1.00 0.93  ? 1910 THR A CA    1 
ATOM   3653  C  C     . THR A 1 1910 ? 173.170 259.126 225.422 1.00 0.49  ? 1910 THR A C     1 
ATOM   3654  O  O     . THR A 1 1910 ? 172.069 259.652 225.238 1.00 2.75  ? 1910 THR A O     1 
ATOM   3655  C  CB    . THR A 1 1910 ? 174.359 260.387 223.629 1.00 1.13  ? 1910 THR A CB    1 
ATOM   3656  O  OG1   . THR A 1 1910 ? 174.546 259.275 222.746 1.00 1.66  ? 1910 THR A OG1   1 
ATOM   3657  C  CG2   . THR A 1 1910 ? 175.427 261.429 223.359 1.00 0.63  ? 1910 THR A CG2   1 
ATOM   3658  N  N     . GLY A 1 1911 ? 173.303 257.899 225.909 1.00 0.15  ? 1911 GLY A N     1 
ATOM   3659  C  CA    . GLY A 1 1911 ? 172.161 257.088 226.262 1.00 0.11  ? 1911 GLY A CA    1 
ATOM   3660  C  C     . GLY A 1 1911 ? 171.649 256.172 225.176 1.00 0.12  ? 1911 GLY A C     1 
ATOM   3661  O  O     . GLY A 1 1911 ? 170.536 255.658 225.308 1.00 0.16  ? 1911 GLY A O     1 
ATOM   3662  N  N     . LYS A 1 1912 ? 172.431 255.959 224.122 1.00 0.22  ? 1912 LYS A N     1 
ATOM   3663  C  CA    . LYS A 1 1912 ? 171.968 255.136 222.975 1.00 0.08  ? 1912 LYS A CA    1 
ATOM   3664  C  C     . LYS A 1 1912 ? 171.596 253.718 223.444 1.00 0.06  ? 1912 LYS A C     1 
ATOM   3665  O  O     . LYS A 1 1912 ? 170.451 253.300 223.189 1.00 0.05  ? 1912 LYS A O     1 
ATOM   3666  C  CB    . LYS A 1 1912 ? 173.050 255.116 221.891 1.00 0.25  ? 1912 LYS A CB    1 
ATOM   3667  C  CG    . LYS A 1 1912 ? 173.292 256.441 221.187 1.00 0.19  ? 1912 LYS A CG    1 
ATOM   3668  C  CD    . LYS A 1 1912 ? 174.288 256.333 220.038 1.00 0.12  ? 1912 LYS A CD    1 
ATOM   3669  C  CE    . LYS A 1 1912 ? 175.616 255.800 220.468 1.00 0.22  ? 1912 LYS A CE    1 
ATOM   3670  N  NZ    . LYS A 1 1912 ? 176.247 256.653 221.479 1.00 0.47  ? 1912 LYS A NZ    1 
ATOM   3671  N  N     . THR A 1 1913 ? 172.516 253.017 224.111 1.00 0.09  ? 1913 THR A N     1 
ATOM   3672  C  CA    . THR A 1 1913 ? 172.276 251.614 224.523 1.00 0.11  ? 1913 THR A CA    1 
ATOM   3673  C  C     . THR A 1 1913 ? 171.212 251.553 225.597 1.00 0.08  ? 1913 THR A C     1 
ATOM   3674  O  O     . THR A 1 1913 ? 170.335 250.670 225.506 1.00 0.05  ? 1913 THR A O     1 
ATOM   3675  C  CB    . THR A 1 1913 ? 173.596 251.000 224.995 1.00 0.18  ? 1913 THR A CB    1 
ATOM   3676  O  OG1   . THR A 1 1913 ? 174.522 251.211 223.933 1.00 0.46  ? 1913 THR A OG1   1 
ATOM   3677  C  CG2   . THR A 1 1913 ? 173.475 249.519 225.306 1.00 0.41  ? 1913 THR A CG2   1 
ATOM   3678  N  N     . GLU A 1 1914 ? 171.270 252.457 226.573 1.00 0.05  ? 1914 GLU A N     1 
ATOM   3679  C  CA    . GLU A 1 1914 ? 170.320 252.414 227.714 1.00 0.09  ? 1914 GLU A CA    1 
ATOM   3680  C  C     . GLU A 1 1914 ? 168.895 252.702 227.215 1.00 0.03  ? 1914 GLU A C     1 
ATOM   3681  O  O     . GLU A 1 1914 ? 167.948 252.107 227.760 1.00 0.04  ? 1914 GLU A O     1 
ATOM   3682  C  CB    . GLU A 1 1914 ? 170.771 253.385 228.805 1.00 0.91  ? 1914 GLU A CB    1 
ATOM   3683  C  CG    . GLU A 1 1914 ? 172.096 252.979 229.441 1.00 0.99  ? 1914 GLU A CG    1 
ATOM   3684  C  CD    . GLU A 1 1914 ? 172.219 251.487 229.691 1.00 4.12  ? 1914 GLU A CD    1 
ATOM   3685  O  OE1   . GLU A 1 1914 ? 171.399 250.944 230.462 1.00 4.40  ? 1914 GLU A OE1   1 
ATOM   3686  O  OE2   . GLU A 1 1914 ? 173.133 250.866 229.109 1.00 5.58  ? 1914 GLU A OE2   1 
ATOM   3687  N  N     . SER A 1 1915 ? 168.761 253.562 226.207 1.00 0.06  ? 1915 SER A N     1 
ATOM   3688  C  CA    . SER A 1 1915 ? 167.434 253.870 225.689 1.00 0.04  ? 1915 SER A CA    1 
ATOM   3689  C  C     . SER A 1 1915 ? 166.819 252.665 224.990 1.00 0.02  ? 1915 SER A C     1 
ATOM   3690  O  O     . SER A 1 1915 ? 165.615 252.415 225.115 1.00 0.04  ? 1915 SER A O     1 
ATOM   3691  C  CB    . SER A 1 1915 ? 167.505 255.063 224.738 1.00 0.06  ? 1915 SER A CB    1 
ATOM   3692  O  OG    . SER A 1 1915 ? 168.039 256.196 225.392 1.00 0.30  ? 1915 SER A OG    1 
ATOM   3693  N  N     . VAL A 1 1916 ? 167.630 251.909 224.246 1.00 0.04  ? 1916 VAL A N     1 
ATOM   3694  C  CA    . VAL A 1 1916 ? 167.130 250.709 223.582 1.00 0.05  ? 1916 VAL A CA    1 
ATOM   3695  C  C     . VAL A 1 1916 ? 166.670 249.688 224.615 1.00 0.05  ? 1916 VAL A C     1 
ATOM   3696  O  O     . VAL A 1 1916 ? 165.597 249.089 224.485 1.00 0.02  ? 1916 VAL A O     1 
ATOM   3697  C  CB    . VAL A 1 1916 ? 168.204 250.125 222.645 1.00 0.03  ? 1916 VAL A CB    1 
ATOM   3698  C  CG1   . VAL A 1 1916 ? 167.795 248.744 222.151 1.00 0.02  ? 1916 VAL A CG1   1 
ATOM   3699  C  CG2   . VAL A 1 1916 ? 168.449 251.058 221.473 1.00 0.06  ? 1916 VAL A CG2   1 
ATOM   3700  N  N     . LYS A 1 1917 ? 167.476 249.479 225.660 1.00 0.02  ? 1917 LYS A N     1 
ATOM   3701  C  CA    . LYS A 1 1917 ? 167.072 248.562 226.722 1.00 0.03  ? 1917 LYS A CA    1 
ATOM   3702  C  C     . LYS A 1 1917 ? 165.853 249.084 227.464 1.00 0.03  ? 1917 LYS A C     1 
ATOM   3703  O  O     . LYS A 1 1917 ? 164.960 248.311 227.826 1.00 0.03  ? 1917 LYS A O     1 
ATOM   3704  C  CB    . LYS A 1 1917 ? 168.227 248.316 227.694 1.00 0.06  ? 1917 LYS A CB    1 
ATOM   3705  C  CG    . LYS A 1 1917 ? 169.409 247.589 227.087 1.00 1.09  ? 1917 LYS A CG    1 
ATOM   3706  C  CD    . LYS A 1 1917 ? 170.342 247.042 228.156 1.00 2.82  ? 1917 LYS A CD    1 
ATOM   3707  C  CE    . LYS A 1 1917 ? 170.873 248.132 229.057 1.00 2.41  ? 1917 LYS A CE    1 
ATOM   3708  N  NZ    . LYS A 1 1917 ? 171.714 247.589 230.155 1.00 1.21  ? 1917 LYS A NZ    1 
ATOM   3709  N  N     . ALA A 1 1918 ? 165.799 250.396 227.706 1.00 0.02  ? 1918 ALA A N     1 
ATOM   3710  C  CA    . ALA A 1 1918 ? 164.654 250.973 228.399 1.00 0.03  ? 1918 ALA A CA    1 
ATOM   3711  C  C     . ALA A 1 1918 ? 163.370 250.747 227.612 1.00 0.04  ? 1918 ALA A C     1 
ATOM   3712  O  O     . ALA A 1 1918 ? 162.336 250.380 228.180 1.00 0.02  ? 1918 ALA A O     1 
ATOM   3713  C  CB    . ALA A 1 1918 ? 164.887 252.462 228.650 1.00 0.03  ? 1918 ALA A CB    1 
ATOM   3714  N  N     . LEU A 1 1919 ? 163.420 250.949 226.294 1.00 0.03  ? 1919 LEU A N     1 
ATOM   3715  C  CA    . LEU A 1 1919 ? 162.254 250.688 225.461 1.00 0.04  ? 1919 LEU A CA    1 
ATOM   3716  C  C     . LEU A 1 1919 ? 161.881 249.210 225.492 1.00 0.06  ? 1919 LEU A C     1 
ATOM   3717  O  O     . LEU A 1 1919 ? 160.700 248.857 225.580 1.00 0.01  ? 1919 LEU A O     1 
ATOM   3718  C  CB    . LEU A 1 1919 ? 162.513 251.149 224.027 1.00 0.08  ? 1919 LEU A CB    1 
ATOM   3719  C  CG    . LEU A 1 1919 ? 161.370 250.884 223.045 1.00 0.02  ? 1919 LEU A CG    1 
ATOM   3720  C  CD1   . LEU A 1 1919 ? 160.074 251.513 223.543 1.00 0.01  ? 1919 LEU A CD1   1 
ATOM   3721  C  CD2   . LEU A 1 1919 ? 161.720 251.390 221.663 1.00 0.03  ? 1919 LEU A CD2   1 
ATOM   3722  N  N     . GLY A 1 1920 ? 162.883 248.333 225.426 1.00 0.20  ? 1920 GLY A N     1 
ATOM   3723  C  CA    . GLY A 1 1920 ? 162.612 246.908 225.525 1.00 0.03  ? 1920 GLY A CA    1 
ATOM   3724  C  C     . GLY A 1 1920 ? 162.020 246.516 226.864 1.00 0.05  ? 1920 GLY A C     1 
ATOM   3725  O  O     . GLY A 1 1920 ? 161.076 245.729 226.933 1.00 0.04  ? 1920 GLY A O     1 
ATOM   3726  N  N     . HIS A 1 1921 ? 162.572 247.060 227.951 1.00 0.03  ? 1921 HIS A N     1 
ATOM   3727  C  CA    . HIS A 1 1921 ? 162.018 246.785 229.271 1.00 0.07  ? 1921 HIS A CA    1 
ATOM   3728  C  C     . HIS A 1 1921 ? 160.631 247.391 229.421 1.00 0.03  ? 1921 HIS A C     1 
ATOM   3729  O  O     . HIS A 1 1921 ? 159.782 246.850 230.137 1.00 0.07  ? 1921 HIS A O     1 
ATOM   3730  C  CB    . HIS A 1 1921 ? 162.957 247.302 230.363 1.00 0.21  ? 1921 HIS A CB    1 
ATOM   3731  C  CG    . HIS A 1 1921 ? 164.329 246.708 230.308 1.00 1.28  ? 1921 HIS A CG    1 
ATOM   3732  N  ND1   . HIS A 1 1921 ? 165.401 247.249 230.986 1.00 11.11 ? 1921 HIS A ND1   1 
ATOM   3733  C  CD2   . HIS A 1 1921 ? 164.804 245.619 229.661 1.00 0.52  ? 1921 HIS A CD2   1 
ATOM   3734  C  CE1   . HIS A 1 1921 ? 166.477 246.517 230.757 1.00 5.25  ? 1921 HIS A CE1   1 
ATOM   3735  N  NE2   . HIS A 1 1921 ? 166.142 245.522 229.956 1.00 5.25  ? 1921 HIS A NE2   1 
ATOM   3736  N  N     . GLN A 1 1922 ? 160.384 248.519 228.754 1.00 0.04  ? 1922 GLN A N     1 
ATOM   3737  C  CA    . GLN A 1 1922 ? 159.046 249.095 228.739 1.00 0.05  ? 1922 GLN A CA    1 
ATOM   3738  C  C     . GLN A 1 1922 ? 158.044 248.136 228.109 1.00 0.03  ? 1922 GLN A C     1 
ATOM   3739  O  O     . GLN A 1 1922 ? 156.907 248.015 228.578 1.00 0.05  ? 1922 GLN A O     1 
ATOM   3740  C  CB    . GLN A 1 1922 ? 159.058 250.425 227.987 1.00 0.09  ? 1922 GLN A CB    1 
ATOM   3741  C  CG    . GLN A 1 1922 ? 157.722 251.128 227.971 1.00 0.21  ? 1922 GLN A CG    1 
ATOM   3742  C  CD    . GLN A 1 1922 ? 157.258 251.515 229.355 1.00 0.61  ? 1922 GLN A CD    1 
ATOM   3743  O  OE1   . GLN A 1 1922 ? 157.819 252.412 229.981 1.00 0.41  ? 1922 GLN A OE1   1 
ATOM   3744  N  NE2   . GLN A 1 1922 ? 156.241 250.824 229.850 1.00 1.07  ? 1922 GLN A NE2   1 
ATOM   3745  N  N     . LEU A 1 1923 ? 158.451 247.446 227.050 1.00 0.04  ? 1923 LEU A N     1 
ATOM   3746  C  CA    . LEU A 1 1923 ? 157.597 246.499 226.351 1.00 0.05  ? 1923 LEU A CA    1 
ATOM   3747  C  C     . LEU A 1 1923 ? 157.686 245.090 226.919 1.00 0.09  ? 1923 LEU A C     1 
ATOM   3748  O  O     . LEU A 1 1923 ? 157.084 244.171 226.352 1.00 0.31  ? 1923 LEU A O     1 
ATOM   3749  C  CB    . LEU A 1 1923 ? 157.946 246.484 224.860 1.00 0.12  ? 1923 LEU A CB    1 
ATOM   3750  C  CG    . LEU A 1 1923 ? 157.804 247.824 224.130 1.00 0.05  ? 1923 LEU A CG    1 
ATOM   3751  C  CD1   . LEU A 1 1923 ? 158.022 247.661 222.636 1.00 0.03  ? 1923 LEU A CD1   1 
ATOM   3752  C  CD2   . LEU A 1 1923 ? 156.452 248.456 224.414 1.00 0.02  ? 1923 LEU A CD2   1 
ATOM   3753  N  N     . GLY A 1 1924 ? 158.411 244.897 228.015 1.00 0.09  ? 1924 GLY A N     1 
ATOM   3754  C  CA    . GLY A 1 1924 ? 158.549 243.586 228.626 1.00 0.09  ? 1924 GLY A CA    1 
ATOM   3755  C  C     . GLY A 1 1924 ? 159.315 242.586 227.789 1.00 0.09  ? 1924 GLY A C     1 
ATOM   3756  O  O     . GLY A 1 1924 ? 158.996 241.393 227.811 1.00 0.26  ? 1924 GLY A O     1 
ATOM   3757  N  N     . ARG A 1 1925 ? 160.326 243.041 227.063 1.00 0.05  ? 1925 ARG A N     1 
ATOM   3758  C  CA    . ARG A 1 1925 ? 161.105 242.183 226.188 1.00 0.07  ? 1925 ARG A CA    1 
ATOM   3759  C  C     . ARG A 1 1925 ? 162.442 241.838 226.826 1.00 0.06  ? 1925 ARG A C     1 
ATOM   3760  O  O     . ARG A 1 1925 ? 162.985 242.596 227.632 1.00 0.06  ? 1925 ARG A O     1 
ATOM   3761  C  CB    . ARG A 1 1925 ? 161.338 242.852 224.831 1.00 0.06  ? 1925 ARG A CB    1 
ATOM   3762  C  CG    . ARG A 1 1925 ? 160.072 243.277 224.120 1.00 0.06  ? 1925 ARG A CG    1 
ATOM   3763  C  CD    . ARG A 1 1925 ? 159.495 242.146 223.289 1.00 0.19  ? 1925 ARG A CD    1 
ATOM   3764  N  NE    . ARG A 1 1925 ? 158.430 242.595 222.401 1.00 0.39  ? 1925 ARG A NE    1 
ATOM   3765  C  CZ    . ARG A 1 1925 ? 157.223 242.973 222.800 1.00 0.63  ? 1925 ARG A CZ    1 
ATOM   3766  N  NH1   . ARG A 1 1925 ? 156.879 242.959 224.077 1.00 0.42  ? 1925 ARG A NH1   1 
ATOM   3767  N  NH2   . ARG A 1 1925 ? 156.335 243.370 221.895 1.00 0.51  ? 1925 ARG A NH2   1 
ATOM   3768  N  N     . PHE A 1 1926 ? 162.966 240.674 226.453 1.00 0.10  ? 1926 PHE A N     1 
ATOM   3769  C  CA    . PHE A 1 1926 ? 164.312 240.269 226.836 1.00 0.11  ? 1926 PHE A CA    1 
ATOM   3770  C  C     . PHE A 1 1926 ? 165.293 240.955 225.890 1.00 0.03  ? 1926 PHE A C     1 
ATOM   3771  O  O     . PHE A 1 1926 ? 165.357 240.621 224.704 1.00 0.04  ? 1926 PHE A O     1 
ATOM   3772  C  CB    . PHE A 1 1926 ? 164.430 238.746 226.781 1.00 0.22  ? 1926 PHE A CB    1 
ATOM   3773  C  CG    . PHE A 1 1926 ? 165.746 238.202 227.267 1.00 0.33  ? 1926 PHE A CG    1 
ATOM   3774  C  CD1   . PHE A 1 1926 ? 166.661 239.005 227.927 1.00 0.25  ? 1926 PHE A CD1   1 
ATOM   3775  C  CD2   . PHE A 1 1926 ? 166.057 236.865 227.075 1.00 0.53  ? 1926 PHE A CD2   1 
ATOM   3776  C  CE1   . PHE A 1 1926 ? 167.863 238.490 228.372 1.00 0.36  ? 1926 PHE A CE1   1 
ATOM   3777  C  CE2   . PHE A 1 1926 ? 167.256 236.345 227.520 1.00 1.08  ? 1926 PHE A CE2   1 
ATOM   3778  C  CZ    . PHE A 1 1926 ? 168.160 237.157 228.169 1.00 1.25  ? 1926 PHE A CZ    1 
ATOM   3779  N  N     . VAL A 1 1927 ? 166.045 241.919 226.407 1.00 0.02  ? 1927 VAL A N     1 
ATOM   3780  C  CA    . VAL A 1 1927 ? 166.994 242.693 225.615 1.00 0.02  ? 1927 VAL A CA    1 
ATOM   3781  C  C     . VAL A 1 1927 ? 168.387 242.135 225.863 1.00 0.02  ? 1927 VAL A C     1 
ATOM   3782  O  O     . VAL A 1 1927 ? 168.845 242.075 227.010 1.00 0.05  ? 1927 VAL A O     1 
ATOM   3783  C  CB    . VAL A 1 1927 ? 166.931 244.189 225.965 1.00 0.03  ? 1927 VAL A CB    1 
ATOM   3784  C  CG1   . VAL A 1 1927 ? 167.830 244.994 225.036 1.00 0.02  ? 1927 VAL A CG1   1 
ATOM   3785  C  CG2   . VAL A 1 1927 ? 165.504 244.694 225.903 1.00 0.02  ? 1927 VAL A CG2   1 
ATOM   3786  N  N     . LEU A 1 1928 ? 169.063 241.730 224.795 1.00 0.03  ? 1928 LEU A N     1 
ATOM   3787  C  CA    . LEU A 1 1928 ? 170.428 241.232 224.872 1.00 0.03  ? 1928 LEU A CA    1 
ATOM   3788  C  C     . LEU A 1 1928 ? 171.366 242.227 224.207 1.00 0.04  ? 1928 LEU A C     1 
ATOM   3789  O  O     . LEU A 1 1928 ? 171.149 242.622 223.058 1.00 0.09  ? 1928 LEU A O     1 
ATOM   3790  C  CB    . LEU A 1 1928 ? 170.574 239.859 224.212 1.00 0.19  ? 1928 LEU A CB    1 
ATOM   3791  C  CG    . LEU A 1 1928 ? 170.076 238.631 224.979 1.00 0.21  ? 1928 LEU A CG    1 
ATOM   3792  C  CD1   . LEU A 1 1928 ? 168.560 238.569 224.995 1.00 0.11  ? 1928 LEU A CD1   1 
ATOM   3793  C  CD2   . LEU A 1 1928 ? 170.674 237.353 224.423 1.00 0.29  ? 1928 LEU A CD2   1 
ATOM   3794  N  N     . VAL A 1 1929 ? 172.399 242.623 224.934 1.00 0.09  ? 1929 VAL A N     1 
ATOM   3795  C  CA    . VAL A 1 1929 ? 173.407 243.555 224.450 1.00 0.12  ? 1929 VAL A CA    1 
ATOM   3796  C  C     . VAL A 1 1929 ? 174.609 242.753 223.982 1.00 0.11  ? 1929 VAL A C     1 
ATOM   3797  O  O     . VAL A 1 1929 ? 175.037 241.810 224.656 1.00 0.32  ? 1929 VAL A O     1 
ATOM   3798  C  CB    . VAL A 1 1929 ? 173.798 244.561 225.548 1.00 0.29  ? 1929 VAL A CB    1 
ATOM   3799  C  CG1   . VAL A 1 1929 ? 175.104 245.253 225.214 1.00 0.93  ? 1929 VAL A CG1   1 
ATOM   3800  C  CG2   . VAL A 1 1929 ? 172.688 245.573 225.752 1.00 0.16  ? 1929 VAL A CG2   1 
ATOM   3801  N  N     . PHE A 1 1930 ? 175.139 243.104 222.814 1.00 0.16  ? 1930 PHE A N     1 
ATOM   3802  C  CA    . PHE A 1 1930 ? 176.352 242.490 222.288 1.00 0.14  ? 1930 PHE A CA    1 
ATOM   3803  C  C     . PHE A 1 1930 ? 177.363 243.583 221.986 1.00 0.56  ? 1930 PHE A C     1 
ATOM   3804  O  O     . PHE A 1 1930 ? 177.052 244.540 221.271 1.00 0.89  ? 1930 PHE A O     1 
ATOM   3805  C  CB    . PHE A 1 1930 ? 176.057 241.661 221.035 1.00 0.16  ? 1930 PHE A CB    1 
ATOM   3806  C  CG    . PHE A 1 1930 ? 175.054 240.568 221.259 1.00 0.08  ? 1930 PHE A CG    1 
ATOM   3807  C  CD1   . PHE A 1 1930 ? 175.463 239.310 221.658 1.00 0.07  ? 1930 PHE A CD1   1 
ATOM   3808  C  CD2   . PHE A 1 1930 ? 173.703 240.801 221.079 1.00 0.07  ? 1930 PHE A CD2   1 
ATOM   3809  C  CE1   . PHE A 1 1930 ? 174.545 238.304 221.871 1.00 0.12  ? 1930 PHE A CE1   1 
ATOM   3810  C  CE2   . PHE A 1 1930 ? 172.782 239.800 221.292 1.00 0.07  ? 1930 PHE A CE2   1 
ATOM   3811  C  CZ    . PHE A 1 1930 ? 173.204 238.549 221.689 1.00 0.09  ? 1930 PHE A CZ    1 
ATOM   3812  N  N     . ASN A 1 1931 ? 178.561 243.450 222.546 1.00 0.66  ? 1931 ASN A N     1 
ATOM   3813  C  CA    . ASN A 1 1931 ? 179.672 244.349 222.245 1.00 0.48  ? 1931 ASN A CA    1 
ATOM   3814  C  C     . ASN A 1 1931 ? 180.360 243.801 221.002 1.00 0.69  ? 1931 ASN A C     1 
ATOM   3815  O  O     . ASN A 1 1931 ? 181.166 242.873 221.080 1.00 1.68  ? 1931 ASN A O     1 
ATOM   3816  C  CB    . ASN A 1 1931 ? 180.622 244.445 223.433 1.00 0.55  ? 1931 ASN A CB    1 
ATOM   3817  C  CG    . ASN A 1 1931 ? 181.733 245.460 223.232 1.00 0.90  ? 1931 ASN A CG    1 
ATOM   3818  O  OD1   . ASN A 1 1931 ? 182.300 245.590 222.148 1.00 2.32  ? 1931 ASN A OD1   1 
ATOM   3819  N  ND2   . ASN A 1 1931 ? 182.064 246.173 224.295 1.00 0.41  ? 1931 ASN A ND2   1 
ATOM   3820  N  N     . CYS A 1 1932 ? 180.038 244.376 219.851 1.00 0.93  ? 1932 CYS A N     1 
ATOM   3821  C  CA    . CYS A 1 1932 ? 180.511 243.859 218.577 1.00 0.95  ? 1932 CYS A CA    1 
ATOM   3822  C  C     . CYS A 1 1932 ? 181.967 244.234 218.330 1.00 1.38  ? 1932 CYS A C     1 
ATOM   3823  O  O     . CYS A 1 1932 ? 182.438 245.294 218.748 1.00 2.62  ? 1932 CYS A O     1 
ATOM   3824  C  CB    . CYS A 1 1932 ? 179.642 244.394 217.440 1.00 1.06  ? 1932 CYS A CB    1 
ATOM   3825  S  SG    . CYS A 1 1932 ? 177.922 243.867 217.493 1.00 4.43  ? 1932 CYS A SG    1 
ATOM   3826  N  N     . ASP A 1 1933 ? 182.681 243.344 217.644 1.00 1.07  ? 1933 ASP A N     1 
ATOM   3827  C  CA    . ASP A 1 1933 ? 184.008 243.653 217.133 1.00 1.60  ? 1933 ASP A CA    1 
ATOM   3828  C  C     . ASP A 1 1933 ? 184.170 242.985 215.773 1.00 1.91  ? 1933 ASP A C     1 
ATOM   3829  O  O     . ASP A 1 1933 ? 183.216 242.441 215.208 1.00 1.69  ? 1933 ASP A O     1 
ATOM   3830  C  CB    . ASP A 1 1933 ? 185.114 243.231 218.114 1.00 3.07  ? 1933 ASP A CB    1 
ATOM   3831  C  CG    . ASP A 1 1933 ? 185.162 241.731 218.362 1.00 3.55  ? 1933 ASP A CG    1 
ATOM   3832  O  OD1   . ASP A 1 1933 ? 184.324 240.984 217.823 1.00 3.23  ? 1933 ASP A OD1   1 
ATOM   3833  O  OD2   . ASP A 1 1933 ? 186.066 241.291 219.101 1.00 14.37 ? 1933 ASP A OD2   1 
ATOM   3834  N  N     . GLU A 1 1934 ? 185.397 243.025 215.251 1.00 4.84  ? 1934 GLU A N     1 
ATOM   3835  C  CA    . GLU A 1 1934 ? 185.682 242.457 213.939 1.00 2.66  ? 1934 GLU A CA    1 
ATOM   3836  C  C     . GLU A 1 1934 ? 185.548 240.939 213.906 1.00 3.13  ? 1934 GLU A C     1 
ATOM   3837  O  O     . GLU A 1 1934 ? 185.502 240.364 212.815 1.00 7.03  ? 1934 GLU A O     1 
ATOM   3838  C  CB    . GLU A 1 1934 ? 187.084 242.868 213.487 1.00 6.08  ? 1934 GLU A CB    1 
ATOM   3839  C  CG    . GLU A 1 1934 ? 188.213 242.178 214.236 1.00 6.68  ? 1934 GLU A CG    1 
ATOM   3840  C  CD    . GLU A 1 1934 ? 188.484 242.800 215.592 1.00 12.71 ? 1934 GLU A CD    1 
ATOM   3841  O  OE1   . GLU A 1 1934 ? 187.888 243.856 215.893 1.00 14.46 ? 1934 GLU A OE1   1 
ATOM   3842  O  OE2   . GLU A 1 1934 ? 189.289 242.230 216.356 1.00 16.55 ? 1934 GLU A OE2   1 
ATOM   3843  N  N     . THR A 1 1935 ? 185.487 240.279 215.062 1.00 3.17  ? 1935 THR A N     1 
ATOM   3844  C  CA    . THR A 1 1935 ? 185.308 238.833 215.099 1.00 1.70  ? 1935 THR A CA    1 
ATOM   3845  C  C     . THR A 1 1935 ? 183.850 238.410 214.972 1.00 2.03  ? 1935 THR A C     1 
ATOM   3846  O  O     . THR A 1 1935 ? 183.580 237.210 214.864 1.00 2.71  ? 1935 THR A O     1 
ATOM   3847  C  CB    . THR A 1 1935 ? 185.902 238.259 216.387 1.00 2.23  ? 1935 THR A CB    1 
ATOM   3848  O  OG1   . THR A 1 1935 ? 185.140 238.710 217.513 1.00 3.63  ? 1935 THR A OG1   1 
ATOM   3849  C  CG2   . THR A 1 1935 ? 187.345 238.697 216.545 1.00 1.80  ? 1935 THR A CG2   1 
ATOM   3850  N  N     . PHE A 1 1936 ? 182.912 239.353 214.987 1.00 2.58  ? 1936 PHE A N     1 
ATOM   3851  C  CA    . PHE A 1 1936 ? 181.500 239.056 214.747 1.00 1.66  ? 1936 PHE A CA    1 
ATOM   3852  C  C     . PHE A 1 1936 ? 181.303 238.931 213.243 1.00 2.39  ? 1936 PHE A C     1 
ATOM   3853  O  O     . PHE A 1 1936 ? 180.966 239.894 212.554 1.00 7.19  ? 1936 PHE A O     1 
ATOM   3854  C  CB    . PHE A 1 1936 ? 180.608 240.140 215.340 1.00 1.07  ? 1936 PHE A CB    1 
ATOM   3855  C  CG    . PHE A 1 1936 ? 180.380 239.999 216.816 1.00 1.33  ? 1936 PHE A CG    1 
ATOM   3856  C  CD1   . PHE A 1 1936 ? 181.414 240.200 217.715 1.00 0.91  ? 1936 PHE A CD1   1 
ATOM   3857  C  CD2   . PHE A 1 1936 ? 179.126 239.672 217.308 1.00 0.94  ? 1936 PHE A CD2   1 
ATOM   3858  C  CE1   . PHE A 1 1936 ? 181.205 240.073 219.071 1.00 0.72  ? 1936 PHE A CE1   1 
ATOM   3859  C  CE2   . PHE A 1 1936 ? 178.912 239.544 218.664 1.00 0.72  ? 1936 PHE A CE2   1 
ATOM   3860  C  CZ    . PHE A 1 1936 ? 179.952 239.745 219.546 1.00 0.70  ? 1936 PHE A CZ    1 
ATOM   3861  N  N     . ASP A 1 1937 ? 181.527 237.730 212.724 1.00 2.36  ? 1937 ASP A N     1 
ATOM   3862  C  CA    . ASP A 1 1937 ? 181.471 237.493 211.290 1.00 1.54  ? 1937 ASP A CA    1 
ATOM   3863  C  C     . ASP A 1 1937 ? 180.064 237.058 210.877 1.00 1.66  ? 1937 ASP A C     1 
ATOM   3864  O  O     . ASP A 1 1937 ? 179.113 237.101 211.661 1.00 1.63  ? 1937 ASP A O     1 
ATOM   3865  C  CB    . ASP A 1 1937 ? 182.543 236.481 210.883 1.00 1.79  ? 1937 ASP A CB    1 
ATOM   3866  C  CG    . ASP A 1 1937 ? 182.418 235.151 211.614 1.00 4.32  ? 1937 ASP A CG    1 
ATOM   3867  O  OD1   . ASP A 1 1937 ? 181.309 234.784 212.051 1.00 3.36  ? 1937 ASP A OD1   1 
ATOM   3868  O  OD2   . ASP A 1 1937 ? 183.451 234.463 211.749 1.00 15.10 ? 1937 ASP A OD2   1 
ATOM   3869  N  N     . PHE A 1 1938 ? 179.929 236.630 209.620 1.00 1.70  ? 1938 PHE A N     1 
ATOM   3870  C  CA    . PHE A 1 1938 ? 178.629 236.224 209.095 1.00 1.11  ? 1938 PHE A CA    1 
ATOM   3871  C  C     . PHE A 1 1938 ? 178.079 235.015 209.844 1.00 0.87  ? 1938 PHE A C     1 
ATOM   3872  O  O     . PHE A 1 1938 ? 176.885 234.955 210.157 1.00 0.60  ? 1938 PHE A O     1 
ATOM   3873  C  CB    . PHE A 1 1938 ? 178.755 235.938 207.597 1.00 1.17  ? 1938 PHE A CB    1 
ATOM   3874  C  CG    . PHE A 1 1938 ? 177.516 235.362 206.977 1.00 0.83  ? 1938 PHE A CG    1 
ATOM   3875  C  CD1   . PHE A 1 1938 ? 176.486 236.184 206.563 1.00 0.62  ? 1938 PHE A CD1   1 
ATOM   3876  C  CD2   . PHE A 1 1938 ? 177.399 233.997 206.779 1.00 0.77  ? 1938 PHE A CD2   1 
ATOM   3877  C  CE1   . PHE A 1 1938 ? 175.352 235.657 205.983 1.00 0.71  ? 1938 PHE A CE1   1 
ATOM   3878  C  CE2   . PHE A 1 1938 ? 176.267 233.466 206.199 1.00 1.14  ? 1938 PHE A CE2   1 
ATOM   3879  C  CZ    . PHE A 1 1938 ? 175.242 234.297 205.803 1.00 0.73  ? 1938 PHE A CZ    1 
ATOM   3880  N  N     . GLN A 1 1939 ? 178.938 234.040 210.137 1.00 1.57  ? 1939 GLN A N     1 
ATOM   3881  C  CA    . GLN A 1 1939 ? 178.480 232.835 210.823 1.00 1.68  ? 1939 GLN A CA    1 
ATOM   3882  C  C     . GLN A 1 1939 ? 178.129 233.118 212.279 1.00 1.62  ? 1939 GLN A C     1 
ATOM   3883  O  O     . GLN A 1 1939 ? 177.168 232.553 212.810 1.00 1.37  ? 1939 GLN A O     1 
ATOM   3884  C  CB    . GLN A 1 1939 ? 179.542 231.743 210.720 1.00 2.99  ? 1939 GLN A CB    1 
ATOM   3885  C  CG    . GLN A 1 1939 ? 179.837 231.313 209.293 1.00 2.47  ? 1939 GLN A CG    1 
ATOM   3886  C  CD    . GLN A 1 1939 ? 180.916 230.255 209.211 1.00 12.51 ? 1939 GLN A CD    1 
ATOM   3887  O  OE1   . GLN A 1 1939 ? 180.769 229.159 209.749 1.00 17.23 ? 1939 GLN A OE1   1 
ATOM   3888  N  NE2   . GLN A 1 1939 ? 182.013 230.581 208.539 1.00 13.50 ? 1939 GLN A NE2   1 
ATOM   3889  N  N     . ALA A 1 1940 ? 178.902 233.981 212.944 1.00 1.22  ? 1940 ALA A N     1 
ATOM   3890  C  CA    . ALA A 1 1940 ? 178.627 234.295 214.342 1.00 0.76  ? 1940 ALA A CA    1 
ATOM   3891  C  C     . ALA A 1 1940 ? 177.341 235.100 214.483 1.00 0.53  ? 1940 ALA A C     1 
ATOM   3892  O  O     . ALA A 1 1940 ? 176.514 234.819 215.357 1.00 0.28  ? 1940 ALA A O     1 
ATOM   3893  C  CB    . ALA A 1 1940 ? 179.808 235.049 214.955 1.00 0.98  ? 1940 ALA A CB    1 
ATOM   3894  N  N     . MET A 1 1941 ? 177.154 236.106 213.625 1.00 0.72  ? 1941 MET A N     1 
ATOM   3895  C  CA    . MET A 1 1941 ? 175.943 236.918 213.680 1.00 0.64  ? 1941 MET A CA    1 
ATOM   3896  C  C     . MET A 1 1941 ? 174.703 236.083 213.399 1.00 0.58  ? 1941 MET A C     1 
ATOM   3897  O  O     . MET A 1 1941 ? 173.667 236.259 214.052 1.00 2.65  ? 1941 MET A O     1 
ATOM   3898  C  CB    . MET A 1 1941 ? 176.043 238.077 212.688 1.00 0.48  ? 1941 MET A CB    1 
ATOM   3899  C  CG    . MET A 1 1941 ? 177.047 239.147 213.077 1.00 0.94  ? 1941 MET A CG    1 
ATOM   3900  S  SD    . MET A 1 1941 ? 176.582 240.038 214.572 1.00 4.37  ? 1941 MET A SD    1 
ATOM   3901  C  CE    . MET A 1 1941 ? 175.063 240.820 214.039 1.00 0.55  ? 1941 MET A CE    1 
ATOM   3902  N  N     . GLY A 1 1942 ? 174.788 235.167 212.433 1.00 0.27  ? 1942 GLY A N     1 
ATOM   3903  C  CA    . GLY A 1 1942 ? 173.634 234.350 212.098 1.00 0.38  ? 1942 GLY A CA    1 
ATOM   3904  C  C     . GLY A 1 1942 ? 173.190 233.470 213.248 1.00 0.53  ? 1942 GLY A C     1 
ATOM   3905  O  O     . GLY A 1 1942 ? 171.995 233.335 213.517 1.00 0.82  ? 1942 GLY A O     1 
ATOM   3906  N  N     . ARG A 1 1943 ? 174.150 232.858 213.943 1.00 0.45  ? 1943 ARG A N     1 
ATOM   3907  C  CA    . ARG A 1 1943 ? 173.810 232.022 215.090 1.00 0.29  ? 1943 ARG A CA    1 
ATOM   3908  C  C     . ARG A 1 1943 ? 173.167 232.843 216.199 1.00 0.22  ? 1943 ARG A C     1 
ATOM   3909  O  O     . ARG A 1 1943 ? 172.234 232.380 216.863 1.00 0.49  ? 1943 ARG A O     1 
ATOM   3910  C  CB    . ARG A 1 1943 ? 175.057 231.298 215.595 1.00 0.78  ? 1943 ARG A CB    1 
ATOM   3911  C  CG    . ARG A 1 1943 ? 174.771 230.254 216.651 1.00 0.65  ? 1943 ARG A CG    1 
ATOM   3912  C  CD    . ARG A 1 1943 ? 175.956 229.325 216.844 1.00 2.98  ? 1943 ARG A CD    1 
ATOM   3913  N  NE    . ARG A 1 1943 ? 175.834 228.507 218.047 1.00 7.82  ? 1943 ARG A NE    1 
ATOM   3914  C  CZ    . ARG A 1 1943 ? 175.806 228.978 219.286 1.00 4.73  ? 1943 ARG A CZ    1 
ATOM   3915  N  NH1   . ARG A 1 1943 ? 175.948 230.268 219.540 1.00 1.92  ? 1943 ARG A NH1   1 
ATOM   3916  N  NH2   . ARG A 1 1943 ? 175.646 228.133 220.298 1.00 6.80  ? 1943 ARG A NH2   1 
ATOM   3917  N  N     . ILE A 1 1944 ? 173.656 234.064 216.417 1.00 0.16  ? 1944 ILE A N     1 
ATOM   3918  C  CA    . ILE A 1 1944 ? 173.028 234.957 217.387 1.00 0.18  ? 1944 ILE A CA    1 
ATOM   3919  C  C     . ILE A 1 1944 ? 171.607 235.295 216.955 1.00 0.21  ? 1944 ILE A C     1 
ATOM   3920  O  O     . ILE A 1 1944 ? 170.688 235.354 217.783 1.00 0.18  ? 1944 ILE A O     1 
ATOM   3921  C  CB    . ILE A 1 1944 ? 173.888 236.219 217.586 1.00 0.19  ? 1944 ILE A CB    1 
ATOM   3922  C  CG1   . ILE A 1 1944 ? 175.255 235.845 218.163 1.00 0.16  ? 1944 ILE A CG1   1 
ATOM   3923  C  CG2   . ILE A 1 1944 ? 173.178 237.226 218.472 1.00 0.09  ? 1944 ILE A CG2   1 
ATOM   3924  C  CD1   . ILE A 1 1944 ? 176.189 237.020 218.341 1.00 0.19  ? 1944 ILE A CD1   1 
ATOM   3925  N  N     . PHE A 1 1945 ? 171.400 235.517 215.655 1.00 0.21  ? 1945 PHE A N     1 
ATOM   3926  C  CA    . PHE A 1 1945 ? 170.056 235.776 215.153 1.00 0.19  ? 1945 PHE A CA    1 
ATOM   3927  C  C     . PHE A 1 1945 ? 169.144 234.575 215.368 1.00 0.17  ? 1945 PHE A C     1 
ATOM   3928  O  O     . PHE A 1 1945 ? 167.962 234.735 215.688 1.00 0.24  ? 1945 PHE A O     1 
ATOM   3929  C  CB    . PHE A 1 1945 ? 170.107 236.150 213.671 1.00 0.28  ? 1945 PHE A CB    1 
ATOM   3930  C  CG    . PHE A 1 1945 ? 170.647 237.524 213.411 1.00 0.18  ? 1945 PHE A CG    1 
ATOM   3931  C  CD1   . PHE A 1 1945 ? 170.364 238.568 214.276 1.00 0.12  ? 1945 PHE A CD1   1 
ATOM   3932  C  CD2   . PHE A 1 1945 ? 171.439 237.772 212.304 1.00 0.20  ? 1945 PHE A CD2   1 
ATOM   3933  C  CE1   . PHE A 1 1945 ? 170.862 239.833 214.040 1.00 0.08  ? 1945 PHE A CE1   1 
ATOM   3934  C  CE2   . PHE A 1 1945 ? 171.938 239.034 212.065 1.00 0.20  ? 1945 PHE A CE2   1 
ATOM   3935  C  CZ    . PHE A 1 1945 ? 171.650 240.068 212.934 1.00 0.12  ? 1945 PHE A CZ    1 
ATOM   3936  N  N     . VAL A 1 1946 ? 169.677 233.365 215.190 1.00 0.32  ? 1946 VAL A N     1 
ATOM   3937  C  CA    . VAL A 1 1946 ? 168.877 232.159 215.384 1.00 0.51  ? 1946 VAL A CA    1 
ATOM   3938  C  C     . VAL A 1 1946 ? 168.361 232.094 216.815 1.00 0.29  ? 1946 VAL A C     1 
ATOM   3939  O  O     . VAL A 1 1946 ? 167.184 231.807 217.058 1.00 0.95  ? 1946 VAL A O     1 
ATOM   3940  C  CB    . VAL A 1 1946 ? 169.700 230.907 215.018 1.00 0.39  ? 1946 VAL A CB    1 
ATOM   3941  C  CG1   . VAL A 1 1946 ? 168.979 229.644 215.455 1.00 0.18  ? 1946 VAL A CG1   1 
ATOM   3942  C  CG2   . VAL A 1 1946 ? 169.974 230.873 213.530 1.00 0.32  ? 1946 VAL A CG2   1 
ATOM   3943  N  N     . GLY A 1 1947 ? 169.235 232.370 217.784 1.00 0.21  ? 1947 GLY A N     1 
ATOM   3944  C  CA    . GLY A 1 1947 ? 168.795 232.414 219.168 1.00 0.23  ? 1947 GLY A CA    1 
ATOM   3945  C  C     . GLY A 1 1947 ? 167.791 233.521 219.429 1.00 0.32  ? 1947 GLY A C     1 
ATOM   3946  O  O     . GLY A 1 1947 ? 166.783 233.310 220.106 1.00 0.77  ? 1947 GLY A O     1 
ATOM   3947  N  N     . LEU A 1 1948 ? 168.051 234.715 218.892 1.00 0.16  ? 1948 LEU A N     1 
ATOM   3948  C  CA    . LEU A 1 1948 ? 167.133 235.833 219.090 1.00 0.33  ? 1948 LEU A CA    1 
ATOM   3949  C  C     . LEU A 1 1948 ? 165.772 235.553 218.465 1.00 0.42  ? 1948 LEU A C     1 
ATOM   3950  O  O     . LEU A 1 1948 ? 164.734 235.867 219.058 1.00 0.69  ? 1948 LEU A O     1 
ATOM   3951  C  CB    . LEU A 1 1948 ? 167.729 237.113 218.508 1.00 0.28  ? 1948 LEU A CB    1 
ATOM   3952  C  CG    . LEU A 1 1948 ? 168.892 237.782 219.241 1.00 0.21  ? 1948 LEU A CG    1 
ATOM   3953  C  CD1   . LEU A 1 1948 ? 169.514 238.850 218.357 1.00 0.05  ? 1948 LEU A CD1   1 
ATOM   3954  C  CD2   . LEU A 1 1948 ? 168.438 238.372 220.566 1.00 0.05  ? 1948 LEU A CD2   1 
ATOM   3955  N  N     . CYS A 1 1949 ? 165.757 234.968 217.265 1.00 0.28  ? 1949 CYS A N     1 
ATOM   3956  C  CA    . CYS A 1 1949 ? 164.497 234.748 216.561 1.00 0.60  ? 1949 CYS A CA    1 
ATOM   3957  C  C     . CYS A 1 1949 ? 163.609 233.745 217.288 1.00 0.83  ? 1949 CYS A C     1 
ATOM   3958  O  O     . CYS A 1 1949 ? 162.399 233.966 217.419 1.00 1.32  ? 1949 CYS A O     1 
ATOM   3959  C  CB    . CYS A 1 1949 ? 164.769 234.284 215.130 1.00 0.99  ? 1949 CYS A CB    1 
ATOM   3960  S  SG    . CYS A 1 1949 ? 165.314 235.594 214.015 1.00 0.74  ? 1949 CYS A SG    1 
ATOM   3961  N  N     . GLN A 1 1950 ? 164.182 232.639 217.761 1.00 1.14  ? 1950 GLN A N     1 
ATOM   3962  C  CA    . GLN A 1 1950 ? 163.365 231.614 218.402 1.00 1.75  ? 1950 GLN A CA    1 
ATOM   3963  C  C     . GLN A 1 1950 ? 162.929 232.036 219.799 1.00 1.44  ? 1950 GLN A C     1 
ATOM   3964  O  O     . GLN A 1 1950 ? 161.798 231.754 220.212 1.00 4.63  ? 1950 GLN A O     1 
ATOM   3965  C  CB    . GLN A 1 1950 ? 164.122 230.291 218.454 1.00 2.93  ? 1950 GLN A CB    1 
ATOM   3966  C  CG    . GLN A 1 1950 ? 164.572 229.779 217.106 1.00 2.78  ? 1950 GLN A CG    1 
ATOM   3967  C  CD    . GLN A 1 1950 ? 165.087 228.361 217.175 1.00 4.90  ? 1950 GLN A CD    1 
ATOM   3968  O  OE1   . GLN A 1 1950 ? 164.326 227.425 217.412 1.00 14.99 ? 1950 GLN A OE1   1 
ATOM   3969  N  NE2   . GLN A 1 1950 ? 166.387 228.194 216.974 1.00 5.68  ? 1950 GLN A NE2   1 
ATOM   3970  N  N     . VAL A 1 1951 ? 163.812 232.702 220.543 1.00 1.14  ? 1951 VAL A N     1 
ATOM   3971  C  CA    . VAL A 1 1951 ? 163.455 233.164 221.881 1.00 0.69  ? 1951 VAL A CA    1 
ATOM   3972  C  C     . VAL A 1 1951 ? 162.413 234.273 221.802 1.00 0.51  ? 1951 VAL A C     1 
ATOM   3973  O  O     . VAL A 1 1951 ? 161.496 234.343 222.628 1.00 1.32  ? 1951 VAL A O     1 
ATOM   3974  C  CB    . VAL A 1 1951 ? 164.715 233.618 222.643 1.00 1.03  ? 1951 VAL A CB    1 
ATOM   3975  C  CG1   . VAL A 1 1951 ? 164.341 234.379 223.904 1.00 0.46  ? 1951 VAL A CG1   1 
ATOM   3976  C  CG2   . VAL A 1 1951 ? 165.583 232.421 222.984 1.00 0.62  ? 1951 VAL A CG2   1 
ATOM   3977  N  N     . GLY A 1 1952 ? 162.521 235.138 220.800 1.00 1.01  ? 1952 GLY A N     1 
ATOM   3978  C  CA    . GLY A 1 1952 ? 161.722 236.343 220.765 1.00 0.64  ? 1952 GLY A CA    1 
ATOM   3979  C  C     . GLY A 1 1952 ? 162.367 237.508 221.466 1.00 0.28  ? 1952 GLY A C     1 
ATOM   3980  O  O     . GLY A 1 1952 ? 161.663 238.400 221.951 1.00 3.14  ? 1952 GLY A O     1 
ATOM   3981  N  N     . ALA A 1 1953 ? 163.689 237.526 221.544 1.00 0.26  ? 1953 ALA A N     1 
ATOM   3982  C  CA    . ALA A 1 1953 ? 164.434 238.523 222.292 1.00 0.32  ? 1953 ALA A CA    1 
ATOM   3983  C  C     . ALA A 1 1953 ? 164.950 239.619 221.370 1.00 0.09  ? 1953 ALA A C     1 
ATOM   3984  O  O     . ALA A 1 1953 ? 165.108 239.431 220.163 1.00 0.30  ? 1953 ALA A O     1 
ATOM   3985  C  CB    . ALA A 1 1953 ? 165.597 237.865 223.036 1.00 0.19  ? 1953 ALA A CB    1 
ATOM   3986  N  N     . TRP A 1 1954 ? 165.206 240.779 221.963 1.00 0.07  ? 1954 TRP A N     1 
ATOM   3987  C  CA    . TRP A 1 1954 ? 165.760 241.917 221.246 1.00 0.03  ? 1954 TRP A CA    1 
ATOM   3988  C  C     . TRP A 1 1954 ? 167.280 241.831 221.247 1.00 0.03  ? 1954 TRP A C     1 
ATOM   3989  O  O     . TRP A 1 1954 ? 167.891 241.572 222.288 1.00 0.04  ? 1954 TRP A O     1 
ATOM   3990  C  CB    . TRP A 1 1954 ? 165.311 243.232 221.883 1.00 0.04  ? 1954 TRP A CB    1 
ATOM   3991  C  CG    . TRP A 1 1954 ? 163.912 243.639 221.553 1.00 0.06  ? 1954 TRP A CG    1 
ATOM   3992  C  CD1   . TRP A 1 1954 ? 162.909 242.836 221.110 1.00 0.03  ? 1954 TRP A CD1   1 
ATOM   3993  C  CD2   . TRP A 1 1954 ? 163.358 244.952 221.661 1.00 0.05  ? 1954 TRP A CD2   1 
ATOM   3994  N  NE1   . TRP A 1 1954 ? 161.764 243.567 220.927 1.00 0.01  ? 1954 TRP A NE1   1 
ATOM   3995  C  CE2   . TRP A 1 1954 ? 162.014 244.871 221.260 1.00 0.02  ? 1954 TRP A CE2   1 
ATOM   3996  C  CE3   . TRP A 1 1954 ? 163.870 246.190 222.058 1.00 0.00  ? 1954 TRP A CE3   1 
ATOM   3997  C  CZ2   . TRP A 1 1954 ? 161.175 245.979 221.241 1.00 0.02  ? 1954 TRP A CZ2   1 
ATOM   3998  C  CZ3   . TRP A 1 1954 ? 163.037 247.286 222.039 1.00 0.02  ? 1954 TRP A CZ3   1 
ATOM   3999  C  CH2   . TRP A 1 1954 ? 161.704 247.175 221.636 1.00 0.02  ? 1954 TRP A CH2   1 
ATOM   4000  N  N     . GLY A 1 1955 ? 167.880 242.049 220.086 1.00 0.03  ? 1955 GLY A N     1 
ATOM   4001  C  CA    . GLY A 1 1955 ? 169.321 242.122 219.991 1.00 0.03  ? 1955 GLY A CA    1 
ATOM   4002  C  C     . GLY A 1 1955 ? 169.807 243.543 219.817 1.00 0.05  ? 1955 GLY A C     1 
ATOM   4003  O  O     . GLY A 1 1955 ? 169.553 244.171 218.785 1.00 0.03  ? 1955 GLY A O     1 
ATOM   4004  N  N     . CYS A 1 1956 ? 170.492 244.072 220.825 1.00 0.03  ? 1956 CYS A N     1 
ATOM   4005  C  CA    . CYS A 1 1956 ? 171.094 245.399 220.755 1.00 0.02  ? 1956 CYS A CA    1 
ATOM   4006  C  C     . CYS A 1 1956 ? 172.581 245.210 220.479 1.00 0.05  ? 1956 CYS A C     1 
ATOM   4007  O  O     . CYS A 1 1956 ? 173.354 244.876 221.378 1.00 0.25  ? 1956 CYS A O     1 
ATOM   4008  C  CB    . CYS A 1 1956 ? 170.850 246.182 222.043 1.00 0.08  ? 1956 CYS A CB    1 
ATOM   4009  S  SG    . CYS A 1 1956 ? 171.630 247.813 222.077 1.00 2.56  ? 1956 CYS A SG    1 
ATOM   4010  N  N     . PHE A 1 1957 ? 172.964 245.413 219.219 1.00 0.05  ? 1957 PHE A N     1 
ATOM   4011  C  CA    . PHE A 1 1957 ? 174.380 245.255 218.800 1.00 0.17  ? 1957 PHE A CA    1 
ATOM   4012  C  C     . PHE A 1 1957 ? 175.086 246.604 218.878 1.00 0.26  ? 1957 PHE A C     1 
ATOM   4013  O  O     . PHE A 1 1957 ? 174.974 247.413 217.940 1.00 0.40  ? 1957 PHE A O     1 
ATOM   4014  C  CB    . PHE A 1 1957 ? 174.367 244.629 217.402 1.00 0.09  ? 1957 PHE A CB    1 
ATOM   4015  C  CG    . PHE A 1 1957 ? 173.741 243.243 217.359 1.00 0.03  ? 1957 PHE A CG    1 
ATOM   4016  C  CD1   . PHE A 1 1957 ? 172.372 243.084 217.185 1.00 0.02  ? 1957 PHE A CD1   1 
ATOM   4017  C  CD2   . PHE A 1 1957 ? 174.525 242.103 217.498 1.00 0.04  ? 1957 PHE A CD2   1 
ATOM   4018  C  CE1   . PHE A 1 1957 ? 171.805 241.821 217.150 1.00 0.02  ? 1957 PHE A CE1   1 
ATOM   4019  C  CE2   . PHE A 1 1957 ? 173.952 240.842 217.461 1.00 0.04  ? 1957 PHE A CE2   1 
ATOM   4020  C  CZ    . PHE A 1 1957 ? 172.595 240.705 217.286 1.00 0.04  ? 1957 PHE A CZ    1 
ATOM   4021  N  N     . ASP A 1 1958 ? 175.820 246.832 219.970 1.00 0.76  ? 1958 ASP A N     1 
ATOM   4022  C  CA    . ASP A 1 1958 ? 176.549 248.113 220.170 1.00 0.59  ? 1958 ASP A CA    1 
ATOM   4023  C  C     . ASP A 1 1958 ? 177.875 248.079 219.405 1.00 1.43  ? 1958 ASP A C     1 
ATOM   4024  O  O     . ASP A 1 1958 ? 178.363 246.966 219.123 1.00 1.92  ? 1958 ASP A O     1 
ATOM   4025  C  CB    . ASP A 1 1958 ? 176.718 248.396 221.654 1.00 1.44  ? 1958 ASP A CB    1 
ATOM   4026  C  CG    . ASP A 1 1958 ? 175.426 248.385 222.458 1.00 4.14  ? 1958 ASP A CG    1 
ATOM   4027  O  OD1   . ASP A 1 1958 ? 174.519 249.172 222.121 1.00 5.32  ? 1958 ASP A OD1   1 
ATOM   4028  O  OD2   . ASP A 1 1958 ? 175.336 247.588 223.411 1.00 8.53  ? 1958 ASP A OD2   1 
ATOM   4029  N  N     . GLU A 1 1959 ? 178.433 249.252 219.089 1.00 2.33  ? 1959 GLU A N     1 
ATOM   4030  C  CA    . GLU A 1 1959 ? 179.689 249.320 218.293 1.00 1.70  ? 1959 GLU A CA    1 
ATOM   4031  C  C     . GLU A 1 1959 ? 179.521 248.409 217.069 1.00 1.12  ? 1959 GLU A C     1 
ATOM   4032  O  O     . GLU A 1 1959 ? 180.482 247.689 216.729 1.00 1.35  ? 1959 GLU A O     1 
ATOM   4033  C  CB    . GLU A 1 1959 ? 180.884 248.971 219.182 1.00 1.90  ? 1959 GLU A CB    1 
ATOM   4034  C  CG    . GLU A 1 1959 ? 181.053 249.934 220.353 1.00 6.64  ? 1959 GLU A CG    1 
ATOM   4035  C  CD    . GLU A 1 1959 ? 180.349 249.521 221.633 1.00 13.61 ? 1959 GLU A CD    1 
ATOM   4036  O  OE1   . GLU A 1 1959 ? 179.846 248.379 221.698 1.00 15.15 ? 1959 GLU A OE1   1 
ATOM   4037  O  OE2   . GLU A 1 1959 ? 180.287 250.355 222.562 1.00 17.15 ? 1959 GLU A OE2   1 
ATOM   4038  N  N     . PHE A 1 1960 ? 178.346 248.452 216.434 1.00 0.92  ? 1960 PHE A N     1 
ATOM   4039  C  CA    . PHE A 1 1960 ? 178.051 247.580 215.302 1.00 0.53  ? 1960 PHE A CA    1 
ATOM   4040  C  C     . PHE A 1 1960 ? 178.923 247.896 214.095 1.00 0.92  ? 1960 PHE A C     1 
ATOM   4041  O  O     . PHE A 1 1960 ? 179.154 247.020 213.254 1.00 0.71  ? 1960 PHE A O     1 
ATOM   4042  C  CB    . PHE A 1 1960 ? 176.567 247.692 214.959 1.00 0.29  ? 1960 PHE A CB    1 
ATOM   4043  C  CG    . PHE A 1 1960 ? 176.129 246.829 213.815 1.00 0.22  ? 1960 PHE A CG    1 
ATOM   4044  C  CD1   . PHE A 1 1960 ? 175.924 245.474 213.993 1.00 0.16  ? 1960 PHE A CD1   1 
ATOM   4045  C  CD2   . PHE A 1 1960 ? 175.864 247.385 212.577 1.00 0.14  ? 1960 PHE A CD2   1 
ATOM   4046  C  CE1   . PHE A 1 1960 ? 175.504 244.683 212.949 1.00 0.08  ? 1960 PHE A CE1   1 
ATOM   4047  C  CE2   . PHE A 1 1960 ? 175.437 246.597 211.532 1.00 0.19  ? 1960 PHE A CE2   1 
ATOM   4048  C  CZ    . PHE A 1 1960 ? 175.258 245.245 211.718 1.00 0.11  ? 1960 PHE A CZ    1 
ATOM   4049  N  N     . ASN A 1 1961 ? 179.432 249.123 213.997 1.00 1.41  ? 1961 ASN A N     1 
ATOM   4050  C  CA    . ASN A 1 1961 ? 180.325 249.486 212.907 1.00 0.73  ? 1961 ASN A CA    1 
ATOM   4051  C  C     . ASN A 1 1961 ? 181.765 249.059 213.156 1.00 0.67  ? 1961 ASN A C     1 
ATOM   4052  O  O     . ASN A 1 1961 ? 182.648 249.435 212.381 1.00 1.22  ? 1961 ASN A O     1 
ATOM   4053  C  CB    . ASN A 1 1961 ? 180.265 250.993 212.639 1.00 1.83  ? 1961 ASN A CB    1 
ATOM   4054  C  CG    . ASN A 1 1961 ? 180.547 251.825 213.874 1.00 3.10  ? 1961 ASN A CG    1 
ATOM   4055  O  OD1   . ASN A 1 1961 ? 180.740 251.297 214.968 1.00 3.73  ? 1961 ASN A OD1   1 
ATOM   4056  N  ND2   . ASN A 1 1961 ? 180.586 253.139 213.699 1.00 4.09  ? 1961 ASN A ND2   1 
ATOM   4057  N  N     . ARG A 1 1962 ? 182.028 248.304 214.223 1.00 1.53  ? 1962 ARG A N     1 
ATOM   4058  C  CA    . ARG A 1 1962 ? 183.340 247.700 214.405 1.00 1.42  ? 1962 ARG A CA    1 
ATOM   4059  C  C     . ARG A 1 1962 ? 183.486 246.396 213.635 1.00 1.11  ? 1962 ARG A C     1 
ATOM   4060  O  O     . ARG A 1 1962 ? 184.597 245.864 213.551 1.00 2.11  ? 1962 ARG A O     1 
ATOM   4061  C  CB    . ARG A 1 1962 ? 183.614 247.477 215.897 1.00 1.05  ? 1962 ARG A CB    1 
ATOM   4062  C  CG    . ARG A 1 1962 ? 183.666 248.781 216.682 1.00 2.36  ? 1962 ARG A CG    1 
ATOM   4063  C  CD    . ARG A 1 1962 ? 184.646 248.765 217.848 1.00 2.73  ? 1962 ARG A CD    1 
ATOM   4064  N  NE    . ARG A 1 1962 ? 184.394 247.694 218.804 1.00 2.07  ? 1962 ARG A NE    1 
ATOM   4065  C  CZ    . ARG A 1 1962 ? 185.302 246.811 219.196 1.00 1.25  ? 1962 ARG A CZ    1 
ATOM   4066  N  NH1   . ARG A 1 1962 ? 186.547 246.858 218.752 1.00 1.16  ? 1962 ARG A NH1   1 
ATOM   4067  N  NH2   . ARG A 1 1962 ? 184.955 245.866 220.064 1.00 1.68  ? 1962 ARG A NH2   1 
ATOM   4068  N  N     . LEU A 1 1963 ? 182.399 245.877 213.068 1.00 1.04  ? 1963 LEU A N     1 
ATOM   4069  C  CA    . LEU A 1 1963 ? 182.488 244.763 212.138 1.00 0.79  ? 1963 LEU A CA    1 
ATOM   4070  C  C     . LEU A 1 1963 ? 183.206 245.194 210.867 1.00 1.58  ? 1963 LEU A C     1 
ATOM   4071  O  O     . LEU A 1 1963 ? 183.214 246.370 210.502 1.00 1.90  ? 1963 LEU A O     1 
ATOM   4072  C  CB    . LEU A 1 1963 ? 181.095 244.245 211.778 1.00 0.90  ? 1963 LEU A CB    1 
ATOM   4073  C  CG    . LEU A 1 1963 ? 180.422 243.171 212.633 1.00 0.94  ? 1963 LEU A CG    1 
ATOM   4074  C  CD1   . LEU A 1 1963 ? 180.139 243.672 214.031 1.00 1.10  ? 1963 LEU A CD1   1 
ATOM   4075  C  CD2   . LEU A 1 1963 ? 179.144 242.699 211.963 1.00 0.43  ? 1963 LEU A CD2   1 
ATOM   4076  N  N     . GLU A 1 1964 ? 183.819 244.227 210.192 1.00 3.93  ? 1964 GLU A N     1 
ATOM   4077  C  CA    . GLU A 1 1964 ? 184.415 244.511 208.895 1.00 3.14  ? 1964 GLU A CA    1 
ATOM   4078  C  C     . GLU A 1 1964 ? 183.331 244.846 207.877 1.00 1.54  ? 1964 GLU A C     1 
ATOM   4079  O  O     . GLU A 1 1964 ? 182.186 244.399 207.984 1.00 1.90  ? 1964 GLU A O     1 
ATOM   4080  C  CB    . GLU A 1 1964 ? 185.250 243.323 208.421 1.00 3.99  ? 1964 GLU A CB    1 
ATOM   4081  C  CG    . GLU A 1 1964 ? 186.471 243.061 209.280 1.00 4.24  ? 1964 GLU A CG    1 
ATOM   4082  C  CD    . GLU A 1 1964 ? 187.489 244.186 209.186 1.00 19.53 ? 1964 GLU A CD    1 
ATOM   4083  O  OE1   . GLU A 1 1964 ? 187.583 244.812 208.110 1.00 20.69 ? 1964 GLU A OE1   1 
ATOM   4084  O  OE2   . GLU A 1 1964 ? 188.189 244.444 210.185 1.00 21.24 ? 1964 GLU A OE2   1 
ATOM   4085  N  N     . GLU A 1 1965 ? 183.700 245.657 206.882 1.00 1.82  ? 1965 GLU A N     1 
ATOM   4086  C  CA    . GLU A 1 1965 ? 182.728 246.086 205.881 1.00 1.11  ? 1965 GLU A CA    1 
ATOM   4087  C  C     . GLU A 1 1965 ? 182.179 244.902 205.095 1.00 0.94  ? 1965 GLU A C     1 
ATOM   4088  O  O     . GLU A 1 1965 ? 180.987 244.865 204.771 1.00 1.12  ? 1965 GLU A O     1 
ATOM   4089  C  CB    . GLU A 1 1965 ? 183.352 247.113 204.938 1.00 1.75  ? 1965 GLU A CB    1 
ATOM   4090  C  CG    . GLU A 1 1965 ? 183.716 248.421 205.608 1.00 5.18  ? 1965 GLU A CG    1 
ATOM   4091  C  CD    . GLU A 1 1965 ? 183.920 249.553 204.623 1.00 15.33 ? 1965 GLU A CD    1 
ATOM   4092  O  OE1   . GLU A 1 1965 ? 184.160 250.694 205.071 1.00 7.57  ? 1965 GLU A OE1   1 
ATOM   4093  O  OE2   . GLU A 1 1965 ? 183.838 249.304 203.402 1.00 21.70 ? 1965 GLU A OE2   1 
ATOM   4094  N  N     . ARG A 1 1966 ? 183.031 243.923 204.778 1.00 0.99  ? 1966 ARG A N     1 
ATOM   4095  C  CA    . ARG A 1 1966 ? 182.548 242.733 204.087 1.00 1.26  ? 1966 ARG A CA    1 
ATOM   4096  C  C     . ARG A 1 1966 ? 181.548 241.959 204.935 1.00 1.08  ? 1966 ARG A C     1 
ATOM   4097  O  O     . ARG A 1 1966 ? 180.584 241.401 204.399 1.00 0.81  ? 1966 ARG A O     1 
ATOM   4098  C  CB    . ARG A 1 1966 ? 183.724 241.839 203.681 1.00 3.39  ? 1966 ARG A CB    1 
ATOM   4099  C  CG    . ARG A 1 1966 ? 184.536 241.259 204.831 1.00 2.10  ? 1966 ARG A CG    1 
ATOM   4100  C  CD    . ARG A 1 1966 ? 185.845 240.667 204.329 1.00 5.63  ? 1966 ARG A CD    1 
ATOM   4101  N  NE    . ARG A 1 1966 ? 186.537 239.892 205.353 1.00 6.89  ? 1966 ARG A NE    1 
ATOM   4102  C  CZ    . ARG A 1 1966 ? 186.519 238.569 205.430 1.00 8.93  ? 1966 ARG A CZ    1 
ATOM   4103  N  NH1   . ARG A 1 1966 ? 185.848 237.834 204.559 1.00 7.37  ? 1966 ARG A NH1   1 
ATOM   4104  N  NH2   . ARG A 1 1966 ? 187.187 237.968 206.410 1.00 23.47 ? 1966 ARG A NH2   1 
ATOM   4105  N  N     . MET A 1 1967 ? 181.745 241.925 206.254 1.00 2.25  ? 1967 MET A N     1 
ATOM   4106  C  CA    . MET A 1 1967 ? 180.799 241.229 207.119 1.00 1.16  ? 1967 MET A CA    1 
ATOM   4107  C  C     . MET A 1 1967 ? 179.485 241.989 207.246 1.00 0.46  ? 1967 MET A C     1 
ATOM   4108  O  O     . MET A 1 1967 ? 178.423 241.368 207.356 1.00 0.30  ? 1967 MET A O     1 
ATOM   4109  C  CB    . MET A 1 1967 ? 181.419 240.998 208.497 1.00 0.95  ? 1967 MET A CB    1 
ATOM   4110  C  CG    . MET A 1 1967 ? 182.370 239.822 208.548 1.00 1.19  ? 1967 MET A CG    1 
ATOM   4111  S  SD    . MET A 1 1967 ? 181.829 238.443 207.520 1.00 8.49  ? 1967 MET A SD    1 
ATOM   4112  C  CE    . MET A 1 1967 ? 183.353 237.524 207.362 1.00 2.70  ? 1967 MET A CE    1 
ATOM   4113  N  N     . LEU A 1 1968 ? 179.535 243.321 207.232 1.00 0.87  ? 1968 LEU A N     1 
ATOM   4114  C  CA    . LEU A 1 1968 ? 178.308 244.109 207.296 1.00 0.64  ? 1968 LEU A CA    1 
ATOM   4115  C  C     . LEU A 1 1968 ? 177.425 243.849 206.084 1.00 0.55  ? 1968 LEU A C     1 
ATOM   4116  O  O     . LEU A 1 1968 ? 176.202 243.723 206.215 1.00 0.53  ? 1968 LEU A O     1 
ATOM   4117  C  CB    . LEU A 1 1968 ? 178.642 245.596 207.409 1.00 0.73  ? 1968 LEU A CB    1 
ATOM   4118  C  CG    . LEU A 1 1968 ? 179.348 246.017 208.697 1.00 0.85  ? 1968 LEU A CG    1 
ATOM   4119  C  CD1   . LEU A 1 1968 ? 179.901 247.426 208.574 1.00 1.58  ? 1968 LEU A CD1   1 
ATOM   4120  C  CD2   . LEU A 1 1968 ? 178.408 245.903 209.885 1.00 0.47  ? 1968 LEU A CD2   1 
ATOM   4121  N  N     . SER A 1 1969 ? 178.026 243.769 204.895 1.00 0.67  ? 1969 SER A N     1 
ATOM   4122  C  CA    . SER A 1 1969 ? 177.260 243.448 203.697 1.00 0.56  ? 1969 SER A CA    1 
ATOM   4123  C  C     . SER A 1 1969 ? 176.634 242.064 203.800 1.00 0.61  ? 1969 SER A C     1 
ATOM   4124  O  O     . SER A 1 1969 ? 175.448 241.887 203.499 1.00 1.29  ? 1969 SER A O     1 
ATOM   4125  C  CB    . SER A 1 1969 ? 178.155 243.544 202.463 1.00 0.49  ? 1969 SER A CB    1 
ATOM   4126  O  OG    . SER A 1 1969 ? 177.533 242.970 201.328 1.00 2.22  ? 1969 SER A OG    1 
ATOM   4127  N  N     . ALA A 1 1970 ? 177.412 241.076 204.246 1.00 0.83  ? 1970 ALA A N     1 
ATOM   4128  C  CA    . ALA A 1 1970 ? 176.899 239.715 204.358 1.00 0.95  ? 1970 ALA A CA    1 
ATOM   4129  C  C     . ALA A 1 1970 ? 175.765 239.627 205.373 1.00 0.52  ? 1970 ALA A C     1 
ATOM   4130  O  O     . ALA A 1 1970 ? 174.769 238.932 205.142 1.00 1.09  ? 1970 ALA A O     1 
ATOM   4131  C  CB    . ALA A 1 1970 ? 178.032 238.765 204.737 1.00 0.91  ? 1970 ALA A CB    1 
ATOM   4132  N  N     . VAL A 1 1971 ? 175.904 240.321 206.503 1.00 0.33  ? 1971 VAL A N     1 
ATOM   4133  C  CA    . VAL A 1 1971 ? 174.888 240.265 207.550 1.00 0.74  ? 1971 VAL A CA    1 
ATOM   4134  C  C     . VAL A 1 1971 ? 173.577 240.879 207.069 1.00 0.50  ? 1971 VAL A C     1 
ATOM   4135  O  O     . VAL A 1 1971 ? 172.493 240.452 207.488 1.00 0.41  ? 1971 VAL A O     1 
ATOM   4136  C  CB    . VAL A 1 1971 ? 175.423 240.944 208.827 1.00 0.38  ? 1971 VAL A CB    1 
ATOM   4137  C  CG1   . VAL A 1 1971 ? 174.293 241.359 209.757 1.00 0.39  ? 1971 VAL A CG1   1 
ATOM   4138  C  CG2   . VAL A 1 1971 ? 176.378 240.010 209.547 1.00 0.31  ? 1971 VAL A CG2   1 
ATOM   4139  N  N     . SER A 1 1972 ? 173.649 241.861 206.165 1.00 0.41  ? 1972 SER A N     1 
ATOM   4140  C  CA    . SER A 1 1972 ? 172.444 242.510 205.656 1.00 0.61  ? 1972 SER A CA    1 
ATOM   4141  C  C     . SER A 1 1972 ? 171.468 241.511 205.044 1.00 0.85  ? 1972 SER A C     1 
ATOM   4142  O  O     . SER A 1 1972 ? 170.253 241.731 205.086 1.00 0.69  ? 1972 SER A O     1 
ATOM   4143  C  CB    . SER A 1 1972 ? 172.823 243.576 204.629 1.00 0.46  ? 1972 SER A CB    1 
ATOM   4144  O  OG    . SER A 1 1972 ? 173.427 242.994 203.490 1.00 0.58  ? 1972 SER A OG    1 
ATOM   4145  N  N     . GLN A 1 1973 ? 171.975 240.418 204.472 1.00 2.07  ? 1973 GLN A N     1 
ATOM   4146  C  CA    . GLN A 1 1973 ? 171.087 239.389 203.943 1.00 1.39  ? 1973 GLN A CA    1 
ATOM   4147  C  C     . GLN A 1 1973 ? 170.293 238.714 205.056 1.00 1.71  ? 1973 GLN A C     1 
ATOM   4148  O  O     . GLN A 1 1973 ? 169.088 238.481 204.913 1.00 1.23  ? 1973 GLN A O     1 
ATOM   4149  C  CB    . GLN A 1 1973 ? 171.894 238.361 203.150 1.00 1.77  ? 1973 GLN A CB    1 
ATOM   4150  C  CG    . GLN A 1 1973 ? 171.064 237.504 202.209 1.00 5.21  ? 1973 GLN A CG    1 
ATOM   4151  C  CD    . GLN A 1 1973 ? 170.402 236.335 202.910 1.00 13.53 ? 1973 GLN A CD    1 
ATOM   4152  O  OE1   . GLN A 1 1973 ? 171.075 235.489 203.496 1.00 16.89 ? 1973 GLN A OE1   1 
ATOM   4153  N  NE2   . GLN A 1 1973 ? 169.076 236.281 202.850 1.00 13.25 ? 1973 GLN A NE2   1 
ATOM   4154  N  N     . GLN A 1 1974 ? 170.951 238.391 206.172 1.00 3.26  ? 1974 GLN A N     1 
ATOM   4155  C  CA    . GLN A 1 1974 ? 170.249 237.760 207.285 1.00 0.79  ? 1974 GLN A CA    1 
ATOM   4156  C  C     . GLN A 1 1974 ? 169.244 238.714 207.917 1.00 0.68  ? 1974 GLN A C     1 
ATOM   4157  O  O     . GLN A 1 1974 ? 168.134 238.305 208.276 1.00 1.35  ? 1974 GLN A O     1 
ATOM   4158  C  CB    . GLN A 1 1974 ? 171.250 237.268 208.330 1.00 0.65  ? 1974 GLN A CB    1 
ATOM   4159  C  CG    . GLN A 1 1974 ? 172.440 236.539 207.741 1.00 0.95  ? 1974 GLN A CG    1 
ATOM   4160  C  CD    . GLN A 1 1974 ? 173.416 236.062 208.795 1.00 0.56  ? 1974 GLN A CD    1 
ATOM   4161  O  OE1   . GLN A 1 1974 ? 173.752 234.881 208.856 1.00 0.90  ? 1974 GLN A OE1   1 
ATOM   4162  N  NE2   . GLN A 1 1974 ? 173.881 236.980 209.629 1.00 0.74  ? 1974 GLN A NE2   1 
ATOM   4163  N  N     . VAL A 1 1975 ? 169.615 239.986 208.068 1.00 1.01  ? 1975 VAL A N     1 
ATOM   4164  C  CA    . VAL A 1 1975 ? 168.698 240.960 208.652 1.00 0.78  ? 1975 VAL A CA    1 
ATOM   4165  C  C     . VAL A 1 1975 ? 167.464 241.112 207.776 1.00 1.13  ? 1975 VAL A C     1 
ATOM   4166  O  O     . VAL A 1 1975 ? 166.337 241.225 208.275 1.00 1.64  ? 1975 VAL A O     1 
ATOM   4167  C  CB    . VAL A 1 1975 ? 169.413 242.308 208.868 1.00 0.57  ? 1975 VAL A CB    1 
ATOM   4168  C  CG1   . VAL A 1 1975 ? 168.419 243.383 209.295 1.00 0.38  ? 1975 VAL A CG1   1 
ATOM   4169  C  CG2   . VAL A 1 1975 ? 170.521 242.162 209.897 1.00 0.17  ? 1975 VAL A CG2   1 
ATOM   4170  N  N     . GLN A 1 1976 ? 167.655 241.104 206.456 1.00 1.11  ? 1976 GLN A N     1 
ATOM   4171  C  CA    . GLN A 1 1976 ? 166.531 241.275 205.544 1.00 0.95  ? 1976 GLN A CA    1 
ATOM   4172  C  C     . GLN A 1 1976 ? 165.555 240.107 205.621 1.00 2.25  ? 1976 GLN A C     1 
ATOM   4173  O  O     . GLN A 1 1976 ? 164.337 240.315 205.682 1.00 5.66  ? 1976 GLN A O     1 
ATOM   4174  C  CB    . GLN A 1 1976 ? 167.040 241.460 204.118 1.00 2.48  ? 1976 GLN A CB    1 
ATOM   4175  C  CG    . GLN A 1 1976 ? 166.034 242.106 203.187 1.00 6.04  ? 1976 GLN A CG    1 
ATOM   4176  C  CD    . GLN A 1 1976 ? 166.649 242.529 201.872 1.00 9.92  ? 1976 GLN A CD    1 
ATOM   4177  O  OE1   . GLN A 1 1976 ? 166.683 243.714 201.542 1.00 14.40 ? 1976 GLN A OE1   1 
ATOM   4178  N  NE2   . GLN A 1 1976 ? 167.151 241.560 201.115 1.00 9.01  ? 1976 GLN A NE2   1 
ATOM   4179  N  N     . CYS A 1 1977 ? 166.061 238.870 205.632 1.00 2.64  ? 1977 CYS A N     1 
ATOM   4180  C  CA    . CYS A 1 1977 ? 165.161 237.718 205.598 1.00 2.24  ? 1977 CYS A CA    1 
ATOM   4181  C  C     . CYS A 1 1977 ? 164.349 237.615 206.884 1.00 2.34  ? 1977 CYS A C     1 
ATOM   4182  O  O     . CYS A 1 1977 ? 163.184 237.201 206.857 1.00 4.43  ? 1977 CYS A O     1 
ATOM   4183  C  CB    . CYS A 1 1977 ? 165.942 236.425 205.348 1.00 2.19  ? 1977 CYS A CB    1 
ATOM   4184  S  SG    . CYS A 1 1977 ? 167.107 235.946 206.634 1.00 32.26 ? 1977 CYS A SG    1 
ATOM   4185  N  N     . ILE A 1 1978 ? 164.945 237.984 208.019 1.00 1.44  ? 1978 ILE A N     1 
ATOM   4186  C  CA    . ILE A 1 1978 ? 164.192 238.033 209.268 1.00 1.78  ? 1978 ILE A CA    1 
ATOM   4187  C  C     . ILE A 1 1978 ? 163.084 239.074 209.177 1.00 1.89  ? 1978 ILE A C     1 
ATOM   4188  O  O     . ILE A 1 1978 ? 161.950 238.837 209.606 1.00 2.66  ? 1978 ILE A O     1 
ATOM   4189  C  CB    . ILE A 1 1978 ? 165.132 238.308 210.457 1.00 2.64  ? 1978 ILE A CB    1 
ATOM   4190  C  CG1   . ILE A 1 1978 ? 166.087 237.132 210.674 1.00 0.59  ? 1978 ILE A CG1   1 
ATOM   4191  C  CG2   . ILE A 1 1978 ? 164.338 238.602 211.720 1.00 1.17  ? 1978 ILE A CG2   1 
ATOM   4192  C  CD1   . ILE A 1 1978 ? 167.399 237.525 211.309 1.00 0.55  ? 1978 ILE A CD1   1 
ATOM   4193  N  N     . GLN A 1 1979 ? 163.395 240.240 208.607 1.00 2.08  ? 1979 GLN A N     1 
ATOM   4194  C  CA    . GLN A 1 1979 ? 162.411 241.313 208.521 1.00 2.23  ? 1979 GLN A CA    1 
ATOM   4195  C  C     . GLN A 1 1979 ? 161.240 240.927 207.623 1.00 3.88  ? 1979 GLN A C     1 
ATOM   4196  O  O     . GLN A 1 1979 ? 160.092 241.288 207.906 1.00 7.10  ? 1979 GLN A O     1 
ATOM   4197  C  CB    . GLN A 1 1979 ? 163.082 242.595 208.031 1.00 2.01  ? 1979 GLN A CB    1 
ATOM   4198  C  CG    . GLN A 1 1979 ? 163.885 243.298 209.110 1.00 1.73  ? 1979 GLN A CG    1 
ATOM   4199  C  CD    . GLN A 1 1979 ? 164.616 244.519 208.603 1.00 0.81  ? 1979 GLN A CD    1 
ATOM   4200  O  OE1   . GLN A 1 1979 ? 164.598 244.819 207.414 1.00 2.86  ? 1979 GLN A OE1   1 
ATOM   4201  N  NE2   . GLN A 1 1979 ? 165.265 245.233 209.509 1.00 0.42  ? 1979 GLN A NE2   1 
ATOM   4202  N  N     . GLU A 1 1980 ? 161.508 240.199 206.533 1.00 3.87  ? 1980 GLU A N     1 
ATOM   4203  C  CA    . GLU A 1 1980 ? 160.412 239.687 205.714 1.00 4.48  ? 1980 GLU A CA    1 
ATOM   4204  C  C     . GLU A 1 1980 ? 159.558 238.699 206.497 1.00 4.99  ? 1980 GLU A C     1 
ATOM   4205  O  O     . GLU A 1 1980 ? 158.329 238.689 206.365 1.00 12.64 ? 1980 GLU A O     1 
ATOM   4206  C  CB    . GLU A 1 1980 ? 160.949 239.033 204.438 1.00 7.85  ? 1980 GLU A CB    1 
ATOM   4207  C  CG    . GLU A 1 1980 ? 162.014 239.814 203.649 1.00 9.75  ? 1980 GLU A CG    1 
ATOM   4208  C  CD    . GLU A 1 1980 ? 161.705 241.293 203.414 1.00 21.30 ? 1980 GLU A CD    1 
ATOM   4209  O  OE1   . GLU A 1 1980 ? 162.625 242.008 202.962 1.00 23.90 ? 1980 GLU A OE1   1 
ATOM   4210  O  OE2   . GLU A 1 1980 ? 160.557 241.742 203.620 1.00 23.70 ? 1980 GLU A OE2   1 
ATOM   4211  N  N     . ALA A 1 1981 ? 160.192 237.857 207.314 1.00 4.68  ? 1981 ALA A N     1 
ATOM   4212  C  CA    . ALA A 1 1981 ? 159.437 236.942 208.161 1.00 7.79  ? 1981 ALA A CA    1 
ATOM   4213  C  C     . ALA A 1 1981 ? 158.603 237.701 209.186 1.00 10.75 ? 1981 ALA A C     1 
ATOM   4214  O  O     . ALA A 1 1981 ? 157.466 237.314 209.482 1.00 14.61 ? 1981 ALA A O     1 
ATOM   4215  C  CB    . ALA A 1 1981 ? 160.387 235.968 208.855 1.00 4.97  ? 1981 ALA A CB    1 
ATOM   4216  N  N     . LEU A 1 1982 ? 159.151 238.783 209.740 1.00 6.70  ? 1982 LEU A N     1 
ATOM   4217  C  CA    . LEU A 1 1982 ? 158.412 239.566 210.727 1.00 6.02  ? 1982 LEU A CA    1 
ATOM   4218  C  C     . LEU A 1 1982 ? 157.148 240.162 210.124 1.00 6.85  ? 1982 LEU A C     1 
ATOM   4219  O  O     . LEU A 1 1982 ? 156.111 240.246 210.794 1.00 10.83 ? 1982 LEU A O     1 
ATOM   4220  C  CB    . LEU A 1 1982 ? 159.305 240.663 211.300 1.00 6.16  ? 1982 LEU A CB    1 
ATOM   4221  C  CG    . LEU A 1 1982 ? 160.393 240.216 212.276 1.00 5.09  ? 1982 LEU A CG    1 
ATOM   4222  C  CD1   . LEU A 1 1982 ? 161.340 241.364 212.578 1.00 3.47  ? 1982 LEU A CD1   1 
ATOM   4223  C  CD2   . LEU A 1 1982 ? 159.771 239.676 213.549 1.00 6.20  ? 1982 LEU A CD2   1 
ATOM   4224  N  N     . ARG A 1 1983 ? 157.212 240.585 208.861 1.00 6.28  ? 1983 ARG A N     1 
ATOM   4225  C  CA    . ARG A 1 1983 ? 156.028 241.102 208.189 1.00 8.05  ? 1983 ARG A CA    1 
ATOM   4226  C  C     . ARG A 1 1983 ? 154.978 240.024 207.948 1.00 12.61 ? 1983 ARG A C     1 
ATOM   4227  O  O     . ARG A 1 1983 ? 153.803 240.357 207.755 1.00 17.07 ? 1983 ARG A O     1 
ATOM   4228  C  CB    . ARG A 1 1983 ? 156.425 241.765 206.870 1.00 4.13  ? 1983 ARG A CB    1 
ATOM   4229  C  CG    . ARG A 1 1983 ? 157.138 243.085 207.070 1.00 3.77  ? 1983 ARG A CG    1 
ATOM   4230  C  CD    . ARG A 1 1983 ? 157.781 243.602 205.802 1.00 2.86  ? 1983 ARG A CD    1 
ATOM   4231  N  NE    . ARG A 1 1983 ? 158.715 244.680 206.102 1.00 4.23  ? 1983 ARG A NE    1 
ATOM   4232  C  CZ    . ARG A 1 1983 ? 160.024 244.617 205.902 1.00 8.83  ? 1983 ARG A CZ    1 
ATOM   4233  N  NH1   . ARG A 1 1983 ? 160.590 243.550 205.360 1.00 6.33  ? 1983 ARG A NH1   1 
ATOM   4234  N  NH2   . ARG A 1 1983 ? 160.784 245.648 206.257 1.00 4.06  ? 1983 ARG A NH2   1 
ATOM   4235  N  N     . GLU A 1 1984 ? 155.367 238.747 207.952 1.00 14.21 ? 1984 GLU A N     1 
ATOM   4236  C  CA    . GLU A 1 1984 ? 154.380 237.683 207.826 1.00 14.62 ? 1984 GLU A CA    1 
ATOM   4237  C  C     . GLU A 1 1984 ? 153.509 237.573 209.074 1.00 16.85 ? 1984 GLU A C     1 
ATOM   4238  O  O     . GLU A 1 1984 ? 152.336 237.192 208.972 1.00 25.98 ? 1984 GLU A O     1 
ATOM   4239  C  CB    . GLU A 1 1984 ? 155.069 236.352 207.525 1.00 14.79 ? 1984 GLU A CB    1 
ATOM   4240  C  CG    . GLU A 1 1984 ? 155.459 236.187 206.065 1.00 17.93 ? 1984 GLU A CG    1 
ATOM   4241  C  CD    . GLU A 1 1984 ? 156.710 235.353 205.872 1.00 24.96 ? 1984 GLU A CD    1 
ATOM   4242  O  OE1   . GLU A 1 1984 ? 156.951 234.435 206.685 1.00 22.89 ? 1984 GLU A OE1   1 
ATOM   4243  O  OE2   . GLU A 1 1984 ? 157.456 235.615 204.904 1.00 20.49 ? 1984 GLU A OE2   1 
ATOM   4244  N  N     . HIS A 1 1985 ? 154.054 237.894 210.250 1.00 14.72 ? 1985 HIS A N     1 
ATOM   4245  C  CA    . HIS A 1 1985 ? 153.219 237.991 211.443 1.00 22.10 ? 1985 HIS A CA    1 
ATOM   4246  C  C     . HIS A 1 1985 ? 152.189 239.102 211.298 1.00 22.48 ? 1985 HIS A C     1 
ATOM   4247  O  O     . HIS A 1 1985 ? 151.023 238.933 211.671 1.00 28.86 ? 1985 HIS A O     1 
ATOM   4248  C  CB    . HIS A 1 1985 ? 154.079 238.244 212.683 1.00 16.88 ? 1985 HIS A CB    1 
ATOM   4249  C  CG    . HIS A 1 1985 ? 154.961 237.096 213.062 1.00 13.32 ? 1985 HIS A CG    1 
ATOM   4250  N  ND1   . HIS A 1 1985 ? 156.283 237.019 212.682 1.00 21.81 ? 1985 HIS A ND1   1 
ATOM   4251  C  CD2   . HIS A 1 1985 ? 154.716 235.992 213.804 1.00 14.41 ? 1985 HIS A CD2   1 
ATOM   4252  C  CE1   . HIS A 1 1985 ? 156.811 235.909 213.163 1.00 17.15 ? 1985 HIS A CE1   1 
ATOM   4253  N  NE2   . HIS A 1 1985 ? 155.881 235.266 213.848 1.00 15.76 ? 1985 HIS A NE2   1 
ATOM   4254  N  N     . SER A 1 1986 ? 152.608 240.246 210.758 1.00 18.84 ? 1986 SER A N     1 
ATOM   4255  C  CA    . SER A 1 1986 ? 151.754 241.421 210.661 1.00 16.57 ? 1986 SER A CA    1 
ATOM   4256  C  C     . SER A 1 1986 ? 150.661 241.284 209.609 1.00 21.08 ? 1986 SER A C     1 
ATOM   4257  O  O     . SER A 1 1986 ? 149.775 242.142 209.553 1.00 25.65 ? 1986 SER A O     1 
ATOM   4258  C  CB    . SER A 1 1986 ? 152.611 242.653 210.362 1.00 11.54 ? 1986 SER A CB    1 
ATOM   4259  O  OG    . SER A 1 1986 ? 152.936 242.729 208.988 1.00 10.33 ? 1986 SER A OG    1 
ATOM   4260  N  N     . ASN A 1 1987 ? 150.702 240.250 208.783 1.00 20.32 ? 1987 ASN A N     1 
ATOM   4261  C  CA    . ASN A 1 1987 ? 149.677 240.068 207.762 1.00 26.31 ? 1987 ASN A CA    1 
ATOM   4262  C  C     . ASN A 1 1987 ? 148.360 239.656 208.409 1.00 34.08 ? 1987 ASN A C     1 
ATOM   4263  O  O     . ASN A 1 1987 ? 148.321 238.644 209.122 1.00 33.54 ? 1987 ASN A O     1 
ATOM   4264  C  CB    . ASN A 1 1987 ? 150.117 239.021 206.743 1.00 26.54 ? 1987 ASN A CB    1 
ATOM   4265  C  CG    . ASN A 1 1987 ? 151.175 239.544 205.790 1.00 32.46 ? 1987 ASN A CG    1 
ATOM   4266  O  OD1   . ASN A 1 1987 ? 152.282 239.013 205.720 1.00 32.94 ? 1987 ASN A OD1   1 
ATOM   4267  N  ND2   . ASN A 1 1987 ? 150.835 240.592 205.049 1.00 27.84 ? 1987 ASN A ND2   1 
ATOM   4268  N  N     . PRO A 1 1988 ? 147.273 240.404 208.205 1.00 36.24 ? 1988 PRO A N     1 
ATOM   4269  C  CA    . PRO A 1 1988 ? 145.980 239.983 208.770 1.00 32.06 ? 1988 PRO A CA    1 
ATOM   4270  C  C     . PRO A 1 1988 ? 145.479 238.663 208.215 1.00 38.08 ? 1988 PRO A C     1 
ATOM   4271  O  O     . PRO A 1 1988 ? 144.757 237.940 208.914 1.00 38.56 ? 1988 PRO A O     1 
ATOM   4272  C  CB    . PRO A 1 1988 ? 145.045 241.144 208.404 1.00 31.33 ? 1988 PRO A CB    1 
ATOM   4273  C  CG    . PRO A 1 1988 ? 145.683 241.778 207.210 1.00 36.74 ? 1988 PRO A CG    1 
ATOM   4274  C  CD    . PRO A 1 1988 ? 147.162 241.650 207.429 1.00 33.08 ? 1988 PRO A CD    1 
ATOM   4275  N  N     . ASN A 1 1989 ? 145.835 238.328 206.971 1.00 36.11 ? 1989 ASN A N     1 
ATOM   4276  C  CA    . ASN A 1 1989 ? 145.373 237.077 206.377 1.00 33.21 ? 1989 ASN A CA    1 
ATOM   4277  C  C     . ASN A 1 1989 ? 145.947 235.873 207.114 1.00 38.35 ? 1989 ASN A C     1 
ATOM   4278  O  O     . ASN A 1 1989 ? 145.284 234.834 207.231 1.00 41.94 ? 1989 ASN A O     1 
ATOM   4279  C  CB    . ASN A 1 1989 ? 145.746 237.031 204.895 1.00 33.84 ? 1989 ASN A CB    1 
ATOM   4280  C  CG    . ASN A 1 1989 ? 147.197 237.396 204.646 1.00 37.31 ? 1989 ASN A CG    1 
ATOM   4281  O  OD1   . ASN A 1 1989 ? 148.110 236.685 205.062 1.00 36.74 ? 1989 ASN A OD1   1 
ATOM   4282  N  ND2   . ASN A 1 1989 ? 147.415 238.514 203.960 1.00 32.03 ? 1989 ASN A ND2   1 
ATOM   4283  N  N     . TYR A 1 1990 ? 147.178 235.988 207.606 1.00 37.09 ? 1990 TYR A N     1 
ATOM   4284  C  CA    . TYR A 1 1990 ? 147.792 234.899 208.354 1.00 35.42 ? 1990 TYR A CA    1 
ATOM   4285  C  C     . TYR A 1 1990 ? 147.020 234.627 209.640 1.00 35.54 ? 1990 TYR A C     1 
ATOM   4286  O  O     . TYR A 1 1990 ? 146.604 235.550 210.343 1.00 37.17 ? 1990 TYR A O     1 
ATOM   4287  C  CB    . TYR A 1 1990 ? 149.251 235.235 208.669 1.00 31.14 ? 1990 TYR A CB    1 
ATOM   4288  C  CG    . TYR A 1 1990 ? 149.792 234.533 209.893 1.00 28.66 ? 1990 TYR A CG    1 
ATOM   4289  C  CD1   . TYR A 1 1990 ? 150.186 233.203 209.838 1.00 32.85 ? 1990 TYR A CD1   1 
ATOM   4290  C  CD2   . TYR A 1 1990 ? 149.916 235.203 211.105 1.00 29.58 ? 1990 TYR A CD2   1 
ATOM   4291  C  CE1   . TYR A 1 1990 ? 150.683 232.558 210.955 1.00 29.00 ? 1990 TYR A CE1   1 
ATOM   4292  C  CE2   . TYR A 1 1990 ? 150.410 234.568 212.226 1.00 30.60 ? 1990 TYR A CE2   1 
ATOM   4293  C  CZ    . TYR A 1 1990 ? 150.787 233.246 212.146 1.00 33.49 ? 1990 TYR A CZ    1 
ATOM   4294  O  OH    . TYR A 1 1990 ? 151.284 232.608 213.260 1.00 31.16 ? 1990 TYR A OH    1 
ATOM   4295  N  N     . ASP A 1 1991 ? 146.834 233.346 209.943 1.00 36.37 ? 1991 ASP A N     1 
ATOM   4296  C  CA    . ASP A 1 1991 ? 146.133 232.910 211.138 1.00 34.31 ? 1991 ASP A CA    1 
ATOM   4297  C  C     . ASP A 1 1991 ? 147.089 232.171 212.067 1.00 37.55 ? 1991 ASP A C     1 
ATOM   4298  O  O     . ASP A 1 1991 ? 147.946 231.404 211.619 1.00 39.00 ? 1991 ASP A O     1 
ATOM   4299  C  CB    . ASP A 1 1991 ? 144.948 232.006 210.784 1.00 34.13 ? 1991 ASP A CB    1 
ATOM   4300  C  CG    . ASP A 1 1991 ? 145.367 230.763 210.023 1.00 40.53 ? 1991 ASP A CG    1 
ATOM   4301  O  OD1   . ASP A 1 1991 ? 146.029 230.902 208.974 1.00 35.72 ? 1991 ASP A OD1   1 
ATOM   4302  O  OD2   . ASP A 1 1991 ? 145.036 229.647 210.477 1.00 39.15 ? 1991 ASP A OD2   1 
ATOM   4303  N  N     . LYS A 1 1992 ? 146.928 232.411 213.371 1.00 36.78 ? 1992 LYS A N     1 
ATOM   4304  C  CA    . LYS A 1 1992 ? 147.835 231.823 214.354 1.00 36.15 ? 1992 LYS A CA    1 
ATOM   4305  C  C     . LYS A 1 1992 ? 147.785 230.300 214.334 1.00 37.35 ? 1992 LYS A C     1 
ATOM   4306  O  O     . LYS A 1 1992 ? 148.758 229.644 214.722 1.00 35.95 ? 1992 LYS A O     1 
ATOM   4307  C  CB    . LYS A 1 1992 ? 147.501 232.345 215.751 1.00 33.61 ? 1992 LYS A CB    1 
ATOM   4308  C  CG    . LYS A 1 1992 ? 147.621 233.855 215.894 1.00 31.44 ? 1992 LYS A CG    1 
ATOM   4309  C  CD    . LYS A 1 1992 ? 147.119 234.324 217.250 1.00 27.57 ? 1992 LYS A CD    1 
ATOM   4310  C  CE    . LYS A 1 1992 ? 145.648 233.992 217.439 1.00 31.43 ? 1992 LYS A CE    1 
ATOM   4311  N  NZ    . LYS A 1 1992 ? 145.132 234.478 218.748 1.00 35.79 ? 1992 LYS A NZ    1 
ATOM   4312  N  N     . THR A 1 1993 ? 146.670 229.722 213.891 1.00 36.86 ? 1993 THR A N     1 
ATOM   4313  C  CA    . THR A 1 1993 ? 146.535 228.268 213.801 1.00 34.59 ? 1993 THR A CA    1 
ATOM   4314  C  C     . THR A 1 1993 ? 146.938 227.777 212.409 1.00 37.64 ? 1993 THR A C     1 
ATOM   4315  O  O     . THR A 1 1993 ? 146.142 227.226 211.649 1.00 39.64 ? 1993 THR A O     1 
ATOM   4316  C  CB    . THR A 1 1993 ? 145.110 227.849 214.146 1.00 33.83 ? 1993 THR A CB    1 
ATOM   4317  O  OG1   . THR A 1 1993 ? 144.192 228.489 213.251 1.00 38.43 ? 1993 THR A OG1   1 
ATOM   4318  C  CG2   . THR A 1 1993 ? 144.771 228.239 215.576 1.00 30.20 ? 1993 THR A CG2   1 
ATOM   4319  N  N     . SER A 1 1994 ? 148.210 227.993 212.083 1.00 35.89 ? 1994 SER A N     1 
ATOM   4320  C  CA    . SER A 1 1994 ? 148.760 227.602 210.792 1.00 36.86 ? 1994 SER A CA    1 
ATOM   4321  C  C     . SER A 1 1994 ? 150.228 227.241 210.986 1.00 35.04 ? 1994 SER A C     1 
ATOM   4322  O  O     . SER A 1 1994 ? 150.715 227.105 212.114 1.00 35.45 ? 1994 SER A O     1 
ATOM   4323  C  CB    . SER A 1 1994 ? 148.571 228.718 209.757 1.00 32.32 ? 1994 SER A CB    1 
ATOM   4324  O  OG    . SER A 1 1994 ? 149.530 229.745 209.941 1.00 34.24 ? 1994 SER A OG    1 
ATOM   4325  N  N     . ALA A 1 1995 ? 150.938 227.082 209.874 1.00 29.07 ? 1995 ALA A N     1 
ATOM   4326  C  CA    . ALA A 1 1995 ? 152.367 226.808 209.933 1.00 30.67 ? 1995 ALA A CA    1 
ATOM   4327  C  C     . ALA A 1 1995 ? 153.104 228.024 210.483 1.00 32.34 ? 1995 ALA A C     1 
ATOM   4328  O  O     . ALA A 1 1995 ? 152.847 229.149 210.040 1.00 31.78 ? 1995 ALA A O     1 
ATOM   4329  C  CB    . ALA A 1 1995 ? 152.902 226.444 208.551 1.00 23.28 ? 1995 ALA A CB    1 
ATOM   4330  N  N     . PRO A 1 1996 ? 154.011 227.845 211.442 1.00 31.17 ? 1996 PRO A N     1 
ATOM   4331  C  CA    . PRO A 1 1996 ? 154.703 229.000 212.026 1.00 26.67 ? 1996 PRO A CA    1 
ATOM   4332  C  C     . PRO A 1 1996 ? 155.544 229.736 210.995 1.00 23.01 ? 1996 PRO A C     1 
ATOM   4333  O  O     . PRO A 1 1996 ? 156.076 229.142 210.055 1.00 23.69 ? 1996 PRO A O     1 
ATOM   4334  C  CB    . PRO A 1 1996 ? 155.581 228.373 213.116 1.00 24.40 ? 1996 PRO A CB    1 
ATOM   4335  C  CG    . PRO A 1 1996 ? 154.942 227.054 213.415 1.00 28.36 ? 1996 PRO A CG    1 
ATOM   4336  C  CD    . PRO A 1 1996 ? 154.377 226.585 212.108 1.00 23.52 ? 1996 PRO A CD    1 
ATOM   4337  N  N     . ILE A 1 1997 ? 155.650 231.052 211.179 1.00 20.51 ? 1997 ILE A N     1 
ATOM   4338  C  CA    . ILE A 1 1997 ? 156.514 231.862 210.331 1.00 13.33 ? 1997 ILE A CA    1 
ATOM   4339  C  C     . ILE A 1 1997 ? 157.958 231.423 210.520 1.00 14.71 ? 1997 ILE A C     1 
ATOM   4340  O  O     . ILE A 1 1997 ? 158.409 231.176 211.646 1.00 15.18 ? 1997 ILE A O     1 
ATOM   4341  C  CB    . ILE A 1 1997 ? 156.345 233.359 210.638 1.00 13.82 ? 1997 ILE A CB    1 
ATOM   4342  C  CG1   . ILE A 1 1997 ? 154.921 233.829 210.332 1.00 18.14 ? 1997 ILE A CG1   1 
ATOM   4343  C  CG2   . ILE A 1 1997 ? 157.358 234.181 209.874 1.00 13.51 ? 1997 ILE A CG2   1 
ATOM   4344  C  CD1   . ILE A 1 1997 ? 153.973 233.689 211.480 1.00 22.05 ? 1997 ILE A CD1   1 
ATOM   4345  N  N     . THR A 1 1998 ? 158.687 231.320 209.415 1.00 11.05 ? 1998 THR A N     1 
ATOM   4346  C  CA    . THR A 1 1998 ? 160.046 230.814 209.419 1.00 9.46  ? 1998 THR A CA    1 
ATOM   4347  C  C     . THR A 1 1998 ? 160.871 231.557 208.377 1.00 10.55 ? 1998 THR A C     1 
ATOM   4348  O  O     . THR A 1 1998 ? 160.404 231.824 207.267 1.00 17.98 ? 1998 THR A O     1 
ATOM   4349  C  CB    . THR A 1 1998 ? 160.059 229.299 209.142 1.00 11.57 ? 1998 THR A CB    1 
ATOM   4350  O  OG1   . THR A 1 1998 ? 159.566 228.596 210.289 1.00 12.97 ? 1998 THR A OG1   1 
ATOM   4351  C  CG2   . THR A 1 1998 ? 161.448 228.822 208.843 1.00 12.64 ? 1998 THR A CG2   1 
ATOM   4352  N  N     . CYS A 1 1999 ? 162.101 231.903 208.748 1.00 6.20  ? 1999 CYS A N     1 
ATOM   4353  C  CA    . CYS A 1 1999 ? 163.069 232.462 207.817 1.00 9.31  ? 1999 CYS A CA    1 
ATOM   4354  C  C     . CYS A 1 1999 ? 164.290 231.553 207.755 1.00 8.55  ? 1999 CYS A C     1 
ATOM   4355  O  O     . CYS A 1 1999 ? 164.524 230.731 208.644 1.00 8.23  ? 1999 CYS A O     1 
ATOM   4356  C  CB    . CYS A 1 1999 ? 163.485 233.884 208.215 1.00 5.31  ? 1999 CYS A CB    1 
ATOM   4357  S  SG    . CYS A 1 1999 ? 164.756 233.972 209.488 1.00 18.41 ? 1999 CYS A SG    1 
ATOM   4358  N  N     . GLU A 1 2000 ? 165.066 231.701 206.687 1.00 6.03  ? 2000 GLU A N     1 
ATOM   4359  C  CA    . GLU A 1 2000 ? 166.242 230.867 206.470 1.00 9.76  ? 2000 GLU A CA    1 
ATOM   4360  C  C     . GLU A 1 2000 ? 167.464 231.554 207.066 1.00 7.29  ? 2000 GLU A C     1 
ATOM   4361  O  O     . GLU A 1 2000 ? 167.921 232.583 206.557 1.00 4.76  ? 2000 GLU A O     1 
ATOM   4362  C  CB    . GLU A 1 2000 ? 166.440 230.583 204.984 1.00 11.36 ? 2000 GLU A CB    1 
ATOM   4363  C  CG    . GLU A 1 2000 ? 167.356 229.404 204.714 1.00 8.78  ? 2000 GLU A CG    1 
ATOM   4364  C  CD    . GLU A 1 2000 ? 167.667 229.229 203.243 1.00 19.53 ? 2000 GLU A CD    1 
ATOM   4365  O  OE1   . GLU A 1 2000 ? 167.147 230.015 202.425 1.00 24.32 ? 2000 GLU A OE1   1 
ATOM   4366  O  OE2   . GLU A 1 2000 ? 168.430 228.302 202.906 1.00 17.40 ? 2000 GLU A OE2   1 
ATOM   4367  N  N     . LEU A 1 2001 ? 167.997 230.981 208.140 1.00 5.34  ? 2001 LEU A N     1 
ATOM   4368  C  CA    . LEU A 1 2001 ? 169.222 231.455 208.769 1.00 4.39  ? 2001 LEU A CA    1 
ATOM   4369  C  C     . LEU A 1 2001 ? 170.244 230.331 208.736 1.00 6.61  ? 2001 LEU A C     1 
ATOM   4370  O  O     . LEU A 1 2001 ? 169.971 229.226 209.218 1.00 11.59 ? 2001 LEU A O     1 
ATOM   4371  C  CB    . LEU A 1 2001 ? 168.963 231.913 210.205 1.00 5.03  ? 2001 LEU A CB    1 
ATOM   4372  C  CG    . LEU A 1 2001 ? 168.241 233.253 210.355 1.00 1.22  ? 2001 LEU A CG    1 
ATOM   4373  C  CD1   . LEU A 1 2001 ? 167.976 233.566 211.820 1.00 0.84  ? 2001 LEU A CD1   1 
ATOM   4374  C  CD2   . LEU A 1 2001 ? 169.052 234.360 209.703 1.00 1.08  ? 2001 LEU A CD2   1 
ATOM   4375  N  N     . LEU A 1 2002 ? 171.416 230.614 208.167 1.00 6.28  ? 2002 LEU A N     1 
ATOM   4376  C  CA    . LEU A 1 2002 ? 172.510 229.646 208.073 1.00 4.87  ? 2002 LEU A CA    1 
ATOM   4377  C  C     . LEU A 1 2002 ? 172.051 228.357 207.394 1.00 7.84  ? 2002 LEU A C     1 
ATOM   4378  O  O     . LEU A 1 2002 ? 172.337 227.247 207.845 1.00 12.90 ? 2002 LEU A O     1 
ATOM   4379  C  CB    . LEU A 1 2002 ? 173.105 229.365 209.454 1.00 3.80  ? 2002 LEU A CB    1 
ATOM   4380  C  CG    . LEU A 1 2002 ? 173.728 230.578 210.146 1.00 4.18  ? 2002 LEU A CG    1 
ATOM   4381  C  CD1   . LEU A 1 2002 ? 174.319 230.198 211.492 1.00 0.98  ? 2002 LEU A CD1   1 
ATOM   4382  C  CD2   . LEU A 1 2002 ? 174.781 231.221 209.256 1.00 4.44  ? 2002 LEU A CD2   1 
ATOM   4383  N  N     . ASN A 1 2003 ? 171.310 228.523 206.294 1.00 8.02  ? 2003 ASN A N     1 
ATOM   4384  C  CA    . ASN A 1 2003 ? 170.826 227.413 205.468 1.00 9.87  ? 2003 ASN A CA    1 
ATOM   4385  C  C     . ASN A 1 2003 ? 169.923 226.466 206.257 1.00 9.53  ? 2003 ASN A C     1 
ATOM   4386  O  O     . ASN A 1 2003 ? 169.845 225.271 205.966 1.00 18.08 ? 2003 ASN A O     1 
ATOM   4387  C  CB    . ASN A 1 2003 ? 171.987 226.646 204.831 1.00 9.20  ? 2003 ASN A CB    1 
ATOM   4388  C  CG    . ASN A 1 2003 ? 172.938 227.549 204.079 1.00 14.24 ? 2003 ASN A CG    1 
ATOM   4389  O  OD1   . ASN A 1 2003 ? 174.108 227.672 204.438 1.00 18.00 ? 2003 ASN A OD1   1 
ATOM   4390  N  ND2   . ASN A 1 2003 ? 172.439 228.192 203.031 1.00 15.10 ? 2003 ASN A ND2   1 
ATOM   4391  N  N     . LYS A 1 2004 ? 169.232 227.001 207.258 1.00 9.11  ? 2004 LYS A N     1 
ATOM   4392  C  CA    . LYS A 1 2004 ? 168.276 226.225 208.033 1.00 6.90  ? 2004 LYS A CA    1 
ATOM   4393  C  C     . LYS A 1 2004 ? 167.007 227.043 208.211 1.00 9.50  ? 2004 LYS A C     1 
ATOM   4394  O  O     . LYS A 1 2004 ? 167.059 228.272 208.296 1.00 8.49  ? 2004 LYS A O     1 
ATOM   4395  C  CB    . LYS A 1 2004 ? 168.840 225.821 209.400 1.00 5.75  ? 2004 LYS A CB    1 
ATOM   4396  C  CG    . LYS A 1 2004 ? 170.067 224.938 209.333 1.00 14.03 ? 2004 LYS A CG    1 
ATOM   4397  C  CD    . LYS A 1 2004 ? 169.725 223.573 208.761 1.00 18.93 ? 2004 LYS A CD    1 
ATOM   4398  C  CE    . LYS A 1 2004 ? 170.930 222.652 208.759 1.00 20.39 ? 2004 LYS A CE    1 
ATOM   4399  N  NZ    . LYS A 1 2004 ? 170.602 221.329 208.160 1.00 24.34 ? 2004 LYS A NZ    1 
ATOM   4400  N  N     . GLN A 1 2005 ? 165.874 226.352 208.271 1.00 9.65  ? 2005 GLN A N     1 
ATOM   4401  C  CA    . GLN A 1 2005 ? 164.585 227.008 208.458 1.00 8.00  ? 2005 GLN A CA    1 
ATOM   4402  C  C     . GLN A 1 2005 ? 164.363 227.258 209.946 1.00 7.23  ? 2005 GLN A C     1 
ATOM   4403  O  O     . GLN A 1 2005 ? 164.209 226.311 210.724 1.00 12.46 ? 2005 GLN A O     1 
ATOM   4404  C  CB    . GLN A 1 2005 ? 163.467 226.151 207.871 1.00 7.17  ? 2005 GLN A CB    1 
ATOM   4405  C  CG    . GLN A 1 2005 ? 163.443 226.112 206.345 1.00 8.99  ? 2005 GLN A CG    1 
ATOM   4406  C  CD    . GLN A 1 2005 ? 163.436 227.491 205.711 1.00 11.22 ? 2005 GLN A CD    1 
ATOM   4407  O  OE1   . GLN A 1 2005 ? 162.548 228.301 205.966 1.00 12.49 ? 2005 GLN A OE1   1 
ATOM   4408  N  NE2   . GLN A 1 2005 ? 164.435 227.763 204.877 1.00 16.18 ? 2005 GLN A NE2   1 
ATOM   4409  N  N     . VAL A 1 2006 ? 164.341 228.528 210.341 1.00 5.10  ? 2006 VAL A N     1 
ATOM   4410  C  CA    . VAL A 1 2006 ? 164.296 228.926 211.743 1.00 5.95  ? 2006 VAL A CA    1 
ATOM   4411  C  C     . VAL A 1 2006 ? 162.991 229.663 212.007 1.00 5.28  ? 2006 VAL A C     1 
ATOM   4412  O  O     . VAL A 1 2006 ? 162.661 230.621 211.300 1.00 9.19  ? 2006 VAL A O     1 
ATOM   4413  C  CB    . VAL A 1 2006 ? 165.503 229.807 212.114 1.00 5.20  ? 2006 VAL A CB    1 
ATOM   4414  C  CG1   . VAL A 1 2006 ? 165.458 230.182 213.586 1.00 4.16  ? 2006 VAL A CG1   1 
ATOM   4415  C  CG2   . VAL A 1 2006 ? 166.805 229.097 211.780 1.00 5.05  ? 2006 VAL A CG2   1 
ATOM   4416  N  N     . LYS A 1 2007 ? 162.256 229.221 213.024 1.00 4.23  ? 2007 LYS A N     1 
ATOM   4417  C  CA    . LYS A 1 2007 ? 161.038 229.913 213.422 1.00 9.07  ? 2007 LYS A CA    1 
ATOM   4418  C  C     . LYS A 1 2007 ? 161.372 231.288 213.989 1.00 8.91  ? 2007 LYS A C     1 
ATOM   4419  O  O     . LYS A 1 2007 ? 162.370 231.464 214.693 1.00 4.13  ? 2007 LYS A O     1 
ATOM   4420  C  CB    . LYS A 1 2007 ? 160.269 229.094 214.458 1.00 7.62  ? 2007 LYS A CB    1 
ATOM   4421  C  CG    . LYS A 1 2007 ? 159.762 227.759 213.947 1.00 14.99 ? 2007 LYS A CG    1 
ATOM   4422  C  CD    . LYS A 1 2007 ? 158.950 227.035 215.010 1.00 25.32 ? 2007 LYS A CD    1 
ATOM   4423  C  CE    . LYS A 1 2007 ? 159.838 226.544 216.141 1.00 21.89 ? 2007 LYS A CE    1 
ATOM   4424  N  NZ    . LYS A 1 2007 ? 160.787 225.489 215.694 1.00 24.86 ? 2007 LYS A NZ    1 
ATOM   4425  N  N     . VAL A 1 2008 ? 160.528 232.267 213.679 1.00 8.28  ? 2008 VAL A N     1 
ATOM   4426  C  CA    . VAL A 1 2008 ? 160.744 233.651 214.077 1.00 3.48  ? 2008 VAL A CA    1 
ATOM   4427  C  C     . VAL A 1 2008 ? 159.619 234.067 215.013 1.00 5.70  ? 2008 VAL A C     1 
ATOM   4428  O  O     . VAL A 1 2008 ? 158.440 233.981 214.653 1.00 14.38 ? 2008 VAL A O     1 
ATOM   4429  C  CB    . VAL A 1 2008 ? 160.819 234.583 212.854 1.00 4.05  ? 2008 VAL A CB    1 
ATOM   4430  C  CG1   . VAL A 1 2008 ? 161.069 236.017 213.292 1.00 5.44  ? 2008 VAL A CG1   1 
ATOM   4431  C  CG2   . VAL A 1 2008 ? 161.905 234.115 211.899 1.00 3.11  ? 2008 VAL A CG2   1 
ATOM   4432  N  N     . SER A 1 2009 ? 159.982 234.501 216.213 1.00 7.41  ? 2009 SER A N     1 
ATOM   4433  C  CA    . SER A 1 2009 ? 158.943 235.015 217.095 1.00 6.28  ? 2009 SER A CA    1 
ATOM   4434  C  C     . SER A 1 2009 ? 158.663 236.480 216.773 1.00 7.74  ? 2009 SER A C     1 
ATOM   4435  O  O     . SER A 1 2009 ? 159.593 237.241 216.491 1.00 10.04 ? 2009 SER A O     1 
ATOM   4436  C  CB    . SER A 1 2009 ? 159.356 234.879 218.556 1.00 4.52  ? 2009 SER A CB    1 
ATOM   4437  O  OG    . SER A 1 2009 ? 158.369 235.414 219.422 1.00 9.84  ? 2009 SER A OG    1 
ATOM   4438  N  N     . PRO A 1 2010 ? 157.395 236.895 216.794 1.00 7.09  ? 2010 PRO A N     1 
ATOM   4439  C  CA    . PRO A 1 2010 ? 157.077 238.294 216.458 1.00 6.71  ? 2010 PRO A CA    1 
ATOM   4440  C  C     . PRO A 1 2010 ? 157.663 239.305 217.426 1.00 4.83  ? 2010 PRO A C     1 
ATOM   4441  O  O     . PRO A 1 2010 ? 157.770 240.485 217.075 1.00 8.75  ? 2010 PRO A O     1 
ATOM   4442  C  CB    . PRO A 1 2010 ? 155.541 238.319 216.483 1.00 7.80  ? 2010 PRO A CB    1 
ATOM   4443  C  CG    . PRO A 1 2010 ? 155.149 237.138 217.304 1.00 4.18  ? 2010 PRO A CG    1 
ATOM   4444  C  CD    . PRO A 1 2010 ? 156.186 236.097 217.045 1.00 6.49  ? 2010 PRO A CD    1 
ATOM   4445  N  N     . ASP A 1 2011 ? 158.045 238.887 218.633 1.00 4.36  ? 2011 ASP A N     1 
ATOM   4446  C  CA    . ASP A 1 2011 ? 158.545 239.817 219.635 1.00 2.57  ? 2011 ASP A CA    1 
ATOM   4447  C  C     . ASP A 1 2011 ? 160.007 240.194 219.443 1.00 1.54  ? 2011 ASP A C     1 
ATOM   4448  O  O     . ASP A 1 2011 ? 160.475 241.126 220.106 1.00 1.35  ? 2011 ASP A O     1 
ATOM   4449  C  CB    . ASP A 1 2011 ? 158.355 239.235 221.037 1.00 1.51  ? 2011 ASP A CB    1 
ATOM   4450  C  CG    . ASP A 1 2011 ? 156.918 239.317 221.514 1.00 8.19  ? 2011 ASP A CG    1 
ATOM   4451  O  OD1   . ASP A 1 2011 ? 156.044 239.708 220.712 1.00 9.79  ? 2011 ASP A OD1   1 
ATOM   4452  O  OD2   . ASP A 1 2011 ? 156.665 239.003 222.693 1.00 9.55  ? 2011 ASP A OD2   1 
ATOM   4453  N  N     . MET A 1 2012 ? 160.739 239.511 218.568 1.00 1.07  ? 2012 MET A N     1 
ATOM   4454  C  CA    . MET A 1 2012 ? 162.161 239.789 218.430 1.00 0.68  ? 2012 MET A CA    1 
ATOM   4455  C  C     . MET A 1 2012 ? 162.388 241.062 217.623 1.00 1.02  ? 2012 MET A C     1 
ATOM   4456  O  O     . MET A 1 2012 ? 161.577 241.435 216.772 1.00 4.09  ? 2012 MET A O     1 
ATOM   4457  C  CB    . MET A 1 2012 ? 162.880 238.600 217.789 1.00 0.62  ? 2012 MET A CB    1 
ATOM   4458  C  CG    . MET A 1 2012 ? 162.612 238.359 216.308 1.00 1.57  ? 2012 MET A CG    1 
ATOM   4459  S  SD    . MET A 1 2012 ? 163.584 239.398 215.197 1.00 16.39 ? 2012 MET A SD    1 
ATOM   4460  C  CE    . MET A 1 2012 ? 165.245 238.995 215.726 1.00 0.61  ? 2012 MET A CE    1 
ATOM   4461  N  N     . ALA A 1 2013 ? 163.509 241.727 217.895 1.00 0.17  ? 2013 ALA A N     1 
ATOM   4462  C  CA    . ALA A 1 2013 ? 163.856 242.965 217.218 1.00 0.03  ? 2013 ALA A CA    1 
ATOM   4463  C  C     . ALA A 1 2013 ? 165.370 243.086 217.165 1.00 0.04  ? 2013 ALA A C     1 
ATOM   4464  O  O     . ALA A 1 2013 ? 166.089 242.470 217.955 1.00 0.06  ? 2013 ALA A O     1 
ATOM   4465  C  CB    . ALA A 1 2013 ? 163.241 244.183 217.917 1.00 0.01  ? 2013 ALA A CB    1 
ATOM   4466  N  N     . ILE A 1 2014 ? 165.848 243.895 216.222 1.00 0.06  ? 2014 ILE A N     1 
ATOM   4467  C  CA    . ILE A 1 2014 ? 167.274 244.118 216.017 1.00 0.03  ? 2014 ILE A CA    1 
ATOM   4468  C  C     . ILE A 1 2014 ? 167.557 245.606 216.156 1.00 0.03  ? 2014 ILE A C     1 
ATOM   4469  O  O     . ILE A 1 2014 ? 166.905 246.431 215.508 1.00 0.04  ? 2014 ILE A O     1 
ATOM   4470  C  CB    . ILE A 1 2014 ? 167.742 243.600 214.644 1.00 0.04  ? 2014 ILE A CB    1 
ATOM   4471  C  CG1   . ILE A 1 2014 ? 167.280 242.159 214.425 1.00 0.04  ? 2014 ILE A CG1   1 
ATOM   4472  C  CG2   . ILE A 1 2014 ? 169.251 243.697 214.521 1.00 0.03  ? 2014 ILE A CG2   1 
ATOM   4473  C  CD1   . ILE A 1 2014 ? 167.662 241.591 213.076 1.00 0.12  ? 2014 ILE A CD1   1 
ATOM   4474  N  N     . PHE A 1 2015 ? 168.524 245.946 216.999 1.00 0.03  ? 2015 PHE A N     1 
ATOM   4475  C  CA    . PHE A 1 2015 ? 168.948 247.324 217.196 1.00 0.04  ? 2015 PHE A CA    1 
ATOM   4476  C  C     . PHE A 1 2015 ? 170.462 247.405 217.096 1.00 0.10  ? 2015 PHE A C     1 
ATOM   4477  O  O     . PHE A 1 2015 ? 171.172 246.513 217.567 1.00 0.03  ? 2015 PHE A O     1 
ATOM   4478  C  CB    . PHE A 1 2015 ? 168.488 247.870 218.552 1.00 0.00  ? 2015 PHE A CB    1 
ATOM   4479  C  CG    . PHE A 1 2015 ? 167.019 248.146 218.630 1.00 0.02  ? 2015 PHE A CG    1 
ATOM   4480  C  CD1   . PHE A 1 2015 ? 166.125 247.133 218.940 1.00 0.00  ? 2015 PHE A CD1   1 
ATOM   4481  C  CD2   . PHE A 1 2015 ? 166.526 249.419 218.399 1.00 0.02  ? 2015 PHE A CD2   1 
ATOM   4482  C  CE1   . PHE A 1 2015 ? 164.774 247.383 219.015 1.00 0.03  ? 2015 PHE A CE1   1 
ATOM   4483  C  CE2   . PHE A 1 2015 ? 165.172 249.675 218.474 1.00 0.01  ? 2015 PHE A CE2   1 
ATOM   4484  C  CZ    . PHE A 1 2015 ? 164.295 248.655 218.782 1.00 0.03  ? 2015 PHE A CZ    1 
ATOM   4485  N  N     . ILE A 1 2016 ? 170.939 248.479 216.475 1.00 0.02  ? 2016 ILE A N     1 
ATOM   4486  C  CA    . ILE A 1 2016 ? 172.405 248.705 216.352 1.00 0.03  ? 2016 ILE A CA    1 
ATOM   4487  C  C     . ILE A 1 2016 ? 172.684 250.124 216.861 1.00 0.05  ? 2016 ILE A C     1 
ATOM   4488  O  O     . ILE A 1 2016 ? 171.944 251.049 216.482 1.00 0.07  ? 2016 ILE A O     1 
ATOM   4489  C  CB    . ILE A 1 2016 ? 172.876 248.491 214.902 1.00 0.07  ? 2016 ILE A CB    1 
ATOM   4490  C  CG1   . ILE A 1 2016 ? 172.215 249.477 213.937 1.00 0.05  ? 2016 ILE A CG1   1 
ATOM   4491  C  CG2   . ILE A 1 2016 ? 172.653 247.042 214.465 1.00 0.02  ? 2016 ILE A CG2   1 
ATOM   4492  C  CD1   . ILE A 1 2016 ? 172.644 249.317 212.490 1.00 0.04  ? 2016 ILE A CD1   1 
ATOM   4493  N  N     . THR A 1 2017 ? 173.685 250.270 217.727 1.00 0.32  ? 2017 THR A N     1 
ATOM   4494  C  CA    . THR A 1 2017 ? 174.064 251.602 218.237 1.00 0.57  ? 2017 THR A CA    1 
ATOM   4495  C  C     . THR A 1 2017 ? 175.464 251.871 217.757 1.00 0.90  ? 2017 THR A C     1 
ATOM   4496  O  O     . THR A 1 2017 ? 176.320 250.979 217.916 1.00 1.63  ? 2017 THR A O     1 
ATOM   4497  C  CB    . THR A 1 2017 ? 173.949 251.636 219.762 1.00 0.87  ? 2017 THR A CB    1 
ATOM   4498  O  OG1   . THR A 1 2017 ? 174.937 250.729 220.240 1.00 3.57  ? 2017 THR A OG1   1 
ATOM   4499  C  CG2   . THR A 1 2017 ? 172.575 251.219 220.253 1.00 0.50  ? 2017 THR A CG2   1 
ATOM   4500  N  N     . MET A 1 2018 ? 175.702 253.043 217.170 1.00 1.32  ? 2018 MET A N     1 
ATOM   4501  C  CA    . MET A 1 2018 ? 177.037 253.287 216.573 1.00 1.11  ? 2018 MET A CA    1 
ATOM   4502  C  C     . MET A 1 2018 ? 177.478 254.741 216.755 1.00 1.13  ? 2018 MET A C     1 
ATOM   4503  O  O     . MET A 1 2018 ? 176.604 255.616 216.911 1.00 1.16  ? 2018 MET A O     1 
ATOM   4504  C  CB    . MET A 1 2018 ? 177.017 253.011 215.065 1.00 2.20  ? 2018 MET A CB    1 
ATOM   4505  C  CG    . MET A 1 2018 ? 176.610 251.605 214.684 1.00 3.50  ? 2018 MET A CG    1 
ATOM   4506  S  SD    . MET A 1 2018 ? 176.448 251.439 212.895 1.00 12.11 ? 2018 MET A SD    1 
ATOM   4507  C  CE    . MET A 1 2018 ? 175.120 252.603 212.560 1.00 3.47  ? 2018 MET A CE    1 
ATOM   4508  N  N     . ASN A 1 2019 ? 178.789 254.972 216.755 1.00 5.67  ? 2019 ASN A N     1 
ATOM   4509  C  CA    . ASN A 1 2019 ? 179.333 256.356 216.793 1.00 4.41  ? 2019 ASN A CA    1 
ATOM   4510  C  C     . ASN A 1 2019 ? 179.896 256.629 215.397 1.00 5.25  ? 2019 ASN A C     1 
ATOM   4511  O  O     . ASN A 1 2019 ? 181.066 256.267 215.144 1.00 13.56 ? 2019 ASN A O     1 
ATOM   4512  C  CB    . ASN A 1 2019 ? 180.349 256.545 217.911 1.00 4.15  ? 2019 ASN A CB    1 
ATOM   4513  C  CG    . ASN A 1 2019 ? 180.803 257.979 218.040 1.00 7.05  ? 2019 ASN A CG    1 
ATOM   4514  O  OD1   . ASN A 1 2019 ? 180.445 258.827 217.215 1.00 6.37  ? 2019 ASN A OD1   1 
ATOM   4515  N  ND2   . ASN A 1 2019 ? 181.594 258.269 219.063 1.00 8.07  ? 2019 ASN A ND2   1 
ATOM   4516  N  N     . PRO A 1 2020 ? 179.117 257.228 214.474 1.00 6.95  ? 2020 PRO A N     1 
ATOM   4517  C  CA    . PRO A 1 2020 ? 179.575 257.420 213.102 1.00 10.02 ? 2020 PRO A CA    1 
ATOM   4518  C  C     . PRO A 1 2020 ? 180.735 258.399 213.005 1.00 12.98 ? 2020 PRO A C     1 
ATOM   4519  O  O     . PRO A 1 2020 ? 181.323 258.527 211.916 1.00 16.50 ? 2020 PRO A O     1 
ATOM   4520  C  CB    . PRO A 1 2020 ? 178.312 257.940 212.386 1.00 7.98  ? 2020 PRO A CB    1 
ATOM   4521  C  CG    . PRO A 1 2020 ? 177.178 257.602 213.327 1.00 5.77  ? 2020 PRO A CG    1 
ATOM   4522  C  CD    . PRO A 1 2020 ? 177.777 257.727 214.714 1.00 6.46  ? 2020 PRO A CD    1 
ATOM   4523  N  N     . GLY A 1 2021 ? 181.058 259.072 214.109 1.00 13.70 ? 2021 GLY A N     1 
ATOM   4524  C  CA    . GLY A 1 2021 ? 182.139 260.075 214.102 1.00 10.66 ? 2021 GLY A CA    1 
ATOM   4525  C  C     . GLY A 1 2021 ? 183.491 259.449 214.373 1.00 15.83 ? 2021 GLY A C     1 
ATOM   4526  O  O     . GLY A 1 2021 ? 184.509 260.147 214.190 1.00 31.39 ? 2021 GLY A O     1 
ATOM   4527  N  N     . TYR A 1 2022 ? 183.514 258.189 214.805 1.00 12.15 ? 2022 TYR A N     1 
ATOM   4528  C  CA    . TYR A 1 2022 ? 184.802 257.531 215.155 1.00 10.72 ? 2022 TYR A CA    1 
ATOM   4529  C  C     . TYR A 1 2022 ? 185.536 257.182 213.862 1.00 11.13 ? 2022 TYR A C     1 
ATOM   4530  O  O     . TYR A 1 2022 ? 184.980 256.441 213.026 1.00 13.67 ? 2022 TYR A O     1 
ATOM   4531  C  CB    . TYR A 1 2022 ? 184.558 256.326 216.074 1.00 9.99  ? 2022 TYR A CB    1 
ATOM   4532  C  CG    . TYR A 1 2022 ? 184.627 256.656 217.558 1.00 12.46 ? 2022 TYR A CG    1 
ATOM   4533  C  CD1   . TYR A 1 2022 ? 184.487 257.964 218.010 1.00 12.68 ? 2022 TYR A CD1   1 
ATOM   4534  C  CD2   . TYR A 1 2022 ? 184.805 255.662 218.511 1.00 9.93  ? 2022 TYR A CD2   1 
ATOM   4535  C  CE1   . TYR A 1 2022 ? 184.547 258.273 219.358 1.00 11.85 ? 2022 TYR A CE1   1 
ATOM   4536  C  CE2   . TYR A 1 2022 ? 184.862 255.957 219.863 1.00 11.56 ? 2022 TYR A CE2   1 
ATOM   4537  C  CZ    . TYR A 1 2022 ? 184.729 257.266 220.288 1.00 16.51 ? 2022 TYR A CZ    1 
ATOM   4538  O  OH    . TYR A 1 2022 ? 184.783 257.565 221.618 1.00 14.04 ? 2022 TYR A OH    1 
ATOM   4539  N  N     . ALA A 1 2023 ? 186.749 257.717 213.695 1.00 15.43 ? 2023 ALA A N     1 
ATOM   4540  C  CA    . ALA A 1 2023 ? 187.565 257.400 212.500 1.00 17.43 ? 2023 ALA A CA    1 
ATOM   4541  C  C     . ALA A 1 2023 ? 188.050 255.951 212.585 1.00 13.89 ? 2023 ALA A C     1 
ATOM   4542  O  O     . ALA A 1 2023 ? 188.214 255.438 213.712 1.00 12.85 ? 2023 ALA A O     1 
ATOM   4543  C  CB    . ALA A 1 2023 ? 188.720 258.364 212.396 1.00 18.72 ? 2023 ALA A CB    1 
ATOM   4544  N  N     . GLY A 1 2024 ? 188.270 255.310 211.434 1.00 13.04 ? 2024 GLY A N     1 
ATOM   4545  C  CA    . GLY A 1 2024 ? 188.686 253.927 211.429 1.00 11.72 ? 2024 GLY A CA    1 
ATOM   4546  C  C     . GLY A 1 2024 ? 187.549 252.929 211.481 1.00 12.80 ? 2024 GLY A C     1 
ATOM   4547  O  O     . GLY A 1 2024 ? 187.780 251.737 211.248 1.00 17.73 ? 2024 GLY A O     1 
ATOM   4548  N  N     . ARG A 1 2025 ? 186.334 253.379 211.781 1.00 9.60  ? 2025 ARG A N     1 
ATOM   4549  C  CA    . ARG A 1 2025 ? 185.185 252.492 211.798 1.00 6.76  ? 2025 ARG A CA    1 
ATOM   4550  C  C     . ARG A 1 2025 ? 184.787 252.111 210.373 1.00 6.77  ? 2025 ARG A C     1 
ATOM   4551  O  O     . ARG A 1 2025 ? 185.165 252.759 209.395 1.00 15.69 ? 2025 ARG A O     1 
ATOM   4552  C  CB    . ARG A 1 2025 ? 184.007 253.148 212.517 1.00 9.96  ? 2025 ARG A CB    1 
ATOM   4553  C  CG    . ARG A 1 2025 ? 184.259 253.435 213.979 1.00 5.05  ? 2025 ARG A CG    1 
ATOM   4554  C  CD    . ARG A 1 2025 ? 184.169 252.175 214.817 1.00 4.47  ? 2025 ARG A CD    1 
ATOM   4555  N  NE    . ARG A 1 2025 ? 184.853 252.331 216.094 1.00 9.38  ? 2025 ARG A NE    1 
ATOM   4556  C  CZ    . ARG A 1 2025 ? 184.251 252.340 217.274 1.00 8.70  ? 2025 ARG A CZ    1 
ATOM   4557  N  NH1   . ARG A 1 2025 ? 182.937 252.238 217.380 1.00 8.81  ? 2025 ARG A NH1   1 
ATOM   4558  N  NH2   . ARG A 1 2025 ? 184.983 252.462 218.374 1.00 9.38  ? 2025 ARG A NH2   1 
ATOM   4559  N  N     . SER A 1 2026 ? 184.011 251.041 210.269 1.00 4.03  ? 2026 SER A N     1 
ATOM   4560  C  CA    . SER A 1 2026 ? 183.525 250.569 208.983 1.00 3.87  ? 2026 SER A CA    1 
ATOM   4561  C  C     . SER A 1 2026 ? 182.280 251.343 208.577 1.00 5.47  ? 2026 SER A C     1 
ATOM   4562  O  O     . SER A 1 2026 ? 181.394 251.598 209.397 1.00 7.08  ? 2026 SER A O     1 
ATOM   4563  C  CB    . SER A 1 2026 ? 183.207 249.077 209.038 1.00 2.81  ? 2026 SER A CB    1 
ATOM   4564  O  OG    . SER A 1 2026 ? 184.273 248.339 209.602 1.00 3.64  ? 2026 SER A OG    1 
ATOM   4565  N  N     . ASN A 1 2027 ? 182.221 251.717 207.304 1.00 6.24  ? 2027 ASN A N     1 
ATOM   4566  C  CA    . ASN A 1 2027 ? 181.026 252.337 206.756 1.00 5.44  ? 2027 ASN A CA    1 
ATOM   4567  C  C     . ASN A 1 2027 ? 180.009 251.261 206.411 1.00 4.37  ? 2027 ASN A C     1 
ATOM   4568  O  O     . ASN A 1 2027 ? 180.347 250.255 205.781 1.00 15.28 ? 2027 ASN A O     1 
ATOM   4569  C  CB    . ASN A 1 2027 ? 181.370 253.165 205.519 1.00 4.99  ? 2027 ASN A CB    1 
ATOM   4570  C  CG    . ASN A 1 2027 ? 182.234 254.363 205.845 1.00 10.79 ? 2027 ASN A CG    1 
ATOM   4571  O  OD1   . ASN A 1 2027 ? 181.933 255.128 206.762 1.00 10.92 ? 2027 ASN A OD1   1 
ATOM   4572  N  ND2   . ASN A 1 2027 ? 183.320 254.532 205.099 1.00 13.46 ? 2027 ASN A ND2   1 
ATOM   4573  N  N     . LEU A 1 2028 ? 178.776 251.458 206.841 1.00 2.77  ? 2028 LEU A N     1 
ATOM   4574  C  CA    . LEU A 1 2028 ? 177.728 250.500 206.527 1.00 3.18  ? 2028 LEU A CA    1 
ATOM   4575  C  C     . LEU A 1 2028 ? 177.339 250.623 205.058 1.00 6.30  ? 2028 LEU A C     1 
ATOM   4576  O  O     . LEU A 1 2028 ? 177.146 251.740 204.567 1.00 16.40 ? 2028 LEU A O     1 
ATOM   4577  C  CB    . LEU A 1 2028 ? 176.506 250.723 207.412 1.00 2.33  ? 2028 LEU A CB    1 
ATOM   4578  C  CG    . LEU A 1 2028 ? 176.429 249.942 208.724 1.00 2.90  ? 2028 LEU A CG    1 
ATOM   4579  C  CD1   . LEU A 1 2028 ? 177.629 250.219 209.621 1.00 0.79  ? 2028 LEU A CD1   1 
ATOM   4580  C  CD2   . LEU A 1 2028 ? 175.122 250.231 209.438 1.00 1.57  ? 2028 LEU A CD2   1 
ATOM   4581  N  N     . PRO A 1 2029 ? 177.234 249.516 204.327 1.00 5.15  ? 2029 PRO A N     1 
ATOM   4582  C  CA    . PRO A 1 2029 ? 176.692 249.588 202.967 1.00 2.93  ? 2029 PRO A CA    1 
ATOM   4583  C  C     . PRO A 1 2029 ? 175.242 250.050 202.986 1.00 2.10  ? 2029 PRO A C     1 
ATOM   4584  O  O     . PRO A 1 2029 ? 174.506 249.817 203.947 1.00 3.74  ? 2029 PRO A O     1 
ATOM   4585  C  CB    . PRO A 1 2029 ? 176.822 248.151 202.452 1.00 2.47  ? 2029 PRO A CB    1 
ATOM   4586  C  CG    . PRO A 1 2029 ? 176.961 247.307 203.677 1.00 1.67  ? 2029 PRO A CG    1 
ATOM   4587  C  CD    . PRO A 1 2029 ? 177.671 248.157 204.683 1.00 2.63  ? 2029 PRO A CD    1 
ATOM   4588  N  N     . ASP A 1 2030 ? 174.838 250.719 201.903 1.00 3.11  ? 2030 ASP A N     1 
ATOM   4589  C  CA    . ASP A 1 2030 ? 173.513 251.331 201.855 1.00 2.46  ? 2030 ASP A CA    1 
ATOM   4590  C  C     . ASP A 1 2030 ? 172.407 250.289 201.969 1.00 1.81  ? 2030 ASP A C     1 
ATOM   4591  O  O     . ASP A 1 2030 ? 171.373 250.542 202.599 1.00 2.95  ? 2030 ASP A O     1 
ATOM   4592  C  CB    . ASP A 1 2030 ? 173.352 252.140 200.570 1.00 4.40  ? 2030 ASP A CB    1 
ATOM   4593  C  CG    . ASP A 1 2030 ? 174.247 253.356 200.531 1.00 11.93 ? 2030 ASP A CG    1 
ATOM   4594  O  OD1   . ASP A 1 2030 ? 174.684 253.739 199.427 1.00 10.73 ? 2030 ASP A OD1   1 
ATOM   4595  O  OD2   . ASP A 1 2030 ? 174.517 253.935 201.605 1.00 19.27 ? 2030 ASP A OD2   1 
ATOM   4596  N  N     . ASN A 1 2031 ? 172.599 249.117 201.362 1.00 2.58  ? 2031 ASN A N     1 
ATOM   4597  C  CA    . ASN A 1 2031 ? 171.576 248.078 201.435 1.00 1.12  ? 2031 ASN A CA    1 
ATOM   4598  C  C     . ASN A 1 2031 ? 171.346 247.617 202.868 1.00 1.86  ? 2031 ASN A C     1 
ATOM   4599  O  O     . ASN A 1 2031 ? 170.239 247.186 203.209 1.00 2.37  ? 2031 ASN A O     1 
ATOM   4600  C  CB    . ASN A 1 2031 ? 171.960 246.898 200.540 1.00 0.79  ? 2031 ASN A CB    1 
ATOM   4601  C  CG    . ASN A 1 2031 ? 173.032 246.025 201.154 1.00 0.77  ? 2031 ASN A CG    1 
ATOM   4602  O  OD1   . ASN A 1 2031 ? 174.116 246.497 201.487 1.00 1.25  ? 2031 ASN A OD1   1 
ATOM   4603  N  ND2   . ASN A 1 2031 ? 172.734 244.741 201.302 1.00 0.60  ? 2031 ASN A ND2   1 
ATOM   4604  N  N     . LEU A 1 2032 ? 172.372 247.691 203.718 1.00 1.30  ? 2032 LEU A N     1 
ATOM   4605  C  CA    . LEU A 1 2032 ? 172.175 247.407 205.134 1.00 0.70  ? 2032 LEU A CA    1 
ATOM   4606  C  C     . LEU A 1 2032 ? 171.493 248.571 205.843 1.00 1.04  ? 2032 LEU A C     1 
ATOM   4607  O  O     . LEU A 1 2032 ? 170.624 248.363 206.698 1.00 0.52  ? 2032 LEU A O     1 
ATOM   4608  C  CB    . LEU A 1 2032 ? 173.514 247.085 205.798 1.00 1.27  ? 2032 LEU A CB    1 
ATOM   4609  C  CG    . LEU A 1 2032 ? 173.501 246.852 207.310 1.00 0.58  ? 2032 LEU A CG    1 
ATOM   4610  C  CD1   . LEU A 1 2032 ? 172.670 245.634 207.670 1.00 0.24  ? 2032 LEU A CD1   1 
ATOM   4611  C  CD2   . LEU A 1 2032 ? 174.916 246.715 207.844 1.00 0.36  ? 2032 LEU A CD2   1 
ATOM   4612  N  N     . LYS A 1 2033 ? 171.864 249.805 205.491 1.00 1.77  ? 2033 LYS A N     1 
ATOM   4613  C  CA    . LYS A 1 2033 ? 171.327 250.974 206.177 1.00 1.12  ? 2033 LYS A CA    1 
ATOM   4614  C  C     . LYS A 1 2033 ? 169.836 251.154 205.924 1.00 0.73  ? 2033 LYS A C     1 
ATOM   4615  O  O     . LYS A 1 2033 ? 169.123 251.658 206.798 1.00 0.73  ? 2033 LYS A O     1 
ATOM   4616  C  CB    . LYS A 1 2033 ? 172.094 252.229 205.758 1.00 1.54  ? 2033 LYS A CB    1 
ATOM   4617  C  CG    . LYS A 1 2033 ? 173.506 252.275 206.301 1.00 1.79  ? 2033 LYS A CG    1 
ATOM   4618  C  CD    . LYS A 1 2033 ? 174.076 253.679 206.318 1.00 3.69  ? 2033 LYS A CD    1 
ATOM   4619  C  CE    . LYS A 1 2033 ? 174.862 253.980 205.059 1.00 8.61  ? 2033 LYS A CE    1 
ATOM   4620  N  NZ    . LYS A 1 2033 ? 175.865 255.052 205.292 1.00 8.17  ? 2033 LYS A NZ    1 
ATOM   4621  N  N     . LYS A 1 2034 ? 169.341 250.748 204.753 1.00 1.06  ? 2034 LYS A N     1 
ATOM   4622  C  CA    . LYS A 1 2034 ? 167.915 250.886 204.478 1.00 1.24  ? 2034 LYS A CA    1 
ATOM   4623  C  C     . LYS A 1 2034 ? 167.069 249.967 205.349 1.00 0.62  ? 2034 LYS A C     1 
ATOM   4624  O  O     . LYS A 1 2034 ? 165.850 250.150 205.420 1.00 0.72  ? 2034 LYS A O     1 
ATOM   4625  C  CB    . LYS A 1 2034 ? 167.621 250.610 203.002 1.00 1.37  ? 2034 LYS A CB    1 
ATOM   4626  C  CG    . LYS A 1 2034 ? 167.886 249.186 202.563 1.00 2.46  ? 2034 LYS A CG    1 
ATOM   4627  C  CD    . LYS A 1 2034 ? 167.615 249.007 201.083 1.00 3.23  ? 2034 LYS A CD    1 
ATOM   4628  C  CE    . LYS A 1 2034 ? 167.866 247.574 200.643 1.00 9.18  ? 2034 LYS A CE    1 
ATOM   4629  N  NZ    . LYS A 1 2034 ? 167.605 247.401 199.187 1.00 9.61  ? 2034 LYS A NZ    1 
ATOM   4630  N  N     . LEU A 1 2035 ? 167.682 248.988 206.008 1.00 0.52  ? 2035 LEU A N     1 
ATOM   4631  C  CA    . LEU A 1 2035 ? 166.975 248.088 206.905 1.00 0.23  ? 2035 LEU A CA    1 
ATOM   4632  C  C     . LEU A 1 2035 ? 166.827 248.651 208.312 1.00 0.14  ? 2035 LEU A C     1 
ATOM   4633  O  O     . LEU A 1 2035 ? 166.192 248.013 209.155 1.00 0.08  ? 2035 LEU A O     1 
ATOM   4634  C  CB    . LEU A 1 2035 ? 167.694 246.739 206.968 1.00 0.44  ? 2035 LEU A CB    1 
ATOM   4635  C  CG    . LEU A 1 2035 ? 167.947 246.039 205.634 1.00 0.51  ? 2035 LEU A CG    1 
ATOM   4636  C  CD1   . LEU A 1 2035 ? 168.826 244.815 205.836 1.00 0.23  ? 2035 LEU A CD1   1 
ATOM   4637  C  CD2   . LEU A 1 2035 ? 166.637 245.664 204.964 1.00 0.87  ? 2035 LEU A CD2   1 
ATOM   4638  N  N     . PHE A 1 2036 ? 167.395 249.821 208.582 1.00 0.13  ? 2036 PHE A N     1 
ATOM   4639  C  CA    . PHE A 1 2036 ? 167.372 250.405 209.913 1.00 0.11  ? 2036 PHE A CA    1 
ATOM   4640  C  C     . PHE A 1 2036 ? 166.887 251.842 209.840 1.00 0.14  ? 2036 PHE A C     1 
ATOM   4641  O  O     . PHE A 1 2036 ? 167.220 252.576 208.906 1.00 0.43  ? 2036 PHE A O     1 
ATOM   4642  C  CB    . PHE A 1 2036 ? 168.760 250.357 210.563 1.00 0.06  ? 2036 PHE A CB    1 
ATOM   4643  C  CG    . PHE A 1 2036 ? 169.231 248.969 210.878 1.00 0.05  ? 2036 PHE A CG    1 
ATOM   4644  C  CD1   . PHE A 1 2036 ? 169.948 248.240 209.945 1.00 0.06  ? 2036 PHE A CD1   1 
ATOM   4645  C  CD2   . PHE A 1 2036 ? 168.948 248.388 212.100 1.00 0.05  ? 2036 PHE A CD2   1 
ATOM   4646  C  CE1   . PHE A 1 2036 ? 170.379 246.961 210.228 1.00 0.08  ? 2036 PHE A CE1   1 
ATOM   4647  C  CE2   . PHE A 1 2036 ? 169.375 247.109 212.389 1.00 0.05  ? 2036 PHE A CE2   1 
ATOM   4648  C  CZ    . PHE A 1 2036 ? 170.093 246.394 211.450 1.00 0.06  ? 2036 PHE A CZ    1 
ATOM   4649  N  N     . ARG A 1 2037 ? 166.091 252.236 210.828 1.00 0.25  ? 2037 ARG A N     1 
ATOM   4650  C  CA    . ARG A 1 2037 ? 165.707 253.627 211.006 1.00 0.18  ? 2037 ARG A CA    1 
ATOM   4651  C  C     . ARG A 1 2037 ? 166.652 254.262 212.017 1.00 0.06  ? 2037 ARG A C     1 
ATOM   4652  O  O     . ARG A 1 2037 ? 166.789 253.771 213.139 1.00 0.13  ? 2037 ARG A O     1 
ATOM   4653  C  CB    . ARG A 1 2037 ? 164.256 253.735 211.471 1.00 0.11  ? 2037 ARG A CB    1 
ATOM   4654  C  CG    . ARG A 1 2037 ? 163.249 253.276 210.430 1.00 0.77  ? 2037 ARG A CG    1 
ATOM   4655  C  CD    . ARG A 1 2037 ? 163.086 254.307 209.323 1.00 0.83  ? 2037 ARG A CD    1 
ATOM   4656  N  NE    . ARG A 1 2037 ? 162.370 255.494 209.778 1.00 2.91  ? 2037 ARG A NE    1 
ATOM   4657  C  CZ    . ARG A 1 2037 ? 161.108 255.505 210.186 1.00 5.59  ? 2037 ARG A CZ    1 
ATOM   4658  N  NH1   . ARG A 1 2037 ? 160.343 254.428 210.109 1.00 3.42  ? 2037 ARG A NH1   1 
ATOM   4659  N  NH2   . ARG A 1 2037 ? 160.594 256.632 210.668 1.00 4.13  ? 2037 ARG A NH2   1 
ATOM   4660  N  N     . SER A 1 2038 ? 167.311 255.339 211.610 1.00 0.10  ? 2038 SER A N     1 
ATOM   4661  C  CA    . SER A 1 2038 ? 168.355 255.954 212.411 1.00 0.09  ? 2038 SER A CA    1 
ATOM   4662  C  C     . SER A 1 2038 ? 167.822 257.182 213.136 1.00 0.15  ? 2038 SER A C     1 
ATOM   4663  O  O     . SER A 1 2038 ? 166.979 257.912 212.610 1.00 0.65  ? 2038 SER A O     1 
ATOM   4664  C  CB    . SER A 1 2038 ? 169.555 256.335 211.542 1.00 0.12  ? 2038 SER A CB    1 
ATOM   4665  O  OG    . SER A 1 2038 ? 169.240 257.401 210.667 1.00 1.00  ? 2038 SER A OG    1 
ATOM   4666  N  N     . LEU A 1 2039 ? 168.313 257.394 214.354 1.00 0.15  ? 2039 LEU A N     1 
ATOM   4667  C  CA    . LEU A 1 2039 ? 167.994 258.581 215.134 1.00 0.15  ? 2039 LEU A CA    1 
ATOM   4668  C  C     . LEU A 1 2039 ? 169.266 259.129 215.753 1.00 0.15  ? 2039 LEU A C     1 
ATOM   4669  O  O     . LEU A 1 2039 ? 170.049 258.376 216.337 1.00 0.10  ? 2039 LEU A O     1 
ATOM   4670  C  CB    . LEU A 1 2039 ? 166.974 258.277 216.233 1.00 0.22  ? 2039 LEU A CB    1 
ATOM   4671  C  CG    . LEU A 1 2039 ? 166.585 259.523 217.029 1.00 0.53  ? 2039 LEU A CG    1 
ATOM   4672  C  CD1   . LEU A 1 2039 ? 165.898 260.551 216.154 1.00 0.76  ? 2039 LEU A CD1   1 
ATOM   4673  C  CD2   . LEU A 1 2039 ? 165.716 259.153 218.184 1.00 0.34  ? 2039 LEU A CD2   1 
ATOM   4674  N  N     . ALA A 1 2040 ? 169.467 260.437 215.629 1.00 0.25  ? 2040 ALA A N     1 
ATOM   4675  C  CA    . ALA A 1 2040 ? 170.634 261.085 216.212 1.00 0.30  ? 2040 ALA A CA    1 
ATOM   4676  C  C     . ALA A 1 2040 ? 170.382 261.362 217.689 1.00 0.35  ? 2040 ALA A C     1 
ATOM   4677  O  O     . ALA A 1 2040 ? 169.441 262.079 218.042 1.00 0.32  ? 2040 ALA A O     1 
ATOM   4678  C  CB    . ALA A 1 2040 ? 170.954 262.379 215.469 1.00 0.36  ? 2040 ALA A CB    1 
ATOM   4679  N  N     . MET A 1 2041 ? 171.210 260.782 218.546 1.00 0.42  ? 2041 MET A N     1 
ATOM   4680  C  CA    . MET A 1 2041 ? 171.189 261.043 219.981 1.00 0.56  ? 2041 MET A CA    1 
ATOM   4681  C  C     . MET A 1 2041 ? 172.515 261.716 220.313 1.00 0.66  ? 2041 MET A C     1 
ATOM   4682  O  O     . MET A 1 2041 ? 173.525 261.042 220.533 1.00 2.12  ? 2041 MET A O     1 
ATOM   4683  C  CB    . MET A 1 2041 ? 170.977 259.756 220.774 1.00 0.52  ? 2041 MET A CB    1 
ATOM   4684  C  CG    . MET A 1 2041 ? 169.664 259.051 220.461 1.00 0.32  ? 2041 MET A CG    1 
ATOM   4685  S  SD    . MET A 1 2041 ? 169.315 257.633 221.516 1.00 13.17 ? 2041 MET A SD    1 
ATOM   4686  C  CE    . MET A 1 2041 ? 169.375 258.381 223.141 1.00 0.39  ? 2041 MET A CE    1 
ATOM   4687  N  N     . THR A 1 2042 ? 172.512 263.044 220.331 1.00 1.07  ? 2042 THR A N     1 
ATOM   4688  C  CA    . THR A 1 2042 ? 173.738 263.826 220.451 1.00 1.48  ? 2042 THR A CA    1 
ATOM   4689  C  C     . THR A 1 2042 ? 173.809 264.656 221.719 1.00 2.68  ? 2042 THR A C     1 
ATOM   4690  O  O     . THR A 1 2042 ? 174.872 264.732 222.337 1.00 7.08  ? 2042 THR A O     1 
ATOM   4691  C  CB    . THR A 1 2042 ? 173.893 264.748 219.228 1.00 2.46  ? 2042 THR A CB    1 
ATOM   4692  O  OG1   . THR A 1 2042 ? 173.718 263.990 218.027 1.00 1.77  ? 2042 THR A OG1   1 
ATOM   4693  C  CG2   . THR A 1 2042 ? 175.271 265.386 219.212 1.00 3.33  ? 2042 THR A CG2   1 
ATOM   4694  N  N     . LYS A 1 2043 ? 172.708 265.286 222.131 1.00 4.61  ? 2043 LYS A N     1 
ATOM   4695  C  CA    . LYS A 1 2043 ? 172.678 266.162 223.302 1.00 2.91  ? 2043 LYS A CA    1 
ATOM   4696  C  C     . LYS A 1 2043 ? 171.694 265.607 224.323 1.00 3.08  ? 2043 LYS A C     1 
ATOM   4697  O  O     . LYS A 1 2043 ? 170.487 265.887 224.253 1.00 4.38  ? 2043 LYS A O     1 
ATOM   4698  C  CB    . LYS A 1 2043 ? 172.305 267.590 222.911 1.00 4.17  ? 2043 LYS A CB    1 
ATOM   4699  C  CG    . LYS A 1 2043 ? 173.277 268.259 221.960 1.00 9.55  ? 2043 LYS A CG    1 
ATOM   4700  C  CD    . LYS A 1 2043 ? 174.623 268.508 222.619 1.00 17.76 ? 2043 LYS A CD    1 
ATOM   4701  C  CE    . LYS A 1 2043 ? 175.564 269.249 221.684 1.00 18.43 ? 2043 LYS A CE    1 
ATOM   4702  N  NZ    . LYS A 1 2043 ? 176.903 269.466 222.297 1.00 27.99 ? 2043 LYS A NZ    1 
ATOM   4703  N  N     . PRO A 1 2044 ? 172.162 264.820 225.289 1.00 3.94  ? 2044 PRO A N     1 
ATOM   4704  C  CA    . PRO A 1 2044 ? 171.270 264.363 226.359 1.00 1.50  ? 2044 PRO A CA    1 
ATOM   4705  C  C     . PRO A 1 2044 ? 170.806 265.521 227.226 1.00 2.89  ? 2044 PRO A C     1 
ATOM   4706  O  O     . PRO A 1 2044 ? 171.508 266.520 227.402 1.00 3.65  ? 2044 PRO A O     1 
ATOM   4707  C  CB    . PRO A 1 2044 ? 172.137 263.382 227.159 1.00 1.66  ? 2044 PRO A CB    1 
ATOM   4708  C  CG    . PRO A 1 2044 ? 173.334 263.114 226.312 1.00 1.11  ? 2044 PRO A CG    1 
ATOM   4709  C  CD    . PRO A 1 2044 ? 173.529 264.304 225.444 1.00 1.97  ? 2044 PRO A CD    1 
ATOM   4710  N  N     . ASP A 1 2045 ? 169.601 265.376 227.774 1.00 2.67  ? 2045 ASP A N     1 
ATOM   4711  C  CA    . ASP A 1 2045 ? 168.984 266.413 228.600 1.00 1.85  ? 2045 ASP A CA    1 
ATOM   4712  C  C     . ASP A 1 2045 ? 169.478 266.249 230.037 1.00 2.15  ? 2045 ASP A C     1 
ATOM   4713  O  O     . ASP A 1 2045 ? 168.806 265.688 230.907 1.00 1.78  ? 2045 ASP A O     1 
ATOM   4714  C  CB    . ASP A 1 2045 ? 167.466 266.335 228.498 1.00 1.92  ? 2045 ASP A CB    1 
ATOM   4715  C  CG    . ASP A 1 2045 ? 166.983 266.331 227.057 1.00 5.47  ? 2045 ASP A CG    1 
ATOM   4716  O  OD1   . ASP A 1 2045 ? 167.452 267.179 226.269 1.00 7.47  ? 2045 ASP A OD1   1 
ATOM   4717  O  OD2   . ASP A 1 2045 ? 166.136 265.486 226.708 1.00 3.83  ? 2045 ASP A OD2   1 
ATOM   4718  N  N     . ARG A 1 2046 ? 170.686 266.768 230.279 1.00 2.04  ? 2046 ARG A N     1 
ATOM   4719  C  CA    . ARG A 1 2046 ? 171.382 266.504 231.536 1.00 1.11  ? 2046 ARG A CA    1 
ATOM   4720  C  C     . ARG A 1 2046 ? 170.651 267.098 232.734 1.00 1.58  ? 2046 ARG A C     1 
ATOM   4721  O  O     . ARG A 1 2046 ? 170.544 266.450 233.781 1.00 1.58  ? 2046 ARG A O     1 
ATOM   4722  C  CB    . ARG A 1 2046 ? 172.807 267.046 231.469 1.00 1.29  ? 2046 ARG A CB    1 
ATOM   4723  C  CG    . ARG A 1 2046 ? 173.702 266.318 230.492 1.00 1.68  ? 2046 ARG A CG    1 
ATOM   4724  C  CD    . ARG A 1 2046 ? 175.090 266.917 230.486 1.00 4.45  ? 2046 ARG A CD    1 
ATOM   4725  N  NE    . ARG A 1 2046 ? 175.967 266.245 229.536 1.00 7.45  ? 2046 ARG A NE    1 
ATOM   4726  C  CZ    . ARG A 1 2046 ? 177.219 266.604 229.292 1.00 13.73 ? 2046 ARG A CZ    1 
ATOM   4727  N  NH1   . ARG A 1 2046 ? 177.778 267.628 229.918 1.00 18.46 ? 2046 ARG A NH1   1 
ATOM   4728  N  NH2   . ARG A 1 2046 ? 177.927 265.922 228.398 1.00 13.74 ? 2046 ARG A NH2   1 
ATOM   4729  N  N     . GLN A 1 2047 ? 170.149 268.328 232.607 1.00 1.69  ? 2047 GLN A N     1 
ATOM   4730  C  CA    . GLN A 1 2047 ? 169.541 268.987 233.758 1.00 1.95  ? 2047 GLN A CA    1 
ATOM   4731  C  C     . GLN A 1 2047 ? 168.254 268.291 234.183 1.00 3.78  ? 2047 GLN A C     1 
ATOM   4732  O  O     . GLN A 1 2047 ? 167.925 268.259 235.375 1.00 5.04  ? 2047 GLN A O     1 
ATOM   4733  C  CB    . GLN A 1 2047 ? 169.307 270.471 233.452 1.00 4.94  ? 2047 GLN A CB    1 
ATOM   4734  C  CG    . GLN A 1 2047 ? 168.342 270.779 232.317 1.00 17.03 ? 2047 GLN A CG    1 
ATOM   4735  C  CD    . GLN A 1 2047 ? 166.889 270.775 232.750 1.00 15.99 ? 2047 GLN A CD    1 
ATOM   4736  O  OE1   . GLN A 1 2047 ? 166.572 271.082 233.899 1.00 15.01 ? 2047 GLN A OE1   1 
ATOM   4737  N  NE2   . GLN A 1 2047 ? 165.997 270.433 231.827 1.00 14.33 ? 2047 GLN A NE2   1 
ATOM   4738  N  N     . LEU A 1 2048 ? 167.514 267.718 233.232 1.00 2.91  ? 2048 LEU A N     1 
ATOM   4739  C  CA    . LEU A 1 2048 ? 166.312 266.973 233.590 1.00 1.28  ? 2048 LEU A CA    1 
ATOM   4740  C  C     . LEU A 1 2048 ? 166.664 265.649 234.259 1.00 1.89  ? 2048 LEU A C     1 
ATOM   4741  O  O     . LEU A 1 2048 ? 166.021 265.249 235.236 1.00 5.01  ? 2048 LEU A O     1 
ATOM   4742  C  CB    . LEU A 1 2048 ? 165.443 266.741 232.353 1.00 2.77  ? 2048 LEU A CB    1 
ATOM   4743  C  CG    . LEU A 1 2048 ? 164.150 265.962 232.610 1.00 2.13  ? 2048 LEU A CG    1 
ATOM   4744  C  CD1   . LEU A 1 2048 ? 163.274 266.684 233.623 1.00 0.47  ? 2048 LEU A CD1   1 
ATOM   4745  C  CD2   . LEU A 1 2048 ? 163.394 265.719 231.318 1.00 1.33  ? 2048 LEU A CD2   1 
ATOM   4746  N  N     . ILE A 1 2049 ? 167.682 264.953 233.747 1.00 1.14  ? 2049 ILE A N     1 
ATOM   4747  C  CA    . ILE A 1 2049 ? 168.120 263.704 234.369 1.00 1.08  ? 2049 ILE A CA    1 
ATOM   4748  C  C     . ILE A 1 2049 ? 168.594 263.959 235.794 1.00 1.82  ? 2049 ILE A C     1 
ATOM   4749  O  O     . ILE A 1 2049 ? 168.252 263.221 236.723 1.00 5.93  ? 2049 ILE A O     1 
ATOM   4750  C  CB    . ILE A 1 2049 ? 169.219 263.032 233.524 1.00 1.06  ? 2049 ILE A CB    1 
ATOM   4751  C  CG1   . ILE A 1 2049 ? 168.716 262.733 232.113 1.00 0.88  ? 2049 ILE A CG1   1 
ATOM   4752  C  CG2   . ILE A 1 2049 ? 169.725 261.772 234.206 1.00 0.39  ? 2049 ILE A CG2   1 
ATOM   4753  C  CD1   . ILE A 1 2049 ? 169.794 262.260 231.163 1.00 0.41  ? 2049 ILE A CD1   1 
ATOM   4754  N  N     . ALA A 1 2050 ? 169.390 265.012 235.984 1.00 1.65  ? 2050 ALA A N     1 
ATOM   4755  C  CA    . ALA A 1 2050 ? 169.891 265.329 237.315 1.00 0.94  ? 2050 ALA A CA    1 
ATOM   4756  C  C     . ALA A 1 2050 ? 168.756 265.697 238.262 1.00 1.50  ? 2050 ALA A C     1 
ATOM   4757  O  O     . ALA A 1 2050 ? 168.752 265.284 239.427 1.00 2.66  ? 2050 ALA A O     1 
ATOM   4758  C  CB    . ALA A 1 2050 ? 170.914 266.461 237.235 1.00 1.10  ? 2050 ALA A CB    1 
ATOM   4759  N  N     . GLN A 1 2051 ? 167.779 266.467 237.779 1.00 2.70  ? 2051 GLN A N     1 
ATOM   4760  C  CA    . GLN A 1 2051 ? 166.696 266.922 238.644 1.00 2.22  ? 2051 GLN A CA    1 
ATOM   4761  C  C     . GLN A 1 2051 ? 165.827 265.755 239.098 1.00 2.37  ? 2051 GLN A C     1 
ATOM   4762  O  O     . GLN A 1 2051 ? 165.465 265.658 240.275 1.00 5.03  ? 2051 GLN A O     1 
ATOM   4763  C  CB    . GLN A 1 2051 ? 165.864 267.981 237.919 1.00 4.15  ? 2051 GLN A CB    1 
ATOM   4764  C  CG    . GLN A 1 2051 ? 164.821 268.678 238.781 1.00 6.67  ? 2051 GLN A CG    1 
ATOM   4765  C  CD    . GLN A 1 2051 ? 163.508 267.923 238.855 1.00 14.94 ? 2051 GLN A CD    1 
ATOM   4766  O  OE1   . GLN A 1 2051 ? 163.131 267.211 237.924 1.00 12.11 ? 2051 GLN A OE1   1 
ATOM   4767  N  NE2   . GLN A 1 2051 ? 162.806 268.070 239.972 1.00 12.72 ? 2051 GLN A NE2   1 
ATOM   4768  N  N     . VAL A 1 2052 ? 165.484 264.855 238.176 1.00 3.92  ? 2052 VAL A N     1 
ATOM   4769  C  CA    . VAL A 1 2052 ? 164.606 263.739 238.517 1.00 2.55  ? 2052 VAL A CA    1 
ATOM   4770  C  C     . VAL A 1 2052 ? 165.323 262.741 239.417 1.00 2.53  ? 2052 VAL A C     1 
ATOM   4771  O  O     . VAL A 1 2052 ? 164.738 262.218 240.373 1.00 4.60  ? 2052 VAL A O     1 
ATOM   4772  C  CB    . VAL A 1 2052 ? 164.065 263.077 237.236 1.00 1.70  ? 2052 VAL A CB    1 
ATOM   4773  C  CG1   . VAL A 1 2052 ? 163.235 261.848 237.572 1.00 0.92  ? 2052 VAL A CG1   1 
ATOM   4774  C  CG2   . VAL A 1 2052 ? 163.239 264.072 236.445 1.00 2.27  ? 2052 VAL A CG2   1 
ATOM   4775  N  N     . MET A 1 2053 ? 166.598 262.456 239.132 1.00 2.37  ? 2053 MET A N     1 
ATOM   4776  C  CA    . MET A 1 2053 ? 167.343 261.506 239.956 1.00 2.69  ? 2053 MET A CA    1 
ATOM   4777  C  C     . MET A 1 2053 ? 167.511 262.009 241.384 1.00 4.77  ? 2053 MET A C     1 
ATOM   4778  O  O     . MET A 1 2053 ? 167.331 261.249 242.341 1.00 7.56  ? 2053 MET A O     1 
ATOM   4779  C  CB    . MET A 1 2053 ? 168.710 261.221 239.339 1.00 3.62  ? 2053 MET A CB    1 
ATOM   4780  C  CG    . MET A 1 2053 ? 168.687 260.245 238.186 1.00 3.14  ? 2053 MET A CG    1 
ATOM   4781  S  SD    . MET A 1 2053 ? 170.314 260.106 237.437 1.00 27.24 ? 2053 MET A SD    1 
ATOM   4782  C  CE    . MET A 1 2053 ? 171.149 259.123 238.679 1.00 4.88  ? 2053 MET A CE    1 
ATOM   4783  N  N     . LEU A 1 2054 ? 167.865 263.285 241.549 1.00 2.71  ? 2054 LEU A N     1 
ATOM   4784  C  CA    . LEU A 1 2054 ? 168.009 263.836 242.892 1.00 3.26  ? 2054 LEU A CA    1 
ATOM   4785  C  C     . LEU A 1 2054 ? 166.670 263.914 243.608 1.00 6.25  ? 2054 LEU A C     1 
ATOM   4786  O  O     . LEU A 1 2054 ? 166.608 263.725 244.827 1.00 11.18 ? 2054 LEU A O     1 
ATOM   4787  C  CB    . LEU A 1 2054 ? 168.665 265.215 242.831 1.00 3.68  ? 2054 LEU A CB    1 
ATOM   4788  C  CG    . LEU A 1 2054 ? 170.141 265.240 242.435 1.00 4.09  ? 2054 LEU A CG    1 
ATOM   4789  C  CD1   . LEU A 1 2054 ? 170.594 266.656 242.132 1.00 3.38  ? 2054 LEU A CD1   1 
ATOM   4790  C  CD2   . LEU A 1 2054 ? 171.009 264.614 243.517 1.00 3.13  ? 2054 LEU A CD2   1 
ATOM   4791  N  N     . TYR A 1 2055 ? 165.594 264.188 242.869 1.00 3.89  ? 2055 TYR A N     1 
ATOM   4792  C  CA    . TYR A 1 2055 ? 164.267 264.229 243.468 1.00 4.62  ? 2055 TYR A CA    1 
ATOM   4793  C  C     . TYR A 1 2055 ? 163.783 262.837 243.858 1.00 3.62  ? 2055 TYR A C     1 
ATOM   4794  O  O     . TYR A 1 2055 ? 163.090 262.685 244.870 1.00 4.60  ? 2055 TYR A O     1 
ATOM   4795  C  CB    . TYR A 1 2055 ? 163.294 264.900 242.498 1.00 5.17  ? 2055 TYR A CB    1 
ATOM   4796  C  CG    . TYR A 1 2055 ? 161.851 264.922 242.941 1.00 3.43  ? 2055 TYR A CG    1 
ATOM   4797  C  CD1   . TYR A 1 2055 ? 161.439 265.730 243.990 1.00 3.14  ? 2055 TYR A CD1   1 
ATOM   4798  C  CD2   . TYR A 1 2055 ? 160.894 264.166 242.283 1.00 4.61  ? 2055 TYR A CD2   1 
ATOM   4799  C  CE1   . TYR A 1 2055 ? 160.119 265.762 244.389 1.00 6.43  ? 2055 TYR A CE1   1 
ATOM   4800  C  CE2   . TYR A 1 2055 ? 159.572 264.194 242.671 1.00 6.62  ? 2055 TYR A CE2   1 
ATOM   4801  C  CZ    . TYR A 1 2055 ? 159.188 264.994 243.724 1.00 11.52 ? 2055 TYR A CZ    1 
ATOM   4802  O  OH    . TYR A 1 2055 ? 157.872 265.022 244.113 1.00 15.46 ? 2055 TYR A OH    1 
ATOM   4803  N  N     . SER A 1 2056 ? 164.138 261.815 243.077 1.00 4.56  ? 2056 SER A N     1 
ATOM   4804  C  CA    . SER A 1 2056 ? 163.742 260.450 243.410 1.00 3.88  ? 2056 SER A CA    1 
ATOM   4805  C  C     . SER A 1 2056 ? 164.558 259.884 244.563 1.00 6.78  ? 2056 SER A C     1 
ATOM   4806  O  O     . SER A 1 2056 ? 164.098 258.964 245.248 1.00 10.39 ? 2056 SER A O     1 
ATOM   4807  C  CB    . SER A 1 2056 ? 163.874 259.549 242.183 1.00 3.73  ? 2056 SER A CB    1 
ATOM   4808  O  OG    . SER A 1 2056 ? 165.213 259.492 241.732 1.00 6.92  ? 2056 SER A OG    1 
ATOM   4809  N  N     . GLN A 1 2057 ? 165.762 260.409 244.790 1.00 7.76  ? 2057 GLN A N     1 
ATOM   4810  C  CA    . GLN A 1 2057 ? 166.599 259.953 245.889 1.00 4.29  ? 2057 GLN A CA    1 
ATOM   4811  C  C     . GLN A 1 2057 ? 166.231 260.594 247.220 1.00 7.81  ? 2057 GLN A C     1 
ATOM   4812  O  O     . GLN A 1 2057 ? 166.718 260.139 248.260 1.00 12.93 ? 2057 GLN A O     1 
ATOM   4813  C  CB    . GLN A 1 2057 ? 168.071 260.228 245.578 1.00 5.99  ? 2057 GLN A CB    1 
ATOM   4814  C  CG    . GLN A 1 2057 ? 168.775 259.105 244.838 1.00 4.59  ? 2057 GLN A CG    1 
ATOM   4815  C  CD    . GLN A 1 2057 ? 169.843 259.613 243.885 1.00 10.09 ? 2057 GLN A CD    1 
ATOM   4816  O  OE1   . GLN A 1 2057 ? 170.329 260.734 244.025 1.00 11.76 ? 2057 GLN A OE1   1 
ATOM   4817  N  NE2   . GLN A 1 2057 ? 170.213 258.787 242.914 1.00 9.17  ? 2057 GLN A NE2   1 
ATOM   4818  N  N     . GLY A 1 2058 ? 165.390 261.622 247.220 1.00 6.71  ? 2058 GLY A N     1 
ATOM   4819  C  CA    . GLY A 1 2058 ? 164.960 262.267 248.441 1.00 5.10  ? 2058 GLY A CA    1 
ATOM   4820  C  C     . GLY A 1 2058 ? 165.590 263.610 248.741 1.00 6.46  ? 2058 GLY A C     1 
ATOM   4821  O  O     . GLY A 1 2058 ? 165.393 264.127 249.846 1.00 13.86 ? 2058 GLY A O     1 
ATOM   4822  N  N     . PHE A 1 2059 ? 166.338 264.192 247.809 1.00 6.12  ? 2059 PHE A N     1 
ATOM   4823  C  CA    . PHE A 1 2059 ? 166.916 265.513 248.027 1.00 6.06  ? 2059 PHE A CA    1 
ATOM   4824  C  C     . PHE A 1 2059 ? 165.822 266.570 247.938 1.00 8.97  ? 2059 PHE A C     1 
ATOM   4825  O  O     . PHE A 1 2059 ? 165.157 266.696 246.905 1.00 14.60 ? 2059 PHE A O     1 
ATOM   4826  C  CB    . PHE A 1 2059 ? 168.011 265.788 247.001 1.00 6.26  ? 2059 PHE A CB    1 
ATOM   4827  C  CG    . PHE A 1 2059 ? 169.274 265.009 247.227 1.00 5.96  ? 2059 PHE A CG    1 
ATOM   4828  C  CD1   . PHE A 1 2059 ? 169.403 263.718 246.744 1.00 6.16  ? 2059 PHE A CD1   1 
ATOM   4829  C  CD2   . PHE A 1 2059 ? 170.339 265.574 247.907 1.00 6.56  ? 2059 PHE A CD2   1 
ATOM   4830  C  CE1   . PHE A 1 2059 ? 170.566 263.003 246.942 1.00 4.99  ? 2059 PHE A CE1   1 
ATOM   4831  C  CE2   . PHE A 1 2059 ? 171.504 264.862 248.108 1.00 8.47  ? 2059 PHE A CE2   1 
ATOM   4832  C  CZ    . PHE A 1 2059 ? 171.617 263.575 247.625 1.00 4.52  ? 2059 PHE A CZ    1 
ATOM   4833  N  N     . ARG A 1 2060 ? 165.634 267.332 249.016 1.00 9.33  ? 2060 ARG A N     1 
ATOM   4834  C  CA    . ARG A 1 2060 ? 164.576 268.336 249.031 1.00 10.77 ? 2060 ARG A CA    1 
ATOM   4835  C  C     . ARG A 1 2060 ? 164.870 269.484 248.073 1.00 11.56 ? 2060 ARG A C     1 
ATOM   4836  O  O     . ARG A 1 2060 ? 163.943 270.045 247.476 1.00 18.41 ? 2060 ARG A O     1 
ATOM   4837  C  CB    . ARG A 1 2060 ? 164.370 268.865 250.449 1.00 17.09 ? 2060 ARG A CB    1 
ATOM   4838  C  CG    . ARG A 1 2060 ? 163.197 269.827 250.588 1.00 31.01 ? 2060 ARG A CG    1 
ATOM   4839  C  CD    . ARG A 1 2060 ? 163.007 270.263 252.032 1.00 26.81 ? 2060 ARG A CD    1 
ATOM   4840  N  NE    . ARG A 1 2060 ? 164.143 271.034 252.519 1.00 28.91 ? 2060 ARG A NE    1 
ATOM   4841  C  CZ    . ARG A 1 2060 ? 164.970 270.625 253.470 1.00 32.99 ? 2060 ARG A CZ    1 
ATOM   4842  N  NH1   . ARG A 1 2060 ? 164.821 269.448 254.056 1.00 34.63 ? 2060 ARG A NH1   1 
ATOM   4843  N  NH2   . ARG A 1 2060 ? 165.974 271.417 253.842 1.00 30.16 ? 2060 ARG A NH2   1 
ATOM   4844  N  N     . THR A 1 2061 ? 166.141 269.841 247.903 1.00 12.96 ? 2061 THR A N     1 
ATOM   4845  C  CA    . THR A 1 2061 ? 166.556 270.936 247.027 1.00 8.63  ? 2061 THR A CA    1 
ATOM   4846  C  C     . THR A 1 2061 ? 167.037 270.429 245.677 1.00 10.97 ? 2061 THR A C     1 
ATOM   4847  O  O     . THR A 1 2061 ? 168.003 270.955 245.116 1.00 14.27 ? 2061 THR A O     1 
ATOM   4848  C  CB    . THR A 1 2061 ? 167.639 271.773 247.700 1.00 10.84 ? 2061 THR A CB    1 
ATOM   4849  O  OG1   . THR A 1 2061 ? 168.669 270.914 248.202 1.00 16.03 ? 2061 THR A OG1   1 
ATOM   4850  C  CG2   . THR A 1 2061 ? 167.054 272.576 248.848 1.00 10.17 ? 2061 THR A CG2   1 
ATOM   4851  N  N     . ALA A 1 2062 ? 166.377 269.396 245.140 1.00 12.82 ? 2062 ALA A N     1 
ATOM   4852  C  CA    . ALA A 1 2062 ? 166.832 268.773 243.902 1.00 7.76  ? 2062 ALA A CA    1 
ATOM   4853  C  C     . ALA A 1 2062 ? 166.881 269.770 242.751 1.00 10.48 ? 2062 ALA A C     1 
ATOM   4854  O  O     . ALA A 1 2062 ? 167.797 269.724 241.922 1.00 15.71 ? 2062 ALA A O     1 
ATOM   4855  C  CB    . ALA A 1 2062 ? 165.929 267.593 243.548 1.00 6.50  ? 2062 ALA A CB    1 
ATOM   4856  N  N     . GLU A 1 2063 ? 165.900 270.674 242.674 1.00 13.62 ? 2063 GLU A N     1 
ATOM   4857  C  CA    . GLU A 1 2063 ? 165.911 271.675 241.613 1.00 13.57 ? 2063 GLU A CA    1 
ATOM   4858  C  C     . GLU A 1 2063 ? 167.104 272.614 241.749 1.00 10.19 ? 2063 GLU A C     1 
ATOM   4859  O  O     . GLU A 1 2063 ? 167.752 272.953 240.751 1.00 13.54 ? 2063 GLU A O     1 
ATOM   4860  C  CB    . GLU A 1 2063 ? 164.602 272.464 241.617 1.00 19.83 ? 2063 GLU A CB    1 
ATOM   4861  C  CG    . GLU A 1 2063 ? 163.385 271.644 241.233 1.00 24.31 ? 2063 GLU A CG    1 
ATOM   4862  C  CD    . GLU A 1 2063 ? 162.103 272.452 241.266 1.00 32.31 ? 2063 GLU A CD    1 
ATOM   4863  O  OE1   . GLU A 1 2063 ? 162.145 273.618 241.709 1.00 32.55 ? 2063 GLU A OE1   1 
ATOM   4864  O  OE2   . GLU A 1 2063 ? 161.054 271.920 240.847 1.00 31.55 ? 2063 GLU A OE2   1 
ATOM   4865  N  N     . VAL A 1 2064 ? 167.405 273.048 242.972 1.00 10.91 ? 2064 VAL A N     1 
ATOM   4866  C  CA    . VAL A 1 2064 ? 168.573 273.896 243.188 1.00 10.75 ? 2064 VAL A CA    1 
ATOM   4867  C  C     . VAL A 1 2064 ? 169.852 273.128 242.885 1.00 10.59 ? 2064 VAL A C     1 
ATOM   4868  O  O     . VAL A 1 2064 ? 170.759 273.642 242.220 1.00 11.66 ? 2064 VAL A O     1 
ATOM   4869  C  CB    . VAL A 1 2064 ? 168.570 274.456 244.621 1.00 10.61 ? 2064 VAL A CB    1 
ATOM   4870  C  CG1   . VAL A 1 2064 ? 169.852 275.227 244.893 1.00 14.71 ? 2064 VAL A CG1   1 
ATOM   4871  C  CG2   . VAL A 1 2064 ? 167.358 275.339 244.842 1.00 8.63  ? 2064 VAL A CG2   1 
ATOM   4872  N  N     . LEU A 1 2065 ? 169.946 271.883 243.360 1.00 10.29 ? 2065 LEU A N     1 
ATOM   4873  C  CA    . LEU A 1 2065 ? 171.151 271.091 243.136 1.00 9.12  ? 2065 LEU A CA    1 
ATOM   4874  C  C     . LEU A 1 2065 ? 171.358 270.794 241.656 1.00 7.05  ? 2065 LEU A C     1 
ATOM   4875  O  O     . LEU A 1 2065 ? 172.490 270.847 241.161 1.00 11.71 ? 2065 LEU A O     1 
ATOM   4876  C  CB    . LEU A 1 2065 ? 171.078 269.794 243.939 1.00 9.40  ? 2065 LEU A CB    1 
ATOM   4877  C  CG    . LEU A 1 2065 ? 171.076 269.951 245.459 1.00 7.86  ? 2065 LEU A CG    1 
ATOM   4878  C  CD1   . LEU A 1 2065 ? 170.912 268.603 246.131 1.00 9.76  ? 2065 LEU A CD1   1 
ATOM   4879  C  CD2   . LEU A 1 2065 ? 172.342 270.636 245.928 1.00 9.46  ? 2065 LEU A CD2   1 
ATOM   4880  N  N     . ALA A 1 2066 ? 170.282 270.478 240.935 1.00 7.94  ? 2066 ALA A N     1 
ATOM   4881  C  CA    . ALA A 1 2066 ? 170.408 270.175 239.513 1.00 8.57  ? 2066 ALA A CA    1 
ATOM   4882  C  C     . ALA A 1 2066 ? 170.828 271.404 238.717 1.00 10.13 ? 2066 ALA A C     1 
ATOM   4883  O  O     . ALA A 1 2066 ? 171.609 271.296 237.765 1.00 9.25  ? 2066 ALA A O     1 
ATOM   4884  C  CB    . ALA A 1 2066 ? 169.095 269.609 238.979 1.00 6.43  ? 2066 ALA A CB    1 
ATOM   4885  N  N     . ASN A 1 2067 ? 170.322 272.582 239.092 1.00 11.48 ? 2067 ASN A N     1 
ATOM   4886  C  CA    . ASN A 1 2067 ? 170.696 273.814 238.406 1.00 11.35 ? 2067 ASN A CA    1 
ATOM   4887  C  C     . ASN A 1 2067 ? 172.138 274.219 238.663 1.00 10.35 ? 2067 ASN A C     1 
ATOM   4888  O  O     . ASN A 1 2067 ? 172.639 275.118 237.982 1.00 21.44 ? 2067 ASN A O     1 
ATOM   4889  C  CB    . ASN A 1 2067 ? 169.768 274.958 238.818 1.00 14.99 ? 2067 ASN A CB    1 
ATOM   4890  C  CG    . ASN A 1 2067 ? 168.427 274.894 238.130 1.00 19.25 ? 2067 ASN A CG    1 
ATOM   4891  O  OD1   . ASN A 1 2067 ? 168.348 274.879 236.903 1.00 20.75 ? 2067 ASN A OD1   1 
ATOM   4892  N  ND2   . ASN A 1 2067 ? 167.359 274.865 238.916 1.00 18.18 ? 2067 ASN A ND2   1 
ATOM   4893  N  N     . LYS A 1 2068 ? 172.809 273.596 239.625 1.00 7.27  ? 2068 LYS A N     1 
ATOM   4894  C  CA    . LYS A 1 2068 ? 174.211 273.873 239.908 1.00 7.43  ? 2068 LYS A CA    1 
ATOM   4895  C  C     . LYS A 1 2068 ? 175.151 272.790 239.409 1.00 7.73  ? 2068 LYS A C     1 
ATOM   4896  O  O     . LYS A 1 2068 ? 176.202 273.108 238.850 1.00 7.07  ? 2068 LYS A O     1 
ATOM   4897  C  CB    . LYS A 1 2068 ? 174.417 274.058 241.416 1.00 8.69  ? 2068 LYS A CB    1 
ATOM   4898  C  CG    . LYS A 1 2068 ? 173.587 275.168 242.026 1.00 12.08 ? 2068 LYS A CG    1 
ATOM   4899  C  CD    . LYS A 1 2068 ? 173.817 275.266 243.521 1.00 8.23  ? 2068 LYS A CD    1 
ATOM   4900  C  CE    . LYS A 1 2068 ? 173.323 276.594 244.063 1.00 13.83 ? 2068 LYS A CE    1 
ATOM   4901  N  NZ    . LYS A 1 2068 ? 173.973 277.743 243.379 1.00 15.60 ? 2068 LYS A NZ    1 
ATOM   4902  N  N     . ILE A 1 2069 ? 174.795 271.517 239.590 1.00 5.57  ? 2069 ILE A N     1 
ATOM   4903  C  CA    . ILE A 1 2069 ? 175.716 270.435 239.260 1.00 4.69  ? 2069 ILE A CA    1 
ATOM   4904  C  C     . ILE A 1 2069 ? 175.925 270.309 237.753 1.00 5.90  ? 2069 ILE A C     1 
ATOM   4905  O  O     . ILE A 1 2069 ? 177.036 270.016 237.300 1.00 6.80  ? 2069 ILE A O     1 
ATOM   4906  C  CB    . ILE A 1 2069 ? 175.233 269.112 239.890 1.00 5.22  ? 2069 ILE A CB    1 
ATOM   4907  C  CG1   . ILE A 1 2069 ? 176.340 268.060 239.809 1.00 8.52  ? 2069 ILE A CG1   1 
ATOM   4908  C  CG2   . ILE A 1 2069 ? 173.950 268.614 239.240 1.00 3.08  ? 2069 ILE A CG2   1 
ATOM   4909  C  CD1   . ILE A 1 2069 ? 177.545 268.409 240.631 1.00 4.49  ? 2069 ILE A CD1   1 
ATOM   4910  N  N     . VAL A 1 2070 ? 174.885 270.529 236.955 1.00 4.55  ? 2070 VAL A N     1 
ATOM   4911  C  CA    . VAL A 1 2070 ? 174.982 270.351 235.509 1.00 4.65  ? 2070 VAL A CA    1 
ATOM   4912  C  C     . VAL A 1 2070 ? 175.812 271.477 234.894 1.00 5.22  ? 2070 VAL A C     1 
ATOM   4913  O  O     . VAL A 1 2070 ? 176.706 271.193 234.084 1.00 4.50  ? 2070 VAL A O     1 
ATOM   4914  C  CB    . VAL A 1 2070 ? 173.590 270.243 234.863 1.00 4.41  ? 2070 VAL A CB    1 
ATOM   4915  C  CG1   . VAL A 1 2070 ? 173.707 270.133 233.353 1.00 1.77  ? 2070 VAL A CG1   1 
ATOM   4916  C  CG2   . VAL A 1 2070 ? 172.847 269.050 235.428 1.00 3.10  ? 2070 VAL A CG2   1 
ATOM   4917  N  N     . PRO A 1 2071 ? 175.571 272.755 235.220 1.00 5.52  ? 2071 PRO A N     1 
ATOM   4918  C  CA    . PRO A 1 2071 ? 176.507 273.793 234.760 1.00 5.87  ? 2071 PRO A CA    1 
ATOM   4919  C  C     . PRO A 1 2071 ? 177.916 273.615 235.295 1.00 6.02  ? 2071 PRO A C     1 
ATOM   4920  O  O     . PRO A 1 2071 ? 178.877 273.979 234.607 1.00 7.32  ? 2071 PRO A O     1 
ATOM   4921  C  CB    . PRO A 1 2071 ? 175.866 275.090 235.272 1.00 5.43  ? 2071 PRO A CB    1 
ATOM   4922  C  CG    . PRO A 1 2071 ? 174.439 274.765 235.398 1.00 9.00  ? 2071 PRO A CG    1 
ATOM   4923  C  CD    . PRO A 1 2071 ? 174.414 273.362 235.903 1.00 5.26  ? 2071 PRO A CD    1 
ATOM   4924  N  N     . PHE A 1 2072 ? 178.067 273.071 236.505 1.00 5.02  ? 2072 PHE A N     1 
ATOM   4925  C  CA    . PHE A 1 2072 ? 179.400 272.870 237.065 1.00 6.14  ? 2072 PHE A CA    1 
ATOM   4926  C  C     . PHE A 1 2072 ? 180.214 271.901 236.218 1.00 8.45  ? 2072 PHE A C     1 
ATOM   4927  O  O     . PHE A 1 2072 ? 181.411 272.114 235.993 1.00 11.58 ? 2072 PHE A O     1 
ATOM   4928  C  CB    . PHE A 1 2072 ? 179.297 272.365 238.504 1.00 5.26  ? 2072 PHE A CB    1 
ATOM   4929  C  CG    . PHE A 1 2072 ? 180.604 271.909 239.077 1.00 9.58  ? 2072 PHE A CG    1 
ATOM   4930  C  CD1   . PHE A 1 2072 ? 181.523 272.827 239.554 1.00 7.77  ? 2072 PHE A CD1   1 
ATOM   4931  C  CD2   . PHE A 1 2072 ? 180.917 270.560 239.141 1.00 8.01  ? 2072 PHE A CD2   1 
ATOM   4932  C  CE1   . PHE A 1 2072 ? 182.726 272.409 240.079 1.00 6.86  ? 2072 PHE A CE1   1 
ATOM   4933  C  CE2   . PHE A 1 2072 ? 182.119 270.139 239.665 1.00 5.59  ? 2072 PHE A CE2   1 
ATOM   4934  C  CZ    . PHE A 1 2072 ? 183.024 271.063 240.136 1.00 7.07  ? 2072 PHE A CZ    1 
ATOM   4935  N  N     . PHE A 1 2073 ? 179.583 270.822 235.749 1.00 6.61  ? 2073 PHE A N     1 
ATOM   4936  C  CA    . PHE A 1 2073 ? 180.273 269.887 234.869 1.00 5.86  ? 2073 PHE A CA    1 
ATOM   4937  C  C     . PHE A 1 2073 ? 180.638 270.552 233.548 1.00 8.65  ? 2073 PHE A C     1 
ATOM   4938  O  O     . PHE A 1 2073 ? 181.699 270.281 232.979 1.00 14.94 ? 2073 PHE A O     1 
ATOM   4939  C  CB    . PHE A 1 2073 ? 179.402 268.654 234.632 1.00 5.31  ? 2073 PHE A CB    1 
ATOM   4940  C  CG    . PHE A 1 2073 ? 179.684 267.524 235.574 1.00 3.55  ? 2073 PHE A CG    1 
ATOM   4941  C  CD1   . PHE A 1 2073 ? 179.313 267.607 236.904 1.00 3.19  ? 2073 PHE A CD1   1 
ATOM   4942  C  CD2   . PHE A 1 2073 ? 180.312 266.376 235.128 1.00 3.49  ? 2073 PHE A CD2   1 
ATOM   4943  C  CE1   . PHE A 1 2073 ? 179.572 266.569 237.774 1.00 3.72  ? 2073 PHE A CE1   1 
ATOM   4944  C  CE2   . PHE A 1 2073 ? 180.571 265.334 235.993 1.00 3.05  ? 2073 PHE A CE2   1 
ATOM   4945  C  CZ    . PHE A 1 2073 ? 180.201 265.431 237.318 1.00 3.57  ? 2073 PHE A CZ    1 
ATOM   4946  N  N     . LYS A 1 2074 ? 179.757 271.420 233.045 1.00 9.57  ? 2074 LYS A N     1 
ATOM   4947  C  CA    . LYS A 1 2074 ? 180.060 272.173 231.833 1.00 9.23  ? 2074 LYS A CA    1 
ATOM   4948  C  C     . LYS A 1 2074 ? 181.257 273.091 232.054 1.00 8.60  ? 2074 LYS A C     1 
ATOM   4949  O  O     . LYS A 1 2074 ? 182.140 273.191 231.196 1.00 9.62  ? 2074 LYS A O     1 
ATOM   4950  C  CB    . LYS A 1 2074 ? 178.821 272.968 231.408 1.00 11.02 ? 2074 LYS A CB    1 
ATOM   4951  C  CG    . LYS A 1 2074 ? 179.015 274.002 230.302 1.00 13.27 ? 2074 LYS A CG    1 
ATOM   4952  C  CD    . LYS A 1 2074 ? 179.806 273.457 229.122 1.00 16.45 ? 2074 LYS A CD    1 
ATOM   4953  C  CE    . LYS A 1 2074 ? 179.462 274.201 227.842 1.00 21.16 ? 2074 LYS A CE    1 
ATOM   4954  N  NZ    . LYS A 1 2074 ? 179.602 275.675 227.995 1.00 23.18 ? 2074 LYS A NZ    1 
ATOM   4955  N  N     . LEU A 1 2075 ? 181.310 273.757 233.211 1.00 8.23  ? 2075 LEU A N     1 
ATOM   4956  C  CA    . LEU A 1 2075 ? 182.436 274.636 233.514 1.00 7.77  ? 2075 LEU A CA    1 
ATOM   4957  C  C     . LEU A 1 2075 ? 183.740 273.856 233.628 1.00 11.58 ? 2075 LEU A C     1 
ATOM   4958  O  O     . LEU A 1 2075 ? 184.789 274.327 233.177 1.00 20.27 ? 2075 LEU A O     1 
ATOM   4959  C  CB    . LEU A 1 2075 ? 182.165 275.413 234.802 1.00 10.92 ? 2075 LEU A CB    1 
ATOM   4960  C  CG    . LEU A 1 2075 ? 181.253 276.635 234.705 1.00 14.09 ? 2075 LEU A CG    1 
ATOM   4961  C  CD1   . LEU A 1 2075 ? 180.507 276.845 236.013 1.00 11.03 ? 2075 LEU A CD1   1 
ATOM   4962  C  CD2   . LEU A 1 2075 ? 182.051 277.875 234.334 1.00 19.61 ? 2075 LEU A CD2   1 
ATOM   4963  N  N     . CYS A 1 2076 ? 183.698 272.665 234.231 1.00 10.88 ? 2076 CYS A N     1 
ATOM   4964  C  CA    . CYS A 1 2076 ? 184.915 271.871 234.381 1.00 10.70 ? 2076 CYS A CA    1 
ATOM   4965  C  C     . CYS A 1 2076 ? 185.491 271.478 233.028 1.00 7.53  ? 2076 CYS A C     1 
ATOM   4966  O  O     . CYS A 1 2076 ? 186.712 271.478 232.840 1.00 8.20  ? 2076 CYS A O     1 
ATOM   4967  C  CB    . CYS A 1 2076 ? 184.634 270.628 235.224 1.00 5.44  ? 2076 CYS A CB    1 
ATOM   4968  S  SG    . CYS A 1 2076 ? 184.482 270.958 236.989 1.00 14.32 ? 2076 CYS A SG    1 
ATOM   4969  N  N     . ASP A 1 2077 ? 184.625 271.146 232.069 1.00 10.07 ? 2077 ASP A N     1 
ATOM   4970  C  CA    . ASP A 1 2077 ? 185.084 270.771 230.739 1.00 6.99  ? 2077 ASP A CA    1 
ATOM   4971  C  C     . ASP A 1 2077 ? 185.786 271.913 230.018 1.00 8.24  ? 2077 ASP A C     1 
ATOM   4972  O  O     . ASP A 1 2077 ? 186.542 271.661 229.074 1.00 15.61 ? 2077 ASP A O     1 
ATOM   4973  C  CB    . ASP A 1 2077 ? 183.905 270.280 229.902 1.00 8.21  ? 2077 ASP A CB    1 
ATOM   4974  C  CG    . ASP A 1 2077 ? 184.341 269.473 228.701 1.00 15.30 ? 2077 ASP A CG    1 
ATOM   4975  O  OD1   . ASP A 1 2077 ? 185.361 268.761 228.801 1.00 21.89 ? 2077 ASP A OD1   1 
ATOM   4976  O  OD2   . ASP A 1 2077 ? 183.665 269.555 227.655 1.00 26.87 ? 2077 ASP A OD2   1 
ATOM   4977  N  N     . GLU A 1 2078 ? 185.564 273.155 230.438 1.00 12.88 ? 2078 GLU A N     1 
ATOM   4978  C  CA    . GLU A 1 2078 ? 186.152 274.317 229.783 1.00 11.52 ? 2078 GLU A CA    1 
ATOM   4979  C  C     . GLU A 1 2078 ? 187.137 275.076 230.656 1.00 12.03 ? 2078 GLU A C     1 
ATOM   4980  O  O     . GLU A 1 2078 ? 188.176 275.511 230.159 1.00 20.90 ? 2078 GLU A O     1 
ATOM   4981  C  CB    . GLU A 1 2078 ? 185.047 275.270 229.321 1.00 13.80 ? 2078 GLU A CB    1 
ATOM   4982  C  CG    . GLU A 1 2078 ? 184.454 274.905 227.976 1.00 17.10 ? 2078 GLU A CG    1 
ATOM   4983  C  CD    . GLU A 1 2078 ? 182.979 275.227 227.882 1.00 24.30 ? 2078 GLU A CD    1 
ATOM   4984  O  OE1   . GLU A 1 2078 ? 182.419 275.738 228.873 1.00 23.66 ? 2078 GLU A OE1   1 
ATOM   4985  O  OE2   . GLU A 1 2078 ? 182.381 274.969 226.818 1.00 21.72 ? 2078 GLU A OE2   1 
ATOM   4986  N  N     . GLN A 1 2079 ? 186.840 275.245 231.945 1.00 10.28 ? 2079 GLN A N     1 
ATOM   4987  C  CA    . GLN A 1 2079 ? 187.730 276.014 232.808 1.00 12.77 ? 2079 GLN A CA    1 
ATOM   4988  C  C     . GLN A 1 2079 ? 189.003 275.235 233.126 1.00 18.17 ? 2079 GLN A C     1 
ATOM   4989  O  O     . GLN A 1 2079 ? 190.088 275.822 233.214 1.00 28.19 ? 2079 GLN A O     1 
ATOM   4990  C  CB    . GLN A 1 2079 ? 187.001 276.405 234.093 1.00 13.59 ? 2079 GLN A CB    1 
ATOM   4991  C  CG    . GLN A 1 2079 ? 185.788 277.301 233.876 1.00 18.28 ? 2079 GLN A CG    1 
ATOM   4992  C  CD    . GLN A 1 2079 ? 186.148 278.667 233.331 1.00 19.07 ? 2079 GLN A CD    1 
ATOM   4993  O  OE1   . GLN A 1 2079 ? 187.148 279.260 233.722 1.00 22.18 ? 2079 GLN A OE1   1 
ATOM   4994  N  NE2   . GLN A 1 2079 ? 185.329 279.172 232.419 1.00 25.48 ? 2079 GLN A NE2   1 
ATOM   4995  N  N     . LEU A 1 2080 ? 188.892 273.922 233.308 1.00 15.20 ? 2080 LEU A N     1 
ATOM   4996  C  CA    . LEU A 1 2080 ? 190.047 273.095 233.620 1.00 11.40 ? 2080 LEU A CA    1 
ATOM   4997  C  C     . LEU A 1 2080 ? 190.872 272.822 232.368 1.00 12.42 ? 2080 LEU A C     1 
ATOM   4998  O  O     . LEU A 1 2080 ? 190.385 272.907 231.237 1.00 20.15 ? 2080 LEU A O     1 
ATOM   4999  C  CB    . LEU A 1 2080 ? 189.612 271.768 234.242 1.00 7.64  ? 2080 LEU A CB    1 
ATOM   5000  C  CG    . LEU A 1 2080 ? 188.770 271.814 235.514 1.00 5.16  ? 2080 LEU A CG    1 
ATOM   5001  C  CD1   . LEU A 1 2080 ? 188.383 270.406 235.937 1.00 11.77 ? 2080 LEU A CD1   1 
ATOM   5002  C  CD2   . LEU A 1 2080 ? 189.514 272.530 236.624 1.00 7.21  ? 2080 LEU A CD2   1 
ATOM   5003  N  N     . SER A 1 2081 ? 192.134 272.469 232.585 1.00 9.64  ? 2081 SER A N     1 
ATOM   5004  C  CA    . SER A 1 2081 ? 193.031 272.167 231.482 1.00 11.11 ? 2081 SER A CA    1 
ATOM   5005  C  C     . SER A 1 2081 ? 192.557 270.927 230.726 1.00 10.41 ? 2081 SER A C     1 
ATOM   5006  O  O     . SER A 1 2081 ? 191.761 270.128 231.222 1.00 11.95 ? 2081 SER A O     1 
ATOM   5007  C  CB    . SER A 1 2081 ? 194.457 271.955 231.986 1.00 13.05 ? 2081 SER A CB    1 
ATOM   5008  O  OG    . SER A 1 2081 ? 194.624 270.653 232.519 1.00 7.32  ? 2081 SER A OG    1 
ATOM   5009  N  N     . SER A 1 2082 ? 193.063 270.778 229.508 1.00 11.93 ? 2082 SER A N     1 
ATOM   5010  C  CA    . SER A 1 2082 ? 192.669 269.680 228.637 1.00 9.57  ? 2082 SER A CA    1 
ATOM   5011  C  C     . SER A 1 2082 ? 193.608 268.500 228.854 1.00 10.41 ? 2082 SER A C     1 
ATOM   5012  O  O     . SER A 1 2082 ? 194.825 268.626 228.675 1.00 8.62  ? 2082 SER A O     1 
ATOM   5013  C  CB    . SER A 1 2082 ? 192.683 270.122 227.177 1.00 13.77 ? 2082 SER A CB    1 
ATOM   5014  O  OG    . SER A 1 2082 ? 191.720 271.135 226.948 1.00 17.42 ? 2082 SER A OG    1 
ATOM   5015  N  N     . GLN A 1 2083 ? 193.043 267.361 229.248 1.00 13.08 ? 2083 GLN A N     1 
ATOM   5016  C  CA    . GLN A 1 2083 ? 193.790 266.129 229.447 1.00 4.84  ? 2083 GLN A CA    1 
ATOM   5017  C  C     . GLN A 1 2083 ? 193.050 264.981 228.777 1.00 2.56  ? 2083 GLN A C     1 
ATOM   5018  O  O     . GLN A 1 2083 ? 191.820 264.982 228.694 1.00 2.65  ? 2083 GLN A O     1 
ATOM   5019  C  CB    . GLN A 1 2083 ? 193.989 265.827 230.939 1.00 2.80  ? 2083 GLN A CB    1 
ATOM   5020  C  CG    . GLN A 1 2083 ? 194.499 267.004 231.757 1.00 2.11  ? 2083 GLN A CG    1 
ATOM   5021  C  CD    . GLN A 1 2083 ? 195.980 267.258 231.569 1.00 3.35  ? 2083 GLN A CD    1 
ATOM   5022  O  OE1   . GLN A 1 2083 ? 196.685 266.468 230.944 1.00 7.37  ? 2083 GLN A OE1   1 
ATOM   5023  N  NE2   . GLN A 1 2083 ? 196.461 268.372 232.104 1.00 3.80  ? 2083 GLN A NE2   1 
ATOM   5024  N  N     . SER A 1 2084 ? 193.812 263.997 228.294 1.00 6.58  ? 2084 SER A N     1 
ATOM   5025  C  CA    . SER A 1 2084 ? 193.200 262.849 227.635 1.00 5.44  ? 2084 SER A CA    1 
ATOM   5026  C  C     . SER A 1 2084 ? 192.396 261.983 228.597 1.00 3.58  ? 2084 SER A C     1 
ATOM   5027  O  O     . SER A 1 2084 ? 191.490 261.267 228.159 1.00 5.75  ? 2084 SER A O     1 
ATOM   5028  C  CB    . SER A 1 2084 ? 194.268 262.004 226.940 1.00 4.17  ? 2084 SER A CB    1 
ATOM   5029  O  OG    . SER A 1 2084 ? 195.393 261.799 227.775 1.00 19.36 ? 2084 SER A OG    1 
ATOM   5030  N  N     . HIS A 1 2085 ? 192.696 262.037 229.894 1.00 1.87  ? 2085 HIS A N     1 
ATOM   5031  C  CA    . HIS A 1 2085 ? 191.990 261.254 230.897 1.00 2.26  ? 2085 HIS A CA    1 
ATOM   5032  C  C     . HIS A 1 2085 ? 190.898 262.056 231.597 1.00 3.03  ? 2085 HIS A C     1 
ATOM   5033  O  O     . HIS A 1 2085 ? 190.523 261.727 232.727 1.00 7.04  ? 2085 HIS A O     1 
ATOM   5034  C  CB    . HIS A 1 2085 ? 192.977 260.697 231.922 1.00 1.31  ? 2085 HIS A CB    1 
ATOM   5035  C  CG    . HIS A 1 2085 ? 193.664 261.749 232.735 1.00 1.29  ? 2085 HIS A CG    1 
ATOM   5036  N  ND1   . HIS A 1 2085 ? 194.759 262.448 232.276 1.00 0.98  ? 2085 HIS A ND1   1 
ATOM   5037  C  CD2   . HIS A 1 2085 ? 193.415 262.216 233.980 1.00 1.52  ? 2085 HIS A CD2   1 
ATOM   5038  C  CE1   . HIS A 1 2085 ? 195.152 263.304 233.202 1.00 0.68  ? 2085 HIS A CE1   1 
ATOM   5039  N  NE2   . HIS A 1 2085 ? 194.353 263.183 234.246 1.00 0.74  ? 2085 HIS A NE2   1 
ATOM   5040  N  N     . TYR A 1 2086 ? 190.382 263.096 230.953 1.00 2.15  ? 2086 TYR A N     1 
ATOM   5041  C  CA    . TYR A 1 2086 ? 189.340 263.933 231.524 1.00 2.08  ? 2086 TYR A CA    1 
ATOM   5042  C  C     . TYR A 1 2086 ? 188.008 263.610 230.862 1.00 4.27  ? 2086 TYR A C     1 
ATOM   5043  O  O     . TYR A 1 2086 ? 187.909 263.588 229.632 1.00 7.91  ? 2086 TYR A O     1 
ATOM   5044  C  CB    . TYR A 1 2086 ? 189.666 265.416 231.345 1.00 2.54  ? 2086 TYR A CB    1 
ATOM   5045  C  CG    . TYR A 1 2086 ? 190.554 265.995 232.422 1.00 3.00  ? 2086 TYR A CG    1 
ATOM   5046  C  CD1   . TYR A 1 2086 ? 191.272 265.171 233.277 1.00 2.22  ? 2086 TYR A CD1   1 
ATOM   5047  C  CD2   . TYR A 1 2086 ? 190.685 267.369 232.572 1.00 3.25  ? 2086 TYR A CD2   1 
ATOM   5048  C  CE1   . TYR A 1 2086 ? 192.085 265.698 234.258 1.00 1.48  ? 2086 TYR A CE1   1 
ATOM   5049  C  CE2   . TYR A 1 2086 ? 191.498 267.904 233.548 1.00 2.90  ? 2086 TYR A CE2   1 
ATOM   5050  C  CZ    . TYR A 1 2086 ? 192.196 267.065 234.389 1.00 3.26  ? 2086 TYR A CZ    1 
ATOM   5051  O  OH    . TYR A 1 2086 ? 193.007 267.595 235.363 1.00 2.03  ? 2086 TYR A OH    1 
ATOM   5052  N  N     . ASP A 1 2087 ? 186.994 263.349 231.681 1.00 4.41  ? 2087 ASP A N     1 
ATOM   5053  C  CA    . ASP A 1 2087 ? 185.640 263.139 231.190 1.00 5.71  ? 2087 ASP A CA    1 
ATOM   5054  C  C     . ASP A 1 2087 ? 184.666 263.849 232.112 1.00 4.65  ? 2087 ASP A C     1 
ATOM   5055  O  O     . ASP A 1 2087 ? 184.702 263.652 233.331 1.00 6.17  ? 2087 ASP A O     1 
ATOM   5056  C  CB    . ASP A 1 2087 ? 185.287 261.651 231.110 1.00 9.48  ? 2087 ASP A CB    1 
ATOM   5057  C  CG    . ASP A 1 2087 ? 183.879 261.421 230.605 1.00 15.26 ? 2087 ASP A CG    1 
ATOM   5058  O  OD1   . ASP A 1 2087 ? 183.554 261.909 229.501 1.00 14.36 ? 2087 ASP A OD1   1 
ATOM   5059  O  OD2   . ASP A 1 2087 ? 183.087 260.775 231.325 1.00 11.62 ? 2087 ASP A OD2   1 
ATOM   5060  N  N     . PHE A 1 2088 ? 183.803 264.672 231.530 1.00 4.44  ? 2088 PHE A N     1 
ATOM   5061  C  CA    . PHE A 1 2088 ? 182.774 265.387 232.267 1.00 4.26  ? 2088 PHE A CA    1 
ATOM   5062  C  C     . PHE A 1 2088 ? 181.430 265.224 231.579 1.00 5.05  ? 2088 PHE A C     1 
ATOM   5063  O  O     . PHE A 1 2088 ? 180.589 266.126 231.584 1.00 11.90 ? 2088 PHE A O     1 
ATOM   5064  C  CB    . PHE A 1 2088 ? 183.144 266.859 232.423 1.00 6.92  ? 2088 PHE A CB    1 
ATOM   5065  C  CG    . PHE A 1 2088 ? 184.459 267.078 233.112 1.00 7.02  ? 2088 PHE A CG    1 
ATOM   5066  C  CD1   . PHE A 1 2088 ? 184.573 266.923 234.482 1.00 5.92  ? 2088 PHE A CD1   1 
ATOM   5067  C  CD2   . PHE A 1 2088 ? 185.585 267.431 232.388 1.00 6.16  ? 2088 PHE A CD2   1 
ATOM   5068  C  CE1   . PHE A 1 2088 ? 185.785 267.120 235.118 1.00 7.20  ? 2088 PHE A CE1   1 
ATOM   5069  C  CE2   . PHE A 1 2088 ? 186.797 267.628 233.018 1.00 4.03  ? 2088 PHE A CE2   1 
ATOM   5070  C  CZ    . PHE A 1 2088 ? 186.897 267.471 234.384 1.00 5.37  ? 2088 PHE A CZ    1 
ATOM   5071  N  N     . GLY A 1 2089 ? 181.213 264.058 230.980 1.00 3.10  ? 2089 GLY A N     1 
ATOM   5072  C  CA    . GLY A 1 2089 ? 179.999 263.764 230.253 1.00 3.28  ? 2089 GLY A CA    1 
ATOM   5073  C  C     . GLY A 1 2089 ? 178.914 263.189 231.136 1.00 2.43  ? 2089 GLY A C     1 
ATOM   5074  O  O     . GLY A 1 2089 ? 178.930 263.329 232.361 1.00 4.68  ? 2089 GLY A O     1 
ATOM   5075  N  N     . LEU A 1 2090 ? 177.952 262.527 230.491 1.00 2.09  ? 2090 LEU A N     1 
ATOM   5076  C  CA    . LEU A 1 2090 ? 176.783 262.032 231.213 1.00 1.49  ? 2090 LEU A CA    1 
ATOM   5077  C  C     . LEU A 1 2090 ? 177.140 260.884 232.152 1.00 1.33  ? 2090 LEU A C     1 
ATOM   5078  O  O     . LEU A 1 2090 ? 176.555 260.764 233.232 1.00 0.99  ? 2090 LEU A O     1 
ATOM   5079  C  CB    . LEU A 1 2090 ? 175.696 261.612 230.227 1.00 1.86  ? 2090 LEU A CB    1 
ATOM   5080  C  CG    . LEU A 1 2090 ? 174.339 261.286 230.853 1.00 1.72  ? 2090 LEU A CG    1 
ATOM   5081  C  CD1   . LEU A 1 2090 ? 173.879 262.418 231.756 1.00 0.95  ? 2090 LEU A CD1   1 
ATOM   5082  C  CD2   . LEU A 1 2090 ? 173.309 261.011 229.778 1.00 0.72  ? 2090 LEU A CD2   1 
ATOM   5083  N  N     . ARG A 1 2091 ? 178.088 260.026 231.759 1.00 1.30  ? 2091 ARG A N     1 
ATOM   5084  C  CA    . ARG A 1 2091 ? 178.532 258.968 232.664 1.00 0.87  ? 2091 ARG A CA    1 
ATOM   5085  C  C     . ARG A 1 2091 ? 179.126 259.551 233.938 1.00 1.18  ? 2091 ARG A C     1 
ATOM   5086  O  O     . ARG A 1 2091 ? 178.834 259.076 235.041 1.00 1.03  ? 2091 ARG A O     1 
ATOM   5087  C  CB    . ARG A 1 2091 ? 179.557 258.063 231.980 1.00 0.71  ? 2091 ARG A CB    1 
ATOM   5088  C  CG    . ARG A 1 2091 ? 179.030 257.212 230.848 1.00 1.30  ? 2091 ARG A CG    1 
ATOM   5089  C  CD    . ARG A 1 2091 ? 180.130 256.294 230.325 1.00 2.23  ? 2091 ARG A CD    1 
ATOM   5090  N  NE    . ARG A 1 2091 ? 179.854 255.783 228.988 1.00 4.96  ? 2091 ARG A NE    1 
ATOM   5091  C  CZ    . ARG A 1 2091 ? 178.849 254.978 228.676 1.00 1.30  ? 2091 ARG A CZ    1 
ATOM   5092  N  NH1   . ARG A 1 2091 ? 178.055 254.467 229.602 1.00 0.99  ? 2091 ARG A NH1   1 
ATOM   5093  N  NH2   . ARG A 1 2091 ? 178.646 254.660 227.402 1.00 0.80  ? 2091 ARG A NH2   1 
ATOM   5094  N  N     . ALA A 1 2092 ? 179.965 260.579 233.803 1.00 1.04  ? 2092 ALA A N     1 
ATOM   5095  C  CA    . ALA A 1 2092 ? 180.536 261.233 234.975 1.00 1.00  ? 2092 ALA A CA    1 
ATOM   5096  C  C     . ALA A 1 2092 ? 179.449 261.876 235.826 1.00 0.99  ? 2092 ALA A C     1 
ATOM   5097  O  O     . ALA A 1 2092 ? 179.465 261.771 237.056 1.00 1.08  ? 2092 ALA A O     1 
ATOM   5098  C  CB    . ALA A 1 2092 ? 181.572 262.268 234.539 1.00 2.69  ? 2092 ALA A CB    1 
ATOM   5099  N  N     . LEU A 1 2093 ? 178.491 262.547 235.181 1.00 1.29  ? 2093 LEU A N     1 
ATOM   5100  C  CA    . LEU A 1 2093 ? 177.373 263.134 235.912 1.00 1.06  ? 2093 LEU A CA    1 
ATOM   5101  C  C     . LEU A 1 2093 ? 176.535 262.058 236.590 1.00 0.81  ? 2093 LEU A C     1 
ATOM   5102  O  O     . LEU A 1 2093 ? 176.147 262.199 237.753 1.00 0.97  ? 2093 LEU A O     1 
ATOM   5103  C  CB    . LEU A 1 2093 ? 176.508 263.969 234.967 1.00 0.93  ? 2093 LEU A CB    1 
ATOM   5104  C  CG    . LEU A 1 2093 ? 175.265 264.601 235.598 1.00 0.61  ? 2093 LEU A CG    1 
ATOM   5105  C  CD1   . LEU A 1 2093 ? 175.651 265.599 236.683 1.00 1.07  ? 2093 LEU A CD1   1 
ATOM   5106  C  CD2   . LEU A 1 2093 ? 174.392 265.252 234.542 1.00 0.94  ? 2093 LEU A CD2   1 
ATOM   5107  N  N     . LYS A 1 2094 ? 176.253 260.968 235.871 1.00 0.91  ? 2094 LYS A N     1 
ATOM   5108  C  CA    . LYS A 1 2094 ? 175.483 259.872 236.451 1.00 0.79  ? 2094 LYS A CA    1 
ATOM   5109  C  C     . LYS A 1 2094 ? 176.204 259.264 237.646 1.00 1.04  ? 2094 LYS A C     1 
ATOM   5110  O  O     . LYS A 1 2094 ? 175.575 258.923 238.653 1.00 1.13  ? 2094 LYS A O     1 
ATOM   5111  C  CB    . LYS A 1 2094 ? 175.216 258.807 235.388 1.00 1.68  ? 2094 LYS A CB    1 
ATOM   5112  C  CG    . LYS A 1 2094 ? 174.169 257.780 235.770 1.00 1.24  ? 2094 LYS A CG    1 
ATOM   5113  C  CD    . LYS A 1 2094 ? 172.769 258.287 235.487 1.00 2.00  ? 2094 LYS A CD    1 
ATOM   5114  C  CE    . LYS A 1 2094 ? 171.732 257.207 235.740 1.00 2.26  ? 2094 LYS A CE    1 
ATOM   5115  N  NZ    . LYS A 1 2094 ? 171.911 256.040 234.841 1.00 2.64  ? 2094 LYS A NZ    1 
ATOM   5116  N  N     . SER A 1 2095 ? 177.528 259.117 237.546 1.00 1.29  ? 2095 SER A N     1 
ATOM   5117  C  CA    . SER A 1 2095 ? 178.310 258.561 238.645 1.00 0.60  ? 2095 SER A CA    1 
ATOM   5118  C  C     . SER A 1 2095 ? 178.192 259.422 239.898 1.00 1.25  ? 2095 SER A C     1 
ATOM   5119  O  O     . SER A 1 2095 ? 178.005 258.907 241.005 1.00 2.03  ? 2095 SER A O     1 
ATOM   5120  C  CB    . SER A 1 2095 ? 179.772 258.423 238.221 1.00 1.16  ? 2095 SER A CB    1 
ATOM   5121  O  OG    . SER A 1 2095 ? 180.589 258.026 239.310 1.00 15.11 ? 2095 SER A OG    1 
ATOM   5122  N  N     . VAL A 1 2096 ? 178.300 260.742 239.738 1.00 0.95  ? 2096 VAL A N     1 
ATOM   5123  C  CA    . VAL A 1 2096 ? 178.177 261.643 240.879 1.00 1.45  ? 2096 VAL A CA    1 
ATOM   5124  C  C     . VAL A 1 2096 ? 176.766 261.594 241.452 1.00 1.63  ? 2096 VAL A C     1 
ATOM   5125  O  O     . VAL A 1 2096 ? 176.578 261.561 242.674 1.00 2.83  ? 2096 VAL A O     1 
ATOM   5126  C  CB    . VAL A 1 2096 ? 178.579 263.075 240.473 1.00 2.90  ? 2096 VAL A CB    1 
ATOM   5127  C  CG1   . VAL A 1 2096 ? 178.265 264.055 241.586 1.00 1.97  ? 2096 VAL A CG1   1 
ATOM   5128  C  CG2   . VAL A 1 2096 ? 180.056 263.126 240.117 1.00 3.70  ? 2096 VAL A CG2   1 
ATOM   5129  N  N     . LEU A 1 2097 ? 175.753 261.589 240.580 1.00 1.52  ? 2097 LEU A N     1 
ATOM   5130  C  CA    . LEU A 1 2097 ? 174.369 261.572 241.047 1.00 1.44  ? 2097 LEU A CA    1 
ATOM   5131  C  C     . LEU A 1 2097 ? 174.053 260.295 241.815 1.00 4.36  ? 2097 LEU A C     1 
ATOM   5132  O  O     . LEU A 1 2097 ? 173.394 260.340 242.861 1.00 5.99  ? 2097 LEU A O     1 
ATOM   5133  C  CB    . LEU A 1 2097 ? 173.417 261.729 239.861 1.00 1.58  ? 2097 LEU A CB    1 
ATOM   5134  C  CG    . LEU A 1 2097 ? 173.427 263.075 239.134 1.00 1.04  ? 2097 LEU A CG    1 
ATOM   5135  C  CD1   . LEU A 1 2097 ? 172.575 263.001 237.878 1.00 0.93  ? 2097 LEU A CD1   1 
ATOM   5136  C  CD2   . LEU A 1 2097 ? 172.954 264.190 240.048 1.00 1.00  ? 2097 LEU A CD2   1 
ATOM   5137  N  N     . VAL A 1 2098 ? 174.498 259.145 241.307 1.00 2.74  ? 2098 VAL A N     1 
ATOM   5138  C  CA    . VAL A 1 2098 ? 174.288 257.889 242.016 1.00 2.59  ? 2098 VAL A CA    1 
ATOM   5139  C  C     . VAL A 1 2098 ? 175.059 257.885 243.330 1.00 3.41  ? 2098 VAL A C     1 
ATOM   5140  O  O     . VAL A 1 2098 ? 174.539 257.465 244.370 1.00 2.84  ? 2098 VAL A O     1 
ATOM   5141  C  CB    . VAL A 1 2098 ? 174.674 256.698 241.118 1.00 3.33  ? 2098 VAL A CB    1 
ATOM   5142  C  CG1   . VAL A 1 2098 ? 174.761 255.414 241.929 1.00 0.96  ? 2098 VAL A CG1   1 
ATOM   5143  C  CG2   . VAL A 1 2098 ? 173.671 256.547 239.987 1.00 5.01  ? 2098 VAL A CG2   1 
ATOM   5144  N  N     . SER A 1 2099 ? 176.308 258.359 243.302 1.00 3.62  ? 2099 SER A N     1 
ATOM   5145  C  CA    . SER A 1 2099 ? 177.095 258.452 244.527 1.00 2.22  ? 2099 SER A CA    1 
ATOM   5146  C  C     . SER A 1 2099 ? 176.473 259.422 245.521 1.00 2.37  ? 2099 SER A C     1 
ATOM   5147  O  O     . SER A 1 2099 ? 176.605 259.233 246.735 1.00 5.26  ? 2099 SER A O     1 
ATOM   5148  C  CB    . SER A 1 2099 ? 178.528 258.874 244.190 1.00 3.76  ? 2099 SER A CB    1 
ATOM   5149  O  OG    . SER A 1 2099 ? 179.366 258.803 245.328 1.00 13.31 ? 2099 SER A OG    1 
ATOM   5150  N  N     . ALA A 1 2100 ? 175.791 260.460 245.032 1.00 3.50  ? 2100 ALA A N     1 
ATOM   5151  C  CA    . ALA A 1 2100 ? 175.139 261.408 245.929 1.00 5.12  ? 2100 ALA A CA    1 
ATOM   5152  C  C     . ALA A 1 2100 ? 174.076 260.724 246.778 1.00 6.50  ? 2100 ALA A C     1 
ATOM   5153  O  O     . ALA A 1 2100 ? 173.963 260.991 247.979 1.00 7.64  ? 2100 ALA A O     1 
ATOM   5154  C  CB    . ALA A 1 2100 ? 174.531 262.558 245.129 1.00 5.02  ? 2100 ALA A CB    1 
ATOM   5155  N  N     . GLY A 1 2101 ? 173.284 259.840 246.171 1.00 5.27  ? 2101 GLY A N     1 
ATOM   5156  C  CA    . GLY A 1 2101 ? 172.294 259.101 246.936 1.00 3.95  ? 2101 GLY A CA    1 
ATOM   5157  C  C     . GLY A 1 2101 ? 172.924 258.171 247.956 1.00 5.71  ? 2101 GLY A C     1 
ATOM   5158  O  O     . GLY A 1 2101 ? 172.418 258.022 249.071 1.00 7.10  ? 2101 GLY A O     1 
ATOM   5159  N  N     . ASN A 1 2102 ? 174.031 257.526 247.584 1.00 6.60  ? 2102 ASN A N     1 
ATOM   5160  C  CA    . ASN A 1 2102 ? 174.732 256.659 248.522 1.00 4.73  ? 2102 ASN A CA    1 
ATOM   5161  C  C     . ASN A 1 2102 ? 175.311 257.455 249.686 1.00 6.22  ? 2102 ASN A C     1 
ATOM   5162  O  O     . ASN A 1 2102 ? 175.242 257.019 250.840 1.00 11.52 ? 2102 ASN A O     1 
ATOM   5163  C  CB    . ASN A 1 2102 ? 175.828 255.880 247.798 1.00 7.16  ? 2102 ASN A CB    1 
ATOM   5164  C  CG    . ASN A 1 2102 ? 175.278 254.750 246.955 1.00 10.57 ? 2102 ASN A CG    1 
ATOM   5165  O  OD1   . ASN A 1 2102 ? 174.447 253.969 247.413 1.00 20.08 ? 2102 ASN A OD1   1 
ATOM   5166  N  ND2   . ASN A 1 2102 ? 175.742 254.654 245.715 1.00 6.35  ? 2102 ASN A ND2   1 
ATOM   5167  N  N     . VAL A 1 2103 ? 175.885 258.627 249.402 1.00 5.62  ? 2103 VAL A N     1 
ATOM   5168  C  CA    . VAL A 1 2103 ? 176.444 259.457 250.466 1.00 6.51  ? 2103 VAL A CA    1 
ATOM   5169  C  C     . VAL A 1 2103 ? 175.338 259.986 251.370 1.00 8.78  ? 2103 VAL A C     1 
ATOM   5170  O  O     . VAL A 1 2103 ? 175.514 260.105 252.589 1.00 10.36 ? 2103 VAL A O     1 
ATOM   5171  C  CB    . VAL A 1 2103 ? 177.289 260.598 249.867 1.00 7.40  ? 2103 VAL A CB    1 
ATOM   5172  C  CG1   . VAL A 1 2103 ? 177.700 261.584 250.946 1.00 5.14  ? 2103 VAL A CG1   1 
ATOM   5173  C  CG2   . VAL A 1 2103 ? 178.519 260.042 249.171 1.00 9.10  ? 2103 VAL A CG2   1 
ATOM   5174  N  N     . LYS A 1 2104 ? 174.183 260.322 250.794 1.00 8.22  ? 2104 LYS A N     1 
ATOM   5175  C  CA    . LYS A 1 2104 ? 173.078 260.803 251.616 1.00 8.04  ? 2104 LYS A CA    1 
ATOM   5176  C  C     . LYS A 1 2104 ? 172.580 259.717 252.563 1.00 7.42  ? 2104 LYS A C     1 
ATOM   5177  O  O     . LYS A 1 2104 ? 172.255 259.998 253.721 1.00 8.16  ? 2104 LYS A O     1 
ATOM   5178  C  CB    . LYS A 1 2104 ? 171.939 261.312 250.733 1.00 10.76 ? 2104 LYS A CB    1 
ATOM   5179  C  CG    . LYS A 1 2104 ? 170.879 262.081 251.503 1.00 7.28  ? 2104 LYS A CG    1 
ATOM   5180  C  CD    . LYS A 1 2104 ? 169.928 262.814 250.579 1.00 9.35  ? 2104 LYS A CD    1 
ATOM   5181  C  CE    . LYS A 1 2104 ? 168.877 261.880 250.008 1.00 11.58 ? 2104 LYS A CE    1 
ATOM   5182  N  NZ    . LYS A 1 2104 ? 167.785 261.613 250.983 1.00 8.13  ? 2104 LYS A NZ    1 
ATOM   5183  N  N     . ARG A 1 2105 ? 172.515 258.472 252.088 1.00 11.36 ? 2105 ARG A N     1 
ATOM   5184  C  CA    . ARG A 1 2105 ? 172.038 257.382 252.934 1.00 7.24  ? 2105 ARG A CA    1 
ATOM   5185  C  C     . ARG A 1 2105 ? 172.993 257.111 254.092 1.00 12.17 ? 2105 ARG A C     1 
ATOM   5186  O  O     . ARG A 1 2105 ? 172.549 256.852 255.215 1.00 19.50 ? 2105 ARG A O     1 
ATOM   5187  C  CB    . ARG A 1 2105 ? 171.833 256.117 252.098 1.00 7.44  ? 2105 ARG A CB    1 
ATOM   5188  C  CG    . ARG A 1 2105 ? 170.535 256.101 251.302 1.00 7.54  ? 2105 ARG A CG    1 
ATOM   5189  C  CD    . ARG A 1 2105 ? 170.293 254.741 250.668 1.00 7.28  ? 2105 ARG A CD    1 
ATOM   5190  N  NE    . ARG A 1 2105 ? 171.135 254.525 249.497 1.00 12.29 ? 2105 ARG A NE    1 
ATOM   5191  C  CZ    . ARG A 1 2105 ? 170.941 255.095 248.316 1.00 10.33 ? 2105 ARG A CZ    1 
ATOM   5192  N  NH1   . ARG A 1 2105 ? 169.917 255.901 248.096 1.00 13.33 ? 2105 ARG A NH1   1 
ATOM   5193  N  NH2   . ARG A 1 2105 ? 171.797 254.848 247.327 1.00 10.63 ? 2105 ARG A NH2   1 
ATOM   5194  N  N     . GLU A 1 2106 ? 174.304 257.164 253.842 1.00 11.75 ? 2106 GLU A N     1 
ATOM   5195  C  CA    . GLU A 1 2106 ? 175.261 256.871 254.905 1.00 15.98 ? 2106 GLU A CA    1 
ATOM   5196  C  C     . GLU A 1 2106 ? 175.265 257.966 255.968 1.00 18.30 ? 2106 GLU A C     1 
ATOM   5197  O  O     . GLU A 1 2106 ? 175.426 257.680 257.160 1.00 25.56 ? 2106 GLU A O     1 
ATOM   5198  C  CB    . GLU A 1 2106 ? 176.662 256.663 254.324 1.00 9.17  ? 2106 GLU A CB    1 
ATOM   5199  C  CG    . GLU A 1 2106 ? 177.275 257.890 253.683 1.00 20.32 ? 2106 GLU A CG    1 
ATOM   5200  C  CD    . GLU A 1 2106 ? 178.631 257.623 253.063 1.00 24.14 ? 2106 GLU A CD    1 
ATOM   5201  O  OE1   . GLU A 1 2106 ? 179.093 256.464 253.110 1.00 19.37 ? 2106 GLU A OE1   1 
ATOM   5202  O  OE2   . GLU A 1 2106 ? 179.233 258.576 252.527 1.00 26.25 ? 2106 GLU A OE2   1 
ATOM   5203  N  N     . ARG A 1 2107 ? 175.093 259.227 255.560 1.00 11.15 ? 2107 ARG A N     1 
ATOM   5204  C  CA    . ARG A 1 2107 ? 175.008 260.307 256.541 1.00 12.30 ? 2107 ARG A CA    1 
ATOM   5205  C  C     . ARG A 1 2107 ? 173.775 260.166 257.420 1.00 17.32 ? 2107 ARG A C     1 
ATOM   5206  O  O     . ARG A 1 2107 ? 173.847 260.376 258.637 1.00 24.87 ? 2107 ARG A O     1 
ATOM   5207  C  CB    . ARG A 1 2107 ? 175.009 261.666 255.849 1.00 12.89 ? 2107 ARG A CB    1 
ATOM   5208  C  CG    . ARG A 1 2107 ? 176.301 262.034 255.162 1.00 13.49 ? 2107 ARG A CG    1 
ATOM   5209  C  CD    . ARG A 1 2107 ? 176.160 263.412 254.560 1.00 19.09 ? 2107 ARG A CD    1 
ATOM   5210  N  NE    . ARG A 1 2107 ? 177.332 263.827 253.800 1.00 26.59 ? 2107 ARG A NE    1 
ATOM   5211  C  CZ    . ARG A 1 2107 ? 178.370 264.462 254.323 1.00 18.53 ? 2107 ARG A CZ    1 
ATOM   5212  N  NH1   . ARG A 1 2107 ? 178.411 264.777 255.607 1.00 21.26 ? 2107 ARG A NH1   1 
ATOM   5213  N  NH2   . ARG A 1 2107 ? 179.388 264.801 253.536 1.00 21.63 ? 2107 ARG A NH2   1 
ATOM   5214  N  N     . ILE A 1 2108 ? 172.631 259.823 256.827 1.00 16.89 ? 2108 ILE A N     1 
ATOM   5215  C  CA    . ILE A 1 2108 ? 171.422 259.624 257.621 1.00 17.81 ? 2108 ILE A CA    1 
ATOM   5216  C  C     . ILE A 1 2108 ? 171.627 258.482 258.607 1.00 22.63 ? 2108 ILE A C     1 
ATOM   5217  O  O     . ILE A 1 2108 ? 171.242 258.578 259.779 1.00 27.37 ? 2108 ILE A O     1 
ATOM   5218  C  CB    . ILE A 1 2108 ? 170.209 259.378 256.704 1.00 16.22 ? 2108 ILE A CB    1 
ATOM   5219  C  CG1   . ILE A 1 2108 ? 169.933 260.616 255.852 1.00 15.13 ? 2108 ILE A CG1   1 
ATOM   5220  C  CG2   . ILE A 1 2108 ? 168.981 259.014 257.523 1.00 14.40 ? 2108 ILE A CG2   1 
ATOM   5221  C  CD1   . ILE A 1 2108 ? 168.737 260.478 254.938 1.00 10.67 ? 2108 ILE A CD1   1 
ATOM   5222  N  N     . GLN A 1 2109 ? 172.249 257.392 258.154 1.00 22.48 ? 2109 GLN A N     1 
ATOM   5223  C  CA    . GLN A 1 2109 ? 172.588 256.303 259.062 1.00 23.03 ? 2109 GLN A CA    1 
ATOM   5224  C  C     . GLN A 1 2109 ? 173.601 256.744 260.109 1.00 27.26 ? 2109 GLN A C     1 
ATOM   5225  O  O     . GLN A 1 2109 ? 173.547 256.287 261.256 1.00 28.54 ? 2109 GLN A O     1 
ATOM   5226  C  CB    . GLN A 1 2109 ? 173.128 255.110 258.275 1.00 20.57 ? 2109 GLN A CB    1 
ATOM   5227  C  CG    . GLN A 1 2109 ? 172.070 254.372 257.477 1.00 23.10 ? 2109 GLN A CG    1 
ATOM   5228  C  CD    . GLN A 1 2109 ? 170.972 253.813 258.354 1.00 33.36 ? 2109 GLN A CD    1 
ATOM   5229  O  OE1   . GLN A 1 2109 ? 169.834 254.280 258.315 1.00 36.67 ? 2109 GLN A OE1   1 
ATOM   5230  N  NE2   . GLN A 1 2109 ? 171.306 252.805 259.150 1.00 29.37 ? 2109 GLN A NE2   1 
ATOM   5231  N  N     . LYS A 1 2110 ? 174.535 257.621 259.735 1.00 21.09 ? 2110 LYS A N     1 
ATOM   5232  C  CA    . LYS A 1 2110 ? 175.521 258.111 260.694 1.00 21.20 ? 2110 LYS A CA    1 
ATOM   5233  C  C     . LYS A 1 2110 ? 174.888 259.062 261.704 1.00 22.79 ? 2110 LYS A C     1 
ATOM   5234  O  O     . LYS A 1 2110 ? 175.237 259.033 262.890 1.00 26.93 ? 2110 LYS A O     1 
ATOM   5235  C  CB    . LYS A 1 2110 ? 176.672 258.795 259.958 1.00 20.08 ? 2110 LYS A CB    1 
ATOM   5236  C  CG    . LYS A 1 2110 ? 177.712 259.419 260.867 1.00 22.38 ? 2110 LYS A CG    1 
ATOM   5237  C  CD    . LYS A 1 2110 ? 178.424 260.571 260.179 1.00 28.08 ? 2110 LYS A CD    1 
ATOM   5238  C  CE    . LYS A 1 2110 ? 179.833 260.751 260.721 1.00 25.18 ? 2110 LYS A CE    1 
ATOM   5239  N  NZ    . LYS A 1 2110 ? 179.826 261.206 262.138 1.00 29.23 ? 2110 LYS A NZ    1 
ATOM   5240  N  N     . ILE A 1 2111 ? 173.965 259.914 261.256 1.00 24.44 ? 2111 ILE A N     1 
ATOM   5241  C  CA    . ILE A 1 2111 ? 173.335 260.877 262.159 1.00 22.73 ? 2111 ILE A CA    1 
ATOM   5242  C  C     . ILE A 1 2111 ? 172.543 260.154 263.240 1.00 26.33 ? 2111 ILE A C     1 
ATOM   5243  O  O     . ILE A 1 2111 ? 172.643 260.477 264.430 1.00 31.89 ? 2111 ILE A O     1 
ATOM   5244  C  CB    . ILE A 1 2111 ? 172.444 261.853 261.369 1.00 17.58 ? 2111 ILE A CB    1 
ATOM   5245  C  CG1   . ILE A 1 2111 ? 173.297 262.809 260.538 1.00 18.51 ? 2111 ILE A CG1   1 
ATOM   5246  C  CG2   . ILE A 1 2111 ? 171.538 262.631 262.309 1.00 16.08 ? 2111 ILE A CG2   1 
ATOM   5247  C  CD1   . ILE A 1 2111 ? 172.490 263.722 259.647 1.00 15.26 ? 2111 ILE A CD1   1 
ATOM   5248  N  N     . LYS A 1 2112 ? 171.750 259.157 262.845 1.00 26.96 ? 2112 LYS A N     1 
ATOM   5249  C  CA    . LYS A 1 2112 ? 170.973 258.411 263.827 1.00 25.62 ? 2112 LYS A CA    1 
ATOM   5250  C  C     . LYS A 1 2112 ? 171.858 257.505 264.674 1.00 30.51 ? 2112 LYS A C     1 
ATOM   5251  O  O     . LYS A 1 2112 ? 171.529 257.233 265.832 1.00 31.27 ? 2112 LYS A O     1 
ATOM   5252  C  CB    . LYS A 1 2112 ? 169.874 257.602 263.135 1.00 26.28 ? 2112 LYS A CB    1 
ATOM   5253  C  CG    . LYS A 1 2112 ? 170.364 256.610 262.103 1.00 26.94 ? 2112 LYS A CG    1 
ATOM   5254  C  CD    . LYS A 1 2112 ? 169.194 255.962 261.382 1.00 34.18 ? 2112 LYS A CD    1 
ATOM   5255  C  CE    . LYS A 1 2112 ? 168.316 257.008 260.709 1.00 33.16 ? 2112 LYS A CE    1 
ATOM   5256  N  NZ    . LYS A 1 2112 ? 167.203 256.387 259.939 1.00 29.39 ? 2112 LYS A NZ    1 
ATOM   5257  N  N     . ARG A 1 2113 ? 172.982 257.035 264.123 1.00 31.95 ? 2113 ARG A N     1 
ATOM   5258  C  CA    . ARG A 1 2113 ? 173.931 256.271 264.929 1.00 24.50 ? 2113 ARG A CA    1 
ATOM   5259  C  C     . ARG A 1 2113 ? 174.486 257.123 266.063 1.00 30.48 ? 2113 ARG A C     1 
ATOM   5260  O  O     . ARG A 1 2113 ? 174.672 256.632 267.185 1.00 36.67 ? 2113 ARG A O     1 
ATOM   5261  C  CB    . ARG A 1 2113 ? 175.062 255.733 264.057 1.00 25.63 ? 2113 ARG A CB    1 
ATOM   5262  C  CG    . ARG A 1 2113 ? 174.847 254.310 263.570 1.00 27.63 ? 2113 ARG A CG    1 
ATOM   5263  C  CD    . ARG A 1 2113 ? 175.929 253.893 262.585 1.00 23.86 ? 2113 ARG A CD    1 
ATOM   5264  N  NE    . ARG A 1 2113 ? 175.821 254.605 261.318 1.00 29.43 ? 2113 ARG A NE    1 
ATOM   5265  C  CZ    . ARG A 1 2113 ? 176.643 254.436 260.292 1.00 32.04 ? 2113 ARG A CZ    1 
ATOM   5266  N  NH1   . ARG A 1 2113 ? 177.654 253.584 260.349 1.00 28.59 ? 2113 ARG A NH1   1 
ATOM   5267  N  NH2   . ARG A 1 2113 ? 176.448 255.139 259.179 1.00 27.16 ? 2113 ARG A NH2   1 
ATOM   5268  N  N     . GLU A 1 2114 ? 174.765 258.399 265.790 1.00 27.41 ? 2114 GLU A N     1 
ATOM   5269  C  CA    . GLU A 1 2114 ? 175.112 259.323 266.864 1.00 30.91 ? 2114 GLU A CA    1 
ATOM   5270  C  C     . GLU A 1 2114 ? 173.944 259.526 267.815 1.00 32.05 ? 2114 GLU A C     1 
ATOM   5271  O  O     . GLU A 1 2114 ? 174.148 259.749 269.015 1.00 34.94 ? 2114 GLU A O     1 
ATOM   5272  C  CB    . GLU A 1 2114 ? 175.562 260.665 266.286 1.00 29.20 ? 2114 GLU A CB    1 
ATOM   5273  C  CG    . GLU A 1 2114 ? 176.697 260.571 265.284 1.00 28.95 ? 2114 GLU A CG    1 
ATOM   5274  C  CD    . GLU A 1 2114 ? 177.760 259.573 265.696 1.00 36.16 ? 2114 GLU A CD    1 
ATOM   5275  O  OE1   . GLU A 1 2114 ? 178.371 259.763 266.770 1.00 35.67 ? 2114 GLU A OE1   1 
ATOM   5276  O  OE2   . GLU A 1 2114 ? 177.983 258.598 264.949 1.00 32.65 ? 2114 GLU A OE2   1 
ATOM   5277  N  N     . LYS A 1 2115 ? 172.714 259.457 267.303 1.00 29.75 ? 2115 LYS A N     1 
ATOM   5278  C  CA    . LYS A 1 2115 ? 171.546 259.664 268.152 1.00 29.63 ? 2115 LYS A CA    1 
ATOM   5279  C  C     . LYS A 1 2115 ? 171.320 258.484 269.090 1.00 31.36 ? 2115 LYS A C     1 
ATOM   5280  O  O     . LYS A 1 2115 ? 170.802 258.661 270.198 1.00 35.74 ? 2115 LYS A O     1 
ATOM   5281  C  CB    . LYS A 1 2115 ? 170.309 259.914 267.291 1.00 27.31 ? 2115 LYS A CB    1 
ATOM   5282  C  CG    . LYS A 1 2115 ? 170.225 261.324 266.725 1.00 29.44 ? 2115 LYS A CG    1 
ATOM   5283  C  CD    . LYS A 1 2115 ? 168.819 261.636 266.241 1.00 32.62 ? 2115 LYS A CD    1 
ATOM   5284  C  CE    . LYS A 1 2115 ? 168.653 263.112 265.934 1.00 25.41 ? 2115 LYS A CE    1 
ATOM   5285  N  NZ    . LYS A 1 2115 ? 169.451 263.533 264.752 1.00 27.16 ? 2115 LYS A NZ    1 
ATOM   5286  N  N     . GLU A 1 2116 ? 171.694 257.273 268.667 1.00 30.58 ? 2116 GLU A N     1 
ATOM   5287  C  CA    . GLU A 1 2116 ? 171.532 256.109 269.535 1.00 33.35 ? 2116 GLU A CA    1 
ATOM   5288  C  C     . GLU A 1 2116 ? 172.352 256.256 270.810 1.00 34.61 ? 2116 GLU A C     1 
ATOM   5289  O  O     . GLU A 1 2116 ? 171.884 255.911 271.902 1.00 32.25 ? 2116 GLU A O     1 
ATOM   5290  C  CB    . GLU A 1 2116 ? 171.921 254.829 268.794 1.00 30.92 ? 2116 GLU A CB    1 
ATOM   5291  C  CG    . GLU A 1 2116 ? 171.166 254.590 267.500 1.00 33.61 ? 2116 GLU A CG    1 
ATOM   5292  C  CD    . GLU A 1 2116 ? 169.689 254.914 267.613 1.00 38.58 ? 2116 GLU A CD    1 
ATOM   5293  O  OE1   . GLU A 1 2116 ? 169.010 254.309 268.469 1.00 36.56 ? 2116 GLU A OE1   1 
ATOM   5294  O  OE2   . GLU A 1 2116 ? 169.209 255.771 266.842 1.00 36.31 ? 2116 GLU A OE2   1 
ATOM   5295  N  N     . GLU A 1 2117 ? 173.574 256.766 270.694 1.00 32.59 ? 2117 GLU A N     1 
ATOM   5296  C  CA    . GLU A 1 2117 ? 174.436 256.996 271.846 1.00 35.78 ? 2117 GLU A CA    1 
ATOM   5297  C  C     . GLU A 1 2117 ? 174.263 258.383 272.454 1.00 33.63 ? 2117 GLU A C     1 
ATOM   5298  O  O     . GLU A 1 2117 ? 174.913 258.687 273.458 1.00 37.81 ? 2117 GLU A O     1 
ATOM   5299  C  CB    . GLU A 1 2117 ? 175.900 256.751 271.456 1.00 33.84 ? 2117 GLU A CB    1 
ATOM   5300  C  CG    . GLU A 1 2117 ? 176.438 257.638 270.337 1.00 38.80 ? 2117 GLU A CG    1 
ATOM   5301  C  CD    . GLU A 1 2117 ? 176.988 258.961 270.829 1.00 41.34 ? 2117 GLU A CD    1 
ATOM   5302  O  OE1   . GLU A 1 2117 ? 177.306 259.067 272.031 1.00 41.46 ? 2117 GLU A OE1   1 
ATOM   5303  O  OE2   . GLU A 1 2117 ? 177.112 259.893 270.006 1.00 40.60 ? 2117 GLU A OE2   1 
ATOM   5304  N  N     . ARG A 1 2118 ? 173.401 259.225 271.879 1.00 33.84 ? 2118 ARG A N     1 
ATOM   5305  C  CA    . ARG A 1 2118 ? 173.047 260.528 272.448 1.00 34.76 ? 2118 ARG A CA    1 
ATOM   5306  C  C     . ARG A 1 2118 ? 171.524 260.638 272.465 1.00 34.74 ? 2118 ARG A C     1 
ATOM   5307  O  O     . ARG A 1 2118 ? 170.921 261.165 271.525 1.00 40.30 ? 2118 ARG A O     1 
ATOM   5308  C  CB    . ARG A 1 2118 ? 173.680 261.676 271.660 1.00 31.25 ? 2118 ARG A CB    1 
ATOM   5309  C  CG    . ARG A 1 2118 ? 175.192 261.744 271.743 1.00 32.04 ? 2118 ARG A CG    1 
ATOM   5310  C  CD    . ARG A 1 2118 ? 175.666 261.815 273.186 1.00 36.32 ? 2118 ARG A CD    1 
ATOM   5311  N  NE    . ARG A 1 2118 ? 174.998 262.876 273.928 1.00 37.68 ? 2118 ARG A NE    1 
ATOM   5312  C  CZ    . ARG A 1 2118 ? 174.274 262.686 275.024 1.00 38.37 ? 2118 ARG A CZ    1 
ATOM   5313  N  NH1   . ARG A 1 2118 ? 174.103 261.478 275.536 1.00 37.83 ? 2118 ARG A NH1   1 
ATOM   5314  N  NH2   . ARG A 1 2118 ? 173.711 263.733 275.620 1.00 38.94 ? 2118 ARG A NH2   1 
ATOM   5315  N  N     . GLY A 1 2119 ? 170.906 260.143 273.533 1.00 32.94 ? 2119 GLY A N     1 
ATOM   5316  C  CA    . GLY A 1 2119 ? 169.472 260.249 273.690 1.00 33.75 ? 2119 GLY A CA    1 
ATOM   5317  C  C     . GLY A 1 2119 ? 168.698 259.258 272.840 1.00 37.03 ? 2119 GLY A C     1 
ATOM   5318  O  O     . GLY A 1 2119 ? 169.216 258.247 272.359 1.00 36.93 ? 2119 GLY A O     1 
ATOM   5319  N  N     . GLU A 1 2120 ? 167.412 259.555 272.682 1.00 32.73 ? 2120 GLU A N     1 
ATOM   5320  C  CA    . GLU A 1 2120 ? 166.496 258.740 271.885 1.00 36.90 ? 2120 GLU A CA    1 
ATOM   5321  C  C     . GLU A 1 2120 ? 165.583 259.643 271.061 1.00 36.07 ? 2120 GLU A C     1 
ATOM   5322  O  O     . GLU A 1 2120 ? 164.364 259.465 271.017 1.00 35.87 ? 2120 GLU A O     1 
ATOM   5323  C  CB    . GLU A 1 2120 ? 165.690 257.793 272.773 1.00 34.90 ? 2120 GLU A CB    1 
ATOM   5324  C  CG    . GLU A 1 2120 ? 166.467 256.571 273.238 1.00 34.48 ? 2120 GLU A CG    1 
ATOM   5325  C  CD    . GLU A 1 2120 ? 165.610 255.601 274.026 1.00 40.32 ? 2120 GLU A CD    1 
ATOM   5326  O  OE1   . GLU A 1 2120 ? 164.589 255.128 273.482 1.00 40.28 ? 2120 GLU A OE1   1 
ATOM   5327  O  OE2   . GLU A 1 2120 ? 165.958 255.307 275.189 1.00 38.65 ? 2120 GLU A OE2   1 
ATOM   5328  N  N     . ALA A 1 2121 ? 166.174 260.634 270.397 1.00 32.58 ? 2121 ALA A N     1 
ATOM   5329  C  CA    . ALA A 1 2121 ? 165.430 261.672 269.688 1.00 31.17 ? 2121 ALA A CA    1 
ATOM   5330  C  C     . ALA A 1 2121 ? 165.331 261.402 268.190 1.00 30.95 ? 2121 ALA A C     1 
ATOM   5331  O  O     . ALA A 1 2121 ? 165.395 262.334 267.385 1.00 31.13 ? 2121 ALA A O     1 
ATOM   5332  C  CB    . ALA A 1 2121 ? 166.062 263.036 269.942 1.00 28.92 ? 2121 ALA A CB    1 
ATOM   5333  N  N     . VAL A 1 2122 ? 165.182 260.138 267.788 1.00 32.16 ? 2122 VAL A N     1 
ATOM   5334  C  CA    . VAL A 1 2122 ? 165.058 259.793 266.375 1.00 29.19 ? 2122 VAL A CA    1 
ATOM   5335  C  C     . VAL A 1 2122 ? 163.796 260.436 265.812 1.00 31.49 ? 2122 VAL A C     1 
ATOM   5336  O  O     . VAL A 1 2122 ? 162.677 260.069 266.180 1.00 34.92 ? 2122 VAL A O     1 
ATOM   5337  C  CB    . VAL A 1 2122 ? 165.041 258.269 266.171 1.00 29.90 ? 2122 VAL A CB    1 
ATOM   5338  C  CG1   . VAL A 1 2122 ? 164.710 257.933 264.723 1.00 31.01 ? 2122 VAL A CG1   1 
ATOM   5339  C  CG2   . VAL A 1 2122 ? 166.377 257.663 266.573 1.00 23.11 ? 2122 VAL A CG2   1 
ATOM   5340  N  N     . ASP A 1 2123 ? 163.978 261.408 264.919 1.00 28.74 ? 2123 ASP A N     1 
ATOM   5341  C  CA    . ASP A 1 2123 ? 162.887 262.200 264.360 1.00 31.15 ? 2123 ASP A CA    1 
ATOM   5342  C  C     . ASP A 1 2123 ? 163.065 262.354 262.854 1.00 33.58 ? 2123 ASP A C     1 
ATOM   5343  O  O     . ASP A 1 2123 ? 163.096 263.471 262.328 1.00 32.73 ? 2123 ASP A O     1 
ATOM   5344  C  CB    . ASP A 1 2123 ? 162.783 263.563 265.043 1.00 28.62 ? 2123 ASP A CB    1 
ATOM   5345  C  CG    . ASP A 1 2123 ? 161.419 264.200 264.863 1.00 35.25 ? 2123 ASP A CG    1 
ATOM   5346  O  OD1   . ASP A 1 2123 ? 160.414 263.572 265.259 1.00 36.80 ? 2123 ASP A OD1   1 
ATOM   5347  O  OD2   . ASP A 1 2123 ? 161.346 265.329 264.337 1.00 39.28 ? 2123 ASP A OD2   1 
ATOM   5348  N  N     . GLU A 1 2124 ? 163.194 261.223 262.151 1.00 31.81 ? 2124 GLU A N     1 
ATOM   5349  C  CA    . GLU A 1 2124 ? 163.638 261.124 260.759 1.00 26.78 ? 2124 GLU A CA    1 
ATOM   5350  C  C     . GLU A 1 2124 ? 163.179 262.275 259.868 1.00 27.01 ? 2124 GLU A C     1 
ATOM   5351  O  O     . GLU A 1 2124 ? 163.956 262.762 259.039 1.00 32.86 ? 2124 GLU A O     1 
ATOM   5352  C  CB    . GLU A 1 2124 ? 163.173 259.795 260.148 1.00 27.87 ? 2124 GLU A CB    1 
ATOM   5353  C  CG    . GLU A 1 2124 ? 161.676 259.505 260.257 1.00 29.75 ? 2124 GLU A CG    1 
ATOM   5354  C  CD    . GLU A 1 2124 ? 161.254 259.008 261.629 1.00 38.06 ? 2124 GLU A CD    1 
ATOM   5355  O  OE1   . GLU A 1 2124 ? 162.129 258.854 262.505 1.00 35.37 ? 2124 GLU A OE1   1 
ATOM   5356  O  OE2   . GLU A 1 2124 ? 160.043 258.770 261.827 1.00 35.94 ? 2124 GLU A OE2   1 
ATOM   5357  N  N     . GLY A 1 2125 ? 161.927 262.704 260.006 1.00 27.26 ? 2125 GLY A N     1 
ATOM   5358  C  CA    . GLY A 1 2125 ? 161.445 263.844 259.253 1.00 31.48 ? 2125 GLY A CA    1 
ATOM   5359  C  C     . GLY A 1 2125 ? 162.266 265.097 259.480 1.00 30.12 ? 2125 GLY A C     1 
ATOM   5360  O  O     . GLY A 1 2125 ? 162.630 265.789 258.526 1.00 30.74 ? 2125 GLY A O     1 
ATOM   5361  N  N     . GLU A 1 2126 ? 162.576 265.394 260.746 1.00 31.54 ? 2126 GLU A N     1 
ATOM   5362  C  CA    . GLU A 1 2126 ? 163.440 266.530 261.045 1.00 32.31 ? 2126 GLU A CA    1 
ATOM   5363  C  C     . GLU A 1 2126 ? 164.887 266.247 260.659 1.00 31.18 ? 2126 GLU A C     1 
ATOM   5364  O  O     . GLU A 1 2126 ? 165.643 267.180 260.365 1.00 27.23 ? 2126 GLU A O     1 
ATOM   5365  C  CB    . GLU A 1 2126 ? 163.344 266.888 262.529 1.00 30.95 ? 2126 GLU A CB    1 
ATOM   5366  C  CG    . GLU A 1 2126 ? 164.209 268.062 262.961 1.00 34.83 ? 2126 GLU A CG    1 
ATOM   5367  C  CD    . GLU A 1 2126 ? 164.068 268.378 264.437 1.00 39.85 ? 2126 GLU A CD    1 
ATOM   5368  O  OE1   . GLU A 1 2126 ? 163.293 267.681 265.125 1.00 41.60 ? 2126 GLU A OE1   1 
ATOM   5369  O  OE2   . GLU A 1 2126 ? 164.733 269.324 264.909 1.00 38.08 ? 2126 GLU A OE2   1 
ATOM   5370  N  N     . ILE A 1 2127 ? 165.285 264.973 260.648 1.00 26.91 ? 2127 ILE A N     1 
ATOM   5371  C  CA    . ILE A 1 2127 ? 166.645 264.622 260.252 1.00 26.88 ? 2127 ILE A CA    1 
ATOM   5372  C  C     . ILE A 1 2127 ? 166.906 265.048 258.814 1.00 26.21 ? 2127 ILE A C     1 
ATOM   5373  O  O     . ILE A 1 2127 ? 167.994 265.539 258.483 1.00 29.68 ? 2127 ILE A O     1 
ATOM   5374  C  CB    . ILE A 1 2127 ? 166.886 263.114 260.455 1.00 28.03 ? 2127 ILE A CB    1 
ATOM   5375  C  CG1   . ILE A 1 2127 ? 166.633 262.728 261.914 1.00 29.69 ? 2127 ILE A CG1   1 
ATOM   5376  C  CG2   . ILE A 1 2127 ? 168.297 262.733 260.036 1.00 17.59 ? 2127 ILE A CG2   1 
ATOM   5377  C  CD1   . ILE A 1 2127 ? 167.004 261.299 262.247 1.00 28.35 ? 2127 ILE A CD1   1 
ATOM   5378  N  N     . ALA A 1 2128 ? 165.916 264.876 257.940 1.00 28.28 ? 2128 ALA A N     1 
ATOM   5379  C  CA    . ALA A 1 2128 ? 166.048 265.326 256.559 1.00 27.22 ? 2128 ALA A CA    1 
ATOM   5380  C  C     . ALA A 1 2128 ? 165.934 266.838 256.422 1.00 30.44 ? 2128 ALA A C     1 
ATOM   5381  O  O     . ALA A 1 2128 ? 166.366 267.386 255.403 1.00 26.69 ? 2128 ALA A O     1 
ATOM   5382  C  CB    . ALA A 1 2128 ? 164.995 264.650 255.680 1.00 19.35 ? 2128 ALA A CB    1 
ATOM   5383  N  N     . GLU A 1 2129 ? 165.358 267.522 257.413 1.00 27.80 ? 2129 GLU A N     1 
ATOM   5384  C  CA    . GLU A 1 2129 ? 165.243 268.976 257.341 1.00 25.08 ? 2129 GLU A CA    1 
ATOM   5385  C  C     . GLU A 1 2129 ? 166.609 269.640 257.455 1.00 27.84 ? 2129 GLU A C     1 
ATOM   5386  O  O     . GLU A 1 2129 ? 166.951 270.519 256.658 1.00 29.48 ? 2129 GLU A O     1 
ATOM   5387  C  CB    . GLU A 1 2129 ? 164.302 269.485 258.433 1.00 29.17 ? 2129 GLU A CB    1 
ATOM   5388  C  CG    . GLU A 1 2129 ? 162.848 269.073 258.252 1.00 29.91 ? 2129 GLU A CG    1 
ATOM   5389  C  CD    . GLU A 1 2129 ? 162.148 269.844 257.147 1.00 39.25 ? 2129 GLU A CD    1 
ATOM   5390  O  OE1   . GLU A 1 2129 ? 162.756 270.782 256.590 1.00 38.03 ? 2129 GLU A OE1   1 
ATOM   5391  O  OE2   . GLU A 1 2129 ? 160.986 269.510 256.834 1.00 46.44 ? 2129 GLU A OE2   1 
ATOM   5392  N  N     . ASN A 1 2130 ? 167.401 269.237 258.449 1.00 27.93 ? 2130 ASN A N     1 
ATOM   5393  C  CA    . ASN A 1 2130 ? 168.750 269.765 258.639 1.00 23.14 ? 2130 ASN A CA    1 
ATOM   5394  C  C     . ASN A 1 2130 ? 169.746 268.744 258.095 1.00 26.02 ? 2130 ASN A C     1 
ATOM   5395  O  O     . ASN A 1 2130 ? 170.413 268.023 258.835 1.00 30.02 ? 2130 ASN A O     1 
ATOM   5396  C  CB    . ASN A 1 2130 ? 169.000 270.078 260.109 1.00 23.75 ? 2130 ASN A CB    1 
ATOM   5397  C  CG    . ASN A 1 2130 ? 168.089 271.168 260.635 1.00 28.63 ? 2130 ASN A CG    1 
ATOM   5398  O  OD1   . ASN A 1 2130 ? 167.249 270.926 261.502 1.00 31.77 ? 2130 ASN A OD1   1 
ATOM   5399  N  ND2   . ASN A 1 2130 ? 168.248 272.377 260.108 1.00 30.36 ? 2130 ASN A ND2   1 
ATOM   5400  N  N     . LEU A 1 2131 ? 169.842 268.692 256.768 1.00 25.48 ? 2131 LEU A N     1 
ATOM   5401  C  CA    . LEU A 1 2131 ? 170.769 267.792 256.091 1.00 19.45 ? 2131 LEU A CA    1 
ATOM   5402  C  C     . LEU A 1 2131 ? 171.509 268.586 255.024 1.00 21.54 ? 2131 LEU A C     1 
ATOM   5403  O  O     . LEU A 1 2131 ? 170.865 269.141 254.109 1.00 25.32 ? 2131 LEU A O     1 
ATOM   5404  C  CB    . LEU A 1 2131 ? 170.036 266.596 255.478 1.00 21.90 ? 2131 LEU A CB    1 
ATOM   5405  C  CG    . LEU A 1 2131 ? 170.932 265.559 254.802 1.00 21.06 ? 2131 LEU A CG    1 
ATOM   5406  C  CD1   . LEU A 1 2131 ? 171.870 264.936 255.823 1.00 20.44 ? 2131 LEU A CD1   1 
ATOM   5407  C  CD2   . LEU A 1 2131 ? 170.101 264.494 254.108 1.00 11.21 ? 2131 LEU A CD2   1 
ATOM   5408  N  N     . PRO A 1 2132 ? 172.840 268.672 255.085 1.00 22.99 ? 2132 PRO A N     1 
ATOM   5409  C  CA    . PRO A 1 2132 ? 173.578 269.491 254.115 1.00 17.69 ? 2132 PRO A CA    1 
ATOM   5410  C  C     . PRO A 1 2132 ? 173.604 268.865 252.731 1.00 15.57 ? 2132 PRO A C     1 
ATOM   5411  O  O     . PRO A 1 2132 ? 174.584 268.216 252.355 1.00 18.31 ? 2132 PRO A O     1 
ATOM   5412  C  CB    . PRO A 1 2132 ? 174.986 269.568 254.720 1.00 20.17 ? 2132 PRO A CB    1 
ATOM   5413  C  CG    . PRO A 1 2132 ? 174.819 269.159 256.156 1.00 17.17 ? 2132 PRO A CG    1 
ATOM   5414  C  CD    . PRO A 1 2132 ? 173.720 268.155 256.141 1.00 16.91 ? 2132 PRO A CD    1 
ATOM   5415  N  N     . GLU A 1 2133 ? 172.526 269.058 251.967 1.00 14.55 ? 2133 GLU A N     1 
ATOM   5416  C  CA    . GLU A 1 2133 ? 172.412 268.416 250.662 1.00 13.32 ? 2133 GLU A CA    1 
ATOM   5417  C  C     . GLU A 1 2133 ? 173.493 268.901 249.703 1.00 12.83 ? 2133 GLU A C     1 
ATOM   5418  O  O     . GLU A 1 2133 ? 174.023 268.112 248.911 1.00 18.99 ? 2133 GLU A O     1 
ATOM   5419  C  CB    . GLU A 1 2133 ? 171.020 268.658 250.080 1.00 17.62 ? 2133 GLU A CB    1 
ATOM   5420  C  CG    . GLU A 1 2133 ? 169.939 267.823 250.736 1.00 13.78 ? 2133 GLU A CG    1 
ATOM   5421  C  CD    . GLU A 1 2133 ? 168.569 268.063 250.138 1.00 14.39 ? 2133 GLU A CD    1 
ATOM   5422  O  OE1   . GLU A 1 2133 ? 168.469 268.863 249.186 1.00 13.59 ? 2133 GLU A OE1   1 
ATOM   5423  O  OE2   . GLU A 1 2133 ? 167.593 267.454 250.621 1.00 17.42 ? 2133 GLU A OE2   1 
ATOM   5424  N  N     . GLN A 1 2134 ? 173.824 270.192 249.746 1.00 11.11 ? 2134 GLN A N     1 
ATOM   5425  C  CA    . GLN A 1 2134 ? 174.912 270.695 248.913 1.00 12.27 ? 2134 GLN A CA    1 
ATOM   5426  C  C     . GLN A 1 2134 ? 176.242 270.057 249.298 1.00 11.08 ? 2134 GLN A C     1 
ATOM   5427  O  O     . GLN A 1 2134 ? 177.034 269.691 248.425 1.00 10.94 ? 2134 GLN A O     1 
ATOM   5428  C  CB    . GLN A 1 2134 ? 174.996 272.217 249.005 1.00 12.15 ? 2134 GLN A CB    1 
ATOM   5429  C  CG    . GLN A 1 2134 ? 173.871 272.939 248.289 1.00 11.02 ? 2134 GLN A CG    1 
ATOM   5430  C  CD    . GLN A 1 2134 ? 174.249 274.339 247.863 1.00 15.46 ? 2134 GLN A CD    1 
ATOM   5431  O  OE1   . GLN A 1 2134 ? 175.397 274.758 248.011 1.00 18.09 ? 2134 GLN A OE1   1 
ATOM   5432  N  NE2   . GLN A 1 2134 ? 173.283 275.074 247.327 1.00 20.27 ? 2134 GLN A NE2   1 
ATOM   5433  N  N     . GLU A 1 2135 ? 176.498 269.908 250.600 1.00 14.21 ? 2135 GLU A N     1 
ATOM   5434  C  CA    . GLU A 1 2135 ? 177.737 269.278 251.043 1.00 10.79 ? 2135 GLU A CA    1 
ATOM   5435  C  C     . GLU A 1 2135 ? 177.804 267.816 250.622 1.00 9.89  ? 2135 GLU A C     1 
ATOM   5436  O  O     . GLU A 1 2135 ? 178.892 267.303 250.335 1.00 12.07 ? 2135 GLU A O     1 
ATOM   5437  C  CB    . GLU A 1 2135 ? 177.878 269.408 252.560 1.00 13.69 ? 2135 GLU A CB    1 
ATOM   5438  C  CG    . GLU A 1 2135 ? 179.211 268.944 253.109 1.00 15.51 ? 2135 GLU A CG    1 
ATOM   5439  C  CD    . GLU A 1 2135 ? 179.087 268.301 254.475 1.00 28.13 ? 2135 GLU A CD    1 
ATOM   5440  O  OE1   . GLU A 1 2135 ? 180.078 268.322 255.236 1.00 34.51 ? 2135 GLU A OE1   1 
ATOM   5441  O  OE2   . GLU A 1 2135 ? 178.000 267.774 254.792 1.00 29.61 ? 2135 GLU A OE2   1 
ATOM   5442  N  N     . ILE A 1 2136 ? 176.658 267.133 250.578 1.00 12.21 ? 2136 ILE A N     1 
ATOM   5443  C  CA    . ILE A 1 2136 ? 176.623 265.752 250.106 1.00 6.73  ? 2136 ILE A CA    1 
ATOM   5444  C  C     . ILE A 1 2136 ? 177.053 265.685 248.646 1.00 6.53  ? 2136 ILE A C     1 
ATOM   5445  O  O     . ILE A 1 2136 ? 177.855 264.829 248.253 1.00 8.12  ? 2136 ILE A O     1 
ATOM   5446  C  CB    . ILE A 1 2136 ? 175.218 265.156 250.306 1.00 10.11 ? 2136 ILE A CB    1 
ATOM   5447  C  CG1   . ILE A 1 2136 ? 174.894 265.052 251.794 1.00 10.12 ? 2136 ILE A CG1   1 
ATOM   5448  C  CG2   . ILE A 1 2136 ? 175.107 263.795 249.638 1.00 7.71  ? 2136 ILE A CG2   1 
ATOM   5449  C  CD1   . ILE A 1 2136 ? 173.455 264.707 252.086 1.00 12.24 ? 2136 ILE A CD1   1 
ATOM   5450  N  N     . LEU A 1 2137 ? 176.527 266.594 247.822 1.00 6.93  ? 2137 LEU A N     1 
ATOM   5451  C  CA    . LEU A 1 2137 ? 176.860 266.596 246.402 1.00 5.61  ? 2137 LEU A CA    1 
ATOM   5452  C  C     . LEU A 1 2137 ? 178.331 266.925 246.176 1.00 7.31  ? 2137 LEU A C     1 
ATOM   5453  O  O     . LEU A 1 2137 ? 178.966 266.368 245.273 1.00 8.78  ? 2137 LEU A O     1 
ATOM   5454  C  CB    . LEU A 1 2137 ? 175.962 267.586 245.659 1.00 4.85  ? 2137 LEU A CB    1 
ATOM   5455  C  CG    . LEU A 1 2137 ? 175.936 267.509 244.132 1.00 5.21  ? 2137 LEU A CG    1 
ATOM   5456  C  CD1   . LEU A 1 2137 ? 175.582 266.111 243.663 1.00 7.96  ? 2137 LEU A CD1   1 
ATOM   5457  C  CD2   . LEU A 1 2137 ? 174.958 268.526 243.570 1.00 8.36  ? 2137 LEU A CD2   1 
ATOM   5458  N  N     . ILE A 1 2138 ? 178.890 267.832 246.980 1.00 4.68  ? 2138 ILE A N     1 
ATOM   5459  C  CA    . ILE A 1 2138 ? 180.296 268.195 246.829 1.00 6.73  ? 2138 ILE A CA    1 
ATOM   5460  C  C     . ILE A 1 2138 ? 181.191 267.006 247.150 1.00 7.23  ? 2138 ILE A C     1 
ATOM   5461  O  O     . ILE A 1 2138 ? 182.209 266.779 246.481 1.00 7.92  ? 2138 ILE A O     1 
ATOM   5462  C  CB    . ILE A 1 2138 ? 180.636 269.413 247.706 1.00 8.89  ? 2138 ILE A CB    1 
ATOM   5463  C  CG1   . ILE A 1 2138 ? 179.763 270.603 247.319 1.00 10.31 ? 2138 ILE A CG1   1 
ATOM   5464  C  CG2   . ILE A 1 2138 ? 182.101 269.778 247.575 1.00 8.07  ? 2138 ILE A CG2   1 
ATOM   5465  C  CD1   . ILE A 1 2138 ? 179.942 271.048 245.906 1.00 11.52 ? 2138 ILE A CD1   1 
ATOM   5466  N  N     . GLN A 1 2139 ? 180.832 266.232 248.174 1.00 5.41  ? 2139 GLN A N     1 
ATOM   5467  C  CA    . GLN A 1 2139 ? 181.614 265.054 248.528 1.00 5.14  ? 2139 GLN A CA    1 
ATOM   5468  C  C     . GLN A 1 2139 ? 181.645 264.048 247.385 1.00 6.97  ? 2139 GLN A C     1 
ATOM   5469  O  O     . GLN A 1 2139 ? 182.699 263.480 247.079 1.00 10.73 ? 2139 GLN A O     1 
ATOM   5470  C  CB    . GLN A 1 2139 ? 181.048 264.416 249.796 1.00 4.83  ? 2139 GLN A CB    1 
ATOM   5471  C  CG    . GLN A 1 2139 ? 181.889 263.290 250.354 1.00 7.20  ? 2139 GLN A CG    1 
ATOM   5472  C  CD    . GLN A 1 2139 ? 181.186 262.531 251.460 1.00 7.50  ? 2139 GLN A CD    1 
ATOM   5473  O  OE1   . GLN A 1 2139 ? 180.615 263.130 252.370 1.00 15.19 ? 2139 GLN A OE1   1 
ATOM   5474  N  NE2   . GLN A 1 2139 ? 181.226 261.208 251.389 1.00 7.80  ? 2139 GLN A NE2   1 
ATOM   5475  N  N     . SER A 1 2140 ? 180.503 263.822 246.735 1.00 6.37  ? 2140 SER A N     1 
ATOM   5476  C  CA    . SER A 1 2140 ? 180.467 262.907 245.600 1.00 5.01  ? 2140 SER A CA    1 
ATOM   5477  C  C     . SER A 1 2140 ? 181.317 263.424 244.446 1.00 4.73  ? 2140 SER A C     1 
ATOM   5478  O  O     . SER A 1 2140 ? 181.997 262.643 243.772 1.00 11.23 ? 2140 SER A O     1 
ATOM   5479  C  CB    . SER A 1 2140 ? 179.026 262.685 245.149 1.00 4.86  ? 2140 SER A CB    1 
ATOM   5480  O  OG    . SER A 1 2140 ? 178.220 262.285 246.241 1.00 13.49 ? 2140 SER A OG    1 
ATOM   5481  N  N     . VAL A 1 2141 ? 181.285 264.735 244.200 1.00 5.72  ? 2141 VAL A N     1 
ATOM   5482  C  CA    . VAL A 1 2141 ? 182.093 265.317 243.132 1.00 5.94  ? 2141 VAL A CA    1 
ATOM   5483  C  C     . VAL A 1 2141 ? 183.576 265.127 243.427 1.00 4.61  ? 2141 VAL A C     1 
ATOM   5484  O  O     . VAL A 1 2141 ? 184.351 264.701 242.565 1.00 5.90  ? 2141 VAL A O     1 
ATOM   5485  C  CB    . VAL A 1 2141 ? 181.744 266.804 242.946 1.00 3.60  ? 2141 VAL A CB    1 
ATOM   5486  C  CG1   . VAL A 1 2141 ? 182.787 267.496 242.085 1.00 6.72  ? 2141 VAL A CG1   1 
ATOM   5487  C  CG2   . VAL A 1 2141 ? 180.369 266.950 242.333 1.00 2.79  ? 2141 VAL A CG2   1 
ATOM   5488  N  N     . CYS A 1 2142 ? 183.989 265.429 244.659 1.00 3.26  ? 2142 CYS A N     1 
ATOM   5489  C  CA    . CYS A 1 2142 ? 185.407 265.372 244.993 1.00 4.89  ? 2142 CYS A CA    1 
ATOM   5490  C  C     . CYS A 1 2142 ? 185.911 263.935 245.062 1.00 6.87  ? 2142 CYS A C     1 
ATOM   5491  O  O     . CYS A 1 2142 ? 187.045 263.652 244.659 1.00 6.28  ? 2142 CYS A O     1 
ATOM   5492  C  CB    . CYS A 1 2142 ? 185.657 266.102 246.310 1.00 5.03  ? 2142 CYS A CB    1 
ATOM   5493  S  SG    . CYS A 1 2142 ? 185.473 267.896 246.190 1.00 12.58 ? 2142 CYS A SG    1 
ATOM   5494  N  N     . GLU A 1 2143 ? 185.087 263.015 245.564 1.00 4.56  ? 2143 GLU A N     1 
ATOM   5495  C  CA    . GLU A 1 2143 ? 185.475 261.611 245.593 1.00 3.61  ? 2143 GLU A CA    1 
ATOM   5496  C  C     . GLU A 1 2143 ? 185.615 261.016 244.198 1.00 4.70  ? 2143 GLU A C     1 
ATOM   5497  O  O     . GLU A 1 2143 ? 186.246 259.966 244.047 1.00 10.31 ? 2143 GLU A O     1 
ATOM   5498  C  CB    . GLU A 1 2143 ? 184.456 260.800 246.394 1.00 6.66  ? 2143 GLU A CB    1 
ATOM   5499  C  CG    . GLU A 1 2143 ? 184.480 261.049 247.891 1.00 7.68  ? 2143 GLU A CG    1 
ATOM   5500  C  CD    . GLU A 1 2143 ? 183.820 259.930 248.668 1.00 14.43 ? 2143 GLU A CD    1 
ATOM   5501  O  OE1   . GLU A 1 2143 ? 183.005 260.224 249.566 1.00 11.66 ? 2143 GLU A OE1   1 
ATOM   5502  O  OE2   . GLU A 1 2143 ? 184.101 258.754 248.366 1.00 26.55 ? 2143 GLU A OE2   1 
ATOM   5503  N  N     . THR A 1 2144 ? 185.053 261.663 243.179 1.00 4.52  ? 2144 THR A N     1 
ATOM   5504  C  CA    . THR A 1 2144 ? 185.010 261.105 241.837 1.00 2.78  ? 2144 THR A CA    1 
ATOM   5505  C  C     . THR A 1 2144 ? 185.794 261.918 240.816 1.00 4.20  ? 2144 THR A C     1 
ATOM   5506  O  O     . THR A 1 2144 ? 186.436 261.331 239.941 1.00 8.85  ? 2144 THR A O     1 
ATOM   5507  C  CB    . THR A 1 2144 ? 183.549 260.968 241.379 1.00 6.98  ? 2144 THR A CB    1 
ATOM   5508  O  OG1   . THR A 1 2144 ? 182.912 259.927 242.125 1.00 10.96 ? 2144 THR A OG1   1 
ATOM   5509  C  CG2   . THR A 1 2144 ? 183.467 260.595 239.919 1.00 13.09 ? 2144 THR A CG2   1 
ATOM   5510  N  N     . MET A 1 2145 ? 185.787 263.248 240.920 1.00 5.64  ? 2145 MET A N     1 
ATOM   5511  C  CA    . MET A 1 2145 ? 186.516 264.128 240.012 1.00 3.42  ? 2145 MET A CA    1 
ATOM   5512  C  C     . MET A 1 2145 ? 187.939 264.443 240.446 1.00 2.02  ? 2145 MET A C     1 
ATOM   5513  O  O     . MET A 1 2145 ? 188.818 264.543 239.590 1.00 2.57  ? 2145 MET A O     1 
ATOM   5514  C  CB    . MET A 1 2145 ? 185.764 265.456 239.839 1.00 6.37  ? 2145 MET A CB    1 
ATOM   5515  C  CG    . MET A 1 2145 ? 184.406 265.388 239.147 1.00 8.61  ? 2145 MET A CG    1 
ATOM   5516  S  SD    . MET A 1 2145 ? 184.473 264.792 237.444 1.00 38.89 ? 2145 MET A SD    1 
ATOM   5517  C  CE    . MET A 1 2145 ? 183.916 263.106 237.606 1.00 11.11 ? 2145 MET A CE    1 
ATOM   5518  N  N     . VAL A 1 2146 ? 188.186 264.619 241.747 1.00 1.64  ? 2146 VAL A N     1 
ATOM   5519  C  CA    . VAL A 1 2146 ? 189.502 265.077 242.200 1.00 1.91  ? 2146 VAL A CA    1 
ATOM   5520  C  C     . VAL A 1 2146 ? 190.629 264.114 241.833 1.00 1.17  ? 2146 VAL A C     1 
ATOM   5521  O  O     . VAL A 1 2146 ? 191.680 264.584 241.364 1.00 1.65  ? 2146 VAL A O     1 
ATOM   5522  C  CB    . VAL A 1 2146 ? 189.462 265.394 243.706 1.00 1.92  ? 2146 VAL A CB    1 
ATOM   5523  C  CG1   . VAL A 1 2146 ? 190.861 265.368 244.305 1.00 1.13  ? 2146 VAL A CG1   1 
ATOM   5524  C  CG2   . VAL A 1 2146 ? 188.805 266.743 243.940 1.00 1.37  ? 2146 VAL A CG2   1 
ATOM   5525  N  N     . PRO A 1 2147 ? 190.499 262.793 242.011 1.00 1.78  ? 2147 PRO A N     1 
ATOM   5526  C  CA    . PRO A 1 2147 ? 191.642 261.909 241.721 1.00 1.55  ? 2147 PRO A CA    1 
ATOM   5527  C  C     . PRO A 1 2147 ? 192.129 261.957 240.282 1.00 0.78  ? 2147 PRO A C     1 
ATOM   5528  O  O     . PRO A 1 2147 ? 193.284 261.596 240.028 1.00 1.55  ? 2147 PRO A O     1 
ATOM   5529  C  CB    . PRO A 1 2147 ? 191.104 260.517 242.081 1.00 1.21  ? 2147 PRO A CB    1 
ATOM   5530  C  CG    . PRO A 1 2147 ? 190.073 260.789 243.099 1.00 0.93  ? 2147 PRO A CG    1 
ATOM   5531  C  CD    . PRO A 1 2147 ? 189.392 262.027 242.612 1.00 0.88  ? 2147 PRO A CD    1 
ATOM   5532  N  N     . LYS A 1 2148 ? 191.296 262.379 239.332 1.00 1.15  ? 2148 LYS A N     1 
ATOM   5533  C  CA    . LYS A 1 2148 ? 191.717 262.465 237.939 1.00 1.07  ? 2148 LYS A CA    1 
ATOM   5534  C  C     . LYS A 1 2148 ? 192.463 263.754 237.621 1.00 1.05  ? 2148 LYS A C     1 
ATOM   5535  O  O     . LYS A 1 2148 ? 193.035 263.865 236.532 1.00 2.51  ? 2148 LYS A O     1 
ATOM   5536  C  CB    . LYS A 1 2148 ? 190.504 262.341 237.015 1.00 1.17  ? 2148 LYS A CB    1 
ATOM   5537  C  CG    . LYS A 1 2148 ? 189.833 263.662 236.678 1.00 2.46  ? 2148 LYS A CG    1 
ATOM   5538  C  CD    . LYS A 1 2148 ? 188.729 263.486 235.653 1.00 4.09  ? 2148 LYS A CD    1 
ATOM   5539  C  CE    . LYS A 1 2148 ? 187.690 262.490 236.132 1.00 10.67 ? 2148 LYS A CE    1 
ATOM   5540  N  NZ    . LYS A 1 2148 ? 186.518 262.426 235.222 1.00 13.03 ? 2148 LYS A NZ    1 
ATOM   5541  N  N     . LEU A 1 2149 ? 192.486 264.714 238.536 1.00 1.23  ? 2149 LEU A N     1 
ATOM   5542  C  CA    . LEU A 1 2149 ? 192.997 266.041 238.233 1.00 1.46  ? 2149 LEU A CA    1 
ATOM   5543  C  C     . LEU A 1 2149 ? 194.516 266.091 238.320 1.00 1.66  ? 2149 LEU A C     1 
ATOM   5544  O  O     . LEU A 1 2149 ? 195.126 265.459 239.186 1.00 2.61  ? 2149 LEU A O     1 
ATOM   5545  C  CB    . LEU A 1 2149 ? 192.397 267.064 239.191 1.00 2.22  ? 2149 LEU A CB    1 
ATOM   5546  C  CG    . LEU A 1 2149 ? 190.892 267.280 239.076 1.00 2.04  ? 2149 LEU A CG    1 
ATOM   5547  C  CD1   . LEU A 1 2149 ? 190.454 268.309 240.094 1.00 2.12  ? 2149 LEU A CD1   1 
ATOM   5548  C  CD2   . LEU A 1 2149 ? 190.506 267.695 237.667 1.00 1.35  ? 2149 LEU A CD2   1 
ATOM   5549  N  N     . VAL A 1 2150 ? 195.125 266.854 237.414 1.00 2.37  ? 2150 VAL A N     1 
ATOM   5550  C  CA    . VAL A 1 2150 ? 196.539 267.185 237.522 1.00 3.63  ? 2150 VAL A CA    1 
ATOM   5551  C  C     . VAL A 1 2150 ? 196.680 268.234 238.616 1.00 4.30  ? 2150 VAL A C     1 
ATOM   5552  O  O     . VAL A 1 2150 ? 195.684 268.809 239.066 1.00 5.12  ? 2150 VAL A O     1 
ATOM   5553  C  CB    . VAL A 1 2150 ? 197.121 267.675 236.182 1.00 3.13  ? 2150 VAL A CB    1 
ATOM   5554  C  CG1   . VAL A 1 2150 ? 197.025 266.577 235.130 1.00 1.27  ? 2150 VAL A CG1   1 
ATOM   5555  C  CG2   . VAL A 1 2150 ? 196.416 268.942 235.718 1.00 4.94  ? 2150 VAL A CG2   1 
ATOM   5556  N  N     . ALA A 1 2151 ? 197.916 268.488 239.051 1.00 4.58  ? 2151 ALA A N     1 
ATOM   5557  C  CA    . ALA A 1 2151 ? 198.130 269.318 240.232 1.00 5.03  ? 2151 ALA A CA    1 
ATOM   5558  C  C     . ALA A 1 2151 ? 197.602 270.735 240.036 1.00 9.15  ? 2151 ALA A C     1 
ATOM   5559  O  O     . ALA A 1 2151 ? 197.019 271.318 240.957 1.00 6.90  ? 2151 ALA A O     1 
ATOM   5560  C  CB    . ALA A 1 2151 ? 199.615 269.347 240.590 1.00 2.84  ? 2151 ALA A CB    1 
ATOM   5561  N  N     . GLU A 1 2152 ? 197.794 271.307 238.845 1.00 9.65  ? 2152 GLU A N     1 
ATOM   5562  C  CA    . GLU A 1 2152 ? 197.413 272.699 238.635 1.00 7.48  ? 2152 GLU A CA    1 
ATOM   5563  C  C     . GLU A 1 2152 ? 195.910 272.866 238.428 1.00 10.18 ? 2152 GLU A C     1 
ATOM   5564  O  O     . GLU A 1 2152 ? 195.402 273.987 238.504 1.00 15.40 ? 2152 GLU A O     1 
ATOM   5565  C  CB    . GLU A 1 2152 ? 198.208 273.285 237.465 1.00 13.18 ? 2152 GLU A CB    1 
ATOM   5566  C  CG    . GLU A 1 2152 ? 198.023 272.581 236.129 1.00 18.37 ? 2152 GLU A CG    1 
ATOM   5567  C  CD    . GLU A 1 2152 ? 196.837 273.087 235.339 1.00 15.11 ? 2152 GLU A CD    1 
ATOM   5568  O  OE1   . GLU A 1 2152 ? 196.355 274.206 235.618 1.00 14.57 ? 2152 GLU A OE1   1 
ATOM   5569  O  OE2   . GLU A 1 2152 ? 196.396 272.367 234.423 1.00 18.37 ? 2152 GLU A OE2   1 
ATOM   5570  N  N     . ASP A 1 2153 ? 195.184 271.774 238.179 1.00 8.57  ? 2153 ASP A N     1 
ATOM   5571  C  CA    . ASP A 1 2153 ? 193.730 271.855 238.076 1.00 6.93  ? 2153 ASP A CA    1 
ATOM   5572  C  C     . ASP A 1 2153 ? 193.026 271.705 239.418 1.00 7.08  ? 2153 ASP A C     1 
ATOM   5573  O  O     . ASP A 1 2153 ? 191.859 272.093 239.530 1.00 11.98 ? 2153 ASP A O     1 
ATOM   5574  C  CB    . ASP A 1 2153 ? 193.202 270.796 237.108 1.00 6.88  ? 2153 ASP A CB    1 
ATOM   5575  C  CG    . ASP A 1 2153 ? 193.378 271.188 235.658 1.00 7.65  ? 2153 ASP A CG    1 
ATOM   5576  O  OD1   . ASP A 1 2153 ? 193.746 272.349 235.394 1.00 17.44 ? 2153 ASP A OD1   1 
ATOM   5577  O  OD2   . ASP A 1 2153 ? 193.146 270.336 234.780 1.00 8.94  ? 2153 ASP A OD2   1 
ATOM   5578  N  N     . ILE A 1 2154 ? 193.700 271.152 240.427 1.00 6.07  ? 2154 ILE A N     1 
ATOM   5579  C  CA    . ILE A 1 2154 ? 193.053 270.953 241.727 1.00 6.47  ? 2154 ILE A CA    1 
ATOM   5580  C  C     . ILE A 1 2154 ? 192.595 272.268 242.350 1.00 8.54  ? 2154 ILE A C     1 
ATOM   5581  O  O     . ILE A 1 2154 ? 191.428 272.353 242.767 1.00 15.53 ? 2154 ILE A O     1 
ATOM   5582  C  CB    . ILE A 1 2154 ? 193.972 270.138 242.655 1.00 4.66  ? 2154 ILE A CB    1 
ATOM   5583  C  CG1   . ILE A 1 2154 ? 194.291 268.779 242.028 1.00 4.93  ? 2154 ILE A CG1   1 
ATOM   5584  C  CG2   . ILE A 1 2154 ? 193.328 269.953 244.018 1.00 7.09  ? 2154 ILE A CG2   1 
ATOM   5585  C  CD1   . ILE A 1 2154 ? 195.367 268.012 242.750 1.00 6.31  ? 2154 ILE A CD1   1 
ATOM   5586  N  N     . PRO A 1 2155 ? 193.428 273.313 242.452 1.00 11.39 ? 2155 PRO A N     1 
ATOM   5587  C  CA    . PRO A 1 2155 ? 192.906 274.593 242.959 1.00 7.72  ? 2155 PRO A CA    1 
ATOM   5588  C  C     . PRO A 1 2155 ? 191.835 275.200 242.071 1.00 9.70  ? 2155 PRO A C     1 
ATOM   5589  O  O     . PRO A 1 2155 ? 190.940 275.885 242.579 1.00 14.45 ? 2155 PRO A O     1 
ATOM   5590  C  CB    . PRO A 1 2155 ? 194.158 275.481 243.026 1.00 8.53  ? 2155 PRO A CB    1 
ATOM   5591  C  CG    . PRO A 1 2155 ? 195.296 274.531 243.055 1.00 7.15  ? 2155 PRO A CG    1 
ATOM   5592  C  CD    . PRO A 1 2155 ? 194.871 273.410 242.173 1.00 6.89  ? 2155 PRO A CD    1 
ATOM   5593  N  N     . LEU A 1 2156 ? 191.907 274.976 240.756 1.00 9.84  ? 2156 LEU A N     1 
ATOM   5594  C  CA    . LEU A 1 2156 ? 190.900 275.518 239.850 1.00 7.57  ? 2156 LEU A CA    1 
ATOM   5595  C  C     . LEU A 1 2156 ? 189.519 274.957 240.154 1.00 8.33  ? 2156 LEU A C     1 
ATOM   5596  O  O     . LEU A 1 2156 ? 188.536 275.705 240.213 1.00 12.54 ? 2156 LEU A O     1 
ATOM   5597  C  CB    . LEU A 1 2156 ? 191.281 275.221 238.400 1.00 9.17  ? 2156 LEU A CB    1 
ATOM   5598  C  CG    . LEU A 1 2156 ? 192.479 275.934 237.776 1.00 10.17 ? 2156 LEU A CG    1 
ATOM   5599  C  CD1   . LEU A 1 2156 ? 192.392 275.859 236.266 1.00 18.59 ? 2156 LEU A CD1   1 
ATOM   5600  C  CD2   . LEU A 1 2156 ? 192.522 277.382 238.220 1.00 16.54 ? 2156 LEU A CD2   1 
ATOM   5601  N  N     . LEU A 1 2157 ? 189.423 273.642 240.357 1.00 14.38 ? 2157 LEU A N     1 
ATOM   5602  C  CA    . LEU A 1 2157 ? 188.119 273.024 240.566 1.00 9.54  ? 2157 LEU A CA    1 
ATOM   5603  C  C     . LEU A 1 2157 ? 187.513 273.442 241.901 1.00 6.90  ? 2157 LEU A C     1 
ATOM   5604  O  O     . LEU A 1 2157 ? 186.292 273.595 242.012 1.00 10.75 ? 2157 LEU A O     1 
ATOM   5605  C  CB    . LEU A 1 2157 ? 188.238 271.501 240.445 1.00 10.59 ? 2157 LEU A CB    1 
ATOM   5606  C  CG    . LEU A 1 2157 ? 186.958 270.655 240.452 1.00 6.08  ? 2157 LEU A CG    1 
ATOM   5607  C  CD1   . LEU A 1 2157 ? 187.146 269.397 239.642 1.00 10.97 ? 2157 LEU A CD1   1 
ATOM   5608  C  CD2   . LEU A 1 2157 ? 186.608 270.265 241.866 1.00 2.43  ? 2157 LEU A CD2   1 
ATOM   5609  N  N     . PHE A 1 2158 ? 188.348 273.641 242.922 1.00 5.67  ? 2158 PHE A N     1 
ATOM   5610  C  CA    . PHE A 1 2158 ? 187.824 274.111 244.200 1.00 10.33 ? 2158 PHE A CA    1 
ATOM   5611  C  C     . PHE A 1 2158 ? 187.388 275.568 244.133 1.00 9.33  ? 2158 PHE A C     1 
ATOM   5612  O  O     . PHE A 1 2158 ? 186.433 275.957 244.813 1.00 10.60 ? 2158 PHE A O     1 
ATOM   5613  C  CB    . PHE A 1 2158 ? 188.855 273.896 245.305 1.00 9.26  ? 2158 PHE A CB    1 
ATOM   5614  C  CG    . PHE A 1 2158 ? 188.900 272.485 245.810 1.00 11.29 ? 2158 PHE A CG    1 
ATOM   5615  C  CD1   . PHE A 1 2158 ? 187.921 272.016 246.666 1.00 8.97  ? 2158 PHE A CD1   1 
ATOM   5616  C  CD2   . PHE A 1 2158 ? 189.909 271.624 245.418 1.00 13.54 ? 2158 PHE A CD2   1 
ATOM   5617  C  CE1   . PHE A 1 2158 ? 187.951 270.717 247.127 1.00 12.44 ? 2158 PHE A CE1   1 
ATOM   5618  C  CE2   . PHE A 1 2158 ? 189.946 270.324 245.877 1.00 10.58 ? 2158 PHE A CE2   1 
ATOM   5619  C  CZ    . PHE A 1 2158 ? 188.966 269.871 246.732 1.00 10.41 ? 2158 PHE A CZ    1 
ATOM   5620  N  N     . SER A 1 2159 ? 188.067 276.389 243.328 1.00 10.44 ? 2159 SER A N     1 
ATOM   5621  C  CA    . SER A 1 2159 ? 187.563 277.732 243.068 1.00 11.54 ? 2159 SER A CA    1 
ATOM   5622  C  C     . SER A 1 2159 ? 186.225 277.674 242.345 1.00 11.59 ? 2159 SER A C     1 
ATOM   5623  O  O     . SER A 1 2159 ? 185.297 278.419 242.680 1.00 12.09 ? 2159 SER A O     1 
ATOM   5624  C  CB    . SER A 1 2159 ? 188.581 278.535 242.261 1.00 13.23 ? 2159 SER A CB    1 
ATOM   5625  O  OG    . SER A 1 2159 ? 189.768 278.725 243.003 1.00 24.39 ? 2159 SER A OG    1 
ATOM   5626  N  N     . LEU A 1 2160 ? 186.105 276.782 241.360 1.00 9.10  ? 2160 LEU A N     1 
ATOM   5627  C  CA    . LEU A 1 2160 ? 184.822 276.574 240.697 1.00 7.99  ? 2160 LEU A CA    1 
ATOM   5628  C  C     . LEU A 1 2160 ? 183.778 276.061 241.678 1.00 10.55 ? 2160 LEU A C     1 
ATOM   5629  O  O     . LEU A 1 2160 ? 182.604 276.442 241.602 1.00 14.47 ? 2160 LEU A O     1 
ATOM   5630  C  CB    . LEU A 1 2160 ? 184.983 275.598 239.534 1.00 6.72  ? 2160 LEU A CB    1 
ATOM   5631  C  CG    . LEU A 1 2160 ? 185.645 276.111 238.256 1.00 9.46  ? 2160 LEU A CG    1 
ATOM   5632  C  CD1   . LEU A 1 2160 ? 185.860 274.962 237.291 1.00 11.44 ? 2160 LEU A CD1   1 
ATOM   5633  C  CD2   . LEU A 1 2160 ? 184.801 277.197 237.614 1.00 14.22 ? 2160 LEU A CD2   1 
ATOM   5634  N  N     . LEU A 1 2161 ? 184.183 275.182 242.598 1.00 9.39  ? 2161 LEU A N     1 
ATOM   5635  C  CA    . LEU A 1 2161 ? 183.246 274.678 243.595 1.00 7.58  ? 2161 LEU A CA    1 
ATOM   5636  C  C     . LEU A 1 2161 ? 182.746 275.797 244.497 1.00 9.68  ? 2161 LEU A C     1 
ATOM   5637  O  O     . LEU A 1 2161 ? 181.556 275.860 244.821 1.00 13.76 ? 2161 LEU A O     1 
ATOM   5638  C  CB    . LEU A 1 2161 ? 183.896 273.580 244.432 1.00 10.31 ? 2161 LEU A CB    1 
ATOM   5639  C  CG    . LEU A 1 2161 ? 183.957 272.175 243.837 1.00 10.31 ? 2161 LEU A CG    1 
ATOM   5640  C  CD1   . LEU A 1 2161 ? 184.829 271.286 244.715 1.00 11.11 ? 2161 LEU A CD1   1 
ATOM   5641  C  CD2   . LEU A 1 2161 ? 182.572 271.590 243.646 1.00 6.13  ? 2161 LEU A CD2   1 
ATOM   5642  N  N     . SER A 1 2162 ? 183.646 276.688 244.921 1.00 10.62 ? 2162 SER A N     1 
ATOM   5643  C  CA    . SER A 1 2162 ? 183.227 277.819 245.737 1.00 12.91 ? 2162 SER A CA    1 
ATOM   5644  C  C     . SER A 1 2162 ? 182.364 278.784 244.939 1.00 12.45 ? 2162 SER A C     1 
ATOM   5645  O  O     . SER A 1 2162 ? 181.505 279.465 245.510 1.00 19.69 ? 2162 SER A O     1 
ATOM   5646  C  CB    . SER A 1 2162 ? 184.446 278.540 246.311 1.00 12.04 ? 2162 SER A CB    1 
ATOM   5647  O  OG    . SER A 1 2162 ? 185.213 279.139 245.284 1.00 17.71 ? 2162 SER A OG    1 
ATOM   5648  N  N     . ASP A 1 2163 ? 182.579 278.855 243.624 1.00 14.38 ? 2163 ASP A N     1 
ATOM   5649  C  CA    . ASP A 1 2163 ? 181.780 279.738 242.782 1.00 10.15 ? 2163 ASP A CA    1 
ATOM   5650  C  C     . ASP A 1 2163 ? 180.336 279.259 242.685 1.00 11.84 ? 2163 ASP A C     1 
ATOM   5651  O  O     . ASP A 1 2163 ? 179.399 280.060 242.765 1.00 21.61 ? 2163 ASP A O     1 
ATOM   5652  C  CB    . ASP A 1 2163 ? 182.408 279.839 241.393 1.00 12.00 ? 2163 ASP A CB    1 
ATOM   5653  C  CG    . ASP A 1 2163 ? 183.532 280.852 241.338 1.00 27.22 ? 2163 ASP A CG    1 
ATOM   5654  O  OD1   . ASP A 1 2163 ? 183.272 282.036 241.633 1.00 37.14 ? 2163 ASP A OD1   1 
ATOM   5655  O  OD2   . ASP A 1 2163 ? 184.669 280.473 240.991 1.00 25.82 ? 2163 ASP A OD2   1 
ATOM   5656  N  N     . VAL A 1 2164 ? 180.137 277.955 242.511 1.00 9.57  ? 2164 VAL A N     1 
ATOM   5657  C  CA    . VAL A 1 2164 ? 178.795 277.421 242.307 1.00 11.14 ? 2164 VAL A CA    1 
ATOM   5658  C  C     . VAL A 1 2164 ? 178.147 276.981 243.620 1.00 11.33 ? 2164 VAL A C     1 
ATOM   5659  O  O     . VAL A 1 2164 ? 176.917 276.955 243.723 1.00 13.59 ? 2164 VAL A O     1 
ATOM   5660  C  CB    . VAL A 1 2164 ? 178.847 276.267 241.290 1.00 10.44 ? 2164 VAL A CB    1 
ATOM   5661  C  CG1   . VAL A 1 2164 ? 177.449 275.855 240.873 1.00 10.44 ? 2164 VAL A CG1   1 
ATOM   5662  C  CG2   . VAL A 1 2164 ? 179.659 276.673 240.074 1.00 10.34 ? 2164 VAL A CG2   1 
ATOM   5663  N  N     . PHE A 1 2165 ? 178.945 276.644 244.630 1.00 9.57  ? 2165 PHE A N     1 
ATOM   5664  C  CA    . PHE A 1 2165 ? 178.446 276.191 245.928 1.00 9.42  ? 2165 PHE A CA    1 
ATOM   5665  C  C     . PHE A 1 2165 ? 179.127 277.002 247.023 1.00 14.88 ? 2165 PHE A C     1 
ATOM   5666  O  O     . PHE A 1 2165 ? 180.019 276.500 247.720 1.00 18.52 ? 2165 PHE A O     1 
ATOM   5667  C  CB    . PHE A 1 2165 ? 178.689 274.694 246.121 1.00 11.24 ? 2165 PHE A CB    1 
ATOM   5668  C  CG    . PHE A 1 2165 ? 178.064 273.829 245.060 1.00 13.02 ? 2165 PHE A CG    1 
ATOM   5669  C  CD1   . PHE A 1 2165 ? 178.723 273.588 243.864 1.00 13.35 ? 2165 PHE A CD1   1 
ATOM   5670  C  CD2   . PHE A 1 2165 ? 176.829 273.239 245.267 1.00 10.20 ? 2165 PHE A CD2   1 
ATOM   5671  C  CE1   . PHE A 1 2165 ? 178.157 272.787 242.894 1.00 8.48  ? 2165 PHE A CE1   1 
ATOM   5672  C  CE2   . PHE A 1 2165 ? 176.258 272.438 244.299 1.00 11.20 ? 2165 PHE A CE2   1 
ATOM   5673  C  CZ    . PHE A 1 2165 ? 176.923 272.210 243.111 1.00 8.14  ? 2165 PHE A CZ    1 
ATOM   5674  N  N     . PRO A 1 2166 ? 178.733 278.264 247.202 1.00 16.23 ? 2166 PRO A N     1 
ATOM   5675  C  CA    . PRO A 1 2166 ? 179.407 279.114 248.193 1.00 12.19 ? 2166 PRO A CA    1 
ATOM   5676  C  C     . PRO A 1 2166 ? 179.249 278.575 249.606 1.00 11.87 ? 2166 PRO A C     1 
ATOM   5677  O  O     . PRO A 1 2166 ? 178.194 278.061 249.985 1.00 20.90 ? 2166 PRO A O     1 
ATOM   5678  C  CB    . PRO A 1 2166 ? 178.707 280.468 248.030 1.00 10.89 ? 2166 PRO A CB    1 
ATOM   5679  C  CG    . PRO A 1 2166 ? 178.064 280.415 246.686 1.00 15.39 ? 2166 PRO A CG    1 
ATOM   5680  C  CD    . PRO A 1 2166 ? 177.664 278.988 246.500 1.00 14.12 ? 2166 PRO A CD    1 
ATOM   5681  N  N     . GLY A 1 2167 ? 180.316 278.703 250.393 1.00 15.71 ? 2167 GLY A N     1 
ATOM   5682  C  CA    . GLY A 1 2167 ? 180.272 278.332 251.792 1.00 14.06 ? 2167 GLY A CA    1 
ATOM   5683  C  C     . GLY A 1 2167 ? 180.221 276.850 252.071 1.00 18.50 ? 2167 GLY A C     1 
ATOM   5684  O  O     . GLY A 1 2167 ? 179.942 276.459 253.207 1.00 20.81 ? 2167 GLY A O     1 
ATOM   5685  N  N     . VAL A 1 2168 ? 180.476 276.009 251.073 1.00 19.67 ? 2168 VAL A N     1 
ATOM   5686  C  CA    . VAL A 1 2168 ? 180.414 274.561 251.223 1.00 12.17 ? 2168 VAL A CA    1 
ATOM   5687  C  C     . VAL A 1 2168 ? 181.833 274.025 251.102 1.00 16.70 ? 2168 VAL A C     1 
ATOM   5688  O  O     . VAL A 1 2168 ? 182.512 274.263 250.097 1.00 20.07 ? 2168 VAL A O     1 
ATOM   5689  C  CB    . VAL A 1 2168 ? 179.484 273.926 250.179 1.00 16.67 ? 2168 VAL A CB    1 
ATOM   5690  C  CG1   . VAL A 1 2168 ? 179.380 272.430 250.408 1.00 20.12 ? 2168 VAL A CG1   1 
ATOM   5691  C  CG2   . VAL A 1 2168 ? 178.114 274.579 250.230 1.00 15.34 ? 2168 VAL A CG2   1 
ATOM   5692  N  N     . GLN A 1 2169 ? 182.274 273.295 252.121 1.00 22.56 ? 2169 GLN A N     1 
ATOM   5693  C  CA    . GLN A 1 2169 ? 183.649 272.829 252.214 1.00 22.19 ? 2169 GLN A CA    1 
ATOM   5694  C  C     . GLN A 1 2169 ? 183.711 271.314 252.092 1.00 22.13 ? 2169 GLN A C     1 
ATOM   5695  O  O     . GLN A 1 2169 ? 182.802 270.604 252.531 1.00 24.66 ? 2169 GLN A O     1 
ATOM   5696  C  CB    . GLN A 1 2169 ? 184.289 273.272 253.533 1.00 25.10 ? 2169 GLN A CB    1 
ATOM   5697  C  CG    . GLN A 1 2169 ? 184.561 274.759 253.610 1.00 21.92 ? 2169 GLN A CG    1 
ATOM   5698  C  CD    . GLN A 1 2169 ? 185.260 275.282 252.369 1.00 27.14 ? 2169 GLN A CD    1 
ATOM   5699  O  OE1   . GLN A 1 2169 ? 184.708 276.095 251.628 1.00 27.71 ? 2169 GLN A OE1   1 
ATOM   5700  N  NE2   . GLN A 1 2169 ? 186.480 274.816 252.137 1.00 30.02 ? 2169 GLN A NE2   1 
ATOM   5701  N  N     . TYR A 1 2170 ? 184.794 270.829 251.494 1.00 18.95 ? 2170 TYR A N     1 
ATOM   5702  C  CA    . TYR A 1 2170 ? 185.041 269.405 251.333 1.00 14.15 ? 2170 TYR A CA    1 
ATOM   5703  C  C     . TYR A 1 2170 ? 186.039 268.949 252.386 1.00 17.76 ? 2170 TYR A C     1 
ATOM   5704  O  O     . TYR A 1 2170 ? 187.112 269.544 252.527 1.00 24.84 ? 2170 TYR A O     1 
ATOM   5705  C  CB    . TYR A 1 2170 ? 185.581 269.100 249.935 1.00 17.46 ? 2170 TYR A CB    1 
ATOM   5706  C  CG    . TYR A 1 2170 ? 185.983 267.657 249.743 1.00 17.47 ? 2170 TYR A CG    1 
ATOM   5707  C  CD1   . TYR A 1 2170 ? 185.093 266.630 250.018 1.00 13.24 ? 2170 TYR A CD1   1 
ATOM   5708  C  CD2   . TYR A 1 2170 ? 187.258 267.323 249.307 1.00 15.46 ? 2170 TYR A CD2   1 
ATOM   5709  C  CE1   . TYR A 1 2170 ? 185.455 265.309 249.850 1.00 16.12 ? 2170 TYR A CE1   1 
ATOM   5710  C  CE2   . TYR A 1 2170 ? 187.630 266.002 249.138 1.00 13.92 ? 2170 TYR A CE2   1 
ATOM   5711  C  CZ    . TYR A 1 2170 ? 186.724 264.999 249.411 1.00 13.97 ? 2170 TYR A CZ    1 
ATOM   5712  O  OH    . TYR A 1 2170 ? 187.084 263.683 249.243 1.00 15.59 ? 2170 TYR A OH    1 
ATOM   5713  N  N     . HIS A 1 2171 ? 185.689 267.898 253.119 1.00 20.64 ? 2171 HIS A N     1 
ATOM   5714  C  CA    . HIS A 1 2171 ? 186.575 267.342 254.138 1.00 24.69 ? 2171 HIS A CA    1 
ATOM   5715  C  C     . HIS A 1 2171 ? 186.583 265.827 253.997 1.00 20.64 ? 2171 HIS A C     1 
ATOM   5716  O  O     . HIS A 1 2171 ? 185.565 265.173 254.239 1.00 28.49 ? 2171 HIS A O     1 
ATOM   5717  C  CB    . HIS A 1 2171 ? 186.140 267.761 255.541 1.00 24.25 ? 2171 HIS A CB    1 
ATOM   5718  C  CG    . HIS A 1 2171 ? 186.380 269.208 255.838 1.00 29.93 ? 2171 HIS A CG    1 
ATOM   5719  N  ND1   . HIS A 1 2171 ? 185.481 270.196 255.504 1.00 33.77 ? 2171 HIS A ND1   1 
ATOM   5720  C  CD2   . HIS A 1 2171 ? 187.424 269.833 256.433 1.00 31.87 ? 2171 HIS A CD2   1 
ATOM   5721  C  CE1   . HIS A 1 2171 ? 185.957 271.368 255.885 1.00 34.58 ? 2171 HIS A CE1   1 
ATOM   5722  N  NE2   . HIS A 1 2171 ? 187.135 271.176 256.451 1.00 37.66 ? 2171 HIS A NE2   1 
ATOM   5723  N  N     . ARG A 1 2172 ? 187.728 265.277 253.604 1.00 19.61 ? 2172 ARG A N     1 
ATOM   5724  C  CA    . ARG A 1 2172 ? 187.865 263.834 253.498 1.00 19.22 ? 2172 ARG A CA    1 
ATOM   5725  C  C     . ARG A 1 2172 ? 187.769 263.190 254.875 1.00 24.60 ? 2172 ARG A C     1 
ATOM   5726  O  O     . ARG A 1 2172 ? 188.150 263.778 255.891 1.00 27.84 ? 2172 ARG A O     1 
ATOM   5727  C  CB    . ARG A 1 2172 ? 189.202 263.464 252.862 1.00 18.59 ? 2172 ARG A CB    1 
ATOM   5728  C  CG    . ARG A 1 2172 ? 189.371 263.905 251.423 1.00 17.40 ? 2172 ARG A CG    1 
ATOM   5729  C  CD    . ARG A 1 2172 ? 190.737 263.501 250.901 1.00 24.76 ? 2172 ARG A CD    1 
ATOM   5730  N  NE    . ARG A 1 2172 ? 190.865 262.053 250.809 1.00 33.48 ? 2172 ARG A NE    1 
ATOM   5731  C  CZ    . ARG A 1 2172 ? 191.631 261.313 251.601 1.00 28.34 ? 2172 ARG A CZ    1 
ATOM   5732  N  NH1   . ARG A 1 2172 ? 192.354 261.855 252.567 1.00 24.62 ? 2172 ARG A NH1   1 
ATOM   5733  N  NH2   . ARG A 1 2172 ? 191.667 259.996 251.422 1.00 20.70 ? 2172 ARG A NH2   1 
ATOM   5734  N  N     . GLY A 1 2173 ? 187.249 261.967 254.903 1.00 24.60 ? 2173 GLY A N     1 
ATOM   5735  C  CA    . GLY A 1 2173 ? 187.304 261.183 256.122 1.00 24.19 ? 2173 GLY A CA    1 
ATOM   5736  C  C     . GLY A 1 2173 ? 188.735 260.793 256.444 1.00 25.34 ? 2173 GLY A C     1 
ATOM   5737  O  O     . GLY A 1 2173 ? 189.498 260.367 255.575 1.00 23.29 ? 2173 GLY A O     1 
ATOM   5738  N  N     . GLU A 1 2174 ? 189.105 260.952 257.712 1.00 25.07 ? 2174 GLU A N     1 
ATOM   5739  C  CA    . GLU A 1 2174 ? 190.449 260.598 258.164 1.00 22.23 ? 2174 GLU A CA    1 
ATOM   5740  C  C     . GLU A 1 2174 ? 190.429 259.098 258.424 1.00 23.57 ? 2174 GLU A C     1 
ATOM   5741  O  O     . GLU A 1 2174 ? 190.027 258.629 259.489 1.00 30.47 ? 2174 GLU A O     1 
ATOM   5742  C  CB    . GLU A 1 2174 ? 190.842 261.404 259.397 1.00 21.06 ? 2174 GLU A CB    1 
ATOM   5743  C  CG    . GLU A 1 2174 ? 192.311 261.290 259.784 1.00 25.77 ? 2174 GLU A CG    1 
ATOM   5744  C  CD    . GLU A 1 2174 ? 192.618 260.072 260.633 1.00 33.66 ? 2174 GLU A CD    1 
ATOM   5745  O  OE1   . GLU A 1 2174 ? 191.724 259.619 261.376 1.00 32.19 ? 2174 GLU A OE1   1 
ATOM   5746  O  OE2   . GLU A 1 2174 ? 193.756 259.564 260.552 1.00 31.02 ? 2174 GLU A OE2   1 
ATOM   5747  N  N     . MET A 1 2175 ? 190.854 258.330 257.418 1.00 17.16 ? 2175 MET A N     1 
ATOM   5748  C  CA    . MET A 1 2175 ? 190.715 256.873 257.427 1.00 14.11 ? 2175 MET A CA    1 
ATOM   5749  C  C     . MET A 1 2175 ? 191.868 256.240 258.206 1.00 12.22 ? 2175 MET A C     1 
ATOM   5750  O  O     . MET A 1 2175 ? 192.812 255.678 257.650 1.00 15.29 ? 2175 MET A O     1 
ATOM   5751  C  CB    . MET A 1 2175 ? 190.640 256.345 256.001 1.00 17.31 ? 2175 MET A CB    1 
ATOM   5752  C  CG    . MET A 1 2175 ? 189.386 256.771 255.261 1.00 17.62 ? 2175 MET A CG    1 
ATOM   5753  S  SD    . MET A 1 2175 ? 189.269 256.096 253.597 1.00 31.78 ? 2175 MET A SD    1 
ATOM   5754  C  CE    . MET A 1 2175 ? 190.481 257.093 252.736 1.00 10.52 ? 2175 MET A CE    1 
ATOM   5755  N  N     . THR A 1 2176 ? 191.756 256.317 259.535 1.00 13.50 ? 2176 THR A N     1 
ATOM   5756  C  CA    . THR A 1 2176 ? 192.812 255.808 260.403 1.00 12.13 ? 2176 THR A CA    1 
ATOM   5757  C  C     . THR A 1 2176 ? 193.030 254.313 260.206 1.00 8.37  ? 2176 THR A C     1 
ATOM   5758  O  O     . THR A 1 2176 ? 194.176 253.853 260.137 1.00 13.65 ? 2176 THR A O     1 
ATOM   5759  C  CB    . THR A 1 2176 ? 192.475 256.100 261.867 1.00 12.67 ? 2176 THR A CB    1 
ATOM   5760  O  OG1   . THR A 1 2176 ? 192.357 257.512 262.058 1.00 12.42 ? 2176 THR A OG1   1 
ATOM   5761  C  CG2   . THR A 1 2176 ? 193.559 255.561 262.783 1.00 18.41 ? 2176 THR A CG2   1 
ATOM   5762  N  N     . ALA A 1 2177 ? 191.946 253.542 260.107 1.00 10.21 ? 2177 ALA A N     1 
ATOM   5763  C  CA    . ALA A 1 2177 ? 192.075 252.092 260.031 1.00 7.15  ? 2177 ALA A CA    1 
ATOM   5764  C  C     . ALA A 1 2177 ? 192.853 251.661 258.793 1.00 8.66  ? 2177 ALA A C     1 
ATOM   5765  O  O     . ALA A 1 2177 ? 193.731 250.795 258.873 1.00 14.35 ? 2177 ALA A O     1 
ATOM   5766  C  CB    . ALA A 1 2177 ? 190.693 251.442 260.051 1.00 8.01  ? 2177 ALA A CB    1 
ATOM   5767  N  N     . LEU A 1 2178 ? 192.553 252.260 257.639 1.00 6.86  ? 2178 LEU A N     1 
ATOM   5768  C  CA    . LEU A 1 2178 ? 193.272 251.895 256.423 1.00 8.23  ? 2178 LEU A CA    1 
ATOM   5769  C  C     . LEU A 1 2178 ? 194.695 252.436 256.436 1.00 8.33  ? 2178 LEU A C     1 
ATOM   5770  O  O     . LEU A 1 2178 ? 195.627 251.757 255.990 1.00 8.62  ? 2178 LEU A O     1 
ATOM   5771  C  CB    . LEU A 1 2178 ? 192.518 252.388 255.189 1.00 7.39  ? 2178 LEU A CB    1 
ATOM   5772  C  CG    . LEU A 1 2178 ? 193.162 252.045 253.844 1.00 3.75  ? 2178 LEU A CG    1 
ATOM   5773  C  CD1   . LEU A 1 2178 ? 193.337 250.543 253.690 1.00 5.69  ? 2178 LEU A CD1   1 
ATOM   5774  C  CD2   . LEU A 1 2178 ? 192.347 252.606 252.696 1.00 2.36  ? 2178 LEU A CD2   1 
ATOM   5775  N  N     . ARG A 1 2179 ? 194.887 253.654 256.951 1.00 9.14  ? 2179 ARG A N     1 
ATOM   5776  C  CA    . ARG A 1 2179 ? 196.221 254.245 256.968 1.00 7.08  ? 2179 ARG A CA    1 
ATOM   5777  C  C     . ARG A 1 2179 ? 197.176 253.454 257.856 1.00 8.97  ? 2179 ARG A C     1 
ATOM   5778  O  O     . ARG A 1 2179 ? 198.364 253.328 257.537 1.00 11.58 ? 2179 ARG A O     1 
ATOM   5779  C  CB    . ARG A 1 2179 ? 196.154 255.706 257.409 1.00 5.82  ? 2179 ARG A CB    1 
ATOM   5780  C  CG    . ARG A 1 2179 ? 195.441 256.619 256.428 1.00 7.66  ? 2179 ARG A CG    1 
ATOM   5781  C  CD    . ARG A 1 2179 ? 195.511 258.069 256.866 1.00 7.11  ? 2179 ARG A CD    1 
ATOM   5782  N  NE    . ARG A 1 2179 ? 196.701 258.725 256.339 1.00 12.27 ? 2179 ARG A NE    1 
ATOM   5783  C  CZ    . ARG A 1 2179 ? 196.679 259.745 255.492 1.00 15.53 ? 2179 ARG A CZ    1 
ATOM   5784  N  NH1   . ARG A 1 2179 ? 195.542 260.278 255.079 1.00 10.20 ? 2179 ARG A NH1   1 
ATOM   5785  N  NH2   . ARG A 1 2179 ? 197.830 260.244 255.051 1.00 18.22 ? 2179 ARG A NH2   1 
ATOM   5786  N  N     . GLU A 1 2180 ? 196.685 252.927 258.980 1.00 7.57  ? 2180 GLU A N     1 
ATOM   5787  C  CA    . GLU A 1 2180 ? 197.541 252.104 259.831 1.00 8.49  ? 2180 GLU A CA    1 
ATOM   5788  C  C     . GLU A 1 2180 ? 197.998 250.845 259.104 1.00 8.71  ? 2180 GLU A C     1 
ATOM   5789  O  O     . GLU A 1 2180 ? 199.170 250.464 259.190 1.00 11.37 ? 2180 GLU A O     1 
ATOM   5790  C  CB    . GLU A 1 2180 ? 196.823 251.745 261.131 1.00 9.56  ? 2180 GLU A CB    1 
ATOM   5791  C  CG    . GLU A 1 2180 ? 196.542 252.925 262.042 1.00 15.89 ? 2180 GLU A CG    1 
ATOM   5792  C  CD    . GLU A 1 2180 ? 197.810 253.547 262.598 1.00 29.07 ? 2180 GLU A CD    1 
ATOM   5793  O  OE1   . GLU A 1 2180 ? 198.796 252.808 262.806 1.00 27.91 ? 2180 GLU A OE1   1 
ATOM   5794  O  OE2   . GLU A 1 2180 ? 197.821 254.773 262.833 1.00 32.87 ? 2180 GLU A OE2   1 
ATOM   5795  N  N     . GLU A 1 2181 ? 197.090 250.187 258.381 1.00 9.57  ? 2181 GLU A N     1 
ATOM   5796  C  CA    . GLU A 1 2181 ? 197.479 248.998 257.633 1.00 5.66  ? 2181 GLU A CA    1 
ATOM   5797  C  C     . GLU A 1 2181 ? 198.408 249.348 256.478 1.00 6.52  ? 2181 GLU A C     1 
ATOM   5798  O  O     . GLU A 1 2181 ? 199.344 248.597 256.182 1.00 9.74  ? 2181 GLU A O     1 
ATOM   5799  C  CB    . GLU A 1 2181 ? 196.240 248.257 257.126 1.00 6.39  ? 2181 GLU A CB    1 
ATOM   5800  C  CG    . GLU A 1 2181 ? 195.325 247.722 258.223 1.00 8.57  ? 2181 GLU A CG    1 
ATOM   5801  C  CD    . GLU A 1 2181 ? 195.895 246.519 258.966 1.00 16.99 ? 2181 GLU A CD    1 
ATOM   5802  O  OE1   . GLU A 1 2181 ? 197.086 246.192 258.781 1.00 23.65 ? 2181 GLU A OE1   1 
ATOM   5803  O  OE2   . GLU A 1 2181 ? 195.143 245.895 259.741 1.00 15.64 ? 2181 GLU A OE2   1 
ATOM   5804  N  N     . LEU A 1 2182 ? 198.170 250.483 255.816 1.00 5.57  ? 2182 LEU A N     1 
ATOM   5805  C  CA    . LEU A 1 2182 ? 199.057 250.911 254.739 1.00 4.66  ? 2182 LEU A CA    1 
ATOM   5806  C  C     . LEU A 1 2182 ? 200.464 251.177 255.258 1.00 6.82  ? 2182 LEU A C     1 
ATOM   5807  O  O     . LEU A 1 2182 ? 201.452 250.826 254.606 1.00 6.91  ? 2182 LEU A O     1 
ATOM   5808  C  CB    . LEU A 1 2182 ? 198.495 252.158 254.056 1.00 2.27  ? 2182 LEU A CB    1 
ATOM   5809  C  CG    . LEU A 1 2182 ? 197.242 251.990 253.197 1.00 3.10  ? 2182 LEU A CG    1 
ATOM   5810  C  CD1   . LEU A 1 2182 ? 196.627 253.340 252.879 1.00 2.03  ? 2182 LEU A CD1   1 
ATOM   5811  C  CD2   . LEU A 1 2182 ? 197.557 251.232 251.922 1.00 1.67  ? 2182 LEU A CD2   1 
ATOM   5812  N  N     . LYS A 1 2183 ? 200.569 251.799 256.434 1.00 7.71  ? 2183 LYS A N     1 
ATOM   5813  C  CA    . LYS A 1 2183 ? 201.878 252.093 257.007 1.00 6.60  ? 2183 LYS A CA    1 
ATOM   5814  C  C     . LYS A 1 2183 ? 202.644 250.813 257.323 1.00 7.19  ? 2183 LYS A C     1 
ATOM   5815  O  O     . LYS A 1 2183 ? 203.861 250.741 257.115 1.00 7.74  ? 2183 LYS A O     1 
ATOM   5816  C  CB    . LYS A 1 2183 ? 201.710 252.955 258.256 1.00 6.02  ? 2183 LYS A CB    1 
ATOM   5817  C  CG    . LYS A 1 2183 ? 203.005 253.378 258.912 1.00 10.83 ? 2183 LYS A CG    1 
ATOM   5818  C  CD    . LYS A 1 2183 ? 202.742 254.319 260.071 1.00 12.13 ? 2183 LYS A CD    1 
ATOM   5819  C  CE    . LYS A 1 2183 ? 204.021 254.630 260.824 1.00 17.30 ? 2183 LYS A CE    1 
ATOM   5820  N  NZ    . LYS A 1 2183 ? 204.975 255.400 259.983 1.00 22.55 ? 2183 LYS A NZ    1 
ATOM   5821  N  N     . LYS A 1 2184 ? 201.949 249.789 257.825 1.00 7.11  ? 2184 LYS A N     1 
ATOM   5822  C  CA    . LYS A 1 2184 ? 202.604 248.513 258.098 1.00 5.95  ? 2184 LYS A CA    1 
ATOM   5823  C  C     . LYS A 1 2184 ? 203.005 247.800 256.811 1.00 5.76  ? 2184 LYS A C     1 
ATOM   5824  O  O     . LYS A 1 2184 ? 204.088 247.209 256.736 1.00 8.59  ? 2184 LYS A O     1 
ATOM   5825  C  CB    . LYS A 1 2184 ? 201.691 247.624 258.942 1.00 6.95  ? 2184 LYS A CB    1 
ATOM   5826  C  CG    . LYS A 1 2184 ? 201.827 247.842 260.440 1.00 9.51  ? 2184 LYS A CG    1 
ATOM   5827  C  CD    . LYS A 1 2184 ? 200.478 247.785 261.140 1.00 14.16 ? 2184 LYS A CD    1 
ATOM   5828  C  CE    . LYS A 1 2184 ? 199.746 246.493 260.824 1.00 17.88 ? 2184 LYS A CE    1 
ATOM   5829  N  NZ    . LYS A 1 2184 ? 198.635 246.233 261.777 1.00 27.38 ? 2184 LYS A NZ    1 
ATOM   5830  N  N     . VAL A 1 2185 ? 202.143 247.836 255.792 1.00 5.20  ? 2185 VAL A N     1 
ATOM   5831  C  CA    . VAL A 1 2185 ? 202.464 247.181 254.527 1.00 2.99  ? 2185 VAL A CA    1 
ATOM   5832  C  C     . VAL A 1 2185 ? 203.655 247.860 253.862 1.00 3.45  ? 2185 VAL A C     1 
ATOM   5833  O  O     . VAL A 1 2185 ? 204.506 247.198 253.258 1.00 6.35  ? 2185 VAL A O     1 
ATOM   5834  C  CB    . VAL A 1 2185 ? 201.225 247.159 253.608 1.00 4.89  ? 2185 VAL A CB    1 
ATOM   5835  C  CG1   . VAL A 1 2185 ? 201.604 246.745 252.192 1.00 3.24  ? 2185 VAL A CG1   1 
ATOM   5836  C  CG2   . VAL A 1 2185 ? 200.175 246.217 254.164 1.00 3.14  ? 2185 VAL A CG2   1 
ATOM   5837  N  N     . CYS A 1 2186 ? 203.740 249.188 253.972 1.00 6.11  ? 2186 CYS A N     1 
ATOM   5838  C  CA    . CYS A 1 2186 ? 204.876 249.912 253.408 1.00 3.73  ? 2186 CYS A CA    1 
ATOM   5839  C  C     . CYS A 1 2186 ? 206.180 249.516 254.090 1.00 2.76  ? 2186 CYS A C     1 
ATOM   5840  O  O     . CYS A 1 2186 ? 207.215 249.377 253.428 1.00 4.17  ? 2186 CYS A O     1 
ATOM   5841  C  CB    . CYS A 1 2186 ? 204.647 251.418 253.520 1.00 3.23  ? 2186 CYS A CB    1 
ATOM   5842  S  SG    . CYS A 1 2186 ? 203.575 252.111 252.243 1.00 4.91  ? 2186 CYS A SG    1 
ATOM   5843  N  N     . GLN A 1 2187 ? 206.149 249.337 255.413 1.00 5.43  ? 2187 GLN A N     1 
ATOM   5844  C  CA    . GLN A 1 2187 ? 207.347 248.924 256.138 1.00 5.05  ? 2187 GLN A CA    1 
ATOM   5845  C  C     . GLN A 1 2187 ? 207.822 247.549 255.685 1.00 6.17  ? 2187 GLN A C     1 
ATOM   5846  O  O     . GLN A 1 2187 ? 209.028 247.315 255.542 1.00 9.63  ? 2187 GLN A O     1 
ATOM   5847  C  CB    . GLN A 1 2187 ? 207.071 248.928 257.640 1.00 3.81  ? 2187 GLN A CB    1 
ATOM   5848  C  CG    . GLN A 1 2187 ? 208.266 248.580 258.518 1.00 10.33 ? 2187 GLN A CG    1 
ATOM   5849  C  CD    . GLN A 1 2187 ? 209.412 249.563 258.385 1.00 17.08 ? 2187 GLN A CD    1 
ATOM   5850  O  OE1   . GLN A 1 2187 ? 210.425 249.272 257.750 1.00 12.83 ? 2187 GLN A OE1   1 
ATOM   5851  N  NE2   . GLN A 1 2187 ? 209.256 250.737 258.985 1.00 16.54 ? 2187 GLN A NE2   1 
ATOM   5852  N  N     . GLU A 1 2188 ? 206.889 246.624 255.456 1.00 5.25  ? 2188 GLU A N     1 
ATOM   5853  C  CA    . GLU A 1 2188 ? 207.270 245.283 255.028 1.00 6.95  ? 2188 GLU A CA    1 
ATOM   5854  C  C     . GLU A 1 2188 ? 207.725 245.268 253.573 1.00 4.34  ? 2188 GLU A C     1 
ATOM   5855  O  O     . GLU A 1 2188 ? 208.462 244.364 253.163 1.00 4.06  ? 2188 GLU A O     1 
ATOM   5856  C  CB    . GLU A 1 2188 ? 206.103 244.318 255.249 1.00 7.42  ? 2188 GLU A CB    1 
ATOM   5857  C  CG    . GLU A 1 2188 ? 206.386 242.867 254.883 1.00 14.22 ? 2188 GLU A CG    1 
ATOM   5858  C  CD    . GLU A 1 2188 ? 207.451 242.233 255.761 1.00 31.58 ? 2188 GLU A CD    1 
ATOM   5859  O  OE1   . GLU A 1 2188 ? 207.627 242.685 256.912 1.00 29.77 ? 2188 GLU A OE1   1 
ATOM   5860  O  OE2   . GLU A 1 2188 ? 208.115 241.281 255.297 1.00 26.99 ? 2188 GLU A OE2   1 
ATOM   5861  N  N     . MET A 1 2189 ? 207.320 246.265 252.789 1.00 5.71  ? 2189 MET A N     1 
ATOM   5862  C  CA    . MET A 1 2189 ? 207.690 246.366 251.385 1.00 3.93  ? 2189 MET A CA    1 
ATOM   5863  C  C     . MET A 1 2189 ? 208.778 247.403 251.134 1.00 2.41  ? 2189 MET A C     1 
ATOM   5864  O  O     . MET A 1 2189 ? 209.011 247.771 249.978 1.00 5.21  ? 2189 MET A O     1 
ATOM   5865  C  CB    . MET A 1 2189 ? 206.454 246.683 250.542 1.00 2.26  ? 2189 MET A CB    1 
ATOM   5866  C  CG    . MET A 1 2189 ? 205.541 245.489 250.329 1.00 2.49  ? 2189 MET A CG    1 
ATOM   5867  S  SD    . MET A 1 2189 ? 204.045 245.878 249.403 1.00 8.11  ? 2189 MET A SD    1 
ATOM   5868  C  CE    . MET A 1 2189 ? 204.681 245.945 247.732 1.00 4.97  ? 2189 MET A CE    1 
ATOM   5869  N  N     . TYR A 1 2190 ? 209.443 247.882 252.189 1.00 2.48  ? 2190 TYR A N     1 
ATOM   5870  C  CA    . TYR A 1 2190 ? 210.535 248.854 252.077 1.00 2.61  ? 2190 TYR A CA    1 
ATOM   5871  C  C     . TYR A 1 2190 ? 210.087 250.125 251.360 1.00 2.83  ? 2190 TYR A C     1 
ATOM   5872  O  O     . TYR A 1 2190 ? 210.846 250.732 250.601 1.00 2.38  ? 2190 TYR A O     1 
ATOM   5873  C  CB    . TYR A 1 2190 ? 211.754 248.242 251.381 1.00 2.39  ? 2190 TYR A CB    1 
ATOM   5874  C  CG    . TYR A 1 2190 ? 212.165 246.903 251.937 1.00 3.88  ? 2190 TYR A CG    1 
ATOM   5875  C  CD1   . TYR A 1 2190 ? 212.899 246.812 253.111 1.00 3.40  ? 2190 TYR A CD1   1 
ATOM   5876  C  CD2   . TYR A 1 2190 ? 211.812 245.727 251.290 1.00 2.78  ? 2190 TYR A CD2   1 
ATOM   5877  C  CE1   . TYR A 1 2190 ? 213.271 245.591 253.623 1.00 4.21  ? 2190 TYR A CE1   1 
ATOM   5878  C  CE2   . TYR A 1 2190 ? 212.181 244.499 251.796 1.00 4.37  ? 2190 TYR A CE2   1 
ATOM   5879  C  CZ    . TYR A 1 2190 ? 212.909 244.436 252.962 1.00 7.09  ? 2190 TYR A CZ    1 
ATOM   5880  O  OH    . TYR A 1 2190 ? 213.280 243.213 253.470 1.00 12.24 ? 2190 TYR A OH    1 
ATOM   5881  N  N     . LEU A 1 2191 ? 208.852 250.539 251.608 1.00 3.74  ? 2191 LEU A N     1 
ATOM   5882  C  CA    . LEU A 1 2191 ? 208.291 251.723 250.980 1.00 0.96  ? 2191 LEU A CA    1 
ATOM   5883  C  C     . LEU A 1 2191 ? 208.195 252.860 251.987 1.00 2.27  ? 2191 LEU A C     1 
ATOM   5884  O  O     . LEU A 1 2191 ? 208.192 252.650 253.203 1.00 7.52  ? 2191 LEU A O     1 
ATOM   5885  C  CB    . LEU A 1 2191 ? 206.913 251.431 250.383 1.00 1.14  ? 2191 LEU A CB    1 
ATOM   5886  C  CG    . LEU A 1 2191 ? 206.896 250.515 249.159 1.00 0.95  ? 2191 LEU A CG    1 
ATOM   5887  C  CD1   . LEU A 1 2191 ? 205.547 250.577 248.478 1.00 2.24  ? 2191 LEU A CD1   1 
ATOM   5888  C  CD2   . LEU A 1 2191 ? 208.005 250.874 248.187 1.00 0.50  ? 2191 LEU A CD2   1 
ATOM   5889  N  N     . THR A 1 2192 ? 208.124 254.076 251.459 1.00 2.35  ? 2192 THR A N     1 
ATOM   5890  C  CA    . THR A 1 2192 ? 208.030 255.272 252.280 1.00 3.05  ? 2192 THR A CA    1 
ATOM   5891  C  C     . THR A 1 2192 ? 206.569 255.663 252.447 1.00 3.02  ? 2192 THR A C     1 
ATOM   5892  O  O     . THR A 1 2192 ? 205.847 255.835 251.460 1.00 1.86  ? 2192 THR A O     1 
ATOM   5893  C  CB    . THR A 1 2192 ? 208.820 256.423 251.655 1.00 3.63  ? 2192 THR A CB    1 
ATOM   5894  O  OG1   . THR A 1 2192 ? 210.210 256.082 251.616 1.00 3.95  ? 2192 THR A OG1   1 
ATOM   5895  C  CG2   . THR A 1 2192 ? 208.635 257.694 252.464 1.00 2.55  ? 2192 THR A CG2   1 
ATOM   5896  N  N     . TYR A 1 2193 ? 206.139 255.796 253.697 1.00 6.46  ? 2193 TYR A N     1 
ATOM   5897  C  CA    . TYR A 1 2193 ? 204.787 256.214 254.030 1.00 3.34  ? 2193 TYR A CA    1 
ATOM   5898  C  C     . TYR A 1 2193 ? 204.836 257.609 254.636 1.00 4.13  ? 2193 TYR A C     1 
ATOM   5899  O  O     . TYR A 1 2193 ? 205.678 257.888 255.495 1.00 9.17  ? 2193 TYR A O     1 
ATOM   5900  C  CB    . TYR A 1 2193 ? 204.131 255.228 255.001 1.00 2.30  ? 2193 TYR A CB    1 
ATOM   5901  C  CG    . TYR A 1 2193 ? 202.769 255.663 255.496 1.00 4.63  ? 2193 TYR A CG    1 
ATOM   5902  C  CD1   . TYR A 1 2193 ? 202.641 256.459 256.627 1.00 6.43  ? 2193 TYR A CD1   1 
ATOM   5903  C  CD2   . TYR A 1 2193 ? 201.614 255.280 254.831 1.00 4.19  ? 2193 TYR A CD2   1 
ATOM   5904  C  CE1   . TYR A 1 2193 ? 201.407 256.861 257.077 1.00 5.08  ? 2193 TYR A CE1   1 
ATOM   5905  C  CE2   . TYR A 1 2193 ? 200.370 255.680 255.277 1.00 5.33  ? 2193 TYR A CE2   1 
ATOM   5906  C  CZ    . TYR A 1 2193 ? 200.275 256.470 256.402 1.00 8.80  ? 2193 TYR A CZ    1 
ATOM   5907  O  OH    . TYR A 1 2193 ? 199.044 256.873 256.855 1.00 16.73 ? 2193 TYR A OH    1 
ATOM   5908  N  N     . GLY A 1 2194 ? 203.930 258.480 254.186 1.00 4.57  ? 2194 GLY A N     1 
ATOM   5909  C  CA    . GLY A 1 2194 ? 203.835 259.820 254.718 1.00 4.76  ? 2194 GLY A CA    1 
ATOM   5910  C  C     . GLY A 1 2194 ? 202.387 260.193 254.981 1.00 8.77  ? 2194 GLY A C     1 
ATOM   5911  O  O     . GLY A 1 2194 ? 201.456 259.516 254.540 1.00 10.51 ? 2194 GLY A O     1 
ATOM   5912  N  N     . ASP A 1 2195 ? 202.217 261.292 255.713 1.00 15.66 ? 2195 ASP A N     1 
ATOM   5913  C  CA    . ASP A 1 2195 ? 200.899 261.811 256.065 1.00 11.01 ? 2195 ASP A CA    1 
ATOM   5914  C  C     . ASP A 1 2195 ? 200.893 263.310 255.809 1.00 12.34 ? 2195 ASP A C     1 
ATOM   5915  O  O     . ASP A 1 2195 ? 201.563 264.067 256.518 1.00 16.82 ? 2195 ASP A O     1 
ATOM   5916  C  CB    . ASP A 1 2195 ? 200.559 261.500 257.524 1.00 8.25  ? 2195 ASP A CB    1 
ATOM   5917  C  CG    . ASP A 1 2195 ? 199.855 260.171 257.688 1.00 18.56 ? 2195 ASP A CG    1 
ATOM   5918  O  OD1   . ASP A 1 2195 ? 199.515 259.544 256.662 1.00 18.53 ? 2195 ASP A OD1   1 
ATOM   5919  O  OD2   . ASP A 1 2195 ? 199.643 259.746 258.842 1.00 24.58 ? 2195 ASP A OD2   1 
ATOM   5920  N  N     . GLY A 1 2196 ? 200.142 263.737 254.798 1.00 11.23 ? 2196 GLY A N     1 
ATOM   5921  C  CA    . GLY A 1 2196 ? 200.050 265.146 254.470 1.00 12.41 ? 2196 GLY A CA    1 
ATOM   5922  C  C     . GLY A 1 2196 ? 201.190 265.642 253.606 1.00 17.87 ? 2196 GLY A C     1 
ATOM   5923  O  O     . GLY A 1 2196 ? 201.356 265.195 252.467 1.00 19.15 ? 2196 GLY A O     1 
ATOM   5924  N  N     . GLU A 1 2197 ? 201.978 266.573 254.135 1.00 14.76 ? 2197 GLU A N     1 
ATOM   5925  C  CA    . GLU A 1 2197 ? 203.096 267.154 253.404 1.00 14.53 ? 2197 GLU A CA    1 
ATOM   5926  C  C     . GLU A 1 2197 ? 204.414 266.440 253.673 1.00 15.10 ? 2197 GLU A C     1 
ATOM   5927  O  O     . GLU A 1 2197 ? 205.452 266.882 253.172 1.00 13.53 ? 2197 GLU A O     1 
ATOM   5928  C  CB    . GLU A 1 2197 ? 203.237 268.641 253.748 1.00 22.40 ? 2197 GLU A CB    1 
ATOM   5929  C  CG    . GLU A 1 2197 ? 201.958 269.437 253.581 1.00 19.86 ? 2197 GLU A CG    1 
ATOM   5930  C  CD    . GLU A 1 2197 ? 201.193 269.056 252.327 1.00 24.32 ? 2197 GLU A CD    1 
ATOM   5931  O  OE1   . GLU A 1 2197 ? 201.620 269.459 251.225 1.00 29.01 ? 2197 GLU A OE1   1 
ATOM   5932  O  OE2   . GLU A 1 2197 ? 200.168 268.352 252.444 1.00 31.31 ? 2197 GLU A OE2   1 
ATOM   5933  N  N     . GLU A 1 2198 ? 204.398 265.357 254.444 1.00 11.56 ? 2198 GLU A N     1 
ATOM   5934  C  CA    . GLU A 1 2198 ? 205.610 264.598 254.694 1.00 9.35  ? 2198 GLU A CA    1 
ATOM   5935  C  C     . GLU A 1 2198 ? 206.066 263.885 253.422 1.00 10.24 ? 2198 GLU A C     1 
ATOM   5936  O  O     . GLU A 1 2198 ? 205.378 263.875 252.397 1.00 9.47  ? 2198 GLU A O     1 
ATOM   5937  C  CB    . GLU A 1 2198 ? 205.386 263.583 255.815 1.00 8.30  ? 2198 GLU A CB    1 
ATOM   5938  C  CG    . GLU A 1 2198 ? 204.754 264.162 257.065 1.00 8.62  ? 2198 GLU A CG    1 
ATOM   5939  C  CD    . GLU A 1 2198 ? 204.251 263.087 258.010 1.00 20.11 ? 2198 GLU A CD    1 
ATOM   5940  O  OE1   . GLU A 1 2198 ? 204.573 261.901 257.789 1.00 17.01 ? 2198 GLU A OE1   1 
ATOM   5941  O  OE2   . GLU A 1 2198 ? 203.534 263.428 258.972 1.00 24.94 ? 2198 GLU A OE2   1 
ATOM   5942  N  N     . VAL A 1 2199 ? 207.254 263.289 253.497 1.00 10.21 ? 2199 VAL A N     1 
ATOM   5943  C  CA    . VAL A 1 2199 ? 207.761 262.500 252.382 1.00 5.10  ? 2199 VAL A CA    1 
ATOM   5944  C  C     . VAL A 1 2199 ? 206.851 261.298 252.187 1.00 4.05  ? 2199 VAL A C     1 
ATOM   5945  O  O     . VAL A 1 2199 ? 206.604 260.530 253.124 1.00 9.15  ? 2199 VAL A O     1 
ATOM   5946  C  CB    . VAL A 1 2199 ? 209.213 262.078 252.630 1.00 6.05  ? 2199 VAL A CB    1 
ATOM   5947  C  CG1   . VAL A 1 2199 ? 209.740 261.265 251.459 1.00 5.02  ? 2199 VAL A CG1   1 
ATOM   5948  C  CG2   . VAL A 1 2199 ? 210.085 263.296 252.872 1.00 4.85  ? 2199 VAL A CG2   1 
ATOM   5949  N  N     . GLY A 1 2200 ? 206.345 261.131 250.969 1.00 2.84  ? 2200 GLY A N     1 
ATOM   5950  C  CA    . GLY A 1 2200 ? 205.409 260.069 250.672 1.00 2.94  ? 2200 GLY A CA    1 
ATOM   5951  C  C     . GLY A 1 2200 ? 203.954 260.407 250.904 1.00 2.52  ? 2200 GLY A C     1 
ATOM   5952  O  O     . GLY A 1 2200 ? 203.090 259.574 250.602 1.00 1.74  ? 2200 GLY A O     1 
ATOM   5953  N  N     . GLY A 1 2201 ? 203.654 261.599 251.422 1.00 5.07  ? 2201 GLY A N     1 
ATOM   5954  C  CA    . GLY A 1 2201 ? 202.271 261.950 251.700 1.00 4.36  ? 2201 GLY A CA    1 
ATOM   5955  C  C     . GLY A 1 2201 ? 201.417 262.034 250.450 1.00 1.73  ? 2201 GLY A C     1 
ATOM   5956  O  O     . GLY A 1 2201 ? 200.261 261.605 250.447 1.00 1.12  ? 2201 GLY A O     1 
ATOM   5957  N  N     . MET A 1 2202 ? 201.969 262.594 249.372 1.00 2.99  ? 2202 MET A N     1 
ATOM   5958  C  CA    . MET A 1 2202 ? 201.228 262.671 248.118 1.00 1.24  ? 2202 MET A CA    1 
ATOM   5959  C  C     . MET A 1 2202 ? 200.902 261.282 247.588 1.00 1.11  ? 2202 MET A C     1 
ATOM   5960  O  O     . MET A 1 2202 ? 199.797 261.040 247.090 1.00 1.36  ? 2202 MET A O     1 
ATOM   5961  C  CB    . MET A 1 2202 ? 202.026 263.461 247.083 1.00 2.64  ? 2202 MET A CB    1 
ATOM   5962  C  CG    . MET A 1 2202 ? 202.026 264.962 247.298 1.00 4.47  ? 2202 MET A CG    1 
ATOM   5963  S  SD    . MET A 1 2202 ? 202.668 265.852 245.868 1.00 32.34 ? 2202 MET A SD    1 
ATOM   5964  C  CE    . MET A 1 2202 ? 204.409 265.929 246.268 1.00 13.18 ? 2202 MET A CE    1 
ATOM   5965  N  N     . TRP A 1 2203 ? 201.857 260.357 247.688 1.00 1.15  ? 2203 TRP A N     1 
ATOM   5966  C  CA    . TRP A 1 2203 ? 201.632 258.992 247.227 1.00 0.52  ? 2203 TRP A CA    1 
ATOM   5967  C  C     . TRP A 1 2203 ? 200.573 258.286 248.067 1.00 0.46  ? 2203 TRP A C     1 
ATOM   5968  O  O     . TRP A 1 2203 ? 199.751 257.537 247.532 1.00 0.56  ? 2203 TRP A O     1 
ATOM   5969  C  CB    . TRP A 1 2203 ? 202.953 258.226 247.243 1.00 0.58  ? 2203 TRP A CB    1 
ATOM   5970  C  CG    . TRP A 1 2203 ? 202.845 256.799 246.828 1.00 0.25  ? 2203 TRP A CG    1 
ATOM   5971  C  CD1   . TRP A 1 2203 ? 202.838 256.315 245.557 1.00 0.13  ? 2203 TRP A CD1   1 
ATOM   5972  C  CD2   . TRP A 1 2203 ? 202.747 255.663 247.692 1.00 0.11  ? 2203 TRP A CD2   1 
ATOM   5973  N  NE1   . TRP A 1 2203 ? 202.734 254.949 245.571 1.00 0.06  ? 2203 TRP A NE1   1 
ATOM   5974  C  CE2   . TRP A 1 2203 ? 202.677 254.523 246.873 1.00 0.08  ? 2203 TRP A CE2   1 
ATOM   5975  C  CE3   . TRP A 1 2203 ? 202.710 255.501 249.079 1.00 0.13  ? 2203 TRP A CE3   1 
ATOM   5976  C  CZ2   . TRP A 1 2203 ? 202.570 253.236 247.392 1.00 0.10  ? 2203 TRP A CZ2   1 
ATOM   5977  C  CZ3   . TRP A 1 2203 ? 202.604 254.226 249.593 1.00 0.35  ? 2203 TRP A CZ3   1 
ATOM   5978  C  CH2   . TRP A 1 2203 ? 202.536 253.109 248.752 1.00 0.97  ? 2203 TRP A CH2   1 
ATOM   5979  N  N     . VAL A 1 2204 ? 200.576 258.517 249.382 1.00 0.40  ? 2204 VAL A N     1 
ATOM   5980  C  CA    . VAL A 1 2204 ? 199.588 257.884 250.252 1.00 0.50  ? 2204 VAL A CA    1 
ATOM   5981  C  C     . VAL A 1 2204 ? 198.189 258.408 249.945 1.00 0.88  ? 2204 VAL A C     1 
ATOM   5982  O  O     . VAL A 1 2204 ? 197.207 257.658 249.996 1.00 0.81  ? 2204 VAL A O     1 
ATOM   5983  C  CB    . VAL A 1 2204 ? 199.970 258.092 251.729 1.00 1.08  ? 2204 VAL A CB    1 
ATOM   5984  C  CG1   . VAL A 1 2204 ? 198.845 257.643 252.650 1.00 1.94  ? 2204 VAL A CG1   1 
ATOM   5985  C  CG2   . VAL A 1 2204 ? 201.247 257.338 252.050 1.00 0.88  ? 2204 VAL A CG2   1 
ATOM   5986  N  N     . GLU A 1 2205 ? 198.075 259.696 249.614 1.00 1.18  ? 2205 GLU A N     1 
ATOM   5987  C  CA    . GLU A 1 2205 ? 196.785 260.237 249.198 1.00 0.82  ? 2205 GLU A CA    1 
ATOM   5988  C  C     . GLU A 1 2205 ? 196.280 259.549 247.936 1.00 1.17  ? 2205 GLU A C     1 
ATOM   5989  O  O     . GLU A 1 2205 ? 195.082 259.275 247.807 1.00 1.52  ? 2205 GLU A O     1 
ATOM   5990  C  CB    . GLU A 1 2205 ? 196.890 261.747 248.979 1.00 1.39  ? 2205 GLU A CB    1 
ATOM   5991  C  CG    . GLU A 1 2205 ? 197.167 262.551 250.239 1.00 7.33  ? 2205 GLU A CG    1 
ATOM   5992  C  CD    . GLU A 1 2205 ? 196.018 262.508 251.228 1.00 17.92 ? 2205 GLU A CD    1 
ATOM   5993  O  OE1   . GLU A 1 2205 ? 194.853 262.412 250.788 1.00 15.45 ? 2205 GLU A OE1   1 
ATOM   5994  O  OE2   . GLU A 1 2205 ? 196.280 262.573 252.446 1.00 22.07 ? 2205 GLU A OE2   1 
ATOM   5995  N  N     . LYS A 1 2206 ? 197.180 259.261 246.991 1.00 0.84  ? 2206 LYS A N     1 
ATOM   5996  C  CA    . LYS A 1 2206 ? 196.771 258.576 245.770 1.00 0.38  ? 2206 LYS A CA    1 
ATOM   5997  C  C     . LYS A 1 2206 ? 196.325 257.147 246.055 1.00 0.35  ? 2206 LYS A C     1 
ATOM   5998  O  O     . LYS A 1 2206 ? 195.414 256.636 245.396 1.00 1.51  ? 2206 LYS A O     1 
ATOM   5999  C  CB    . LYS A 1 2206 ? 197.907 258.599 244.749 1.00 0.41  ? 2206 LYS A CB    1 
ATOM   6000  C  CG    . LYS A 1 2206 ? 198.090 259.951 244.085 1.00 0.53  ? 2206 LYS A CG    1 
ATOM   6001  C  CD    . LYS A 1 2206 ? 196.820 260.370 243.373 1.00 0.82  ? 2206 LYS A CD    1 
ATOM   6002  C  CE    . LYS A 1 2206 ? 196.867 261.821 242.948 1.00 0.27  ? 2206 LYS A CE    1 
ATOM   6003  N  NZ    . LYS A 1 2206 ? 195.695 262.176 242.113 1.00 0.13  ? 2206 LYS A NZ    1 
ATOM   6004  N  N     . VAL A 1 2207 ? 196.958 256.485 247.023 1.00 0.50  ? 2207 VAL A N     1 
ATOM   6005  C  CA    . VAL A 1 2207 ? 196.504 255.158 247.428 1.00 0.41  ? 2207 VAL A CA    1 
ATOM   6006  C  C     . VAL A 1 2207 ? 195.101 255.235 248.015 1.00 0.48  ? 2207 VAL A C     1 
ATOM   6007  O  O     . VAL A 1 2207 ? 194.238 254.405 247.708 1.00 0.45  ? 2207 VAL A O     1 
ATOM   6008  C  CB    . VAL A 1 2207 ? 197.501 254.526 248.418 1.00 0.37  ? 2207 VAL A CB    1 
ATOM   6009  C  CG1   . VAL A 1 2207 ? 197.018 253.158 248.861 1.00 0.27  ? 2207 VAL A CG1   1 
ATOM   6010  C  CG2   . VAL A 1 2207 ? 198.885 254.431 247.798 1.00 0.16  ? 2207 VAL A CG2   1 
ATOM   6011  N  N     . LEU A 1 2208 ? 194.851 256.231 248.866 1.00 0.62  ? 2208 LEU A N     1 
ATOM   6012  C  CA    . LEU A 1 2208 ? 193.522 256.404 249.444 1.00 0.53  ? 2208 LEU A CA    1 
ATOM   6013  C  C     . LEU A 1 2208 ? 192.500 256.795 248.385 1.00 0.31  ? 2208 LEU A C     1 
ATOM   6014  O  O     . LEU A 1 2208 ? 191.357 256.330 248.420 1.00 0.91  ? 2208 LEU A O     1 
ATOM   6015  C  CB    . LEU A 1 2208 ? 193.574 257.448 250.558 1.00 0.94  ? 2208 LEU A CB    1 
ATOM   6016  C  CG    . LEU A 1 2208 ? 194.474 257.086 251.738 1.00 1.25  ? 2208 LEU A CG    1 
ATOM   6017  C  CD1   . LEU A 1 2208 ? 194.594 258.253 252.693 1.00 1.85  ? 2208 LEU A CD1   1 
ATOM   6018  C  CD2   . LEU A 1 2208 ? 193.943 255.860 252.455 1.00 1.74  ? 2208 LEU A CD2   1 
ATOM   6019  N  N     . GLN A 1 2209 ? 192.888 257.656 247.442 1.00 0.34  ? 2209 GLN A N     1 
ATOM   6020  C  CA    . GLN A 1 2209 ? 191.990 258.007 246.346 1.00 0.37  ? 2209 GLN A CA    1 
ATOM   6021  C  C     . GLN A 1 2209 ? 191.668 256.789 245.493 1.00 0.41  ? 2209 GLN A C     1 
ATOM   6022  O  O     . GLN A 1 2209 ? 190.526 256.611 245.054 1.00 0.46  ? 2209 GLN A O     1 
ATOM   6023  C  CB    . GLN A 1 2209 ? 192.610 259.107 245.487 1.00 0.34  ? 2209 GLN A CB    1 
ATOM   6024  C  CG    . GLN A 1 2209 ? 192.666 260.470 246.147 1.00 0.32  ? 2209 GLN A CG    1 
ATOM   6025  C  CD    . GLN A 1 2209 ? 193.322 261.511 245.264 1.00 0.53  ? 2209 GLN A CD    1 
ATOM   6026  O  OE1   . GLN A 1 2209 ? 193.725 261.220 244.142 1.00 0.80  ? 2209 GLN A OE1   1 
ATOM   6027  N  NE2   . GLN A 1 2209 ? 193.435 262.731 245.771 1.00 1.31  ? 2209 GLN A NE2   1 
ATOM   6028  N  N     . LEU A 1 2210 ? 192.666 255.936 245.249 1.00 0.55  ? 2210 LEU A N     1 
ATOM   6029  C  CA    . LEU A 1 2210 ? 192.434 254.713 244.491 1.00 0.25  ? 2210 LEU A CA    1 
ATOM   6030  C  C     . LEU A 1 2210 ? 191.444 253.801 245.205 1.00 0.42  ? 2210 LEU A C     1 
ATOM   6031  O  O     . LEU A 1 2210 ? 190.613 253.152 244.561 1.00 0.47  ? 2210 LEU A O     1 
ATOM   6032  C  CB    . LEU A 1 2210 ? 193.764 253.998 244.253 1.00 0.24  ? 2210 LEU A CB    1 
ATOM   6033  C  CG    . LEU A 1 2210 ? 193.727 252.608 243.625 1.00 0.25  ? 2210 LEU A CG    1 
ATOM   6034  C  CD1   . LEU A 1 2210 ? 193.330 252.696 242.163 1.00 0.17  ? 2210 LEU A CD1   1 
ATOM   6035  C  CD2   . LEU A 1 2210 ? 195.074 251.926 243.784 1.00 0.04  ? 2210 LEU A CD2   1 
ATOM   6036  N  N     . TYR A 1 2211 ? 191.520 253.736 246.537 1.00 0.51  ? 2211 TYR A N     1 
ATOM   6037  C  CA    . TYR A 1 2211 ? 190.569 252.933 247.297 1.00 0.43  ? 2211 TYR A CA    1 
ATOM   6038  C  C     . TYR A 1 2211 ? 189.150 253.463 247.139 1.00 1.15  ? 2211 TYR A C     1 
ATOM   6039  O  O     . TYR A 1 2211 ? 188.200 252.684 247.019 1.00 2.06  ? 2211 TYR A O     1 
ATOM   6040  C  CB    . TYR A 1 2211 ? 190.962 252.900 248.773 1.00 0.48  ? 2211 TYR A CB    1 
ATOM   6041  C  CG    . TYR A 1 2211 ? 189.989 252.130 249.637 1.00 2.19  ? 2211 TYR A CG    1 
ATOM   6042  C  CD1   . TYR A 1 2211 ? 189.427 252.703 250.769 1.00 3.54  ? 2211 TYR A CD1   1 
ATOM   6043  C  CD2   . TYR A 1 2211 ? 189.633 250.826 249.318 1.00 2.44  ? 2211 TYR A CD2   1 
ATOM   6044  C  CE1   . TYR A 1 2211 ? 188.541 251.999 251.556 1.00 5.61  ? 2211 TYR A CE1   1 
ATOM   6045  C  CE2   . TYR A 1 2211 ? 188.747 250.119 250.098 1.00 4.05  ? 2211 TYR A CE2   1 
ATOM   6046  C  CZ    . TYR A 1 2211 ? 188.206 250.707 251.216 1.00 7.52  ? 2211 TYR A CZ    1 
ATOM   6047  O  OH    . TYR A 1 2211 ? 187.323 249.999 251.995 1.00 12.72 ? 2211 TYR A OH    1 
ATOM   6048  N  N     . GLN A 1 2212 ? 188.990 254.787 247.149 1.00 2.08  ? 2212 GLN A N     1 
ATOM   6049  C  CA    . GLN A 1 2212 ? 187.663 255.371 246.984 1.00 1.82  ? 2212 GLN A CA    1 
ATOM   6050  C  C     . GLN A 1 2212 ? 187.076 255.021 245.623 1.00 2.18  ? 2212 GLN A C     1 
ATOM   6051  O  O     . GLN A 1 2212 ? 185.880 254.733 245.512 1.00 6.82  ? 2212 GLN A O     1 
ATOM   6052  C  CB    . GLN A 1 2212 ? 187.731 256.885 247.167 1.00 4.65  ? 2212 GLN A CB    1 
ATOM   6053  C  CG    . GLN A 1 2212 ? 188.155 257.330 248.556 1.00 7.60  ? 2212 GLN A CG    1 
ATOM   6054  C  CD    . GLN A 1 2212 ? 187.147 256.971 249.626 1.00 19.68 ? 2212 GLN A CD    1 
ATOM   6055  O  OE1   . GLN A 1 2212 ? 185.938 257.052 249.410 1.00 13.60 ? 2212 GLN A OE1   1 
ATOM   6056  N  NE2   . GLN A 1 2212 ? 187.639 256.571 250.794 1.00 27.07 ? 2212 GLN A NE2   1 
ATOM   6057  N  N     . ILE A 1 2213 ? 187.905 255.036 244.577 1.00 1.13  ? 2213 ILE A N     1 
ATOM   6058  C  CA    . ILE A 1 2213 ? 187.429 254.701 243.239 1.00 1.44  ? 2213 ILE A CA    1 
ATOM   6059  C  C     . ILE A 1 2213 ? 187.032 253.231 243.162 1.00 1.99  ? 2213 ILE A C     1 
ATOM   6060  O  O     . ILE A 1 2213 ? 186.077 252.872 242.464 1.00 2.03  ? 2213 ILE A O     1 
ATOM   6061  C  CB    . ILE A 1 2213 ? 188.497 255.066 242.191 1.00 2.33  ? 2213 ILE A CB    1 
ATOM   6062  C  CG1   . ILE A 1 2213 ? 188.842 256.553 242.286 1.00 1.38  ? 2213 ILE A CG1   1 
ATOM   6063  C  CG2   . ILE A 1 2213 ? 188.019 254.726 240.790 1.00 1.55  ? 2213 ILE A CG2   1 
ATOM   6064  C  CD1   . ILE A 1 2213 ? 187.736 257.470 241.815 1.00 1.20  ? 2213 ILE A CD1   1 
ATOM   6065  N  N     . THR A 1 2214 ? 187.746 252.357 243.878 1.00 1.42  ? 2214 THR A N     1 
ATOM   6066  C  CA    . THR A 1 2214 ? 187.398 250.939 243.881 1.00 2.18  ? 2214 THR A CA    1 
ATOM   6067  C  C     . THR A 1 2214 ? 186.020 250.685 244.473 1.00 2.24  ? 2214 THR A C     1 
ATOM   6068  O  O     . THR A 1 2214 ? 185.399 249.667 244.152 1.00 4.84  ? 2214 THR A O     1 
ATOM   6069  C  CB    . THR A 1 2214 ? 188.431 250.120 244.660 1.00 0.97  ? 2214 THR A CB    1 
ATOM   6070  O  OG1   . THR A 1 2214 ? 188.633 250.700 245.955 1.00 6.74  ? 2214 THR A OG1   1 
ATOM   6071  C  CG2   . THR A 1 2214 ? 189.745 250.077 243.927 1.00 0.41  ? 2214 THR A CG2   1 
ATOM   6072  N  N     . GLN A 1 2215 ? 185.536 251.576 245.333 1.00 2.26  ? 2215 GLN A N     1 
ATOM   6073  C  CA    . GLN A 1 2215 ? 184.235 251.414 245.968 1.00 2.87  ? 2215 GLN A CA    1 
ATOM   6074  C  C     . GLN A 1 2215 ? 183.095 252.021 245.163 1.00 4.36  ? 2215 GLN A C     1 
ATOM   6075  O  O     . GLN A 1 2215 ? 181.932 251.833 245.534 1.00 10.99 ? 2215 GLN A O     1 
ATOM   6076  C  CB    . GLN A 1 2215 ? 184.257 252.036 247.368 1.00 2.53  ? 2215 GLN A CB    1 
ATOM   6077  C  CG    . GLN A 1 2215 ? 185.271 251.403 248.307 1.00 3.66  ? 2215 GLN A CG    1 
ATOM   6078  C  CD    . GLN A 1 2215 ? 185.526 252.243 249.542 1.00 8.07  ? 2215 GLN A CD    1 
ATOM   6079  O  OE1   . GLN A 1 2215 ? 186.041 253.356 249.455 1.00 16.96 ? 2215 GLN A OE1   1 
ATOM   6080  N  NE2   . GLN A 1 2215 ? 185.167 251.710 250.703 1.00 8.39  ? 2215 GLN A NE2   1 
ATOM   6081  N  N     . ILE A 1 2216 ? 183.393 252.738 244.081 1.00 3.89  ? 2216 ILE A N     1 
ATOM   6082  C  CA    . ILE A 1 2216 ? 182.364 253.406 243.292 1.00 3.94  ? 2216 ILE A CA    1 
ATOM   6083  C  C     . ILE A 1 2216 ? 182.337 252.831 241.882 1.00 3.33  ? 2216 ILE A C     1 
ATOM   6084  O  O     . ILE A 1 2216 ? 181.279 252.763 241.247 1.00 7.84  ? 2216 ILE A O     1 
ATOM   6085  C  CB    . ILE A 1 2216 ? 182.602 254.928 243.266 1.00 4.59  ? 2216 ILE A CB    1 
ATOM   6086  C  CG1   . ILE A 1 2216 ? 182.593 255.491 244.686 1.00 6.15  ? 2216 ILE A CG1   1 
ATOM   6087  C  CG2   . ILE A 1 2216 ? 181.559 255.628 242.413 1.00 10.78 ? 2216 ILE A CG2   1 
ATOM   6088  C  CD1   . ILE A 1 2216 ? 181.288 255.287 245.412 1.00 7.56  ? 2216 ILE A CD1   1 
ATOM   6089  N  N     . ASN A 1 2217 ? 183.491 252.390 241.393 1.00 1.90  ? 2217 ASN A N     1 
ATOM   6090  C  CA    . ASN A 1 2217 ? 183.628 251.900 240.029 1.00 1.83  ? 2217 ASN A CA    1 
ATOM   6091  C  C     . ASN A 1 2217 ? 184.099 250.457 240.036 1.00 1.28  ? 2217 ASN A C     1 
ATOM   6092  O  O     . ASN A 1 2217 ? 184.913 250.062 240.876 1.00 7.05  ? 2217 ASN A O     1 
ATOM   6093  C  CB    . ASN A 1 2217 ? 184.616 252.754 239.220 1.00 1.18  ? 2217 ASN A CB    1 
ATOM   6094  C  CG    . ASN A 1 2217 ? 184.377 254.241 239.384 1.00 1.52  ? 2217 ASN A CG    1 
ATOM   6095  O  OD1   . ASN A 1 2217 ? 184.499 254.786 240.480 1.00 6.31  ? 2217 ASN A OD1   1 
ATOM   6096  N  ND2   . ASN A 1 2217 ? 184.034 254.906 238.290 1.00 1.66  ? 2217 ASN A ND2   1 
ATOM   6097  N  N     . HIS A 1 2218 ? 183.572 249.665 239.105 1.00 0.57  ? 2218 HIS A N     1 
ATOM   6098  C  CA    . HIS A 1 2218 ? 184.111 248.337 238.854 1.00 0.43  ? 2218 HIS A CA    1 
ATOM   6099  C  C     . HIS A 1 2218 ? 185.215 248.349 237.805 1.00 0.28  ? 2218 HIS A C     1 
ATOM   6100  O  O     . HIS A 1 2218 ? 185.921 247.346 237.655 1.00 0.16  ? 2218 HIS A O     1 
ATOM   6101  C  CB    . HIS A 1 2218 ? 182.994 247.380 238.427 1.00 0.27  ? 2218 HIS A CB    1 
ATOM   6102  C  CG    . HIS A 1 2218 ? 182.288 247.791 237.175 1.00 0.37  ? 2218 HIS A CG    1 
ATOM   6103  N  ND1   . HIS A 1 2218 ? 181.157 248.577 237.184 1.00 0.60  ? 2218 HIS A ND1   1 
ATOM   6104  C  CD2   . HIS A 1 2218 ? 182.549 247.525 235.875 1.00 0.49  ? 2218 HIS A CD2   1 
ATOM   6105  C  CE1   . HIS A 1 2218 ? 180.754 248.780 235.943 1.00 0.59  ? 2218 HIS A CE1   1 
ATOM   6106  N  NE2   . HIS A 1 2218 ? 181.582 248.150 235.129 1.00 0.53  ? 2218 HIS A NE2   1 
ATOM   6107  N  N     . GLY A 1 2219 ? 185.378 249.459 237.090 1.00 0.27  ? 2219 GLY A N     1 
ATOM   6108  C  CA    . GLY A 1 2219 ? 186.470 249.644 236.157 1.00 0.15  ? 2219 GLY A CA    1 
ATOM   6109  C  C     . GLY A 1 2219 ? 187.162 250.974 236.379 1.00 0.26  ? 2219 GLY A C     1 
ATOM   6110  O  O     . GLY A 1 2219 ? 186.503 252.014 236.444 1.00 0.54  ? 2219 GLY A O     1 
ATOM   6111  N  N     . LEU A 1 2220 ? 188.486 250.959 236.506 1.00 0.17  ? 2220 LEU A N     1 
ATOM   6112  C  CA    . LEU A 1 2220 ? 189.233 252.165 236.826 1.00 0.12  ? 2220 LEU A CA    1 
ATOM   6113  C  C     . LEU A 1 2220 ? 190.601 252.131 236.163 1.00 0.10  ? 2220 LEU A C     1 
ATOM   6114  O  O     . LEU A 1 2220 ? 191.163 251.064 235.914 1.00 0.08  ? 2220 LEU A O     1 
ATOM   6115  C  CB    . LEU A 1 2220 ? 189.369 252.339 238.346 1.00 0.29  ? 2220 LEU A CB    1 
ATOM   6116  C  CG    . LEU A 1 2220 ? 190.095 251.279 239.182 1.00 0.21  ? 2220 LEU A CG    1 
ATOM   6117  C  CD1   . LEU A 1 2220 ? 191.614 251.417 239.158 1.00 0.14  ? 2220 LEU A CD1   1 
ATOM   6118  C  CD2   . LEU A 1 2220 ? 189.578 251.320 240.603 1.00 1.35  ? 2220 LEU A CD2   1 
ATOM   6119  N  N     . MET A 1 2221 ? 191.137 253.319 235.891 1.00 0.26  ? 2221 MET A N     1 
ATOM   6120  C  CA    . MET A 1 2221 ? 192.464 253.462 235.309 1.00 0.05  ? 2221 MET A CA    1 
ATOM   6121  C  C     . MET A 1 2221 ? 193.356 254.266 236.238 1.00 0.04  ? 2221 MET A C     1 
ATOM   6122  O  O     . MET A 1 2221 ? 192.931 255.288 236.786 1.00 0.05  ? 2221 MET A O     1 
ATOM   6123  C  CB    . MET A 1 2221 ? 192.416 254.119 233.928 1.00 0.08  ? 2221 MET A CB    1 
ATOM   6124  C  CG    . MET A 1 2221 ? 191.760 253.262 232.887 1.00 0.18  ? 2221 MET A CG    1 
ATOM   6125  S  SD    . MET A 1 2221 ? 191.684 253.991 231.250 1.00 26.23 ? 2221 MET A SD    1 
ATOM   6126  C  CE    . MET A 1 2221 ? 190.780 252.701 230.408 1.00 2.54  ? 2221 MET A CE    1 
ATOM   6127  N  N     . MET A 1 2222 ? 194.585 253.793 236.412 1.00 0.07  ? 2222 MET A N     1 
ATOM   6128  C  CA    . MET A 1 2222 ? 195.652 254.556 237.046 1.00 0.02  ? 2222 MET A CA    1 
ATOM   6129  C  C     . MET A 1 2222 ? 196.552 255.077 235.935 1.00 0.02  ? 2222 MET A C     1 
ATOM   6130  O  O     . MET A 1 2222 ? 197.236 254.299 235.265 1.00 0.04  ? 2222 MET A O     1 
ATOM   6131  C  CB    . MET A 1 2222 ? 196.422 253.677 238.027 1.00 0.03  ? 2222 MET A CB    1 
ATOM   6132  C  CG    . MET A 1 2222 ? 195.571 253.128 239.148 1.00 0.05  ? 2222 MET A CG    1 
ATOM   6133  S  SD    . MET A 1 2222 ? 196.390 251.836 240.092 1.00 0.09  ? 2222 MET A SD    1 
ATOM   6134  C  CE    . MET A 1 2222 ? 195.865 250.395 239.167 1.00 0.03  ? 2222 MET A CE    1 
ATOM   6135  N  N     . VAL A 1 2223 ? 196.539 256.389 235.725 1.00 0.03  ? 2223 VAL A N     1 
ATOM   6136  C  CA    . VAL A 1 2223 ? 197.238 257.017 234.613 1.00 0.03  ? 2223 VAL A CA    1 
ATOM   6137  C  C     . VAL A 1 2223 ? 198.348 257.896 235.166 1.00 0.04  ? 2223 VAL A C     1 
ATOM   6138  O  O     . VAL A 1 2223 ? 198.110 258.725 236.051 1.00 0.09  ? 2223 VAL A O     1 
ATOM   6139  C  CB    . VAL A 1 2223 ? 196.277 257.837 233.736 1.00 0.03  ? 2223 VAL A CB    1 
ATOM   6140  C  CG1   . VAL A 1 2223 ? 196.997 258.342 232.498 1.00 0.07  ? 2223 VAL A CG1   1 
ATOM   6141  C  CG2   . VAL A 1 2223 ? 195.060 257.007 233.363 1.00 0.05  ? 2223 VAL A CG2   1 
ATOM   6142  N  N     . GLY A 1 2224 ? 199.555 257.717 234.645 1.00 0.06  ? 2224 GLY A N     1 
ATOM   6143  C  CA    . GLY A 1 2224 ? 200.679 258.523 235.045 1.00 0.10  ? 2224 GLY A CA    1 
ATOM   6144  C  C     . GLY A 1 2224 ? 201.963 258.105 234.368 1.00 0.18  ? 2224 GLY A C     1 
ATOM   6145  O  O     . GLY A 1 2224 ? 202.109 256.967 233.917 1.00 0.22  ? 2224 GLY A O     1 
ATOM   6146  N  N     . PRO A 1 2225 ? 202.933 259.016 234.306 1.00 0.55  ? 2225 PRO A N     1 
ATOM   6147  C  CA    . PRO A 1 2225 ? 204.201 258.705 233.639 1.00 0.21  ? 2225 PRO A CA    1 
ATOM   6148  C  C     . PRO A 1 2225 ? 204.899 257.526 234.296 1.00 0.30  ? 2225 PRO A C     1 
ATOM   6149  O  O     . PRO A 1 2225 ? 204.650 257.184 235.452 1.00 0.43  ? 2225 PRO A O     1 
ATOM   6150  C  CB    . PRO A 1 2225 ? 205.016 259.994 233.806 1.00 0.52  ? 2225 PRO A CB    1 
ATOM   6151  C  CG    . PRO A 1 2225 ? 204.001 261.055 234.045 1.00 0.46  ? 2225 PRO A CG    1 
ATOM   6152  C  CD    . PRO A 1 2225 ? 202.900 260.398 234.810 1.00 0.20  ? 2225 PRO A CD    1 
ATOM   6153  N  N     . SER A 1 2226 ? 205.783 256.893 233.529 1.00 0.48  ? 2226 SER A N     1 
ATOM   6154  C  CA    . SER A 1 2226 ? 206.501 255.730 234.027 1.00 0.26  ? 2226 SER A CA    1 
ATOM   6155  C  C     . SER A 1 2226 ? 207.320 256.108 235.254 1.00 0.38  ? 2226 SER A C     1 
ATOM   6156  O  O     . SER A 1 2226 ? 208.112 257.056 235.221 1.00 1.35  ? 2226 SER A O     1 
ATOM   6157  C  CB    . SER A 1 2226 ? 207.398 255.154 232.932 1.00 0.45  ? 2226 SER A CB    1 
ATOM   6158  O  OG    . SER A 1 2226 ? 208.277 254.174 233.453 1.00 0.45  ? 2226 SER A OG    1 
ATOM   6159  N  N     . GLY A 1 2227 ? 207.117 255.374 236.343 1.00 0.15  ? 2227 GLY A N     1 
ATOM   6160  C  CA    . GLY A 1 2227 ? 207.796 255.663 237.588 1.00 0.17  ? 2227 GLY A CA    1 
ATOM   6161  C  C     . GLY A 1 2227 ? 207.074 256.683 238.443 1.00 0.54  ? 2227 GLY A C     1 
ATOM   6162  O  O     . GLY A 1 2227 ? 207.702 257.558 239.042 1.00 1.46  ? 2227 GLY A O     1 
ATOM   6163  N  N     . SER A 1 2228 ? 205.748 256.582 238.499 1.00 1.05  ? 2228 SER A N     1 
ATOM   6164  C  CA    . SER A 1 2228 ? 204.925 257.474 239.306 1.00 0.65  ? 2228 SER A CA    1 
ATOM   6165  C  C     . SER A 1 2228 ? 204.364 256.785 240.541 1.00 0.33  ? 2228 SER A C     1 
ATOM   6166  O  O     . SER A 1 2228 ? 203.604 257.402 241.292 1.00 0.42  ? 2228 SER A O     1 
ATOM   6167  C  CB    . SER A 1 2228 ? 203.785 258.045 238.463 1.00 0.37  ? 2228 SER A CB    1 
ATOM   6168  O  OG    . SER A 1 2228 ? 204.284 258.848 237.412 1.00 1.93  ? 2228 SER A OG    1 
ATOM   6169  N  N     . GLY A 1 2229 ? 204.717 255.523 240.765 1.00 0.06  ? 2229 GLY A N     1 
ATOM   6170  C  CA    . GLY A 1 2229 ? 204.203 254.796 241.904 1.00 0.04  ? 2229 GLY A CA    1 
ATOM   6171  C  C     . GLY A 1 2229 ? 202.842 254.178 241.710 1.00 0.05  ? 2229 GLY A C     1 
ATOM   6172  O  O     . GLY A 1 2229 ? 202.170 253.876 242.697 1.00 0.03  ? 2229 GLY A O     1 
ATOM   6173  N  N     . LYS A 1 2230 ? 202.418 254.038 240.460 1.00 0.01  ? 2230 LYS A N     1 
ATOM   6174  C  CA    . LYS A 1 2230 ? 201.070 253.485 240.178 1.00 0.05  ? 2230 LYS A CA    1 
ATOM   6175  C  C     . LYS A 1 2230 ? 201.027 252.016 240.635 1.00 0.02  ? 2230 LYS A C     1 
ATOM   6176  O  O     . LYS A 1 2230 ? 200.081 251.659 241.364 1.00 0.03  ? 2230 LYS A O     1 
ATOM   6177  C  CB    . LYS A 1 2230 ? 200.722 253.674 238.697 1.00 0.00  ? 2230 LYS A CB    1 
ATOM   6178  C  CG    . LYS A 1 2230 ? 200.880 255.071 238.133 1.00 0.04  ? 2230 LYS A CG    1 
ATOM   6179  C  CD    . LYS A 1 2230 ? 200.496 255.141 236.661 1.00 0.02  ? 2230 LYS A CD    1 
ATOM   6180  C  CE    . LYS A 1 2230 ? 201.285 254.197 235.808 1.00 0.02  ? 2230 LYS A CE    1 
ATOM   6181  N  NZ    . LYS A 1 2230 ? 202.722 254.475 235.848 1.00 0.02  ? 2230 LYS A NZ    1 
ATOM   6182  N  N     . SER A 1 2231 ? 202.015 251.207 240.249 1.00 0.03  ? 2231 SER A N     1 
ATOM   6183  C  CA    . SER A 1 2231 ? 202.003 249.755 240.586 1.00 0.03  ? 2231 SER A CA    1 
ATOM   6184  C  C     . SER A 1 2231 ? 202.032 249.556 242.105 1.00 0.05  ? 2231 SER A C     1 
ATOM   6185  O  O     . SER A 1 2231 ? 201.207 248.767 242.614 1.00 0.12  ? 2231 SER A O     1 
ATOM   6186  C  CB    . SER A 1 2231 ? 203.146 249.022 239.928 1.00 0.02  ? 2231 SER A CB    1 
ATOM   6187  O  OG    . SER A 1 2231 ? 203.013 249.008 238.517 1.00 0.08  ? 2231 SER A OG    1 
ATOM   6188  N  N     . MET A 1 2232 ? 202.936 250.246 242.794 1.00 0.04  ? 2232 MET A N     1 
ATOM   6189  C  CA    . MET A 1 2232 ? 203.074 250.084 244.262 1.00 0.04  ? 2232 MET A CA    1 
ATOM   6190  C  C     . MET A 1 2232 ? 201.792 250.573 244.949 1.00 0.05  ? 2232 MET A C     1 
ATOM   6191  O  O     . MET A 1 2232 ? 201.456 250.017 246.011 1.00 0.13  ? 2232 MET A O     1 
ATOM   6192  C  CB    . MET A 1 2232 ? 204.307 250.832 244.784 1.00 0.12  ? 2232 MET A CB    1 
ATOM   6193  C  CG    . MET A 1 2232 ? 205.630 250.237 244.342 1.00 0.11  ? 2232 MET A CG    1 
ATOM   6194  S  SD    . MET A 1 2232 ? 205.780 248.492 244.774 1.00 13.92 ? 2232 MET A SD    1 
ATOM   6195  C  CE    . MET A 1 2232 ? 207.528 248.224 244.450 1.00 6.08  ? 2232 MET A CE    1 
ATOM   6196  N  N     . ALA A 1 2233 ? 201.094 251.546 244.350 1.00 0.05  ? 2233 ALA A N     1 
ATOM   6197  C  CA    . ALA A 1 2233 ? 199.877 252.078 244.952 1.00 0.04  ? 2233 ALA A CA    1 
ATOM   6198  C  C     . ALA A 1 2233 ? 198.791 251.015 245.055 1.00 0.09  ? 2233 ALA A C     1 
ATOM   6199  O  O     . ALA A 1 2233 ? 198.110 250.916 246.082 1.00 1.04  ? 2233 ALA A O     1 
ATOM   6200  C  CB    . ALA A 1 2233 ? 199.375 253.280 244.156 1.00 0.05  ? 2233 ALA A CB    1 
ATOM   6201  N  N     . TRP A 1 2234 ? 198.610 250.212 244.009 1.00 0.04  ? 2234 TRP A N     1 
ATOM   6202  C  CA    . TRP A 1 2234 ? 197.579 249.183 244.055 1.00 0.06  ? 2234 TRP A CA    1 
ATOM   6203  C  C     . TRP A 1 2234 ? 198.078 247.866 244.628 1.00 0.23  ? 2234 TRP A C     1 
ATOM   6204  O  O     . TRP A 1 2234 ? 197.266 247.090 245.144 1.00 3.72  ? 2234 TRP A O     1 
ATOM   6205  C  CB    . TRP A 1 2234 ? 196.963 248.962 242.664 1.00 0.04  ? 2234 TRP A CB    1 
ATOM   6206  C  CG    . TRP A 1 2234 ? 197.826 248.265 241.640 1.00 0.04  ? 2234 TRP A CG    1 
ATOM   6207  C  CD1   . TRP A 1 2234 ? 198.472 248.845 240.593 1.00 0.02  ? 2234 TRP A CD1   1 
ATOM   6208  C  CD2   . TRP A 1 2234 ? 198.091 246.860 241.542 1.00 0.04  ? 2234 TRP A CD2   1 
ATOM   6209  N  NE1   . TRP A 1 2234 ? 199.135 247.900 239.860 1.00 0.02  ? 2234 TRP A NE1   1 
ATOM   6210  C  CE2   . TRP A 1 2234 ? 198.920 246.671 240.421 1.00 0.03  ? 2234 TRP A CE2   1 
ATOM   6211  C  CE3   . TRP A 1 2234 ? 197.717 245.746 242.298 1.00 0.02  ? 2234 TRP A CE3   1 
ATOM   6212  C  CZ2   . TRP A 1 2234 ? 199.383 245.416 240.040 1.00 0.04  ? 2234 TRP A CZ2   1 
ATOM   6213  C  CZ3   . TRP A 1 2234 ? 198.179 244.505 241.920 1.00 0.02  ? 2234 TRP A CZ3   1 
ATOM   6214  C  CH2   . TRP A 1 2234 ? 199.002 244.348 240.799 1.00 0.04  ? 2234 TRP A CH2   1 
ATOM   6215  N  N     . ARG A 1 2235 ? 199.382 247.590 244.554 1.00 0.11  ? 2235 ARG A N     1 
ATOM   6216  C  CA    . ARG A 1 2235 ? 199.910 246.397 245.208 1.00 0.11  ? 2235 ARG A CA    1 
ATOM   6217  C  C     . ARG A 1 2235 ? 199.881 246.542 246.724 1.00 0.28  ? 2235 ARG A C     1 
ATOM   6218  O  O     . ARG A 1 2235 ? 199.586 245.578 247.439 1.00 0.58  ? 2235 ARG A O     1 
ATOM   6219  C  CB    . ARG A 1 2235 ? 201.329 246.107 244.716 1.00 0.30  ? 2235 ARG A CB    1 
ATOM   6220  C  CG    . ARG A 1 2235 ? 201.404 245.529 243.311 1.00 0.75  ? 2235 ARG A CG    1 
ATOM   6221  C  CD    . ARG A 1 2235 ? 202.848 245.300 242.881 1.00 2.79  ? 2235 ARG A CD    1 
ATOM   6222  N  NE    . ARG A 1 2235 ? 202.961 244.466 241.687 1.00 6.27  ? 2235 ARG A NE    1 
ATOM   6223  C  CZ    . ARG A 1 2235 ? 202.631 243.182 241.624 1.00 6.85  ? 2235 ARG A CZ    1 
ATOM   6224  N  NH1   . ARG A 1 2235 ? 202.180 242.530 242.682 1.00 8.50  ? 2235 ARG A NH1   1 
ATOM   6225  N  NH2   . ARG A 1 2235 ? 202.766 242.535 240.473 1.00 2.92  ? 2235 ARG A NH2   1 
ATOM   6226  N  N     . VAL A 1 2236 ? 200.193 247.734 247.234 1.00 0.32  ? 2236 VAL A N     1 
ATOM   6227  C  CA    . VAL A 1 2236 ? 200.126 247.972 248.673 1.00 0.45  ? 2236 VAL A CA    1 
ATOM   6228  C  C     . VAL A 1 2236 ? 198.677 248.005 249.145 1.00 0.40  ? 2236 VAL A C     1 
ATOM   6229  O  O     . VAL A 1 2236 ? 198.344 247.458 250.201 1.00 0.33  ? 2236 VAL A O     1 
ATOM   6230  C  CB    . VAL A 1 2236 ? 200.877 249.266 249.035 1.00 0.29  ? 2236 VAL A CB    1 
ATOM   6231  C  CG1   . VAL A 1 2236 ? 200.499 249.747 250.420 1.00 0.58  ? 2236 VAL A CG1   1 
ATOM   6232  C  CG2   . VAL A 1 2236 ? 202.369 249.042 248.949 1.00 0.53  ? 2236 VAL A CG2   1 
ATOM   6233  N  N     . LEU A 1 2237 ? 197.796 248.643 248.370 1.00 0.48  ? 2237 LEU A N     1 
ATOM   6234  C  CA    . LEU A 1 2237 ? 196.389 248.714 248.756 1.00 0.32  ? 2237 LEU A CA    1 
ATOM   6235  C  C     . LEU A 1 2237 ? 195.765 247.327 248.815 1.00 0.42  ? 2237 LEU A C     1 
ATOM   6236  O  O     . LEU A 1 2237 ? 194.970 247.036 249.714 1.00 0.50  ? 2237 LEU A O     1 
ATOM   6237  C  CB    . LEU A 1 2237 ? 195.619 249.608 247.783 1.00 0.26  ? 2237 LEU A CB    1 
ATOM   6238  C  CG    . LEU A 1 2237 ? 194.110 249.735 248.021 1.00 0.20  ? 2237 LEU A CG    1 
ATOM   6239  C  CD1   . LEU A 1 2237 ? 193.815 250.296 249.404 1.00 0.23  ? 2237 LEU A CD1   1 
ATOM   6240  C  CD2   . LEU A 1 2237 ? 193.459 250.584 246.947 1.00 0.15  ? 2237 LEU A CD2   1 
ATOM   6241  N  N     . LEU A 1 2238 ? 196.117 246.455 247.866 1.00 0.58  ? 2238 LEU A N     1 
ATOM   6242  C  CA    . LEU A 1 2238 ? 195.566 245.105 247.855 1.00 0.24  ? 2238 LEU A CA    1 
ATOM   6243  C  C     . LEU A 1 2238 ? 195.964 244.334 249.106 1.00 0.64  ? 2238 LEU A C     1 
ATOM   6244  O  O     . LEU A 1 2238 ? 195.136 243.637 249.704 1.00 1.45  ? 2238 LEU A O     1 
ATOM   6245  C  CB    . LEU A 1 2238 ? 196.018 244.365 246.596 1.00 0.26  ? 2238 LEU A CB    1 
ATOM   6246  C  CG    . LEU A 1 2238 ? 195.343 243.027 246.282 1.00 0.32  ? 2238 LEU A CG    1 
ATOM   6247  C  CD1   . LEU A 1 2238 ? 193.840 243.199 246.126 1.00 0.18  ? 2238 LEU A CD1   1 
ATOM   6248  C  CD2   . LEU A 1 2238 ? 195.941 242.405 245.034 1.00 0.09  ? 2238 LEU A CD2   1 
ATOM   6249  N  N     . LYS A 1 2239 ? 197.229 244.443 249.519 1.00 0.71  ? 2239 LYS A N     1 
ATOM   6250  C  CA    . LYS A 1 2239 ? 197.667 243.784 250.745 1.00 0.80  ? 2239 LYS A CA    1 
ATOM   6251  C  C     . LYS A 1 2239 ? 197.022 244.408 251.976 1.00 0.84  ? 2239 LYS A C     1 
ATOM   6252  O  O     . LYS A 1 2239 ? 196.652 243.696 252.915 1.00 2.68  ? 2239 LYS A O     1 
ATOM   6253  C  CB    . LYS A 1 2239 ? 199.193 243.837 250.855 1.00 1.15  ? 2239 LYS A CB    1 
ATOM   6254  C  CG    . LYS A 1 2239 ? 199.914 243.074 249.768 1.00 4.57  ? 2239 LYS A CG    1 
ATOM   6255  C  CD    . LYS A 1 2239 ? 201.406 243.351 249.787 1.00 4.44  ? 2239 LYS A CD    1 
ATOM   6256  C  CE    . LYS A 1 2239 ? 202.147 242.425 248.838 1.00 3.45  ? 2239 LYS A CE    1 
ATOM   6257  N  NZ    . LYS A 1 2239 ? 203.600 242.727 248.786 1.00 5.59  ? 2239 LYS A NZ    1 
ATOM   6258  N  N     . ALA A 1 2240 ? 196.890 245.737 251.994 1.00 0.74  ? 2240 ALA A N     1 
ATOM   6259  C  CA    . ALA A 1 2240 ? 196.304 246.410 253.148 1.00 1.65  ? 2240 ALA A CA    1 
ATOM   6260  C  C     . ALA A 1 2240 ? 194.844 246.014 253.339 1.00 1.82  ? 2240 ALA A C     1 
ATOM   6261  O  O     . ALA A 1 2240 ? 194.394 245.810 254.473 1.00 2.83  ? 2240 ALA A O     1 
ATOM   6262  C  CB    . ALA A 1 2240 ? 196.436 247.924 252.995 1.00 1.08  ? 2240 ALA A CB    1 
ATOM   6263  N  N     . LEU A 1 2241 ? 194.092 245.908 252.244 1.00 1.03  ? 2241 LEU A N     1 
ATOM   6264  C  CA    . LEU A 1 2241 ? 192.698 245.493 252.347 1.00 1.23  ? 2241 LEU A CA    1 
ATOM   6265  C  C     . LEU A 1 2241 ? 192.574 244.051 252.818 1.00 3.25  ? 2241 LEU A C     1 
ATOM   6266  O  O     . LEU A 1 2241 ? 191.595 243.702 253.485 1.00 6.83  ? 2241 LEU A O     1 
ATOM   6267  C  CB    . LEU A 1 2241 ? 191.994 245.682 251.005 1.00 0.74  ? 2241 LEU A CB    1 
ATOM   6268  C  CG    . LEU A 1 2241 ? 191.896 247.135 250.540 1.00 0.74  ? 2241 LEU A CG    1 
ATOM   6269  C  CD1   . LEU A 1 2241 ? 191.302 247.230 249.145 1.00 0.31  ? 2241 LEU A CD1   1 
ATOM   6270  C  CD2   . LEU A 1 2241 ? 191.100 247.959 251.534 1.00 1.61  ? 2241 LEU A CD2   1 
ATOM   6271  N  N     . GLU A 1 2242 ? 193.547 243.202 252.480 1.00 2.33  ? 2242 GLU A N     1 
ATOM   6272  C  CA    . GLU A 1 2242 ? 193.539 241.834 252.986 1.00 2.72  ? 2242 GLU A CA    1 
ATOM   6273  C  C     . GLU A 1 2242 ? 193.660 241.811 254.503 1.00 3.92  ? 2242 GLU A C     1 
ATOM   6274  O  O     . GLU A 1 2242 ? 192.988 241.024 255.177 1.00 7.12  ? 2242 GLU A O     1 
ATOM   6275  C  CB    . GLU A 1 2242 ? 194.668 241.027 252.345 1.00 3.40  ? 2242 GLU A CB    1 
ATOM   6276  C  CG    . GLU A 1 2242 ? 194.726 239.578 252.795 1.00 3.06  ? 2242 GLU A CG    1 
ATOM   6277  C  CD    . GLU A 1 2242 ? 195.314 238.659 251.744 1.00 9.97  ? 2242 GLU A CD    1 
ATOM   6278  O  OE1   . GLU A 1 2242 ? 195.643 239.144 250.641 1.00 6.50  ? 2242 GLU A OE1   1 
ATOM   6279  O  OE2   . GLU A 1 2242 ? 195.446 237.448 252.021 1.00 15.04 ? 2242 GLU A OE2   1 
ATOM   6280  N  N     . ARG A 1 2243 ? 194.519 242.667 255.056 1.00 4.39  ? 2243 ARG A N     1 
ATOM   6281  C  CA    . ARG A 1 2243 ? 194.709 242.715 256.501 1.00 6.62  ? 2243 ARG A CA    1 
ATOM   6282  C  C     . ARG A 1 2243 ? 193.556 243.435 257.189 1.00 5.58  ? 2243 ARG A C     1 
ATOM   6283  O  O     . ARG A 1 2243 ? 193.121 243.027 258.270 1.00 11.87 ? 2243 ARG A O     1 
ATOM   6284  C  CB    . ARG A 1 2243 ? 196.033 243.405 256.818 1.00 6.18  ? 2243 ARG A CB    1 
ATOM   6285  C  CG    . ARG A 1 2243 ? 197.248 242.617 256.376 1.00 9.13  ? 2243 ARG A CG    1 
ATOM   6286  C  CD    . ARG A 1 2243 ? 198.528 243.350 256.711 1.00 15.54 ? 2243 ARG A CD    1 
ATOM   6287  N  NE    . ARG A 1 2243 ? 199.711 242.619 256.273 1.00 15.19 ? 2243 ARG A NE    1 
ATOM   6288  C  CZ    . ARG A 1 2243 ? 200.952 243.067 256.394 1.00 17.32 ? 2243 ARG A CZ    1 
ATOM   6289  N  NH1   . ARG A 1 2243 ? 201.214 244.227 256.970 1.00 15.71 ? 2243 ARG A NH1   1 
ATOM   6290  N  NH2   . ARG A 1 2243 ? 201.957 242.332 255.929 1.00 18.06 ? 2243 ARG A NH2   1 
ATOM   6291  N  N     . LEU A 1 2244 ? 193.050 244.503 256.570 1.00 5.98  ? 2244 LEU A N     1 
ATOM   6292  C  CA    . LEU A 1 2244 ? 191.988 245.293 257.181 1.00 5.10  ? 2244 LEU A CA    1 
ATOM   6293  C  C     . LEU A 1 2244 ? 190.664 244.540 257.188 1.00 5.80  ? 2244 LEU A C     1 
ATOM   6294  O  O     . LEU A 1 2244 ? 189.969 244.494 258.208 1.00 9.92  ? 2244 LEU A O     1 
ATOM   6295  C  CB    . LEU A 1 2244 ? 191.845 246.621 256.439 1.00 4.03  ? 2244 LEU A CB    1 
ATOM   6296  C  CG    . LEU A 1 2244 ? 190.840 247.623 257.007 1.00 6.94  ? 2244 LEU A CG    1 
ATOM   6297  C  CD1   . LEU A 1 2244 ? 191.448 248.383 258.167 1.00 8.76  ? 2244 LEU A CD1   1 
ATOM   6298  C  CD2   . LEU A 1 2244 ? 190.358 248.576 255.923 1.00 5.34  ? 2244 LEU A CD2   1 
ATOM   6299  N  N     . GLU A 1 2245 ? 190.300 243.939 256.055 1.00 5.53  ? 2245 GLU A N     1 
ATOM   6300  C  CA    . GLU A 1 2245 ? 188.980 243.353 255.874 1.00 4.32  ? 2245 GLU A CA    1 
ATOM   6301  C  C     . GLU A 1 2245 ? 188.956 241.841 256.051 1.00 6.88  ? 2245 GLU A C     1 
ATOM   6302  O  O     . GLU A 1 2245 ? 187.870 241.269 256.183 1.00 12.02 ? 2245 GLU A O     1 
ATOM   6303  C  CB    . GLU A 1 2245 ? 188.445 243.704 254.480 1.00 8.25  ? 2245 GLU A CB    1 
ATOM   6304  C  CG    . GLU A 1 2245 ? 188.152 245.181 254.282 1.00 10.42 ? 2245 GLU A CG    1 
ATOM   6305  C  CD    . GLU A 1 2245 ? 187.646 245.489 252.889 1.00 18.32 ? 2245 GLU A CD    1 
ATOM   6306  O  OE1   . GLU A 1 2245 ? 187.642 244.574 252.040 1.00 14.97 ? 2245 GLU A OE1   1 
ATOM   6307  O  OE2   . GLU A 1 2245 ? 187.252 246.650 252.641 1.00 24.07 ? 2245 GLU A OE2   1 
ATOM   6308  N  N     . GLY A 1 2246 ? 190.114 241.187 256.055 1.00 3.41  ? 2246 GLY A N     1 
ATOM   6309  C  CA    . GLY A 1 2246 ? 190.168 239.745 256.141 1.00 2.66  ? 2246 GLY A CA    1 
ATOM   6310  C  C     . GLY A 1 2246 ? 189.929 239.018 254.837 1.00 5.58  ? 2246 GLY A C     1 
ATOM   6311  O  O     . GLY A 1 2246 ? 189.953 237.780 254.826 1.00 6.50  ? 2246 GLY A O     1 
ATOM   6312  N  N     . VAL A 1 2247 ? 189.709 239.738 253.744 1.00 4.94  ? 2247 VAL A N     1 
ATOM   6313  C  CA    . VAL A 1 2247 ? 189.427 239.133 252.448 1.00 5.05  ? 2247 VAL A CA    1 
ATOM   6314  C  C     . VAL A 1 2247 ? 190.725 239.022 251.663 1.00 3.76  ? 2247 VAL A C     1 
ATOM   6315  O  O     . VAL A 1 2247 ? 191.437 240.015 251.478 1.00 5.16  ? 2247 VAL A O     1 
ATOM   6316  C  CB    . VAL A 1 2247 ? 188.382 239.954 251.677 1.00 3.09  ? 2247 VAL A CB    1 
ATOM   6317  C  CG1   . VAL A 1 2247 ? 188.131 239.353 250.306 1.00 1.74  ? 2247 VAL A CG1   1 
ATOM   6318  C  CG2   . VAL A 1 2247 ? 187.089 240.044 252.475 1.00 2.19  ? 2247 VAL A CG2   1 
ATOM   6319  N  N     . GLU A 1 2248 ? 191.036 237.813 251.205 1.00 3.62  ? 2248 GLU A N     1 
ATOM   6320  C  CA    . GLU A 1 2248 ? 192.252 237.589 250.436 1.00 3.76  ? 2248 GLU A CA    1 
ATOM   6321  C  C     . GLU A 1 2248 ? 192.187 238.337 249.110 1.00 4.10  ? 2248 GLU A C     1 
ATOM   6322  O  O     . GLU A 1 2248 ? 191.169 238.301 248.412 1.00 5.35  ? 2248 GLU A O     1 
ATOM   6323  C  CB    . GLU A 1 2248 ? 192.457 236.095 250.194 1.00 4.99  ? 2248 GLU A CB    1 
ATOM   6324  C  CG    . GLU A 1 2248 ? 193.544 235.768 249.186 1.00 7.63  ? 2248 GLU A CG    1 
ATOM   6325  C  CD    . GLU A 1 2248 ? 193.662 234.281 248.923 1.00 21.10 ? 2248 GLU A CD    1 
ATOM   6326  O  OE1   . GLU A 1 2248 ? 192.955 233.500 249.593 1.00 22.87 ? 2248 GLU A OE1   1 
ATOM   6327  O  OE2   . GLU A 1 2248 ? 194.460 233.892 248.045 1.00 23.85 ? 2248 GLU A OE2   1 
ATOM   6328  N  N     . GLY A 1 2249 ? 193.276 239.018 248.764 1.00 3.47  ? 2249 GLY A N     1 
ATOM   6329  C  CA    . GLY A 1 2249 ? 193.353 239.784 247.535 1.00 1.25  ? 2249 GLY A CA    1 
ATOM   6330  C  C     . GLY A 1 2249 ? 194.213 239.076 246.506 1.00 0.97  ? 2249 GLY A C     1 
ATOM   6331  O  O     . GLY A 1 2249 ? 195.343 238.673 246.792 1.00 3.91  ? 2249 GLY A O     1 
ATOM   6332  N  N     . VAL A 1 2250 ? 193.661 238.927 245.306 1.00 0.76  ? 2250 VAL A N     1 
ATOM   6333  C  CA    . VAL A 1 2250 ? 194.334 238.254 244.203 1.00 0.31  ? 2250 VAL A CA    1 
ATOM   6334  C  C     . VAL A 1 2250 ? 194.362 239.201 243.015 1.00 0.17  ? 2250 VAL A C     1 
ATOM   6335  O  O     . VAL A 1 2250 ? 193.323 239.740 242.620 1.00 0.24  ? 2250 VAL A O     1 
ATOM   6336  C  CB    . VAL A 1 2250 ? 193.633 236.934 243.829 1.00 0.27  ? 2250 VAL A CB    1 
ATOM   6337  C  CG1   . VAL A 1 2250 ? 194.258 236.334 242.578 1.00 0.20  ? 2250 VAL A CG1   1 
ATOM   6338  C  CG2   . VAL A 1 2250 ? 193.697 235.957 244.987 1.00 1.41  ? 2250 VAL A CG2   1 
ATOM   6339  N  N     . ALA A 1 2251 ? 195.545 239.401 242.445 1.00 0.12  ? 2251 ALA A N     1 
ATOM   6340  C  CA    . ALA A 1 2251 ? 195.722 240.254 241.280 1.00 0.03  ? 2251 ALA A CA    1 
ATOM   6341  C  C     . ALA A 1 2251 ? 196.187 239.414 240.099 1.00 0.04  ? 2251 ALA A C     1 
ATOM   6342  O  O     . ALA A 1 2251 ? 197.156 238.658 240.214 1.00 0.08  ? 2251 ALA A O     1 
ATOM   6343  C  CB    . ALA A 1 2251 ? 196.726 241.372 241.560 1.00 0.02  ? 2251 ALA A CB    1 
ATOM   6344  N  N     . HIS A 1 2252 ? 195.490 239.544 238.976 1.00 0.03  ? 2252 HIS A N     1 
ATOM   6345  C  CA    . HIS A 1 2252 ? 195.897 238.951 237.709 1.00 0.02  ? 2252 HIS A CA    1 
ATOM   6346  C  C     . HIS A 1 2252 ? 196.372 240.089 236.820 1.00 0.03  ? 2252 HIS A C     1 
ATOM   6347  O  O     . HIS A 1 2252 ? 195.561 240.888 236.340 1.00 0.06  ? 2252 HIS A O     1 
ATOM   6348  C  CB    . HIS A 1 2252 ? 194.745 238.189 237.054 1.00 0.03  ? 2252 HIS A CB    1 
ATOM   6349  C  CG    . HIS A 1 2252 ? 194.087 237.193 237.955 1.00 0.05  ? 2252 HIS A CG    1 
ATOM   6350  N  ND1   . HIS A 1 2252 ? 194.420 235.856 237.958 1.00 0.05  ? 2252 HIS A ND1   1 
ATOM   6351  C  CD2   . HIS A 1 2252 ? 193.105 237.338 238.875 1.00 0.11  ? 2252 HIS A CD2   1 
ATOM   6352  C  CE1   . HIS A 1 2252 ? 193.675 235.220 238.846 1.00 0.04  ? 2252 HIS A CE1   1 
ATOM   6353  N  NE2   . HIS A 1 2252 ? 192.869 236.097 239.415 1.00 0.07  ? 2252 HIS A NE2   1 
ATOM   6354  N  N     . ILE A 1 2253 ? 197.680 240.175 236.610 1.00 0.03  ? 2253 ILE A N     1 
ATOM   6355  C  CA    . ILE A 1 2253 ? 198.266 241.260 235.834 1.00 0.01  ? 2253 ILE A CA    1 
ATOM   6356  C  C     . ILE A 1 2253 ? 198.449 240.774 234.402 1.00 0.05  ? 2253 ILE A C     1 
ATOM   6357  O  O     . ILE A 1 2253 ? 199.089 239.748 234.163 1.00 0.03  ? 2253 ILE A O     1 
ATOM   6358  C  CB    . ILE A 1 2253 ? 199.600 241.729 236.435 1.00 0.06  ? 2253 ILE A CB    1 
ATOM   6359  C  CG1   . ILE A 1 2253 ? 199.399 242.297 237.841 1.00 0.04  ? 2253 ILE A CG1   1 
ATOM   6360  C  CG2   . ILE A 1 2253 ? 200.220 242.793 235.557 1.00 0.04  ? 2253 ILE A CG2   1 
ATOM   6361  C  CD1   . ILE A 1 2253 ? 199.476 241.275 238.948 1.00 0.03  ? 2253 ILE A CD1   1 
ATOM   6362  N  N     . ILE A 1 2254 ? 197.882 241.511 233.451 1.00 0.07  ? 2254 ILE A N     1 
ATOM   6363  C  CA    . ILE A 1 2254 ? 197.899 241.143 232.043 1.00 0.07  ? 2254 ILE A CA    1 
ATOM   6364  C  C     . ILE A 1 2254 ? 198.532 242.278 231.254 1.00 0.07  ? 2254 ILE A C     1 
ATOM   6365  O  O     . ILE A 1 2254 ? 198.193 243.447 231.462 1.00 0.15  ? 2254 ILE A O     1 
ATOM   6366  C  CB    . ILE A 1 2254 ? 196.483 240.841 231.517 1.00 0.05  ? 2254 ILE A CB    1 
ATOM   6367  C  CG1   . ILE A 1 2254 ? 195.884 239.640 232.246 1.00 0.02  ? 2254 ILE A CG1   1 
ATOM   6368  C  CG2   . ILE A 1 2254 ? 196.504 240.610 230.012 1.00 0.07  ? 2254 ILE A CG2   1 
ATOM   6369  C  CD1   . ILE A 1 2254 ? 194.470 239.319 231.829 1.00 0.01  ? 2254 ILE A CD1   1 
ATOM   6370  N  N     . ASP A 1 2255 ? 199.462 241.936 230.360 1.00 0.13  ? 2255 ASP A N     1 
ATOM   6371  C  CA    . ASP A 1 2255 ? 199.927 242.892 229.366 1.00 0.15  ? 2255 ASP A CA    1 
ATOM   6372  C  C     . ASP A 1 2255 ? 199.103 242.680 228.104 1.00 0.17  ? 2255 ASP A C     1 
ATOM   6373  O  O     . ASP A 1 2255 ? 199.382 241.746 227.337 1.00 0.19  ? 2255 ASP A O     1 
ATOM   6374  C  CB    . ASP A 1 2255 ? 201.419 242.716 229.078 1.00 0.13  ? 2255 ASP A CB    1 
ATOM   6375  C  CG    . ASP A 1 2255 ? 202.035 243.945 228.428 1.00 1.35  ? 2255 ASP A CG    1 
ATOM   6376  O  OD1   . ASP A 1 2255 ? 201.354 244.600 227.614 1.00 0.50  ? 2255 ASP A OD1   1 
ATOM   6377  O  OD2   . ASP A 1 2255 ? 203.205 244.255 228.733 1.00 6.11  ? 2255 ASP A OD2   1 
ATOM   6378  N  N     . PRO A 1 2256 ? 198.075 243.494 227.854 1.00 0.20  ? 2256 PRO A N     1 
ATOM   6379  C  CA    . PRO A 1 2256 ? 197.189 243.231 226.711 1.00 0.31  ? 2256 PRO A CA    1 
ATOM   6380  C  C     . PRO A 1 2256 ? 197.872 243.322 225.358 1.00 0.36  ? 2256 PRO A C     1 
ATOM   6381  O  O     . PRO A 1 2256 ? 197.469 242.611 224.431 1.00 1.42  ? 2256 PRO A O     1 
ATOM   6382  C  CB    . PRO A 1 2256 ? 196.101 244.299 226.871 1.00 0.08  ? 2256 PRO A CB    1 
ATOM   6383  C  CG    . PRO A 1 2256 ? 196.791 245.401 227.591 1.00 0.07  ? 2256 PRO A CG    1 
ATOM   6384  C  CD    . PRO A 1 2256 ? 197.724 244.742 228.549 1.00 0.11  ? 2256 PRO A CD    1 
ATOM   6385  N  N     . LYS A 1 2257 ? 198.880 244.176 225.206 1.00 0.29  ? 2257 LYS A N     1 
ATOM   6386  C  CA    . LYS A 1 2257 ? 199.541 244.370 223.922 1.00 0.32  ? 2257 LYS A CA    1 
ATOM   6387  C  C     . LYS A 1 2257 ? 200.780 243.505 223.747 1.00 0.35  ? 2257 LYS A C     1 
ATOM   6388  O  O     . LYS A 1 2257 ? 201.415 243.565 222.692 1.00 0.61  ? 2257 LYS A O     1 
ATOM   6389  C  CB    . LYS A 1 2257 ? 199.906 245.845 223.735 1.00 0.62  ? 2257 LYS A CB    1 
ATOM   6390  C  CG    . LYS A 1 2257 ? 198.707 246.766 223.598 1.00 0.36  ? 2257 LYS A CG    1 
ATOM   6391  C  CD    . LYS A 1 2257 ? 198.028 246.602 222.253 1.00 0.36  ? 2257 LYS A CD    1 
ATOM   6392  C  CE    . LYS A 1 2257 ? 198.884 247.142 221.120 1.00 2.08  ? 2257 LYS A CE    1 
ATOM   6393  N  NZ    . LYS A 1 2257 ? 198.643 248.588 220.868 1.00 0.55  ? 2257 LYS A NZ    1 
ATOM   6394  N  N     . ALA A 1 2258 ? 201.144 242.708 224.752 1.00 0.28  ? 2258 ALA A N     1 
ATOM   6395  C  CA    . ALA A 1 2258 ? 202.231 241.751 224.599 1.00 0.18  ? 2258 ALA A CA    1 
ATOM   6396  C  C     . ALA A 1 2258 ? 201.800 240.501 223.849 1.00 0.37  ? 2258 ALA A C     1 
ATOM   6397  O  O     . ALA A 1 2258 ? 202.654 239.691 223.477 1.00 0.65  ? 2258 ALA A O     1 
ATOM   6398  C  CB    . ALA A 1 2258 ? 202.791 241.362 225.969 1.00 0.08  ? 2258 ALA A CB    1 
ATOM   6399  N  N     . ILE A 1 2259 ? 200.499 240.332 223.624 1.00 0.66  ? 2259 ILE A N     1 
ATOM   6400  C  CA    . ILE A 1 2259 ? 199.939 239.189 222.923 1.00 0.61  ? 2259 ILE A CA    1 
ATOM   6401  C  C     . ILE A 1 2259 ? 198.972 239.708 221.868 1.00 0.56  ? 2259 ILE A C     1 
ATOM   6402  O  O     . ILE A 1 2259 ? 198.567 240.871 221.882 1.00 1.15  ? 2259 ILE A O     1 
ATOM   6403  C  CB    . ILE A 1 2259 ? 199.227 238.211 223.881 1.00 0.35  ? 2259 ILE A CB    1 
ATOM   6404  C  CG1   . ILE A 1 2259 ? 198.024 238.899 224.534 1.00 0.15  ? 2259 ILE A CG1   1 
ATOM   6405  C  CG2   . ILE A 1 2259 ? 200.191 237.697 224.936 1.00 0.07  ? 2259 ILE A CG2   1 
ATOM   6406  C  CD1   . ILE A 1 2259 ? 197.284 238.041 225.520 1.00 0.09  ? 2259 ILE A CD1   1 
ATOM   6407  N  N     . SER A 1 2260 ? 198.607 238.829 220.941 1.00 0.44  ? 2260 SER A N     1 
ATOM   6408  C  CA    . SER A 1 2260 ? 197.613 239.191 219.944 1.00 0.83  ? 2260 SER A CA    1 
ATOM   6409  C  C     . SER A 1 2260 ? 196.239 239.336 220.596 1.00 0.65  ? 2260 SER A C     1 
ATOM   6410  O  O     . SER A 1 2260 ? 195.962 238.772 221.658 1.00 0.47  ? 2260 SER A O     1 
ATOM   6411  C  CB    . SER A 1 2260 ? 197.562 238.148 218.829 1.00 1.54  ? 2260 SER A CB    1 
ATOM   6412  O  OG    . SER A 1 2260 ? 197.087 236.904 219.305 1.00 1.54  ? 2260 SER A OG    1 
ATOM   6413  N  N     . LYS A 1 2261 ? 195.378 240.122 219.948 1.00 0.33  ? 2261 LYS A N     1 
ATOM   6414  C  CA    . LYS A 1 2261 ? 194.015 240.275 220.443 1.00 0.62  ? 2261 LYS A CA    1 
ATOM   6415  C  C     . LYS A 1 2261 ? 193.266 238.950 220.416 1.00 0.60  ? 2261 LYS A C     1 
ATOM   6416  O  O     . LYS A 1 2261 ? 192.374 238.721 221.240 1.00 0.36  ? 2261 LYS A O     1 
ATOM   6417  C  CB    . LYS A 1 2261 ? 193.272 241.331 219.626 1.00 1.32  ? 2261 LYS A CB    1 
ATOM   6418  C  CG    . LYS A 1 2261 ? 191.875 241.633 220.129 1.00 0.71  ? 2261 LYS A CG    1 
ATOM   6419  C  CD    . LYS A 1 2261 ? 191.135 242.544 219.179 1.00 2.98  ? 2261 LYS A CD    1 
ATOM   6420  C  CE    . LYS A 1 2261 ? 189.708 242.766 219.633 1.00 2.60  ? 2261 LYS A CE    1 
ATOM   6421  N  NZ    . LYS A 1 2261 ? 188.970 243.634 218.680 1.00 4.46  ? 2261 LYS A NZ    1 
ATOM   6422  N  N     . ASP A 1 2262 ? 193.624 238.063 219.485 1.00 1.37  ? 2262 ASP A N     1 
ATOM   6423  C  CA    . ASP A 1 2262 ? 193.064 236.718 219.480 1.00 0.98  ? 2262 ASP A CA    1 
ATOM   6424  C  C     . ASP A 1 2262 ? 193.434 235.966 220.753 1.00 1.19  ? 2262 ASP A C     1 
ATOM   6425  O  O     . ASP A 1 2262 ? 192.619 235.214 221.299 1.00 1.33  ? 2262 ASP A O     1 
ATOM   6426  C  CB    . ASP A 1 2262 ? 193.552 235.955 218.249 1.00 5.15  ? 2262 ASP A CB    1 
ATOM   6427  C  CG    . ASP A 1 2262 ? 192.973 236.498 216.960 1.00 11.26 ? 2262 ASP A CG    1 
ATOM   6428  O  OD1   . ASP A 1 2262 ? 191.848 237.038 216.987 1.00 15.74 ? 2262 ASP A OD1   1 
ATOM   6429  O  OD2   . ASP A 1 2262 ? 193.644 236.379 215.913 1.00 13.74 ? 2262 ASP A OD2   1 
ATOM   6430  N  N     . HIS A 1 2263 ? 194.663 236.147 221.235 1.00 1.28  ? 2263 HIS A N     1 
ATOM   6431  C  CA    . HIS A 1 2263 ? 195.099 235.479 222.453 1.00 0.55  ? 2263 HIS A CA    1 
ATOM   6432  C  C     . HIS A 1 2263 ? 194.601 236.170 223.715 1.00 0.17  ? 2263 HIS A C     1 
ATOM   6433  O  O     . HIS A 1 2263 ? 194.653 235.572 224.793 1.00 0.13  ? 2263 HIS A O     1 
ATOM   6434  C  CB    . HIS A 1 2263 ? 196.626 235.386 222.478 1.00 0.40  ? 2263 HIS A CB    1 
ATOM   6435  C  CG    . HIS A 1 2263 ? 197.180 234.344 221.559 1.00 0.89  ? 2263 HIS A CG    1 
ATOM   6436  N  ND1   . HIS A 1 2263 ? 198.427 234.447 220.982 1.00 3.07  ? 2263 HIS A ND1   1 
ATOM   6437  C  CD2   . HIS A 1 2263 ? 196.656 233.178 221.116 1.00 1.74  ? 2263 HIS A CD2   1 
ATOM   6438  C  CE1   . HIS A 1 2263 ? 198.647 233.389 220.224 1.00 2.37  ? 2263 HIS A CE1   1 
ATOM   6439  N  NE2   . HIS A 1 2263 ? 197.588 232.603 220.287 1.00 4.37  ? 2263 HIS A NE2   1 
ATOM   6440  N  N     . LEU A 1 2264 ? 194.117 237.407 223.607 1.00 0.21  ? 2264 LEU A N     1 
ATOM   6441  C  CA    . LEU A 1 2264 ? 193.604 238.115 224.776 1.00 0.09  ? 2264 LEU A CA    1 
ATOM   6442  C  C     . LEU A 1 2264 ? 192.165 237.716 225.084 1.00 0.03  ? 2264 LEU A C     1 
ATOM   6443  O  O     . LEU A 1 2264 ? 191.828 237.422 226.234 1.00 0.05  ? 2264 LEU A O     1 
ATOM   6444  C  CB    . LEU A 1 2264 ? 193.710 239.626 224.559 1.00 0.09  ? 2264 LEU A CB    1 
ATOM   6445  C  CG    . LEU A 1 2264 ? 193.206 240.535 225.682 1.00 0.03  ? 2264 LEU A CG    1 
ATOM   6446  C  CD1   . LEU A 1 2264 ? 193.981 240.294 226.971 1.00 0.04  ? 2264 LEU A CD1   1 
ATOM   6447  C  CD2   . LEU A 1 2264 ? 193.303 241.992 225.263 1.00 0.04  ? 2264 LEU A CD2   1 
ATOM   6448  N  N     . TYR A 1 2265 ? 191.308 237.688 224.068 1.00 0.04  ? 2265 TYR A N     1 
ATOM   6449  C  CA    . TYR A 1 2265 ? 189.892 237.412 224.263 1.00 0.11  ? 2265 TYR A CA    1 
ATOM   6450  C  C     . TYR A 1 2265 ? 189.457 236.035 223.794 1.00 0.09  ? 2265 TYR A C     1 
ATOM   6451  O  O     . TYR A 1 2265 ? 188.478 235.504 224.318 1.00 0.08  ? 2265 TYR A O     1 
ATOM   6452  C  CB    . TYR A 1 2265 ? 189.043 238.466 223.547 1.00 0.04  ? 2265 TYR A CB    1 
ATOM   6453  C  CG    . TYR A 1 2265 ? 189.204 239.853 224.114 1.00 0.02  ? 2265 TYR A CG    1 
ATOM   6454  C  CD1   . TYR A 1 2265 ? 188.760 240.153 225.393 1.00 0.05  ? 2265 TYR A CD1   1 
ATOM   6455  C  CD2   . TYR A 1 2265 ? 189.800 240.863 223.371 1.00 0.04  ? 2265 TYR A CD2   1 
ATOM   6456  C  CE1   . TYR A 1 2265 ? 188.901 241.419 225.915 1.00 0.09  ? 2265 TYR A CE1   1 
ATOM   6457  C  CE2   . TYR A 1 2265 ? 189.946 242.130 223.885 1.00 0.08  ? 2265 TYR A CE2   1 
ATOM   6458  C  CZ    . TYR A 1 2265 ? 189.495 242.403 225.159 1.00 0.09  ? 2265 TYR A CZ    1 
ATOM   6459  O  OH    . TYR A 1 2265 ? 189.638 243.665 225.678 1.00 0.18  ? 2265 TYR A OH    1 
ATOM   6460  N  N     . GLY A 1 2266 ? 190.147 235.450 222.829 1.00 0.15  ? 2266 GLY A N     1 
ATOM   6461  C  CA    . GLY A 1 2266 ? 189.805 234.145 222.310 1.00 0.21  ? 2266 GLY A CA    1 
ATOM   6462  C  C     . GLY A 1 2266 ? 189.454 234.194 220.837 1.00 0.30  ? 2266 GLY A C     1 
ATOM   6463  O  O     . GLY A 1 2266 ? 189.345 235.255 220.224 1.00 0.81  ? 2266 GLY A O     1 
ATOM   6464  N  N     . THR A 1 2267 ? 189.282 233.004 220.272 1.00 0.53  ? 2267 THR A N     1 
ATOM   6465  C  CA    . THR A 1 2267 ? 188.978 232.849 218.858 1.00 0.95  ? 2267 THR A CA    1 
ATOM   6466  C  C     . THR A 1 2267 ? 187.817 231.886 218.691 1.00 0.84  ? 2267 THR A C     1 
ATOM   6467  O  O     . THR A 1 2267 ? 187.627 230.967 219.492 1.00 0.50  ? 2267 THR A O     1 
ATOM   6468  C  CB    . THR A 1 2267 ? 190.173 232.318 218.052 1.00 0.89  ? 2267 THR A CB    1 
ATOM   6469  O  OG1   . THR A 1 2267 ? 190.576 231.045 218.570 1.00 3.36  ? 2267 THR A OG1   1 
ATOM   6470  C  CG2   . THR A 1 2267 ? 191.336 233.276 218.117 1.00 1.16  ? 2267 THR A CG2   1 
ATOM   6471  N  N     . LEU A 1 2268 ? 187.046 232.108 217.636 1.00 1.28  ? 2268 LEU A N     1 
ATOM   6472  C  CA    . LEU A 1 2268 ? 186.014 231.182 217.196 1.00 2.88  ? 2268 LEU A CA    1 
ATOM   6473  C  C     . LEU A 1 2268 ? 186.554 230.446 215.976 1.00 3.37  ? 2268 LEU A C     1 
ATOM   6474  O  O     . LEU A 1 2268 ? 186.988 231.082 215.010 1.00 5.11  ? 2268 LEU A O     1 
ATOM   6475  C  CB    . LEU A 1 2268 ? 184.721 231.929 216.873 1.00 1.78  ? 2268 LEU A CB    1 
ATOM   6476  C  CG    . LEU A 1 2268 ? 183.412 231.145 216.867 1.00 3.22  ? 2268 LEU A CG    1 
ATOM   6477  C  CD1   . LEU A 1 2268 ? 183.307 230.265 218.097 1.00 2.67  ? 2268 LEU A CD1   1 
ATOM   6478  C  CD2   . LEU A 1 2268 ? 182.246 232.116 216.808 1.00 3.29  ? 2268 LEU A CD2   1 
ATOM   6479  N  N     . ASP A 1 2269 ? 186.546 229.120 216.031 1.00 6.89  ? 2269 ASP A N     1 
ATOM   6480  C  CA    . ASP A 1 2269 ? 187.136 228.319 214.969 1.00 9.55  ? 2269 ASP A CA    1 
ATOM   6481  C  C     . ASP A 1 2269 ? 186.380 228.548 213.661 1.00 10.89 ? 2269 ASP A C     1 
ATOM   6482  O  O     . ASP A 1 2269 ? 185.142 228.462 213.644 1.00 14.07 ? 2269 ASP A O     1 
ATOM   6483  C  CB    . ASP A 1 2269 ? 187.122 226.838 215.341 1.00 10.28 ? 2269 ASP A CB    1 
ATOM   6484  C  CG    . ASP A 1 2269 ? 187.840 225.965 214.321 1.00 17.95 ? 2269 ASP A CG    1 
ATOM   6485  O  OD1   . ASP A 1 2269 ? 187.409 225.911 213.149 1.00 20.87 ? 2269 ASP A OD1   1 
ATOM   6486  O  OD2   . ASP A 1 2269 ? 188.847 225.330 214.693 1.00 20.12 ? 2269 ASP A OD2   1 
ATOM   6487  N  N     . PRO A 1 2270 ? 187.075 228.845 212.563 1.00 9.63  ? 2270 PRO A N     1 
ATOM   6488  C  CA    . PRO A 1 2270 ? 186.376 229.112 211.294 1.00 11.30 ? 2270 PRO A CA    1 
ATOM   6489  C  C     . PRO A 1 2270 ? 185.524 227.958 210.795 1.00 17.32 ? 2270 PRO A C     1 
ATOM   6490  O  O     . PRO A 1 2270 ? 184.490 228.199 210.157 1.00 20.01 ? 2270 PRO A O     1 
ATOM   6491  C  CB    . PRO A 1 2270 ? 187.529 229.416 210.326 1.00 14.74 ? 2270 PRO A CB    1 
ATOM   6492  C  CG    . PRO A 1 2270 ? 188.645 229.882 211.201 1.00 11.63 ? 2270 PRO A CG    1 
ATOM   6493  C  CD    . PRO A 1 2270 ? 188.523 229.083 212.462 1.00 10.19 ? 2270 PRO A CD    1 
ATOM   6494  N  N     . ASN A 1 2271 ? 185.912 226.712 211.070 1.00 14.30 ? 2271 ASN A N     1 
ATOM   6495  C  CA    . ASN A 1 2271 ? 185.235 225.550 210.509 1.00 15.08 ? 2271 ASN A CA    1 
ATOM   6496  C  C     . ASN A 1 2271 ? 184.433 224.782 211.550 1.00 15.35 ? 2271 ASN A C     1 
ATOM   6497  O  O     . ASN A 1 2271 ? 183.226 224.591 211.380 1.00 20.30 ? 2271 ASN A O     1 
ATOM   6498  C  CB    . ASN A 1 2271 ? 186.261 224.628 209.837 1.00 18.90 ? 2271 ASN A CB    1 
ATOM   6499  C  CG    . ASN A 1 2271 ? 187.265 225.391 208.999 1.00 20.87 ? 2271 ASN A CG    1 
ATOM   6500  O  OD1   . ASN A 1 2271 ? 186.897 226.089 208.053 1.00 27.50 ? 2271 ASN A OD1   1 
ATOM   6501  N  ND2   . ASN A 1 2271 ? 188.539 225.264 209.341 1.00 16.21 ? 2271 ASN A ND2   1 
ATOM   6502  N  N     . THR A 1 2272 ? 185.068 224.336 212.637 1.00 12.52 ? 2272 THR A N     1 
ATOM   6503  C  CA    . THR A 1 2272 ? 184.338 223.589 213.654 1.00 10.79 ? 2272 THR A CA    1 
ATOM   6504  C  C     . THR A 1 2272 ? 183.472 224.494 214.518 1.00 8.23  ? 2272 THR A C     1 
ATOM   6505  O  O     . THR A 1 2272 ? 182.621 223.992 215.258 1.00 12.41 ? 2272 THR A O     1 
ATOM   6506  C  CB    . THR A 1 2272 ? 185.304 222.800 214.541 1.00 16.85 ? 2272 THR A CB    1 
ATOM   6507  O  OG1   . THR A 1 2272 ? 186.179 223.700 215.229 1.00 20.55 ? 2272 THR A OG1   1 
ATOM   6508  C  CG2   . THR A 1 2272 ? 186.140 221.848 213.699 1.00 20.17 ? 2272 THR A CG2   1 
ATOM   6509  N  N     . ARG A 1 2273 ? 183.672 225.812 214.433 1.00 11.14 ? 2273 ARG A N     1 
ATOM   6510  C  CA    . ARG A 1 2273 ? 182.930 226.798 215.223 1.00 9.47  ? 2273 ARG A CA    1 
ATOM   6511  C  C     . ARG A 1 2273 ? 183.100 226.564 216.723 1.00 11.07 ? 2273 ARG A C     1 
ATOM   6512  O  O     . ARG A 1 2273 ? 182.208 226.867 217.516 1.00 11.71 ? 2273 ARG A O     1 
ATOM   6513  C  CB    . ARG A 1 2273 ? 181.446 226.826 214.846 1.00 10.71 ? 2273 ARG A CB    1 
ATOM   6514  C  CG    . ARG A 1 2273 ? 181.183 226.711 213.350 1.00 12.43 ? 2273 ARG A CG    1 
ATOM   6515  C  CD    . ARG A 1 2273 ? 181.775 227.875 212.575 1.00 10.91 ? 2273 ARG A CD    1 
ATOM   6516  N  NE    . ARG A 1 2273 ? 181.372 229.169 213.108 1.00 9.57  ? 2273 ARG A NE    1 
ATOM   6517  C  CZ    . ARG A 1 2273 ? 182.013 230.305 212.873 1.00 8.03  ? 2273 ARG A CZ    1 
ATOM   6518  N  NH1   . ARG A 1 2273 ? 183.101 230.342 212.121 1.00 9.25  ? 2273 ARG A NH1   1 
ATOM   6519  N  NH2   . ARG A 1 2273 ? 181.552 231.433 213.406 1.00 5.73  ? 2273 ARG A NH2   1 
ATOM   6520  N  N     . GLU A 1 2274 ? 184.249 226.022 217.113 1.00 11.61 ? 2274 GLU A N     1 
ATOM   6521  C  CA    . GLU A 1 2274 ? 184.571 225.803 218.514 1.00 9.80  ? 2274 GLU A CA    1 
ATOM   6522  C  C     . GLU A 1 2274 ? 185.212 227.055 219.094 1.00 7.42  ? 2274 GLU A C     1 
ATOM   6523  O  O     . GLU A 1 2274 ? 186.041 227.700 218.445 1.00 6.47  ? 2274 GLU A O     1 
ATOM   6524  C  CB    . GLU A 1 2274 ? 185.515 224.609 218.665 1.00 11.19 ? 2274 GLU A CB    1 
ATOM   6525  C  CG    . GLU A 1 2274 ? 185.880 224.268 220.099 1.00 12.76 ? 2274 GLU A CG    1 
ATOM   6526  C  CD    . GLU A 1 2274 ? 184.690 223.801 220.915 1.00 21.38 ? 2274 GLU A CD    1 
ATOM   6527  O  OE1   . GLU A 1 2274 ? 183.725 223.279 220.318 1.00 27.20 ? 2274 GLU A OE1   1 
ATOM   6528  O  OE2   . GLU A 1 2274 ? 184.722 223.956 222.153 1.00 21.89 ? 2274 GLU A OE2   1 
ATOM   6529  N  N     . TRP A 1 2275 ? 184.824 227.401 220.317 1.00 4.40  ? 2275 TRP A N     1 
ATOM   6530  C  CA    . TRP A 1 2275 ? 185.345 228.592 220.970 1.00 2.13  ? 2275 TRP A CA    1 
ATOM   6531  C  C     . TRP A 1 2275 ? 186.504 228.233 221.889 1.00 2.66  ? 2275 TRP A C     1 
ATOM   6532  O  O     . TRP A 1 2275 ? 186.390 227.334 222.727 1.00 6.86  ? 2275 TRP A O     1 
ATOM   6533  C  CB    . TRP A 1 2275 ? 184.255 229.308 221.765 1.00 1.50  ? 2275 TRP A CB    1 
ATOM   6534  C  CG    . TRP A 1 2275 ? 184.803 230.442 222.566 1.00 0.90  ? 2275 TRP A CG    1 
ATOM   6535  C  CD1   . TRP A 1 2275 ? 185.056 230.456 223.903 1.00 0.41  ? 2275 TRP A CD1   1 
ATOM   6536  C  CD2   . TRP A 1 2275 ? 185.210 231.720 222.067 1.00 0.39  ? 2275 TRP A CD2   1 
ATOM   6537  N  NE1   . TRP A 1 2275 ? 185.579 231.670 224.272 1.00 0.32  ? 2275 TRP A NE1   1 
ATOM   6538  C  CE2   . TRP A 1 2275 ? 185.684 232.464 223.163 1.00 0.23  ? 2275 TRP A CE2   1 
ATOM   6539  C  CE3   . TRP A 1 2275 ? 185.215 232.310 220.799 1.00 0.45  ? 2275 TRP A CE3   1 
ATOM   6540  C  CZ2   . TRP A 1 2275 ? 186.153 233.767 223.032 1.00 0.17  ? 2275 TRP A CZ2   1 
ATOM   6541  C  CZ3   . TRP A 1 2275 ? 185.682 233.605 220.672 1.00 0.71  ? 2275 TRP A CZ3   1 
ATOM   6542  C  CH2   . TRP A 1 2275 ? 186.144 234.319 221.782 1.00 0.40  ? 2275 TRP A CH2   1 
ATOM   6543  N  N     . THR A 1 2276 ? 187.615 228.941 221.726 1.00 0.80  ? 2276 THR A N     1 
ATOM   6544  C  CA    . THR A 1 2276 ? 188.763 228.841 222.615 1.00 0.93  ? 2276 THR A CA    1 
ATOM   6545  C  C     . THR A 1 2276 ? 188.881 230.142 223.394 1.00 0.53  ? 2276 THR A C     1 
ATOM   6546  O  O     . THR A 1 2276 ? 188.854 231.224 222.801 1.00 0.46  ? 2276 THR A O     1 
ATOM   6547  C  CB    . THR A 1 2276 ? 190.052 228.570 221.835 1.00 1.11  ? 2276 THR A CB    1 
ATOM   6548  O  OG1   . THR A 1 2276 ? 189.966 227.296 221.186 1.00 6.66  ? 2276 THR A OG1   1 
ATOM   6549  C  CG2   . THR A 1 2276 ? 191.251 228.576 222.768 1.00 0.48  ? 2276 THR A CG2   1 
ATOM   6550  N  N     . ASP A 1 2277 ? 188.995 230.036 224.714 1.00 0.39  ? 2277 ASP A N     1 
ATOM   6551  C  CA    . ASP A 1 2277 ? 189.108 231.226 225.546 1.00 0.20  ? 2277 ASP A CA    1 
ATOM   6552  C  C     . ASP A 1 2277 ? 190.469 231.884 225.372 1.00 0.43  ? 2277 ASP A C     1 
ATOM   6553  O  O     . ASP A 1 2277 ? 191.494 231.212 225.231 1.00 0.20  ? 2277 ASP A O     1 
ATOM   6554  C  CB    . ASP A 1 2277 ? 188.892 230.874 227.018 1.00 0.15  ? 2277 ASP A CB    1 
ATOM   6555  C  CG    . ASP A 1 2277 ? 187.441 230.960 227.430 1.00 0.35  ? 2277 ASP A CG    1 
ATOM   6556  O  OD1   . ASP A 1 2277 ? 186.600 231.322 226.584 1.00 6.03  ? 2277 ASP A OD1   1 
ATOM   6557  O  OD2   . ASP A 1 2277 ? 187.141 230.667 228.603 1.00 0.78  ? 2277 ASP A OD2   1 
ATOM   6558  N  N     . GLY A 1 2278 ? 190.471 233.213 225.380 1.00 2.24  ? 2278 GLY A N     1 
ATOM   6559  C  CA    . GLY A 1 2278 ? 191.694 233.978 225.459 1.00 0.06  ? 2278 GLY A CA    1 
ATOM   6560  C  C     . GLY A 1 2278 ? 192.149 234.130 226.894 1.00 0.03  ? 2278 GLY A C     1 
ATOM   6561  O  O     . GLY A 1 2278 ? 191.598 233.543 227.824 1.00 0.04  ? 2278 GLY A O     1 
ATOM   6562  N  N     . LEU A 1 2279 ? 193.183 234.952 227.071 1.00 0.04  ? 2279 LEU A N     1 
ATOM   6563  C  CA    . LEU A 1 2279 ? 193.775 235.120 228.396 1.00 0.03  ? 2279 LEU A CA    1 
ATOM   6564  C  C     . LEU A 1 2279 ? 192.804 235.791 229.361 1.00 0.01  ? 2279 LEU A C     1 
ATOM   6565  O  O     . LEU A 1 2279 ? 192.576 235.293 230.468 1.00 0.03  ? 2279 LEU A O     1 
ATOM   6566  C  CB    . LEU A 1 2279 ? 195.073 235.918 228.286 1.00 0.04  ? 2279 LEU A CB    1 
ATOM   6567  C  CG    . LEU A 1 2279 ? 195.777 236.284 229.593 1.00 0.02  ? 2279 LEU A CG    1 
ATOM   6568  C  CD1   . LEU A 1 2279 ? 196.032 235.051 230.440 1.00 0.03  ? 2279 LEU A CD1   1 
ATOM   6569  C  CD2   . LEU A 1 2279 ? 197.071 237.008 229.293 1.00 0.04  ? 2279 LEU A CD2   1 
ATOM   6570  N  N     . PHE A 1 2280 ? 192.215 236.918 228.958 1.00 0.02  ? 2280 PHE A N     1 
ATOM   6571  C  CA    . PHE A 1 2280 ? 191.292 237.616 229.848 1.00 0.05  ? 2280 PHE A CA    1 
ATOM   6572  C  C     . PHE A 1 2280 ? 190.005 236.826 230.045 1.00 0.15  ? 2280 PHE A C     1 
ATOM   6573  O  O     . PHE A 1 2280 ? 189.474 236.764 231.158 1.00 0.05  ? 2280 PHE A O     1 
ATOM   6574  C  CB    . PHE A 1 2280 ? 190.985 239.012 229.308 1.00 0.02  ? 2280 PHE A CB    1 
ATOM   6575  C  CG    . PHE A 1 2280 ? 189.860 239.700 230.024 1.00 0.05  ? 2280 PHE A CG    1 
ATOM   6576  C  CD1   . PHE A 1 2280 ? 190.041 240.207 231.299 1.00 0.02  ? 2280 PHE A CD1   1 
ATOM   6577  C  CD2   . PHE A 1 2280 ? 188.619 239.832 229.425 1.00 0.01  ? 2280 PHE A CD2   1 
ATOM   6578  C  CE1   . PHE A 1 2280 ? 189.009 240.839 231.961 1.00 0.02  ? 2280 PHE A CE1   1 
ATOM   6579  C  CE2   . PHE A 1 2280 ? 187.583 240.461 230.084 1.00 0.04  ? 2280 PHE A CE2   1 
ATOM   6580  C  CZ    . PHE A 1 2280 ? 187.778 240.966 231.353 1.00 0.26  ? 2280 PHE A CZ    1 
ATOM   6581  N  N     . THR A 1 2281 ? 189.490 236.217 228.975 1.00 0.05  ? 2281 THR A N     1 
ATOM   6582  C  CA    . THR A 1 2281 ? 188.258 235.443 229.085 1.00 0.05  ? 2281 THR A CA    1 
ATOM   6583  C  C     . THR A 1 2281 ? 188.440 234.246 230.007 1.00 0.04  ? 2281 THR A C     1 
ATOM   6584  O  O     . THR A 1 2281 ? 187.542 233.911 230.785 1.00 0.05  ? 2281 THR A O     1 
ATOM   6585  C  CB    . THR A 1 2281 ? 187.797 234.990 227.699 1.00 0.10  ? 2281 THR A CB    1 
ATOM   6586  O  OG1   . THR A 1 2281 ? 187.899 236.085 226.781 1.00 0.14  ? 2281 THR A OG1   1 
ATOM   6587  C  CG2   . THR A 1 2281 ? 186.361 234.507 227.746 1.00 0.06  ? 2281 THR A CG2   1 
ATOM   6588  N  N     . HIS A 1 2282 ? 189.600 233.588 229.930 1.00 0.05  ? 2282 HIS A N     1 
ATOM   6589  C  CA    . HIS A 1 2282 ? 189.865 232.444 230.795 1.00 0.05  ? 2282 HIS A CA    1 
ATOM   6590  C  C     . HIS A 1 2282 ? 189.923 232.857 232.261 1.00 0.04  ? 2282 HIS A C     1 
ATOM   6591  O  O     . HIS A 1 2282 ? 189.383 232.164 233.131 1.00 0.09  ? 2282 HIS A O     1 
ATOM   6592  C  CB    . HIS A 1 2282 ? 191.166 231.764 230.370 1.00 0.08  ? 2282 HIS A CB    1 
ATOM   6593  C  CG    . HIS A 1 2282 ? 191.737 230.839 231.399 1.00 0.24  ? 2282 HIS A CG    1 
ATOM   6594  N  ND1   . HIS A 1 2282 ? 192.705 231.232 232.297 1.00 0.41  ? 2282 HIS A ND1   1 
ATOM   6595  C  CD2   . HIS A 1 2282 ? 191.481 229.537 231.667 1.00 0.16  ? 2282 HIS A CD2   1 
ATOM   6596  C  CE1   . HIS A 1 2282 ? 193.017 230.213 233.077 1.00 2.18  ? 2282 HIS A CE1   1 
ATOM   6597  N  NE2   . HIS A 1 2282 ? 192.288 229.172 232.717 1.00 1.40  ? 2282 HIS A NE2   1 
ATOM   6598  N  N     . VAL A 1 2283 ? 190.577 233.983 232.556 1.00 0.03  ? 2283 VAL A N     1 
ATOM   6599  C  CA    . VAL A 1 2283 ? 190.703 234.437 233.940 1.00 0.04  ? 2283 VAL A CA    1 
ATOM   6600  C  C     . VAL A 1 2283 ? 189.335 234.786 234.512 1.00 0.07  ? 2283 VAL A C     1 
ATOM   6601  O  O     . VAL A 1 2283 ? 188.982 234.376 235.623 1.00 0.11  ? 2283 VAL A O     1 
ATOM   6602  C  CB    . VAL A 1 2283 ? 191.672 235.630 234.027 1.00 0.06  ? 2283 VAL A CB    1 
ATOM   6603  C  CG1   . VAL A 1 2283 ? 191.601 236.282 235.400 1.00 0.05  ? 2283 VAL A CG1   1 
ATOM   6604  C  CG2   . VAL A 1 2283 ? 193.091 235.184 233.722 1.00 0.05  ? 2283 VAL A CG2   1 
ATOM   6605  N  N     . LEU A 1 2284 ? 188.541 235.545 233.754 1.00 0.06  ? 2284 LEU A N     1 
ATOM   6606  C  CA    . LEU A 1 2284 ? 187.224 235.949 234.229 1.00 0.08  ? 2284 LEU A CA    1 
ATOM   6607  C  C     . LEU A 1 2284 ? 186.294 234.752 234.373 1.00 0.10  ? 2284 LEU A C     1 
ATOM   6608  O  O     . LEU A 1 2284 ? 185.514 234.677 235.329 1.00 0.38  ? 2284 LEU A O     1 
ATOM   6609  C  CB    . LEU A 1 2284 ? 186.628 236.996 233.289 1.00 0.10  ? 2284 LEU A CB    1 
ATOM   6610  C  CG    . LEU A 1 2284 ? 185.162 237.387 233.482 1.00 0.10  ? 2284 LEU A CG    1 
ATOM   6611  C  CD1   . LEU A 1 2284 ? 184.934 237.978 234.864 1.00 1.57  ? 2284 LEU A CD1   1 
ATOM   6612  C  CD2   . LEU A 1 2284 ? 184.737 238.360 232.406 1.00 0.28  ? 2284 LEU A CD2   1 
ATOM   6613  N  N     . ARG A 1 2285 ? 186.362 233.802 233.437 1.00 0.08  ? 2285 ARG A N     1 
ATOM   6614  C  CA    . ARG A 1 2285 ? 185.523 232.612 233.529 1.00 0.20  ? 2285 ARG A CA    1 
ATOM   6615  C  C     . ARG A 1 2285 ? 185.907 231.747 234.722 1.00 0.50  ? 2285 ARG A C     1 
ATOM   6616  O  O     . ARG A 1 2285 ? 185.039 231.123 235.340 1.00 0.59  ? 2285 ARG A O     1 
ATOM   6617  C  CB    . ARG A 1 2285 ? 185.612 231.804 232.236 1.00 0.17  ? 2285 ARG A CB    1 
ATOM   6618  C  CG    . ARG A 1 2285 ? 184.579 230.700 232.124 1.00 0.40  ? 2285 ARG A CG    1 
ATOM   6619  C  CD    . ARG A 1 2285 ? 184.907 229.760 230.981 1.00 0.40  ? 2285 ARG A CD    1 
ATOM   6620  N  NE    . ARG A 1 2285 ? 184.861 230.432 229.688 1.00 0.35  ? 2285 ARG A NE    1 
ATOM   6621  C  CZ    . ARG A 1 2285 ? 183.749 230.770 229.052 1.00 0.50  ? 2285 ARG A CZ    1 
ATOM   6622  N  NH1   . ARG A 1 2285 ? 182.556 230.508 229.559 1.00 0.57  ? 2285 ARG A NH1   1 
ATOM   6623  N  NH2   . ARG A 1 2285 ? 183.835 231.384 227.877 1.00 0.64  ? 2285 ARG A NH2   1 
ATOM   6624  N  N     . LYS A 1 2286 ? 187.199 231.695 235.057 1.00 0.39  ? 2286 LYS A N     1 
ATOM   6625  C  CA    . LYS A 1 2286 ? 187.635 230.949 236.232 1.00 0.48  ? 2286 LYS A CA    1 
ATOM   6626  C  C     . LYS A 1 2286 ? 187.060 231.551 237.511 1.00 0.42  ? 2286 LYS A C     1 
ATOM   6627  O  O     . LYS A 1 2286 ? 186.699 230.822 238.440 1.00 0.86  ? 2286 LYS A O     1 
ATOM   6628  C  CB    . LYS A 1 2286 ? 189.162 230.917 236.286 1.00 1.01  ? 2286 LYS A CB    1 
ATOM   6629  C  CG    . LYS A 1 2286 ? 189.743 229.692 236.967 1.00 1.49  ? 2286 LYS A CG    1 
ATOM   6630  C  CD    . LYS A 1 2286 ? 191.230 229.865 237.216 1.00 2.54  ? 2286 LYS A CD    1 
ATOM   6631  C  CE    . LYS A 1 2286 ? 191.924 228.528 237.401 1.00 5.81  ? 2286 LYS A CE    1 
ATOM   6632  N  NZ    . LYS A 1 2286 ? 191.044 227.519 238.048 1.00 12.57 ? 2286 LYS A NZ    1 
ATOM   6633  N  N     . ILE A 1 2287 ? 186.971 232.881 237.575 1.00 0.32  ? 2287 ILE A N     1 
ATOM   6634  C  CA    . ILE A 1 2287 ? 186.413 233.538 238.755 1.00 0.53  ? 2287 ILE A CA    1 
ATOM   6635  C  C     . ILE A 1 2287 ? 184.909 233.301 238.846 1.00 0.73  ? 2287 ILE A C     1 
ATOM   6636  O  O     . ILE A 1 2287 ? 184.372 233.067 239.933 1.00 2.52  ? 2287 ILE A O     1 
ATOM   6637  C  CB    . ILE A 1 2287 ? 186.755 235.038 238.737 1.00 0.39  ? 2287 ILE A CB    1 
ATOM   6638  C  CG1   . ILE A 1 2287 ? 188.271 235.238 238.754 1.00 0.29  ? 2287 ILE A CG1   1 
ATOM   6639  C  CG2   . ILE A 1 2287 ? 186.105 235.754 239.909 1.00 0.34  ? 2287 ILE A CG2   1 
ATOM   6640  C  CD1   . ILE A 1 2287 ? 188.708 236.646 238.431 1.00 0.09  ? 2287 ILE A CD1   1 
ATOM   6641  N  N     . ILE A 1 2288 ? 184.207 233.364 237.713 1.00 0.55  ? 2288 ILE A N     1 
ATOM   6642  C  CA    . ILE A 1 2288 ? 182.763 233.146 237.715 1.00 0.67  ? 2288 ILE A CA    1 
ATOM   6643  C  C     . ILE A 1 2288 ? 182.431 231.712 238.113 1.00 0.95  ? 2288 ILE A C     1 
ATOM   6644  O  O     . ILE A 1 2288 ? 181.504 231.469 238.891 1.00 1.45  ? 2288 ILE A O     1 
ATOM   6645  C  CB    . ILE A 1 2288 ? 182.168 233.507 236.342 1.00 0.84  ? 2288 ILE A CB    1 
ATOM   6646  C  CG1   . ILE A 1 2288 ? 182.394 234.986 236.030 1.00 0.45  ? 2288 ILE A CG1   1 
ATOM   6647  C  CG2   . ILE A 1 2288 ? 180.686 233.165 236.289 1.00 0.52  ? 2288 ILE A CG2   1 
ATOM   6648  C  CD1   . ILE A 1 2288 ? 182.226 235.332 234.568 1.00 0.27  ? 2288 ILE A CD1   1 
ATOM   6649  N  N     . ASP A 1 2289 ? 183.179 230.741 237.580 1.00 1.46  ? 2289 ASP A N     1 
ATOM   6650  C  CA    . ASP A 1 2289 ? 182.915 229.340 237.895 1.00 1.45  ? 2289 ASP A CA    1 
ATOM   6651  C  C     . ASP A 1 2289 ? 183.141 229.053 239.372 1.00 3.91  ? 2289 ASP A C     1 
ATOM   6652  O  O     . ASP A 1 2289 ? 182.405 228.263 239.976 1.00 6.57  ? 2289 ASP A O     1 
ATOM   6653  C  CB    . ASP A 1 2289 ? 183.782 228.436 237.024 1.00 2.88  ? 2289 ASP A CB    1 
ATOM   6654  C  CG    . ASP A 1 2289 ? 183.355 228.451 235.569 1.00 17.56 ? 2289 ASP A CG    1 
ATOM   6655  O  OD1   . ASP A 1 2289 ? 184.206 228.190 234.693 1.00 12.95 ? 2289 ASP A OD1   1 
ATOM   6656  O  OD2   . ASP A 1 2289 ? 182.165 228.725 235.300 1.00 20.02 ? 2289 ASP A OD2   1 
ATOM   6657  N  N     . SER A 1 2290 ? 184.155 229.681 239.966 1.00 2.59  ? 2290 SER A N     1 
ATOM   6658  C  CA    . SER A 1 2290 ? 184.405 229.632 241.406 1.00 2.23  ? 2290 SER A CA    1 
ATOM   6659  C  C     . SER A 1 2290 ? 184.571 228.195 241.900 1.00 3.05  ? 2290 SER A C     1 
ATOM   6660  O  O     . SER A 1 2290 ? 183.996 227.786 242.912 1.00 3.00  ? 2290 SER A O     1 
ATOM   6661  C  CB    . SER A 1 2290 ? 183.302 230.352 242.178 1.00 2.88  ? 2290 SER A CB    1 
ATOM   6662  O  OG    . SER A 1 2290 ? 183.686 230.579 243.522 1.00 5.46  ? 2290 SER A OG    1 
ATOM   6663  N  N     . VAL A 1 2291 ? 185.376 227.424 241.168 1.00 3.64  ? 2291 VAL A N     1 
ATOM   6664  C  CA    . VAL A 1 2291 ? 185.680 226.063 241.585 1.00 3.01  ? 2291 VAL A CA    1 
ATOM   6665  C  C     . VAL A 1 2291 ? 186.496 226.047 242.870 1.00 3.47  ? 2291 VAL A C     1 
ATOM   6666  O  O     . VAL A 1 2291 ? 186.293 225.172 243.721 1.00 5.28  ? 2291 VAL A O     1 
ATOM   6667  C  CB    . VAL A 1 2291 ? 186.398 225.318 240.442 1.00 3.34  ? 2291 VAL A CB    1 
ATOM   6668  C  CG1   . VAL A 1 2291 ? 187.038 224.031 240.939 1.00 1.94  ? 2291 VAL A CG1   1 
ATOM   6669  C  CG2   . VAL A 1 2291 ? 185.423 225.036 239.306 1.00 2.58  ? 2291 VAL A CG2   1 
ATOM   6670  N  N     . ARG A 1 2292 ? 187.396 227.008 243.051 1.00 2.56  ? 2292 ARG A N     1 
ATOM   6671  C  CA    . ARG A 1 2292 ? 188.284 227.066 244.205 1.00 4.01  ? 2292 ARG A CA    1 
ATOM   6672  C  C     . ARG A 1 2292 ? 188.036 228.322 245.033 1.00 5.07  ? 2292 ARG A C     1 
ATOM   6673  O  O     . ARG A 1 2292 ? 188.964 228.921 245.582 1.00 7.52  ? 2292 ARG A O     1 
ATOM   6674  C  CB    . ARG A 1 2292 ? 189.741 226.985 243.757 1.00 3.30  ? 2292 ARG A CB    1 
ATOM   6675  C  CG    . ARG A 1 2292 ? 190.042 225.731 242.966 1.00 2.55  ? 2292 ARG A CG    1 
ATOM   6676  C  CD    . ARG A 1 2292 ? 191.440 225.742 242.379 1.00 2.75  ? 2292 ARG A CD    1 
ATOM   6677  N  NE    . ARG A 1 2292 ? 191.718 224.539 241.601 1.00 5.24  ? 2292 ARG A NE    1 
ATOM   6678  C  CZ    . ARG A 1 2292 ? 191.077 224.182 240.494 1.00 5.20  ? 2292 ARG A CZ    1 
ATOM   6679  N  NH1   . ARG A 1 2292 ? 190.151 224.954 239.949 1.00 8.30  ? 2292 ARG A NH1   1 
ATOM   6680  N  NH2   . ARG A 1 2292 ? 191.385 223.027 239.910 1.00 3.33  ? 2292 ARG A NH2   1 
ATOM   6681  N  N     . GLY A 1 2293 ? 186.776 228.732 245.135 1.00 3.89  ? 2293 GLY A N     1 
ATOM   6682  C  CA    . GLY A 1 2293 ? 186.398 229.857 245.974 1.00 2.52  ? 2293 GLY A CA    1 
ATOM   6683  C  C     . GLY A 1 2293 ? 186.921 231.209 245.533 1.00 4.79  ? 2293 GLY A C     1 
ATOM   6684  O  O     . GLY A 1 2293 ? 187.305 232.024 246.380 1.00 7.38  ? 2293 GLY A O     1 
ATOM   6685  N  N     . GLU A 1 2294 ? 186.936 231.473 244.226 1.00 3.29  ? 2294 GLU A N     1 
ATOM   6686  C  CA    . GLU A 1 2294 ? 187.371 232.774 243.730 1.00 2.48  ? 2294 GLU A CA    1 
ATOM   6687  C  C     . GLU A 1 2294 ? 186.345 233.875 243.967 1.00 3.28  ? 2294 GLU A C     1 
ATOM   6688  O  O     . GLU A 1 2294 ? 186.721 235.051 243.971 1.00 5.36  ? 2294 GLU A O     1 
ATOM   6689  C  CB    . GLU A 1 2294 ? 187.718 232.692 242.237 1.00 1.89  ? 2294 GLU A CB    1 
ATOM   6690  C  CG    . GLU A 1 2294 ? 188.803 231.678 241.845 1.00 1.35  ? 2294 GLU A CG    1 
ATOM   6691  C  CD    . GLU A 1 2294 ? 188.389 230.221 241.958 1.00 4.52  ? 2294 GLU A CD    1 
ATOM   6692  O  OE1   . GLU A 1 2294 ? 187.272 229.936 242.426 1.00 6.64  ? 2294 GLU A OE1   1 
ATOM   6693  O  OE2   . GLU A 1 2294 ? 189.195 229.354 241.569 1.00 10.17 ? 2294 GLU A OE2   1 
ATOM   6694  N  N     . LEU A 1 2295 ? 185.072 233.535 244.173 1.00 2.67  ? 2295 LEU A N     1 
ATOM   6695  C  CA    . LEU A 1 2295 ? 184.064 234.561 244.412 1.00 1.91  ? 2295 LEU A CA    1 
ATOM   6696  C  C     . LEU A 1 2295 ? 184.101 235.125 245.824 1.00 2.32  ? 2295 LEU A C     1 
ATOM   6697  O  O     . LEU A 1 2295 ? 183.468 236.155 246.076 1.00 4.56  ? 2295 LEU A O     1 
ATOM   6698  C  CB    . LEU A 1 2295 ? 182.663 234.020 244.124 1.00 2.02  ? 2295 LEU A CB    1 
ATOM   6699  C  CG    . LEU A 1 2295 ? 182.324 233.727 242.665 1.00 1.70  ? 2295 LEU A CG    1 
ATOM   6700  C  CD1   . LEU A 1 2295 ? 180.947 233.091 242.552 1.00 0.97  ? 2295 LEU A CD1   1 
ATOM   6701  C  CD2   . LEU A 1 2295 ? 182.408 234.993 241.834 1.00 0.77  ? 2295 LEU A CD2   1 
ATOM   6702  N  N     . GLN A 1 2296 ? 184.812 234.482 246.747 1.00 3.88  ? 2296 GLN A N     1 
ATOM   6703  C  CA    . GLN A 1 2296 ? 184.941 234.978 248.110 1.00 3.13  ? 2296 GLN A CA    1 
ATOM   6704  C  C     . GLN A 1 2296 ? 186.197 235.812 248.308 1.00 3.15  ? 2296 GLN A C     1 
ATOM   6705  O  O     . GLN A 1 2296 ? 186.457 236.261 249.428 1.00 6.55  ? 2296 GLN A O     1 
ATOM   6706  C  CB    . GLN A 1 2296 ? 184.929 233.812 249.104 1.00 3.20  ? 2296 GLN A CB    1 
ATOM   6707  C  CG    . GLN A 1 2296 ? 183.977 232.681 248.747 1.00 3.53  ? 2296 GLN A CG    1 
ATOM   6708  C  CD    . GLN A 1 2296 ? 182.593 233.167 248.363 1.00 6.03  ? 2296 GLN A CD    1 
ATOM   6709  O  OE1   . GLN A 1 2296 ? 182.103 232.880 247.272 1.00 3.37  ? 2296 GLN A OE1   1 
ATOM   6710  N  NE2   . GLN A 1 2296 ? 181.957 233.909 249.261 1.00 9.85  ? 2296 GLN A NE2   1 
ATOM   6711  N  N     . LYS A 1 2297 ? 186.973 236.033 247.253 1.00 4.38  ? 2297 LYS A N     1 
ATOM   6712  C  CA    . LYS A 1 2297 ? 188.210 236.789 247.322 1.00 2.36  ? 2297 LYS A CA    1 
ATOM   6713  C  C     . LYS A 1 2297 ? 188.073 238.071 246.514 1.00 1.22  ? 2297 LYS A C     1 
ATOM   6714  O  O     . LYS A 1 2297 ? 187.237 238.177 245.615 1.00 2.06  ? 2297 LYS A O     1 
ATOM   6715  C  CB    . LYS A 1 2297 ? 189.392 235.971 246.788 1.00 3.38  ? 2297 LYS A CB    1 
ATOM   6716  C  CG    . LYS A 1 2297 ? 189.554 234.610 247.430 1.00 7.13  ? 2297 LYS A CG    1 
ATOM   6717  C  CD    . LYS A 1 2297 ? 190.685 233.838 246.779 1.00 9.48  ? 2297 LYS A CD    1 
ATOM   6718  C  CE    . LYS A 1 2297 ? 190.771 232.422 247.317 1.00 10.26 ? 2297 LYS A CE    1 
ATOM   6719  N  NZ    . LYS A 1 2297 ? 191.904 231.674 246.711 1.00 14.54 ? 2297 LYS A NZ    1 
ATOM   6720  N  N     . ARG A 1 2298 ? 188.903 239.051 246.852 1.00 1.22  ? 2298 ARG A N     1 
ATOM   6721  C  CA    . ARG A 1 2298 ? 189.000 240.266 246.058 1.00 0.62  ? 2298 ARG A CA    1 
ATOM   6722  C  C     . ARG A 1 2298 ? 189.831 239.969 244.813 1.00 0.66  ? 2298 ARG A C     1 
ATOM   6723  O  O     . ARG A 1 2298 ? 191.011 239.617 244.916 1.00 1.08  ? 2298 ARG A O     1 
ATOM   6724  C  CB    . ARG A 1 2298 ? 189.616 241.392 246.881 1.00 0.36  ? 2298 ARG A CB    1 
ATOM   6725  C  CG    . ARG A 1 2298 ? 190.008 242.619 246.083 1.00 0.35  ? 2298 ARG A CG    1 
ATOM   6726  C  CD    . ARG A 1 2298 ? 190.364 243.779 246.996 1.00 0.52  ? 2298 ARG A CD    1 
ATOM   6727  N  NE    . ARG A 1 2298 ? 189.182 244.413 247.567 1.00 1.08  ? 2298 ARG A NE    1 
ATOM   6728  C  CZ    . ARG A 1 2298 ? 188.835 244.343 248.845 1.00 1.09  ? 2298 ARG A CZ    1 
ATOM   6729  N  NH1   . ARG A 1 2298 ? 189.554 243.663 249.721 1.00 0.65  ? 2298 ARG A NH1   1 
ATOM   6730  N  NH2   . ARG A 1 2298 ? 187.736 244.970 249.253 1.00 1.18  ? 2298 ARG A NH2   1 
ATOM   6731  N  N     . GLN A 1 2299 ? 189.213 240.091 243.642 1.00 0.40  ? 2299 GLN A N     1 
ATOM   6732  C  CA    . GLN A 1 2299 ? 189.842 239.734 242.375 1.00 0.17  ? 2299 GLN A CA    1 
ATOM   6733  C  C     . GLN A 1 2299 ? 190.079 241.003 241.569 1.00 0.05  ? 2299 GLN A C     1 
ATOM   6734  O  O     . GLN A 1 2299 ? 189.127 241.663 241.144 1.00 0.16  ? 2299 GLN A O     1 
ATOM   6735  C  CB    . GLN A 1 2299 ? 188.972 238.748 241.600 1.00 0.21  ? 2299 GLN A CB    1 
ATOM   6736  C  CG    . GLN A 1 2299 ? 188.729 237.438 242.323 1.00 0.28  ? 2299 GLN A CG    1 
ATOM   6737  C  CD    . GLN A 1 2299 ? 189.891 236.476 242.201 1.00 0.50  ? 2299 GLN A CD    1 
ATOM   6738  O  OE1   . GLN A 1 2299 ? 190.896 236.777 241.563 1.00 0.47  ? 2299 GLN A OE1   1 
ATOM   6739  N  NE2   . GLN A 1 2299 ? 189.761 235.312 242.819 1.00 3.23  ? 2299 GLN A NE2   1 
ATOM   6740  N  N     . TRP A 1 2300 ? 191.346 241.339 241.354 1.00 0.04  ? 2300 TRP A N     1 
ATOM   6741  C  CA    . TRP A 1 2300 ? 191.726 242.504 240.568 1.00 0.03  ? 2300 TRP A CA    1 
ATOM   6742  C  C     . TRP A 1 2300 ? 192.401 242.036 239.287 1.00 0.03  ? 2300 TRP A C     1 
ATOM   6743  O  O     . TRP A 1 2300 ? 193.399 241.313 239.336 1.00 0.04  ? 2300 TRP A O     1 
ATOM   6744  C  CB    . TRP A 1 2300 ? 192.650 243.427 241.362 1.00 0.05  ? 2300 TRP A CB    1 
ATOM   6745  C  CG    . TRP A 1 2300 ? 191.942 244.207 242.431 1.00 0.04  ? 2300 TRP A CG    1 
ATOM   6746  C  CD1   . TRP A 1 2300 ? 190.624 244.129 242.762 1.00 0.03  ? 2300 TRP A CD1   1 
ATOM   6747  C  CD2   . TRP A 1 2300 ? 192.518 245.182 243.303 1.00 0.05  ? 2300 TRP A CD2   1 
ATOM   6748  N  NE1   . TRP A 1 2300 ? 190.342 244.995 243.784 1.00 0.05  ? 2300 TRP A NE1   1 
ATOM   6749  C  CE2   . TRP A 1 2300 ? 191.487 245.654 244.137 1.00 0.07  ? 2300 TRP A CE2   1 
ATOM   6750  C  CE3   . TRP A 1 2300 ? 193.805 245.704 243.460 1.00 0.06  ? 2300 TRP A CE3   1 
ATOM   6751  C  CZ2   . TRP A 1 2300 ? 191.703 246.620 245.113 1.00 0.07  ? 2300 TRP A CZ2   1 
ATOM   6752  C  CZ3   . TRP A 1 2300 ? 194.015 246.662 244.428 1.00 0.09  ? 2300 TRP A CZ3   1 
ATOM   6753  C  CH2   . TRP A 1 2300 ? 192.971 247.111 245.244 1.00 0.14  ? 2300 TRP A CH2   1 
ATOM   6754  N  N     . ILE A 1 2301 ? 191.855 242.445 238.150 1.00 0.04  ? 2301 ILE A N     1 
ATOM   6755  C  CA    . ILE A 1 2301 ? 192.441 242.159 236.848 1.00 0.05  ? 2301 ILE A CA    1 
ATOM   6756  C  C     . ILE A 1 2301 ? 193.078 243.448 236.353 1.00 0.06  ? 2301 ILE A C     1 
ATOM   6757  O  O     . ILE A 1 2301 ? 192.381 244.389 235.956 1.00 0.05  ? 2301 ILE A O     1 
ATOM   6758  C  CB    . ILE A 1 2301 ? 191.399 241.617 235.862 1.00 0.02  ? 2301 ILE A CB    1 
ATOM   6759  C  CG1   . ILE A 1 2301 ? 190.734 240.366 236.437 1.00 0.08  ? 2301 ILE A CG1   1 
ATOM   6760  C  CG2   . ILE A 1 2301 ? 192.045 241.317 234.518 1.00 0.02  ? 2301 ILE A CG2   1 
ATOM   6761  C  CD1   . ILE A 1 2301 ? 189.567 239.861 235.635 1.00 0.02  ? 2301 ILE A CD1   1 
ATOM   6762  N  N     . VAL A 1 2302 ? 194.402 243.497 236.377 1.00 0.04  ? 2302 VAL A N     1 
ATOM   6763  C  CA    . VAL A 1 2302 ? 195.151 244.705 236.063 1.00 0.03  ? 2302 VAL A CA    1 
ATOM   6764  C  C     . VAL A 1 2302 ? 195.703 244.574 234.653 1.00 0.06  ? 2302 VAL A C     1 
ATOM   6765  O  O     . VAL A 1 2302 ? 196.541 243.709 234.381 1.00 0.04  ? 2302 VAL A O     1 
ATOM   6766  C  CB    . VAL A 1 2302 ? 196.278 244.942 237.081 1.00 0.04  ? 2302 VAL A CB    1 
ATOM   6767  C  CG1   . VAL A 1 2302 ? 196.967 246.272 236.815 1.00 0.03  ? 2302 VAL A CG1   1 
ATOM   6768  C  CG2   . VAL A 1 2302 ? 195.731 244.887 238.499 1.00 0.03  ? 2302 VAL A CG2   1 
ATOM   6769  N  N     . PHE A 1 2303 ? 195.220 245.440 233.762 1.00 0.05  ? 2303 PHE A N     1 
ATOM   6770  C  CA    . PHE A 1 2303 ? 195.779 245.478 232.387 1.00 0.03  ? 2303 PHE A CA    1 
ATOM   6771  C  C     . PHE A 1 2303 ? 196.951 246.457 232.413 1.00 0.03  ? 2303 PHE A C     1 
ATOM   6772  O  O     . PHE A 1 2303 ? 196.731 247.661 232.206 1.00 0.11  ? 2303 PHE A O     1 
ATOM   6773  C  CB    . PHE A 1 2303 ? 194.705 245.851 231.362 1.00 0.03  ? 2303 PHE A CB    1 
ATOM   6774  C  CG    . PHE A 1 2303 ? 193.600 244.827 231.146 1.00 0.03  ? 2303 PHE A CG    1 
ATOM   6775  C  CD1   . PHE A 1 2303 ? 193.779 243.760 230.273 1.00 0.04  ? 2303 PHE A CD1   1 
ATOM   6776  C  CD2   . PHE A 1 2303 ? 192.374 244.952 231.788 1.00 0.02  ? 2303 PHE A CD2   1 
ATOM   6777  C  CE1   . PHE A 1 2303 ? 192.770 242.834 230.069 1.00 0.02  ? 2303 PHE A CE1   1 
ATOM   6778  C  CE2   . PHE A 1 2303 ? 191.367 244.025 231.580 1.00 0.02  ? 2303 PHE A CE2   1 
ATOM   6779  C  CZ    . PHE A 1 2303 ? 191.566 242.971 230.720 1.00 0.02  ? 2303 PHE A CZ    1 
ATOM   6780  N  N     . ASP A 1 2304 ? 198.156 245.957 232.701 1.00 0.07  ? 2304 ASP A N     1 
ATOM   6781  C  CA    . ASP A 1 2304 ? 199.374 246.814 232.740 1.00 0.12  ? 2304 ASP A CA    1 
ATOM   6782  C  C     . ASP A 1 2304 ? 199.986 246.876 231.338 1.00 0.16  ? 2304 ASP A C     1 
ATOM   6783  O  O     . ASP A 1 2304 ? 200.722 245.940 230.966 1.00 0.31  ? 2304 ASP A O     1 
ATOM   6784  C  CB    . ASP A 1 2304 ? 200.369 246.331 233.782 1.00 0.12  ? 2304 ASP A CB    1 
ATOM   6785  C  CG    . ASP A 1 2304 ? 201.574 247.231 234.012 1.00 0.13  ? 2304 ASP A CG    1 
ATOM   6786  O  OD1   . ASP A 1 2304 ? 201.636 248.305 233.379 1.00 0.18  ? 2304 ASP A OD1   1 
ATOM   6787  O  OD2   . ASP A 1 2304 ? 202.444 246.846 234.819 1.00 0.35  ? 2304 ASP A OD2   1 
ATOM   6788  N  N     . GLY A 1 2305 ? 199.698 247.946 230.600 1.00 0.11  ? 2305 GLY A N     1 
ATOM   6789  C  CA    . GLY A 1 2305 ? 200.189 248.060 229.219 1.00 0.29  ? 2305 GLY A CA    1 
ATOM   6790  C  C     . GLY A 1 2305 ? 199.510 249.188 228.475 1.00 0.45  ? 2305 GLY A C     1 
ATOM   6791  O  O     . GLY A 1 2305 ? 198.790 249.972 229.120 1.00 0.91  ? 2305 GLY A O     1 
ATOM   6792  N  N     . ASP A 1 2306 ? 199.724 249.265 227.165 1.00 0.53  ? 2306 ASP A N     1 
ATOM   6793  C  CA    . ASP A 1 2306 ? 199.171 250.335 226.349 1.00 0.66  ? 2306 ASP A CA    1 
ATOM   6794  C  C     . ASP A 1 2306 ? 197.689 250.111 226.079 1.00 0.66  ? 2306 ASP A C     1 
ATOM   6795  O  O     . ASP A 1 2306 ? 197.236 248.977 225.907 1.00 2.88  ? 2306 ASP A O     1 
ATOM   6796  C  CB    . ASP A 1 2306 ? 199.926 250.445 225.025 1.00 1.42  ? 2306 ASP A CB    1 
ATOM   6797  C  CG    . ASP A 1 2306 ? 201.355 250.897 225.210 1.00 3.42  ? 2306 ASP A CG    1 
ATOM   6798  O  OD1   . ASP A 1 2306 ? 201.664 251.470 226.276 1.00 6.30  ? 2306 ASP A OD1   1 
ATOM   6799  O  OD2   . ASP A 1 2306 ? 202.167 250.690 224.287 1.00 6.01  ? 2306 ASP A OD2   1 
ATOM   6800  N  N     . VAL A 1 2307 ? 196.938 251.205 226.033 1.00 0.51  ? 2307 VAL A N     1 
ATOM   6801  C  CA    . VAL A 1 2307 ? 195.513 251.172 225.732 1.00 0.68  ? 2307 VAL A CA    1 
ATOM   6802  C  C     . VAL A 1 2307 ? 195.311 251.686 224.314 1.00 1.14  ? 2307 VAL A C     1 
ATOM   6803  O  O     . VAL A 1 2307 ? 195.723 252.805 223.985 1.00 2.95  ? 2307 VAL A O     1 
ATOM   6804  C  CB    . VAL A 1 2307 ? 194.703 252.003 226.740 1.00 0.83  ? 2307 VAL A CB    1 
ATOM   6805  C  CG1   . VAL A 1 2307 ? 193.318 252.301 226.189 1.00 0.72  ? 2307 VAL A CG1   1 
ATOM   6806  C  CG2   . VAL A 1 2307 ? 194.589 251.271 228.065 1.00 0.18  ? 2307 VAL A CG2   1 
ATOM   6807  N  N     . ASP A 1 2308 ? 194.692 250.871 223.474 1.00 0.63  ? 2308 ASP A N     1 
ATOM   6808  C  CA    . ASP A 1 2308 ? 194.280 251.267 222.137 1.00 1.00  ? 2308 ASP A CA    1 
ATOM   6809  C  C     . ASP A 1 2308 ? 192.840 250.835 221.910 1.00 1.15  ? 2308 ASP A C     1 
ATOM   6810  O  O     . ASP A 1 2308 ? 192.357 249.895 222.549 1.00 0.68  ? 2308 ASP A O     1 
ATOM   6811  C  CB    . ASP A 1 2308 ? 195.240 250.705 221.067 1.00 1.10  ? 2308 ASP A CB    1 
ATOM   6812  C  CG    . ASP A 1 2308 ? 195.060 249.208 220.759 1.00 2.03  ? 2308 ASP A CG    1 
ATOM   6813  O  OD1   . ASP A 1 2308 ? 194.029 248.576 221.053 1.00 2.91  ? 2308 ASP A OD1   1 
ATOM   6814  O  OD2   . ASP A 1 2308 ? 196.010 248.639 220.189 1.00 4.65  ? 2308 ASP A OD2   1 
ATOM   6815  N  N     . PRO A 1 2309 ? 192.109 251.529 221.033 1.00 1.66  ? 2309 PRO A N     1 
ATOM   6816  C  CA    . PRO A 1 2309 ? 190.690 251.192 220.842 1.00 1.09  ? 2309 PRO A CA    1 
ATOM   6817  C  C     . PRO A 1 2309 ? 190.457 249.792 220.306 1.00 1.33  ? 2309 PRO A C     1 
ATOM   6818  O  O     . PRO A 1 2309 ? 189.356 249.258 220.479 1.00 1.14  ? 2309 PRO A O     1 
ATOM   6819  C  CB    . PRO A 1 2309 ? 190.207 252.259 219.849 1.00 1.34  ? 2309 PRO A CB    1 
ATOM   6820  C  CG    . PRO A 1 2309 ? 191.441 252.752 219.188 1.00 1.99  ? 2309 PRO A CG    1 
ATOM   6821  C  CD    . PRO A 1 2309 ? 192.510 252.689 220.223 1.00 1.85  ? 2309 PRO A CD    1 
ATOM   6822  N  N     . GLU A 1 2310 ? 191.456 249.174 219.671 1.00 2.34  ? 2310 GLU A N     1 
ATOM   6823  C  CA    . GLU A 1 2310 ? 191.238 247.876 219.039 1.00 1.85  ? 2310 GLU A CA    1 
ATOM   6824  C  C     . GLU A 1 2310 ? 190.887 246.802 220.063 1.00 3.47  ? 2310 GLU A C     1 
ATOM   6825  O  O     . GLU A 1 2310 ? 190.004 245.973 219.820 1.00 8.90  ? 2310 GLU A O     1 
ATOM   6826  C  CB    . GLU A 1 2310 ? 192.470 247.471 218.231 1.00 5.17  ? 2310 GLU A CB    1 
ATOM   6827  C  CG    . GLU A 1 2310 ? 192.300 246.166 217.471 1.00 10.72 ? 2310 GLU A CG    1 
ATOM   6828  C  CD    . GLU A 1 2310 ? 193.514 245.808 216.635 1.00 26.61 ? 2310 GLU A CD    1 
ATOM   6829  O  OE1   . GLU A 1 2310 ? 194.504 246.570 216.661 1.00 24.30 ? 2310 GLU A OE1   1 
ATOM   6830  O  OE2   . GLU A 1 2310 ? 193.476 244.764 215.949 1.00 27.51 ? 2310 GLU A OE2   1 
ATOM   6831  N  N     . TRP A 1 2311 ? 191.559 246.795 221.216 1.00 1.52  ? 2311 TRP A N     1 
ATOM   6832  C  CA    . TRP A 1 2311 ? 191.300 245.760 222.208 1.00 0.59  ? 2311 TRP A CA    1 
ATOM   6833  C  C     . TRP A 1 2311 ? 190.442 246.223 223.380 1.00 0.44  ? 2311 TRP A C     1 
ATOM   6834  O  O     . TRP A 1 2311 ? 189.646 245.430 223.887 1.00 3.71  ? 2311 TRP A O     1 
ATOM   6835  C  CB    . TRP A 1 2311 ? 192.617 245.172 222.742 1.00 0.31  ? 2311 TRP A CB    1 
ATOM   6836  C  CG    . TRP A 1 2311 ? 193.362 246.036 223.718 1.00 0.33  ? 2311 TRP A CG    1 
ATOM   6837  C  CD1   . TRP A 1 2311 ? 194.375 246.899 223.435 1.00 0.17  ? 2311 TRP A CD1   1 
ATOM   6838  C  CD2   . TRP A 1 2311 ? 193.155 246.117 225.134 1.00 0.14  ? 2311 TRP A CD2   1 
ATOM   6839  N  NE1   . TRP A 1 2311 ? 194.807 247.514 224.577 1.00 0.17  ? 2311 TRP A NE1   1 
ATOM   6840  C  CE2   . TRP A 1 2311 ? 194.079 247.047 225.636 1.00 0.08  ? 2311 TRP A CE2   1 
ATOM   6841  C  CE3   . TRP A 1 2311 ? 192.281 245.490 226.022 1.00 0.04  ? 2311 TRP A CE3   1 
ATOM   6842  C  CZ2   . TRP A 1 2311 ? 194.143 247.380 226.985 1.00 0.04  ? 2311 TRP A CZ2   1 
ATOM   6843  C  CZ3   . TRP A 1 2311 ? 192.352 245.815 227.358 1.00 0.03  ? 2311 TRP A CZ3   1 
ATOM   6844  C  CH2   . TRP A 1 2311 ? 193.278 246.748 227.828 1.00 0.02  ? 2311 TRP A CH2   1 
ATOM   6845  N  N     . VAL A 1 2312 ? 190.560 247.477 223.825 1.00 0.23  ? 2312 VAL A N     1 
ATOM   6846  C  CA    . VAL A 1 2312 ? 189.845 247.866 225.039 1.00 0.38  ? 2312 VAL A CA    1 
ATOM   6847  C  C     . VAL A 1 2312 ? 188.359 248.083 224.777 1.00 0.38  ? 2312 VAL A C     1 
ATOM   6848  O  O     . VAL A 1 2312 ? 187.549 247.955 225.702 1.00 0.37  ? 2312 VAL A O     1 
ATOM   6849  C  CB    . VAL A 1 2312 ? 190.448 249.129 225.680 1.00 0.24  ? 2312 VAL A CB    1 
ATOM   6850  C  CG1   . VAL A 1 2312 ? 190.217 250.363 224.805 1.00 0.47  ? 2312 VAL A CG1   1 
ATOM   6851  C  CG2   . VAL A 1 2312 ? 189.946 249.322 227.105 1.00 0.13  ? 2312 VAL A CG2   1 
ATOM   6852  N  N     . GLU A 1 2313 ? 187.972 248.395 223.541 1.00 0.27  ? 2313 GLU A N     1 
ATOM   6853  C  CA    . GLU A 1 2313 ? 186.564 248.578 223.218 1.00 0.50  ? 2313 GLU A CA    1 
ATOM   6854  C  C     . GLU A 1 2313 ? 185.779 247.273 223.214 1.00 0.79  ? 2313 GLU A C     1 
ATOM   6855  O  O     . GLU A 1 2313 ? 184.549 247.314 223.127 1.00 2.49  ? 2313 GLU A O     1 
ATOM   6856  C  CB    . GLU A 1 2313 ? 186.426 249.297 221.876 1.00 1.35  ? 2313 GLU A CB    1 
ATOM   6857  C  CG    . GLU A 1 2313 ? 186.927 250.730 221.934 1.00 2.65  ? 2313 GLU A CG    1 
ATOM   6858  C  CD    . GLU A 1 2313 ? 186.821 251.449 220.613 1.00 15.99 ? 2313 GLU A CD    1 
ATOM   6859  O  OE1   . GLU A 1 2313 ? 186.473 250.797 219.604 1.00 16.62 ? 2313 GLU A OE1   1 
ATOM   6860  O  OE2   . GLU A 1 2313 ? 187.082 252.670 220.579 1.00 14.66 ? 2313 GLU A OE2   1 
ATOM   6861  N  N     . ASN A 1 2314 ? 186.453 246.125 223.300 1.00 0.89  ? 2314 ASN A N     1 
ATOM   6862  C  CA    . ASN A 1 2314 ? 185.776 244.877 223.630 1.00 0.44  ? 2314 ASN A CA    1 
ATOM   6863  C  C     . ASN A 1 2314 ? 185.271 244.862 225.065 1.00 0.26  ? 2314 ASN A C     1 
ATOM   6864  O  O     . ASN A 1 2314 ? 184.444 244.010 225.405 1.00 0.39  ? 2314 ASN A O     1 
ATOM   6865  C  CB    . ASN A 1 2314 ? 186.708 243.685 223.411 1.00 0.66  ? 2314 ASN A CB    1 
ATOM   6866  C  CG    . ASN A 1 2314 ? 186.854 243.315 221.950 1.00 1.40  ? 2314 ASN A CG    1 
ATOM   6867  O  OD1   . ASN A 1 2314 ? 187.013 244.180 221.092 1.00 4.16  ? 2314 ASN A OD1   1 
ATOM   6868  N  ND2   . ASN A 1 2314 ? 186.803 242.023 221.662 1.00 0.26  ? 2314 ASN A ND2   1 
ATOM   6869  N  N     . LEU A 1 2315 ? 185.751 245.775 225.904 1.00 0.29  ? 2315 LEU A N     1 
ATOM   6870  C  CA    . LEU A 1 2315 ? 185.351 245.871 227.300 1.00 0.23  ? 2315 LEU A CA    1 
ATOM   6871  C  C     . LEU A 1 2315 ? 184.324 246.967 227.543 1.00 0.26  ? 2315 LEU A C     1 
ATOM   6872  O  O     . LEU A 1 2315 ? 184.050 247.294 228.700 1.00 0.37  ? 2315 LEU A O     1 
ATOM   6873  C  CB    . LEU A 1 2315 ? 186.579 246.112 228.180 1.00 0.17  ? 2315 LEU A CB    1 
ATOM   6874  C  CG    . LEU A 1 2315 ? 187.679 245.051 228.151 1.00 0.11  ? 2315 LEU A CG    1 
ATOM   6875  C  CD1   . LEU A 1 2315 ? 188.901 245.536 228.914 1.00 0.08  ? 2315 LEU A CD1   1 
ATOM   6876  C  CD2   . LEU A 1 2315 ? 187.172 243.741 228.722 1.00 0.07  ? 2315 LEU A CD2   1 
ATOM   6877  N  N     . ASN A 1 2316 ? 183.754 247.545 226.482 1.00 0.51  ? 2316 ASN A N     1 
ATOM   6878  C  CA    . ASN A 1 2316 ? 182.771 248.611 226.661 1.00 0.49  ? 2316 ASN A CA    1 
ATOM   6879  C  C     . ASN A 1 2316 ? 181.568 248.117 227.452 1.00 0.38  ? 2316 ASN A C     1 
ATOM   6880  O  O     . ASN A 1 2316 ? 181.099 248.792 228.372 1.00 0.78  ? 2316 ASN A O     1 
ATOM   6881  C  CB    . ASN A 1 2316 ? 182.338 249.169 225.305 1.00 0.84  ? 2316 ASN A CB    1 
ATOM   6882  C  CG    . ASN A 1 2316 ? 183.289 250.217 224.773 1.00 1.45  ? 2316 ASN A CG    1 
ATOM   6883  O  OD1   . ASN A 1 2316 ? 184.257 250.587 225.434 1.00 3.04  ? 2316 ASN A OD1   1 
ATOM   6884  N  ND2   . ASN A 1 2316 ? 183.017 250.705 223.569 1.00 1.99  ? 2316 ASN A ND2   1 
ATOM   6885  N  N     . SER A 1 2317 ? 181.066 246.927 227.119 1.00 0.41  ? 2317 SER A N     1 
ATOM   6886  C  CA    . SER A 1 2317 ? 179.959 246.359 227.879 1.00 0.47  ? 2317 SER A CA    1 
ATOM   6887  C  C     . SER A 1 2317 ? 180.402 245.832 229.238 1.00 0.36  ? 2317 SER A C     1 
ATOM   6888  O  O     . SER A 1 2317 ? 179.553 245.601 230.104 1.00 0.81  ? 2317 SER A O     1 
ATOM   6889  C  CB    . SER A 1 2317 ? 179.279 245.248 227.076 1.00 0.44  ? 2317 SER A CB    1 
ATOM   6890  O  OG    . SER A 1 2317 ? 180.189 244.213 226.750 1.00 0.44  ? 2317 SER A OG    1 
ATOM   6891  N  N     . VAL A 1 2318 ? 181.705 245.625 229.442 1.00 0.32  ? 2318 VAL A N     1 
ATOM   6892  C  CA    . VAL A 1 2318 ? 182.205 245.229 230.753 1.00 0.34  ? 2318 VAL A CA    1 
ATOM   6893  C  C     . VAL A 1 2318 ? 182.299 246.436 231.678 1.00 0.26  ? 2318 VAL A C     1 
ATOM   6894  O  O     . VAL A 1 2318 ? 181.911 246.373 232.851 1.00 0.32  ? 2318 VAL A O     1 
ATOM   6895  C  CB    . VAL A 1 2318 ? 183.569 244.523 230.619 1.00 0.37  ? 2318 VAL A CB    1 
ATOM   6896  C  CG1   . VAL A 1 2318 ? 184.108 244.135 231.987 1.00 0.12  ? 2318 VAL A CG1   1 
ATOM   6897  C  CG2   . VAL A 1 2318 ? 183.455 243.303 229.727 1.00 0.14  ? 2318 VAL A CG2   1 
ATOM   6898  N  N     . LEU A 1 2319 ? 182.811 247.551 231.165 1.00 0.40  ? 2319 LEU A N     1 
ATOM   6899  C  CA    . LEU A 1 2319 ? 183.076 248.725 231.984 1.00 0.45  ? 2319 LEU A CA    1 
ATOM   6900  C  C     . LEU A 1 2319 ? 181.844 249.589 232.230 1.00 1.13  ? 2319 LEU A C     1 
ATOM   6901  O  O     . LEU A 1 2319 ? 181.879 250.430 233.133 1.00 2.26  ? 2319 LEU A O     1 
ATOM   6902  C  CB    . LEU A 1 2319 ? 184.174 249.565 231.334 1.00 0.65  ? 2319 LEU A CB    1 
ATOM   6903  C  CG    . LEU A 1 2319 ? 185.501 248.838 231.099 1.00 0.22  ? 2319 LEU A CG    1 
ATOM   6904  C  CD1   . LEU A 1 2319 ? 186.456 249.692 230.288 1.00 0.57  ? 2319 LEU A CD1   1 
ATOM   6905  C  CD2   . LEU A 1 2319 ? 186.132 248.420 232.416 1.00 0.12  ? 2319 LEU A CD2   1 
ATOM   6906  N  N     . ASP A 1 2320 ? 180.764 249.413 231.472 1.00 1.03  ? 2320 ASP A N     1 
ATOM   6907  C  CA    . ASP A 1 2320 ? 179.551 250.180 231.714 1.00 1.94  ? 2320 ASP A CA    1 
ATOM   6908  C  C     . ASP A 1 2320 ? 178.642 249.402 232.666 1.00 2.18  ? 2320 ASP A C     1 
ATOM   6909  O  O     . ASP A 1 2320 ? 179.052 248.424 233.296 1.00 1.99  ? 2320 ASP A O     1 
ATOM   6910  C  CB    . ASP A 1 2320 ? 178.849 250.539 230.402 1.00 1.62  ? 2320 ASP A CB    1 
ATOM   6911  C  CG    . ASP A 1 2320 ? 178.500 249.329 229.558 1.00 3.28  ? 2320 ASP A CG    1 
ATOM   6912  O  OD1   . ASP A 1 2320 ? 178.531 248.194 230.074 1.00 5.47  ? 2320 ASP A OD1   1 
ATOM   6913  O  OD2   . ASP A 1 2320 ? 178.187 249.517 228.365 1.00 3.08  ? 2320 ASP A OD2   1 
ATOM   6914  N  N     . ASP A 1 2321 ? 177.387 249.839 232.783 1.00 3.05  ? 2321 ASP A N     1 
ATOM   6915  C  CA    . ASP A 1 2321 ? 176.467 249.231 233.737 1.00 3.82  ? 2321 ASP A CA    1 
ATOM   6916  C  C     . ASP A 1 2321 ? 176.010 247.838 233.320 1.00 2.35  ? 2321 ASP A C     1 
ATOM   6917  O  O     . ASP A 1 2321 ? 175.429 247.124 234.143 1.00 6.83  ? 2321 ASP A O     1 
ATOM   6918  C  CB    . ASP A 1 2321 ? 175.262 250.152 233.949 1.00 7.51  ? 2321 ASP A CB    1 
ATOM   6919  C  CG    . ASP A 1 2321 ? 174.447 250.364 232.683 1.00 18.61 ? 2321 ASP A CG    1 
ATOM   6920  O  OD1   . ASP A 1 2321 ? 174.825 249.839 231.614 1.00 18.02 ? 2321 ASP A OD1   1 
ATOM   6921  O  OD2   . ASP A 1 2321 ? 173.422 251.074 232.757 1.00 19.22 ? 2321 ASP A OD2   1 
ATOM   6922  N  N     . ASN A 1 2322 ? 176.254 247.436 232.069 1.00 2.15  ? 2322 ASN A N     1 
ATOM   6923  C  CA    . ASN A 1 2322 ? 175.923 246.077 231.652 1.00 1.66  ? 2322 ASN A CA    1 
ATOM   6924  C  C     . ASN A 1 2322 ? 176.731 245.046 232.432 1.00 1.24  ? 2322 ASN A C     1 
ATOM   6925  O  O     . ASN A 1 2322 ? 176.200 243.998 232.817 1.00 1.18  ? 2322 ASN A O     1 
ATOM   6926  C  CB    . ASN A 1 2322 ? 176.155 245.905 230.151 1.00 2.04  ? 2322 ASN A CB    1 
ATOM   6927  C  CG    . ASN A 1 2322 ? 175.160 246.676 229.314 1.00 1.54  ? 2322 ASN A CG    1 
ATOM   6928  O  OD1   . ASN A 1 2322 ? 173.961 246.412 229.363 1.00 1.84  ? 2322 ASN A OD1   1 
ATOM   6929  N  ND2   . ASN A 1 2322 ? 175.652 247.633 228.540 1.00 2.39  ? 2322 ASN A ND2   1 
ATOM   6930  N  N     . LYS A 1 2323 ? 178.013 245.329 232.673 1.00 1.10  ? 2323 LYS A N     1 
ATOM   6931  C  CA    . LYS A 1 2323 ? 178.910 244.419 233.389 1.00 0.89  ? 2323 LYS A CA    1 
ATOM   6932  C  C     . LYS A 1 2323 ? 178.935 243.042 232.733 1.00 0.41  ? 2323 LYS A C     1 
ATOM   6933  O  O     . LYS A 1 2323 ? 178.912 242.008 233.400 1.00 0.55  ? 2323 LYS A O     1 
ATOM   6934  C  CB    . LYS A 1 2323 ? 178.528 244.313 234.865 1.00 1.08  ? 2323 LYS A CB    1 
ATOM   6935  C  CG    . LYS A 1 2323 ? 178.710 245.595 235.653 1.00 1.22  ? 2323 LYS A CG    1 
ATOM   6936  C  CD    . LYS A 1 2323 ? 178.181 245.445 237.066 1.00 1.89  ? 2323 LYS A CD    1 
ATOM   6937  C  CE    . LYS A 1 2323 ? 178.376 246.718 237.869 1.00 8.95  ? 2323 LYS A CE    1 
ATOM   6938  N  NZ    . LYS A 1 2323 ? 177.964 246.553 239.286 1.00 14.75 ? 2323 LYS A NZ    1 
ATOM   6939  N  N     . LEU A 1 2324 ? 178.973 243.031 231.403 1.00 0.57  ? 2324 LEU A N     1 
ATOM   6940  C  CA    . LEU A 1 2324 ? 178.904 241.802 230.628 1.00 0.43  ? 2324 LEU A CA    1 
ATOM   6941  C  C     . LEU A 1 2324 ? 180.040 241.772 229.619 1.00 0.27  ? 2324 LEU A C     1 
ATOM   6942  O  O     . LEU A 1 2324 ? 180.259 242.748 228.898 1.00 0.61  ? 2324 LEU A O     1 
ATOM   6943  C  CB    . LEU A 1 2324 ? 177.560 241.688 229.904 1.00 0.87  ? 2324 LEU A CB    1 
ATOM   6944  C  CG    . LEU A 1 2324 ? 176.370 241.171 230.710 1.00 0.65  ? 2324 LEU A CG    1 
ATOM   6945  C  CD1   . LEU A 1 2324 ? 175.085 241.390 229.934 1.00 0.98  ? 2324 LEU A CD1   1 
ATOM   6946  C  CD2   . LEU A 1 2324 ? 176.545 239.703 231.063 1.00 0.50  ? 2324 LEU A CD2   1 
ATOM   6947  N  N     . LEU A 1 2325 ? 180.758 240.656 229.573 1.00 0.24  ? 2325 LEU A N     1 
ATOM   6948  C  CA    . LEU A 1 2325 ? 181.702 240.374 228.499 1.00 0.15  ? 2325 LEU A CA    1 
ATOM   6949  C  C     . LEU A 1 2325 ? 180.965 239.543 227.459 1.00 0.24  ? 2325 LEU A C     1 
ATOM   6950  O  O     . LEU A 1 2325 ? 180.600 238.393 227.719 1.00 0.66  ? 2325 LEU A O     1 
ATOM   6951  C  CB    . LEU A 1 2325 ? 182.939 239.644 229.016 1.00 0.15  ? 2325 LEU A CB    1 
ATOM   6952  C  CG    . LEU A 1 2325 ? 183.943 239.206 227.946 1.00 0.10  ? 2325 LEU A CG    1 
ATOM   6953  C  CD1   . LEU A 1 2325 ? 184.644 240.405 227.330 1.00 0.08  ? 2325 LEU A CD1   1 
ATOM   6954  C  CD2   . LEU A 1 2325 ? 184.951 238.217 228.511 1.00 0.15  ? 2325 LEU A CD2   1 
ATOM   6955  N  N     . THR A 1 2326 ? 180.731 240.127 226.290 1.00 0.15  ? 2326 THR A N     1 
ATOM   6956  C  CA    . THR A 1 2326 ? 179.999 239.457 225.226 1.00 0.56  ? 2326 THR A CA    1 
ATOM   6957  C  C     . THR A 1 2326 ? 180.984 238.864 224.231 1.00 0.45  ? 2326 THR A C     1 
ATOM   6958  O  O     . THR A 1 2326 ? 181.906 239.547 223.776 1.00 0.66  ? 2326 THR A O     1 
ATOM   6959  C  CB    . THR A 1 2326 ? 179.039 240.416 224.520 1.00 0.57  ? 2326 THR A CB    1 
ATOM   6960  O  OG1   . THR A 1 2326 ? 179.781 241.482 223.920 1.00 2.00  ? 2326 THR A OG1   1 
ATOM   6961  C  CG2   . THR A 1 2326 ? 178.047 240.992 225.513 1.00 0.17  ? 2326 THR A CG2   1 
ATOM   6962  N  N     . LEU A 1 2327 ? 180.787 237.604 223.904 1.00 0.44  ? 2327 LEU A N     1 
ATOM   6963  C  CA    . LEU A 1 2327 ? 181.668 236.886 223.011 1.00 0.80  ? 2327 LEU A CA    1 
ATOM   6964  C  C     . LEU A 1 2327 ? 180.957 236.589 221.695 1.00 1.14  ? 2327 LEU A C     1 
ATOM   6965  O  O     . LEU A 1 2327 ? 179.730 236.446 221.666 1.00 1.69  ? 2327 LEU A O     1 
ATOM   6966  C  CB    . LEU A 1 2327 ? 182.133 235.577 223.660 1.00 2.60  ? 2327 LEU A CB    1 
ATOM   6967  C  CG    . LEU A 1 2327 ? 183.035 235.704 224.890 1.00 0.94  ? 2327 LEU A CG    1 
ATOM   6968  C  CD1   . LEU A 1 2327 ? 183.482 234.334 225.369 1.00 0.47  ? 2327 LEU A CD1   1 
ATOM   6969  C  CD2   . LEU A 1 2327 ? 184.232 236.596 224.608 1.00 0.18  ? 2327 LEU A CD2   1 
ATOM   6970  N  N     . PRO A 1 2328 ? 181.693 236.496 220.585 1.00 1.93  ? 2328 PRO A N     1 
ATOM   6971  C  CA    . PRO A 1 2328 ? 181.038 236.235 219.292 1.00 0.97  ? 2328 PRO A CA    1 
ATOM   6972  C  C     . PRO A 1 2328 ? 180.307 234.903 219.213 1.00 2.40  ? 2328 PRO A C     1 
ATOM   6973  O  O     . PRO A 1 2328 ? 179.455 234.743 218.330 1.00 6.57  ? 2328 PRO A O     1 
ATOM   6974  C  CB    . PRO A 1 2328 ? 182.200 236.309 218.290 1.00 0.90  ? 2328 PRO A CB    1 
ATOM   6975  C  CG    . PRO A 1 2328 ? 183.426 236.084 219.113 1.00 1.07  ? 2328 PRO A CG    1 
ATOM   6976  C  CD    . PRO A 1 2328 ? 183.129 236.769 220.411 1.00 1.31  ? 2328 PRO A CD    1 
ATOM   6977  N  N     . ASN A 1 2329 ? 180.596 233.942 220.091 1.00 1.43  ? 2329 ASN A N     1 
ATOM   6978  C  CA    . ASN A 1 2329 ? 179.817 232.709 220.110 1.00 1.50  ? 2329 ASN A CA    1 
ATOM   6979  C  C     . ASN A 1 2329 ? 178.465 232.872 220.795 1.00 1.37  ? 2329 ASN A C     1 
ATOM   6980  O  O     . ASN A 1 2329 ? 177.780 231.871 221.018 1.00 1.89  ? 2329 ASN A O     1 
ATOM   6981  C  CB    . ASN A 1 2329 ? 180.601 231.573 220.779 1.00 2.63  ? 2329 ASN A CB    1 
ATOM   6982  C  CG    . ASN A 1 2329 ? 180.881 231.826 222.256 1.00 2.23  ? 2329 ASN A CG    1 
ATOM   6983  O  OD1   . ASN A 1 2329 ? 180.558 232.881 222.797 1.00 3.17  ? 2329 ASN A OD1   1 
ATOM   6984  N  ND2   . ASN A 1 2329 ? 181.487 230.846 222.911 1.00 3.69  ? 2329 ASN A ND2   1 
ATOM   6985  N  N     . GLY A 1 2330 ? 178.070 234.099 221.134 1.00 1.22  ? 2330 GLY A N     1 
ATOM   6986  C  CA    . GLY A 1 2330 ? 176.807 234.357 221.787 1.00 1.01  ? 2330 GLY A CA    1 
ATOM   6987  C  C     . GLY A 1 2330 ? 176.846 234.303 223.298 1.00 1.69  ? 2330 GLY A C     1 
ATOM   6988  O  O     . GLY A 1 2330 ? 175.853 234.664 223.939 1.00 2.17  ? 2330 GLY A O     1 
ATOM   6989  N  N     . GLU A 1 2331 ? 177.957 233.872 223.883 1.00 1.94  ? 2331 GLU A N     1 
ATOM   6990  C  CA    . GLU A 1 2331 ? 178.069 233.751 225.327 1.00 1.85  ? 2331 GLU A CA    1 
ATOM   6991  C  C     . GLU A 1 2331 ? 178.253 235.123 225.966 1.00 1.53  ? 2331 GLU A C     1 
ATOM   6992  O  O     . GLU A 1 2331 ? 178.907 236.005 225.404 1.00 1.36  ? 2331 GLU A O     1 
ATOM   6993  C  CB    . GLU A 1 2331 ? 179.240 232.838 225.687 1.00 1.47  ? 2331 GLU A CB    1 
ATOM   6994  C  CG    . GLU A 1 2331 ? 179.012 231.971 226.904 1.00 3.79  ? 2331 GLU A CG    1 
ATOM   6995  C  CD    . GLU A 1 2331 ? 180.285 231.303 227.383 1.00 11.08 ? 2331 GLU A CD    1 
ATOM   6996  O  OE1   . GLU A 1 2331 ? 181.076 230.851 226.528 1.00 8.31  ? 2331 GLU A OE1   1 
ATOM   6997  O  OE2   . GLU A 1 2331 ? 180.492 231.229 228.611 1.00 18.23 ? 2331 GLU A OE2   1 
ATOM   6998  N  N     . ARG A 1 2332 ? 177.660 235.303 227.143 1.00 1.65  ? 2332 ARG A N     1 
ATOM   6999  C  CA    . ARG A 1 2332 ? 177.744 236.554 227.887 1.00 1.27  ? 2332 ARG A CA    1 
ATOM   7000  C  C     . ARG A 1 2332 ? 178.170 236.247 229.315 1.00 1.26  ? 2332 ARG A C     1 
ATOM   7001  O  O     . ARG A 1 2332 ? 177.472 235.523 230.031 1.00 2.37  ? 2332 ARG A O     1 
ATOM   7002  C  CB    . ARG A 1 2332 ? 176.405 237.298 227.861 1.00 1.63  ? 2332 ARG A CB    1 
ATOM   7003  C  CG    . ARG A 1 2332 ? 175.883 237.567 226.455 1.00 4.08  ? 2332 ARG A CG    1 
ATOM   7004  C  CD    . ARG A 1 2332 ? 174.392 237.833 226.438 1.00 3.00  ? 2332 ARG A CD    1 
ATOM   7005  N  NE    . ARG A 1 2332 ? 174.083 239.255 226.513 1.00 1.64  ? 2332 ARG A NE    1 
ATOM   7006  C  CZ    . ARG A 1 2332 ? 173.201 239.784 227.351 1.00 4.36  ? 2332 ARG A CZ    1 
ATOM   7007  N  NH1   . ARG A 1 2332 ? 172.514 239.033 228.196 1.00 2.79  ? 2332 ARG A NH1   1 
ATOM   7008  N  NH2   . ARG A 1 2332 ? 173.005 241.099 227.340 1.00 0.68  ? 2332 ARG A NH2   1 
ATOM   7009  N  N     . LEU A 1 2333 ? 179.308 236.798 229.725 1.00 1.07  ? 2333 LEU A N     1 
ATOM   7010  C  CA    . LEU A 1 2333 ? 179.870 236.554 231.048 1.00 0.67  ? 2333 LEU A CA    1 
ATOM   7011  C  C     . LEU A 1 2333 ? 179.628 237.774 231.928 1.00 0.53  ? 2333 LEU A C     1 
ATOM   7012  O  O     . LEU A 1 2333 ? 180.072 238.878 231.601 1.00 0.95  ? 2333 LEU A O     1 
ATOM   7013  C  CB    . LEU A 1 2333 ? 181.366 236.243 230.957 1.00 0.40  ? 2333 LEU A CB    1 
ATOM   7014  C  CG    . LEU A 1 2333 ? 181.801 234.894 230.370 1.00 0.72  ? 2333 LEU A CG    1 
ATOM   7015  C  CD1   . LEU A 1 2333 ? 181.727 234.884 228.851 1.00 1.30  ? 2333 LEU A CD1   1 
ATOM   7016  C  CD2   . LEU A 1 2333 ? 183.202 234.540 230.836 1.00 0.29  ? 2333 LEU A CD2   1 
ATOM   7017  N  N     . SER A 1 2334 ? 178.928 237.570 233.040 1.00 0.90  ? 2334 SER A N     1 
ATOM   7018  C  CA    . SER A 1 2334 ? 178.635 238.654 233.967 1.00 0.30  ? 2334 SER A CA    1 
ATOM   7019  C  C     . SER A 1 2334 ? 179.823 238.915 234.881 1.00 0.68  ? 2334 SER A C     1 
ATOM   7020  O  O     . SER A 1 2334 ? 180.459 237.984 235.379 1.00 2.38  ? 2334 SER A O     1 
ATOM   7021  C  CB    . SER A 1 2334 ? 177.401 238.323 234.806 1.00 0.69  ? 2334 SER A CB    1 
ATOM   7022  O  OG    . SER A 1 2334 ? 176.276 238.068 233.988 1.00 5.73  ? 2334 SER A OG    1 
ATOM   7023  N  N     . LEU A 1 2335 ? 180.118 240.188 235.102 1.00 0.63  ? 2335 LEU A N     1 
ATOM   7024  C  CA    . LEU A 1 2335 ? 181.191 240.560 236.012 1.00 0.47  ? 2335 LEU A CA    1 
ATOM   7025  C  C     . LEU A 1 2335 ? 180.718 240.408 237.453 1.00 1.52  ? 2335 LEU A C     1 
ATOM   7026  O  O     . LEU A 1 2335 ? 179.754 241.070 237.849 1.00 1.29  ? 2335 LEU A O     1 
ATOM   7027  C  CB    . LEU A 1 2335 ? 181.640 241.990 235.754 1.00 0.29  ? 2335 LEU A CB    1 
ATOM   7028  C  CG    . LEU A 1 2335 ? 183.049 242.340 236.231 1.00 0.43  ? 2335 LEU A CG    1 
ATOM   7029  C  CD1   . LEU A 1 2335 ? 184.086 241.540 235.457 1.00 0.16  ? 2335 LEU A CD1   1 
ATOM   7030  C  CD2   . LEU A 1 2335 ? 183.309 243.832 236.101 1.00 0.48  ? 2335 LEU A CD2   1 
ATOM   7031  N  N     . PRO A 1 2336 ? 181.355 239.558 238.259 1.00 0.59  ? 2336 PRO A N     1 
ATOM   7032  C  CA    . PRO A 1 2336 ? 180.922 239.411 239.647 1.00 0.40  ? 2336 PRO A CA    1 
ATOM   7033  C  C     . PRO A 1 2336 ? 181.261 240.651 240.452 1.00 0.74  ? 2336 PRO A C     1 
ATOM   7034  O  O     . PRO A 1 2336 ? 182.200 241.392 240.114 1.00 0.75  ? 2336 PRO A O     1 
ATOM   7035  C  CB    . PRO A 1 2336 ? 181.717 238.186 240.139 1.00 0.55  ? 2336 PRO A CB    1 
ATOM   7036  C  CG    . PRO A 1 2336 ? 182.297 237.557 238.912 1.00 0.34  ? 2336 PRO A CG    1 
ATOM   7037  C  CD    . PRO A 1 2336 ? 182.471 238.661 237.929 1.00 0.43  ? 2336 PRO A CD    1 
ATOM   7038  N  N     . PRO A 1 2337 ? 180.523 240.920 241.533 1.00 0.80  ? 2337 PRO A N     1 
ATOM   7039  C  CA    . PRO A 1 2337 ? 180.764 242.150 242.306 1.00 0.38  ? 2337 PRO A CA    1 
ATOM   7040  C  C     . PRO A 1 2337 ? 182.137 242.225 242.954 1.00 0.55  ? 2337 PRO A C     1 
ATOM   7041  O  O     . PRO A 1 2337 ? 182.588 243.330 243.277 1.00 1.04  ? 2337 PRO A O     1 
ATOM   7042  C  CB    . PRO A 1 2337 ? 179.650 242.119 243.361 1.00 0.59  ? 2337 PRO A CB    1 
ATOM   7043  C  CG    . PRO A 1 2337 ? 179.293 240.675 243.475 1.00 0.65  ? 2337 PRO A CG    1 
ATOM   7044  C  CD    . PRO A 1 2337 ? 179.397 240.146 242.081 1.00 1.03  ? 2337 PRO A CD    1 
ATOM   7045  N  N     . ASN A 1 2338 ? 182.814 241.099 243.158 1.00 0.53  ? 2338 ASN A N     1 
ATOM   7046  C  CA    . ASN A 1 2338 ? 184.121 241.100 243.804 1.00 0.26  ? 2338 ASN A CA    1 
ATOM   7047  C  C     . ASN A 1 2338 ? 185.263 241.373 242.836 1.00 0.23  ? 2338 ASN A C     1 
ATOM   7048  O  O     . ASN A 1 2338 ? 186.420 241.420 243.267 1.00 0.27  ? 2338 ASN A O     1 
ATOM   7049  C  CB    . ASN A 1 2338 ? 184.356 239.764 244.515 1.00 0.40  ? 2338 ASN A CB    1 
ATOM   7050  C  CG    . ASN A 1 2338 ? 184.581 238.619 243.547 1.00 0.86  ? 2338 ASN A CG    1 
ATOM   7051  O  OD1   . ASN A 1 2338 ? 183.773 238.382 242.650 1.00 1.00  ? 2338 ASN A OD1   1 
ATOM   7052  N  ND2   . ASN A 1 2338 ? 185.683 237.902 243.725 1.00 0.72  ? 2338 ASN A ND2   1 
ATOM   7053  N  N     . VAL A 1 2339 ? 184.974 241.558 241.552 1.00 0.21  ? 2339 VAL A N     1 
ATOM   7054  C  CA    . VAL A 1 2339 ? 185.993 241.742 240.527 1.00 0.17  ? 2339 VAL A CA    1 
ATOM   7055  C  C     . VAL A 1 2339 ? 186.112 243.224 240.205 1.00 0.07  ? 2339 VAL A C     1 
ATOM   7056  O  O     . VAL A 1 2339 ? 185.101 243.916 240.038 1.00 0.11  ? 2339 VAL A O     1 
ATOM   7057  C  CB    . VAL A 1 2339 ? 185.664 240.927 239.263 1.00 0.11  ? 2339 VAL A CB    1 
ATOM   7058  C  CG1   . VAL A 1 2339 ? 186.632 241.266 238.143 1.00 0.05  ? 2339 VAL A CG1   1 
ATOM   7059  C  CG2   . VAL A 1 2339 ? 185.702 239.442 239.568 1.00 0.09  ? 2339 VAL A CG2   1 
ATOM   7060  N  N     . ARG A 1 2340 ? 187.346 243.712 240.133 1.00 0.03  ? 2340 ARG A N     1 
ATOM   7061  C  CA    . ARG A 1 2340 ? 187.645 245.049 239.642 1.00 0.05  ? 2340 ARG A CA    1 
ATOM   7062  C  C     . ARG A 1 2340 ? 188.497 244.928 238.389 1.00 0.03  ? 2340 ARG A C     1 
ATOM   7063  O  O     . ARG A 1 2340 ? 189.471 244.170 238.368 1.00 0.04  ? 2340 ARG A O     1 
ATOM   7064  C  CB    . ARG A 1 2340 ? 188.380 245.880 240.698 1.00 0.07  ? 2340 ARG A CB    1 
ATOM   7065  C  CG    . ARG A 1 2340 ? 187.555 246.219 241.918 1.00 0.08  ? 2340 ARG A CG    1 
ATOM   7066  C  CD    . ARG A 1 2340 ? 186.318 247.020 241.562 1.00 0.13  ? 2340 ARG A CD    1 
ATOM   7067  N  NE    . ARG A 1 2340 ? 185.502 247.296 242.738 1.00 1.06  ? 2340 ARG A NE    1 
ATOM   7068  C  CZ    . ARG A 1 2340 ? 184.791 246.389 243.393 1.00 0.69  ? 2340 ARG A CZ    1 
ATOM   7069  N  NH1   . ARG A 1 2340 ? 184.723 245.132 242.982 1.00 0.19  ? 2340 ARG A NH1   1 
ATOM   7070  N  NH2   . ARG A 1 2340 ? 184.128 246.751 244.487 1.00 0.84  ? 2340 ARG A NH2   1 
ATOM   7071  N  N     . ILE A 1 2341 ? 188.130 245.663 237.347 1.00 0.03  ? 2341 ILE A N     1 
ATOM   7072  C  CA    . ILE A 1 2341 ? 188.932 245.755 236.135 1.00 0.03  ? 2341 ILE A CA    1 
ATOM   7073  C  C     . ILE A 1 2341 ? 189.763 247.025 236.228 1.00 0.04  ? 2341 ILE A C     1 
ATOM   7074  O  O     . ILE A 1 2341 ? 189.218 248.130 236.305 1.00 0.14  ? 2341 ILE A O     1 
ATOM   7075  C  CB    . ILE A 1 2341 ? 188.060 245.748 234.871 1.00 0.01  ? 2341 ILE A CB    1 
ATOM   7076  C  CG1   . ILE A 1 2341 ? 187.136 244.528 234.863 1.00 0.01  ? 2341 ILE A CG1   1 
ATOM   7077  C  CG2   . ILE A 1 2341 ? 188.929 245.757 233.627 1.00 0.02  ? 2341 ILE A CG2   1 
ATOM   7078  C  CD1   . ILE A 1 2341 ? 187.863 243.207 234.953 1.00 0.01  ? 2341 ILE A CD1   1 
ATOM   7079  N  N     . MET A 1 2342 ? 191.083 246.870 236.232 1.00 0.03  ? 2342 MET A N     1 
ATOM   7080  C  CA    . MET A 1 2342 ? 191.999 247.982 236.413 1.00 0.03  ? 2342 MET A CA    1 
ATOM   7081  C  C     . MET A 1 2342 ? 192.927 248.101 235.214 1.00 0.04  ? 2342 MET A C     1 
ATOM   7082  O  O     . MET A 1 2342 ? 193.287 247.105 234.582 1.00 0.03  ? 2342 MET A O     1 
ATOM   7083  C  CB    . MET A 1 2342 ? 192.824 247.819 237.691 1.00 0.02  ? 2342 MET A CB    1 
ATOM   7084  C  CG    . MET A 1 2342 ? 191.999 247.597 238.945 1.00 0.02  ? 2342 MET A CG    1 
ATOM   7085  S  SD    . MET A 1 2342 ? 192.963 247.848 240.444 1.00 7.99  ? 2342 MET A SD    1 
ATOM   7086  C  CE    . MET A 1 2342 ? 191.664 248.075 241.648 1.00 0.34  ? 2342 MET A CE    1 
ATOM   7087  N  N     . PHE A 1 2343 ? 193.308 249.339 234.907 1.00 0.04  ? 2343 PHE A N     1 
ATOM   7088  C  CA    . PHE A 1 2343 ? 194.218 249.608 233.765 1.00 0.03  ? 2343 PHE A CA    1 
ATOM   7089  C  C     . PHE A 1 2343 ? 195.353 250.480 234.258 1.00 0.03  ? 2343 PHE A C     1 
ATOM   7090  O  O     . PHE A 1 2343 ? 195.114 251.673 234.529 1.00 0.05  ? 2343 PHE A O     1 
ATOM   7091  C  CB    . PHE A 1 2343 ? 193.462 250.316 232.638 1.00 0.02  ? 2343 PHE A CB    1 
ATOM   7092  C  CG    . PHE A 1 2343 ? 192.297 249.553 232.023 1.00 0.04  ? 2343 PHE A CG    1 
ATOM   7093  C  CD1   . PHE A 1 2343 ? 191.031 249.605 232.592 1.00 0.06  ? 2343 PHE A CD1   1 
ATOM   7094  C  CD2   . PHE A 1 2343 ? 192.468 248.812 230.859 1.00 0.02  ? 2343 PHE A CD2   1 
ATOM   7095  C  CE1   . PHE A 1 2343 ? 189.971 248.917 232.024 1.00 0.03  ? 2343 PHE A CE1   1 
ATOM   7096  C  CE2   . PHE A 1 2343 ? 191.404 248.126 230.296 1.00 0.03  ? 2343 PHE A CE2   1 
ATOM   7097  C  CZ    . PHE A 1 2343 ? 190.160 248.181 230.879 1.00 0.03  ? 2343 PHE A CZ    1 
ATOM   7098  N  N     . GLU A 1 2344 ? 196.551 249.912 234.399 1.00 0.03  ? 2344 GLU A N     1 
ATOM   7099  C  CA    . GLU A 1 2344 ? 197.736 250.723 234.784 1.00 0.03  ? 2344 GLU A CA    1 
ATOM   7100  C  C     . GLU A 1 2344 ? 198.437 251.150 233.493 1.00 0.03  ? 2344 GLU A C     1 
ATOM   7101  O  O     . GLU A 1 2344 ? 198.985 250.272 232.799 1.00 0.06  ? 2344 GLU A O     1 
ATOM   7102  C  CB    . GLU A 1 2344 ? 198.672 249.950 235.708 1.00 0.04  ? 2344 GLU A CB    1 
ATOM   7103  C  CG    . GLU A 1 2344 ? 199.775 250.815 236.307 1.00 0.03  ? 2344 GLU A CG    1 
ATOM   7104  C  CD    . GLU A 1 2344 ? 200.908 249.963 236.834 1.00 0.03  ? 2344 GLU A CD    1 
ATOM   7105  O  OE1   . GLU A 1 2344 ? 200.644 249.091 237.686 1.00 0.05  ? 2344 GLU A OE1   1 
ATOM   7106  O  OE2   . GLU A 1 2344 ? 202.053 250.174 236.395 1.00 0.04  ? 2344 GLU A OE2   1 
ATOM   7107  N  N     . VAL A 1 2345 ? 198.407 252.443 233.182 1.00 0.07  ? 2345 VAL A N     1 
ATOM   7108  C  CA    . VAL A 1 2345 ? 198.960 252.915 231.883 1.00 0.13  ? 2345 VAL A CA    1 
ATOM   7109  C  C     . VAL A 1 2345 ? 199.803 254.179 232.093 1.00 0.11  ? 2345 VAL A C     1 
ATOM   7110  O  O     . VAL A 1 2345 ? 199.610 254.851 233.121 1.00 0.06  ? 2345 VAL A O     1 
ATOM   7111  C  CB    . VAL A 1 2345 ? 197.790 253.179 230.914 1.00 0.18  ? 2345 VAL A CB    1 
ATOM   7112  C  CG1   . VAL A 1 2345 ? 196.885 251.963 230.764 1.00 0.06  ? 2345 VAL A CG1   1 
ATOM   7113  C  CG2   . VAL A 1 2345 ? 196.978 254.401 231.326 1.00 0.08  ? 2345 VAL A CG2   1 
ATOM   7114  N  N     . GLN A 1 2346 ? 200.690 254.485 231.148 1.00 1.29  ? 2346 GLN A N     1 
ATOM   7115  C  CA    . GLN A 1 2346 ? 201.490 255.699 231.219 1.00 0.98  ? 2346 GLN A CA    1 
ATOM   7116  C  C     . GLN A 1 2346 ? 200.849 256.873 230.497 1.00 0.70  ? 2346 GLN A C     1 
ATOM   7117  O  O     . GLN A 1 2346 ? 201.200 258.023 230.781 1.00 0.77  ? 2346 GLN A O     1 
ATOM   7118  C  CB    . GLN A 1 2346 ? 202.893 255.460 230.650 1.00 0.67  ? 2346 GLN A CB    1 
ATOM   7119  C  CG    . GLN A 1 2346 ? 202.922 254.816 229.279 1.00 3.42  ? 2346 GLN A CG    1 
ATOM   7120  C  CD    . GLN A 1 2346 ? 204.305 254.836 228.657 1.00 7.18  ? 2346 GLN A CD    1 
ATOM   7121  O  OE1   . GLN A 1 2346 ? 205.208 255.512 229.148 1.00 5.72  ? 2346 GLN A OE1   1 
ATOM   7122  N  NE2   . GLN A 1 2346 ? 204.479 254.083 227.579 1.00 8.64  ? 2346 GLN A NE2   1 
ATOM   7123  N  N     . ASP A 1 2347 ? 199.917 256.612 229.586 1.00 1.30  ? 2347 ASP A N     1 
ATOM   7124  C  CA    . ASP A 1 2347 ? 199.249 257.664 228.834 1.00 2.16  ? 2347 ASP A CA    1 
ATOM   7125  C  C     . ASP A 1 2347 ? 197.963 257.091 228.261 1.00 2.49  ? 2347 ASP A C     1 
ATOM   7126  O  O     . ASP A 1 2347 ? 197.744 255.879 228.265 1.00 2.51  ? 2347 ASP A O     1 
ATOM   7127  C  CB    . ASP A 1 2347 ? 200.156 258.226 227.731 1.00 2.78  ? 2347 ASP A CB    1 
ATOM   7128  C  CG    . ASP A 1 2347 ? 200.562 257.174 226.714 1.00 6.99  ? 2347 ASP A CG    1 
ATOM   7129  O  OD1   . ASP A 1 2347 ? 199.714 256.773 225.890 1.00 8.71  ? 2347 ASP A OD1   1 
ATOM   7130  O  OD2   . ASP A 1 2347 ? 201.730 256.740 226.746 1.00 5.99  ? 2347 ASP A OD2   1 
ATOM   7131  N  N     . LEU A 1 2348 ? 197.107 257.982 227.769 1.00 4.89  ? 2348 LEU A N     1 
ATOM   7132  C  CA    . LEU A 1 2348 ? 195.852 257.605 227.133 1.00 2.66  ? 2348 LEU A CA    1 
ATOM   7133  C  C     . LEU A 1 2348 ? 195.671 258.350 225.822 1.00 4.78  ? 2348 LEU A C     1 
ATOM   7134  O  O     . LEU A 1 2348 ? 194.552 258.699 225.433 1.00 14.58 ? 2348 LEU A O     1 
ATOM   7135  C  CB    . LEU A 1 2348 ? 194.668 257.855 228.062 1.00 2.65  ? 2348 LEU A CB    1 
ATOM   7136  C  CG    . LEU A 1 2348 ? 194.448 256.837 229.184 1.00 3.45  ? 2348 LEU A CG    1 
ATOM   7137  C  CD1   . LEU A 1 2348 ? 193.241 257.220 230.015 1.00 1.96  ? 2348 LEU A CD1   1 
ATOM   7138  C  CD2   . LEU A 1 2348 ? 194.290 255.436 228.614 1.00 1.16  ? 2348 LEU A CD2   1 
ATOM   7139  N  N     . LYS A 1 2349 ? 196.769 258.595 225.108 1.00 6.06  ? 2349 LYS A N     1 
ATOM   7140  C  CA    . LYS A 1 2349 ? 196.715 259.387 223.888 1.00 6.11  ? 2349 LYS A CA    1 
ATOM   7141  C  C     . LYS A 1 2349 ? 196.064 258.658 222.720 1.00 5.57  ? 2349 LYS A C     1 
ATOM   7142  O  O     . LYS A 1 2349 ? 195.808 259.286 221.688 1.00 12.08 ? 2349 LYS A O     1 
ATOM   7143  C  CB    . LYS A 1 2349 ? 198.121 259.845 223.491 1.00 6.74  ? 2349 LYS A CB    1 
ATOM   7144  C  CG    . LYS A 1 2349 ? 199.139 258.734 223.375 1.00 5.93  ? 2349 LYS A CG    1 
ATOM   7145  C  CD    . LYS A 1 2349 ? 200.390 259.213 222.659 1.00 10.17 ? 2349 LYS A CD    1 
ATOM   7146  C  CE    . LYS A 1 2349 ? 200.060 259.769 221.283 1.00 10.50 ? 2349 LYS A CE    1 
ATOM   7147  N  NZ    . LYS A 1 2349 ? 201.285 260.038 220.485 1.00 17.34 ? 2349 LYS A NZ    1 
ATOM   7148  N  N     . TYR A 1 2350 ? 195.791 257.361 222.847 1.00 2.82  ? 2350 TYR A N     1 
ATOM   7149  C  CA    . TYR A 1 2350 ? 195.069 256.625 221.822 1.00 1.61  ? 2350 TYR A CA    1 
ATOM   7150  C  C     . TYR A 1 2350 ? 193.718 256.105 222.287 1.00 3.97  ? 2350 TYR A C     1 
ATOM   7151  O  O     . TYR A 1 2350 ? 192.966 255.574 221.463 1.00 9.17  ? 2350 TYR A O     1 
ATOM   7152  C  CB    . TYR A 1 2350 ? 195.916 255.452 221.302 1.00 2.73  ? 2350 TYR A CB    1 
ATOM   7153  C  CG    . TYR A 1 2350 ? 197.219 255.898 220.688 1.00 3.22  ? 2350 TYR A CG    1 
ATOM   7154  C  CD1   . TYR A 1 2350 ? 197.262 256.409 219.398 1.00 2.26  ? 2350 TYR A CD1   1 
ATOM   7155  C  CD2   . TYR A 1 2350 ? 198.406 255.825 221.404 1.00 3.94  ? 2350 TYR A CD2   1 
ATOM   7156  C  CE1   . TYR A 1 2350 ? 198.449 256.828 218.837 1.00 2.90  ? 2350 TYR A CE1   1 
ATOM   7157  C  CE2   . TYR A 1 2350 ? 199.598 256.240 220.849 1.00 2.81  ? 2350 TYR A CE2   1 
ATOM   7158  C  CZ    . TYR A 1 2350 ? 199.614 256.740 219.566 1.00 3.25  ? 2350 TYR A CZ    1 
ATOM   7159  O  OH    . TYR A 1 2350 ? 200.800 257.155 219.010 1.00 8.87  ? 2350 TYR A OH    1 
ATOM   7160  N  N     . ALA A 1 2351 ? 193.387 256.243 223.567 1.00 5.98  ? 2351 ALA A N     1 
ATOM   7161  C  CA    . ALA A 1 2351 ? 192.078 255.828 224.050 1.00 3.51  ? 2351 ALA A CA    1 
ATOM   7162  C  C     . ALA A 1 2351 ? 191.005 256.805 223.589 1.00 3.59  ? 2351 ALA A C     1 
ATOM   7163  O  O     . ALA A 1 2351 ? 191.226 258.017 223.533 1.00 4.62  ? 2351 ALA A O     1 
ATOM   7164  C  CB    . ALA A 1 2351 ? 192.081 255.733 225.575 1.00 2.22  ? 2351 ALA A CB    1 
ATOM   7165  N  N     . THR A 1 2352 ? 189.837 256.272 223.256 1.00 5.69  ? 2352 THR A N     1 
ATOM   7166  C  CA    . THR A 1 2352 ? 188.719 257.098 222.829 1.00 2.99  ? 2352 THR A CA    1 
ATOM   7167  C  C     . THR A 1 2352 ? 187.877 257.524 224.029 1.00 2.95  ? 2352 THR A C     1 
ATOM   7168  O  O     . THR A 1 2352 ? 188.058 257.053 225.154 1.00 2.50  ? 2352 THR A O     1 
ATOM   7169  C  CB    . THR A 1 2352 ? 187.855 256.356 221.808 1.00 3.86  ? 2352 THR A CB    1 
ATOM   7170  O  OG1   . THR A 1 2352 ? 187.321 255.168 222.404 1.00 9.17  ? 2352 THR A OG1   1 
ATOM   7171  C  CG2   . THR A 1 2352 ? 188.680 255.984 220.586 1.00 2.72  ? 2352 THR A CG2   1 
ATOM   7172  N  N     . LEU A 1 2353 ? 186.914 258.415 223.784 1.00 4.34  ? 2353 LEU A N     1 
ATOM   7173  C  CA    . LEU A 1 2353 ? 186.026 258.895 224.877 1.00 2.64  ? 2353 LEU A CA    1 
ATOM   7174  C  C     . LEU A 1 2353 ? 185.211 257.716 225.429 1.00 3.15  ? 2353 LEU A C     1 
ATOM   7175  O  O     . LEU A 1 2353 ? 184.996 257.664 226.658 1.00 2.05  ? 2353 LEU A O     1 
ATOM   7176  C  CB    . LEU A 1 2353 ? 185.126 260.004 224.335 1.00 3.08  ? 2353 LEU A CB    1 
ATOM   7177  C  CG    . LEU A 1 2353 ? 184.277 260.760 225.362 1.00 5.88  ? 2353 LEU A CG    1 
ATOM   7178  C  CD1   . LEU A 1 2353 ? 183.862 262.104 224.791 1.00 13.06 ? 2353 LEU A CD1   1 
ATOM   7179  C  CD2   . LEU A 1 2353 ? 183.046 259.966 225.761 1.00 10.79 ? 2353 LEU A CD2   1 
ATOM   7180  N  N     . ALA A 1 2354 ? 184.791 256.800 224.554 1.00 3.10  ? 2354 ALA A N     1 
ATOM   7181  C  CA    . ALA A 1 2354 ? 183.958 255.656 224.988 1.00 3.80  ? 2354 ALA A CA    1 
ATOM   7182  C  C     . ALA A 1 2354 ? 184.628 254.944 226.165 1.00 5.94  ? 2354 ALA A C     1 
ATOM   7183  O  O     . ALA A 1 2354 ? 183.925 254.599 227.137 1.00 4.58  ? 2354 ALA A O     1 
ATOM   7184  C  CB    . ALA A 1 2354 ? 183.741 254.719 223.827 1.00 3.71  ? 2354 ALA A CB    1 
ATOM   7185  N  N     . THR A 1 2355 ? 185.945 254.747 226.086 1.00 4.41  ? 2355 THR A N     1 
ATOM   7186  C  CA    . THR A 1 2355 ? 186.674 254.034 227.152 1.00 1.68  ? 2355 THR A CA    1 
ATOM   7187  C  C     . THR A 1 2355 ? 186.909 254.967 228.317 1.00 1.58  ? 2355 THR A C     1 
ATOM   7188  O  O     . THR A 1 2355 ? 186.665 254.542 229.466 1.00 2.09  ? 2355 THR A O     1 
ATOM   7189  C  CB    . THR A 1 2355 ? 187.986 253.489 226.588 1.00 1.10  ? 2355 THR A CB    1 
ATOM   7190  O  OG1   . THR A 1 2355 ? 187.612 252.613 225.531 1.00 3.26  ? 2355 THR A OG1   1 
ATOM   7191  C  CG2   . THR A 1 2355 ? 188.795 252.733 227.627 1.00 0.53  ? 2355 THR A CG2   1 
ATOM   7192  N  N     . VAL A 1 2356 ? 187.343 256.199 228.049 1.00 1.87  ? 2356 VAL A N     1 
ATOM   7193  C  CA    . VAL A 1 2356 ? 187.692 257.096 229.149 1.00 1.68  ? 2356 VAL A CA    1 
ATOM   7194  C  C     . VAL A 1 2356 ? 186.476 257.379 230.023 1.00 2.84  ? 2356 VAL A C     1 
ATOM   7195  O  O     . VAL A 1 2356 ? 186.573 257.406 231.254 1.00 3.71  ? 2356 VAL A O     1 
ATOM   7196  C  CB    . VAL A 1 2356 ? 188.318 258.393 228.603 1.00 3.25  ? 2356 VAL A CB    1 
ATOM   7197  C  CG1   . VAL A 1 2356 ? 188.584 259.379 229.727 1.00 2.67  ? 2356 VAL A CG1   1 
ATOM   7198  C  CG2   . VAL A 1 2356 ? 189.604 258.082 227.856 1.00 2.12  ? 2356 VAL A CG2   1 
ATOM   7199  N  N     . SER A 1 2357 ? 185.320 257.582 229.386 1.00 2.80  ? 2357 SER A N     1 
ATOM   7200  C  CA    . SER A 1 2357 ? 184.076 257.925 230.128 1.00 2.03  ? 2357 SER A CA    1 
ATOM   7201  C  C     . SER A 1 2357 ? 183.582 256.752 230.983 1.00 1.64  ? 2357 SER A C     1 
ATOM   7202  O  O     . SER A 1 2357 ? 182.844 257.009 231.955 1.00 2.09  ? 2357 SER A O     1 
ATOM   7203  C  CB    . SER A 1 2357 ? 183.001 258.367 229.170 1.00 2.55  ? 2357 SER A CB    1 
ATOM   7204  O  OG    . SER A 1 2357 ? 182.631 257.313 228.294 1.00 8.55  ? 2357 SER A OG    1 
ATOM   7205  N  N     . ARG A 1 2358 ? 183.969 255.522 230.648 1.00 1.60  ? 2358 ARG A N     1 
ATOM   7206  C  CA    . ARG A 1 2358 ? 183.426 254.340 231.369 1.00 1.92  ? 2358 ARG A CA    1 
ATOM   7207  C  C     . ARG A 1 2358 ? 184.321 253.930 232.546 1.00 1.66  ? 2358 ARG A C     1 
ATOM   7208  O  O     . ARG A 1 2358 ? 184.010 252.902 233.174 1.00 5.28  ? 2358 ARG A O     1 
ATOM   7209  C  CB    . ARG A 1 2358 ? 183.308 253.138 230.426 1.00 1.36  ? 2358 ARG A CB    1 
ATOM   7210  C  CG    . ARG A 1 2358 ? 182.158 253.124 229.432 1.00 1.22  ? 2358 ARG A CG    1 
ATOM   7211  C  CD    . ARG A 1 2358 ? 182.193 251.807 228.673 1.00 1.20  ? 2358 ARG A CD    1 
ATOM   7212  N  NE    . ARG A 1 2358 ? 181.016 251.563 227.834 1.00 1.86  ? 2358 ARG A NE    1 
ATOM   7213  C  CZ    . ARG A 1 2358 ? 180.657 252.286 226.783 1.00 0.98  ? 2358 ARG A CZ    1 
ATOM   7214  N  NH1   . ARG A 1 2358 ? 181.453 253.237 226.324 1.00 1.17  ? 2358 ARG A NH1   1 
ATOM   7215  N  NH2   . ARG A 1 2358 ? 179.505 252.046 226.187 1.00 1.33  ? 2358 ARG A NH2   1 
ATOM   7216  N  N     . CYS A 1 2359 ? 185.381 254.681 232.844 1.00 1.83  ? 2359 CYS A N     1 
ATOM   7217  C  CA    . CYS A 1 2359 ? 186.311 254.206 233.903 1.00 1.38  ? 2359 CYS A CA    1 
ATOM   7218  C  C     . CYS A 1 2359 ? 186.691 255.298 234.903 1.00 1.60  ? 2359 CYS A C     1 
ATOM   7219  O  O     . CYS A 1 2359 ? 186.963 256.433 234.459 1.00 9.11  ? 2359 CYS A O     1 
ATOM   7220  C  CB    . CYS A 1 2359 ? 187.623 253.706 233.309 1.00 1.22  ? 2359 CYS A CB    1 
ATOM   7221  S  SG    . CYS A 1 2359 ? 187.477 252.153 232.389 1.00 6.37  ? 2359 CYS A SG    1 
ATOM   7222  N  N     . GLY A 1 2360 ? 186.691 254.974 236.198 1.00 0.55  ? 2360 GLY A N     1 
ATOM   7223  C  CA    . GLY A 1 2360 ? 187.205 255.895 237.193 1.00 0.49  ? 2360 GLY A CA    1 
ATOM   7224  C  C     . GLY A 1 2360 ? 188.683 256.161 236.961 1.00 0.69  ? 2360 GLY A C     1 
ATOM   7225  O  O     . GLY A 1 2360 ? 189.450 255.260 236.620 1.00 0.45  ? 2360 GLY A O     1 
ATOM   7226  N  N     . MET A 1 2361 ? 189.080 257.414 237.132 1.00 1.40  ? 2361 MET A N     1 
ATOM   7227  C  CA    . MET A 1 2361 ? 190.434 257.845 236.825 1.00 0.57  ? 2361 MET A CA    1 
ATOM   7228  C  C     . MET A 1 2361 ? 191.148 258.269 238.096 1.00 0.22  ? 2361 MET A C     1 
ATOM   7229  O  O     . MET A 1 2361 ? 190.624 259.075 238.869 1.00 1.03  ? 2361 MET A O     1 
ATOM   7230  C  CB    . MET A 1 2361 ? 190.432 258.994 235.816 1.00 1.00  ? 2361 MET A CB    1 
ATOM   7231  C  CG    . MET A 1 2361 ? 189.901 258.622 234.451 1.00 2.25  ? 2361 MET A CG    1 
ATOM   7232  S  SD    . MET A 1 2361 ? 190.918 257.389 233.626 1.00 11.60 ? 2361 MET A SD    1 
ATOM   7233  C  CE    . MET A 1 2361 ? 189.901 257.023 232.205 1.00 5.50  ? 2361 MET A CE    1 
ATOM   7234  N  N     . VAL A 1 2362 ? 192.332 257.711 238.314 1.00 0.23  ? 2362 VAL A N     1 
ATOM   7235  C  CA    . VAL A 1 2362 ? 193.271 258.194 239.317 1.00 0.29  ? 2362 VAL A CA    1 
ATOM   7236  C  C     . VAL A 1 2362 ? 194.538 258.595 238.582 1.00 0.12  ? 2362 VAL A C     1 
ATOM   7237  O  O     . VAL A 1 2362 ? 195.206 257.747 237.979 1.00 0.09  ? 2362 VAL A O     1 
ATOM   7238  C  CB    . VAL A 1 2362 ? 193.570 257.142 240.396 1.00 0.13  ? 2362 VAL A CB    1 
ATOM   7239  C  CG1   . VAL A 1 2362 ? 194.441 257.745 241.483 1.00 0.20  ? 2362 VAL A CG1   1 
ATOM   7240  C  CG2   . VAL A 1 2362 ? 192.286 256.597 240.982 1.00 0.14  ? 2362 VAL A CG2   1 
ATOM   7241  N  N     . TRP A 1 2363 ? 194.864 259.881 238.620 1.00 0.19  ? 2363 TRP A N     1 
ATOM   7242  C  CA    . TRP A 1 2363 ? 196.018 260.417 237.915 1.00 0.12  ? 2363 TRP A CA    1 
ATOM   7243  C  C     . TRP A 1 2363 ? 197.224 260.430 238.839 1.00 0.05  ? 2363 TRP A C     1 
ATOM   7244  O  O     . TRP A 1 2363 ? 197.149 260.935 239.960 1.00 0.12  ? 2363 TRP A O     1 
ATOM   7245  C  CB    . TRP A 1 2363 ? 195.745 261.828 237.395 1.00 0.24  ? 2363 TRP A CB    1 
ATOM   7246  C  CG    . TRP A 1 2363 ? 196.995 262.573 237.039 1.00 0.08  ? 2363 TRP A CG    1 
ATOM   7247  C  CD1   . TRP A 1 2363 ? 197.626 263.519 237.789 1.00 0.12  ? 2363 TRP A CD1   1 
ATOM   7248  C  CD2   . TRP A 1 2363 ? 197.773 262.423 235.846 1.00 0.07  ? 2363 TRP A CD2   1 
ATOM   7249  N  NE1   . TRP A 1 2363 ? 198.744 263.972 237.139 1.00 0.18  ? 2363 TRP A NE1   1 
ATOM   7250  C  CE2   . TRP A 1 2363 ? 198.857 263.315 235.942 1.00 0.10  ? 2363 TRP A CE2   1 
ATOM   7251  C  CE3   . TRP A 1 2363 ? 197.653 261.626 234.705 1.00 0.08  ? 2363 TRP A CE3   1 
ATOM   7252  C  CZ2   . TRP A 1 2363 ? 199.817 263.434 234.941 1.00 0.11  ? 2363 TRP A CZ2   1 
ATOM   7253  C  CZ3   . TRP A 1 2363 ? 198.607 261.744 233.713 1.00 0.06  ? 2363 TRP A CZ3   1 
ATOM   7254  C  CH2   . TRP A 1 2363 ? 199.675 262.640 233.837 1.00 0.10  ? 2363 TRP A CH2   1 
ATOM   7255  N  N     . PHE A 1 2364 ? 198.329 259.875 238.364 1.00 0.05  ? 2364 PHE A N     1 
ATOM   7256  C  CA    . PHE A 1 2364 ? 199.601 259.931 239.061 1.00 0.06  ? 2364 PHE A CA    1 
ATOM   7257  C  C     . PHE A 1 2364 ? 200.513 260.886 238.307 1.00 0.11  ? 2364 PHE A C     1 
ATOM   7258  O  O     . PHE A 1 2364 ? 200.614 260.815 237.080 1.00 0.17  ? 2364 PHE A O     1 
ATOM   7259  C  CB    . PHE A 1 2364 ? 200.246 258.546 239.160 1.00 0.12  ? 2364 PHE A CB    1 
ATOM   7260  C  CG    . PHE A 1 2364 ? 199.547 257.608 240.106 1.00 0.01  ? 2364 PHE A CG    1 
ATOM   7261  C  CD1   . PHE A 1 2364 ? 198.270 257.144 239.830 1.00 0.02  ? 2364 PHE A CD1   1 
ATOM   7262  C  CD2   . PHE A 1 2364 ? 200.176 257.165 241.254 1.00 0.03  ? 2364 PHE A CD2   1 
ATOM   7263  C  CE1   . PHE A 1 2364 ? 197.635 256.281 240.685 1.00 0.02  ? 2364 PHE A CE1   1 
ATOM   7264  C  CE2   . PHE A 1 2364 ? 199.545 256.297 242.112 1.00 0.09  ? 2364 PHE A CE2   1 
ATOM   7265  C  CZ    . PHE A 1 2364 ? 198.271 255.855 241.829 1.00 0.02  ? 2364 PHE A CZ    1 
ATOM   7266  N  N     . SER A 1 2365 ? 201.149 261.792 239.034 1.00 0.86  ? 2365 SER A N     1 
ATOM   7267  C  CA    . SER A 1 2365 ? 202.180 262.640 238.466 1.00 1.38  ? 2365 SER A CA    1 
ATOM   7268  C  C     . SER A 1 2365 ? 203.546 262.149 238.921 1.00 2.98  ? 2365 SER A C     1 
ATOM   7269  O  O     . SER A 1 2365 ? 203.671 261.418 239.906 1.00 3.58  ? 2365 SER A O     1 
ATOM   7270  C  CB    . SER A 1 2365 ? 201.977 264.102 238.871 1.00 1.12  ? 2365 SER A CB    1 
ATOM   7271  O  OG    . SER A 1 2365 ? 202.164 264.281 240.262 1.00 3.92  ? 2365 SER A OG    1 
ATOM   7272  N  N     . GLU A 1 2366 ? 204.579 262.548 238.181 1.00 2.83  ? 2366 GLU A N     1 
ATOM   7273  C  CA    . GLU A 1 2366 ? 205.935 262.205 238.588 1.00 3.81  ? 2366 GLU A CA    1 
ATOM   7274  C  C     . GLU A 1 2366 ? 206.319 262.848 239.911 1.00 6.07  ? 2366 GLU A C     1 
ATOM   7275  O  O     . GLU A 1 2366 ? 207.279 262.398 240.545 1.00 15.46 ? 2366 GLU A O     1 
ATOM   7276  C  CB    . GLU A 1 2366 ? 206.928 262.603 237.496 1.00 6.47  ? 2366 GLU A CB    1 
ATOM   7277  C  CG    . GLU A 1 2366 ? 207.125 261.537 236.432 1.00 12.66 ? 2366 GLU A CG    1 
ATOM   7278  C  CD    . GLU A 1 2366 ? 208.239 261.873 235.458 1.00 22.53 ? 2366 GLU A CD    1 
ATOM   7279  O  OE1   . GLU A 1 2366 ? 208.159 262.931 234.800 1.00 21.73 ? 2366 GLU A OE1   1 
ATOM   7280  O  OE2   . GLU A 1 2366 ? 209.193 261.076 235.348 1.00 20.91 ? 2366 GLU A OE2   1 
ATOM   7281  N  N     . ASP A 1 2367 ? 205.594 263.880 240.342 1.00 5.17  ? 2367 ASP A N     1 
ATOM   7282  C  CA    . ASP A 1 2367 ? 205.838 264.481 241.647 1.00 3.90  ? 2367 ASP A CA    1 
ATOM   7283  C  C     . ASP A 1 2367 ? 205.270 263.638 242.780 1.00 3.51  ? 2367 ASP A C     1 
ATOM   7284  O  O     . ASP A 1 2367 ? 205.672 263.811 243.936 1.00 9.11  ? 2367 ASP A O     1 
ATOM   7285  C  CB    . ASP A 1 2367 ? 205.245 265.889 241.688 1.00 7.70  ? 2367 ASP A CB    1 
ATOM   7286  C  CG    . ASP A 1 2367 ? 205.988 266.857 240.790 1.00 19.06 ? 2367 ASP A CG    1 
ATOM   7287  O  OD1   . ASP A 1 2367 ? 207.203 266.661 240.579 1.00 20.58 ? 2367 ASP A OD1   1 
ATOM   7288  O  OD2   . ASP A 1 2367 ? 205.358 267.817 240.297 1.00 25.60 ? 2367 ASP A OD2   1 
ATOM   7289  N  N     . VAL A 1 2368 ? 204.341 262.732 242.474 1.00 4.01  ? 2368 VAL A N     1 
ATOM   7290  C  CA    . VAL A 1 2368 ? 203.776 261.858 243.500 1.00 2.30  ? 2368 VAL A CA    1 
ATOM   7291  C  C     . VAL A 1 2368 ? 204.860 260.968 244.094 1.00 2.66  ? 2368 VAL A C     1 
ATOM   7292  O  O     . VAL A 1 2368 ? 204.925 260.769 245.312 1.00 1.63  ? 2368 VAL A O     1 
ATOM   7293  C  CB    . VAL A 1 2368 ? 202.616 261.033 242.912 1.00 2.03  ? 2368 VAL A CB    1 
ATOM   7294  C  CG1   . VAL A 1 2368 ? 202.161 259.976 243.890 1.00 1.33  ? 2368 VAL A CG1   1 
ATOM   7295  C  CG2   . VAL A 1 2368 ? 201.461 261.945 242.541 1.00 4.57  ? 2368 VAL A CG2   1 
ATOM   7296  N  N     . LEU A 1 2369 ? 205.723 260.424 243.245 1.00 5.45  ? 2369 LEU A N     1 
ATOM   7297  C  CA    . LEU A 1 2369 ? 206.871 259.630 243.675 1.00 1.72  ? 2369 LEU A CA    1 
ATOM   7298  C  C     . LEU A 1 2369 ? 208.095 260.537 243.652 1.00 1.66  ? 2369 LEU A C     1 
ATOM   7299  O  O     . LEU A 1 2369 ? 208.630 260.845 242.587 1.00 6.43  ? 2369 LEU A O     1 
ATOM   7300  C  CB    . LEU A 1 2369 ? 207.049 258.416 242.772 1.00 1.47  ? 2369 LEU A CB    1 
ATOM   7301  C  CG    . LEU A 1 2369 ? 208.227 257.491 243.078 1.00 0.69  ? 2369 LEU A CG    1 
ATOM   7302  C  CD1   . LEU A 1 2369 ? 208.179 256.991 244.509 1.00 0.42  ? 2369 LEU A CD1   1 
ATOM   7303  C  CD2   . LEU A 1 2369 ? 208.240 256.341 242.101 1.00 0.32  ? 2369 LEU A CD2   1 
ATOM   7304  N  N     . SER A 1 2370 ? 208.532 260.970 244.829 1.00 1.61  ? 2370 SER A N     1 
ATOM   7305  C  CA    . SER A 1 2370 ? 209.688 261.843 244.928 1.00 2.57  ? 2370 SER A CA    1 
ATOM   7306  C  C     . SER A 1 2370 ? 210.983 261.036 244.858 1.00 3.25  ? 2370 SER A C     1 
ATOM   7307  O  O     . SER A 1 2370 ? 211.028 259.847 245.181 1.00 2.60  ? 2370 SER A O     1 
ATOM   7308  C  CB    . SER A 1 2370 ? 209.640 262.655 246.223 1.00 3.02  ? 2370 SER A CB    1 
ATOM   7309  O  OG    . SER A 1 2370 ? 209.916 261.842 247.348 1.00 2.00  ? 2370 SER A OG    1 
ATOM   7310  N  N     . THR A 1 2371 ? 212.049 261.708 244.419 1.00 2.95  ? 2371 THR A N     1 
ATOM   7311  C  CA    . THR A 1 2371 ? 213.349 261.051 244.320 1.00 2.35  ? 2371 THR A CA    1 
ATOM   7312  C  C     . THR A 1 2371 ? 213.875 260.648 245.692 1.00 3.52  ? 2371 THR A C     1 
ATOM   7313  O  O     . THR A 1 2371 ? 214.611 259.663 245.810 1.00 2.73  ? 2371 THR A O     1 
ATOM   7314  C  CB    . THR A 1 2371 ? 214.346 261.967 243.607 1.00 2.73  ? 2371 THR A CB    1 
ATOM   7315  O  OG1   . THR A 1 2371 ? 213.741 262.502 242.424 1.00 7.50  ? 2371 THR A OG1   1 
ATOM   7316  C  CG2   . THR A 1 2371 ? 215.590 261.199 243.214 1.00 2.65  ? 2371 THR A CG2   1 
ATOM   7317  N  N     . ASP A 1 2372 ? 213.497 261.386 246.736 1.00 6.62  ? 2372 ASP A N     1 
ATOM   7318  C  CA    . ASP A 1 2372 ? 213.849 260.991 248.095 1.00 3.75  ? 2372 ASP A CA    1 
ATOM   7319  C  C     . ASP A 1 2372 ? 213.220 259.650 248.457 1.00 3.29  ? 2372 ASP A C     1 
ATOM   7320  O  O     . ASP A 1 2372 ? 213.841 258.827 249.137 1.00 5.75  ? 2372 ASP A O     1 
ATOM   7321  C  CB    . ASP A 1 2372 ? 213.413 262.078 249.079 1.00 5.56  ? 2372 ASP A CB    1 
ATOM   7322  C  CG    . ASP A 1 2372 ? 213.798 261.763 250.509 1.00 16.89 ? 2372 ASP A CG    1 
ATOM   7323  O  OD1   . ASP A 1 2372 ? 214.862 261.143 250.718 1.00 25.17 ? 2372 ASP A OD1   1 
ATOM   7324  O  OD2   . ASP A 1 2372 ? 213.036 262.140 251.423 1.00 15.87 ? 2372 ASP A OD2   1 
ATOM   7325  N  N     . MET A 1 2373 ? 211.981 259.420 248.017 1.00 3.19  ? 2373 MET A N     1 
ATOM   7326  C  CA    . MET A 1 2373 ? 211.319 258.148 248.287 1.00 1.90  ? 2373 MET A CA    1 
ATOM   7327  C  C     . MET A 1 2373 ? 212.051 256.990 247.619 1.00 2.00  ? 2373 MET A C     1 
ATOM   7328  O  O     . MET A 1 2373 ? 212.234 255.929 248.226 1.00 2.13  ? 2373 MET A O     1 
ATOM   7329  C  CB    . MET A 1 2373 ? 209.870 258.210 247.810 1.00 3.05  ? 2373 MET A CB    1 
ATOM   7330  C  CG    . MET A 1 2373 ? 208.951 259.008 248.710 1.00 2.70  ? 2373 MET A CG    1 
ATOM   7331  S  SD    . MET A 1 2373 ? 207.483 259.586 247.842 1.00 4.45  ? 2373 MET A SD    1 
ATOM   7332  C  CE    . MET A 1 2373 ? 206.604 258.049 247.601 1.00 0.71  ? 2373 MET A CE    1 
ATOM   7333  N  N     . ILE A 1 2374 ? 212.475 257.179 246.368 1.00 2.90  ? 2374 ILE A N     1 
ATOM   7334  C  CA    . ILE A 1 2374 ? 213.208 256.137 245.655 1.00 1.57  ? 2374 ILE A CA    1 
ATOM   7335  C  C     . ILE A 1 2374 ? 214.542 255.863 246.336 1.00 2.56  ? 2374 ILE A C     1 
ATOM   7336  O  O     . ILE A 1 2374 ? 214.970 254.709 246.456 1.00 4.59  ? 2374 ILE A O     1 
ATOM   7337  C  CB    . ILE A 1 2374 ? 213.391 256.530 244.178 1.00 1.67  ? 2374 ILE A CB    1 
ATOM   7338  C  CG1   . ILE A 1 2374 ? 212.028 256.760 243.521 1.00 0.93  ? 2374 ILE A CG1   1 
ATOM   7339  C  CG2   . ILE A 1 2374 ? 214.186 255.466 243.432 1.00 1.26  ? 2374 ILE A CG2   1 
ATOM   7340  C  CD1   . ILE A 1 2374 ? 212.096 257.450 242.183 1.00 0.83  ? 2374 ILE A CD1   1 
ATOM   7341  N  N     . PHE A 1 2375 ? 215.219 256.918 246.792 1.00 1.82  ? 2375 PHE A N     1 
ATOM   7342  C  CA    . PHE A 1 2375 ? 216.483 256.739 247.500 1.00 1.77  ? 2375 PHE A CA    1 
ATOM   7343  C  C     . PHE A 1 2375 ? 216.284 255.968 248.798 1.00 3.24  ? 2375 PHE A C     1 
ATOM   7344  O  O     . PHE A 1 2375 ? 217.095 255.103 249.144 1.00 8.30  ? 2375 PHE A O     1 
ATOM   7345  C  CB    . PHE A 1 2375 ? 217.129 258.095 247.775 1.00 3.04  ? 2375 PHE A CB    1 
ATOM   7346  C  CG    . PHE A 1 2375 ? 217.660 258.771 246.545 1.00 2.55  ? 2375 PHE A CG    1 
ATOM   7347  C  CD1   . PHE A 1 2375 ? 217.836 258.062 245.370 1.00 2.13  ? 2375 PHE A CD1   1 
ATOM   7348  C  CD2   . PHE A 1 2375 ? 217.981 260.116 246.564 1.00 2.33  ? 2375 PHE A CD2   1 
ATOM   7349  C  CE1   . PHE A 1 2375 ? 218.320 258.681 244.242 1.00 3.11  ? 2375 PHE A CE1   1 
ATOM   7350  C  CE2   . PHE A 1 2375 ? 218.467 260.739 245.437 1.00 4.26  ? 2375 PHE A CE2   1 
ATOM   7351  C  CZ    . PHE A 1 2375 ? 218.640 260.022 244.275 1.00 3.31  ? 2375 PHE A CZ    1 
ATOM   7352  N  N     . ASN A 1 2376 ? 215.209 256.271 249.531 1.00 2.78  ? 2376 ASN A N     1 
ATOM   7353  C  CA    . ASN A 1 2376 ? 214.921 255.537 250.760 1.00 2.42  ? 2376 ASN A CA    1 
ATOM   7354  C  C     . ASN A 1 2376 ? 214.681 254.063 250.477 1.00 3.10  ? 2376 ASN A C     1 
ATOM   7355  O  O     . ASN A 1 2376 ? 215.151 253.195 251.221 1.00 4.14  ? 2376 ASN A O     1 
ATOM   7356  C  CB    . ASN A 1 2376 ? 213.703 256.138 251.462 1.00 3.10  ? 2376 ASN A CB    1 
ATOM   7357  C  CG    . ASN A 1 2376 ? 213.954 257.535 251.977 1.00 6.74  ? 2376 ASN A CG    1 
ATOM   7358  O  OD1   . ASN A 1 2376 ? 215.091 258.003 252.016 1.00 9.96  ? 2376 ASN A OD1   1 
ATOM   7359  N  ND2   . ASN A 1 2376 ? 212.885 258.217 252.369 1.00 6.55  ? 2376 ASN A ND2   1 
ATOM   7360  N  N     . ASN A 1 2377 ? 213.943 253.761 249.407 1.00 2.13  ? 2377 ASN A N     1 
ATOM   7361  C  CA    . ASN A 1 2377 ? 213.650 252.373 249.072 1.00 2.08  ? 2377 ASN A CA    1 
ATOM   7362  C  C     . ASN A 1 2377 ? 214.924 251.602 248.760 1.00 3.31  ? 2377 ASN A C     1 
ATOM   7363  O  O     . ASN A 1 2377 ? 215.094 250.463 249.208 1.00 4.66  ? 2377 ASN A O     1 
ATOM   7364  C  CB    . ASN A 1 2377 ? 212.682 252.320 247.890 1.00 2.03  ? 2377 ASN A CB    1 
ATOM   7365  C  CG    . ASN A 1 2377 ? 212.385 250.906 247.442 1.00 1.77  ? 2377 ASN A CG    1 
ATOM   7366  O  OD1   . ASN A 1 2377 ? 212.668 250.533 246.306 1.00 6.99  ? 2377 ASN A OD1   1 
ATOM   7367  N  ND2   . ASN A 1 2377 ? 211.805 250.111 248.331 1.00 1.65  ? 2377 ASN A ND2   1 
ATOM   7368  N  N     . PHE A 1 2378 ? 215.836 252.211 247.998 1.00 4.01  ? 2378 PHE A N     1 
ATOM   7369  C  CA    . PHE A 1 2378 ? 217.093 251.548 247.675 1.00 2.05  ? 2378 PHE A CA    1 
ATOM   7370  C  C     . PHE A 1 2378 ? 217.940 251.331 248.923 1.00 2.80  ? 2378 PHE A C     1 
ATOM   7371  O  O     . PHE A 1 2378 ? 218.556 250.273 249.088 1.00 3.38  ? 2378 PHE A O     1 
ATOM   7372  C  CB    . PHE A 1 2378 ? 217.854 252.362 246.629 1.00 2.16  ? 2378 PHE A CB    1 
ATOM   7373  C  CG    . PHE A 1 2378 ? 219.335 252.135 246.642 1.00 1.89  ? 2378 PHE A CG    1 
ATOM   7374  C  CD1   . PHE A 1 2378 ? 219.875 250.973 246.119 1.00 0.83  ? 2378 PHE A CD1   1 
ATOM   7375  C  CD2   . PHE A 1 2378 ? 220.190 253.085 247.176 1.00 2.50  ? 2378 PHE A CD2   1 
ATOM   7376  C  CE1   . PHE A 1 2378 ? 221.235 250.762 246.130 1.00 1.33  ? 2378 PHE A CE1   1 
ATOM   7377  C  CE2   . PHE A 1 2378 ? 221.552 252.877 247.190 1.00 2.97  ? 2378 PHE A CE2   1 
ATOM   7378  C  CZ    . PHE A 1 2378 ? 222.075 251.714 246.666 1.00 3.29  ? 2378 PHE A CZ    1 
ATOM   7379  N  N     . LEU A 1 2379 ? 217.983 252.323 249.814 1.00 2.83  ? 2379 LEU A N     1 
ATOM   7380  C  CA    . LEU A 1 2379 ? 218.774 252.184 251.032 1.00 4.35  ? 2379 LEU A CA    1 
ATOM   7381  C  C     . LEU A 1 2379 ? 218.143 251.193 252.002 1.00 6.14  ? 2379 LEU A C     1 
ATOM   7382  O  O     . LEU A 1 2379 ? 218.855 250.426 252.661 1.00 9.69  ? 2379 LEU A O     1 
ATOM   7383  C  CB    . LEU A 1 2379 ? 218.959 253.547 251.697 1.00 4.30  ? 2379 LEU A CB    1 
ATOM   7384  C  CG    . LEU A 1 2379 ? 219.985 254.454 251.020 1.00 4.04  ? 2379 LEU A CG    1 
ATOM   7385  C  CD1   . LEU A 1 2379 ? 220.083 255.783 251.735 1.00 7.12  ? 2379 LEU A CD1   1 
ATOM   7386  C  CD2   . LEU A 1 2379 ? 221.344 253.774 250.964 1.00 4.32  ? 2379 LEU A CD2   1 
ATOM   7387  N  N     . ALA A 1 2380 ? 216.813 251.195 252.111 1.00 4.83  ? 2380 ALA A N     1 
ATOM   7388  C  CA    . ALA A 1 2380 ? 216.146 250.251 253.002 1.00 2.50  ? 2380 ALA A CA    1 
ATOM   7389  C  C     . ALA A 1 2380 ? 216.380 248.815 252.553 1.00 3.98  ? 2380 ALA A C     1 
ATOM   7390  O  O     . ALA A 1 2380 ? 216.642 247.932 253.380 1.00 7.73  ? 2380 ALA A O     1 
ATOM   7391  C  CB    . ALA A 1 2380 ? 214.652 250.556 253.074 1.00 3.12  ? 2380 ALA A CB    1 
ATOM   7392  N  N     . ARG A 1 2381 ? 216.286 248.561 251.246 1.00 3.83  ? 2381 ARG A N     1 
ATOM   7393  C  CA    . ARG A 1 2381 ? 216.570 247.227 250.729 1.00 3.17  ? 2381 ARG A CA    1 
ATOM   7394  C  C     . ARG A 1 2381 ? 218.037 246.862 250.923 1.00 4.97  ? 2381 ARG A C     1 
ATOM   7395  O  O     . ARG A 1 2381 ? 218.360 245.712 251.243 1.00 5.84  ? 2381 ARG A O     1 
ATOM   7396  C  CB    . ARG A 1 2381 ? 216.184 247.139 249.253 1.00 2.41  ? 2381 ARG A CB    1 
ATOM   7397  C  CG    . ARG A 1 2381 ? 214.707 247.346 248.984 1.00 4.00  ? 2381 ARG A CG    1 
ATOM   7398  C  CD    . ARG A 1 2381 ? 214.433 247.511 247.499 1.00 2.74  ? 2381 ARG A CD    1 
ATOM   7399  N  NE    . ARG A 1 2381 ? 214.816 246.328 246.740 1.00 6.37  ? 2381 ARG A NE    1 
ATOM   7400  C  CZ    . ARG A 1 2381 ? 214.180 245.166 246.781 1.00 7.46  ? 2381 ARG A CZ    1 
ATOM   7401  N  NH1   . ARG A 1 2381 ? 213.087 244.998 247.509 1.00 7.45  ? 2381 ARG A NH1   1 
ATOM   7402  N  NH2   . ARG A 1 2381 ? 214.650 244.145 246.072 1.00 16.86 ? 2381 ARG A NH2   1 
ATOM   7403  N  N     . LEU A 1 2382 ? 218.938 247.829 250.729 1.00 3.44  ? 2382 LEU A N     1 
ATOM   7404  C  CA    . LEU A 1 2382 ? 220.361 247.562 250.904 1.00 4.91  ? 2382 LEU A CA    1 
ATOM   7405  C  C     . LEU A 1 2382 ? 220.693 247.191 252.343 1.00 8.42  ? 2382 LEU A C     1 
ATOM   7406  O  O     . LEU A 1 2382 ? 221.623 246.415 252.585 1.00 9.09  ? 2382 LEU A O     1 
ATOM   7407  C  CB    . LEU A 1 2382 ? 221.181 248.778 250.468 1.00 6.32  ? 2382 LEU A CB    1 
ATOM   7408  C  CG    . LEU A 1 2382 ? 222.699 248.591 250.417 1.00 8.86  ? 2382 LEU A CG    1 
ATOM   7409  C  CD1   . LEU A 1 2382 ? 223.078 247.521 249.408 1.00 6.13  ? 2382 LEU A CD1   1 
ATOM   7410  C  CD2   . LEU A 1 2382 ? 223.397 249.902 250.099 1.00 6.07  ? 2382 LEU A CD2   1 
ATOM   7411  N  N     . ARG A 1 2383 ? 219.944 247.725 253.305 1.00 4.91  ? 2383 ARG A N     1 
ATOM   7412  C  CA    . ARG A 1 2383 ? 220.190 247.457 254.714 1.00 4.95  ? 2383 ARG A CA    1 
ATOM   7413  C  C     . ARG A 1 2383 ? 219.476 246.214 255.229 1.00 5.75  ? 2383 ARG A C     1 
ATOM   7414  O  O     . ARG A 1 2383 ? 219.708 245.821 256.376 1.00 8.43  ? 2383 ARG A O     1 
ATOM   7415  C  CB    . ARG A 1 2383 ? 219.770 248.666 255.558 1.00 4.66  ? 2383 ARG A CB    1 
ATOM   7416  C  CG    . ARG A 1 2383 ? 220.706 249.850 255.440 1.00 7.28  ? 2383 ARG A CG    1 
ATOM   7417  C  CD    . ARG A 1 2383 ? 220.199 251.050 256.213 1.00 6.24  ? 2383 ARG A CD    1 
ATOM   7418  N  NE    . ARG A 1 2383 ? 221.273 251.992 256.504 1.00 7.70  ? 2383 ARG A NE    1 
ATOM   7419  C  CZ    . ARG A 1 2383 ? 221.316 253.242 256.060 1.00 7.43  ? 2383 ARG A CZ    1 
ATOM   7420  N  NH1   . ARG A 1 2383 ? 220.354 253.738 255.301 1.00 5.48  ? 2383 ARG A NH1   1 
ATOM   7421  N  NH2   . ARG A 1 2383 ? 222.353 254.008 256.382 1.00 8.07  ? 2383 ARG A NH2   1 
ATOM   7422  N  N     . SER A 1 2384 ? 218.624 245.594 254.427 1.00 5.99  ? 2384 SER A N     1 
ATOM   7423  C  CA    . SER A 1 2384 ? 217.847 244.463 254.917 1.00 5.75  ? 2384 SER A CA    1 
ATOM   7424  C  C     . SER A 1 2384 ? 217.985 243.210 254.064 1.00 9.48  ? 2384 SER A C     1 
ATOM   7425  O  O     . SER A 1 2384 ? 218.047 242.109 254.610 1.00 12.85 ? 2384 SER A O     1 
ATOM   7426  C  CB    . SER A 1 2384 ? 216.367 244.855 255.017 1.00 7.49  ? 2384 SER A CB    1 
ATOM   7427  O  OG    . SER A 1 2384 ? 216.203 246.043 255.771 1.00 16.79 ? 2384 SER A OG    1 
ATOM   7428  N  N     . ILE A 1 2385 ? 218.034 243.347 252.745 1.00 8.59  ? 2385 ILE A N     1 
ATOM   7429  C  CA    . ILE A 1 2385 ? 218.071 242.207 251.832 1.00 8.33  ? 2385 ILE A CA    1 
ATOM   7430  C  C     . ILE A 1 2385 ? 219.528 241.929 251.481 1.00 11.46 ? 2385 ILE A C     1 
ATOM   7431  O  O     . ILE A 1 2385 ? 220.180 242.789 250.872 1.00 10.44 ? 2385 ILE A O     1 
ATOM   7432  C  CB    . ILE A 1 2385 ? 217.240 242.466 250.568 1.00 8.76  ? 2385 ILE A CB    1 
ATOM   7433  C  CG1   . ILE A 1 2385 ? 215.840 242.952 250.945 1.00 5.35  ? 2385 ILE A CG1   1 
ATOM   7434  C  CG2   . ILE A 1 2385 ? 217.172 241.209 249.715 1.00 5.12  ? 2385 ILE A CG2   1 
ATOM   7435  C  CD1   . ILE A 1 2385 ? 214.986 243.329 249.760 1.00 5.26  ? 2385 ILE A CD1   1 
ATOM   7436  N  N     . PRO A 1 2386 ? 220.071 240.767 251.837 1.00 14.20 ? 2386 PRO A N     1 
ATOM   7437  C  CA    . PRO A 1 2386 ? 221.455 240.461 251.461 1.00 12.21 ? 2386 PRO A CA    1 
ATOM   7438  C  C     . PRO A 1 2386 ? 221.563 240.166 249.974 1.00 13.75 ? 2386 PRO A C     1 
ATOM   7439  O  O     . PRO A 1 2386 ? 220.688 239.531 249.381 1.00 25.14 ? 2386 PRO A O     1 
ATOM   7440  C  CB    . PRO A 1 2386 ? 221.791 239.225 252.305 1.00 16.66 ? 2386 PRO A CB    1 
ATOM   7441  C  CG    . PRO A 1 2386 ? 220.660 239.084 253.294 1.00 11.80 ? 2386 PRO A CG    1 
ATOM   7442  C  CD    . PRO A 1 2386 ? 219.470 239.697 252.642 1.00 8.28  ? 2386 PRO A CD    1 
ATOM   7443  N  N     . LEU A 1 2387 ? 222.650 240.646 249.371 1.00 12.43 ? 2387 LEU A N     1 
ATOM   7444  C  CA    . LEU A 1 2387 ? 222.872 240.431 247.948 1.00 9.63  ? 2387 LEU A CA    1 
ATOM   7445  C  C     . LEU A 1 2387 ? 223.403 239.039 247.634 1.00 15.20 ? 2387 LEU A C     1 
ATOM   7446  O  O     . LEU A 1 2387 ? 223.225 238.567 246.505 1.00 17.12 ? 2387 LEU A O     1 
ATOM   7447  C  CB    . LEU A 1 2387 ? 223.840 241.483 247.402 1.00 13.94 ? 2387 LEU A CB    1 
ATOM   7448  C  CG    . LEU A 1 2387 ? 223.391 242.943 247.475 1.00 12.04 ? 2387 LEU A CG    1 
ATOM   7449  C  CD1   . LEU A 1 2387 ? 224.583 243.869 247.324 1.00 9.29  ? 2387 LEU A CD1   1 
ATOM   7450  C  CD2   . LEU A 1 2387 ? 222.336 243.242 246.423 1.00 5.23  ? 2387 LEU A CD2   1 
ATOM   7451  N  N     . ASP A 1 2388 ? 224.050 238.376 248.597 1.00 21.61 ? 2388 ASP A N     1 
ATOM   7452  C  CA    . ASP A 1 2388 ? 224.634 237.064 248.330 1.00 18.04 ? 2388 ASP A CA    1 
ATOM   7453  C  C     . ASP A 1 2388 ? 223.560 236.026 248.028 1.00 25.47 ? 2388 ASP A C     1 
ATOM   7454  O  O     . ASP A 1 2388 ? 223.731 235.193 247.130 1.00 30.18 ? 2388 ASP A O     1 
ATOM   7455  C  CB    . ASP A 1 2388 ? 225.504 236.622 249.506 1.00 16.23 ? 2388 ASP A CB    1 
ATOM   7456  C  CG    . ASP A 1 2388 ? 224.744 236.582 250.816 1.00 30.47 ? 2388 ASP A CG    1 
ATOM   7457  O  OD1   . ASP A 1 2388 ? 224.268 237.645 251.260 1.00 32.82 ? 2388 ASP A OD1   1 
ATOM   7458  O  OD2   . ASP A 1 2388 ? 224.623 235.486 251.404 1.00 41.17 ? 2388 ASP A OD2   1 
ATOM   7459  N  N     . GLU A 1 2389 ? 222.449 236.059 248.759 1.00 23.88 ? 2389 GLU A N     1 
ATOM   7460  C  CA    . GLU A 1 2389 ? 221.349 235.131 248.525 1.00 31.17 ? 2389 GLU A CA    1 
ATOM   7461  C  C     . GLU A 1 2389 ? 220.060 235.640 249.158 1.00 24.66 ? 2389 GLU A C     1 
ATOM   7462  O  O     . GLU A 1 2389 ? 220.076 236.235 250.237 0.00 21.55 ? 2389 GLU A O     1 
ATOM   7463  C  CB    . GLU A 1 2389 ? 221.692 233.741 249.073 1.00 29.92 ? 2389 GLU A CB    1 
ATOM   7464  C  CG    . GLU A 1 2389 ? 220.581 232.704 248.932 1.00 29.77 ? 2389 GLU A CG    1 
ATOM   7465  C  CD    . GLU A 1 2389 ? 220.322 232.293 247.492 1.00 40.30 ? 2389 GLU A CD    1 
ATOM   7466  O  OE1   . GLU A 1 2389 ? 219.823 233.124 246.703 1.00 40.99 ? 2389 GLU A OE1   1 
ATOM   7467  O  OE2   . GLU A 1 2389 ? 220.621 231.129 247.145 1.00 38.91 ? 2389 GLU A OE2   1 
ATOM   7468  N  N     . SER A 1 2410 ? 224.905 238.912 258.876 1.00 20.88 ? 2410 SER A N     1 
ATOM   7469  C  CA    . SER A 1 2410 ? 225.520 238.331 257.689 1.00 19.98 ? 2410 SER A CA    1 
ATOM   7470  C  C     . SER A 1 2410 ? 226.726 239.148 257.252 1.00 22.24 ? 2410 SER A C     1 
ATOM   7471  O  O     . SER A 1 2410 ? 226.673 240.378 257.237 1.00 20.14 ? 2410 SER A O     1 
ATOM   7472  C  CB    . SER A 1 2410 ? 224.507 238.240 256.547 1.00 19.54 ? 2410 SER A CB    1 
ATOM   7473  O  OG    . SER A 1 2410 ? 225.121 237.776 255.357 1.00 19.95 ? 2410 SER A OG    1 
ATOM   7474  N  N     . PRO A 1 2411 ? 227.820 238.466 256.906 1.00 21.35 ? 2411 PRO A N     1 
ATOM   7475  C  CA    . PRO A 1 2411 ? 229.007 239.193 256.430 1.00 20.40 ? 2411 PRO A CA    1 
ATOM   7476  C  C     . PRO A 1 2411 ? 228.737 240.020 255.187 1.00 16.34 ? 2411 PRO A C     1 
ATOM   7477  O  O     . PRO A 1 2411 ? 229.316 241.104 255.035 1.00 20.64 ? 2411 PRO A O     1 
ATOM   7478  C  CB    . PRO A 1 2411 ? 230.019 238.071 256.164 1.00 14.98 ? 2411 PRO A CB    1 
ATOM   7479  C  CG    . PRO A 1 2411 ? 229.184 236.858 255.933 1.00 17.23 ? 2411 PRO A CG    1 
ATOM   7480  C  CD    . PRO A 1 2411 ? 227.999 237.007 256.837 1.00 15.68 ? 2411 PRO A CD    1 
ATOM   7481  N  N     . MET A 1 2412 ? 227.872 239.542 254.292 1.00 14.07 ? 2412 MET A N     1 
ATOM   7482  C  CA    . MET A 1 2412 ? 227.507 240.335 253.123 1.00 15.88 ? 2412 MET A CA    1 
ATOM   7483  C  C     . MET A 1 2412 ? 226.589 241.489 253.507 1.00 13.98 ? 2412 MET A C     1 
ATOM   7484  O  O     . MET A 1 2412 ? 226.771 242.617 253.035 1.00 12.70 ? 2412 MET A O     1 
ATOM   7485  C  CB    . MET A 1 2412 ? 226.844 239.443 252.075 1.00 16.45 ? 2412 MET A CB    1 
ATOM   7486  C  CG    . MET A 1 2412 ? 226.563 240.134 250.757 1.00 17.95 ? 2412 MET A CG    1 
ATOM   7487  S  SD    . MET A 1 2412 ? 228.047 240.850 250.029 1.00 26.27 ? 2412 MET A SD    1 
ATOM   7488  C  CE    . MET A 1 2412 ? 227.411 242.404 249.421 1.00 12.56 ? 2412 MET A CE    1 
ATOM   7489  N  N     . LEU A 1 2413 ? 225.599 241.226 254.364 1.00 14.74 ? 2413 LEU A N     1 
ATOM   7490  C  CA    . LEU A 1 2413 ? 224.716 242.287 254.839 1.00 12.58 ? 2413 LEU A CA    1 
ATOM   7491  C  C     . LEU A 1 2413 ? 225.480 243.331 255.643 1.00 12.66 ? 2413 LEU A C     1 
ATOM   7492  O  O     . LEU A 1 2413 ? 225.167 244.525 255.570 1.00 15.41 ? 2413 LEU A O     1 
ATOM   7493  C  CB    . LEU A 1 2413 ? 223.581 241.694 255.671 1.00 13.64 ? 2413 LEU A CB    1 
ATOM   7494  C  CG    . LEU A 1 2413 ? 222.291 242.510 255.742 1.00 11.53 ? 2413 LEU A CG    1 
ATOM   7495  C  CD1   . LEU A 1 2413 ? 221.479 242.384 254.471 1.00 10.99 ? 2413 LEU A CD1   1 
ATOM   7496  C  CD2   . LEU A 1 2413 ? 221.471 242.064 256.935 1.00 13.81 ? 2413 LEU A CD2   1 
ATOM   7497  N  N     . GLN A 1 2414 ? 226.475 242.902 256.420 1.00 15.28 ? 2414 GLN A N     1 
ATOM   7498  C  CA    . GLN A 1 2414 ? 227.272 243.852 257.188 1.00 14.69 ? 2414 GLN A CA    1 
ATOM   7499  C  C     . GLN A 1 2414 ? 228.021 244.810 256.272 1.00 15.75 ? 2414 GLN A C     1 
ATOM   7500  O  O     . GLN A 1 2414 ? 228.178 245.993 256.594 1.00 21.62 ? 2414 GLN A O     1 
ATOM   7501  C  CB    . GLN A 1 2414 ? 228.245 243.105 258.102 1.00 19.06 ? 2414 GLN A CB    1 
ATOM   7502  C  CG    . GLN A 1 2414 ? 228.834 243.926 259.258 1.00 19.65 ? 2414 GLN A CG    1 
ATOM   7503  C  CD    . GLN A 1 2414 ? 227.873 244.933 259.881 1.00 19.74 ? 2414 GLN A CD    1 
ATOM   7504  O  OE1   . GLN A 1 2414 ? 226.663 244.711 259.954 1.00 20.08 ? 2414 GLN A OE1   1 
ATOM   7505  N  NE2   . GLN A 1 2414 ? 228.418 246.055 260.332 1.00 23.19 ? 2414 GLN A NE2   1 
ATOM   7506  N  N     . ILE A 1 2415 ? 228.509 244.313 255.133 1.00 14.11 ? 2415 ILE A N     1 
ATOM   7507  C  CA    . ILE A 1 2415 ? 229.152 245.191 254.160 1.00 13.16 ? 2415 ILE A CA    1 
ATOM   7508  C  C     . ILE A 1 2415 ? 228.144 246.174 253.580 1.00 12.62 ? 2415 ILE A C     1 
ATOM   7509  O  O     . ILE A 1 2415 ? 228.426 247.371 253.451 1.00 16.96 ? 2415 ILE A O     1 
ATOM   7510  C  CB    . ILE A 1 2415 ? 229.837 244.365 253.059 1.00 17.19 ? 2415 ILE A CB    1 
ATOM   7511  C  CG1   . ILE A 1 2415 ? 231.076 243.666 253.616 1.00 11.93 ? 2415 ILE A CG1   1 
ATOM   7512  C  CG2   . ILE A 1 2415 ? 230.206 245.246 251.873 1.00 11.53 ? 2415 ILE A CG2   1 
ATOM   7513  C  CD1   . ILE A 1 2415 ? 231.800 242.823 252.600 1.00 10.34 ? 2415 ILE A CD1   1 
ATOM   7514  N  N     . GLN A 1 2416 ? 226.954 245.686 253.224 1.00 11.77 ? 2416 GLN A N     1 
ATOM   7515  C  CA    . GLN A 1 2416 ? 225.926 246.563 252.674 1.00 5.98  ? 2416 GLN A CA    1 
ATOM   7516  C  C     . GLN A 1 2416 ? 225.498 247.617 253.689 1.00 10.48 ? 2416 GLN A C     1 
ATOM   7517  O  O     . GLN A 1 2416 ? 225.305 248.785 253.335 1.00 10.42 ? 2416 GLN A O     1 
ATOM   7518  C  CB    . GLN A 1 2416 ? 224.722 245.742 252.218 1.00 7.63  ? 2416 GLN A CB    1 
ATOM   7519  C  CG    . GLN A 1 2416 ? 225.041 244.665 251.196 1.00 8.20  ? 2416 GLN A CG    1 
ATOM   7520  C  CD    . GLN A 1 2416 ? 223.913 243.665 251.029 1.00 7.88  ? 2416 GLN A CD    1 
ATOM   7521  O  OE1   . GLN A 1 2416 ? 224.146 242.488 250.766 1.00 13.46 ? 2416 GLN A OE1   1 
ATOM   7522  N  NE2   . GLN A 1 2416 ? 222.681 244.133 251.181 1.00 10.16 ? 2416 GLN A NE2   1 
ATOM   7523  N  N     . ARG A 1 2417 ? 225.345 247.221 254.955 1.00 13.61 ? 2417 ARG A N     1 
ATOM   7524  C  CA    . ARG A 1 2417 ? 224.910 248.165 255.978 1.00 11.88 ? 2417 ARG A CA    1 
ATOM   7525  C  C     . ARG A 1 2417 ? 225.940 249.264 256.197 1.00 10.82 ? 2417 ARG A C     1 
ATOM   7526  O  O     . ARG A 1 2417 ? 225.588 250.444 256.295 1.00 12.30 ? 2417 ARG A O     1 
ATOM   7527  C  CB    . ARG A 1 2417 ? 224.622 247.426 257.285 1.00 10.93 ? 2417 ARG A CB    1 
ATOM   7528  C  CG    . ARG A 1 2417 ? 223.361 246.588 257.240 1.00 11.31 ? 2417 ARG A CG    1 
ATOM   7529  C  CD    . ARG A 1 2417 ? 222.790 246.362 258.624 1.00 12.05 ? 2417 ARG A CD    1 
ATOM   7530  N  NE    . ARG A 1 2417 ? 221.485 245.716 258.564 1.00 11.31 ? 2417 ARG A NE    1 
ATOM   7531  C  CZ    . ARG A 1 2417 ? 221.159 244.620 259.235 1.00 9.78  ? 2417 ARG A CZ    1 
ATOM   7532  N  NH1   . ARG A 1 2417 ? 222.019 244.022 260.043 1.00 11.87 ? 2417 ARG A NH1   1 
ATOM   7533  N  NH2   . ARG A 1 2417 ? 219.939 244.110 259.091 1.00 9.46  ? 2417 ARG A NH2   1 
ATOM   7534  N  N     . ASP A 1 2418 ? 227.222 248.896 256.278 1.00 15.30 ? 2418 ASP A N     1 
ATOM   7535  C  CA    . ASP A 1 2418 ? 228.269 249.906 256.396 1.00 12.81 ? 2418 ASP A CA    1 
ATOM   7536  C  C     . ASP A 1 2418 ? 228.345 250.767 255.142 1.00 11.37 ? 2418 ASP A C     1 
ATOM   7537  O  O     . ASP A 1 2418 ? 228.559 251.981 255.230 1.00 10.20 ? 2418 ASP A O     1 
ATOM   7538  C  CB    . ASP A 1 2418 ? 229.617 249.243 256.676 1.00 16.11 ? 2418 ASP A CB    1 
ATOM   7539  C  CG    . ASP A 1 2418 ? 229.686 248.620 258.055 1.00 29.21 ? 2418 ASP A CG    1 
ATOM   7540  O  OD1   . ASP A 1 2418 ? 229.001 249.121 258.971 1.00 32.15 ? 2418 ASP A OD1   1 
ATOM   7541  O  OD2   . ASP A 1 2418 ? 230.432 247.633 258.226 1.00 31.99 ? 2418 ASP A OD2   1 
ATOM   7542  N  N     . ALA A 1 2419 ? 228.177 250.155 253.970 1.00 11.21 ? 2419 ALA A N     1 
ATOM   7543  C  CA    . ALA A 1 2419 ? 228.172 250.920 252.726 1.00 10.42 ? 2419 ALA A CA    1 
ATOM   7544  C  C     . ALA A 1 2419 ? 226.961 251.841 252.649 1.00 10.15 ? 2419 ALA A C     1 
ATOM   7545  O  O     . ALA A 1 2419 ? 227.049 252.945 252.099 1.00 13.37 ? 2419 ALA A O     1 
ATOM   7546  C  CB    . ALA A 1 2419 ? 228.207 249.972 251.529 1.00 9.32  ? 2419 ALA A CB    1 
ATOM   7547  N  N     . ALA A 1 2420 ? 225.820 251.401 253.188 1.00 10.64 ? 2420 ALA A N     1 
ATOM   7548  C  CA    . ALA A 1 2420 ? 224.631 252.247 253.202 1.00 9.78  ? 2420 ALA A CA    1 
ATOM   7549  C  C     . ALA A 1 2420 ? 224.859 253.505 254.028 1.00 9.25  ? 2420 ALA A C     1 
ATOM   7550  O  O     . ALA A 1 2420 ? 224.402 254.592 253.656 1.00 9.70  ? 2420 ALA A O     1 
ATOM   7551  C  CB    . ALA A 1 2420 ? 223.436 251.463 253.739 1.00 7.08  ? 2420 ALA A CB    1 
ATOM   7552  N  N     . THR A 1 2421 ? 225.564 253.375 255.156 1.00 7.75  ? 2421 THR A N     1 
ATOM   7553  C  CA    . THR A 1 2421 ? 225.877 254.541 255.973 1.00 8.73  ? 2421 THR A CA    1 
ATOM   7554  C  C     . THR A 1 2421 ? 226.756 255.523 255.215 1.00 11.25 ? 2421 THR A C     1 
ATOM   7555  O  O     . THR A 1 2421 ? 226.586 256.742 255.333 1.00 17.53 ? 2421 THR A O     1 
ATOM   7556  C  CB    . THR A 1 2421 ? 226.557 254.104 257.272 1.00 12.11 ? 2421 THR A CB    1 
ATOM   7557  O  OG1   . THR A 1 2421 ? 225.779 253.078 257.902 1.00 12.55 ? 2421 THR A OG1   1 
ATOM   7558  C  CG2   . THR A 1 2421 ? 226.698 255.280 258.222 1.00 14.44 ? 2421 THR A CG2   1 
ATOM   7559  N  N     . ILE A 1 2422 ? 227.705 255.010 254.431 1.00 8.28  ? 2422 ILE A N     1 
ATOM   7560  C  CA    . ILE A 1 2422 ? 228.582 255.873 253.646 1.00 9.65  ? 2422 ILE A CA    1 
ATOM   7561  C  C     . ILE A 1 2422 ? 227.803 256.573 252.537 1.00 9.47  ? 2422 ILE A C     1 
ATOM   7562  O  O     . ILE A 1 2422 ? 228.013 257.762 252.271 1.00 10.94 ? 2422 ILE A O     1 
ATOM   7563  C  CB    . ILE A 1 2422 ? 229.759 255.055 253.086 1.00 13.73 ? 2422 ILE A CB    1 
ATOM   7564  C  CG1   . ILE A 1 2422 ? 230.478 254.324 254.219 1.00 10.89 ? 2422 ILE A CG1   1 
ATOM   7565  C  CG2   . ILE A 1 2422 ? 230.727 255.953 252.332 1.00 13.46 ? 2422 ILE A CG2   1 
ATOM   7566  C  CD1   . ILE A 1 2422 ? 231.409 253.237 253.748 1.00 10.33 ? 2422 ILE A CD1   1 
ATOM   7567  N  N     . MET A 1 2423 ? 226.899 255.851 251.868 1.00 8.11  ? 2423 MET A N     1 
ATOM   7568  C  CA    . MET A 1 2423 ? 226.155 256.446 250.761 1.00 8.30  ? 2423 MET A CA    1 
ATOM   7569  C  C     . MET A 1 2423 ? 225.081 257.411 251.244 1.00 12.35 ? 2423 MET A C     1 
ATOM   7570  O  O     . MET A 1 2423 ? 224.646 258.279 250.479 1.00 18.46 ? 2423 MET A O     1 
ATOM   7571  C  CB    . MET A 1 2423 ? 225.501 255.364 249.899 1.00 9.33  ? 2423 MET A CB    1 
ATOM   7572  C  CG    . MET A 1 2423 ? 226.450 254.478 249.128 1.00 11.90 ? 2423 MET A CG    1 
ATOM   7573  S  SD    . MET A 1 2423 ? 225.560 253.113 248.357 1.00 20.84 ? 2423 MET A SD    1 
ATOM   7574  C  CE    . MET A 1 2423 ? 226.586 251.724 248.809 1.00 14.98 ? 2423 MET A CE    1 
ATOM   7575  N  N     . GLN A 1 2424 ? 224.642 257.275 252.494 1.00 11.68 ? 2424 GLN A N     1 
ATOM   7576  C  CA    . GLN A 1 2424 ? 223.487 258.021 252.993 1.00 11.73 ? 2424 GLN A CA    1 
ATOM   7577  C  C     . GLN A 1 2424 ? 223.600 259.531 252.819 1.00 10.95 ? 2424 GLN A C     1 
ATOM   7578  O  O     . GLN A 1 2424 ? 222.616 260.146 252.375 1.00 12.12 ? 2424 GLN A O     1 
ATOM   7579  C  CB    . GLN A 1 2424 ? 223.256 257.649 254.465 1.00 12.02 ? 2424 GLN A CB    1 
ATOM   7580  C  CG    . GLN A 1 2424 ? 222.016 258.264 255.084 1.00 11.02 ? 2424 GLN A CG    1 
ATOM   7581  C  CD    . GLN A 1 2424 ? 220.776 257.425 254.854 1.00 13.42 ? 2424 GLN A CD    1 
ATOM   7582  O  OE1   . GLN A 1 2424 ? 220.693 256.288 255.315 1.00 19.54 ? 2424 GLN A OE1   1 
ATOM   7583  N  NE2   . GLN A 1 2424 ? 219.803 257.982 254.145 1.00 9.28  ? 2424 GLN A NE2   1 
ATOM   7584  N  N     . PRO A 1 2425 ? 224.724 260.191 253.140 1.00 12.40 ? 2425 PRO A N     1 
ATOM   7585  C  CA    . PRO A 1 2425 ? 224.777 261.653 252.949 1.00 8.05  ? 2425 PRO A CA    1 
ATOM   7586  C  C     . PRO A 1 2425 ? 224.538 262.101 251.518 1.00 10.47 ? 2425 PRO A C     1 
ATOM   7587  O  O     . PRO A 1 2425 ? 223.924 263.152 251.300 1.00 18.30 ? 2425 PRO A O     1 
ATOM   7588  C  CB    . PRO A 1 2425 ? 226.194 262.010 253.422 1.00 7.72  ? 2425 PRO A CB    1 
ATOM   7589  C  CG    . PRO A 1 2425 ? 226.550 260.941 254.368 1.00 6.42  ? 2425 PRO A CG    1 
ATOM   7590  C  CD    . PRO A 1 2425 ? 225.940 259.697 253.810 1.00 8.41  ? 2425 PRO A CD    1 
ATOM   7591  N  N     . TYR A 1 2426 ? 225.005 261.337 250.533 1.00 11.76 ? 2426 TYR A N     1 
ATOM   7592  C  CA    . TYR A 1 2426 ? 224.859 261.724 249.136 1.00 7.97  ? 2426 TYR A CA    1 
ATOM   7593  C  C     . TYR A 1 2426 ? 223.482 261.418 248.567 1.00 9.49  ? 2426 TYR A C     1 
ATOM   7594  O  O     . TYR A 1 2426 ? 223.150 261.931 247.494 1.00 12.99 ? 2426 TYR A O     1 
ATOM   7595  C  CB    . TYR A 1 2426 ? 225.929 261.036 248.288 1.00 12.27 ? 2426 TYR A CB    1 
ATOM   7596  C  CG    . TYR A 1 2426 ? 227.322 261.191 248.839 1.00 9.20  ? 2426 TYR A CG    1 
ATOM   7597  C  CD1   . TYR A 1 2426 ? 227.900 260.198 249.618 1.00 10.01 ? 2426 TYR A CD1   1 
ATOM   7598  C  CD2   . TYR A 1 2426 ? 228.059 262.337 248.586 1.00 7.30  ? 2426 TYR A CD2   1 
ATOM   7599  C  CE1   . TYR A 1 2426 ? 229.174 260.346 250.126 1.00 10.19 ? 2426 TYR A CE1   1 
ATOM   7600  C  CE2   . TYR A 1 2426 ? 229.329 262.491 249.086 1.00 8.30  ? 2426 TYR A CE2   1 
ATOM   7601  C  CZ    . TYR A 1 2426 ? 229.882 261.496 249.856 1.00 13.22 ? 2426 TYR A CZ    1 
ATOM   7602  O  OH    . TYR A 1 2426 ? 231.153 261.658 250.352 1.00 21.45 ? 2426 TYR A OH    1 
ATOM   7603  N  N     . PHE A 1 2427 ? 222.678 260.610 249.251 1.00 11.10 ? 2427 PHE A N     1 
ATOM   7604  C  CA    . PHE A 1 2427 ? 221.350 260.247 248.778 1.00 10.00 ? 2427 PHE A CA    1 
ATOM   7605  C  C     . PHE A 1 2427 ? 220.247 261.036 249.466 1.00 9.53  ? 2427 PHE A C     1 
ATOM   7606  O  O     . PHE A 1 2427 ? 219.075 260.659 249.367 1.00 20.91 ? 2427 PHE A O     1 
ATOM   7607  C  CB    . PHE A 1 2427 ? 221.119 258.748 248.958 1.00 8.88  ? 2427 PHE A CB    1 
ATOM   7608  C  CG    . PHE A 1 2427 ? 221.698 257.919 247.855 1.00 7.51  ? 2427 PHE A CG    1 
ATOM   7609  C  CD1   . PHE A 1 2427 ? 221.076 257.858 246.621 1.00 4.89  ? 2427 PHE A CD1   1 
ATOM   7610  C  CD2   . PHE A 1 2427 ? 222.872 257.211 248.044 1.00 9.00  ? 2427 PHE A CD2   1 
ATOM   7611  C  CE1   . PHE A 1 2427 ? 221.607 257.100 245.603 1.00 6.49  ? 2427 PHE A CE1   1 
ATOM   7612  C  CE2   . PHE A 1 2427 ? 223.409 256.451 247.027 1.00 5.54  ? 2427 PHE A CE2   1 
ATOM   7613  C  CZ    . PHE A 1 2427 ? 222.775 256.394 245.805 1.00 2.99  ? 2427 PHE A CZ    1 
ATOM   7614  N  N     . THR A 1 2428 ? 220.593 262.105 250.172 1.00 13.66 ? 2428 THR A N     1 
ATOM   7615  C  CA    . THR A 1 2428 ? 219.591 263.000 250.724 1.00 16.24 ? 2428 THR A CA    1 
ATOM   7616  C  C     . THR A 1 2428 ? 219.059 263.926 249.635 1.00 17.10 ? 2428 THR A C     1 
ATOM   7617  O  O     . THR A 1 2428 ? 219.654 264.075 248.565 1.00 21.27 ? 2428 THR A O     1 
ATOM   7618  C  CB    . THR A 1 2428 ? 220.175 263.830 251.867 1.00 15.37 ? 2428 THR A CB    1 
ATOM   7619  O  OG1   . THR A 1 2428 ? 221.080 264.804 251.333 1.00 15.11 ? 2428 THR A OG1   1 
ATOM   7620  C  CG2   . THR A 1 2428 ? 220.918 262.938 252.850 1.00 11.20 ? 2428 THR A CG2   1 
ATOM   7621  N  N     . SER A 1 2429 ? 217.916 264.546 249.920 1.00 21.28 ? 2429 SER A N     1 
ATOM   7622  C  CA    . SER A 1 2429 ? 217.369 265.540 249.008 1.00 15.94 ? 2429 SER A CA    1 
ATOM   7623  C  C     . SER A 1 2429 ? 218.328 266.719 248.888 1.00 20.14 ? 2429 SER A C     1 
ATOM   7624  O  O     . SER A 1 2429 ? 218.918 267.163 249.878 1.00 24.58 ? 2429 SER A O     1 
ATOM   7625  C  CB    . SER A 1 2429 ? 215.999 266.013 249.497 1.00 24.19 ? 2429 SER A CB    1 
ATOM   7626  O  OG    . SER A 1 2429 ? 216.081 266.534 250.812 1.00 30.48 ? 2429 SER A OG    1 
ATOM   7627  N  N     . ASN A 1 2430 ? 218.482 267.224 247.662 1.00 18.30 ? 2430 ASN A N     1 
ATOM   7628  C  CA    . ASN A 1 2430 ? 219.483 268.243 247.337 1.00 15.04 ? 2430 ASN A CA    1 
ATOM   7629  C  C     . ASN A 1 2430 ? 220.897 267.750 247.622 1.00 16.80 ? 2430 ASN A C     1 
ATOM   7630  O  O     . ASN A 1 2430 ? 221.781 268.532 247.982 1.00 20.22 ? 2430 ASN A O     1 
ATOM   7631  C  CB    . ASN A 1 2430 ? 219.215 269.558 248.077 1.00 17.57 ? 2430 ASN A CB    1 
ATOM   7632  C  CG    . ASN A 1 2430 ? 217.923 270.215 247.645 1.00 25.11 ? 2430 ASN A CG    1 
ATOM   7633  O  OD1   . ASN A 1 2430 ? 217.217 269.708 246.776 1.00 21.56 ? 2430 ASN A OD1   1 
ATOM   7634  N  ND2   . ASN A 1 2430 ? 217.604 271.351 248.254 1.00 24.73 ? 2430 ASN A ND2   1 
ATOM   7635  N  N     . GLY A 1 2431 ? 221.119 266.447 247.470 1.00 13.97 ? 2431 GLY A N     1 
ATOM   7636  C  CA    . GLY A 1 2431 ? 222.434 265.863 247.607 1.00 9.44  ? 2431 GLY A CA    1 
ATOM   7637  C  C     . GLY A 1 2431 ? 223.162 265.790 246.278 1.00 11.35 ? 2431 GLY A C     1 
ATOM   7638  O  O     . GLY A 1 2431 ? 222.774 266.404 245.282 1.00 12.20 ? 2431 GLY A O     1 
ATOM   7639  N  N     . LEU A 1 2432 ? 224.252 265.022 246.278 1.00 10.82 ? 2432 LEU A N     1 
ATOM   7640  C  CA    . LEU A 1 2432 ? 225.058 264.878 245.071 1.00 5.70  ? 2432 LEU A CA    1 
ATOM   7641  C  C     . LEU A 1 2432 ? 224.269 264.209 243.952 1.00 6.14  ? 2432 LEU A C     1 
ATOM   7642  O  O     . LEU A 1 2432 ? 224.281 264.671 242.806 1.00 11.13 ? 2432 LEU A O     1 
ATOM   7643  C  CB    . LEU A 1 2432 ? 226.325 264.085 245.387 1.00 4.78  ? 2432 LEU A CB    1 
ATOM   7644  C  CG    . LEU A 1 2432 ? 227.206 263.705 244.197 1.00 5.37  ? 2432 LEU A CG    1 
ATOM   7645  C  CD1   . LEU A 1 2432 ? 227.845 264.940 243.586 1.00 11.70 ? 2432 LEU A CD1   1 
ATOM   7646  C  CD2   . LEU A 1 2432 ? 228.266 262.708 244.620 1.00 8.82  ? 2432 LEU A CD2   1 
ATOM   7647  N  N     . VAL A 1 2433 ? 223.568 263.121 244.270 1.00 6.96  ? 2433 VAL A N     1 
ATOM   7648  C  CA    . VAL A 1 2433 ? 222.867 262.364 243.237 1.00 3.68  ? 2433 VAL A CA    1 
ATOM   7649  C  C     . VAL A 1 2433 ? 221.692 263.162 242.688 1.00 5.49  ? 2433 VAL A C     1 
ATOM   7650  O  O     . VAL A 1 2433 ? 221.403 263.120 241.486 1.00 6.68  ? 2433 VAL A O     1 
ATOM   7651  C  CB    . VAL A 1 2433 ? 222.421 260.997 243.789 1.00 4.37  ? 2433 VAL A CB    1 
ATOM   7652  C  CG1   . VAL A 1 2433 ? 221.769 260.175 242.698 1.00 3.11  ? 2433 VAL A CG1   1 
ATOM   7653  C  CG2   . VAL A 1 2433 ? 223.603 260.258 244.388 1.00 6.14  ? 2433 VAL A CG2   1 
ATOM   7654  N  N     . THR A 1 2434 ? 220.989 263.895 243.555 1.00 10.88 ? 2434 THR A N     1 
ATOM   7655  C  CA    . THR A 1 2434 ? 219.866 264.708 243.100 1.00 6.25  ? 2434 THR A CA    1 
ATOM   7656  C  C     . THR A 1 2434 ? 220.332 265.810 242.157 1.00 6.40  ? 2434 THR A C     1 
ATOM   7657  O  O     . THR A 1 2434 ? 219.732 266.032 241.100 1.00 7.04  ? 2434 THR A O     1 
ATOM   7658  C  CB    . THR A 1 2434 ? 219.126 265.296 244.302 1.00 10.42 ? 2434 THR A CB    1 
ATOM   7659  O  OG1   . THR A 1 2434 ? 218.631 264.235 245.127 1.00 15.33 ? 2434 THR A OG1   1 
ATOM   7660  C  CG2   . THR A 1 2434 ? 217.956 266.152 243.846 1.00 8.20  ? 2434 THR A CG2   1 
ATOM   7661  N  N     . LYS A 1 2435 ? 221.408 266.513 242.523 1.00 6.67  ? 2435 LYS A N     1 
ATOM   7662  C  CA    . LYS A 1 2435 ? 221.921 267.573 241.662 1.00 5.67  ? 2435 LYS A CA    1 
ATOM   7663  C  C     . LYS A 1 2435 ? 222.472 267.013 240.358 1.00 6.46  ? 2435 LYS A C     1 
ATOM   7664  O  O     . LYS A 1 2435 ? 222.295 267.615 239.291 1.00 7.44  ? 2435 LYS A O     1 
ATOM   7665  C  CB    . LYS A 1 2435 ? 222.996 268.380 242.390 1.00 8.15  ? 2435 LYS A CB    1 
ATOM   7666  C  CG    . LYS A 1 2435 ? 222.483 269.185 243.567 1.00 10.54 ? 2435 LYS A CG    1 
ATOM   7667  C  CD    . LYS A 1 2435 ? 223.569 270.084 244.133 1.00 11.38 ? 2435 LYS A CD    1 
ATOM   7668  C  CE    . LYS A 1 2435 ? 224.600 269.291 244.909 1.00 19.74 ? 2435 LYS A CE    1 
ATOM   7669  N  NZ    . LYS A 1 2435 ? 225.605 270.182 245.554 1.00 26.56 ? 2435 LYS A NZ    1 
ATOM   7670  N  N     . ALA A 1 2436 ? 223.152 265.868 240.425 1.00 8.76  ? 2436 ALA A N     1 
ATOM   7671  C  CA    . ALA A 1 2436 ? 223.655 265.233 239.212 1.00 3.07  ? 2436 ALA A CA    1 
ATOM   7672  C  C     . ALA A 1 2436 ? 222.510 264.824 238.293 1.00 2.83  ? 2436 ALA A C     1 
ATOM   7673  O  O     . ALA A 1 2436 ? 222.603 264.975 237.070 1.00 6.07  ? 2436 ALA A O     1 
ATOM   7674  C  CB    . ALA A 1 2436 ? 224.515 264.024 239.572 1.00 3.67  ? 2436 ALA A CB    1 
ATOM   7675  N  N     . LEU A 1 2437 ? 221.427 264.299 238.867 1.00 2.81  ? 2437 LEU A N     1 
ATOM   7676  C  CA    . LEU A 1 2437 ? 220.286 263.871 238.064 1.00 3.47  ? 2437 LEU A CA    1 
ATOM   7677  C  C     . LEU A 1 2437 ? 219.647 265.049 237.339 1.00 5.34  ? 2437 LEU A C     1 
ATOM   7678  O  O     . LEU A 1 2437 ? 219.306 264.952 236.155 1.00 5.17  ? 2437 LEU A O     1 
ATOM   7679  C  CB    . LEU A 1 2437 ? 219.264 263.161 238.952 1.00 3.91  ? 2437 LEU A CB    1 
ATOM   7680  C  CG    . LEU A 1 2437 ? 218.110 262.451 238.247 1.00 6.61  ? 2437 LEU A CG    1 
ATOM   7681  C  CD1   . LEU A 1 2437 ? 218.638 261.379 237.309 1.00 8.67  ? 2437 LEU A CD1   1 
ATOM   7682  C  CD2   . LEU A 1 2437 ? 217.159 261.856 239.269 1.00 6.87  ? 2437 LEU A CD2   1 
ATOM   7683  N  N     . GLU A 1 2438 ? 219.484 266.177 238.034 1.00 5.68  ? 2438 GLU A N     1 
ATOM   7684  C  CA    . GLU A 1 2438 ? 218.882 267.353 237.414 1.00 10.37 ? 2438 GLU A CA    1 
ATOM   7685  C  C     . GLU A 1 2438 ? 219.737 267.868 236.263 1.00 7.60  ? 2438 GLU A C     1 
ATOM   7686  O  O     . GLU A 1 2438 ? 219.214 268.279 235.219 1.00 6.30  ? 2438 GLU A O     1 
ATOM   7687  C  CB    . GLU A 1 2438 ? 218.671 268.448 238.462 1.00 7.95  ? 2438 GLU A CB    1 
ATOM   7688  C  CG    . GLU A 1 2438 ? 217.651 268.096 239.530 1.00 18.79 ? 2438 GLU A CG    1 
ATOM   7689  C  CD    . GLU A 1 2438 ? 216.240 267.977 238.980 1.00 29.60 ? 2438 GLU A CD    1 
ATOM   7690  O  OE1   . GLU A 1 2438 ? 215.913 268.694 238.010 1.00 31.60 ? 2438 GLU A OE1   1 
ATOM   7691  O  OE2   . GLU A 1 2438 ? 215.460 267.163 239.514 1.00 34.40 ? 2438 GLU A OE2   1 
ATOM   7692  N  N     . HIS A 1 2439 ? 221.059 267.861 236.439 1.00 4.65  ? 2439 HIS A N     1 
ATOM   7693  C  CA    . HIS A 1 2439 ? 221.949 268.324 235.380 1.00 6.72  ? 2439 HIS A CA    1 
ATOM   7694  C  C     . HIS A 1 2439 ? 221.946 267.368 234.195 1.00 6.63  ? 2439 HIS A C     1 
ATOM   7695  O  O     . HIS A 1 2439 ? 222.062 267.796 233.041 1.00 6.03  ? 2439 HIS A O     1 
ATOM   7696  C  CB    . HIS A 1 2439 ? 223.365 268.491 235.927 1.00 9.28  ? 2439 HIS A CB    1 
ATOM   7697  C  CG    . HIS A 1 2439 ? 224.302 269.171 234.982 1.00 10.56 ? 2439 HIS A CG    1 
ATOM   7698  N  ND1   . HIS A 1 2439 ? 224.171 270.496 234.628 1.00 8.70  ? 2439 HIS A ND1   1 
ATOM   7699  C  CD2   . HIS A 1 2439 ? 225.387 268.710 234.316 1.00 14.87 ? 2439 HIS A CD2   1 
ATOM   7700  C  CE1   . HIS A 1 2439 ? 225.133 270.821 233.782 1.00 13.49 ? 2439 HIS A CE1   1 
ATOM   7701  N  NE2   . HIS A 1 2439 ? 225.885 269.755 233.578 1.00 11.13 ? 2439 HIS A NE2   1 
ATOM   7702  N  N     . ALA A 1 2440 ? 221.818 266.065 234.461 1.00 6.89  ? 2440 ALA A N     1 
ATOM   7703  C  CA    . ALA A 1 2440 ? 221.844 265.079 233.385 1.00 3.70  ? 2440 ALA A CA    1 
ATOM   7704  C  C     . ALA A 1 2440 ? 220.667 265.258 232.436 1.00 3.13  ? 2440 ALA A C     1 
ATOM   7705  O  O     . ALA A 1 2440 ? 220.802 265.052 231.224 1.00 4.59  ? 2440 ALA A O     1 
ATOM   7706  C  CB    . ALA A 1 2440 ? 221.857 263.668 233.971 1.00 3.87  ? 2440 ALA A CB    1 
ATOM   7707  N  N     . PHE A 1 2441 ? 219.499 265.632 232.967 1.00 3.98  ? 2441 PHE A N     1 
ATOM   7708  C  CA    . PHE A 1 2441 ? 218.333 265.842 232.113 1.00 5.14  ? 2441 PHE A CA    1 
ATOM   7709  C  C     . PHE A 1 2441 ? 218.544 266.998 231.144 1.00 5.08  ? 2441 PHE A C     1 
ATOM   7710  O  O     . PHE A 1 2441 ? 217.879 267.066 230.106 1.00 7.85  ? 2441 PHE A O     1 
ATOM   7711  C  CB    . PHE A 1 2441 ? 217.087 266.084 232.965 1.00 2.35  ? 2441 PHE A CB    1 
ATOM   7712  C  CG    . PHE A 1 2441 ? 216.408 264.823 233.418 1.00 2.89  ? 2441 PHE A CG    1 
ATOM   7713  C  CD1   . PHE A 1 2441 ? 215.450 264.216 232.624 1.00 3.09  ? 2441 PHE A CD1   1 
ATOM   7714  C  CD2   . PHE A 1 2441 ? 216.727 264.246 234.634 1.00 2.95  ? 2441 PHE A CD2   1 
ATOM   7715  C  CE1   . PHE A 1 2441 ? 214.825 263.055 233.035 1.00 2.05  ? 2441 PHE A CE1   1 
ATOM   7716  C  CE2   . PHE A 1 2441 ? 216.105 263.084 235.051 1.00 3.34  ? 2441 PHE A CE2   1 
ATOM   7717  C  CZ    . PHE A 1 2441 ? 215.151 262.489 234.249 1.00 5.70  ? 2441 PHE A CZ    1 
ATOM   7718  N  N     . GLN A 1 2442 ? 219.459 267.915 231.462 1.00 5.97  ? 2442 GLN A N     1 
ATOM   7719  C  CA    . GLN A 1 2442 ? 219.745 269.019 230.559 1.00 7.14  ? 2442 GLN A CA    1 
ATOM   7720  C  C     . GLN A 1 2442 ? 220.629 268.598 229.394 1.00 8.47  ? 2442 GLN A C     1 
ATOM   7721  O  O     . GLN A 1 2442 ? 220.700 269.316 228.394 1.00 15.12 ? 2442 GLN A O     1 
ATOM   7722  C  CB    . GLN A 1 2442 ? 220.400 270.165 231.328 1.00 8.46  ? 2442 GLN A CB    1 
ATOM   7723  C  CG    . GLN A 1 2442 ? 219.484 270.784 232.363 1.00 9.44  ? 2442 GLN A CG    1 
ATOM   7724  C  CD    . GLN A 1 2442 ? 218.254 271.406 231.742 1.00 22.94 ? 2442 GLN A CD    1 
ATOM   7725  O  OE1   . GLN A 1 2442 ? 217.144 270.891 231.890 1.00 28.40 ? 2442 GLN A OE1   1 
ATOM   7726  N  NE2   . GLN A 1 2442 ? 218.439 272.521 231.045 1.00 17.08 ? 2442 GLN A NE2   1 
ATOM   7727  N  N     . LEU A 1 2443 ? 221.293 267.452 229.497 1.00 8.29  ? 2443 LEU A N     1 
ATOM   7728  C  CA    . LEU A 1 2443 ? 222.213 267.002 228.469 1.00 6.22  ? 2443 LEU A CA    1 
ATOM   7729  C  C     . LEU A 1 2443 ? 221.481 266.210 227.391 1.00 6.10  ? 2443 LEU A C     1 
ATOM   7730  O  O     . LEU A 1 2443 ? 220.310 265.849 227.529 1.00 10.89 ? 2443 LEU A O     1 
ATOM   7731  C  CB    . LEU A 1 2443 ? 223.322 266.153 229.084 1.00 5.39  ? 2443 LEU A CB    1 
ATOM   7732  C  CG    . LEU A 1 2443 ? 224.122 266.898 230.144 1.00 8.81  ? 2443 LEU A CG    1 
ATOM   7733  C  CD1   . LEU A 1 2443 ? 225.123 265.989 230.837 1.00 10.33 ? 2443 LEU A CD1   1 
ATOM   7734  C  CD2   . LEU A 1 2443 ? 224.813 268.075 229.496 1.00 5.54  ? 2443 LEU A CD2   1 
ATOM   7735  N  N     . GLU A 1 2444 ? 222.192 265.947 226.301 1.00 5.80  ? 2444 GLU A N     1 
ATOM   7736  C  CA    . GLU A 1 2444 ? 221.654 265.155 225.206 1.00 7.62  ? 2444 GLU A CA    1 
ATOM   7737  C  C     . GLU A 1 2444 ? 222.074 263.701 225.362 1.00 6.20  ? 2444 GLU A C     1 
ATOM   7738  O  O     . GLU A 1 2444 ? 223.235 263.402 225.656 1.00 6.20  ? 2444 GLU A O     1 
ATOM   7739  C  CB    . GLU A 1 2444 ? 222.116 265.699 223.854 1.00 8.67  ? 2444 GLU A CB    1 
ATOM   7740  C  CG    . GLU A 1 2444 ? 221.576 267.078 223.530 1.00 16.93 ? 2444 GLU A CG    1 
ATOM   7741  C  CD    . GLU A 1 2444 ? 220.072 267.086 223.329 1.00 23.97 ? 2444 GLU A CD    1 
ATOM   7742  O  OE1   . GLU A 1 2444 ? 219.525 266.068 222.853 1.00 23.85 ? 2444 GLU A OE1   1 
ATOM   7743  O  OE2   . GLU A 1 2444 ? 219.433 268.110 223.649 1.00 26.58 ? 2444 GLU A OE2   1 
ATOM   7744  N  N     . HIS A 1 2445 ? 221.118 262.802 225.172 1.00 5.50  ? 2445 HIS A N     1 
ATOM   7745  C  CA    . HIS A 1 2445 ? 221.340 261.375 225.320 1.00 2.85  ? 2445 HIS A CA    1 
ATOM   7746  C  C     . HIS A 1 2445 ? 220.862 260.659 224.067 1.00 2.85  ? 2445 HIS A C     1 
ATOM   7747  O  O     . HIS A 1 2445 ? 219.952 261.123 223.378 1.00 3.44  ? 2445 HIS A O     1 
ATOM   7748  C  CB    . HIS A 1 2445 ? 220.615 260.832 226.556 1.00 2.56  ? 2445 HIS A CB    1 
ATOM   7749  C  CG    . HIS A 1 2445 ? 220.838 261.647 227.789 1.00 4.94  ? 2445 HIS A CG    1 
ATOM   7750  N  ND1   . HIS A 1 2445 ? 221.865 261.393 228.674 1.00 5.27  ? 2445 HIS A ND1   1 
ATOM   7751  C  CD2   . HIS A 1 2445 ? 220.179 262.721 228.280 1.00 4.30  ? 2445 HIS A CD2   1 
ATOM   7752  C  CE1   . HIS A 1 2445 ? 221.823 262.269 229.659 1.00 2.38  ? 2445 HIS A CE1   1 
ATOM   7753  N  NE2   . HIS A 1 2445 ? 220.811 263.089 229.443 1.00 4.27  ? 2445 HIS A NE2   1 
ATOM   7754  N  N     . ILE A 1 2446 ? 221.494 259.519 223.774 1.00 1.59  ? 2446 ILE A N     1 
ATOM   7755  C  CA    . ILE A 1 2446 ? 221.146 258.774 222.567 1.00 2.09  ? 2446 ILE A CA    1 
ATOM   7756  C  C     . ILE A 1 2446 ? 219.713 258.263 222.644 1.00 2.21  ? 2446 ILE A C     1 
ATOM   7757  O  O     . ILE A 1 2446 ? 219.053 258.082 221.615 1.00 3.28  ? 2446 ILE A O     1 
ATOM   7758  C  CB    . ILE A 1 2446 ? 222.160 257.633 222.329 1.00 2.79  ? 2446 ILE A CB    1 
ATOM   7759  C  CG1   . ILE A 1 2446 ? 222.259 257.307 220.838 1.00 3.24  ? 2446 ILE A CG1   1 
ATOM   7760  C  CG2   . ILE A 1 2446 ? 221.801 256.390 223.127 1.00 2.17  ? 2446 ILE A CG2   1 
ATOM   7761  C  CD1   . ILE A 1 2446 ? 222.681 258.478 219.987 1.00 2.31  ? 2446 ILE A CD1   1 
ATOM   7762  N  N     . MET A 1 2447 ? 219.204 258.041 223.852 1.00 2.97  ? 2447 MET A N     1 
ATOM   7763  C  CA    . MET A 1 2447 ? 217.814 257.679 224.069 1.00 2.09  ? 2447 MET A CA    1 
ATOM   7764  C  C     . MET A 1 2447 ? 217.193 258.672 225.039 1.00 2.09  ? 2447 MET A C     1 
ATOM   7765  O  O     . MET A 1 2447 ? 217.894 259.391 225.751 1.00 2.12  ? 2447 MET A O     1 
ATOM   7766  C  CB    . MET A 1 2447 ? 217.677 256.252 224.614 1.00 4.33  ? 2447 MET A CB    1 
ATOM   7767  C  CG    . MET A 1 2447 ? 217.958 255.178 223.589 1.00 4.30  ? 2447 MET A CG    1 
ATOM   7768  S  SD    . MET A 1 2447 ? 217.375 253.559 224.110 1.00 12.05 ? 2447 MET A SD    1 
ATOM   7769  C  CE    . MET A 1 2447 ? 217.882 252.581 222.708 1.00 0.94  ? 2447 MET A CE    1 
ATOM   7770  N  N     . ASP A 1 2448 ? 215.861 258.715 225.045 1.00 2.66  ? 2448 ASP A N     1 
ATOM   7771  C  CA    . ASP A 1 2448 ? 215.150 259.581 225.977 1.00 1.74  ? 2448 ASP A CA    1 
ATOM   7772  C  C     . ASP A 1 2448 ? 215.523 259.230 227.410 1.00 2.38  ? 2448 ASP A C     1 
ATOM   7773  O  O     . ASP A 1 2448 ? 215.609 258.054 227.773 1.00 5.06  ? 2448 ASP A O     1 
ATOM   7774  C  CB    . ASP A 1 2448 ? 213.644 259.457 225.771 1.00 3.07  ? 2448 ASP A CB    1 
ATOM   7775  C  CG    . ASP A 1 2448 ? 213.165 260.170 224.524 1.00 12.52 ? 2448 ASP A CG    1 
ATOM   7776  O  OD1   . ASP A 1 2448 ? 213.970 260.894 223.902 1.00 15.40 ? 2448 ASP A OD1   1 
ATOM   7777  O  OD2   . ASP A 1 2448 ? 211.982 260.004 224.163 1.00 13.85 ? 2448 ASP A OD2   1 
ATOM   7778  N  N     . LEU A 1 2449 ? 215.750 260.252 228.224 1.00 2.69  ? 2449 LEU A N     1 
ATOM   7779  C  CA    . LEU A 1 2449 ? 216.254 260.054 229.573 1.00 1.55  ? 2449 LEU A CA    1 
ATOM   7780  C  C     . LEU A 1 2449 ? 215.093 260.057 230.556 1.00 3.01  ? 2449 LEU A C     1 
ATOM   7781  O  O     . LEU A 1 2449 ? 214.257 260.966 230.536 1.00 4.68  ? 2449 LEU A O     1 
ATOM   7782  C  CB    . LEU A 1 2449 ? 217.254 261.150 229.939 1.00 2.24  ? 2449 LEU A CB    1 
ATOM   7783  C  CG    . LEU A 1 2449 ? 217.922 260.921 231.291 1.00 4.76  ? 2449 LEU A CG    1 
ATOM   7784  C  CD1   . LEU A 1 2449 ? 218.733 259.650 231.173 1.00 1.92  ? 2449 LEU A CD1   1 
ATOM   7785  C  CD2   . LEU A 1 2449 ? 218.776 262.087 231.740 1.00 3.89  ? 2449 LEU A CD2   1 
ATOM   7786  N  N     . THR A 1 2450 ? 215.036 259.037 231.408 1.00 2.06  ? 2450 THR A N     1 
ATOM   7787  C  CA    . THR A 1 2450 ? 214.054 258.975 232.479 1.00 1.24  ? 2450 THR A CA    1 
ATOM   7788  C  C     . THR A 1 2450 ? 214.767 258.778 233.810 1.00 1.37  ? 2450 THR A C     1 
ATOM   7789  O  O     . THR A 1 2450 ? 215.886 258.263 233.872 1.00 4.17  ? 2450 THR A O     1 
ATOM   7790  C  CB    . THR A 1 2450 ? 213.027 257.849 232.258 1.00 2.53  ? 2450 THR A CB    1 
ATOM   7791  O  OG1   . THR A 1 2450 ? 213.668 256.572 232.363 1.00 9.05  ? 2450 THR A OG1   1 
ATOM   7792  C  CG2   . THR A 1 2450 ? 212.364 257.984 230.895 1.00 1.72  ? 2450 THR A CG2   1 
ATOM   7793  N  N     . ARG A 1 2451 ? 214.098 259.211 234.881 1.00 1.77  ? 2451 ARG A N     1 
ATOM   7794  C  CA    . ARG A 1 2451 ? 214.713 259.193 236.203 1.00 2.02  ? 2451 ARG A CA    1 
ATOM   7795  C  C     . ARG A 1 2451 ? 215.052 257.775 236.647 1.00 0.88  ? 2451 ARG A C     1 
ATOM   7796  O  O     . ARG A 1 2451 ? 216.126 257.532 237.207 1.00 1.31  ? 2451 ARG A O     1 
ATOM   7797  C  CB    . ARG A 1 2451 ? 213.786 259.865 237.217 1.00 2.60  ? 2451 ARG A CB    1 
ATOM   7798  C  CG    . ARG A 1 2451 ? 214.174 259.623 238.665 1.00 1.74  ? 2451 ARG A CG    1 
ATOM   7799  C  CD    . ARG A 1 2451 ? 213.235 260.321 239.628 1.00 3.75  ? 2451 ARG A CD    1 
ATOM   7800  N  NE    . ARG A 1 2451 ? 211.844 259.924 239.441 1.00 2.64  ? 2451 ARG A NE    1 
ATOM   7801  C  CZ    . ARG A 1 2451 ? 210.851 260.288 240.240 1.00 2.26  ? 2451 ARG A CZ    1 
ATOM   7802  N  NH1   . ARG A 1 2451 ? 211.060 261.055 241.296 1.00 2.06  ? 2451 ARG A NH1   1 
ATOM   7803  N  NH2   . ARG A 1 2451 ? 209.619 259.866 239.977 1.00 3.05  ? 2451 ARG A NH2   1 
ATOM   7804  N  N     . LEU A 1 2452 ? 214.152 256.825 236.401 1.00 1.11  ? 2452 LEU A N     1 
ATOM   7805  C  CA    . LEU A 1 2452 ? 214.342 255.478 236.921 1.00 0.65  ? 2452 LEU A CA    1 
ATOM   7806  C  C     . LEU A 1 2452 ? 215.359 254.674 236.120 1.00 0.95  ? 2452 LEU A C     1 
ATOM   7807  O  O     . LEU A 1 2452 ? 215.952 253.734 236.660 1.00 0.99  ? 2452 LEU A O     1 
ATOM   7808  C  CB    . LEU A 1 2452 ? 213.002 254.752 236.979 1.00 0.82  ? 2452 LEU A CB    1 
ATOM   7809  C  CG    . LEU A 1 2452 ? 212.155 255.201 238.173 1.00 0.70  ? 2452 LEU A CG    1 
ATOM   7810  C  CD1   . LEU A 1 2452 ? 210.993 254.273 238.389 1.00 0.65  ? 2452 LEU A CD1   1 
ATOM   7811  C  CD2   . LEU A 1 2452 ? 213.010 255.277 239.427 1.00 0.62  ? 2452 LEU A CD2   1 
ATOM   7812  N  N     . ARG A 1 2453 ? 215.579 255.009 234.846 1.00 1.38  ? 2453 ARG A N     1 
ATOM   7813  C  CA    . ARG A 1 2453 ? 216.651 254.349 234.109 1.00 1.00  ? 2453 ARG A CA    1 
ATOM   7814  C  C     . ARG A 1 2453 ? 218.010 254.692 234.703 1.00 1.02  ? 2453 ARG A C     1 
ATOM   7815  O  O     . ARG A 1 2453 ? 218.878 253.821 234.834 1.00 2.52  ? 2453 ARG A O     1 
ATOM   7816  C  CB    . ARG A 1 2453 ? 216.603 254.715 232.625 1.00 0.91  ? 2453 ARG A CB    1 
ATOM   7817  C  CG    . ARG A 1 2453 ? 217.687 254.010 231.813 1.00 0.77  ? 2453 ARG A CG    1 
ATOM   7818  C  CD    . ARG A 1 2453 ? 217.497 254.114 230.307 1.00 0.72  ? 2453 ARG A CD    1 
ATOM   7819  N  NE    . ARG A 1 2453 ? 217.490 255.484 229.815 1.00 3.74  ? 2453 ARG A NE    1 
ATOM   7820  C  CZ    . ARG A 1 2453 ? 218.531 256.083 229.253 1.00 2.50  ? 2453 ARG A CZ    1 
ATOM   7821  N  NH1   . ARG A 1 2453 ? 219.708 255.490 229.172 1.00 1.49  ? 2453 ARG A NH1   1 
ATOM   7822  N  NH2   . ARG A 1 2453 ? 218.388 257.313 228.770 1.00 5.48  ? 2453 ARG A NH2   1 
ATOM   7823  N  N     . CYS A 1 2454 ? 218.209 255.956 235.082 1.00 1.50  ? 2454 CYS A N     1 
ATOM   7824  C  CA    . CYS A 1 2454 ? 219.456 256.355 235.725 1.00 1.41  ? 2454 CYS A CA    1 
ATOM   7825  C  C     . CYS A 1 2454 ? 219.602 255.705 237.091 1.00 0.91  ? 2454 CYS A C     1 
ATOM   7826  O  O     . CYS A 1 2454 ? 220.647 255.127 237.410 1.00 1.48  ? 2454 CYS A O     1 
ATOM   7827  C  CB    . CYS A 1 2454 ? 219.511 257.874 235.868 1.00 3.58  ? 2454 CYS A CB    1 
ATOM   7828  S  SG    . CYS A 1 2454 ? 219.165 258.772 234.373 1.00 12.23 ? 2454 CYS A SG    1 
ATOM   7829  N  N     . LEU A 1 2455 ? 218.561 255.806 237.920 1.00 1.09  ? 2455 LEU A N     1 
ATOM   7830  C  CA    . LEU A 1 2455 ? 218.640 255.283 239.278 1.00 0.82  ? 2455 LEU A CA    1 
ATOM   7831  C  C     . LEU A 1 2455 ? 218.711 253.763 239.277 1.00 0.54  ? 2455 LEU A C     1 
ATOM   7832  O  O     . LEU A 1 2455 ? 219.443 253.171 240.079 1.00 1.24  ? 2455 LEU A O     1 
ATOM   7833  C  CB    . LEU A 1 2455 ? 217.448 255.780 240.093 1.00 0.90  ? 2455 LEU A CB    1 
ATOM   7834  C  CG    . LEU A 1 2455 ? 217.443 257.291 240.345 1.00 0.99  ? 2455 LEU A CG    1 
ATOM   7835  C  CD1   . LEU A 1 2455 ? 216.333 257.680 241.306 1.00 1.32  ? 2455 LEU A CD1   1 
ATOM   7836  C  CD2   . LEU A 1 2455 ? 218.794 257.761 240.859 1.00 0.76  ? 2455 LEU A CD2   1 
ATOM   7837  N  N     . GLY A 1 2456 ? 217.965 253.113 238.383 1.00 0.79  ? 2456 GLY A N     1 
ATOM   7838  C  CA    . GLY A 1 2456 ? 218.082 251.671 238.250 1.00 0.99  ? 2456 GLY A CA    1 
ATOM   7839  C  C     . GLY A 1 2456 ? 219.490 251.242 237.890 1.00 1.26  ? 2456 GLY A C     1 
ATOM   7840  O  O     . GLY A 1 2456 ? 220.012 250.268 238.437 1.00 1.16  ? 2456 GLY A O     1 
ATOM   7841  N  N     . SER A 1 2457 ? 220.123 251.965 236.965 1.00 1.13  ? 2457 SER A N     1 
ATOM   7842  C  CA    . SER A 1 2457 ? 221.526 251.712 236.656 1.00 0.84  ? 2457 SER A CA    1 
ATOM   7843  C  C     . SER A 1 2457 ? 222.420 252.037 237.844 1.00 1.21  ? 2457 SER A C     1 
ATOM   7844  O  O     . SER A 1 2457 ? 223.344 251.279 238.158 1.00 1.87  ? 2457 SER A O     1 
ATOM   7845  C  CB    . SER A 1 2457 ? 221.945 252.523 235.431 1.00 0.53  ? 2457 SER A CB    1 
ATOM   7846  O  OG    . SER A 1 2457 ? 223.336 252.402 235.194 1.00 1.50  ? 2457 SER A OG    1 
ATOM   7847  N  N     . LEU A 1 2458 ? 222.161 253.160 238.518 1.00 1.10  ? 2458 LEU A N     1 
ATOM   7848  C  CA    . LEU A 1 2458 ? 223.005 253.571 239.635 1.00 0.99  ? 2458 LEU A CA    1 
ATOM   7849  C  C     . LEU A 1 2458 ? 222.942 252.570 240.780 1.00 1.53  ? 2458 LEU A C     1 
ATOM   7850  O  O     . LEU A 1 2458 ? 223.967 252.256 241.396 1.00 1.45  ? 2458 LEU A O     1 
ATOM   7851  C  CB    . LEU A 1 2458 ? 222.592 254.962 240.117 1.00 1.39  ? 2458 LEU A CB    1 
ATOM   7852  C  CG    . LEU A 1 2458 ? 223.302 255.465 241.375 1.00 1.85  ? 2458 LEU A CG    1 
ATOM   7853  C  CD1   . LEU A 1 2458 ? 224.775 255.717 241.094 1.00 1.27  ? 2458 LEU A CD1   1 
ATOM   7854  C  CD2   . LEU A 1 2458 ? 222.634 256.712 241.917 1.00 0.55  ? 2458 LEU A CD2   1 
ATOM   7855  N  N     . PHE A 1 2459 ? 221.748 252.061 241.083 1.00 4.10  ? 2459 PHE A N     1 
ATOM   7856  C  CA    . PHE A 1 2459 ? 221.608 251.121 242.190 1.00 1.67  ? 2459 PHE A CA    1 
ATOM   7857  C  C     . PHE A 1 2459 ? 222.221 249.768 241.860 1.00 1.93  ? 2459 PHE A C     1 
ATOM   7858  O  O     . PHE A 1 2459 ? 222.766 249.104 242.751 1.00 3.06  ? 2459 PHE A O     1 
ATOM   7859  C  CB    . PHE A 1 2459 ? 220.133 250.967 242.562 1.00 1.32  ? 2459 PHE A CB    1 
ATOM   7860  C  CG    . PHE A 1 2459 ? 219.474 252.254 242.976 1.00 0.92  ? 2459 PHE A CG    1 
ATOM   7861  C  CD1   . PHE A 1 2459 ? 220.214 253.276 243.543 1.00 1.38  ? 2459 PHE A CD1   1 
ATOM   7862  C  CD2   . PHE A 1 2459 ? 218.114 252.437 242.795 1.00 0.88  ? 2459 PHE A CD2   1 
ATOM   7863  C  CE1   . PHE A 1 2459 ? 219.608 254.458 243.921 1.00 1.59  ? 2459 PHE A CE1   1 
ATOM   7864  C  CE2   . PHE A 1 2459 ? 217.506 253.618 243.170 1.00 1.09  ? 2459 PHE A CE2   1 
ATOM   7865  C  CZ    . PHE A 1 2459 ? 218.253 254.629 243.733 1.00 1.48  ? 2459 PHE A CZ    1 
ATOM   7866  N  N     . SER A 1 2460 ? 222.142 249.338 240.599 1.00 3.15  ? 2460 SER A N     1 
ATOM   7867  C  CA    . SER A 1 2460 ? 222.790 248.092 240.201 1.00 1.31  ? 2460 SER A CA    1 
ATOM   7868  C  C     . SER A 1 2460 ? 224.302 248.186 240.352 1.00 1.82  ? 2460 SER A C     1 
ATOM   7869  O  O     . SER A 1 2460 ? 224.946 247.238 240.813 1.00 4.22  ? 2460 SER A O     1 
ATOM   7870  C  CB    . SER A 1 2460 ? 222.420 247.741 238.760 1.00 1.36  ? 2460 SER A CB    1 
ATOM   7871  O  OG    . SER A 1 2460 ? 221.028 247.531 238.626 1.00 3.45  ? 2460 SER A OG    1 
ATOM   7872  N  N     . MET A 1 2461 ? 224.885 249.320 239.964 1.00 2.39  ? 2461 MET A N     1 
ATOM   7873  C  CA    . MET A 1 2461 ? 226.329 249.491 240.073 1.00 1.30  ? 2461 MET A CA    1 
ATOM   7874  C  C     . MET A 1 2461 ? 226.780 249.512 241.527 1.00 2.53  ? 2461 MET A C     1 
ATOM   7875  O  O     . MET A 1 2461 ? 227.812 248.924 241.870 1.00 9.94  ? 2461 MET A O     1 
ATOM   7876  C  CB    . MET A 1 2461 ? 226.759 250.767 239.351 1.00 2.13  ? 2461 MET A CB    1 
ATOM   7877  C  CG    . MET A 1 2461 ? 226.412 250.772 237.871 1.00 1.18  ? 2461 MET A CG    1 
ATOM   7878  S  SD    . MET A 1 2461 ? 227.251 252.047 236.917 1.00 1.65  ? 2461 MET A SD    1 
ATOM   7879  C  CE    . MET A 1 2461 ? 228.946 251.775 237.409 1.00 1.27  ? 2461 MET A CE    1 
ATOM   7880  N  N     . LEU A 1 2462 ? 226.019 250.176 242.399 1.00 2.59  ? 2462 LEU A N     1 
ATOM   7881  C  CA    . LEU A 1 2462 ? 226.383 250.222 243.811 1.00 2.23  ? 2462 LEU A CA    1 
ATOM   7882  C  C     . LEU A 1 2462 ? 226.284 248.850 244.462 1.00 2.75  ? 2462 LEU A C     1 
ATOM   7883  O  O     . LEU A 1 2462 ? 227.074 248.533 245.358 1.00 4.08  ? 2462 LEU A O     1 
ATOM   7884  C  CB    . LEU A 1 2462 ? 225.506 251.231 244.548 1.00 1.56  ? 2462 LEU A CB    1 
ATOM   7885  C  CG    . LEU A 1 2462 ? 225.719 252.694 244.157 1.00 2.17  ? 2462 LEU A CG    1 
ATOM   7886  C  CD1   . LEU A 1 2462 ? 224.709 253.589 244.852 1.00 3.31  ? 2462 LEU A CD1   1 
ATOM   7887  C  CD2   . LEU A 1 2462 ? 227.139 253.139 244.467 1.00 3.16  ? 2462 LEU A CD2   1 
ATOM   7888  N  N     . HIS A 1 2463 ? 225.324 248.026 244.035 1.00 3.64  ? 2463 HIS A N     1 
ATOM   7889  C  CA    . HIS A 1 2463 ? 225.255 246.655 244.527 1.00 4.88  ? 2463 HIS A CA    1 
ATOM   7890  C  C     . HIS A 1 2463 ? 226.501 245.873 244.135 1.00 7.38  ? 2463 HIS A C     1 
ATOM   7891  O  O     . HIS A 1 2463 ? 227.003 245.056 244.915 1.00 10.33 ? 2463 HIS A O     1 
ATOM   7892  C  CB    . HIS A 1 2463 ? 224.001 245.965 243.992 1.00 5.04  ? 2463 HIS A CB    1 
ATOM   7893  C  CG    . HIS A 1 2463 ? 222.736 246.400 244.662 1.00 4.25  ? 2463 HIS A CG    1 
ATOM   7894  N  ND1   . HIS A 1 2463 ? 221.497 246.261 244.075 1.00 5.79  ? 2463 HIS A ND1   1 
ATOM   7895  C  CD2   . HIS A 1 2463 ? 222.518 246.977 245.868 1.00 4.38  ? 2463 HIS A CD2   1 
ATOM   7896  C  CE1   . HIS A 1 2463 ? 220.571 246.729 244.890 1.00 4.73  ? 2463 HIS A CE1   1 
ATOM   7897  N  NE2   . HIS A 1 2463 ? 221.163 247.170 245.985 1.00 6.94  ? 2463 HIS A NE2   1 
ATOM   7898  N  N     . GLN A 1 2464 ? 227.009 246.108 242.923 1.00 9.34  ? 2464 GLN A N     1 
ATOM   7899  C  CA    . GLN A 1 2464 ? 228.244 245.462 242.490 1.00 6.79  ? 2464 GLN A CA    1 
ATOM   7900  C  C     . GLN A 1 2464 ? 229.426 245.913 243.336 1.00 7.28  ? 2464 GLN A C     1 
ATOM   7901  O  O     . GLN A 1 2464 ? 230.327 245.119 243.630 1.00 8.05  ? 2464 GLN A O     1 
ATOM   7902  C  CB    . GLN A 1 2464 ? 228.493 245.760 241.010 1.00 7.62  ? 2464 GLN A CB    1 
ATOM   7903  C  CG    . GLN A 1 2464 ? 229.715 245.081 240.415 1.00 9.28  ? 2464 GLN A CG    1 
ATOM   7904  C  CD    . GLN A 1 2464 ? 229.728 243.586 240.643 1.00 7.78  ? 2464 GLN A CD    1 
ATOM   7905  O  OE1   . GLN A 1 2464 ? 228.758 242.892 240.341 1.00 10.67 ? 2464 GLN A OE1   1 
ATOM   7906  N  NE2   . GLN A 1 2464 ? 230.834 243.080 241.173 1.00 10.54 ? 2464 GLN A NE2   1 
ATOM   7907  N  N     . ALA A 1 2465 ? 229.444 247.187 243.734 1.00 7.24  ? 2465 ALA A N     1 
ATOM   7908  C  CA    . ALA A 1 2465 ? 230.513 247.681 244.593 1.00 4.49  ? 2465 ALA A CA    1 
ATOM   7909  C  C     . ALA A 1 2465 ? 230.513 246.962 245.935 1.00 8.49  ? 2465 ALA A C     1 
ATOM   7910  O  O     . ALA A 1 2465 ? 231.577 246.666 246.489 1.00 9.55  ? 2465 ALA A O     1 
ATOM   7911  C  CB    . ALA A 1 2465 ? 230.373 249.187 244.795 1.00 5.20  ? 2465 ALA A CB    1 
ATOM   7912  N  N     . CYS A 1 2466 ? 229.326 246.684 246.478 1.00 11.55 ? 2466 CYS A N     1 
ATOM   7913  C  CA    . CYS A 1 2466 ? 229.243 245.899 247.705 1.00 6.77  ? 2466 CYS A CA    1 
ATOM   7914  C  C     . CYS A 1 2466 ? 229.779 244.491 247.487 1.00 7.80  ? 2466 CYS A C     1 
ATOM   7915  O  O     . CYS A 1 2466 ? 230.460 243.937 248.357 1.00 11.12 ? 2466 CYS A O     1 
ATOM   7916  C  CB    . CYS A 1 2466 ? 227.800 245.862 248.205 1.00 7.56  ? 2466 CYS A CB    1 
ATOM   7917  S  SG    . CYS A 1 2466 ? 227.159 247.464 248.736 1.00 21.05 ? 2466 CYS A SG    1 
ATOM   7918  N  N     . ARG A 1 2467 ? 229.482 243.898 246.329 1.00 10.39 ? 2467 ARG A N     1 
ATOM   7919  C  CA    . ARG A 1 2467 ? 230.039 242.591 245.999 1.00 7.11  ? 2467 ARG A CA    1 
ATOM   7920  C  C     . ARG A 1 2467 ? 231.551 242.648 245.829 1.00 6.30  ? 2467 ARG A C     1 
ATOM   7921  O  O     . ARG A 1 2467 ? 232.242 241.668 246.128 1.00 10.69 ? 2467 ARG A O     1 
ATOM   7922  C  CB    . ARG A 1 2467 ? 229.382 242.046 244.732 1.00 6.49  ? 2467 ARG A CB    1 
ATOM   7923  C  CG    . ARG A 1 2467 ? 227.926 241.675 244.902 1.00 10.23 ? 2467 ARG A CG    1 
ATOM   7924  C  CD    . ARG A 1 2467 ? 227.294 241.314 243.573 1.00 11.85 ? 2467 ARG A CD    1 
ATOM   7925  N  NE    . ARG A 1 2467 ? 225.842 241.419 243.615 1.00 14.34 ? 2467 ARG A NE    1 
ATOM   7926  C  CZ    . ARG A 1 2467 ? 225.035 240.477 244.084 1.00 16.54 ? 2467 ARG A CZ    1 
ATOM   7927  N  NH1   . ARG A 1 2467 ? 225.504 239.330 244.547 1.00 9.11  ? 2467 ARG A NH1   1 
ATOM   7928  N  NH2   . ARG A 1 2467 ? 223.722 240.690 244.086 1.00 13.91 ? 2467 ARG A NH2   1 
ATOM   7929  N  N     . ASN A 1 2468 ? 232.082 243.775 245.350 1.00 6.67  ? 2468 ASN A N     1 
ATOM   7930  C  CA    . ASN A 1 2468 ? 233.529 243.913 245.209 1.00 7.90  ? 2468 ASN A CA    1 
ATOM   7931  C  C     . ASN A 1 2468 ? 234.224 243.832 246.562 1.00 8.59  ? 2468 ASN A C     1 
ATOM   7932  O  O     . ASN A 1 2468 ? 235.265 243.178 246.696 1.00 15.52 ? 2468 ASN A O     1 
ATOM   7933  C  CB    . ASN A 1 2468 ? 233.872 245.233 244.520 1.00 5.57  ? 2468 ASN A CB    1 
ATOM   7934  C  CG    . ASN A 1 2468 ? 233.489 245.245 243.057 1.00 7.08  ? 2468 ASN A CG    1 
ATOM   7935  O  OD1   . ASN A 1 2468 ? 233.129 244.216 242.487 1.00 10.01 ? 2468 ASN A OD1   1 
ATOM   7936  N  ND2   . ASN A 1 2468 ? 233.554 246.420 242.440 1.00 6.11  ? 2468 ASN A ND2   1 
ATOM   7937  N  N     . VAL A 1 2469 ? 233.662 244.491 247.576 1.00 9.98  ? 2469 VAL A N     1 
ATOM   7938  C  CA    . VAL A 1 2469 ? 234.266 244.479 248.906 1.00 9.07  ? 2469 VAL A CA    1 
ATOM   7939  C  C     . VAL A 1 2469 ? 234.235 243.074 249.492 1.00 10.12 ? 2469 VAL A C     1 
ATOM   7940  O  O     . VAL A 1 2469 ? 235.205 242.624 250.114 1.00 13.65 ? 2469 VAL A O     1 
ATOM   7941  C  CB    . VAL A 1 2469 ? 233.559 245.498 249.818 1.00 8.53  ? 2469 VAL A CB    1 
ATOM   7942  C  CG1   . VAL A 1 2469 ? 234.145 245.461 251.218 1.00 11.02 ? 2469 VAL A CG1   1 
ATOM   7943  C  CG2   . VAL A 1 2469 ? 233.666 246.892 249.224 1.00 8.42  ? 2469 VAL A CG2   1 
ATOM   7944  N  N     . ALA A 1 2470 ? 233.122 242.360 249.308 1.00 9.18  ? 2470 ALA A N     1 
ATOM   7945  C  CA    . ALA A 1 2470 ? 233.050 240.977 249.765 1.00 11.05 ? 2470 ALA A CA    1 
ATOM   7946  C  C     . ALA A 1 2470 ? 234.059 240.100 249.038 1.00 15.49 ? 2470 ALA A C     1 
ATOM   7947  O  O     . ALA A 1 2470 ? 234.715 239.251 249.653 1.00 20.63 ? 2470 ALA A O     1 
ATOM   7948  C  CB    . ALA A 1 2470 ? 231.635 240.435 249.576 1.00 10.57 ? 2470 ALA A CB    1 
ATOM   7949  N  N     . GLN A 1 2471 ? 234.195 240.292 247.725 1.00 15.49 ? 2471 GLN A N     1 
ATOM   7950  C  CA    . GLN A 1 2471 ? 235.157 239.510 246.958 1.00 17.55 ? 2471 GLN A CA    1 
ATOM   7951  C  C     . GLN A 1 2471 ? 236.582 239.825 247.395 1.00 18.80 ? 2471 GLN A C     1 
ATOM   7952  O  O     . GLN A 1 2471 ? 237.453 238.948 247.389 1.00 21.32 ? 2471 GLN A O     1 
ATOM   7953  C  CB    . GLN A 1 2471 ? 234.962 239.775 245.464 1.00 17.51 ? 2471 GLN A CB    1 
ATOM   7954  C  CG    . GLN A 1 2471 ? 235.762 238.882 244.526 1.00 13.21 ? 2471 GLN A CG    1 
ATOM   7955  C  CD    . GLN A 1 2471 ? 237.162 239.392 244.262 1.00 22.92 ? 2471 GLN A CD    1 
ATOM   7956  O  OE1   . GLN A 1 2471 ? 238.083 238.615 244.009 1.00 32.94 ? 2471 GLN A OE1   1 
ATOM   7957  N  NE2   . GLN A 1 2471 ? 237.337 240.704 244.348 1.00 22.74 ? 2471 GLN A NE2   1 
ATOM   7958  N  N     . TYR A 1 2472 ? 236.836 241.078 247.783 1.00 15.31 ? 2472 TYR A N     1 
ATOM   7959  C  CA    . TYR A 1 2472 ? 238.135 241.427 248.347 1.00 14.68 ? 2472 TYR A CA    1 
ATOM   7960  C  C     . TYR A 1 2472 ? 238.378 240.695 249.661 1.00 17.22 ? 2472 TYR A C     1 
ATOM   7961  O  O     . TYR A 1 2472 ? 239.492 240.226 249.923 1.00 21.21 ? 2472 TYR A O     1 
ATOM   7962  C  CB    . TYR A 1 2472 ? 238.233 242.945 248.526 1.00 11.44 ? 2472 TYR A CB    1 
ATOM   7963  C  CG    . TYR A 1 2472 ? 239.437 243.439 249.305 1.00 14.90 ? 2472 TYR A CG    1 
ATOM   7964  C  CD1   . TYR A 1 2472 ? 240.508 244.035 248.655 1.00 13.39 ? 2472 TYR A CD1   1 
ATOM   7965  C  CD2   . TYR A 1 2472 ? 239.474 243.372 250.694 1.00 15.76 ? 2472 TYR A CD2   1 
ATOM   7966  C  CE1   . TYR A 1 2472 ? 241.600 244.502 249.357 1.00 18.02 ? 2472 TYR A CE1   1 
ATOM   7967  C  CE2   . TYR A 1 2472 ? 240.561 243.836 251.402 1.00 21.18 ? 2472 TYR A CE2   1 
ATOM   7968  C  CZ    . TYR A 1 2472 ? 241.621 244.401 250.730 1.00 21.79 ? 2472 TYR A CZ    1 
ATOM   7969  O  OH    . TYR A 1 2472 ? 242.703 244.868 251.437 1.00 25.86 ? 2472 TYR A OH    1 
ATOM   7970  N  N     . ASN A 1 2473 ? 237.350 240.594 250.507 1.00 22.58 ? 2473 ASN A N     1 
ATOM   7971  C  CA    . ASN A 1 2473 ? 237.507 239.892 251.777 1.00 20.66 ? 2473 ASN A CA    1 
ATOM   7972  C  C     . ASN A 1 2473 ? 237.794 238.412 251.558 1.00 19.95 ? 2473 ASN A C     1 
ATOM   7973  O  O     . ASN A 1 2473 ? 238.505 237.787 252.352 1.00 21.84 ? 2473 ASN A O     1 
ATOM   7974  C  CB    . ASN A 1 2473 ? 236.263 240.082 252.645 1.00 14.72 ? 2473 ASN A CB    1 
ATOM   7975  C  CG    . ASN A 1 2473 ? 236.135 241.495 253.180 1.00 20.22 ? 2473 ASN A CG    1 
ATOM   7976  O  OD1   . ASN A 1 2473 ? 236.960 242.358 252.884 1.00 19.98 ? 2473 ASN A OD1   1 
ATOM   7977  N  ND2   . ASN A 1 2473 ? 235.099 241.738 253.972 1.00 19.23 ? 2473 ASN A ND2   1 
ATOM   7978  N  N     . ALA A 1 2474 ? 237.243 237.833 250.490 1.00 18.71 ? 2474 ALA A N     1 
ATOM   7979  C  CA    . ALA A 1 2474 ? 237.590 236.462 250.135 1.00 19.43 ? 2474 ALA A CA    1 
ATOM   7980  C  C     . ALA A 1 2474 ? 239.060 236.351 249.752 1.00 25.87 ? 2474 ALA A C     1 
ATOM   7981  O  O     . ALA A 1 2474 ? 239.743 235.396 250.144 1.00 26.75 ? 2474 ALA A O     1 
ATOM   7982  C  CB    . ALA A 1 2474 ? 236.697 235.973 248.995 1.00 14.78 ? 2474 ALA A CB    1 
ATOM   7983  N  N     . ASN A 1 2475 ? 239.570 237.321 248.986 1.00 22.11 ? 2475 ASN A N     1 
ATOM   7984  C  CA    . ASN A 1 2475 ? 240.983 237.337 248.631 1.00 21.64 ? 2475 ASN A CA    1 
ATOM   7985  C  C     . ASN A 1 2475 ? 241.878 237.615 249.828 1.00 22.45 ? 2475 ASN A C     1 
ATOM   7986  O  O     . ASN A 1 2475 ? 243.052 237.230 249.811 1.00 30.36 ? 2475 ASN A O     1 
ATOM   7987  C  CB    . ASN A 1 2475 ? 241.251 238.386 247.553 1.00 23.68 ? 2475 ASN A CB    1 
ATOM   7988  C  CG    . ASN A 1 2475 ? 240.415 238.178 246.312 1.00 27.00 ? 2475 ASN A CG    1 
ATOM   7989  O  OD1   . ASN A 1 2475 ? 239.731 237.165 246.169 1.00 20.26 ? 2475 ASN A OD1   1 
ATOM   7990  N  ND2   . ASN A 1 2475 ? 240.468 239.142 245.401 1.00 24.66 ? 2475 ASN A ND2   1 
ATOM   7991  N  N     . HIS A 1 2476 ? 241.356 238.271 250.859 1.00 17.01 ? 2476 HIS A N     1 
ATOM   7992  C  CA    . HIS A 1 2476 ? 242.121 238.629 252.054 1.00 21.33 ? 2476 HIS A CA    1 
ATOM   7993  C  C     . HIS A 1 2476 ? 241.379 238.120 253.282 1.00 26.68 ? 2476 HIS A C     1 
ATOM   7994  O  O     . HIS A 1 2476 ? 240.792 238.905 254.037 1.00 32.55 ? 2476 HIS A O     1 
ATOM   7995  C  CB    . HIS A 1 2476 ? 242.334 240.140 252.144 1.00 18.81 ? 2476 HIS A CB    1 
ATOM   7996  C  CG    . HIS A 1 2476 ? 242.975 240.742 250.934 1.00 17.74 ? 2476 HIS A CG    1 
ATOM   7997  N  ND1   . HIS A 1 2476 ? 242.317 240.873 249.731 1.00 20.85 ? 2476 HIS A ND1   1 
ATOM   7998  C  CD2   . HIS A 1 2476 ? 244.206 241.277 250.750 1.00 17.40 ? 2476 HIS A CD2   1 
ATOM   7999  C  CE1   . HIS A 1 2476 ? 243.120 241.445 248.852 1.00 24.90 ? 2476 HIS A CE1   1 
ATOM   8000  N  NE2   . HIS A 1 2476 ? 244.270 241.703 249.446 1.00 22.17 ? 2476 HIS A NE2   1 
ATOM   8001  N  N     . PRO A 1 2477 ? 241.375 236.805 253.509 1.00 24.90 ? 2477 PRO A N     1 
ATOM   8002  C  CA    . PRO A 1 2477 ? 240.707 236.279 254.710 1.00 21.95 ? 2477 PRO A CA    1 
ATOM   8003  C  C     . PRO A 1 2477 ? 241.340 236.765 255.997 1.00 29.36 ? 2477 PRO A C     1 
ATOM   8004  O  O     . PRO A 1 2477 ? 240.677 236.758 257.042 1.00 33.41 ? 2477 PRO A O     1 
ATOM   8005  C  CB    . PRO A 1 2477 ? 240.844 234.757 254.557 1.00 27.59 ? 2477 PRO A CB    1 
ATOM   8006  C  CG    . PRO A 1 2477 ? 241.186 234.534 253.119 1.00 21.20 ? 2477 PRO A CG    1 
ATOM   8007  C  CD    . PRO A 1 2477 ? 241.977 235.730 252.705 1.00 24.74 ? 2477 PRO A CD    1 
ATOM   8008  N  N     . ASP A 1 2478 ? 242.602 237.192 255.954 1.00 29.26 ? 2478 ASP A N     1 
ATOM   8009  C  CA    . ASP A 1 2478 ? 243.282 237.670 257.150 1.00 33.18 ? 2478 ASP A CA    1 
ATOM   8010  C  C     . ASP A 1 2478 ? 242.807 239.065 257.541 1.00 31.17 ? 2478 ASP A C     1 
ATOM   8011  O  O     . ASP A 1 2478 ? 242.374 239.290 258.676 1.00 39.99 ? 2478 ASP A O     1 
ATOM   8012  C  CB    . ASP A 1 2478 ? 244.797 237.653 256.926 1.00 31.25 ? 2478 ASP A CB    1 
ATOM   8013  C  CG    . ASP A 1 2478 ? 245.555 238.418 257.990 1.00 41.67 ? 2478 ASP A CG    1 
ATOM   8014  O  OD1   . ASP A 1 2478 ? 245.326 238.156 259.190 1.00 42.43 ? 2478 ASP A OD1   1 
ATOM   8015  O  OD2   . ASP A 1 2478 ? 246.385 239.275 257.625 1.00 43.84 ? 2478 ASP A OD2   1 
ATOM   8016  N  N     . PHE A 1 2479 ? 242.870 240.014 256.609 1.00 33.32 ? 2479 PHE A N     1 
ATOM   8017  C  CA    . PHE A 1 2479 ? 242.535 241.409 256.891 1.00 37.16 ? 2479 PHE A CA    1 
ATOM   8018  C  C     . PHE A 1 2479 ? 241.374 241.864 256.021 1.00 32.83 ? 2479 PHE A C     1 
ATOM   8019  O  O     . PHE A 1 2479 ? 241.587 242.308 254.878 1.00 32.99 ? 2479 PHE A O     1 
ATOM   8020  C  CB    . PHE A 1 2479 ? 243.748 242.310 256.671 1.00 29.88 ? 2479 PHE A CB    1 
ATOM   8021  C  CG    . PHE A 1 2479 ? 244.845 242.107 257.674 1.00 33.93 ? 2479 PHE A CG    1 
ATOM   8022  C  CD1   . PHE A 1 2479 ? 244.566 241.601 258.933 1.00 37.05 ? 2479 PHE A CD1   1 
ATOM   8023  C  CD2   . PHE A 1 2479 ? 246.156 242.422 257.359 1.00 36.45 ? 2479 PHE A CD2   1 
ATOM   8024  C  CE1   . PHE A 1 2479 ? 245.574 241.415 259.861 1.00 38.72 ? 2479 PHE A CE1   1 
ATOM   8025  C  CE2   . PHE A 1 2479 ? 247.169 242.237 258.282 1.00 33.04 ? 2479 PHE A CE2   1 
ATOM   8026  C  CZ    . PHE A 1 2479 ? 246.878 241.733 259.534 1.00 35.92 ? 2479 PHE A CZ    1 
ATOM   8027  N  N     . PRO A 1 2480 ? 240.138 241.778 256.505 1.00 29.98 ? 2480 PRO A N     1 
ATOM   8028  C  CA    . PRO A 1 2480 ? 239.013 242.341 255.755 1.00 26.07 ? 2480 PRO A CA    1 
ATOM   8029  C  C     . PRO A 1 2480 ? 239.088 243.859 255.717 1.00 25.95 ? 2480 PRO A C     1 
ATOM   8030  O  O     . PRO A 1 2480 ? 239.685 244.505 256.585 1.00 27.47 ? 2480 PRO A O     1 
ATOM   8031  C  CB    . PRO A 1 2480 ? 237.785 241.861 256.533 1.00 26.18 ? 2480 PRO A CB    1 
ATOM   8032  C  CG    . PRO A 1 2480 ? 238.290 241.625 257.916 1.00 28.65 ? 2480 PRO A CG    1 
ATOM   8033  C  CD    . PRO A 1 2480 ? 239.705 241.142 257.760 1.00 31.58 ? 2480 PRO A CD    1 
ATOM   8034  N  N     . MET A 1 2481 ? 238.475 244.424 254.681 1.00 20.33 ? 2481 MET A N     1 
ATOM   8035  C  CA    . MET A 1 2481 ? 238.525 245.863 254.464 1.00 21.36 ? 2481 MET A CA    1 
ATOM   8036  C  C     . MET A 1 2481 ? 237.968 246.611 255.668 1.00 23.18 ? 2481 MET A C     1 
ATOM   8037  O  O     . MET A 1 2481 ? 236.907 246.265 256.196 1.00 26.18 ? 2481 MET A O     1 
ATOM   8038  C  CB    . MET A 1 2481 ? 237.738 246.229 253.207 1.00 19.00 ? 2481 MET A CB    1 
ATOM   8039  C  CG    . MET A 1 2481 ? 237.823 247.691 252.823 1.00 18.55 ? 2481 MET A CG    1 
ATOM   8040  S  SD    . MET A 1 2481 ? 236.886 248.061 251.330 1.00 37.20 ? 2481 MET A SD    1 
ATOM   8041  C  CE    . MET A 1 2481 ? 237.908 247.281 250.088 1.00 20.06 ? 2481 MET A CE    1 
ATOM   8042  N  N     . GLN A 1 2482 ? 238.694 247.633 256.106 1.00 22.42 ? 2482 GLN A N     1 
ATOM   8043  C  CA    . GLN A 1 2482 ? 238.273 248.459 257.224 1.00 17.77 ? 2482 GLN A CA    1 
ATOM   8044  C  C     . GLN A 1 2482 ? 237.380 249.595 256.740 1.00 18.42 ? 2482 GLN A C     1 
ATOM   8045  O  O     . GLN A 1 2482 ? 237.302 249.897 255.547 1.00 24.56 ? 2482 GLN A O     1 
ATOM   8046  C  CB    . GLN A 1 2482 ? 239.487 249.008 257.973 1.00 18.07 ? 2482 GLN A CB    1 
ATOM   8047  C  CG    . GLN A 1 2482 ? 240.320 247.934 258.641 1.00 20.19 ? 2482 GLN A CG    1 
ATOM   8048  C  CD    . GLN A 1 2482 ? 239.471 246.930 259.393 1.00 21.00 ? 2482 GLN A CD    1 
ATOM   8049  O  OE1   . GLN A 1 2482 ? 238.741 247.287 260.318 1.00 26.11 ? 2482 GLN A OE1   1 
ATOM   8050  N  NE2   . GLN A 1 2482 ? 239.556 245.669 258.995 1.00 23.40 ? 2482 GLN A NE2   1 
ATOM   8051  N  N     . ILE A 1 2483 ? 236.703 250.236 257.696 1.00 18.04 ? 2483 ILE A N     1 
ATOM   8052  C  CA    . ILE A 1 2483 ? 235.753 251.294 257.360 1.00 16.25 ? 2483 ILE A CA    1 
ATOM   8053  C  C     . ILE A 1 2483 ? 236.453 252.446 256.657 1.00 21.48 ? 2483 ILE A C     1 
ATOM   8054  O  O     . ILE A 1 2483 ? 235.889 253.058 255.741 1.00 27.85 ? 2483 ILE A O     1 
ATOM   8055  C  CB    . ILE A 1 2483 ? 235.012 251.773 258.623 1.00 22.77 ? 2483 ILE A CB    1 
ATOM   8056  C  CG1   . ILE A 1 2483 ? 234.532 250.579 259.448 1.00 24.19 ? 2483 ILE A CG1   1 
ATOM   8057  C  CG2   . ILE A 1 2483 ? 233.835 252.653 258.246 1.00 19.04 ? 2483 ILE A CG2   1 
ATOM   8058  C  CD1   . ILE A 1 2483 ? 233.610 249.644 258.695 1.00 19.02 ? 2483 ILE A CD1   1 
ATOM   8059  N  N     . GLU A 1 2484 ? 237.682 252.764 257.065 1.00 18.52 ? 2484 GLU A N     1 
ATOM   8060  C  CA    . GLU A 1 2484 ? 238.425 253.840 256.416 1.00 15.32 ? 2484 GLU A CA    1 
ATOM   8061  C  C     . GLU A 1 2484 ? 238.671 253.523 254.945 1.00 20.04 ? 2484 GLU A C     1 
ATOM   8062  O  O     . GLU A 1 2484 ? 238.517 254.390 254.077 1.00 16.08 ? 2484 GLU A O     1 
ATOM   8063  C  CB    . GLU A 1 2484 ? 239.739 254.082 257.168 1.00 15.63 ? 2484 GLU A CB    1 
ATOM   8064  C  CG    . GLU A 1 2484 ? 240.615 255.204 256.631 1.00 22.74 ? 2484 GLU A CG    1 
ATOM   8065  C  CD    . GLU A 1 2484 ? 241.482 254.775 255.465 1.00 26.39 ? 2484 GLU A CD    1 
ATOM   8066  O  OE1   . GLU A 1 2484 ? 241.908 255.651 254.685 1.00 22.47 ? 2484 GLU A OE1   1 
ATOM   8067  O  OE2   . GLU A 1 2484 ? 241.742 253.561 255.329 1.00 28.84 ? 2484 GLU A OE2   1 
ATOM   8068  N  N     . GLN A 1 2485 ? 239.051 252.280 254.642 1.00 20.84 ? 2485 GLN A N     1 
ATOM   8069  C  CA    . GLN A 1 2485 ? 239.173 251.878 253.244 1.00 16.76 ? 2485 GLN A CA    1 
ATOM   8070  C  C     . GLN A 1 2485 ? 237.801 251.698 252.608 1.00 18.08 ? 2485 GLN A C     1 
ATOM   8071  O  O     . GLN A 1 2485 ? 237.604 252.049 251.439 1.00 18.27 ? 2485 GLN A O     1 
ATOM   8072  C  CB    . GLN A 1 2485 ? 239.989 250.592 253.125 1.00 20.54 ? 2485 GLN A CB    1 
ATOM   8073  C  CG    . GLN A 1 2485 ? 240.238 250.160 251.685 1.00 16.94 ? 2485 GLN A CG    1 
ATOM   8074  C  CD    . GLN A 1 2485 ? 241.093 248.915 251.581 1.00 22.00 ? 2485 GLN A CD    1 
ATOM   8075  O  OE1   . GLN A 1 2485 ? 241.412 248.459 250.484 1.00 25.94 ? 2485 GLN A OE1   1 
ATOM   8076  N  NE2   . GLN A 1 2485 ? 241.467 248.354 252.724 1.00 26.78 ? 2485 GLN A NE2   1 
ATOM   8077  N  N     . LEU A 1 2486 ? 236.841 251.153 253.363 1.00 17.85 ? 2486 LEU A N     1 
ATOM   8078  C  CA    . LEU A 1 2486 ? 235.485 251.006 252.845 1.00 14.46 ? 2486 LEU A CA    1 
ATOM   8079  C  C     . LEU A 1 2486 ? 234.871 252.359 252.520 1.00 14.59 ? 2486 LEU A C     1 
ATOM   8080  O  O     . LEU A 1 2486 ? 234.253 252.529 251.464 1.00 15.50 ? 2486 LEU A O     1 
ATOM   8081  C  CB    . LEU A 1 2486 ? 234.613 250.256 253.848 1.00 16.03 ? 2486 LEU A CB    1 
ATOM   8082  C  CG    . LEU A 1 2486 ? 233.194 249.929 253.374 1.00 17.09 ? 2486 LEU A CG    1 
ATOM   8083  C  CD1   . LEU A 1 2486 ? 233.225 249.147 252.072 1.00 11.24 ? 2486 LEU A CD1   1 
ATOM   8084  C  CD2   . LEU A 1 2486 ? 232.434 249.165 254.441 1.00 14.52 ? 2486 LEU A CD2   1 
ATOM   8085  N  N     . GLU A 1 2487 ? 235.036 253.336 253.414 1.00 13.77 ? 2487 GLU A N     1 
ATOM   8086  C  CA    . GLU A 1 2487 ? 234.565 254.684 253.121 1.00 15.54 ? 2487 GLU A CA    1 
ATOM   8087  C  C     . GLU A 1 2487 ? 235.282 255.247 251.907 1.00 13.49 ? 2487 GLU A C     1 
ATOM   8088  O  O     . GLU A 1 2487 ? 234.666 255.885 251.047 1.00 13.28 ? 2487 GLU A O     1 
ATOM   8089  C  CB    . GLU A 1 2487 ? 234.772 255.594 254.332 1.00 12.90 ? 2487 GLU A CB    1 
ATOM   8090  C  CG    . GLU A 1 2487 ? 234.095 256.945 254.213 1.00 17.59 ? 2487 GLU A CG    1 
ATOM   8091  C  CD    . GLU A 1 2487 ? 233.912 257.625 255.554 1.00 30.85 ? 2487 GLU A CD    1 
ATOM   8092  O  OE1   . GLU A 1 2487 ? 234.920 257.809 256.267 1.00 28.88 ? 2487 GLU A OE1   1 
ATOM   8093  O  OE2   . GLU A 1 2487 ? 232.762 257.976 255.894 1.00 35.59 ? 2487 GLU A OE2   1 
ATOM   8094  N  N     . ARG A 1 2488 ? 236.587 255.004 251.813 1.00 17.89 ? 2488 ARG A N     1 
ATOM   8095  C  CA    . ARG A 1 2488 ? 237.381 255.606 250.751 1.00 14.92 ? 2488 ARG A CA    1 
ATOM   8096  C  C     . ARG A 1 2488 ? 236.990 255.034 249.390 1.00 13.24 ? 2488 ARG A C     1 
ATOM   8097  O  O     . ARG A 1 2488 ? 237.040 255.736 248.373 1.00 15.77 ? 2488 ARG A O     1 
ATOM   8098  C  CB    . ARG A 1 2488 ? 238.865 255.387 251.055 1.00 17.31 ? 2488 ARG A CB    1 
ATOM   8099  C  CG    . ARG A 1 2488 ? 239.795 256.120 250.136 1.00 21.49 ? 2488 ARG A CG    1 
ATOM   8100  C  CD    . ARG A 1 2488 ? 241.265 255.972 250.482 1.00 20.26 ? 2488 ARG A CD    1 
ATOM   8101  N  NE    . ARG A 1 2488 ? 241.747 254.608 250.319 1.00 19.52 ? 2488 ARG A NE    1 
ATOM   8102  C  CZ    . ARG A 1 2488 ? 242.147 253.830 251.314 1.00 21.34 ? 2488 ARG A CZ    1 
ATOM   8103  N  NH1   . ARG A 1 2488 ? 242.105 254.240 252.569 1.00 20.48 ? 2488 ARG A NH1   1 
ATOM   8104  N  NH2   . ARG A 1 2488 ? 242.608 252.614 251.041 1.00 27.66 ? 2488 ARG A NH2   1 
ATOM   8105  N  N     . TYR A 1 2489 ? 236.587 253.760 249.359 1.00 13.33 ? 2489 TYR A N     1 
ATOM   8106  C  CA    . TYR A 1 2489 ? 236.174 253.118 248.113 1.00 6.35  ? 2489 TYR A CA    1 
ATOM   8107  C  C     . TYR A 1 2489 ? 234.781 253.559 247.670 1.00 9.42  ? 2489 TYR A C     1 
ATOM   8108  O  O     . TYR A 1 2489 ? 234.560 253.820 246.482 1.00 11.22 ? 2489 TYR A O     1 
ATOM   8109  C  CB    . TYR A 1 2489 ? 236.218 251.599 248.281 1.00 7.30  ? 2489 TYR A CB    1 
ATOM   8110  C  CG    . TYR A 1 2489 ? 235.841 250.819 247.042 1.00 6.23  ? 2489 TYR A CG    1 
ATOM   8111  C  CD1   . TYR A 1 2489 ? 236.506 251.013 245.840 1.00 7.17  ? 2489 TYR A CD1   1 
ATOM   8112  C  CD2   . TYR A 1 2489 ? 234.807 249.892 247.075 1.00 6.94  ? 2489 TYR A CD2   1 
ATOM   8113  C  CE1   . TYR A 1 2489 ? 236.155 250.300 244.709 1.00 7.75  ? 2489 TYR A CE1   1 
ATOM   8114  C  CE2   . TYR A 1 2489 ? 234.450 249.175 245.948 1.00 5.34  ? 2489 TYR A CE2   1 
ATOM   8115  C  CZ    . TYR A 1 2489 ? 235.127 249.384 244.770 1.00 6.94  ? 2489 TYR A CZ    1 
ATOM   8116  O  OH    . TYR A 1 2489 ? 234.773 248.673 243.647 1.00 9.79  ? 2489 TYR A OH    1 
ATOM   8117  N  N     . ILE A 1 2490 ? 233.830 253.635 248.603 1.00 11.02 ? 2490 ILE A N     1 
ATOM   8118  C  CA    . ILE A 1 2490 ? 232.427 253.819 248.231 1.00 5.85  ? 2490 ILE A CA    1 
ATOM   8119  C  C     . ILE A 1 2490 ? 232.201 255.198 247.621 1.00 4.93  ? 2490 ILE A C     1 
ATOM   8120  O  O     . ILE A 1 2490 ? 231.477 255.341 246.629 1.00 6.66  ? 2490 ILE A O     1 
ATOM   8121  C  CB    . ILE A 1 2490 ? 231.511 253.577 249.445 1.00 6.75  ? 2490 ILE A CB    1 
ATOM   8122  C  CG1   . ILE A 1 2490 ? 231.569 252.113 249.883 1.00 5.74  ? 2490 ILE A CG1   1 
ATOM   8123  C  CG2   . ILE A 1 2490 ? 230.077 253.956 249.122 1.00 8.93  ? 2490 ILE A CG2   1 
ATOM   8124  C  CD1   . ILE A 1 2490 ? 231.169 251.131 248.806 1.00 5.42  ? 2490 ILE A CD1   1 
ATOM   8125  N  N     . GLN A 1 2491 ? 232.811 256.234 248.204 1.00 4.26  ? 2491 GLN A N     1 
ATOM   8126  C  CA    . GLN A 1 2491 ? 232.578 257.593 247.722 1.00 5.10  ? 2491 GLN A CA    1 
ATOM   8127  C  C     . GLN A 1 2491 ? 233.047 257.764 246.284 1.00 9.26  ? 2491 GLN A C     1 
ATOM   8128  O  O     . GLN A 1 2491 ? 232.349 258.370 245.463 1.00 8.21  ? 2491 GLN A O     1 
ATOM   8129  C  CB    . GLN A 1 2491 ? 233.275 258.604 248.633 1.00 7.80  ? 2491 GLN A CB    1 
ATOM   8130  C  CG    . GLN A 1 2491 ? 233.137 258.306 250.106 1.00 11.21 ? 2491 GLN A CG    1 
ATOM   8131  C  CD    . GLN A 1 2491 ? 233.143 259.550 250.963 1.00 19.13 ? 2491 GLN A CD    1 
ATOM   8132  O  OE1   . GLN A 1 2491 ? 233.897 260.488 250.713 1.00 17.25 ? 2491 GLN A OE1   1 
ATOM   8133  N  NE2   . GLN A 1 2491 ? 232.295 259.564 251.984 1.00 25.67 ? 2491 GLN A NE2   1 
ATOM   8134  N  N     . ARG A 1 2492 ? 234.228 257.236 245.959 1.00 10.64 ? 2492 ARG A N     1 
ATOM   8135  C  CA    . ARG A 1 2492 ? 234.718 257.320 244.587 1.00 5.02  ? 2492 ARG A CA    1 
ATOM   8136  C  C     . ARG A 1 2492 ? 233.925 256.426 243.647 1.00 3.58  ? 2492 ARG A C     1 
ATOM   8137  O  O     . ARG A 1 2492 ? 233.648 256.816 242.506 1.00 4.53  ? 2492 ARG A O     1 
ATOM   8138  C  CB    . ARG A 1 2492 ? 236.203 256.982 244.544 1.00 6.18  ? 2492 ARG A CB    1 
ATOM   8139  C  CG    . ARG A 1 2492 ? 237.046 258.026 245.212 1.00 9.47  ? 2492 ARG A CG    1 
ATOM   8140  C  CD    . ARG A 1 2492 ? 238.510 257.676 245.172 1.00 12.80 ? 2492 ARG A CD    1 
ATOM   8141  N  NE    . ARG A 1 2492 ? 239.306 258.725 245.791 1.00 15.28 ? 2492 ARG A NE    1 
ATOM   8142  C  CZ    . ARG A 1 2492 ? 239.619 258.755 247.076 1.00 13.14 ? 2492 ARG A CZ    1 
ATOM   8143  N  NH1   . ARG A 1 2492 ? 239.105 257.890 247.924 1.00 9.97  ? 2492 ARG A NH1   1 
ATOM   8144  N  NH2   . ARG A 1 2492 ? 240.442 259.698 247.526 1.00 14.24 ? 2492 ARG A NH2   1 
ATOM   8145  N  N     . TYR A 1 2493 ? 233.543 255.231 244.098 1.00 2.29  ? 2493 TYR A N     1 
ATOM   8146  C  CA    . TYR A 1 2493 ? 232.732 254.375 243.241 1.00 2.49  ? 2493 TYR A CA    1 
ATOM   8147  C  C     . TYR A 1 2493 ? 231.370 255.002 242.977 1.00 5.22  ? 2493 TYR A C     1 
ATOM   8148  O  O     . TYR A 1 2493 ? 230.828 254.877 241.873 1.00 6.56  ? 2493 TYR A O     1 
ATOM   8149  C  CB    . TYR A 1 2493 ? 232.575 252.988 243.858 1.00 3.67  ? 2493 TYR A CB    1 
ATOM   8150  C  CG    . TYR A 1 2493 ? 232.036 251.966 242.881 1.00 5.18  ? 2493 TYR A CG    1 
ATOM   8151  C  CD1   . TYR A 1 2493 ? 230.675 251.880 242.615 1.00 5.04  ? 2493 TYR A CD1   1 
ATOM   8152  C  CD2   . TYR A 1 2493 ? 232.888 251.095 242.219 1.00 3.44  ? 2493 TYR A CD2   1 
ATOM   8153  C  CE1   . TYR A 1 2493 ? 230.181 250.956 241.723 1.00 4.41  ? 2493 TYR A CE1   1 
ATOM   8154  C  CE2   . TYR A 1 2493 ? 232.400 250.166 241.327 1.00 4.05  ? 2493 TYR A CE2   1 
ATOM   8155  C  CZ    . TYR A 1 2493 ? 231.046 250.101 241.082 1.00 6.44  ? 2493 TYR A CZ    1 
ATOM   8156  O  OH    . TYR A 1 2493 ? 230.553 249.176 240.192 1.00 11.33 ? 2493 TYR A OH    1 
ATOM   8157  N  N     . LEU A 1 2494 ? 230.806 255.679 243.978 1.00 6.87  ? 2494 LEU A N     1 
ATOM   8158  C  CA    . LEU A 1 2494 ? 229.534 256.363 243.779 1.00 3.54  ? 2494 LEU A CA    1 
ATOM   8159  C  C     . LEU A 1 2494 ? 229.644 257.427 242.697 1.00 2.93  ? 2494 LEU A C     1 
ATOM   8160  O  O     . LEU A 1 2494 ? 228.772 257.532 241.828 1.00 3.33  ? 2494 LEU A O     1 
ATOM   8161  C  CB    . LEU A 1 2494 ? 229.063 256.979 245.095 1.00 5.19  ? 2494 LEU A CB    1 
ATOM   8162  C  CG    . LEU A 1 2494 ? 227.851 257.906 245.029 1.00 2.62  ? 2494 LEU A CG    1 
ATOM   8163  C  CD1   . LEU A 1 2494 ? 226.603 257.147 244.607 1.00 2.08  ? 2494 LEU A CD1   1 
ATOM   8164  C  CD2   . LEU A 1 2494 ? 227.645 258.563 246.372 1.00 7.39  ? 2494 LEU A CD2   1 
ATOM   8165  N  N     . VAL A 1 2495 ? 230.718 258.220 242.727 1.00 4.90  ? 2495 VAL A N     1 
ATOM   8166  C  CA    . VAL A 1 2495 ? 230.954 259.197 241.666 1.00 3.59  ? 2495 VAL A CA    1 
ATOM   8167  C  C     . VAL A 1 2495 ? 231.142 258.489 240.331 1.00 3.36  ? 2495 VAL A C     1 
ATOM   8168  O  O     . VAL A 1 2495 ? 230.592 258.907 239.305 1.00 2.96  ? 2495 VAL A O     1 
ATOM   8169  C  CB    . VAL A 1 2495 ? 232.168 260.076 242.017 1.00 3.00  ? 2495 VAL A CB    1 
ATOM   8170  C  CG1   . VAL A 1 2495 ? 232.551 260.955 240.834 1.00 3.72  ? 2495 VAL A CG1   1 
ATOM   8171  C  CG2   . VAL A 1 2495 ? 231.875 260.918 243.243 1.00 3.96  ? 2495 VAL A CG2   1 
ATOM   8172  N  N     . TYR A 1 2496 ? 231.914 257.401 240.329 1.00 4.15  ? 2496 TYR A N     1 
ATOM   8173  C  CA    . TYR A 1 2496 ? 232.100 256.612 239.118 1.00 2.37  ? 2496 TYR A CA    1 
ATOM   8174  C  C     . TYR A 1 2496 ? 230.774 256.056 238.613 1.00 3.70  ? 2496 TYR A C     1 
ATOM   8175  O  O     . TYR A 1 2496 ? 230.490 256.104 237.412 1.00 3.44  ? 2496 TYR A O     1 
ATOM   8176  C  CB    . TYR A 1 2496 ? 233.098 255.487 239.399 1.00 2.70  ? 2496 TYR A CB    1 
ATOM   8177  C  CG    . TYR A 1 2496 ? 233.118 254.364 238.390 1.00 2.69  ? 2496 TYR A CG    1 
ATOM   8178  C  CD1   . TYR A 1 2496 ? 233.880 254.457 237.233 1.00 1.93  ? 2496 TYR A CD1   1 
ATOM   8179  C  CD2   . TYR A 1 2496 ? 232.398 253.198 238.606 1.00 3.12  ? 2496 TYR A CD2   1 
ATOM   8180  C  CE1   . TYR A 1 2496 ? 233.908 253.430 236.315 1.00 3.83  ? 2496 TYR A CE1   1 
ATOM   8181  C  CE2   . TYR A 1 2496 ? 232.419 252.168 237.694 1.00 2.60  ? 2496 TYR A CE2   1 
ATOM   8182  C  CZ    . TYR A 1 2496 ? 233.174 252.286 236.551 1.00 3.19  ? 2496 TYR A CZ    1 
ATOM   8183  O  OH    . TYR A 1 2496 ? 233.196 251.257 235.642 1.00 6.92  ? 2496 TYR A OH    1 
ATOM   8184  N  N     . ALA A 1 2497 ? 229.941 255.542 239.520 1.00 2.61  ? 2497 ALA A N     1 
ATOM   8185  C  CA    . ALA A 1 2497 ? 228.660 254.976 239.115 1.00 1.52  ? 2497 ALA A CA    1 
ATOM   8186  C  C     . ALA A 1 2497 ? 227.704 256.053 238.615 1.00 1.28  ? 2497 ALA A C     1 
ATOM   8187  O  O     . ALA A 1 2497 ? 226.919 255.809 237.693 1.00 1.15  ? 2497 ALA A O     1 
ATOM   8188  C  CB    . ALA A 1 2497 ? 228.039 254.199 240.275 1.00 3.45  ? 2497 ALA A CB    1 
ATOM   8189  N  N     . ILE A 1 2498 ? 227.759 257.246 239.211 1.00 2.00  ? 2498 ILE A N     1 
ATOM   8190  C  CA    . ILE A 1 2498 ? 226.879 258.337 238.791 1.00 1.56  ? 2498 ILE A CA    1 
ATOM   8191  C  C     . ILE A 1 2498 ? 227.175 258.742 237.353 1.00 1.34  ? 2498 ILE A C     1 
ATOM   8192  O  O     . ILE A 1 2498 ? 226.256 258.969 236.556 1.00 1.14  ? 2498 ILE A O     1 
ATOM   8193  C  CB    . ILE A 1 2498 ? 227.013 259.529 239.760 1.00 2.01  ? 2498 ILE A CB    1 
ATOM   8194  C  CG1   . ILE A 1 2498 ? 226.254 259.251 241.057 1.00 1.64  ? 2498 ILE A CG1   1 
ATOM   8195  C  CG2   . ILE A 1 2498 ? 226.524 260.816 239.114 1.00 1.48  ? 2498 ILE A CG2   1 
ATOM   8196  C  CD1   . ILE A 1 2498 ? 226.481 260.292 242.127 1.00 2.32  ? 2498 ILE A CD1   1 
ATOM   8197  N  N     . LEU A 1 2499 ? 228.457 258.842 236.999 1.00 1.78  ? 2499 LEU A N     1 
ATOM   8198  C  CA    . LEU A 1 2499 ? 228.826 259.270 235.651 1.00 1.81  ? 2499 LEU A CA    1 
ATOM   8199  C  C     . LEU A 1 2499 ? 228.328 258.291 234.595 1.00 1.41  ? 2499 LEU A C     1 
ATOM   8200  O  O     . LEU A 1 2499 ? 227.783 258.704 233.566 1.00 1.54  ? 2499 LEU A O     1 
ATOM   8201  C  CB    . LEU A 1 2499 ? 230.340 259.430 235.553 1.00 2.23  ? 2499 LEU A CB    1 
ATOM   8202  C  CG    . LEU A 1 2499 ? 230.932 260.723 236.103 1.00 3.16  ? 2499 LEU A CG    1 
ATOM   8203  C  CD1   . LEU A 1 2499 ? 232.433 260.593 236.186 1.00 3.50  ? 2499 LEU A CD1   1 
ATOM   8204  C  CD2   . LEU A 1 2499 ? 230.546 261.898 235.226 1.00 4.65  ? 2499 LEU A CD2   1 
ATOM   8205  N  N     . TRP A 1 2500 ? 228.502 256.991 234.833 1.00 0.88  ? 2500 TRP A N     1 
ATOM   8206  C  CA    . TRP A 1 2500 ? 228.104 256.003 233.840 1.00 0.78  ? 2500 TRP A CA    1 
ATOM   8207  C  C     . TRP A 1 2500 ? 226.601 255.773 233.814 1.00 0.91  ? 2500 TRP A C     1 
ATOM   8208  O  O     . TRP A 1 2500 ? 226.046 255.461 232.756 1.00 1.23  ? 2500 TRP A O     1 
ATOM   8209  C  CB    . TRP A 1 2500 ? 228.845 254.690 234.083 1.00 1.06  ? 2500 TRP A CB    1 
ATOM   8210  C  CG    . TRP A 1 2500 ? 230.265 254.759 233.640 1.00 0.75  ? 2500 TRP A CG    1 
ATOM   8211  C  CD1   . TRP A 1 2500 ? 231.369 254.847 234.433 1.00 0.70  ? 2500 TRP A CD1   1 
ATOM   8212  C  CD2   . TRP A 1 2500 ? 230.736 254.776 232.291 1.00 0.73  ? 2500 TRP A CD2   1 
ATOM   8213  N  NE1   . TRP A 1 2500 ? 232.501 254.904 233.661 1.00 1.68  ? 2500 TRP A NE1   1 
ATOM   8214  C  CE2   . TRP A 1 2500 ? 232.139 254.863 232.342 1.00 2.45  ? 2500 TRP A CE2   1 
ATOM   8215  C  CE3   . TRP A 1 2500 ? 230.108 254.723 231.044 1.00 0.86  ? 2500 TRP A CE3   1 
ATOM   8216  C  CZ2   . TRP A 1 2500 ? 232.926 254.896 231.193 1.00 2.12  ? 2500 TRP A CZ2   1 
ATOM   8217  C  CZ3   . TRP A 1 2500 ? 230.889 254.757 229.906 1.00 1.23  ? 2500 TRP A CZ3   1 
ATOM   8218  C  CH2   . TRP A 1 2500 ? 232.281 254.842 229.989 1.00 1.70  ? 2500 TRP A CH2   1 
ATOM   8219  N  N     . SER A 1 2501 ? 225.927 255.919 234.952 1.00 1.48  ? 2501 SER A N     1 
ATOM   8220  C  CA    . SER A 1 2501 ? 224.483 255.738 234.992 1.00 0.63  ? 2501 SER A CA    1 
ATOM   8221  C  C     . SER A 1 2501 ? 223.728 256.909 234.384 1.00 1.13  ? 2501 SER A C     1 
ATOM   8222  O  O     . SER A 1 2501 ? 222.598 256.728 233.922 1.00 3.99  ? 2501 SER A O     1 
ATOM   8223  C  CB    . SER A 1 2501 ? 224.024 255.519 236.432 1.00 0.72  ? 2501 SER A CB    1 
ATOM   8224  O  OG    . SER A 1 2501 ? 224.693 254.412 237.007 1.00 0.61  ? 2501 SER A OG    1 
ATOM   8225  N  N     . LEU A 1 2502 ? 224.323 258.102 234.373 1.00 0.75  ? 2502 LEU A N     1 
ATOM   8226  C  CA    . LEU A 1 2502 ? 223.647 259.301 233.905 1.00 1.19  ? 2502 LEU A CA    1 
ATOM   8227  C  C     . LEU A 1 2502 ? 224.166 259.816 232.572 1.00 2.66  ? 2502 LEU A C     1 
ATOM   8228  O  O     . LEU A 1 2502 ? 223.478 260.617 231.932 1.00 6.38  ? 2502 LEU A O     1 
ATOM   8229  C  CB    . LEU A 1 2502 ? 223.767 260.422 234.947 1.00 2.10  ? 2502 LEU A CB    1 
ATOM   8230  C  CG    . LEU A 1 2502 ? 222.762 260.484 236.102 1.00 2.79  ? 2502 LEU A CG    1 
ATOM   8231  C  CD1   . LEU A 1 2502 ? 222.705 259.184 236.893 1.00 1.36  ? 2502 LEU A CD1   1 
ATOM   8232  C  CD2   . LEU A 1 2502 ? 223.109 261.640 237.019 1.00 0.77  ? 2502 LEU A CD2   1 
ATOM   8233  N  N     . SER A 1 2503 ? 225.348 259.383 232.141 1.00 3.89  ? 2503 SER A N     1 
ATOM   8234  C  CA    . SER A 1 2503 ? 225.928 259.845 230.892 1.00 2.21  ? 2503 SER A CA    1 
ATOM   8235  C  C     . SER A 1 2503 ? 226.479 258.719 230.029 1.00 1.80  ? 2503 SER A C     1 
ATOM   8236  O  O     . SER A 1 2503 ? 226.985 258.994 228.936 1.00 4.32  ? 2503 SER A O     1 
ATOM   8237  C  CB    . SER A 1 2503 ? 227.042 260.867 231.164 1.00 2.68  ? 2503 SER A CB    1 
ATOM   8238  O  OG    . SER A 1 2503 ? 228.161 260.253 231.777 1.00 3.60  ? 2503 SER A OG    1 
ATOM   8239  N  N     . GLY A 1 2504 ? 226.392 257.466 230.479 1.00 1.49  ? 2504 GLY A N     1 
ATOM   8240  C  CA    . GLY A 1 2504 ? 226.858 256.348 229.676 1.00 2.13  ? 2504 GLY A CA    1 
ATOM   8241  C  C     . GLY A 1 2504 ? 226.120 256.187 228.365 1.00 0.68  ? 2504 GLY A C     1 
ATOM   8242  O  O     . GLY A 1 2504 ? 226.623 255.516 227.458 1.00 2.90  ? 2504 GLY A O     1 
ATOM   8243  N  N     . ASP A 1 2505 ? 224.940 256.784 228.241 1.00 0.56  ? 2505 ASP A N     1 
ATOM   8244  C  CA    . ASP A 1 2505 ? 224.171 256.772 227.006 1.00 0.97  ? 2505 ASP A CA    1 
ATOM   8245  C  C     . ASP A 1 2505 ? 224.347 258.053 226.201 1.00 2.21  ? 2505 ASP A C     1 
ATOM   8246  O  O     . ASP A 1 2505 ? 223.565 258.312 225.281 1.00 2.46  ? 2505 ASP A O     1 
ATOM   8247  C  CB    . ASP A 1 2505 ? 222.693 256.528 227.317 1.00 1.19  ? 2505 ASP A CB    1 
ATOM   8248  C  CG    . ASP A 1 2505 ? 222.004 257.750 227.881 1.00 6.00  ? 2505 ASP A CG    1 
ATOM   8249  O  OD1   . ASP A 1 2505 ? 222.637 258.498 228.658 1.00 2.81  ? 2505 ASP A OD1   1 
ATOM   8250  O  OD2   . ASP A 1 2505 ? 220.815 257.951 227.563 1.00 11.64 ? 2505 ASP A OD2   1 
ATOM   8251  N  N     . SER A 1 2506 ? 225.354 258.854 226.524 1.00 1.89  ? 2506 SER A N     1 
ATOM   8252  C  CA    . SER A 1 2506 ? 225.635 260.102 225.840 1.00 3.21  ? 2506 SER A CA    1 
ATOM   8253  C  C     . SER A 1 2506 ? 227.033 260.053 225.238 1.00 3.57  ? 2506 SER A C     1 
ATOM   8254  O  O     . SER A 1 2506 ? 227.843 259.183 225.560 1.00 6.28  ? 2506 SER A O     1 
ATOM   8255  C  CB    . SER A 1 2506 ? 225.495 261.293 226.798 1.00 4.48  ? 2506 SER A CB    1 
ATOM   8256  O  OG    . SER A 1 2506 ? 226.596 261.372 227.684 1.00 7.11  ? 2506 SER A OG    1 
ATOM   8257  N  N     . ARG A 1 2507 ? 227.309 261.004 224.349 1.00 4.64  ? 2507 ARG A N     1 
ATOM   8258  C  CA    . ARG A 1 2507 ? 228.605 261.061 223.694 1.00 3.98  ? 2507 ARG A CA    1 
ATOM   8259  C  C     . ARG A 1 2507 ? 229.684 261.530 224.668 1.00 5.12  ? 2507 ARG A C     1 
ATOM   8260  O  O     . ARG A 1 2507 ? 229.411 261.946 225.798 1.00 12.42 ? 2507 ARG A O     1 
ATOM   8261  C  CB    . ARG A 1 2507 ? 228.560 261.986 222.480 1.00 5.04  ? 2507 ARG A CB    1 
ATOM   8262  C  CG    . ARG A 1 2507 ? 227.251 261.964 221.722 1.00 8.13  ? 2507 ARG A CG    1 
ATOM   8263  C  CD    . ARG A 1 2507 ? 227.195 263.082 220.696 1.00 13.43 ? 2507 ARG A CD    1 
ATOM   8264  N  NE    . ARG A 1 2507 ? 227.252 264.402 221.311 1.00 12.14 ? 2507 ARG A NE    1 
ATOM   8265  C  CZ    . ARG A 1 2507 ? 226.233 265.250 221.354 1.00 17.97 ? 2507 ARG A CZ    1 
ATOM   8266  N  NH1   . ARG A 1 2507 ? 225.058 264.946 220.827 1.00 20.82 ? 2507 ARG A NH1   1 
ATOM   8267  N  NH2   . ARG A 1 2507 ? 226.395 266.432 221.940 1.00 17.81 ? 2507 ARG A NH2   1 
ATOM   8268  N  N     . LEU A 1 2508 ? 230.933 261.462 224.203 1.00 8.78  ? 2508 LEU A N     1 
ATOM   8269  C  CA    . LEU A 1 2508 ? 232.075 261.783 225.051 1.00 10.98 ? 2508 LEU A CA    1 
ATOM   8270  C  C     . LEU A 1 2508 ? 232.013 263.218 225.559 1.00 10.36 ? 2508 LEU A C     1 
ATOM   8271  O  O     . LEU A 1 2508 ? 232.336 263.486 226.722 1.00 7.81  ? 2508 LEU A O     1 
ATOM   8272  C  CB    . LEU A 1 2508 ? 233.377 261.539 224.287 1.00 8.50  ? 2508 LEU A CB    1 
ATOM   8273  C  CG    . LEU A 1 2508 ? 234.653 262.120 224.894 1.00 13.31 ? 2508 LEU A CG    1 
ATOM   8274  C  CD1   . LEU A 1 2508 ? 235.173 261.247 226.031 1.00 17.37 ? 2508 LEU A CD1   1 
ATOM   8275  C  CD2   . LEU A 1 2508 ? 235.713 262.303 223.827 1.00 13.71 ? 2508 LEU A CD2   1 
ATOM   8276  N  N     . LYS A 1 2509 ? 231.606 264.154 224.701 1.00 7.99  ? 2509 LYS A N     1 
ATOM   8277  C  CA    . LYS A 1 2509 ? 231.531 265.550 225.117 1.00 9.92  ? 2509 LYS A CA    1 
ATOM   8278  C  C     . LYS A 1 2509 ? 230.509 265.732 226.234 1.00 13.76 ? 2509 LYS A C     1 
ATOM   8279  O  O     . LYS A 1 2509 ? 230.735 266.501 227.174 1.00 12.83 ? 2509 LYS A O     1 
ATOM   8280  C  CB    . LYS A 1 2509 ? 231.205 266.435 223.911 1.00 14.17 ? 2509 LYS A CB    1 
ATOM   8281  C  CG    . LYS A 1 2509 ? 231.121 267.931 224.202 1.00 15.89 ? 2509 LYS A CG    1 
ATOM   8282  C  CD    . LYS A 1 2509 ? 229.703 268.392 224.499 1.00 17.80 ? 2509 LYS A CD    1 
ATOM   8283  C  CE    . LYS A 1 2509 ? 228.839 268.355 223.251 1.00 24.44 ? 2509 LYS A CE    1 
ATOM   8284  N  NZ    . LYS A 1 2509 ? 227.451 268.817 223.524 1.00 22.41 ? 2509 LYS A NZ    1 
ATOM   8285  N  N     . MET A 1 2510 ? 229.376 265.031 226.148 1.00 14.20 ? 2510 MET A N     1 
ATOM   8286  C  CA    . MET A 1 2510 ? 228.389 265.097 227.222 1.00 8.02  ? 2510 MET A CA    1 
ATOM   8287  C  C     . MET A 1 2510 ? 228.862 264.339 228.457 1.00 9.01  ? 2510 MET A C     1 
ATOM   8288  O  O     . MET A 1 2510 ? 228.596 264.763 229.588 1.00 12.06 ? 2510 MET A O     1 
ATOM   8289  C  CB    . MET A 1 2510 ? 227.047 264.558 226.733 1.00 6.41  ? 2510 MET A CB    1 
ATOM   8290  C  CG    . MET A 1 2510 ? 226.368 265.454 225.717 1.00 11.53 ? 2510 MET A CG    1 
ATOM   8291  S  SD    . MET A 1 2510 ? 226.116 267.125 226.340 1.00 18.75 ? 2510 MET A SD    1 
ATOM   8292  C  CE    . MET A 1 2510 ? 224.815 267.705 225.260 1.00 14.80 ? 2510 MET A CE    1 
ATOM   8293  N  N     . ARG A 1 2511 ? 229.559 263.217 228.265 1.00 7.43  ? 2511 ARG A N     1 
ATOM   8294  C  CA    . ARG A 1 2511 ? 230.154 262.517 229.400 1.00 5.90  ? 2511 ARG A CA    1 
ATOM   8295  C  C     . ARG A 1 2511 ? 231.176 263.394 230.101 1.00 10.93 ? 2511 ARG A C     1 
ATOM   8296  O  O     . ARG A 1 2511 ? 231.275 263.385 231.334 1.00 10.36 ? 2511 ARG A O     1 
ATOM   8297  C  CB    . ARG A 1 2511 ? 230.806 261.213 228.947 1.00 5.21  ? 2511 ARG A CB    1 
ATOM   8298  C  CG    . ARG A 1 2511 ? 229.854 260.168 228.432 1.00 5.23  ? 2511 ARG A CG    1 
ATOM   8299  C  CD    . ARG A 1 2511 ? 230.619 258.954 227.952 1.00 5.12  ? 2511 ARG A CD    1 
ATOM   8300  N  NE    . ARG A 1 2511 ? 229.736 257.874 227.531 1.00 2.02  ? 2511 ARG A NE    1 
ATOM   8301  C  CZ    . ARG A 1 2511 ? 230.154 256.744 226.979 1.00 3.26  ? 2511 ARG A CZ    1 
ATOM   8302  N  NH1   . ARG A 1 2511 ? 231.437 256.520 226.753 1.00 2.82  ? 2511 ARG A NH1   1 
ATOM   8303  N  NH2   . ARG A 1 2511 ? 229.262 255.818 226.644 1.00 3.29  ? 2511 ARG A NH2   1 
ATOM   8304  N  N     . ALA A 1 2512 ? 231.960 264.148 229.329 1.00 14.59 ? 2512 ALA A N     1 
ATOM   8305  C  CA    . ALA A 1 2512 ? 232.913 265.069 229.932 1.00 9.12  ? 2512 ALA A CA    1 
ATOM   8306  C  C     . ALA A 1 2512 ? 232.202 266.158 230.722 1.00 6.76  ? 2512 ALA A C     1 
ATOM   8307  O  O     . ALA A 1 2512 ? 232.546 266.405 231.882 1.00 5.60  ? 2512 ALA A O     1 
ATOM   8308  C  CB    . ALA A 1 2512 ? 233.807 265.680 228.854 1.00 9.20  ? 2512 ALA A CB    1 
ATOM   8309  N  N     . GLU A 1 2513 ? 231.177 266.782 230.132 1.00 10.01 ? 2513 GLU A N     1 
ATOM   8310  C  CA    . GLU A 1 2513 ? 230.579 267.967 230.741 1.00 10.15 ? 2513 GLU A CA    1 
ATOM   8311  C  C     . GLU A 1 2513 ? 229.951 267.639 232.090 1.00 10.83 ? 2513 GLU A C     1 
ATOM   8312  O  O     . GLU A 1 2513 ? 230.030 268.438 233.031 1.00 14.97 ? 2513 GLU A O     1 
ATOM   8313  C  CB    . GLU A 1 2513 ? 229.537 268.585 229.810 1.00 9.04  ? 2513 GLU A CB    1 
ATOM   8314  C  CG    . GLU A 1 2513 ? 229.240 270.044 230.134 1.00 18.06 ? 2513 GLU A CG    1 
ATOM   8315  C  CD    . GLU A 1 2513 ? 228.096 270.228 231.111 1.00 20.65 ? 2513 GLU A CD    1 
ATOM   8316  O  OE1   . GLU A 1 2513 ? 226.993 269.720 230.844 1.00 26.62 ? 2513 GLU A OE1   1 
ATOM   8317  O  OE2   . GLU A 1 2513 ? 228.302 270.891 232.148 1.00 23.16 ? 2513 GLU A OE2   1 
ATOM   8318  N  N     . LEU A 1 2514 ? 229.309 266.473 232.199 1.00 9.43  ? 2514 LEU A N     1 
ATOM   8319  C  CA    . LEU A 1 2514 ? 228.815 266.024 233.496 1.00 7.12  ? 2514 LEU A CA    1 
ATOM   8320  C  C     . LEU A 1 2514 ? 229.963 265.856 234.484 1.00 6.51  ? 2514 LEU A C     1 
ATOM   8321  O  O     . LEU A 1 2514 ? 229.772 265.990 235.697 1.00 8.28  ? 2514 LEU A O     1 
ATOM   8322  C  CB    . LEU A 1 2514 ? 228.042 264.712 233.334 1.00 8.72  ? 2514 LEU A CB    1 
ATOM   8323  C  CG    . LEU A 1 2514 ? 227.380 264.109 234.577 1.00 6.81  ? 2514 LEU A CG    1 
ATOM   8324  C  CD1   . LEU A 1 2514 ? 226.381 265.081 235.187 1.00 7.08  ? 2514 LEU A CD1   1 
ATOM   8325  C  CD2   . LEU A 1 2514 ? 226.709 262.789 234.245 1.00 2.89  ? 2514 LEU A CD2   1 
ATOM   8326  N  N     . GLY A 1 2515 ? 231.163 265.563 233.978 1.00 6.97  ? 2515 GLY A N     1 
ATOM   8327  C  CA    . GLY A 1 2515 ? 232.317 265.426 234.851 1.00 6.26  ? 2515 GLY A CA    1 
ATOM   8328  C  C     . GLY A 1 2515 ? 232.710 266.718 235.542 1.00 10.15 ? 2515 GLY A C     1 
ATOM   8329  O  O     . GLY A 1 2515 ? 232.955 266.733 236.750 1.00 9.71  ? 2515 GLY A O     1 
ATOM   8330  N  N     . GLU A 1 2516 ? 232.790 267.823 234.789 1.00 8.25  ? 2516 GLU A N     1 
ATOM   8331  C  CA    . GLU A 1 2516 ? 233.138 269.091 235.426 1.00 10.15 ? 2516 GLU A CA    1 
ATOM   8332  C  C     . GLU A 1 2516 ? 232.053 269.539 236.395 1.00 12.48 ? 2516 GLU A C     1 
ATOM   8333  O  O     . GLU A 1 2516 ? 232.357 270.067 237.470 1.00 15.88 ? 2516 GLU A O     1 
ATOM   8334  C  CB    . GLU A 1 2516 ? 233.414 270.202 234.403 1.00 18.30 ? 2516 GLU A CB    1 
ATOM   8335  C  CG    . GLU A 1 2516 ? 234.670 270.035 233.560 1.00 13.93 ? 2516 GLU A CG    1 
ATOM   8336  C  CD    . GLU A 1 2516 ? 234.450 269.186 232.339 1.00 19.27 ? 2516 GLU A CD    1 
ATOM   8337  O  OE1   . GLU A 1 2516 ? 233.293 268.806 232.112 1.00 25.80 ? 2516 GLU A OE1   1 
ATOM   8338  O  OE2   . GLU A 1 2516 ? 235.425 268.901 231.615 1.00 22.87 ? 2516 GLU A OE2   1 
ATOM   8339  N  N     . TYR A 1 2517 ? 230.783 269.339 236.035 1.00 9.59  ? 2517 TYR A N     1 
ATOM   8340  C  CA    . TYR A 1 2517 ? 229.706 269.743 236.932 1.00 12.79 ? 2517 TYR A CA    1 
ATOM   8341  C  C     . TYR A 1 2517 ? 229.781 268.990 238.251 1.00 13.39 ? 2517 TYR A C     1 
ATOM   8342  O  O     . TYR A 1 2517 ? 229.584 269.576 239.323 1.00 15.80 ? 2517 TYR A O     1 
ATOM   8343  C  CB    . TYR A 1 2517 ? 228.345 269.522 236.279 1.00 11.97 ? 2517 TYR A CB    1 
ATOM   8344  C  CG    . TYR A 1 2517 ? 227.208 269.809 237.226 1.00 12.07 ? 2517 TYR A CG    1 
ATOM   8345  C  CD1   . TYR A 1 2517 ? 226.962 271.102 237.670 1.00 12.95 ? 2517 TYR A CD1   1 
ATOM   8346  C  CD2   . TYR A 1 2517 ? 226.396 268.790 237.700 1.00 13.01 ? 2517 TYR A CD2   1 
ATOM   8347  C  CE1   . TYR A 1 2517 ? 225.935 271.372 238.542 1.00 11.63 ? 2517 TYR A CE1   1 
ATOM   8348  C  CE2   . TYR A 1 2517 ? 225.362 269.054 238.575 1.00 14.09 ? 2517 TYR A CE2   1 
ATOM   8349  C  CZ    . TYR A 1 2517 ? 225.135 270.346 238.992 1.00 12.38 ? 2517 TYR A CZ    1 
ATOM   8350  O  OH    . TYR A 1 2517 ? 224.107 270.616 239.862 1.00 12.75 ? 2517 TYR A OH    1 
ATOM   8351  N  N     . ILE A 1 2518 ? 230.051 267.684 238.195 1.00 10.71 ? 2518 ILE A N     1 
ATOM   8352  C  CA    . ILE A 1 2518 ? 230.259 266.921 239.420 1.00 10.28 ? 2518 ILE A CA    1 
ATOM   8353  C  C     . ILE A 1 2518 ? 231.469 267.455 240.170 1.00 12.34 ? 2518 ILE A C     1 
ATOM   8354  O  O     . ILE A 1 2518 ? 231.428 267.638 241.392 1.00 17.58 ? 2518 ILE A O     1 
ATOM   8355  C  CB    . ILE A 1 2518 ? 230.400 265.420 239.102 1.00 6.34  ? 2518 ILE A CB    1 
ATOM   8356  C  CG1   . ILE A 1 2518 ? 229.062 264.846 238.636 1.00 6.54  ? 2518 ILE A CG1   1 
ATOM   8357  C  CG2   . ILE A 1 2518 ? 230.910 264.657 240.313 1.00 7.34  ? 2518 ILE A CG2   1 
ATOM   8358  C  CD1   . ILE A 1 2518 ? 229.121 263.378 238.286 1.00 5.53  ? 2518 ILE A CD1   1 
ATOM   8359  N  N     . ARG A 1 2519 ? 232.552 267.746 239.445 1.00 11.19 ? 2519 ARG A N     1 
ATOM   8360  C  CA    . ARG A 1 2519 ? 233.771 268.241 240.078 1.00 11.30 ? 2519 ARG A CA    1 
ATOM   8361  C  C     . ARG A 1 2519 ? 233.526 269.533 240.846 1.00 16.17 ? 2519 ARG A C     1 
ATOM   8362  O  O     . ARG A 1 2519 ? 234.147 269.759 241.890 1.00 19.75 ? 2519 ARG A O     1 
ATOM   8363  C  CB    . ARG A 1 2519 ? 234.856 268.438 239.020 1.00 12.25 ? 2519 ARG A CB    1 
ATOM   8364  C  CG    . ARG A 1 2519 ? 236.151 269.028 239.544 1.00 14.57 ? 2519 ARG A CG    1 
ATOM   8365  C  CD    . ARG A 1 2519 ? 237.122 269.296 238.407 1.00 10.16 ? 2519 ARG A CD    1 
ATOM   8366  N  NE    . ARG A 1 2519 ? 237.614 268.058 237.816 1.00 8.96  ? 2519 ARG A NE    1 
ATOM   8367  C  CZ    . ARG A 1 2519 ? 238.429 267.203 238.420 1.00 13.36 ? 2519 ARG A CZ    1 
ATOM   8368  N  NH1   . ARG A 1 2519 ? 238.910 267.441 239.628 1.00 13.41 ? 2519 ARG A NH1   1 
ATOM   8369  N  NH2   . ARG A 1 2519 ? 238.772 266.082 237.792 1.00 10.33 ? 2519 ARG A NH2   1 
ATOM   8370  N  N     . ARG A 1 2520 ? 232.620 270.383 240.358 1.00 13.21 ? 2520 ARG A N     1 
ATOM   8371  C  CA    . ARG A 1 2520 ? 232.307 271.616 241.071 1.00 11.79 ? 2520 ARG A CA    1 
ATOM   8372  C  C     . ARG A 1 2520 ? 231.546 271.340 242.363 1.00 17.68 ? 2520 ARG A C     1 
ATOM   8373  O  O     . ARG A 1 2520 ? 231.886 271.888 243.418 1.00 20.08 ? 2520 ARG A O     1 
ATOM   8374  C  CB    . ARG A 1 2520 ? 231.505 272.554 240.168 1.00 11.88 ? 2520 ARG A CB    1 
ATOM   8375  C  CG    . ARG A 1 2520 ? 232.184 272.873 238.849 1.00 14.79 ? 2520 ARG A CG    1 
ATOM   8376  C  CD    . ARG A 1 2520 ? 231.676 274.169 238.243 1.00 13.27 ? 2520 ARG A CD    1 
ATOM   8377  N  NE    . ARG A 1 2520 ? 230.258 274.107 237.908 1.00 17.26 ? 2520 ARG A NE    1 
ATOM   8378  C  CZ    . ARG A 1 2520 ? 229.783 273.709 236.736 1.00 18.53 ? 2520 ARG A CZ    1 
ATOM   8379  N  NH1   . ARG A 1 2520 ? 230.585 273.307 235.763 1.00 18.10 ? 2520 ARG A NH1   1 
ATOM   8380  N  NH2   . ARG A 1 2520 ? 228.469 273.712 236.534 1.00 21.43 ? 2520 ARG A NH2   1 
ATOM   8381  N  N     . ILE A 1 2521 ? 230.529 270.483 242.310 1.00 16.30 ? 2521 ILE A N     1 
ATOM   8382  C  CA    . ILE A 1 2521 ? 229.598 270.376 243.429 1.00 13.14 ? 2521 ILE A CA    1 
ATOM   8383  C  C     . ILE A 1 2521 ? 229.963 269.273 244.420 1.00 12.04 ? 2521 ILE A C     1 
ATOM   8384  O  O     . ILE A 1 2521 ? 229.490 269.296 245.560 1.00 16.64 ? 2521 ILE A O     1 
ATOM   8385  C  CB    . ILE A 1 2521 ? 228.166 270.181 242.906 1.00 12.14 ? 2521 ILE A CB    1 
ATOM   8386  C  CG1   . ILE A 1 2521 ? 228.018 268.805 242.255 1.00 15.41 ? 2521 ILE A CG1   1 
ATOM   8387  C  CG2   . ILE A 1 2521 ? 227.805 271.282 241.927 1.00 12.55 ? 2521 ILE A CG2   1 
ATOM   8388  C  CD1   . ILE A 1 2521 ? 226.648 268.549 241.700 1.00 13.44 ? 2521 ILE A CD1   1 
ATOM   8389  N  N     . THR A 1 2522 ? 230.780 268.301 244.027 1.00 14.88 ? 2522 THR A N     1 
ATOM   8390  C  CA    . THR A 1 2522 ? 231.052 267.211 244.950 1.00 15.98 ? 2522 THR A CA    1 
ATOM   8391  C  C     . THR A 1 2522 ? 232.147 267.599 245.938 1.00 14.60 ? 2522 THR A C     1 
ATOM   8392  O  O     . THR A 1 2522 ? 232.936 268.521 245.711 1.00 14.02 ? 2522 THR A O     1 
ATOM   8393  C  CB    . THR A 1 2522 ? 231.472 265.938 244.216 1.00 15.88 ? 2522 THR A CB    1 
ATOM   8394  O  OG1   . THR A 1 2522 ? 231.550 264.860 245.156 1.00 14.19 ? 2522 THR A OG1   1 
ATOM   8395  C  CG2   . THR A 1 2522 ? 232.851 266.111 243.599 1.00 18.02 ? 2522 THR A CG2   1 
ATOM   8396  N  N     . THR A 1 2523 ? 232.179 266.877 247.054 1.00 16.02 ? 2523 THR A N     1 
ATOM   8397  C  CA    . THR A 1 2523 ? 233.278 266.946 248.001 1.00 13.17 ? 2523 THR A CA    1 
ATOM   8398  C  C     . THR A 1 2523 ? 234.095 265.664 248.024 1.00 13.39 ? 2523 THR A C     1 
ATOM   8399  O  O     . THR A 1 2523 ? 235.060 265.570 248.789 1.00 16.89 ? 2523 THR A O     1 
ATOM   8400  C  CB    . THR A 1 2523 ? 232.757 267.259 249.408 1.00 16.99 ? 2523 THR A CB    1 
ATOM   8401  O  OG1   . THR A 1 2523 ? 231.877 266.215 249.839 1.00 29.08 ? 2523 THR A OG1   1 
ATOM   8402  C  CG2   . THR A 1 2523 ? 232.008 268.578 249.410 1.00 14.91 ? 2523 THR A CG2   1 
ATOM   8403  N  N     . VAL A 1 2524 ? 233.725 264.678 247.217 1.00 13.75 ? 2524 VAL A N     1 
ATOM   8404  C  CA    . VAL A 1 2524 ? 234.520 263.452 247.094 1.00 11.28 ? 2524 VAL A CA    1 
ATOM   8405  C  C     . VAL A 1 2524 ? 235.838 263.782 246.404 1.00 13.40 ? 2524 VAL A C     1 
ATOM   8406  O  O     . VAL A 1 2524 ? 235.841 264.526 245.407 1.00 13.28 ? 2524 VAL A O     1 
ATOM   8407  C  CB    . VAL A 1 2524 ? 233.738 262.393 246.314 1.00 11.56 ? 2524 VAL A CB    1 
ATOM   8408  C  CG1   . VAL A 1 2524 ? 234.534 261.105 246.206 1.00 13.03 ? 2524 VAL A CG1   1 
ATOM   8409  C  CG2   . VAL A 1 2524 ? 232.394 262.140 246.973 1.00 12.17 ? 2524 VAL A CG2   1 
ATOM   8410  N  N     . PRO A 1 2525 ? 236.973 263.286 246.897 1.00 14.23 ? 2525 PRO A N     1 
ATOM   8411  C  CA    . PRO A 1 2525 ? 238.240 263.524 246.197 1.00 12.06 ? 2525 PRO A CA    1 
ATOM   8412  C  C     . PRO A 1 2525 ? 238.196 262.967 244.781 1.00 14.57 ? 2525 PRO A C     1 
ATOM   8413  O  O     . PRO A 1 2525 ? 237.634 261.903 244.526 1.00 21.87 ? 2525 PRO A O     1 
ATOM   8414  C  CB    . PRO A 1 2525 ? 239.266 262.786 247.063 1.00 8.35  ? 2525 PRO A CB    1 
ATOM   8415  C  CG    . PRO A 1 2525 ? 238.647 262.734 248.414 1.00 13.57 ? 2525 PRO A CG    1 
ATOM   8416  C  CD    . PRO A 1 2525 ? 237.169 262.613 248.191 1.00 11.84 ? 2525 PRO A CD    1 
ATOM   8417  N  N     . LEU A 1 2526 ? 238.805 263.702 243.863 1.00 11.99 ? 2526 LEU A N     1 
ATOM   8418  C  CA    . LEU A 1 2526 ? 238.755 263.421 242.439 1.00 12.16 ? 2526 LEU A CA    1 
ATOM   8419  C  C     . LEU A 1 2526 ? 240.161 263.447 241.863 1.00 17.73 ? 2526 LEU A C     1 
ATOM   8420  O  O     . LEU A 1 2526 ? 241.078 264.006 242.473 1.00 22.93 ? 2526 LEU A O     1 
ATOM   8421  C  CB    . LEU A 1 2526 ? 237.869 264.449 241.719 1.00 9.34  ? 2526 LEU A CB    1 
ATOM   8422  C  CG    . LEU A 1 2526 ? 236.386 264.416 242.086 1.00 6.99  ? 2526 LEU A CG    1 
ATOM   8423  C  CD1   . LEU A 1 2526 ? 235.612 265.347 241.186 1.00 8.46  ? 2526 LEU A CD1   1 
ATOM   8424  C  CD2   . LEU A 1 2526 ? 235.830 263.004 241.988 1.00 12.43 ? 2526 LEU A CD2   1 
ATOM   8425  N  N     . PRO A 1 2527 ? 240.373 262.820 240.705 1.00 15.81 ? 2527 PRO A N     1 
ATOM   8426  C  CA    . PRO A 1 2527 ? 241.693 262.889 240.070 1.00 13.83 ? 2527 PRO A CA    1 
ATOM   8427  C  C     . PRO A 1 2527 ? 242.088 264.329 239.777 1.00 18.75 ? 2527 PRO A C     1 
ATOM   8428  O  O     . PRO A 1 2527 ? 241.266 265.149 239.364 1.00 19.49 ? 2527 PRO A O     1 
ATOM   8429  C  CB    . PRO A 1 2527 ? 241.508 262.080 238.783 1.00 13.43 ? 2527 PRO A CB    1 
ATOM   8430  C  CG    . PRO A 1 2527 ? 240.381 261.158 239.082 1.00 9.16  ? 2527 PRO A CG    1 
ATOM   8431  C  CD    . PRO A 1 2527 ? 239.457 261.933 239.967 1.00 11.29 ? 2527 PRO A CD    1 
ATOM   8432  N  N     . THR A 1 2528 ? 243.368 264.626 239.989 1.00 18.05 ? 2528 THR A N     1 
ATOM   8433  C  CA    . THR A 1 2528 ? 243.889 265.981 239.892 1.00 19.64 ? 2528 THR A CA    1 
ATOM   8434  C  C     . THR A 1 2528 ? 244.526 266.276 238.540 1.00 25.18 ? 2528 THR A C     1 
ATOM   8435  O  O     . THR A 1 2528 ? 245.222 267.287 238.405 1.00 27.80 ? 2528 THR A O     1 
ATOM   8436  C  CB    . THR A 1 2528 ? 244.904 266.233 241.008 1.00 21.56 ? 2528 THR A CB    1 
ATOM   8437  O  OG1   . THR A 1 2528 ? 245.998 265.319 240.875 1.00 21.66 ? 2528 THR A OG1   1 
ATOM   8438  C  CG2   . THR A 1 2528 ? 244.255 266.047 242.371 1.00 16.88 ? 2528 THR A CG2   1 
ATOM   8439  N  N     . ALA A 1 2529 ? 244.311 265.420 237.546 1.00 29.55 ? 2529 ALA A N     1 
ATOM   8440  C  CA    . ALA A 1 2529 ? 244.871 265.661 236.228 1.00 18.30 ? 2529 ALA A CA    1 
ATOM   8441  C  C     . ALA A 1 2529 ? 244.276 266.937 235.638 1.00 25.48 ? 2529 ALA A C     1 
ATOM   8442  O  O     . ALA A 1 2529 ? 243.105 267.249 235.885 1.00 29.63 ? 2529 ALA A O     1 
ATOM   8443  C  CB    . ALA A 1 2529 ? 244.600 264.475 235.303 1.00 24.44 ? 2529 ALA A CB    1 
ATOM   8444  N  N     . PRO A 1 2530 ? 245.051 267.702 234.862 1.00 26.62 ? 2530 PRO A N     1 
ATOM   8445  C  CA    . PRO A 1 2530 ? 244.533 268.995 234.388 1.00 25.09 ? 2530 PRO A CA    1 
ATOM   8446  C  C     . PRO A 1 2530 ? 243.430 268.874 233.352 1.00 24.85 ? 2530 PRO A C     1 
ATOM   8447  O  O     . PRO A 1 2530 ? 242.422 269.585 233.452 1.00 27.72 ? 2530 PRO A O     1 
ATOM   8448  C  CB    . PRO A 1 2530 ? 245.786 269.671 233.815 1.00 23.95 ? 2530 PRO A CB    1 
ATOM   8449  C  CG    . PRO A 1 2530 ? 246.648 268.533 233.384 1.00 24.00 ? 2530 PRO A CG    1 
ATOM   8450  C  CD    . PRO A 1 2530 ? 246.433 267.460 234.413 1.00 26.84 ? 2530 PRO A CD    1 
ATOM   8451  N  N     . ASN A 1 2531 ? 243.582 267.993 232.359 1.00 20.80 ? 2531 ASN A N     1 
ATOM   8452  C  CA    . ASN A 1 2531 ? 242.661 267.957 231.228 1.00 24.14 ? 2531 ASN A CA    1 
ATOM   8453  C  C     . ASN A 1 2531 ? 242.141 266.552 230.934 1.00 20.43 ? 2531 ASN A C     1 
ATOM   8454  O  O     . ASN A 1 2531 ? 241.708 266.283 229.808 1.00 23.79 ? 2531 ASN A O     1 
ATOM   8455  C  CB    . ASN A 1 2531 ? 243.326 268.539 229.978 1.00 21.65 ? 2531 ASN A CB    1 
ATOM   8456  C  CG    . ASN A 1 2531 ? 244.029 269.855 230.252 1.00 31.91 ? 2531 ASN A CG    1 
ATOM   8457  O  OD1   . ASN A 1 2531 ? 245.246 269.965 230.106 1.00 31.19 ? 2531 ASN A OD1   1 
ATOM   8458  N  ND2   . ASN A 1 2531 ? 243.262 270.861 230.654 1.00 25.94 ? 2531 ASN A ND2   1 
ATOM   8459  N  N     . ILE A 1 2532 ? 242.167 265.656 231.910 1.00 17.71 ? 2532 ILE A N     1 
ATOM   8460  C  CA    . ILE A 1 2532 ? 241.707 264.281 231.734 1.00 11.19 ? 2532 ILE A CA    1 
ATOM   8461  C  C     . ILE A 1 2532 ? 240.309 264.168 232.330 1.00 11.93 ? 2532 ILE A C     1 
ATOM   8462  O  O     . ILE A 1 2532 ? 240.137 264.439 233.529 1.00 12.46 ? 2532 ILE A O     1 
ATOM   8463  C  CB    . ILE A 1 2532 ? 242.668 263.275 232.383 1.00 12.85 ? 2532 ILE A CB    1 
ATOM   8464  C  CG1   . ILE A 1 2532 ? 244.062 263.411 231.773 1.00 14.55 ? 2532 ILE A CG1   1 
ATOM   8465  C  CG2   . ILE A 1 2532 ? 242.153 261.857 232.203 1.00 11.57 ? 2532 ILE A CG2   1 
ATOM   8466  C  CD1   . ILE A 1 2532 ? 244.102 263.135 230.288 1.00 16.02 ? 2532 ILE A CD1   1 
ATOM   8467  N  N     . PRO A 1 2533 ? 239.298 263.787 231.550 1.00 8.96  ? 2533 PRO A N     1 
ATOM   8468  C  CA    . PRO A 1 2533 ? 237.945 263.660 232.105 1.00 8.63  ? 2533 PRO A CA    1 
ATOM   8469  C  C     . PRO A 1 2533 ? 237.878 262.586 233.179 1.00 8.40  ? 2533 PRO A C     1 
ATOM   8470  O  O     . PRO A 1 2533 ? 238.648 261.624 233.177 1.00 17.53 ? 2533 PRO A O     1 
ATOM   8471  C  CB    . PRO A 1 2533 ? 237.090 263.287 230.887 1.00 9.79  ? 2533 PRO A CB    1 
ATOM   8472  C  CG    . PRO A 1 2533 ? 238.044 262.797 229.863 1.00 6.26  ? 2533 PRO A CG    1 
ATOM   8473  C  CD    . PRO A 1 2533 ? 239.348 263.484 230.112 1.00 7.33  ? 2533 PRO A CD    1 
ATOM   8474  N  N     . ILE A 1 2534 ? 236.946 262.774 234.115 1.00 8.51  ? 2534 ILE A N     1 
ATOM   8475  C  CA    . ILE A 1 2534 ? 236.802 261.835 235.223 1.00 7.16  ? 2534 ILE A CA    1 
ATOM   8476  C  C     . ILE A 1 2534 ? 236.353 260.473 234.712 1.00 5.28  ? 2534 ILE A C     1 
ATOM   8477  O  O     . ILE A 1 2534 ? 236.723 259.433 235.269 1.00 5.73  ? 2534 ILE A O     1 
ATOM   8478  C  CB    . ILE A 1 2534 ? 235.822 262.400 236.270 1.00 6.36  ? 2534 ILE A CB    1 
ATOM   8479  C  CG1   . ILE A 1 2534 ? 236.373 263.693 236.861 1.00 8.36  ? 2534 ILE A CG1   1 
ATOM   8480  C  CG2   . ILE A 1 2534 ? 235.624 261.409 237.403 1.00 4.20  ? 2534 ILE A CG2   1 
ATOM   8481  C  CD1   . ILE A 1 2534 ? 235.370 264.449 237.698 1.00 12.46 ? 2534 ILE A CD1   1 
ATOM   8482  N  N     . ILE A 1 2535 ? 235.567 260.454 233.633 1.00 4.84  ? 2535 ILE A N     1 
ATOM   8483  C  CA    . ILE A 1 2535 ? 235.107 259.217 233.022 1.00 4.57  ? 2535 ILE A CA    1 
ATOM   8484  C  C     . ILE A 1 2535 ? 236.259 258.345 232.536 1.00 6.11  ? 2535 ILE A C     1 
ATOM   8485  O  O     . ILE A 1 2535 ? 236.047 257.175 232.209 1.00 6.97  ? 2535 ILE A O     1 
ATOM   8486  C  CB    . ILE A 1 2535 ? 234.134 259.545 231.866 1.00 7.68  ? 2535 ILE A CB    1 
ATOM   8487  C  CG1   . ILE A 1 2535 ? 233.193 258.373 231.592 1.00 6.74  ? 2535 ILE A CG1   1 
ATOM   8488  C  CG2   . ILE A 1 2535 ? 234.898 259.923 230.607 1.00 6.61  ? 2535 ILE A CG2   1 
ATOM   8489  C  CD1   . ILE A 1 2535 ? 232.058 258.266 232.574 1.00 2.24  ? 2535 ILE A CD1   1 
ATOM   8490  N  N     . ASP A 1 2536 ? 237.473 258.886 232.490 1.00 5.95  ? 2536 ASP A N     1 
ATOM   8491  C  CA    . ASP A 1 2536 ? 238.663 258.151 232.086 1.00 5.12  ? 2536 ASP A CA    1 
ATOM   8492  C  C     . ASP A 1 2536 ? 239.344 257.445 233.252 1.00 4.81  ? 2536 ASP A C     1 
ATOM   8493  O  O     . ASP A 1 2536 ? 240.438 256.899 233.078 1.00 6.00  ? 2536 ASP A O     1 
ATOM   8494  C  CB    . ASP A 1 2536 ? 239.660 259.096 231.407 1.00 6.09  ? 2536 ASP A CB    1 
ATOM   8495  C  CG    . ASP A 1 2536 ? 239.260 259.445 229.987 1.00 12.60 ? 2536 ASP A CG    1 
ATOM   8496  O  OD1   . ASP A 1 2536 ? 238.217 258.945 229.520 1.00 14.10 ? 2536 ASP A OD1   1 
ATOM   8497  O  OD2   . ASP A 1 2536 ? 239.988 260.223 229.340 1.00 17.31 ? 2536 ASP A OD2   1 
ATOM   8498  N  N     . TYR A 1 2537 ? 238.730 257.449 234.431 1.00 5.81  ? 2537 TYR A N     1 
ATOM   8499  C  CA    . TYR A 1 2537 ? 239.308 256.862 235.629 1.00 3.82  ? 2537 TYR A CA    1 
ATOM   8500  C  C     . TYR A 1 2537 ? 238.369 255.805 236.191 1.00 4.62  ? 2537 TYR A C     1 
ATOM   8501  O  O     . TYR A 1 2537 ? 237.147 255.984 236.190 1.00 7.71  ? 2537 TYR A O     1 
ATOM   8502  C  CB    . TYR A 1 2537 ? 239.566 257.930 236.698 1.00 4.45  ? 2537 TYR A CB    1 
ATOM   8503  C  CG    . TYR A 1 2537 ? 240.800 258.771 236.477 1.00 5.05  ? 2537 TYR A CG    1 
ATOM   8504  C  CD1   . TYR A 1 2537 ? 240.741 259.937 235.728 1.00 5.48  ? 2537 TYR A CD1   1 
ATOM   8505  C  CD2   . TYR A 1 2537 ? 242.017 258.412 237.035 1.00 6.88  ? 2537 TYR A CD2   1 
ATOM   8506  C  CE1   . TYR A 1 2537 ? 241.861 260.715 235.532 1.00 6.13  ? 2537 TYR A CE1   1 
ATOM   8507  C  CE2   . TYR A 1 2537 ? 243.146 259.184 236.842 1.00 5.10  ? 2537 TYR A CE2   1 
ATOM   8508  C  CZ    . TYR A 1 2537 ? 243.061 260.335 236.090 1.00 8.75  ? 2537 TYR A CZ    1 
ATOM   8509  O  OH    . TYR A 1 2537 ? 244.179 261.111 235.891 1.00 17.76 ? 2537 TYR A OH    1 
ATOM   8510  N  N     . GLU A 1 2538 ? 238.940 254.708 236.669 1.00 6.20  ? 2538 GLU A N     1 
ATOM   8511  C  CA    . GLU A 1 2538 ? 238.208 253.720 237.448 1.00 8.86  ? 2538 GLU A CA    1 
ATOM   8512  C  C     . GLU A 1 2538 ? 238.536 253.900 238.926 1.00 7.01  ? 2538 GLU A C     1 
ATOM   8513  O  O     . GLU A 1 2538 ? 239.334 254.758 239.312 1.00 8.63  ? 2538 GLU A O     1 
ATOM   8514  C  CB    . GLU A 1 2538 ? 238.539 252.300 236.991 1.00 6.49  ? 2538 GLU A CB    1 
ATOM   8515  C  CG    . GLU A 1 2538 ? 239.995 251.938 237.154 1.00 7.12  ? 2538 GLU A CG    1 
ATOM   8516  C  CD    . GLU A 1 2538 ? 240.208 250.453 237.308 1.00 13.71 ? 2538 GLU A CD    1 
ATOM   8517  O  OE1   . GLU A 1 2538 ? 241.010 250.058 238.182 1.00 14.87 ? 2538 GLU A OE1   1 
ATOM   8518  O  OE2   . GLU A 1 2538 ? 239.571 249.681 236.565 1.00 16.39 ? 2538 GLU A OE2   1 
ATOM   8519  N  N     . VAL A 1 2539 ? 237.916 253.070 239.756 1.00 5.23  ? 2539 VAL A N     1 
ATOM   8520  C  CA    . VAL A 1 2539 ? 238.140 253.086 241.196 1.00 5.33  ? 2539 VAL A CA    1 
ATOM   8521  C  C     . VAL A 1 2539 ? 238.695 251.728 241.595 1.00 6.30  ? 2539 VAL A C     1 
ATOM   8522  O  O     . VAL A 1 2539 ? 238.006 250.709 241.473 1.00 8.81  ? 2539 VAL A O     1 
ATOM   8523  C  CB    . VAL A 1 2539 ? 236.854 253.405 241.976 1.00 5.78  ? 2539 VAL A CB    1 
ATOM   8524  C  CG1   . VAL A 1 2539 ? 237.165 253.597 243.449 1.00 4.87  ? 2539 VAL A CG1   1 
ATOM   8525  C  CG2   . VAL A 1 2539 ? 236.176 254.641 241.404 1.00 2.78  ? 2539 VAL A CG2   1 
ATOM   8526  N  N     . SER A 1 2540 ? 239.939 251.712 242.063 1.00 8.62  ? 2540 SER A N     1 
ATOM   8527  C  CA    . SER A 1 2540 ? 240.538 250.483 242.553 1.00 9.64  ? 2540 SER A CA    1 
ATOM   8528  C  C     . SER A 1 2540 ? 239.966 250.131 243.923 1.00 11.38 ? 2540 SER A C     1 
ATOM   8529  O  O     . SER A 1 2540 ? 239.471 250.990 244.659 1.00 13.19 ? 2540 SER A O     1 
ATOM   8530  C  CB    . SER A 1 2540 ? 242.058 250.614 242.630 1.00 10.23 ? 2540 SER A CB    1 
ATOM   8531  O  OG    . SER A 1 2540 ? 242.440 251.660 243.507 1.00 20.57 ? 2540 SER A OG    1 
ATOM   8532  N  N     . ILE A 1 2541 ? 240.049 248.845 244.267 1.00 10.35 ? 2541 ILE A N     1 
ATOM   8533  C  CA    . ILE A 1 2541 ? 239.470 248.349 245.506 1.00 10.55 ? 2541 ILE A CA    1 
ATOM   8534  C  C     . ILE A 1 2541 ? 240.119 248.975 246.733 1.00 13.87 ? 2541 ILE A C     1 
ATOM   8535  O  O     . ILE A 1 2541 ? 239.552 248.917 247.828 1.00 15.79 ? 2541 ILE A O     1 
ATOM   8536  C  CB    . ILE A 1 2541 ? 239.564 246.805 245.545 1.00 12.86 ? 2541 ILE A CB    1 
ATOM   8537  C  CG1   . ILE A 1 2541 ? 238.690 246.231 246.661 1.00 17.22 ? 2541 ILE A CG1   1 
ATOM   8538  C  CG2   . ILE A 1 2541 ? 241.002 246.362 245.730 1.00 9.28  ? 2541 ILE A CG2   1 
ATOM   8539  C  CD1   . ILE A 1 2541 ? 237.212 246.445 246.450 1.00 10.40 ? 2541 ILE A CD1   1 
ATOM   8540  N  N     . SER A 1 2542 ? 241.286 249.594 246.575 1.00 15.24 ? 2542 SER A N     1 
ATOM   8541  C  CA    . SER A 1 2542 ? 241.953 250.312 247.651 1.00 11.48 ? 2542 SER A CA    1 
ATOM   8542  C  C     . SER A 1 2542 ? 241.434 251.737 247.823 1.00 15.93 ? 2542 SER A C     1 
ATOM   8543  O  O     . SER A 1 2542 ? 242.051 252.523 248.546 1.00 18.61 ? 2542 SER A O     1 
ATOM   8544  C  CB    . SER A 1 2542 ? 243.463 250.343 247.408 1.00 14.45 ? 2542 SER A CB    1 
ATOM   8545  O  OG    . SER A 1 2542 ? 243.784 251.197 246.324 1.00 16.24 ? 2542 SER A OG    1 
ATOM   8546  N  N     . GLY A 1 2543 ? 240.327 252.082 247.176 1.00 14.82 ? 2543 GLY A N     1 
ATOM   8547  C  CA    . GLY A 1 2543 ? 239.772 253.419 247.285 1.00 11.70 ? 2543 GLY A CA    1 
ATOM   8548  C  C     . GLY A 1 2543 ? 240.633 254.500 246.673 1.00 14.20 ? 2543 GLY A C     1 
ATOM   8549  O  O     . GLY A 1 2543 ? 240.674 255.622 247.191 1.00 17.15 ? 2543 GLY A O     1 
ATOM   8550  N  N     . GLU A 1 2544 ? 241.325 254.192 245.584 1.00 13.53 ? 2544 GLU A N     1 
ATOM   8551  C  CA    . GLU A 1 2544 ? 242.139 255.163 244.874 1.00 11.31 ? 2544 GLU A CA    1 
ATOM   8552  C  C     . GLU A 1 2544 ? 241.653 255.257 243.439 1.00 14.47 ? 2544 GLU A C     1 
ATOM   8553  O  O     . GLU A 1 2544 ? 241.296 254.242 242.831 1.00 17.32 ? 2544 GLU A O     1 
ATOM   8554  C  CB    . GLU A 1 2544 ? 243.626 254.780 244.893 1.00 9.82  ? 2544 GLU A CB    1 
ATOM   8555  C  CG    . GLU A 1 2544 ? 244.229 254.635 246.281 1.00 13.29 ? 2544 GLU A CG    1 
ATOM   8556  C  CD    . GLU A 1 2544 ? 244.026 255.859 247.152 1.00 21.38 ? 2544 GLU A CD    1 
ATOM   8557  O  OE1   . GLU A 1 2544 ? 244.208 256.991 246.658 1.00 23.93 ? 2544 GLU A OE1   1 
ATOM   8558  O  OE2   . GLU A 1 2544 ? 243.689 255.686 248.342 1.00 23.07 ? 2544 GLU A OE2   1 
ATOM   8559  N  N     . TRP A 1 2545 ? 241.618 256.471 242.906 1.00 10.57 ? 2545 TRP A N     1 
ATOM   8560  C  CA    . TRP A 1 2545 ? 241.401 256.636 241.479 1.00 9.48  ? 2545 TRP A CA    1 
ATOM   8561  C  C     . TRP A 1 2545 ? 242.590 256.059 240.724 1.00 12.51 ? 2545 TRP A C     1 
ATOM   8562  O  O     . TRP A 1 2545 ? 243.744 256.345 241.053 1.00 20.57 ? 2545 TRP A O     1 
ATOM   8563  C  CB    . TRP A 1 2545 ? 241.216 258.110 241.124 1.00 11.45 ? 2545 TRP A CB    1 
ATOM   8564  C  CG    . TRP A 1 2545 ? 239.919 258.690 241.585 1.00 9.81  ? 2545 TRP A CG    1 
ATOM   8565  C  CD1   . TRP A 1 2545 ? 239.731 259.519 242.649 1.00 9.11  ? 2545 TRP A CD1   1 
ATOM   8566  C  CD2   . TRP A 1 2545 ? 238.625 258.478 241.007 1.00 8.80  ? 2545 TRP A CD2   1 
ATOM   8567  N  NE1   . TRP A 1 2545 ? 238.404 259.848 242.764 1.00 8.28  ? 2545 TRP A NE1   1 
ATOM   8568  C  CE2   . TRP A 1 2545 ? 237.702 259.219 241.771 1.00 8.02  ? 2545 TRP A CE2   1 
ATOM   8569  C  CE3   . TRP A 1 2545 ? 238.158 257.740 239.915 1.00 9.10  ? 2545 TRP A CE3   1 
ATOM   8570  C  CZ2   . TRP A 1 2545 ? 236.339 259.240 241.479 1.00 7.51  ? 2545 TRP A CZ2   1 
ATOM   8571  C  CZ3   . TRP A 1 2545 ? 236.805 257.765 239.629 1.00 6.72  ? 2545 TRP A CZ3   1 
ATOM   8572  C  CH2   . TRP A 1 2545 ? 235.912 258.508 240.408 1.00 6.15  ? 2545 TRP A CH2   1 
ATOM   8573  N  N     . SER A 1 2546 ? 242.311 255.232 239.721 1.00 9.60  ? 2546 SER A N     1 
ATOM   8574  C  CA    . SER A 1 2546 ? 243.352 254.680 238.871 1.00 6.70  ? 2546 SER A CA    1 
ATOM   8575  C  C     . SER A 1 2546 ? 242.967 254.939 237.421 1.00 9.23  ? 2546 SER A C     1 
ATOM   8576  O  O     . SER A 1 2546 ? 241.822 254.667 237.027 1.00 10.76 ? 2546 SER A O     1 
ATOM   8577  C  CB    . SER A 1 2546 ? 243.554 253.181 239.120 1.00 10.67 ? 2546 SER A CB    1 
ATOM   8578  O  OG    . SER A 1 2546 ? 242.316 252.499 239.183 1.00 13.32 ? 2546 SER A OG    1 
ATOM   8579  N  N     . PRO A 1 2547 ? 243.875 255.475 236.608 1.00 8.25  ? 2547 PRO A N     1 
ATOM   8580  C  CA    . PRO A 1 2547 ? 243.531 255.756 235.210 1.00 6.18  ? 2547 PRO A CA    1 
ATOM   8581  C  C     . PRO A 1 2547 ? 243.199 254.481 234.450 1.00 5.94  ? 2547 PRO A C     1 
ATOM   8582  O  O     . PRO A 1 2547 ? 243.812 253.432 234.658 1.00 7.98  ? 2547 PRO A O     1 
ATOM   8583  C  CB    . PRO A 1 2547 ? 244.793 256.432 234.665 1.00 5.35  ? 2547 PRO A CB    1 
ATOM   8584  C  CG    . PRO A 1 2547 ? 245.888 255.954 235.553 1.00 6.21  ? 2547 PRO A CG    1 
ATOM   8585  C  CD    . PRO A 1 2547 ? 245.277 255.803 236.912 1.00 5.43  ? 2547 PRO A CD    1 
ATOM   8586  N  N     . TRP A 1 2548 ? 242.212 254.583 233.560 1.00 4.60  ? 2548 TRP A N     1 
ATOM   8587  C  CA    . TRP A 1 2548 ? 241.844 253.452 232.722 1.00 4.28  ? 2548 TRP A CA    1 
ATOM   8588  C  C     . TRP A 1 2548 ? 242.954 253.075 231.749 1.00 6.03  ? 2548 TRP A C     1 
ATOM   8589  O  O     . TRP A 1 2548 ? 242.979 251.939 231.265 1.00 6.86  ? 2548 TRP A O     1 
ATOM   8590  C  CB    . TRP A 1 2548 ? 240.567 253.768 231.946 1.00 3.91  ? 2548 TRP A CB    1 
ATOM   8591  C  CG    . TRP A 1 2548 ? 239.296 253.406 232.652 1.00 3.93  ? 2548 TRP A CG    1 
ATOM   8592  C  CD1   . TRP A 1 2548 ? 238.291 254.255 233.013 1.00 3.90  ? 2548 TRP A CD1   1 
ATOM   8593  C  CD2   . TRP A 1 2548 ? 238.883 252.097 233.066 1.00 3.66  ? 2548 TRP A CD2   1 
ATOM   8594  N  NE1   . TRP A 1 2548 ? 237.280 253.560 233.628 1.00 3.30  ? 2548 TRP A NE1   1 
ATOM   8595  C  CE2   . TRP A 1 2548 ? 237.619 252.233 233.674 1.00 3.74  ? 2548 TRP A CE2   1 
ATOM   8596  C  CE3   . TRP A 1 2548 ? 239.459 250.829 232.987 1.00 2.21  ? 2548 TRP A CE3   1 
ATOM   8597  C  CZ2   . TRP A 1 2548 ? 236.923 251.147 234.198 1.00 4.95  ? 2548 TRP A CZ2   1 
ATOM   8598  C  CZ3   . TRP A 1 2548 ? 238.767 249.754 233.507 1.00 2.96  ? 2548 TRP A CZ3   1 
ATOM   8599  C  CH2   . TRP A 1 2548 ? 237.514 249.920 234.107 1.00 4.48  ? 2548 TRP A CH2   1 
ATOM   8600  N  N     . GLN A 1 2549 ? 243.870 254.003 231.457 1.00 6.58  ? 2549 GLN A N     1 
ATOM   8601  C  CA    . GLN A 1 2549 ? 244.960 253.729 230.530 1.00 8.36  ? 2549 GLN A CA    1 
ATOM   8602  C  C     . GLN A 1 2549 ? 245.928 252.682 231.065 1.00 12.06 ? 2549 GLN A C     1 
ATOM   8603  O  O     . GLN A 1 2549 ? 246.647 252.062 230.275 1.00 15.96 ? 2549 GLN A O     1 
ATOM   8604  C  CB    . GLN A 1 2549 ? 245.711 255.022 230.216 1.00 8.62  ? 2549 GLN A CB    1 
ATOM   8605  C  CG    . GLN A 1 2549 ? 246.512 254.989 228.926 1.00 12.38 ? 2549 GLN A CG    1 
ATOM   8606  C  CD    . GLN A 1 2549 ? 245.629 254.939 227.696 1.00 14.88 ? 2549 GLN A CD    1 
ATOM   8607  O  OE1   . GLN A 1 2549 ? 244.823 255.839 227.461 1.00 19.96 ? 2549 GLN A OE1   1 
ATOM   8608  N  NE2   . GLN A 1 2549 ? 245.781 253.889 226.901 1.00 15.65 ? 2549 GLN A NE2   1 
ATOM   8609  N  N     . ALA A 1 2550 ? 245.963 252.471 232.382 1.00 10.36 ? 2550 ALA A N     1 
ATOM   8610  C  CA    . ALA A 1 2550 ? 246.821 251.439 232.949 1.00 6.69  ? 2550 ALA A CA    1 
ATOM   8611  C  C     . ALA A 1 2550 ? 246.378 250.038 232.553 1.00 10.65 ? 2550 ALA A C     1 
ATOM   8612  O  O     . ALA A 1 2550 ? 247.180 249.103 232.630 1.00 14.85 ? 2550 ALA A O     1 
ATOM   8613  C  CB    . ALA A 1 2550 ? 246.858 251.563 234.472 1.00 8.77  ? 2550 ALA A CB    1 
ATOM   8614  N  N     . LYS A 1 2551 ? 245.123 249.872 232.136 1.00 11.25 ? 2551 LYS A N     1 
ATOM   8615  C  CA    . LYS A 1 2551 ? 244.598 248.590 231.691 1.00 9.29  ? 2551 LYS A CA    1 
ATOM   8616  C  C     . LYS A 1 2551 ? 244.479 248.511 230.175 1.00 9.62  ? 2551 LYS A C     1 
ATOM   8617  O  O     . LYS A 1 2551 ? 243.723 247.681 229.659 1.00 15.33 ? 2551 LYS A O     1 
ATOM   8618  C  CB    . LYS A 1 2551 ? 243.244 248.321 232.347 1.00 7.76  ? 2551 LYS A CB    1 
ATOM   8619  C  CG    . LYS A 1 2551 ? 243.323 248.083 233.843 1.00 9.89  ? 2551 LYS A CG    1 
ATOM   8620  C  CD    . LYS A 1 2551 ? 241.986 247.637 234.403 1.00 12.64 ? 2551 LYS A CD    1 
ATOM   8621  C  CE    . LYS A 1 2551 ? 242.045 247.485 235.911 1.00 9.40  ? 2551 LYS A CE    1 
ATOM   8622  N  NZ    . LYS A 1 2551 ? 240.687 247.394 236.507 1.00 10.76 ? 2551 LYS A NZ    1 
ATOM   8623  N  N     . VAL A 1 2552 ? 245.208 249.355 229.452 1.00 12.40 ? 2552 VAL A N     1 
ATOM   8624  C  CA    . VAL A 1 2552 ? 245.184 249.353 227.992 1.00 10.15 ? 2552 VAL A CA    1 
ATOM   8625  C  C     . VAL A 1 2552 ? 246.620 249.178 227.513 1.00 16.28 ? 2552 VAL A C     1 
ATOM   8626  O  O     . VAL A 1 2552 ? 247.298 250.166 227.191 1.00 12.15 ? 2552 VAL A O     1 
ATOM   8627  C  CB    . VAL A 1 2552 ? 244.546 250.636 227.434 1.00 10.41 ? 2552 VAL A CB    1 
ATOM   8628  C  CG1   . VAL A 1 2552 ? 244.582 250.649 225.908 1.00 8.11  ? 2552 VAL A CG1   1 
ATOM   8629  C  CG2   . VAL A 1 2552 ? 243.126 250.790 227.936 1.00 9.88  ? 2552 VAL A CG2   1 
ATOM   8630  N  N     . PRO A 1 2553 ? 247.139 247.956 227.488 1.00 17.20 ? 2553 PRO A N     1 
ATOM   8631  C  CA    . PRO A 1 2553 ? 248.493 247.737 226.977 1.00 16.43 ? 2553 PRO A CA    1 
ATOM   8632  C  C     . PRO A 1 2553 ? 248.532 247.729 225.458 1.00 20.30 ? 2553 PRO A C     1 
ATOM   8633  O  O     . PRO A 1 2553 ? 247.553 247.409 224.782 1.00 22.26 ? 2553 PRO A O     1 
ATOM   8634  C  CB    . PRO A 1 2553 ? 248.855 246.359 227.541 1.00 16.11 ? 2553 PRO A CB    1 
ATOM   8635  C  CG    . PRO A 1 2553 ? 247.544 245.658 227.604 1.00 18.25 ? 2553 PRO A CG    1 
ATOM   8636  C  CD    . PRO A 1 2553 ? 246.534 246.708 227.986 1.00 9.06  ? 2553 PRO A CD    1 
ATOM   8637  N  N     . GLN A 1 2554 ? 249.693 248.098 224.925 1.00 22.40 ? 2554 GLN A N     1 
ATOM   8638  C  CA    . GLN A 1 2554 ? 249.945 247.999 223.488 1.00 16.68 ? 2554 GLN A CA    1 
ATOM   8639  C  C     . GLN A 1 2554 ? 250.340 246.559 223.192 1.00 21.24 ? 2554 GLN A C     1 
ATOM   8640  O  O     . GLN A 1 2554 ? 251.511 246.184 223.257 1.00 25.21 ? 2554 GLN A O     1 
ATOM   8641  C  CB    . GLN A 1 2554 ? 251.027 248.979 223.054 1.00 15.28 ? 2554 GLN A CB    1 
ATOM   8642  C  CG    . GLN A 1 2554 ? 251.274 248.988 221.556 1.00 23.91 ? 2554 GLN A CG    1 
ATOM   8643  C  CD    . GLN A 1 2554 ? 252.582 249.652 221.183 1.00 29.92 ? 2554 GLN A CD    1 
ATOM   8644  O  OE1   . GLN A 1 2554 ? 252.963 249.684 220.013 1.00 29.13 ? 2554 GLN A OE1   1 
ATOM   8645  N  NE2   . GLN A 1 2554 ? 253.280 250.185 222.178 1.00 27.74 ? 2554 GLN A NE2   1 
ATOM   8646  N  N     . ILE A 1 2555 ? 249.343 245.738 222.870 1.00 19.42 ? 2555 ILE A N     1 
ATOM   8647  C  CA    . ILE A 1 2555 ? 249.585 244.318 222.656 1.00 13.86 ? 2555 ILE A CA    1 
ATOM   8648  C  C     . ILE A 1 2555 ? 250.211 244.098 221.283 1.00 17.05 ? 2555 ILE A C     1 
ATOM   8649  O  O     . ILE A 1 2555 ? 250.145 244.946 220.389 1.00 15.80 ? 2555 ILE A O     1 
ATOM   8650  C  CB    . ILE A 1 2555 ? 248.288 243.505 222.798 1.00 15.51 ? 2555 ILE A CB    1 
ATOM   8651  C  CG1   . ILE A 1 2555 ? 247.279 243.934 221.733 1.00 14.23 ? 2555 ILE A CG1   1 
ATOM   8652  C  CG2   . ILE A 1 2555 ? 247.694 243.692 224.182 1.00 19.55 ? 2555 ILE A CG2   1 
ATOM   8653  C  CD1   . ILE A 1 2555 ? 246.076 243.037 221.642 1.00 11.53 ? 2555 ILE A CD1   1 
ATOM   8654  N  N     . GLU A 1 2556 ? 250.831 242.934 221.122 1.00 18.28 ? 2556 GLU A N     1 
ATOM   8655  C  CA    . GLU A 1 2556 ? 251.218 242.413 219.820 1.00 12.89 ? 2556 GLU A CA    1 
ATOM   8656  C  C     . GLU A 1 2556 ? 250.399 241.153 219.573 1.00 17.21 ? 2556 GLU A C     1 
ATOM   8657  O  O     . GLU A 1 2556 ? 250.423 240.226 220.389 1.00 23.19 ? 2556 GLU A O     1 
ATOM   8658  C  CB    . GLU A 1 2556 ? 252.717 242.115 219.753 1.00 9.03  ? 2556 GLU A CB    1 
ATOM   8659  C  CG    . GLU A 1 2556 ? 253.614 243.316 220.017 1.00 12.09 ? 2556 GLU A CG    1 
ATOM   8660  C  CD    . GLU A 1 2556 ? 253.361 244.473 219.068 1.00 20.61 ? 2556 GLU A CD    1 
ATOM   8661  O  OE1   . GLU A 1 2556 ? 253.417 244.266 217.838 1.00 30.70 ? 2556 GLU A OE1   1 
ATOM   8662  O  OE2   . GLU A 1 2556 ? 253.114 245.596 219.555 1.00 22.78 ? 2556 GLU A OE2   1 
ATOM   8663  N  N     . VAL A 1 2557 ? 249.673 241.128 218.468 1.00 13.11 ? 2557 VAL A N     1 
ATOM   8664  C  CA    . VAL A 1 2557 ? 248.730 240.058 218.170 1.00 4.64  ? 2557 VAL A CA    1 
ATOM   8665  C  C     . VAL A 1 2557 ? 249.449 238.959 217.399 1.00 11.70 ? 2557 VAL A C     1 
ATOM   8666  O  O     . VAL A 1 2557 ? 250.291 239.233 216.537 1.00 14.42 ? 2557 VAL A O     1 
ATOM   8667  C  CB    . VAL A 1 2557 ? 247.523 240.611 217.385 1.00 7.81  ? 2557 VAL A CB    1 
ATOM   8668  C  CG1   . VAL A 1 2557 ? 246.767 239.505 216.672 1.00 7.60  ? 2557 VAL A CG1   1 
ATOM   8669  C  CG2   . VAL A 1 2557 ? 246.597 241.375 218.316 1.00 11.09 ? 2557 VAL A CG2   1 
ATOM   8670  N  N     . GLU A 1 2558 ? 249.135 237.705 217.728 1.00 16.66 ? 2558 GLU A N     1 
ATOM   8671  C  CA    . GLU A 1 2558 ? 249.689 236.576 216.994 1.00 17.18 ? 2558 GLU A CA    1 
ATOM   8672  C  C     . GLU A 1 2558 ? 249.311 236.674 215.520 1.00 16.37 ? 2558 GLU A C     1 
ATOM   8673  O  O     . GLU A 1 2558 ? 248.181 237.032 215.177 1.00 13.40 ? 2558 GLU A O     1 
ATOM   8674  C  CB    . GLU A 1 2558 ? 249.183 235.261 217.585 1.00 16.30 ? 2558 GLU A CB    1 
ATOM   8675  C  CG    . GLU A 1 2558 ? 249.664 234.976 218.999 1.00 20.39 ? 2558 GLU A CG    1 
ATOM   8676  C  CD    . GLU A 1 2558 ? 251.160 234.738 219.076 1.00 26.48 ? 2558 GLU A CD    1 
ATOM   8677  O  OE1   . GLU A 1 2558 ? 251.735 234.206 218.101 1.00 28.45 ? 2558 GLU A OE1   1 
ATOM   8678  O  OE2   . GLU A 1 2558 ? 251.760 235.073 220.118 1.00 30.23 ? 2558 GLU A OE2   1 
ATOM   8679  N  N     . THR A 1 2559 ? 250.267 236.350 214.648 1.00 18.15 ? 2559 THR A N     1 
ATOM   8680  C  CA    . THR A 1 2559 ? 250.112 236.638 213.226 1.00 13.21 ? 2559 THR A CA    1 
ATOM   8681  C  C     . THR A 1 2559 ? 248.959 235.877 212.586 1.00 17.91 ? 2559 THR A C     1 
ATOM   8682  O  O     . THR A 1 2559 ? 248.463 236.302 211.539 1.00 17.89 ? 2559 THR A O     1 
ATOM   8683  C  CB    . THR A 1 2559 ? 251.414 236.335 212.477 1.00 13.56 ? 2559 THR A CB    1 
ATOM   8684  O  OG1   . THR A 1 2559 ? 251.301 236.784 211.121 1.00 20.25 ? 2559 THR A OG1   1 
ATOM   8685  C  CG2   . THR A 1 2559 ? 251.705 234.847 212.485 1.00 16.15 ? 2559 THR A CG2   1 
ATOM   8686  N  N     . HIS A 1 2560 ? 248.515 234.771 213.181 1.00 17.28 ? 2560 HIS A N     1 
ATOM   8687  C  CA    . HIS A 1 2560 ? 247.404 234.017 212.616 1.00 13.33 ? 2560 HIS A CA    1 
ATOM   8688  C  C     . HIS A 1 2560 ? 246.046 234.482 213.123 1.00 18.20 ? 2560 HIS A C     1 
ATOM   8689  O  O     . HIS A 1 2560 ? 245.019 233.999 212.631 1.00 22.69 ? 2560 HIS A O     1 
ATOM   8690  C  CB    . HIS A 1 2560 ? 247.572 232.522 212.905 1.00 18.43 ? 2560 HIS A CB    1 
ATOM   8691  C  CG    . HIS A 1 2560 ? 247.270 232.137 214.320 1.00 17.00 ? 2560 HIS A CG    1 
ATOM   8692  N  ND1   . HIS A 1 2560 ? 248.198 232.234 215.333 1.00 24.19 ? 2560 HIS A ND1   1 
ATOM   8693  C  CD2   . HIS A 1 2560 ? 246.145 231.641 214.887 1.00 17.07 ? 2560 HIS A CD2   1 
ATOM   8694  C  CE1   . HIS A 1 2560 ? 247.656 231.823 216.465 1.00 21.94 ? 2560 HIS A CE1   1 
ATOM   8695  N  NE2   . HIS A 1 2560 ? 246.411 231.456 216.221 1.00 18.97 ? 2560 HIS A NE2   1 
ATOM   8696  N  N     . LYS A 1 2561 ? 246.007 235.410 214.080 1.00 15.58 ? 2561 LYS A N     1 
ATOM   8697  C  CA    . LYS A 1 2561 ? 244.760 235.948 214.603 1.00 10.15 ? 2561 LYS A CA    1 
ATOM   8698  C  C     . LYS A 1 2561 ? 244.505 237.375 214.138 1.00 12.61 ? 2561 LYS A C     1 
ATOM   8699  O  O     . LYS A 1 2561 ? 243.746 238.106 214.785 1.00 17.22 ? 2561 LYS A O     1 
ATOM   8700  C  CB    . LYS A 1 2561 ? 244.753 235.890 216.131 1.00 15.51 ? 2561 LYS A CB    1 
ATOM   8701  C  CG    . LYS A 1 2561 ? 245.251 234.586 216.720 1.00 19.20 ? 2561 LYS A CG    1 
ATOM   8702  C  CD    . LYS A 1 2561 ? 245.306 234.672 218.238 1.00 18.67 ? 2561 LYS A CD    1 
ATOM   8703  C  CE    . LYS A 1 2561 ? 245.637 233.328 218.864 1.00 26.07 ? 2561 LYS A CE    1 
ATOM   8704  N  NZ    . LYS A 1 2561 ? 244.613 232.298 218.540 1.00 22.94 ? 2561 LYS A NZ    1 
ATOM   8705  N  N     . VAL A 1 2562 ? 245.123 237.788 213.033 1.00 13.99 ? 2562 VAL A N     1 
ATOM   8706  C  CA    . VAL A 1 2562 ? 245.031 239.169 212.575 1.00 11.82 ? 2562 VAL A CA    1 
ATOM   8707  C  C     . VAL A 1 2562 ? 243.601 239.460 212.142 1.00 14.59 ? 2562 VAL A C     1 
ATOM   8708  O  O     . VAL A 1 2562 ? 243.076 238.826 211.220 1.00 21.61 ? 2562 VAL A O     1 
ATOM   8709  C  CB    . VAL A 1 2562 ? 246.020 239.431 211.434 1.00 11.12 ? 2562 VAL A CB    1 
ATOM   8710  C  CG1   . VAL A 1 2562 ? 245.767 240.787 210.827 1.00 13.65 ? 2562 VAL A CG1   1 
ATOM   8711  C  CG2   . VAL A 1 2562 ? 247.444 239.332 211.933 1.00 13.29 ? 2562 VAL A CG2   1 
ATOM   8712  N  N     . ALA A 1 2563 ? 242.969 240.431 212.804 1.00 11.78 ? 2563 ALA A N     1 
ATOM   8713  C  CA    . ALA A 1 2563 ? 241.594 240.842 212.514 1.00 6.59  ? 2563 ALA A CA    1 
ATOM   8714  C  C     . ALA A 1 2563 ? 240.619 239.668 212.582 1.00 9.72  ? 2563 ALA A C     1 
ATOM   8715  O  O     . ALA A 1 2563 ? 239.653 239.605 211.817 1.00 11.81 ? 2563 ALA A O     1 
ATOM   8716  C  CB    . ALA A 1 2563 ? 241.496 241.544 211.158 1.00 6.34  ? 2563 ALA A CB    1 
ATOM   8717  N  N     . ALA A 1 2564 ? 240.867 238.729 213.490 1.00 13.36 ? 2564 ALA A N     1 
ATOM   8718  C  CA    . ALA A 1 2564 ? 239.946 237.625 213.684 1.00 11.22 ? 2564 ALA A CA    1 
ATOM   8719  C  C     . ALA A 1 2564 ? 238.712 238.102 214.454 1.00 18.47 ? 2564 ALA A C     1 
ATOM   8720  O  O     . ALA A 1 2564 ? 238.783 239.071 215.214 1.00 17.91 ? 2564 ALA A O     1 
ATOM   8721  C  CB    . ALA A 1 2564 ? 240.628 236.482 214.433 1.00 9.16  ? 2564 ALA A CB    1 
ATOM   8722  N  N     . PRO A 1 2565 ? 237.565 237.444 214.264 1.00 18.79 ? 2565 PRO A N     1 
ATOM   8723  C  CA    . PRO A 1 2565 ? 236.327 237.934 214.898 1.00 17.64 ? 2565 PRO A CA    1 
ATOM   8724  C  C     . PRO A 1 2565 ? 236.364 237.956 216.416 1.00 18.42 ? 2565 PRO A C     1 
ATOM   8725  O  O     . PRO A 1 2565 ? 235.632 238.741 217.030 1.00 27.05 ? 2565 PRO A O     1 
ATOM   8726  C  CB    . PRO A 1 2565 ? 235.265 236.957 214.374 1.00 15.79 ? 2565 PRO A CB    1 
ATOM   8727  C  CG    . PRO A 1 2565 ? 236.038 235.739 213.981 1.00 18.90 ? 2565 PRO A CG    1 
ATOM   8728  C  CD    . PRO A 1 2565 ? 237.301 236.279 213.404 1.00 14.47 ? 2565 PRO A CD    1 
ATOM   8729  N  N     . ASP A 1 2566 ? 237.183 237.118 217.047 1.00 13.72 ? 2566 ASP A N     1 
ATOM   8730  C  CA    . ASP A 1 2566 ? 237.212 237.009 218.499 1.00 15.70 ? 2566 ASP A CA    1 
ATOM   8731  C  C     . ASP A 1 2566 ? 238.260 237.916 219.137 1.00 13.95 ? 2566 ASP A C     1 
ATOM   8732  O  O     . ASP A 1 2566 ? 238.287 238.047 220.365 1.00 12.74 ? 2566 ASP A O     1 
ATOM   8733  C  CB    . ASP A 1 2566 ? 237.457 235.551 218.898 1.00 17.82 ? 2566 ASP A CB    1 
ATOM   8734  C  CG    . ASP A 1 2566 ? 237.347 235.321 220.391 1.00 23.17 ? 2566 ASP A CG    1 
ATOM   8735  O  OD1   . ASP A 1 2566 ? 236.211 235.316 220.906 1.00 26.89 ? 2566 ASP A OD1   1 
ATOM   8736  O  OD2   . ASP A 1 2566 ? 238.394 235.147 221.049 1.00 23.59 ? 2566 ASP A OD2   1 
ATOM   8737  N  N     . VAL A 1 2567 ? 239.105 238.565 218.341 1.00 11.92 ? 2567 VAL A N     1 
ATOM   8738  C  CA    . VAL A 1 2567 ? 240.231 239.340 218.848 1.00 5.08  ? 2567 VAL A CA    1 
ATOM   8739  C  C     . VAL A 1 2567 ? 239.807 240.790 219.019 1.00 4.06  ? 2567 VAL A C     1 
ATOM   8740  O  O     . VAL A 1 2567 ? 239.261 241.402 218.092 1.00 10.69 ? 2567 VAL A O     1 
ATOM   8741  C  CB    . VAL A 1 2567 ? 241.451 239.231 217.917 1.00 7.30  ? 2567 VAL A CB    1 
ATOM   8742  C  CG1   . VAL A 1 2567 ? 242.666 239.860 218.566 1.00 6.12  ? 2567 VAL A CG1   1 
ATOM   8743  C  CG2   . VAL A 1 2567 ? 241.727 237.780 217.590 1.00 10.05 ? 2567 VAL A CG2   1 
ATOM   8744  N  N     . VAL A 1 2568 ? 240.055 241.338 220.204 1.00 3.59  ? 2568 VAL A N     1 
ATOM   8745  C  CA    . VAL A 1 2568 ? 239.744 242.724 220.529 1.00 1.91  ? 2568 VAL A CA    1 
ATOM   8746  C  C     . VAL A 1 2568 ? 241.039 243.407 220.936 1.00 1.22  ? 2568 VAL A C     1 
ATOM   8747  O  O     . VAL A 1 2568 ? 241.713 242.963 221.872 1.00 3.08  ? 2568 VAL A O     1 
ATOM   8748  C  CB    . VAL A 1 2568 ? 238.701 242.828 221.654 1.00 2.39  ? 2568 VAL A CB    1 
ATOM   8749  C  CG1   . VAL A 1 2568 ? 238.334 244.281 221.913 1.00 0.58  ? 2568 VAL A CG1   1 
ATOM   8750  C  CG2   . VAL A 1 2568 ? 237.472 242.003 221.319 1.00 2.08  ? 2568 VAL A CG2   1 
ATOM   8751  N  N     . VAL A 1 2569 ? 241.389 244.478 220.233 1.00 1.25  ? 2569 VAL A N     1 
ATOM   8752  C  CA    . VAL A 1 2569 ? 242.552 245.278 220.604 1.00 1.38  ? 2569 VAL A CA    1 
ATOM   8753  C  C     . VAL A 1 2569 ? 242.130 246.223 221.720 1.00 1.64  ? 2569 VAL A C     1 
ATOM   8754  O  O     . VAL A 1 2569 ? 241.187 247.007 221.545 1.00 2.59  ? 2569 VAL A O     1 
ATOM   8755  C  CB    . VAL A 1 2569 ? 243.123 246.039 219.397 1.00 2.03  ? 2569 VAL A CB    1 
ATOM   8756  C  CG1   . VAL A 1 2569 ? 244.296 246.907 219.825 1.00 1.51  ? 2569 VAL A CG1   1 
ATOM   8757  C  CG2   . VAL A 1 2569 ? 243.542 245.063 218.312 1.00 1.33  ? 2569 VAL A CG2   1 
ATOM   8758  N  N     . PRO A 1 2570 ? 242.777 246.171 222.882 1.00 3.55  ? 2570 PRO A N     1 
ATOM   8759  C  CA    . PRO A 1 2570 ? 242.368 247.026 224.006 1.00 2.42  ? 2570 PRO A CA    1 
ATOM   8760  C  C     . PRO A 1 2570 ? 242.532 248.501 223.684 1.00 3.94  ? 2570 PRO A C     1 
ATOM   8761  O  O     . PRO A 1 2570 ? 243.609 248.958 223.298 1.00 4.79  ? 2570 PRO A O     1 
ATOM   8762  C  CB    . PRO A 1 2570 ? 243.303 246.585 225.137 1.00 2.53  ? 2570 PRO A CB    1 
ATOM   8763  C  CG    . PRO A 1 2570 ? 243.708 245.205 224.772 1.00 5.23  ? 2570 PRO A CG    1 
ATOM   8764  C  CD    . PRO A 1 2570 ? 243.805 245.197 223.280 1.00 5.08  ? 2570 PRO A CD    1 
ATOM   8765  N  N     . THR A 1 2571 ? 241.444 249.246 223.844 1.00 4.42  ? 2571 THR A N     1 
ATOM   8766  C  CA    . THR A 1 2571 ? 241.446 250.696 223.733 1.00 3.42  ? 2571 THR A CA    1 
ATOM   8767  C  C     . THR A 1 2571 ? 240.822 251.281 224.990 1.00 3.72  ? 2571 THR A C     1 
ATOM   8768  O  O     . THR A 1 2571 ? 240.324 250.559 225.857 1.00 6.14  ? 2571 THR A O     1 
ATOM   8769  C  CB    . THR A 1 2571 ? 240.692 251.180 222.484 1.00 5.19  ? 2571 THR A CB    1 
ATOM   8770  O  OG1   . THR A 1 2571 ? 239.292 250.907 222.624 1.00 5.62  ? 2571 THR A OG1   1 
ATOM   8771  C  CG2   . THR A 1 2571 ? 241.219 250.493 221.233 1.00 2.93  ? 2571 THR A CG2   1 
ATOM   8772  N  N     . LEU A 1 2572 ? 240.859 252.611 225.083 1.00 6.34  ? 2572 LEU A N     1 
ATOM   8773  C  CA    . LEU A 1 2572 ? 240.286 253.287 226.241 1.00 3.14  ? 2572 LEU A CA    1 
ATOM   8774  C  C     . LEU A 1 2572 ? 238.794 253.007 226.361 1.00 5.25  ? 2572 LEU A C     1 
ATOM   8775  O  O     . LEU A 1 2572 ? 238.281 252.799 227.466 1.00 9.67  ? 2572 LEU A O     1 
ATOM   8776  C  CB    . LEU A 1 2572 ? 240.543 254.791 226.146 1.00 7.07  ? 2572 LEU A CB    1 
ATOM   8777  C  CG    . LEU A 1 2572 ? 240.060 255.639 227.326 1.00 7.35  ? 2572 LEU A CG    1 
ATOM   8778  C  CD1   . LEU A 1 2572 ? 240.790 255.249 228.597 1.00 6.75  ? 2572 LEU A CD1   1 
ATOM   8779  C  CD2   . LEU A 1 2572 ? 240.223 257.122 227.037 1.00 10.90 ? 2572 LEU A CD2   1 
ATOM   8780  N  N     . ASP A 1 2573 ? 238.082 252.991 225.234 1.00 5.60  ? 2573 ASP A N     1 
ATOM   8781  C  CA    . ASP A 1 2573 ? 236.640 252.772 225.275 1.00 4.40  ? 2573 ASP A CA    1 
ATOM   8782  C  C     . ASP A 1 2573 ? 236.297 251.320 225.582 1.00 4.63  ? 2573 ASP A C     1 
ATOM   8783  O  O     . ASP A 1 2573 ? 235.334 251.048 226.309 1.00 7.75  ? 2573 ASP A O     1 
ATOM   8784  C  CB    . ASP A 1 2573 ? 236.008 253.208 223.953 1.00 5.24  ? 2573 ASP A CB    1 
ATOM   8785  C  CG    . ASP A 1 2573 ? 236.055 254.708 223.753 1.00 14.99 ? 2573 ASP A CG    1 
ATOM   8786  O  OD1   . ASP A 1 2573 ? 236.039 255.444 224.759 1.00 18.04 ? 2573 ASP A OD1   1 
ATOM   8787  O  OD2   . ASP A 1 2573 ? 236.106 255.157 222.590 1.00 17.62 ? 2573 ASP A OD2   1 
ATOM   8788  N  N     . THR A 1 2574 ? 237.062 250.374 225.033 1.00 3.39  ? 2574 THR A N     1 
ATOM   8789  C  CA    . THR A 1 2574 ? 236.719 248.963 225.202 1.00 2.69  ? 2574 THR A CA    1 
ATOM   8790  C  C     . THR A 1 2574 ? 236.837 248.523 226.657 1.00 2.06  ? 2574 THR A C     1 
ATOM   8791  O  O     . THR A 1 2574 ? 235.966 247.809 227.162 1.00 1.66  ? 2574 THR A O     1 
ATOM   8792  C  CB    . THR A 1 2574 ? 237.599 248.090 224.304 1.00 2.11  ? 2574 THR A CB    1 
ATOM   8793  O  OG1   . THR A 1 2574 ? 238.975 248.446 224.478 1.00 5.40  ? 2574 THR A OG1   1 
ATOM   8794  C  CG2   . THR A 1 2574 ? 237.210 248.263 222.846 1.00 1.00  ? 2574 THR A CG2   1 
ATOM   8795  N  N     . VAL A 1 2575 ? 237.904 248.933 227.344 1.00 2.89  ? 2575 VAL A N     1 
ATOM   8796  C  CA    . VAL A 1 2575 ? 238.093 248.511 228.729 1.00 2.96  ? 2575 VAL A CA    1 
ATOM   8797  C  C     . VAL A 1 2575 ? 237.046 249.149 229.640 1.00 2.86  ? 2575 VAL A C     1 
ATOM   8798  O  O     . VAL A 1 2575 ? 236.602 248.535 230.615 1.00 4.99  ? 2575 VAL A O     1 
ATOM   8799  C  CB    . VAL A 1 2575 ? 239.530 248.814 229.199 1.00 4.79  ? 2575 VAL A CB    1 
ATOM   8800  C  CG1   . VAL A 1 2575 ? 240.533 248.151 228.276 1.00 4.59  ? 2575 VAL A CG1   1 
ATOM   8801  C  CG2   . VAL A 1 2575 ? 239.779 250.313 229.274 1.00 6.88  ? 2575 VAL A CG2   1 
ATOM   8802  N  N     . ARG A 1 2576 ? 236.642 250.387 229.346 1.00 3.01  ? 2576 ARG A N     1 
ATOM   8803  C  CA    . ARG A 1 2576 ? 235.605 251.034 230.143 1.00 2.34  ? 2576 ARG A CA    1 
ATOM   8804  C  C     . ARG A 1 2576 ? 234.246 250.398 229.889 1.00 1.90  ? 2576 ARG A C     1 
ATOM   8805  O  O     . ARG A 1 2576 ? 233.499 250.105 230.830 1.00 1.69  ? 2576 ARG A O     1 
ATOM   8806  C  CB    . ARG A 1 2576 ? 235.556 252.532 229.838 1.00 3.05  ? 2576 ARG A CB    1 
ATOM   8807  C  CG    . ARG A 1 2576 ? 236.807 253.272 230.226 1.00 4.68  ? 2576 ARG A CG    1 
ATOM   8808  C  CD    . ARG A 1 2576 ? 236.701 254.766 229.972 1.00 4.48  ? 2576 ARG A CD    1 
ATOM   8809  N  NE    . ARG A 1 2576 ? 236.157 255.085 228.659 1.00 4.68  ? 2576 ARG A NE    1 
ATOM   8810  C  CZ    . ARG A 1 2576 ? 236.222 256.286 228.102 1.00 10.79 ? 2576 ARG A CZ    1 
ATOM   8811  N  NH1   . ARG A 1 2576 ? 236.802 257.304 228.718 1.00 8.04  ? 2576 ARG A NH1   1 
ATOM   8812  N  NH2   . ARG A 1 2576 ? 235.695 256.471 226.896 1.00 8.95  ? 2576 ARG A NH2   1 
ATOM   8813  N  N     . HIS A 1 2577 ? 233.906 250.183 228.618 1.00 2.04  ? 2577 HIS A N     1 
ATOM   8814  C  CA    . HIS A 1 2577 ? 232.616 249.591 228.285 1.00 1.48  ? 2577 HIS A CA    1 
ATOM   8815  C  C     . HIS A 1 2577 ? 232.517 248.160 228.795 1.00 1.57  ? 2577 HIS A C     1 
ATOM   8816  O  O     . HIS A 1 2577 ? 231.453 247.735 229.256 1.00 3.53  ? 2577 HIS A O     1 
ATOM   8817  C  CB    . HIS A 1 2577 ? 232.391 249.647 226.775 1.00 1.85  ? 2577 HIS A CB    1 
ATOM   8818  C  CG    . HIS A 1 2577 ? 232.121 251.023 226.254 1.00 1.79  ? 2577 HIS A CG    1 
ATOM   8819  N  ND1   . HIS A 1 2577 ? 232.178 251.337 224.913 1.00 3.79  ? 2577 HIS A ND1   1 
ATOM   8820  C  CD2   . HIS A 1 2577 ? 231.799 252.172 226.895 1.00 1.58  ? 2577 HIS A CD2   1 
ATOM   8821  C  CE1   . HIS A 1 2577 ? 231.895 252.617 224.750 1.00 1.89  ? 2577 HIS A CE1   1 
ATOM   8822  N  NE2   . HIS A 1 2577 ? 231.664 253.147 225.937 1.00 1.36  ? 2577 HIS A NE2   1 
ATOM   8823  N  N     . GLU A 1 2578 ? 233.613 247.403 228.714 1.00 1.53  ? 2578 GLU A N     1 
ATOM   8824  C  CA    . GLU A 1 2578 ? 233.603 246.024 229.197 1.00 1.58  ? 2578 GLU A CA    1 
ATOM   8825  C  C     . GLU A 1 2578 ? 233.371 245.971 230.701 1.00 1.94  ? 2578 GLU A C     1 
ATOM   8826  O  O     . GLU A 1 2578 ? 232.614 245.124 231.190 1.00 2.60  ? 2578 GLU A O     1 
ATOM   8827  C  CB    . GLU A 1 2578 ? 234.915 245.332 228.817 1.00 4.12  ? 2578 GLU A CB    1 
ATOM   8828  C  CG    . GLU A 1 2578 ? 234.952 243.828 229.051 1.00 7.63  ? 2578 GLU A CG    1 
ATOM   8829  C  CD    . GLU A 1 2578 ? 235.302 243.453 230.480 1.00 18.21 ? 2578 GLU A CD    1 
ATOM   8830  O  OE1   . GLU A 1 2578 ? 236.021 244.228 231.143 1.00 20.09 ? 2578 GLU A OE1   1 
ATOM   8831  O  OE2   . GLU A 1 2578 ? 234.856 242.379 230.941 1.00 18.08 ? 2578 GLU A OE2   1 
ATOM   8832  N  N     . ALA A 1 2579 ? 234.015 246.867 231.451 1.00 2.47  ? 2579 ALA A N     1 
ATOM   8833  C  CA    . ALA A 1 2579 ? 233.808 246.913 232.895 1.00 1.03  ? 2579 ALA A CA    1 
ATOM   8834  C  C     . ALA A 1 2579 ? 232.373 247.292 233.239 1.00 1.12  ? 2579 ALA A C     1 
ATOM   8835  O  O     . ALA A 1 2579 ? 231.772 246.708 234.146 1.00 1.33  ? 2579 ALA A O     1 
ATOM   8836  C  CB    . ALA A 1 2579 ? 234.789 247.893 233.533 1.00 0.76  ? 2579 ALA A CB    1 
ATOM   8837  N  N     . LEU A 1 2580 ? 231.812 248.275 232.529 1.00 1.05  ? 2580 LEU A N     1 
ATOM   8838  C  CA    . LEU A 1 2580 ? 230.425 248.661 232.766 1.00 0.76  ? 2580 LEU A CA    1 
ATOM   8839  C  C     . LEU A 1 2580 ? 229.468 247.535 232.400 1.00 0.92  ? 2580 LEU A C     1 
ATOM   8840  O  O     . LEU A 1 2580 ? 228.502 247.270 233.125 1.00 1.08  ? 2580 LEU A O     1 
ATOM   8841  C  CB    . LEU A 1 2580 ? 230.090 249.927 231.978 1.00 0.63  ? 2580 LEU A CB    1 
ATOM   8842  C  CG    . LEU A 1 2580 ? 228.675 250.474 232.171 1.00 1.24  ? 2580 LEU A CG    1 
ATOM   8843  C  CD1   . LEU A 1 2580 ? 228.497 251.006 233.585 1.00 1.38  ? 2580 LEU A CD1   1 
ATOM   8844  C  CD2   . LEU A 1 2580 ? 228.363 251.546 231.147 1.00 1.16  ? 2580 LEU A CD2   1 
ATOM   8845  N  N     . LEU A 1 2581 ? 229.716 246.864 231.274 1.00 1.40  ? 2581 LEU A N     1 
ATOM   8846  C  CA    . LEU A 1 2581 ? 228.886 245.727 230.890 1.00 1.07  ? 2581 LEU A CA    1 
ATOM   8847  C  C     . LEU A 1 2581 ? 228.996 244.602 231.907 1.00 1.11  ? 2581 LEU A C     1 
ATOM   8848  O  O     . LEU A 1 2581 ? 228.008 243.921 232.200 1.00 1.61  ? 2581 LEU A O     1 
ATOM   8849  C  CB    . LEU A 1 2581 ? 229.283 245.230 229.502 1.00 1.10  ? 2581 LEU A CB    1 
ATOM   8850  C  CG    . LEU A 1 2581 ? 228.771 246.027 228.306 1.00 1.35  ? 2581 LEU A CG    1 
ATOM   8851  C  CD1   . LEU A 1 2581 ? 229.027 245.262 227.026 1.00 0.66  ? 2581 LEU A CD1   1 
ATOM   8852  C  CD2   . LEU A 1 2581 ? 227.294 246.332 228.461 1.00 0.83  ? 2581 LEU A CD2   1 
ATOM   8853  N  N     . TYR A 1 2582 ? 230.195 244.392 232.455 1.00 0.87  ? 2582 TYR A N     1 
ATOM   8854  C  CA    . TYR A 1 2582 ? 230.388 243.355 233.461 1.00 1.56  ? 2582 TYR A CA    1 
ATOM   8855  C  C     . TYR A 1 2582 ? 229.493 243.586 234.671 1.00 3.50  ? 2582 TYR A C     1 
ATOM   8856  O  O     . TYR A 1 2582 ? 228.873 242.647 235.179 1.00 8.97  ? 2582 TYR A O     1 
ATOM   8857  C  CB    . TYR A 1 2582 ? 231.858 243.313 233.882 1.00 2.28  ? 2582 TYR A CB    1 
ATOM   8858  C  CG    . TYR A 1 2582 ? 232.235 242.138 234.749 1.00 5.11  ? 2582 TYR A CG    1 
ATOM   8859  C  CD1   . TYR A 1 2582 ? 232.012 242.157 236.121 1.00 6.00  ? 2582 TYR A CD1   1 
ATOM   8860  C  CD2   . TYR A 1 2582 ? 232.831 241.012 234.199 1.00 11.03 ? 2582 TYR A CD2   1 
ATOM   8861  C  CE1   . TYR A 1 2582 ? 232.362 241.086 236.914 1.00 6.08  ? 2582 TYR A CE1   1 
ATOM   8862  C  CE2   . TYR A 1 2582 ? 233.189 239.939 234.984 1.00 6.87  ? 2582 TYR A CE2   1 
ATOM   8863  C  CZ    . TYR A 1 2582 ? 232.950 239.980 236.341 1.00 11.74 ? 2582 TYR A CZ    1 
ATOM   8864  O  OH    . TYR A 1 2582 ? 233.304 238.907 237.128 1.00 25.69 ? 2582 TYR A OH    1 
ATOM   8865  N  N     . THR A 1 2583 ? 229.409 244.831 235.139 1.00 2.57  ? 2583 THR A N     1 
ATOM   8866  C  CA    . THR A 1 2583 ? 228.612 245.133 236.323 1.00 1.99  ? 2583 THR A CA    1 
ATOM   8867  C  C     . THR A 1 2583 ? 227.138 244.823 236.090 1.00 2.45  ? 2583 THR A C     1 
ATOM   8868  O  O     . THR A 1 2583 ? 226.505 244.124 236.888 1.00 8.27  ? 2583 THR A O     1 
ATOM   8869  C  CB    . THR A 1 2583 ? 228.805 246.597 236.717 1.00 3.78  ? 2583 THR A CB    1 
ATOM   8870  O  OG1   . THR A 1 2583 ? 230.101 246.769 237.302 1.00 3.93  ? 2583 THR A OG1   1 
ATOM   8871  C  CG2   . THR A 1 2583 ? 227.740 247.035 237.709 1.00 3.40  ? 2583 THR A CG2   1 
ATOM   8872  N  N     . TRP A 1 2584 ? 226.576 245.333 234.991 1.00 1.25  ? 2584 TRP A N     1 
ATOM   8873  C  CA    . TRP A 1 2584 ? 225.166 245.093 234.705 1.00 1.01  ? 2584 TRP A CA    1 
ATOM   8874  C  C     . TRP A 1 2584 ? 224.893 243.615 234.446 1.00 1.91  ? 2584 TRP A C     1 
ATOM   8875  O  O     . TRP A 1 2584 ? 223.892 243.071 234.924 1.00 1.99  ? 2584 TRP A O     1 
ATOM   8876  C  CB    . TRP A 1 2584 ? 224.724 245.939 233.512 1.00 0.77  ? 2584 TRP A CB    1 
ATOM   8877  C  CG    . TRP A 1 2584 ? 224.808 247.420 233.733 1.00 1.23  ? 2584 TRP A CG    1 
ATOM   8878  C  CD1   . TRP A 1 2584 ? 224.881 248.069 234.930 1.00 1.49  ? 2584 TRP A CD1   1 
ATOM   8879  C  CD2   . TRP A 1 2584 ? 224.825 248.435 232.725 1.00 0.92  ? 2584 TRP A CD2   1 
ATOM   8880  N  NE1   . TRP A 1 2584 ? 224.945 249.425 234.729 1.00 0.67  ? 2584 TRP A NE1   1 
ATOM   8881  C  CE2   . TRP A 1 2584 ? 224.911 249.676 233.384 1.00 0.90  ? 2584 TRP A CE2   1 
ATOM   8882  C  CE3   . TRP A 1 2584 ? 224.774 248.415 231.327 1.00 0.61  ? 2584 TRP A CE3   1 
ATOM   8883  C  CZ2   . TRP A 1 2584 ? 224.946 250.887 232.694 1.00 2.45  ? 2584 TRP A CZ2   1 
ATOM   8884  C  CZ3   . TRP A 1 2584 ? 224.809 249.618 230.644 1.00 0.66  ? 2584 TRP A CZ3   1 
ATOM   8885  C  CH2   . TRP A 1 2584 ? 224.893 250.836 231.330 1.00 0.78  ? 2584 TRP A CH2   1 
ATOM   8886  N  N     . LEU A 1 2585 ? 225.770 242.951 233.688 1.00 2.34  ? 2585 LEU A N     1 
ATOM   8887  C  CA    . LEU A 1 2585 ? 225.556 241.544 233.364 1.00 1.28  ? 2585 LEU A CA    1 
ATOM   8888  C  C     . LEU A 1 2585 ? 225.660 240.661 234.601 1.00 3.65  ? 2585 LEU A C     1 
ATOM   8889  O  O     . LEU A 1 2585 ? 224.871 239.725 234.766 1.00 2.85  ? 2585 LEU A O     1 
ATOM   8890  C  CB    . LEU A 1 2585 ? 226.559 241.092 232.304 1.00 0.96  ? 2585 LEU A CB    1 
ATOM   8891  C  CG    . LEU A 1 2585 ? 226.272 241.512 230.863 1.00 0.65  ? 2585 LEU A CG    1 
ATOM   8892  C  CD1   . LEU A 1 2585 ? 227.556 241.517 230.054 1.00 0.73  ? 2585 LEU A CD1   1 
ATOM   8893  C  CD2   . LEU A 1 2585 ? 225.248 240.588 230.243 1.00 0.38  ? 2585 LEU A CD2   1 
ATOM   8894  N  N     . ALA A 1 2586 ? 226.629 240.941 235.478 1.00 3.68  ? 2586 ALA A N     1 
ATOM   8895  C  CA    . ALA A 1 2586 ? 226.811 240.118 236.669 1.00 2.70  ? 2586 ALA A CA    1 
ATOM   8896  C  C     . ALA A 1 2586 ? 225.617 240.218 237.607 1.00 2.87  ? 2586 ALA A C     1 
ATOM   8897  O  O     . ALA A 1 2586 ? 225.361 239.294 238.387 1.00 3.64  ? 2586 ALA A O     1 
ATOM   8898  C  CB    . ALA A 1 2586 ? 228.096 240.515 237.395 1.00 2.94  ? 2586 ALA A CB    1 
ATOM   8899  N  N     . GLU A 1 2587 ? 224.881 241.321 237.548 1.00 3.69  ? 2587 GLU A N     1 
ATOM   8900  C  CA    . GLU A 1 2587 ? 223.677 241.500 238.343 1.00 3.49  ? 2587 GLU A CA    1 
ATOM   8901  C  C     . GLU A 1 2587 ? 222.424 241.011 237.631 1.00 2.37  ? 2587 GLU A C     1 
ATOM   8902  O  O     . GLU A 1 2587 ? 221.325 241.161 238.174 1.00 6.64  ? 2587 GLU A O     1 
ATOM   8903  C  CB    . GLU A 1 2587 ? 223.514 242.977 238.723 1.00 4.01  ? 2587 GLU A CB    1 
ATOM   8904  C  CG    . GLU A 1 2587 ? 224.634 243.560 239.592 1.00 6.49  ? 2587 GLU A CG    1 
ATOM   8905  C  CD    . GLU A 1 2587 ? 224.739 242.951 240.989 1.00 16.40 ? 2587 GLU A CD    1 
ATOM   8906  O  OE1   . GLU A 1 2587 ? 224.120 241.903 241.263 1.00 14.39 ? 2587 GLU A OE1   1 
ATOM   8907  O  OE2   . GLU A 1 2587 ? 225.462 243.533 241.825 1.00 16.33 ? 2587 GLU A OE2   1 
ATOM   8908  N  N     . HIS A 1 2588 ? 222.565 240.442 236.433 1.00 1.12  ? 2588 HIS A N     1 
ATOM   8909  C  CA    . HIS A 1 2588 ? 221.453 239.960 235.614 1.00 0.87  ? 2588 HIS A CA    1 
ATOM   8910  C  C     . HIS A 1 2588 ? 220.493 241.082 235.232 1.00 0.86  ? 2588 HIS A C     1 
ATOM   8911  O  O     . HIS A 1 2588 ? 219.323 240.833 234.937 1.00 1.54  ? 2588 HIS A O     1 
ATOM   8912  C  CB    . HIS A 1 2588 ? 220.704 238.823 236.316 1.00 0.39  ? 2588 HIS A CB    1 
ATOM   8913  C  CG    . HIS A 1 2588 ? 221.609 237.768 236.867 1.00 0.51  ? 2588 HIS A CG    1 
ATOM   8914  N  ND1   . HIS A 1 2588 ? 222.583 237.154 236.111 1.00 1.05  ? 2588 HIS A ND1   1 
ATOM   8915  C  CD2   . HIS A 1 2588 ? 221.711 237.240 238.110 1.00 0.30  ? 2588 HIS A CD2   1 
ATOM   8916  C  CE1   . HIS A 1 2588 ? 223.235 236.282 236.857 1.00 0.47  ? 2588 HIS A CE1   1 
ATOM   8917  N  NE2   . HIS A 1 2588 ? 222.725 236.315 238.074 1.00 0.42  ? 2588 HIS A NE2   1 
ATOM   8918  N  N     . LYS A 1 2589 ? 220.984 242.311 235.235 1.00 1.35  ? 2589 LYS A N     1 
ATOM   8919  C  CA    . LYS A 1 2589 ? 220.197 243.477 234.861 1.00 1.15  ? 2589 LYS A CA    1 
ATOM   8920  C  C     . LYS A 1 2589 ? 220.110 243.575 233.342 1.00 0.47  ? 2589 LYS A C     1 
ATOM   8921  O  O     . LYS A 1 2589 ? 221.145 243.566 232.668 1.00 1.05  ? 2589 LYS A O     1 
ATOM   8922  C  CB    . LYS A 1 2589 ? 220.832 244.742 235.438 1.00 1.62  ? 2589 LYS A CB    1 
ATOM   8923  C  CG    . LYS A 1 2589 ? 220.085 246.033 235.149 1.00 2.18  ? 2589 LYS A CG    1 
ATOM   8924  C  CD    . LYS A 1 2589 ? 219.021 246.304 236.201 1.00 4.10  ? 2589 LYS A CD    1 
ATOM   8925  C  CE    . LYS A 1 2589 ? 218.568 247.756 236.168 1.00 3.16  ? 2589 LYS A CE    1 
ATOM   8926  N  NZ    . LYS A 1 2589 ? 217.473 248.020 237.138 1.00 5.47  ? 2589 LYS A NZ    1 
ATOM   8927  N  N     . PRO A 1 2590 ? 218.909 243.649 232.770 1.00 0.34  ? 2590 PRO A N     1 
ATOM   8928  C  CA    . PRO A 1 2590 ? 218.801 243.836 231.319 1.00 0.19  ? 2590 PRO A CA    1 
ATOM   8929  C  C     . PRO A 1 2590 ? 219.440 245.149 230.890 1.00 0.20  ? 2590 PRO A C     1 
ATOM   8930  O  O     . PRO A 1 2590 ? 219.344 246.161 231.584 1.00 0.50  ? 2590 PRO A O     1 
ATOM   8931  C  CB    . PRO A 1 2590 ? 217.289 243.836 231.072 1.00 0.12  ? 2590 PRO A CB    1 
ATOM   8932  C  CG    . PRO A 1 2590 ? 216.697 244.221 232.381 1.00 0.17  ? 2590 PRO A CG    1 
ATOM   8933  C  CD    . PRO A 1 2590 ? 217.592 243.624 233.421 1.00 0.22  ? 2590 PRO A CD    1 
ATOM   8934  N  N     . LEU A 1 2591 ? 220.096 245.127 229.734 1.00 0.16  ? 2591 LEU A N     1 
ATOM   8935  C  CA    . LEU A 1 2591 ? 220.819 246.300 229.269 1.00 0.08  ? 2591 LEU A CA    1 
ATOM   8936  C  C     . LEU A 1 2591 ? 220.689 246.393 227.757 1.00 0.07  ? 2591 LEU A C     1 
ATOM   8937  O  O     . LEU A 1 2591 ? 220.396 245.406 227.077 1.00 0.03  ? 2591 LEU A O     1 
ATOM   8938  C  CB    . LEU A 1 2591 ? 222.292 246.253 229.704 1.00 0.22  ? 2591 LEU A CB    1 
ATOM   8939  C  CG    . LEU A 1 2591 ? 223.193 245.123 229.194 1.00 0.08  ? 2591 LEU A CG    1 
ATOM   8940  C  CD1   . LEU A 1 2591 ? 223.790 245.458 227.827 1.00 0.06  ? 2591 LEU A CD1   1 
ATOM   8941  C  CD2   . LEU A 1 2591 ? 224.280 244.767 230.193 1.00 0.31  ? 2591 LEU A CD2   1 
ATOM   8942  N  N     . VAL A 1 2592 ? 220.904 247.596 227.237 1.00 0.05  ? 2592 VAL A N     1 
ATOM   8943  C  CA    . VAL A 1 2592 ? 220.905 247.846 225.804 1.00 0.03  ? 2592 VAL A CA    1 
ATOM   8944  C  C     . VAL A 1 2592 ? 222.171 248.606 225.441 1.00 0.03  ? 2592 VAL A C     1 
ATOM   8945  O  O     . VAL A 1 2592 ? 222.490 249.624 226.063 1.00 0.04  ? 2592 VAL A O     1 
ATOM   8946  C  CB    . VAL A 1 2592 ? 219.650 248.623 225.353 1.00 0.04  ? 2592 VAL A CB    1 
ATOM   8947  C  CG1   . VAL A 1 2592 ? 219.895 249.321 224.030 1.00 0.06  ? 2592 VAL A CG1   1 
ATOM   8948  C  CG2   . VAL A 1 2592 ? 218.473 247.679 225.223 1.00 0.02  ? 2592 VAL A CG2   1 
ATOM   8949  N  N     . LEU A 1 2593 ? 222.894 248.102 224.447 1.00 0.04  ? 2593 LEU A N     1 
ATOM   8950  C  CA    . LEU A 1 2593 ? 223.992 248.827 223.824 1.00 0.04  ? 2593 LEU A CA    1 
ATOM   8951  C  C     . LEU A 1 2593 ? 223.458 249.547 222.595 1.00 0.04  ? 2593 LEU A C     1 
ATOM   8952  O  O     . LEU A 1 2593 ? 222.840 248.925 221.727 1.00 0.09  ? 2593 LEU A O     1 
ATOM   8953  C  CB    . LEU A 1 2593 ? 225.132 247.886 223.432 1.00 0.05  ? 2593 LEU A CB    1 
ATOM   8954  C  CG    . LEU A 1 2593 ? 225.745 246.995 224.511 1.00 0.07  ? 2593 LEU A CG    1 
ATOM   8955  C  CD1   . LEU A 1 2593 ? 225.176 245.593 224.427 1.00 0.07  ? 2593 LEU A CD1   1 
ATOM   8956  C  CD2   . LEU A 1 2593 ? 227.255 246.966 224.379 1.00 0.21  ? 2593 LEU A CD2   1 
ATOM   8957  N  N     . CYS A 1 2594 ? 223.684 250.853 222.528 1.00 0.07  ? 2594 CYS A N     1 
ATOM   8958  C  CA    . CYS A 1 2594 ? 223.219 251.665 221.415 1.00 0.13  ? 2594 CYS A CA    1 
ATOM   8959  C  C     . CYS A 1 2594 ? 224.408 252.334 220.742 1.00 0.14  ? 2594 CYS A C     1 
ATOM   8960  O  O     . CYS A 1 2594 ? 225.315 252.833 221.415 1.00 0.31  ? 2594 CYS A O     1 
ATOM   8961  C  CB    . CYS A 1 2594 ? 222.211 252.721 221.874 1.00 0.16  ? 2594 CYS A CB    1 
ATOM   8962  S  SG    . CYS A 1 2594 ? 221.360 253.564 220.526 1.00 0.80  ? 2594 CYS A SG    1 
ATOM   8963  N  N     . GLY A 1 2595 ? 224.399 252.336 219.414 1.00 0.15  ? 2595 GLY A N     1 
ATOM   8964  C  CA    . GLY A 1 2595 ? 225.457 252.945 218.651 1.00 0.09  ? 2595 GLY A CA    1 
ATOM   8965  C  C     . GLY A 1 2595 ? 225.289 252.735 217.164 1.00 0.10  ? 2595 GLY A C     1 
ATOM   8966  O  O     . GLY A 1 2595 ? 224.421 251.983 216.713 1.00 0.37  ? 2595 GLY A O     1 
ATOM   8967  N  N     . PRO A 1 2596 ? 226.121 253.406 216.368 1.00 0.47  ? 2596 PRO A N     1 
ATOM   8968  C  CA    . PRO A 1 2596 ? 226.037 253.236 214.921 1.00 0.17  ? 2596 PRO A CA    1 
ATOM   8969  C  C     . PRO A 1 2596 ? 226.417 251.822 214.526 1.00 0.16  ? 2596 PRO A C     1 
ATOM   8970  O  O     . PRO A 1 2596 ? 227.222 251.165 215.209 1.00 0.16  ? 2596 PRO A O     1 
ATOM   8971  C  CB    . PRO A 1 2596 ? 227.052 254.263 214.383 1.00 0.22  ? 2596 PRO A CB    1 
ATOM   8972  C  CG    . PRO A 1 2596 ? 227.333 255.175 215.523 1.00 0.41  ? 2596 PRO A CG    1 
ATOM   8973  C  CD    . PRO A 1 2596 ? 227.186 254.346 216.747 1.00 0.60  ? 2596 PRO A CD    1 
ATOM   8974  N  N     . PRO A 1 2597 ? 225.861 251.306 213.428 1.00 0.18  ? 2597 PRO A N     1 
ATOM   8975  C  CA    . PRO A 1 2597 ? 226.156 249.922 213.022 1.00 0.23  ? 2597 PRO A CA    1 
ATOM   8976  C  C     . PRO A 1 2597 ? 227.641 249.714 212.779 1.00 0.28  ? 2597 PRO A C     1 
ATOM   8977  O  O     . PRO A 1 2597 ? 228.259 250.406 211.966 1.00 1.62  ? 2597 PRO A O     1 
ATOM   8978  C  CB    . PRO A 1 2597 ? 225.337 249.749 211.737 1.00 0.16  ? 2597 PRO A CB    1 
ATOM   8979  C  CG    . PRO A 1 2597 ? 225.003 251.141 211.293 1.00 0.15  ? 2597 PRO A CG    1 
ATOM   8980  C  CD    . PRO A 1 2597 ? 224.891 251.951 212.532 1.00 0.22  ? 2597 PRO A CD    1 
ATOM   8981  N  N     . GLY A 1 2598 ? 228.215 248.753 213.495 1.00 0.14  ? 2598 GLY A N     1 
ATOM   8982  C  CA    . GLY A 1 2598 ? 229.628 248.466 213.411 1.00 0.19  ? 2598 GLY A CA    1 
ATOM   8983  C  C     . GLY A 1 2598 ? 230.500 249.160 214.431 1.00 0.18  ? 2598 GLY A C     1 
ATOM   8984  O  O     . GLY A 1 2598 ? 231.726 249.152 214.277 1.00 0.20  ? 2598 GLY A O     1 
ATOM   8985  N  N     . SER A 1 2599 ? 229.916 249.755 215.471 1.00 0.18  ? 2599 SER A N     1 
ATOM   8986  C  CA    . SER A 1 2599 ? 230.693 250.502 216.452 1.00 0.34  ? 2599 SER A CA    1 
ATOM   8987  C  C     . SER A 1 2599 ? 231.328 249.616 217.514 1.00 0.28  ? 2599 SER A C     1 
ATOM   8988  O  O     . SER A 1 2599 ? 232.110 250.119 218.327 1.00 0.30  ? 2599 SER A O     1 
ATOM   8989  C  CB    . SER A 1 2599 ? 229.817 251.561 217.128 1.00 0.20  ? 2599 SER A CB    1 
ATOM   8990  O  OG    . SER A 1 2599 ? 228.732 250.971 217.822 1.00 0.16  ? 2599 SER A OG    1 
ATOM   8991  N  N     . GLY A 1 2600 ? 231.025 248.327 217.525 1.00 0.13  ? 2600 GLY A N     1 
ATOM   8992  C  CA    . GLY A 1 2600 ? 231.597 247.407 218.473 1.00 0.17  ? 2600 GLY A CA    1 
ATOM   8993  C  C     . GLY A 1 2600 ? 230.676 246.927 219.576 1.00 0.27  ? 2600 GLY A C     1 
ATOM   8994  O  O     . GLY A 1 2600 ? 231.174 246.492 220.618 1.00 1.66  ? 2600 GLY A O     1 
ATOM   8995  N  N     . LYS A 1 2601 ? 229.358 246.995 219.382 1.00 0.22  ? 2601 LYS A N     1 
ATOM   8996  C  CA    . LYS A 1 2601 ? 228.429 246.593 220.433 1.00 0.21  ? 2601 LYS A CA    1 
ATOM   8997  C  C     . LYS A 1 2601 ? 228.471 245.088 220.665 1.00 0.70  ? 2601 LYS A C     1 
ATOM   8998  O  O     . LYS A 1 2601 ? 228.573 244.631 221.809 1.00 0.71  ? 2601 LYS A O     1 
ATOM   8999  C  CB    . LYS A 1 2601 ? 227.016 247.052 220.077 1.00 0.14  ? 2601 LYS A CB    1 
ATOM   9000  C  CG    . LYS A 1 2601 ? 226.873 248.565 219.998 1.00 0.10  ? 2601 LYS A CG    1 
ATOM   9001  C  CD    . LYS A 1 2601 ? 225.473 248.978 219.589 1.00 0.06  ? 2601 LYS A CD    1 
ATOM   9002  C  CE    . LYS A 1 2601 ? 225.125 248.463 218.205 1.00 0.08  ? 2601 LYS A CE    1 
ATOM   9003  N  NZ    . LYS A 1 2601 ? 226.015 249.024 217.154 1.00 0.05  ? 2601 LYS A NZ    1 
ATOM   9004  N  N     . THR A 1 2602 ? 228.393 244.299 219.591 1.00 1.18  ? 2602 THR A N     1 
ATOM   9005  C  CA    . THR A 1 2602 ? 228.514 242.852 219.734 1.00 0.99  ? 2602 THR A CA    1 
ATOM   9006  C  C     . THR A 1 2602 ? 229.902 242.469 220.227 1.00 1.06  ? 2602 THR A C     1 
ATOM   9007  O  O     . THR A 1 2602 ? 230.047 241.558 221.049 1.00 1.26  ? 2602 THR A O     1 
ATOM   9008  C  CB    . THR A 1 2602 ? 228.208 242.159 218.405 1.00 1.24  ? 2602 THR A CB    1 
ATOM   9009  O  OG1   . THR A 1 2602 ? 226.972 242.652 217.878 1.00 9.14  ? 2602 THR A OG1   1 
ATOM   9010  C  CG2   . THR A 1 2602 ? 228.110 240.657 218.599 1.00 0.98  ? 2602 THR A CG2   1 
ATOM   9011  N  N     . MET A 1 2603 ? 230.932 243.156 219.733 1.00 0.58  ? 2603 MET A N     1 
ATOM   9012  C  CA    . MET A 1 2603 ? 232.298 242.865 220.151 1.00 0.47  ? 2603 MET A CA    1 
ATOM   9013  C  C     . MET A 1 2603 ? 232.488 243.124 221.640 1.00 0.81  ? 2603 MET A C     1 
ATOM   9014  O  O     . MET A 1 2603 ? 233.091 242.313 222.350 1.00 0.94  ? 2603 MET A O     1 
ATOM   9015  C  CB    . MET A 1 2603 ? 233.275 243.703 219.326 1.00 0.40  ? 2603 MET A CB    1 
ATOM   9016  C  CG    . MET A 1 2603 ? 234.726 243.394 219.587 1.00 0.40  ? 2603 MET A CG    1 
ATOM   9017  S  SD    . MET A 1 2603 ? 235.819 244.760 219.169 1.00 0.22  ? 2603 MET A SD    1 
ATOM   9018  C  CE    . MET A 1 2603 ? 235.254 246.021 220.305 1.00 0.30  ? 2603 MET A CE    1 
ATOM   9019  N  N     . THR A 1 2604 ? 231.972 244.252 222.133 1.00 0.55  ? 2604 THR A N     1 
ATOM   9020  C  CA    . THR A 1 2604 ? 232.119 244.570 223.549 1.00 0.80  ? 2604 THR A CA    1 
ATOM   9021  C  C     . THR A 1 2604 ? 231.316 243.610 224.421 1.00 0.80  ? 2604 THR A C     1 
ATOM   9022  O  O     . THR A 1 2604 ? 231.804 243.156 225.461 1.00 1.29  ? 2604 THR A O     1 
ATOM   9023  C  CB    . THR A 1 2604 ? 231.697 246.015 223.810 1.00 1.22  ? 2604 THR A CB    1 
ATOM   9024  O  OG1   . THR A 1 2604 ? 232.402 246.886 222.918 1.00 2.05  ? 2604 THR A OG1   1 
ATOM   9025  C  CG2   . THR A 1 2604 ? 232.013 246.407 225.239 1.00 0.86  ? 2604 THR A CG2   1 
ATOM   9026  N  N     . LEU A 1 2605 ? 230.087 243.290 224.013 1.00 0.67  ? 2605 LEU A N     1 
ATOM   9027  C  CA    . LEU A 1 2605 ? 229.251 242.394 224.805 1.00 0.61  ? 2605 LEU A CA    1 
ATOM   9028  C  C     . LEU A 1 2605 ? 229.872 241.006 224.911 1.00 0.97  ? 2605 LEU A C     1 
ATOM   9029  O  O     . LEU A 1 2605 ? 229.933 240.423 225.997 1.00 1.53  ? 2605 LEU A O     1 
ATOM   9030  C  CB    . LEU A 1 2605 ? 227.851 242.307 224.202 1.00 1.80  ? 2605 LEU A CB    1 
ATOM   9031  C  CG    . LEU A 1 2605 ? 226.978 241.193 224.785 1.00 1.06  ? 2605 LEU A CG    1 
ATOM   9032  C  CD1   . LEU A 1 2605 ? 226.611 241.487 226.231 1.00 0.37  ? 2605 LEU A CD1   1 
ATOM   9033  C  CD2   . LEU A 1 2605 ? 225.743 240.985 223.939 1.00 0.62  ? 2605 LEU A CD2   1 
ATOM   9034  N  N     . PHE A 1 2606 ? 230.344 240.465 223.788 1.00 1.19  ? 2606 PHE A N     1 
ATOM   9035  C  CA    . PHE A 1 2606 ? 230.947 239.135 223.812 1.00 1.25  ? 2606 PHE A CA    1 
ATOM   9036  C  C     . PHE A 1 2606 ? 232.293 239.143 224.522 1.00 1.50  ? 2606 PHE A C     1 
ATOM   9037  O  O     . PHE A 1 2606 ? 232.672 238.139 225.134 1.00 3.15  ? 2606 PHE A O     1 
ATOM   9038  C  CB    . PHE A 1 2606 ? 231.092 238.584 222.391 1.00 1.17  ? 2606 PHE A CB    1 
ATOM   9039  C  CG    . PHE A 1 2606 ? 229.783 238.230 221.727 1.00 1.70  ? 2606 PHE A CG    1 
ATOM   9040  C  CD1   . PHE A 1 2606 ? 228.570 238.576 222.301 1.00 2.01  ? 2606 PHE A CD1   1 
ATOM   9041  C  CD2   . PHE A 1 2606 ? 229.771 237.552 220.523 1.00 3.23  ? 2606 PHE A CD2   1 
ATOM   9042  C  CE1   . PHE A 1 2606 ? 227.375 238.252 221.687 1.00 1.54  ? 2606 PHE A CE1   1 
ATOM   9043  C  CE2   . PHE A 1 2606 ? 228.579 237.224 219.905 1.00 6.42  ? 2606 PHE A CE2   1 
ATOM   9044  C  CZ    . PHE A 1 2606 ? 227.381 237.574 220.489 1.00 1.84  ? 2606 PHE A CZ    1 
ATOM   9045  N  N     . SER A 1 2607 ? 233.027 240.254 224.451 1.00 1.84  ? 2607 SER A N     1 
ATOM   9046  C  CA    . SER A 1 2607 ? 234.268 240.365 225.208 1.00 1.68  ? 2607 SER A CA    1 
ATOM   9047  C  C     . SER A 1 2607 ? 234.002 240.349 226.707 1.00 3.41  ? 2607 SER A C     1 
ATOM   9048  O  O     . SER A 1 2607 ? 234.737 239.710 227.467 1.00 9.76  ? 2607 SER A O     1 
ATOM   9049  C  CB    . SER A 1 2607 ? 235.014 241.636 224.804 1.00 1.98  ? 2607 SER A CB    1 
ATOM   9050  O  OG    . SER A 1 2607 ? 236.211 241.789 225.543 1.00 12.41 ? 2607 SER A OG    1 
ATOM   9051  N  N     . ALA A 1 2608 ? 232.952 241.042 227.151 1.00 2.52  ? 2608 ALA A N     1 
ATOM   9052  C  CA    . ALA A 1 2608 ? 232.609 241.050 228.567 1.00 2.18  ? 2608 ALA A CA    1 
ATOM   9053  C  C     . ALA A 1 2608 ? 232.079 239.698 229.028 1.00 2.65  ? 2608 ALA A C     1 
ATOM   9054  O  O     . ALA A 1 2608 ? 232.300 239.309 230.179 1.00 3.18  ? 2608 ALA A O     1 
ATOM   9055  C  CB    . ALA A 1 2608 ? 231.585 242.149 228.852 1.00 1.71  ? 2608 ALA A CB    1 
ATOM   9056  N  N     . LEU A 1 2609 ? 231.382 238.974 228.150 1.00 2.31  ? 2609 LEU A N     1 
ATOM   9057  C  CA    . LEU A 1 2609 ? 230.849 237.669 228.524 1.00 3.35  ? 2609 LEU A CA    1 
ATOM   9058  C  C     . LEU A 1 2609 ? 231.954 236.642 228.731 1.00 6.28  ? 2609 LEU A C     1 
ATOM   9059  O  O     . LEU A 1 2609 ? 231.765 235.677 229.480 1.00 5.71  ? 2609 LEU A O     1 
ATOM   9060  C  CB    . LEU A 1 2609 ? 229.864 237.184 227.462 1.00 2.45  ? 2609 LEU A CB    1 
ATOM   9061  C  CG    . LEU A 1 2609 ? 228.514 237.898 227.443 1.00 1.52  ? 2609 LEU A CG    1 
ATOM   9062  C  CD1   . LEU A 1 2609 ? 227.718 237.503 226.216 1.00 1.03  ? 2609 LEU A CD1   1 
ATOM   9063  C  CD2   . LEU A 1 2609 ? 227.739 237.594 228.711 1.00 1.90  ? 2609 LEU A CD2   1 
ATOM   9064  N  N     . ARG A 1 2610 ? 233.102 236.820 228.074 1.00 8.09  ? 2610 ARG A N     1 
ATOM   9065  C  CA    . ARG A 1 2610 ? 234.210 235.885 228.255 1.00 5.48  ? 2610 ARG A CA    1 
ATOM   9066  C  C     . ARG A 1 2610 ? 234.753 235.942 229.676 1.00 9.36  ? 2610 ARG A C     1 
ATOM   9067  O  O     . ARG A 1 2610 ? 235.142 234.912 230.238 1.00 17.13 ? 2610 ARG A O     1 
ATOM   9068  C  CB    . ARG A 1 2610 ? 235.313 236.174 227.237 1.00 7.83  ? 2610 ARG A CB    1 
ATOM   9069  C  CG    . ARG A 1 2610 ? 234.872 235.946 225.803 1.00 5.62  ? 2610 ARG A CG    1 
ATOM   9070  C  CD    . ARG A 1 2610 ? 235.921 236.367 224.792 1.00 8.41  ? 2610 ARG A CD    1 
ATOM   9071  N  NE    . ARG A 1 2610 ? 235.328 236.515 223.468 1.00 9.98  ? 2610 ARG A NE    1 
ATOM   9072  C  CZ    . ARG A 1 2610 ? 235.441 237.596 222.710 1.00 8.19  ? 2610 ARG A CZ    1 
ATOM   9073  N  NH1   . ARG A 1 2610 ? 236.162 238.637 223.091 1.00 10.40 ? 2610 ARG A NH1   1 
ATOM   9074  N  NH2   . ARG A 1 2610 ? 234.817 237.632 221.537 1.00 9.07  ? 2610 ARG A NH2   1 
ATOM   9075  N  N     . ALA A 1 2611 ? 234.781 237.130 230.273 1.00 5.62  ? 2611 ALA A N     1 
ATOM   9076  C  CA    . ALA A 1 2611 ? 235.187 237.284 231.662 1.00 8.70  ? 2611 ALA A CA    1 
ATOM   9077  C  C     . ALA A 1 2611 ? 234.082 236.920 232.641 1.00 8.33  ? 2611 ALA A C     1 
ATOM   9078  O  O     . ALA A 1 2611 ? 234.284 237.043 233.854 1.00 16.28 ? 2611 ALA A O     1 
ATOM   9079  C  CB    . ALA A 1 2611 ? 235.648 238.721 231.922 1.00 7.83  ? 2611 ALA A CB    1 
ATOM   9080  N  N     . LEU A 1 2612 ? 232.928 236.477 232.150 1.00 5.77  ? 2612 LEU A N     1 
ATOM   9081  C  CA    . LEU A 1 2612 ? 231.775 236.155 232.985 1.00 8.32  ? 2612 LEU A CA    1 
ATOM   9082  C  C     . LEU A 1 2612 ? 231.303 234.753 232.623 1.00 6.23  ? 2612 LEU A C     1 
ATOM   9083  O  O     . LEU A 1 2612 ? 230.323 234.582 231.886 1.00 9.54  ? 2612 LEU A O     1 
ATOM   9084  C  CB    . LEU A 1 2612 ? 230.670 237.196 232.814 1.00 6.02  ? 2612 LEU A CB    1 
ATOM   9085  C  CG    . LEU A 1 2612 ? 229.731 237.432 233.995 1.00 7.05  ? 2612 LEU A CG    1 
ATOM   9086  C  CD1   . LEU A 1 2612 ? 230.519 237.725 235.250 1.00 6.15  ? 2612 LEU A CD1   1 
ATOM   9087  C  CD2   . LEU A 1 2612 ? 228.822 238.603 233.681 1.00 10.84 ? 2612 LEU A CD2   1 
ATOM   9088  N  N     . PRO A 1 2613 ? 231.983 233.720 233.127 1.00 8.96  ? 2613 PRO A N     1 
ATOM   9089  C  CA    . PRO A 1 2613 ? 231.548 232.348 232.845 1.00 9.24  ? 2613 PRO A CA    1 
ATOM   9090  C  C     . PRO A 1 2613 ? 230.211 232.042 233.496 1.00 22.98 ? 2613 PRO A C     1 
ATOM   9091  O  O     . PRO A 1 2613 ? 229.640 232.895 234.184 1.00 24.68 ? 2613 PRO A O     1 
ATOM   9092  C  CB    . PRO A 1 2613 ? 232.676 231.493 233.436 1.00 6.40  ? 2613 PRO A CB    1 
ATOM   9093  C  CG    . PRO A 1 2613 ? 233.251 232.337 234.512 1.00 10.43 ? 2613 PRO A CG    1 
ATOM   9094  C  CD    . PRO A 1 2613 ? 233.147 233.757 234.031 1.00 11.97 ? 2613 PRO A CD    1 
ATOM   9095  N  N     . ASP A 1 2614 ? 229.708 230.828 233.287 1.00 16.71 ? 2614 ASP A N     1 
ATOM   9096  C  CA    . ASP A 1 2614 ? 228.383 230.416 233.735 1.00 12.70 ? 2614 ASP A CA    1 
ATOM   9097  C  C     . ASP A 1 2614 ? 227.276 231.245 233.092 1.00 9.31  ? 2614 ASP A C     1 
ATOM   9098  O  O     . ASP A 1 2614 ? 226.207 231.428 233.682 1.00 13.10 ? 2614 ASP A O     1 
ATOM   9099  C  CB    . ASP A 1 2614 ? 228.265 230.471 235.265 1.00 14.68 ? 2614 ASP A CB    1 
ATOM   9100  C  CG    . ASP A 1 2614 ? 229.110 229.418 235.950 1.00 28.55 ? 2614 ASP A CG    1 
ATOM   9101  O  OD1   . ASP A 1 2614 ? 229.331 228.347 235.346 1.00 31.08 ? 2614 ASP A OD1   1 
ATOM   9102  O  OD2   . ASP A 1 2614 ? 229.557 229.662 237.091 1.00 28.22 ? 2614 ASP A OD2   1 
ATOM   9103  N  N     . MET A 1 2615 ? 227.517 231.753 231.884 1.00 7.93  ? 2615 MET A N     1 
ATOM   9104  C  CA    . MET A 1 2615 ? 226.528 232.521 231.139 1.00 6.35  ? 2615 MET A CA    1 
ATOM   9105  C  C     . MET A 1 2615 ? 226.640 232.176 229.662 1.00 6.21  ? 2615 MET A C     1 
ATOM   9106  O  O     . MET A 1 2615 ? 227.701 232.361 229.058 1.00 10.03 ? 2615 MET A O     1 
ATOM   9107  C  CB    . MET A 1 2615 ? 226.706 234.026 231.367 1.00 5.76  ? 2615 MET A CB    1 
ATOM   9108  C  CG    . MET A 1 2615 ? 225.939 234.538 232.577 1.00 10.48 ? 2615 MET A CG    1 
ATOM   9109  S  SD    . MET A 1 2615 ? 226.373 236.202 233.111 1.00 22.84 ? 2615 MET A SD    1 
ATOM   9110  C  CE    . MET A 1 2615 ? 225.743 237.191 231.763 1.00 2.27  ? 2615 MET A CE    1 
ATOM   9111  N  N     . GLU A 1 2616 ? 225.550 231.672 229.092 1.00 5.54  ? 2616 GLU A N     1 
ATOM   9112  C  CA    . GLU A 1 2616 ? 225.478 231.308 227.682 1.00 4.55  ? 2616 GLU A CA    1 
ATOM   9113  C  C     . GLU A 1 2616 ? 224.691 232.369 226.926 1.00 2.11  ? 2616 GLU A C     1 
ATOM   9114  O  O     . GLU A 1 2616 ? 223.595 232.751 227.346 1.00 5.42  ? 2616 GLU A O     1 
ATOM   9115  C  CB    . GLU A 1 2616 ? 224.817 229.941 227.502 1.00 9.87  ? 2616 GLU A CB    1 
ATOM   9116  C  CG    . GLU A 1 2616 ? 224.780 229.468 226.056 1.00 15.97 ? 2616 GLU A CG    1 
ATOM   9117  C  CD    . GLU A 1 2616 ? 224.164 228.091 225.892 1.00 23.01 ? 2616 GLU A CD    1 
ATOM   9118  O  OE1   . GLU A 1 2616 ? 223.739 227.498 226.904 1.00 24.34 ? 2616 GLU A OE1   1 
ATOM   9119  O  OE2   . GLU A 1 2616 ? 224.103 227.603 224.744 1.00 29.09 ? 2616 GLU A OE2   1 
ATOM   9120  N  N     . VAL A 1 2617 ? 225.245 232.831 225.810 1.00 1.12  ? 2617 VAL A N     1 
ATOM   9121  C  CA    . VAL A 1 2617 ? 224.617 233.860 224.988 1.00 0.83  ? 2617 VAL A CA    1 
ATOM   9122  C  C     . VAL A 1 2617 ? 223.948 233.197 223.792 1.00 0.35  ? 2617 VAL A C     1 
ATOM   9123  O  O     . VAL A 1 2617 ? 224.518 232.295 223.166 1.00 0.79  ? 2617 VAL A O     1 
ATOM   9124  C  CB    . VAL A 1 2617 ? 225.639 234.927 224.548 1.00 0.73  ? 2617 VAL A CB    1 
ATOM   9125  C  CG1   . VAL A 1 2617 ? 226.758 234.313 223.720 1.00 1.35  ? 2617 VAL A CG1   1 
ATOM   9126  C  CG2   . VAL A 1 2617 ? 224.948 236.045 223.778 1.00 0.63  ? 2617 VAL A CG2   1 
ATOM   9127  N  N     . VAL A 1 2618 ? 222.722 233.614 223.501 1.00 0.49  ? 2618 VAL A N     1 
ATOM   9128  C  CA    . VAL A 1 2618 ? 221.977 233.151 222.337 1.00 0.51  ? 2618 VAL A CA    1 
ATOM   9129  C  C     . VAL A 1 2618 ? 221.554 234.378 221.547 1.00 0.26  ? 2618 VAL A C     1 
ATOM   9130  O  O     . VAL A 1 2618 ? 220.783 235.207 222.045 1.00 0.52  ? 2618 VAL A O     1 
ATOM   9131  C  CB    . VAL A 1 2618 ? 220.761 232.299 222.733 1.00 0.41  ? 2618 VAL A CB    1 
ATOM   9132  C  CG1   . VAL A 1 2618 ? 219.840 232.107 221.544 1.00 0.45  ? 2618 VAL A CG1   1 
ATOM   9133  C  CG2   . VAL A 1 2618 ? 221.213 230.962 223.285 1.00 0.42  ? 2618 VAL A CG2   1 
ATOM   9134  N  N     . GLY A 1 2619 ? 222.051 234.491 220.320 1.00 0.21  ? 2619 GLY A N     1 
ATOM   9135  C  CA    . GLY A 1 2619 ? 221.797 235.666 219.512 1.00 0.45  ? 2619 GLY A CA    1 
ATOM   9136  C  C     . GLY A 1 2619 ? 220.493 235.631 218.742 1.00 0.34  ? 2619 GLY A C     1 
ATOM   9137  O  O     . GLY A 1 2619 ? 220.263 234.729 217.933 1.00 0.50  ? 2619 GLY A O     1 
ATOM   9138  N  N     . LEU A 1 2620 ? 219.632 236.610 218.991 1.00 0.74  ? 2620 LEU A N     1 
ATOM   9139  C  CA    . LEU A 1 2620 ? 218.395 236.795 218.247 1.00 0.68  ? 2620 LEU A CA    1 
ATOM   9140  C  C     . LEU A 1 2620 ? 218.515 238.058 217.409 1.00 0.66  ? 2620 LEU A C     1 
ATOM   9141  O  O     . LEU A 1 2620 ? 219.009 239.081 217.893 1.00 1.81  ? 2620 LEU A O     1 
ATOM   9142  C  CB    . LEU A 1 2620 ? 217.187 236.892 219.182 1.00 0.32  ? 2620 LEU A CB    1 
ATOM   9143  C  CG    . LEU A 1 2620 ? 216.802 235.639 219.968 1.00 0.51  ? 2620 LEU A CG    1 
ATOM   9144  C  CD1   . LEU A 1 2620 ? 217.514 235.597 221.311 1.00 0.98  ? 2620 LEU A CD1   1 
ATOM   9145  C  CD2   . LEU A 1 2620 ? 215.297 235.571 220.150 1.00 0.40  ? 2620 LEU A CD2   1 
ATOM   9146  N  N     . ASN A 1 2621 ? 218.075 237.983 216.162 1.00 0.75  ? 2621 ASN A N     1 
ATOM   9147  C  CA    . ASN A 1 2621 ? 218.197 239.087 215.216 1.00 1.05  ? 2621 ASN A CA    1 
ATOM   9148  C  C     . ASN A 1 2621 ? 216.799 239.603 214.899 1.00 0.79  ? 2621 ASN A C     1 
ATOM   9149  O  O     . ASN A 1 2621 ? 216.053 238.985 214.138 1.00 5.81  ? 2621 ASN A O     1 
ATOM   9150  C  CB    . ASN A 1 2621 ? 218.936 238.637 213.963 1.00 2.12  ? 2621 ASN A CB    1 
ATOM   9151  C  CG    . ASN A 1 2621 ? 220.360 238.236 214.254 1.00 5.56  ? 2621 ASN A CG    1 
ATOM   9152  O  OD1   . ASN A 1 2621 ? 220.656 237.058 214.442 1.00 2.97  ? 2621 ASN A OD1   1 
ATOM   9153  N  ND2   . ASN A 1 2621 ? 221.255 239.216 214.303 1.00 5.16  ? 2621 ASN A ND2   1 
ATOM   9154  N  N     . PHE A 1 2622 ? 216.451 240.738 215.491 1.00 0.63  ? 2622 PHE A N     1 
ATOM   9155  C  CA    . PHE A 1 2622 ? 215.131 241.314 215.300 1.00 0.46  ? 2622 PHE A CA    1 
ATOM   9156  C  C     . PHE A 1 2622 ? 215.031 241.968 213.929 1.00 0.88  ? 2622 PHE A C     1 
ATOM   9157  O  O     . PHE A 1 2622 ? 216.003 242.522 213.412 1.00 1.29  ? 2622 PHE A O     1 
ATOM   9158  C  CB    . PHE A 1 2622 ? 214.828 242.341 216.392 1.00 0.36  ? 2622 PHE A CB    1 
ATOM   9159  C  CG    . PHE A 1 2622 ? 214.432 241.738 217.712 1.00 0.57  ? 2622 PHE A CG    1 
ATOM   9160  C  CD1   . PHE A 1 2622 ? 214.698 240.408 217.998 1.00 0.36  ? 2622 PHE A CD1   1 
ATOM   9161  C  CD2   . PHE A 1 2622 ? 213.803 242.508 218.676 1.00 0.25  ? 2622 PHE A CD2   1 
ATOM   9162  C  CE1   . PHE A 1 2622 ? 214.339 239.861 219.211 1.00 0.27  ? 2622 PHE A CE1   1 
ATOM   9163  C  CE2   . PHE A 1 2622 ? 213.440 241.964 219.890 1.00 0.12  ? 2622 PHE A CE2   1 
ATOM   9164  C  CZ    . PHE A 1 2622 ? 213.708 240.639 220.157 1.00 0.13  ? 2622 PHE A CZ    1 
ATOM   9165  N  N     . SER A 1 2623 ? 213.850 241.887 213.341 1.00 0.71  ? 2623 SER A N     1 
ATOM   9166  C  CA    . SER A 1 2623 ? 213.521 242.595 212.114 1.00 0.75  ? 2623 SER A CA    1 
ATOM   9167  C  C     . SER A 1 2623 ? 212.299 243.466 212.382 1.00 0.56  ? 2623 SER A C     1 
ATOM   9168  O  O     . SER A 1 2623 ? 211.827 243.576 213.515 1.00 0.67  ? 2623 SER A O     1 
ATOM   9169  C  CB    . SER A 1 2623 ? 213.290 241.609 210.968 1.00 1.17  ? 2623 SER A CB    1 
ATOM   9170  O  OG    . SER A 1 2623 ? 212.115 240.846 211.178 1.00 1.54  ? 2623 SER A OG    1 
ATOM   9171  N  N     . SER A 1 2624 ? 211.787 244.097 211.326 1.00 0.81  ? 2624 SER A N     1 
ATOM   9172  C  CA    . SER A 1 2624 ? 210.543 244.847 211.466 1.00 1.04  ? 2624 SER A CA    1 
ATOM   9173  C  C     . SER A 1 2624 ? 209.369 243.923 211.763 1.00 0.82  ? 2624 SER A C     1 
ATOM   9174  O  O     . SER A 1 2624 ? 208.405 244.338 212.412 1.00 1.86  ? 2624 SER A O     1 
ATOM   9175  C  CB    . SER A 1 2624 ? 210.277 245.668 210.205 1.00 2.14  ? 2624 SER A CB    1 
ATOM   9176  O  OG    . SER A 1 2624 ? 210.214 244.842 209.057 1.00 5.90  ? 2624 SER A OG    1 
ATOM   9177  N  N     . ALA A 1 2625 ? 209.445 242.671 211.321 1.00 0.73  ? 2625 ALA A N     1 
ATOM   9178  C  CA    . ALA A 1 2625 ? 208.369 241.706 211.490 1.00 0.62  ? 2625 ALA A CA    1 
ATOM   9179  C  C     . ALA A 1 2625 ? 208.563 240.804 212.702 1.00 1.23  ? 2625 ALA A C     1 
ATOM   9180  O  O     . ALA A 1 2625 ? 207.834 239.818 212.847 1.00 2.34  ? 2625 ALA A O     1 
ATOM   9181  C  CB    . ALA A 1 2625 ? 208.226 240.853 210.228 1.00 1.62  ? 2625 ALA A CB    1 
ATOM   9182  N  N     . THR A 1 2626 ? 209.527 241.107 213.566 1.00 1.27  ? 2626 THR A N     1 
ATOM   9183  C  CA    . THR A 1 2626 ? 209.776 240.266 214.729 1.00 0.95  ? 2626 THR A CA    1 
ATOM   9184  C  C     . THR A 1 2626 ? 208.631 240.385 215.729 1.00 0.93  ? 2626 THR A C     1 
ATOM   9185  O  O     . THR A 1 2626 ? 208.233 241.490 216.109 1.00 1.18  ? 2626 THR A O     1 
ATOM   9186  C  CB    . THR A 1 2626 ? 211.102 240.648 215.388 1.00 0.66  ? 2626 THR A CB    1 
ATOM   9187  O  OG1   . THR A 1 2626 ? 212.187 240.194 214.572 1.00 1.07  ? 2626 THR A OG1   1 
ATOM   9188  C  CG2   . THR A 1 2626 ? 211.224 240.017 216.767 1.00 0.49  ? 2626 THR A CG2   1 
ATOM   9189  N  N     . THR A 1 2627 ? 208.104 239.242 216.150 1.00 1.65  ? 2627 THR A N     1 
ATOM   9190  C  CA    . THR A 1 2627 ? 207.033 239.161 217.134 1.00 1.10  ? 2627 THR A CA    1 
ATOM   9191  C  C     . THR A 1 2627 ? 207.564 238.433 218.364 1.00 1.15  ? 2627 THR A C     1 
ATOM   9192  O  O     . THR A 1 2627 ? 208.688 237.917 218.331 1.00 1.68  ? 2627 THR A O     1 
ATOM   9193  C  CB    . THR A 1 2627 ? 205.815 238.440 216.547 1.00 2.90  ? 2627 THR A CB    1 
ATOM   9194  O  OG1   . THR A 1 2627 ? 206.120 237.055 216.356 1.00 6.72  ? 2627 THR A OG1   1 
ATOM   9195  C  CG2   . THR A 1 2627 ? 205.418 239.057 215.216 1.00 2.18  ? 2627 THR A CG2   1 
ATOM   9196  N  N     . PRO A 1 2628 ? 206.813 238.378 219.469 1.00 2.12  ? 2628 PRO A N     1 
ATOM   9197  C  CA    . PRO A 1 2628 ? 207.276 237.584 220.617 1.00 1.36  ? 2628 PRO A CA    1 
ATOM   9198  C  C     . PRO A 1 2628 ? 207.496 236.120 220.289 1.00 1.41  ? 2628 PRO A C     1 
ATOM   9199  O  O     . PRO A 1 2628 ? 208.216 235.437 221.024 1.00 1.13  ? 2628 PRO A O     1 
ATOM   9200  C  CB    . PRO A 1 2628 ? 206.144 237.765 221.634 1.00 0.67  ? 2628 PRO A CB    1 
ATOM   9201  C  CG    . PRO A 1 2628 ? 205.610 239.105 221.330 1.00 0.45  ? 2628 PRO A CG    1 
ATOM   9202  C  CD    . PRO A 1 2628 ? 205.660 239.222 219.832 1.00 0.72  ? 2628 PRO A CD    1 
ATOM   9203  N  N     . GLU A 1 2629 ? 206.905 235.625 219.201 1.00 2.13  ? 2629 GLU A N     1 
ATOM   9204  C  CA    . GLU A 1 2629 ? 207.020 234.213 218.863 1.00 2.04  ? 2629 GLU A CA    1 
ATOM   9205  C  C     . GLU A 1 2629 ? 208.463 233.835 218.536 1.00 3.52  ? 2629 GLU A C     1 
ATOM   9206  O  O     . GLU A 1 2629 ? 208.859 232.680 218.725 1.00 4.24  ? 2629 GLU A O     1 
ATOM   9207  C  CB    . GLU A 1 2629 ? 206.091 233.897 217.693 1.00 3.31  ? 2629 GLU A CB    1 
ATOM   9208  C  CG    . GLU A 1 2629 ? 206.070 232.448 217.279 1.00 11.98 ? 2629 GLU A CG    1 
ATOM   9209  C  CD    . GLU A 1 2629 ? 205.494 231.558 218.367 1.00 17.79 ? 2629 GLU A CD    1 
ATOM   9210  O  OE1   . GLU A 1 2629 ? 204.694 232.054 219.186 1.00 16.67 ? 2629 GLU A OE1   1 
ATOM   9211  O  OE2   . GLU A 1 2629 ? 205.830 230.360 218.407 1.00 27.46 ? 2629 GLU A OE2   1 
ATOM   9212  N  N     . LEU A 1 2630 ? 209.260 234.792 218.048 1.00 1.41  ? 2630 LEU A N     1 
ATOM   9213  C  CA    . LEU A 1 2630 ? 210.685 234.544 217.853 1.00 0.95  ? 2630 LEU A CA    1 
ATOM   9214  C  C     . LEU A 1 2630 ? 211.380 234.244 219.173 1.00 1.80  ? 2630 LEU A C     1 
ATOM   9215  O  O     . LEU A 1 2630 ? 212.246 233.363 219.240 1.00 3.32  ? 2630 LEU A O     1 
ATOM   9216  C  CB    . LEU A 1 2630 ? 211.343 235.745 217.173 1.00 2.75  ? 2630 LEU A CB    1 
ATOM   9217  C  CG    . LEU A 1 2630 ? 212.820 235.572 216.811 1.00 0.84  ? 2630 LEU A CG    1 
ATOM   9218  C  CD1   . LEU A 1 2630 ? 212.979 234.717 215.570 1.00 3.56  ? 2630 LEU A CD1   1 
ATOM   9219  C  CD2   . LEU A 1 2630 ? 213.502 236.920 216.637 1.00 0.39  ? 2630 LEU A CD2   1 
ATOM   9220  N  N     . LEU A 1 2631 ? 211.029 234.978 220.228 1.00 1.37  ? 2631 LEU A N     1 
ATOM   9221  C  CA    . LEU A 1 2631 ? 211.568 234.679 221.549 1.00 0.76  ? 2631 LEU A CA    1 
ATOM   9222  C  C     . LEU A 1 2631 ? 211.099 233.314 222.037 1.00 1.12  ? 2631 LEU A C     1 
ATOM   9223  O  O     . LEU A 1 2631 ? 211.859 232.586 222.685 1.00 1.12  ? 2631 LEU A O     1 
ATOM   9224  C  CB    . LEU A 1 2631 ? 211.162 235.769 222.540 1.00 1.09  ? 2631 LEU A CB    1 
ATOM   9225  C  CG    . LEU A 1 2631 ? 211.767 237.165 222.369 1.00 0.50  ? 2631 LEU A CG    1 
ATOM   9226  C  CD1   . LEU A 1 2631 ? 211.077 238.160 223.278 1.00 0.20  ? 2631 LEU A CD1   1 
ATOM   9227  C  CD2   . LEU A 1 2631 ? 213.254 237.160 222.639 1.00 1.24  ? 2631 LEU A CD2   1 
ATOM   9228  N  N     . LEU A 1 2632 ? 209.851 232.952 221.730 1.00 1.52  ? 2632 LEU A N     1 
ATOM   9229  C  CA    . LEU A 1 2632 ? 209.287 231.705 222.232 1.00 0.98  ? 2632 LEU A CA    1 
ATOM   9230  C  C     . LEU A 1 2632 ? 209.957 230.490 221.600 1.00 1.94  ? 2632 LEU A C     1 
ATOM   9231  O  O     . LEU A 1 2632 ? 210.149 229.467 222.267 1.00 2.45  ? 2632 LEU A O     1 
ATOM   9232  C  CB    . LEU A 1 2632 ? 207.779 231.682 221.991 1.00 1.48  ? 2632 LEU A CB    1 
ATOM   9233  C  CG    . LEU A 1 2632 ? 207.005 232.754 222.760 1.00 1.13  ? 2632 LEU A CG    1 
ATOM   9234  C  CD1   . LEU A 1 2632 ? 205.566 232.837 222.286 1.00 2.24  ? 2632 LEU A CD1   1 
ATOM   9235  C  CD2   . LEU A 1 2632 ? 207.068 232.490 224.253 1.00 0.31  ? 2632 LEU A CD2   1 
ATOM   9236  N  N     . LYS A 1 2633 ? 210.306 230.576 220.314 1.00 3.13  ? 2633 LYS A N     1 
ATOM   9237  C  CA    . LYS A 1 2633 ? 211.052 229.491 219.682 1.00 1.89  ? 2633 LYS A CA    1 
ATOM   9238  C  C     . LYS A 1 2633 ? 212.418 229.310 220.327 1.00 2.07  ? 2633 LYS A C     1 
ATOM   9239  O  O     . LYS A 1 2633 ? 212.876 228.179 220.520 1.00 4.10  ? 2633 LYS A O     1 
ATOM   9240  C  CB    . LYS A 1 2633 ? 211.204 229.743 218.184 1.00 2.31  ? 2633 LYS A CB    1 
ATOM   9241  C  CG    . LYS A 1 2633 ? 209.915 229.811 217.402 1.00 3.22  ? 2633 LYS A CG    1 
ATOM   9242  C  CD    . LYS A 1 2633 ? 209.220 228.466 217.405 1.00 9.43  ? 2633 LYS A CD    1 
ATOM   9243  C  CE    . LYS A 1 2633 ? 208.031 228.458 216.474 1.00 14.12 ? 2633 LYS A CE    1 
ATOM   9244  N  NZ    . LYS A 1 2633 ? 206.920 229.303 216.934 1.00 18.10 ? 2633 LYS A NZ    1 
ATOM   9245  N  N     . THR A 1 2634 ? 213.084 230.416 220.665 1.00 1.71  ? 2634 THR A N     1 
ATOM   9246  C  CA    . THR A 1 2634 ? 214.355 230.331 221.375 1.00 1.33  ? 2634 THR A CA    1 
ATOM   9247  C  C     . THR A 1 2634 ? 214.178 229.671 222.737 1.00 1.25  ? 2634 THR A C     1 
ATOM   9248  O  O     . THR A 1 2634 ? 215.030 228.890 223.175 1.00 2.93  ? 2634 THR A O     1 
ATOM   9249  C  CB    . THR A 1 2634 ? 214.963 231.727 221.517 1.00 1.13  ? 2634 THR A CB    1 
ATOM   9250  O  OG1   . THR A 1 2634 ? 215.226 232.263 220.217 1.00 1.29  ? 2634 THR A OG1   1 
ATOM   9251  C  CG2   . THR A 1 2634 ? 216.257 231.676 222.301 1.00 0.88  ? 2634 THR A CG2   1 
ATOM   9252  N  N     . PHE A 1 2635 ? 213.070 229.966 223.420 1.00 0.80  ? 2635 PHE A N     1 
ATOM   9253  C  CA    . PHE A 1 2635 ? 212.781 229.299 224.685 1.00 1.00  ? 2635 PHE A CA    1 
ATOM   9254  C  C     . PHE A 1 2635 ? 212.553 227.807 224.481 1.00 2.23  ? 2635 PHE A C     1 
ATOM   9255  O  O     . PHE A 1 2635 ? 212.987 226.988 225.298 1.00 5.52  ? 2635 PHE A O     1 
ATOM   9256  C  CB    . PHE A 1 2635 ? 211.565 229.941 225.351 1.00 1.14  ? 2635 PHE A CB    1 
ATOM   9257  C  CG    . PHE A 1 2635 ? 211.809 231.334 225.855 1.00 0.80  ? 2635 PHE A CG    1 
ATOM   9258  C  CD1   . PHE A 1 2635 ? 213.083 231.745 226.203 1.00 0.49  ? 2635 PHE A CD1   1 
ATOM   9259  C  CD2   . PHE A 1 2635 ? 210.761 232.231 225.985 1.00 0.58  ? 2635 PHE A CD2   1 
ATOM   9260  C  CE1   . PHE A 1 2635 ? 213.308 233.023 226.668 1.00 0.51  ? 2635 PHE A CE1   1 
ATOM   9261  C  CE2   . PHE A 1 2635 ? 210.981 233.511 226.450 1.00 0.41  ? 2635 PHE A CE2   1 
ATOM   9262  C  CZ    . PHE A 1 2635 ? 212.257 233.908 226.792 1.00 0.43  ? 2635 PHE A CZ    1 
ATOM   9263  N  N     . ASP A 1 2636 ? 211.875 227.432 223.393 1.00 2.75  ? 2636 ASP A N     1 
ATOM   9264  C  CA    . ASP A 1 2636 ? 211.585 226.022 223.149 1.00 2.32  ? 2636 ASP A CA    1 
ATOM   9265  C  C     . ASP A 1 2636 ? 212.852 225.211 222.925 1.00 5.50  ? 2636 ASP A C     1 
ATOM   9266  O  O     . ASP A 1 2636 ? 212.905 224.032 223.291 1.00 9.14  ? 2636 ASP A O     1 
ATOM   9267  C  CB    . ASP A 1 2636 ? 210.656 225.878 221.945 1.00 2.65  ? 2636 ASP A CB    1 
ATOM   9268  C  CG    . ASP A 1 2636 ? 209.218 226.186 222.282 1.00 12.85 ? 2636 ASP A CG    1 
ATOM   9269  O  OD1   . ASP A 1 2636 ? 208.783 225.853 223.406 1.00 16.69 ? 2636 ASP A OD1   1 
ATOM   9270  O  OD2   . ASP A 1 2636 ? 208.518 226.760 221.422 1.00 21.01 ? 2636 ASP A OD2   1 
ATOM   9271  N  N     . HIS A 1 2637 ? 213.877 225.816 222.330 1.00 2.48  ? 2637 HIS A N     1 
ATOM   9272  C  CA    . HIS A 1 2637 ? 215.095 225.094 221.993 1.00 1.95  ? 2637 HIS A CA    1 
ATOM   9273  C  C     . HIS A 1 2637 ? 216.095 225.050 223.145 1.00 3.34  ? 2637 HIS A C     1 
ATOM   9274  O  O     . HIS A 1 2637 ? 216.742 224.022 223.362 1.00 2.92  ? 2637 HIS A O     1 
ATOM   9275  C  CB    . HIS A 1 2637 ? 215.748 225.722 220.761 1.00 1.91  ? 2637 HIS A CB    1 
ATOM   9276  C  CG    . HIS A 1 2637 ? 217.001 225.034 220.325 1.00 5.52  ? 2637 HIS A CG    1 
ATOM   9277  N  ND1   . HIS A 1 2637 ? 218.249 225.395 220.788 1.00 5.67  ? 2637 HIS A ND1   1 
ATOM   9278  C  CD2   . HIS A 1 2637 ? 217.202 224.003 219.471 1.00 5.70  ? 2637 HIS A CD2   1 
ATOM   9279  C  CE1   . HIS A 1 2637 ? 219.163 224.619 220.237 1.00 7.64  ? 2637 HIS A CE1   1 
ATOM   9280  N  NE2   . HIS A 1 2637 ? 218.555 223.764 219.434 1.00 6.21  ? 2637 HIS A NE2   1 
ATOM   9281  N  N     . TYR A 1 2638 ? 216.231 226.145 223.890 1.00 3.37  ? 2638 TYR A N     1 
ATOM   9282  C  CA    . TYR A 1 2638 ? 217.243 226.250 224.928 1.00 2.10  ? 2638 TYR A CA    1 
ATOM   9283  C  C     . TYR A 1 2638 ? 216.708 226.078 226.341 1.00 3.03  ? 2638 TYR A C     1 
ATOM   9284  O  O     . TYR A 1 2638 ? 217.509 225.954 227.272 1.00 4.12  ? 2638 TYR A O     1 
ATOM   9285  C  CB    . TYR A 1 2638 ? 217.957 227.605 224.835 1.00 1.94  ? 2638 TYR A CB    1 
ATOM   9286  C  CG    . TYR A 1 2638 ? 218.749 227.809 223.570 1.00 2.51  ? 2638 TYR A CG    1 
ATOM   9287  C  CD1   . TYR A 1 2638 ? 220.065 227.374 223.476 1.00 3.71  ? 2638 TYR A CD1   1 
ATOM   9288  C  CD2   . TYR A 1 2638 ? 218.188 228.442 222.470 1.00 1.60  ? 2638 TYR A CD2   1 
ATOM   9289  C  CE1   . TYR A 1 2638 ? 220.796 227.559 222.320 1.00 3.15  ? 2638 TYR A CE1   1 
ATOM   9290  C  CE2   . TYR A 1 2638 ? 218.911 228.631 221.312 1.00 2.24  ? 2638 TYR A CE2   1 
ATOM   9291  C  CZ    . TYR A 1 2638 ? 220.213 228.189 221.243 1.00 3.12  ? 2638 TYR A CZ    1 
ATOM   9292  O  OH    . TYR A 1 2638 ? 220.938 228.376 220.089 1.00 12.05 ? 2638 TYR A OH    1 
ATOM   9293  N  N     . CYS A 1 2639 ? 215.395 226.064 226.529 1.00 2.78  ? 2639 CYS A N     1 
ATOM   9294  C  CA    . CYS A 1 2639 ? 214.810 226.073 227.858 1.00 1.47  ? 2639 CYS A CA    1 
ATOM   9295  C  C     . CYS A 1 2639 ? 213.725 225.010 227.954 1.00 1.17  ? 2639 CYS A C     1 
ATOM   9296  O  O     . CYS A 1 2639 ? 213.205 224.528 226.946 1.00 1.63  ? 2639 CYS A O     1 
ATOM   9297  C  CB    . CYS A 1 2639 ? 214.232 227.454 228.200 1.00 1.39  ? 2639 CYS A CB    1 
ATOM   9298  S  SG    . CYS A 1 2639 ? 215.449 228.789 228.240 1.00 5.27  ? 2639 CYS A SG    1 
ATOM   9299  N  N     . GLU A 1 2640 ? 213.393 224.644 229.186 1.00 1.97  ? 2640 GLU A N     1 
ATOM   9300  C  CA    . GLU A 1 2640 ? 212.326 223.693 229.456 1.00 2.81  ? 2640 GLU A CA    1 
ATOM   9301  C  C     . GLU A 1 2640 ? 211.290 224.321 230.379 1.00 1.80  ? 2640 GLU A C     1 
ATOM   9302  O  O     . GLU A 1 2640 ? 211.615 225.130 231.250 1.00 1.16  ? 2640 GLU A O     1 
ATOM   9303  C  CB    . GLU A 1 2640 ? 212.869 222.398 230.082 1.00 2.54  ? 2640 GLU A CB    1 
ATOM   9304  C  CG    . GLU A 1 2640 ? 213.478 222.569 231.463 1.00 9.39  ? 2640 GLU A CG    1 
ATOM   9305  C  CD    . GLU A 1 2640 ? 214.056 221.278 232.011 1.00 25.04 ? 2640 GLU A CD    1 
ATOM   9306  O  OE1   . GLU A 1 2640 ? 214.001 220.251 231.304 1.00 21.27 ? 2640 GLU A OE1   1 
ATOM   9307  O  OE2   . GLU A 1 2640 ? 214.559 221.289 233.155 1.00 27.26 ? 2640 GLU A OE2   1 
ATOM   9308  N  N     . TYR A 1 2641 ? 210.033 223.949 230.160 1.00 3.56  ? 2641 TYR A N     1 
ATOM   9309  C  CA    . TYR A 1 2641 ? 208.944 224.291 231.066 1.00 1.71  ? 2641 TYR A CA    1 
ATOM   9310  C  C     . TYR A 1 2641 ? 208.771 223.151 232.058 1.00 1.61  ? 2641 TYR A C     1 
ATOM   9311  O  O     . TYR A 1 2641 ? 208.592 221.998 231.654 1.00 5.80  ? 2641 TYR A O     1 
ATOM   9312  C  CB    . TYR A 1 2641 ? 207.644 224.527 230.300 1.00 1.56  ? 2641 TYR A CB    1 
ATOM   9313  C  CG    . TYR A 1 2641 ? 207.665 225.699 229.348 1.00 1.53  ? 2641 TYR A CG    1 
ATOM   9314  C  CD1   . TYR A 1 2641 ? 208.153 225.561 228.056 1.00 2.33  ? 2641 TYR A CD1   1 
ATOM   9315  C  CD2   . TYR A 1 2641 ? 207.174 226.939 229.733 1.00 0.83  ? 2641 TYR A CD2   1 
ATOM   9316  C  CE1   . TYR A 1 2641 ? 208.168 226.627 227.179 1.00 1.87  ? 2641 TYR A CE1   1 
ATOM   9317  C  CE2   . TYR A 1 2641 ? 207.183 228.012 228.863 1.00 1.15  ? 2641 TYR A CE2   1 
ATOM   9318  C  CZ    . TYR A 1 2641 ? 207.681 227.851 227.588 1.00 1.80  ? 2641 TYR A CZ    1 
ATOM   9319  O  OH    . TYR A 1 2641 ? 207.692 228.913 226.719 1.00 2.93  ? 2641 TYR A OH    1 
ATOM   9320  N  N     . ARG A 1 2642 ? 208.836 223.462 233.350 1.00 1.75  ? 2642 ARG A N     1 
ATOM   9321  C  CA    . ARG A 1 2642 ? 208.659 222.461 234.389 1.00 3.36  ? 2642 ARG A CA    1 
ATOM   9322  C  C     . ARG A 1 2642 ? 207.571 222.897 235.362 1.00 5.43  ? 2642 ARG A C     1 
ATOM   9323  O  O     . ARG A 1 2642 ? 207.481 224.074 235.726 1.00 4.19  ? 2642 ARG A O     1 
ATOM   9324  C  CB    . ARG A 1 2642 ? 209.983 222.181 235.126 1.00 3.66  ? 2642 ARG A CB    1 
ATOM   9325  C  CG    . ARG A 1 2642 ? 210.445 223.240 236.115 1.00 3.62  ? 2642 ARG A CG    1 
ATOM   9326  C  CD    . ARG A 1 2642 ? 211.564 222.692 236.998 1.00 3.72  ? 2642 ARG A CD    1 
ATOM   9327  N  NE    . ARG A 1 2642 ? 211.967 223.618 238.051 1.00 5.87  ? 2642 ARG A NE    1 
ATOM   9328  C  CZ    . ARG A 1 2642 ? 212.708 224.701 237.857 1.00 6.56  ? 2642 ARG A CZ    1 
ATOM   9329  N  NH1   . ARG A 1 2642 ? 213.172 225.019 236.660 1.00 9.62  ? 2642 ARG A NH1   1 
ATOM   9330  N  NH2   . ARG A 1 2642 ? 212.996 225.483 238.893 1.00 4.16  ? 2642 ARG A NH2   1 
ATOM   9331  N  N     . ARG A 1 2643 ? 206.730 221.943 235.752 1.00 12.44 ? 2643 ARG A N     1 
ATOM   9332  C  CA    . ARG A 1 2643 ? 205.689 222.163 236.745 1.00 7.61  ? 2643 ARG A CA    1 
ATOM   9333  C  C     . ARG A 1 2643 ? 206.310 222.136 238.136 1.00 6.71  ? 2643 ARG A C     1 
ATOM   9334  O  O     . ARG A 1 2643 ? 206.953 221.152 238.518 1.00 8.24  ? 2643 ARG A O     1 
ATOM   9335  C  CB    . ARG A 1 2643 ? 204.595 221.102 236.617 1.00 7.82  ? 2643 ARG A CB    1 
ATOM   9336  C  CG    . ARG A 1 2643 ? 203.456 221.204 237.632 1.00 16.91 ? 2643 ARG A CG    1 
ATOM   9337  C  CD    . ARG A 1 2643 ? 202.593 222.452 237.498 1.00 19.64 ? 2643 ARG A CD    1 
ATOM   9338  N  NE    . ARG A 1 2643 ? 201.848 222.493 236.244 1.00 21.45 ? 2643 ARG A NE    1 
ATOM   9339  C  CZ    . ARG A 1 2643 ? 201.212 223.565 235.788 1.00 23.04 ? 2643 ARG A CZ    1 
ATOM   9340  N  NH1   . ARG A 1 2643 ? 201.169 224.689 236.483 1.00 17.83 ? 2643 ARG A NH1   1 
ATOM   9341  N  NH2   . ARG A 1 2643 ? 200.592 223.501 234.613 1.00 16.85 ? 2643 ARG A NH2   1 
ATOM   9342  N  N     . THR A 1 2644 ? 206.125 223.217 238.881 1.00 6.91  ? 2644 THR A N     1 
ATOM   9343  C  CA    . THR A 1 2644 ? 206.572 223.356 240.255 1.00 6.76  ? 2644 THR A CA    1 
ATOM   9344  C  C     . THR A 1 2644 ? 205.368 223.644 241.142 1.00 9.43  ? 2644 THR A C     1 
ATOM   9345  O  O     . THR A 1 2644 ? 204.310 224.049 240.647 1.00 12.73 ? 2644 THR A O     1 
ATOM   9346  C  CB    . THR A 1 2644 ? 207.607 224.485 240.395 1.00 8.84  ? 2644 THR A CB    1 
ATOM   9347  O  OG1   . THR A 1 2644 ? 206.949 225.756 240.323 1.00 11.77 ? 2644 THR A OG1   1 
ATOM   9348  C  CG2   . THR A 1 2644 ? 208.665 224.393 239.305 1.00 6.78  ? 2644 THR A CG2   1 
ATOM   9349  N  N     . PRO A 1 2645 ? 205.484 223.431 242.456 1.00 10.74 ? 2645 PRO A N     1 
ATOM   9350  C  CA    . PRO A 1 2645 ? 204.343 223.726 243.339 1.00 11.09 ? 2645 PRO A CA    1 
ATOM   9351  C  C     . PRO A 1 2645 ? 203.885 225.171 243.278 1.00 8.87  ? 2645 PRO A C     1 
ATOM   9352  O  O     . PRO A 1 2645 ? 202.718 225.452 243.578 1.00 10.29 ? 2645 PRO A O     1 
ATOM   9353  C  CB    . PRO A 1 2645 ? 204.879 223.365 244.731 1.00 8.99  ? 2645 PRO A CB    1 
ATOM   9354  C  CG    . PRO A 1 2645 ? 205.933 222.355 244.469 1.00 8.66  ? 2645 PRO A CG    1 
ATOM   9355  C  CD    . PRO A 1 2645 ? 206.585 222.781 243.189 1.00 6.08  ? 2645 PRO A CD    1 
ATOM   9356  N  N     . ASN A 1 2646 ? 204.764 226.098 242.905 1.00 8.58  ? 2646 ASN A N     1 
ATOM   9357  C  CA    . ASN A 1 2646 ? 204.421 227.510 242.824 1.00 8.53  ? 2646 ASN A CA    1 
ATOM   9358  C  C     . ASN A 1 2646 ? 204.042 227.958 241.419 1.00 9.33  ? 2646 ASN A C     1 
ATOM   9359  O  O     . ASN A 1 2646 ? 203.757 229.143 241.221 1.00 14.19 ? 2646 ASN A O     1 
ATOM   9360  C  CB    . ASN A 1 2646 ? 205.582 228.362 243.343 1.00 7.01  ? 2646 ASN A CB    1 
ATOM   9361  C  CG    . ASN A 1 2646 ? 205.592 228.468 244.850 1.00 15.81 ? 2646 ASN A CG    1 
ATOM   9362  O  OD1   . ASN A 1 2646 ? 206.053 227.564 245.545 1.00 15.50 ? 2646 ASN A OD1   1 
ATOM   9363  N  ND2   . ASN A 1 2646 ? 205.072 229.573 245.368 1.00 15.63 ? 2646 ASN A ND2   1 
ATOM   9364  N  N     . GLY A 1 2647 ? 204.031 227.054 240.447 1.00 6.72  ? 2647 GLY A N     1 
ATOM   9365  C  CA    . GLY A 1 2647 ? 203.664 227.374 239.085 1.00 2.71  ? 2647 GLY A CA    1 
ATOM   9366  C  C     . GLY A 1 2647 ? 204.691 226.877 238.094 1.00 3.51  ? 2647 GLY A C     1 
ATOM   9367  O  O     . GLY A 1 2647 ? 205.662 226.204 238.439 1.00 3.58  ? 2647 GLY A O     1 
ATOM   9368  N  N     . VAL A 1 2648 ? 204.463 227.226 236.834 1.00 1.88  ? 2648 VAL A N     1 
ATOM   9369  C  CA    . VAL A 1 2648 ? 205.354 226.823 235.753 1.00 1.26  ? 2648 VAL A CA    1 
ATOM   9370  C  C     . VAL A 1 2648 ? 206.580 227.725 235.751 1.00 1.04  ? 2648 VAL A C     1 
ATOM   9371  O  O     . VAL A 1 2648 ? 206.465 228.954 235.813 1.00 1.10  ? 2648 VAL A O     1 
ATOM   9372  C  CB    . VAL A 1 2648 ? 204.626 226.871 234.401 1.00 2.33  ? 2648 VAL A CB    1 
ATOM   9373  C  CG1   . VAL A 1 2648 ? 205.564 226.475 233.273 1.00 0.93  ? 2648 VAL A CG1   1 
ATOM   9374  C  CG2   . VAL A 1 2648 ? 203.410 225.963 234.426 1.00 1.27  ? 2648 VAL A CG2   1 
ATOM   9375  N  N     . VAL A 1 2649 ? 207.760 227.114 235.686 1.00 1.26  ? 2649 VAL A N     1 
ATOM   9376  C  CA    . VAL A 1 2649 ? 209.028 227.830 235.656 1.00 0.73  ? 2649 VAL A CA    1 
ATOM   9377  C  C     . VAL A 1 2649 ? 209.739 227.489 234.355 1.00 1.29  ? 2649 VAL A C     1 
ATOM   9378  O  O     . VAL A 1 2649 ? 209.856 226.312 233.998 1.00 2.62  ? 2649 VAL A O     1 
ATOM   9379  C  CB    . VAL A 1 2649 ? 209.907 227.484 236.872 1.00 1.72  ? 2649 VAL A CB    1 
ATOM   9380  C  CG1   . VAL A 1 2649 ? 211.336 227.944 236.648 1.00 2.43  ? 2649 VAL A CG1   1 
ATOM   9381  C  CG2   . VAL A 1 2649 ? 209.337 228.110 238.127 1.00 2.06  ? 2649 VAL A CG2   1 
ATOM   9382  N  N     . LEU A 1 2650 ? 210.192 228.516 233.641 1.00 1.21  ? 2650 LEU A N     1 
ATOM   9383  C  CA    . LEU A 1 2650 ? 210.985 228.347 232.430 1.00 0.39  ? 2650 LEU A CA    1 
ATOM   9384  C  C     . LEU A 1 2650 ? 212.444 228.632 232.763 1.00 0.32  ? 2650 LEU A C     1 
ATOM   9385  O  O     . LEU A 1 2650 ? 212.786 229.750 233.159 1.00 0.60  ? 2650 LEU A O     1 
ATOM   9386  C  CB    . LEU A 1 2650 ? 210.491 229.273 231.320 1.00 0.45  ? 2650 LEU A CB    1 
ATOM   9387  C  CG    . LEU A 1 2650 ? 211.162 229.142 229.952 1.00 0.25  ? 2650 LEU A CG    1 
ATOM   9388  C  CD1   . LEU A 1 2650 ? 210.822 227.807 229.319 1.00 0.45  ? 2650 LEU A CD1   1 
ATOM   9389  C  CD2   . LEU A 1 2650 ? 210.747 230.289 229.049 1.00 0.24  ? 2650 LEU A CD2   1 
ATOM   9390  N  N     . ALA A 1 2651 ? 213.293 227.623 232.604 1.00 0.47  ? 2651 ALA A N     1 
ATOM   9391  C  CA    . ALA A 1 2651 ? 214.705 227.719 232.934 1.00 0.66  ? 2651 ALA A CA    1 
ATOM   9392  C  C     . ALA A 1 2651 ? 215.528 227.096 231.817 1.00 1.05  ? 2651 ALA A C     1 
ATOM   9393  O  O     . ALA A 1 2651 ? 215.036 226.218 231.099 1.00 1.37  ? 2651 ALA A O     1 
ATOM   9394  C  CB    . ALA A 1 2651 ? 215.021 227.021 234.266 1.00 0.45  ? 2651 ALA A CB    1 
ATOM   9395  N  N     . PRO A 1 2652 ? 216.777 227.528 231.648 1.00 1.47  ? 2652 PRO A N     1 
ATOM   9396  C  CA    . PRO A 1 2652 ? 217.626 226.935 230.608 1.00 1.93  ? 2652 PRO A CA    1 
ATOM   9397  C  C     . PRO A 1 2652 ? 217.840 225.449 230.843 1.00 2.68  ? 2652 PRO A C     1 
ATOM   9398  O  O     . PRO A 1 2652 ? 217.892 224.975 231.980 1.00 2.20  ? 2652 PRO A O     1 
ATOM   9399  C  CB    . PRO A 1 2652 ? 218.942 227.714 230.733 1.00 2.14  ? 2652 PRO A CB    1 
ATOM   9400  C  CG    . PRO A 1 2652 ? 218.575 228.971 231.422 1.00 1.46  ? 2652 PRO A CG    1 
ATOM   9401  C  CD    . PRO A 1 2652 ? 217.459 228.630 232.346 1.00 0.99  ? 2652 PRO A CD    1 
ATOM   9402  N  N     . VAL A 1 2653 ? 217.966 224.712 229.738 1.00 5.81  ? 2653 VAL A N     1 
ATOM   9403  C  CA    . VAL A 1 2653 ? 218.164 223.266 229.812 1.00 3.40  ? 2653 VAL A CA    1 
ATOM   9404  C  C     . VAL A 1 2653 ? 219.450 222.948 230.562 1.00 4.55  ? 2653 VAL A C     1 
ATOM   9405  O  O     . VAL A 1 2653 ? 219.484 222.067 231.430 1.00 8.96  ? 2653 VAL A O     1 
ATOM   9406  C  CB    . VAL A 1 2653 ? 218.161 222.655 228.400 1.00 5.65  ? 2653 VAL A CB    1 
ATOM   9407  C  CG1   . VAL A 1 2653 ? 218.735 221.248 228.422 1.00 5.21  ? 2653 VAL A CG1   1 
ATOM   9408  C  CG2   . VAL A 1 2653 ? 216.752 222.650 227.833 1.00 3.61  ? 2653 VAL A CG2   1 
ATOM   9409  N  N     . GLN A 1 2654 ? 220.521 223.670 230.249 1.00 7.40  ? 2654 GLN A N     1 
ATOM   9410  C  CA    . GLN A 1 2654 ? 221.780 223.484 230.954 1.00 8.00  ? 2654 GLN A CA    1 
ATOM   9411  C  C     . GLN A 1 2654 ? 221.682 224.056 232.365 1.00 4.50  ? 2654 GLN A C     1 
ATOM   9412  O  O     . GLN A 1 2654 ? 221.276 225.207 232.554 1.00 5.66  ? 2654 GLN A O     1 
ATOM   9413  C  CB    . GLN A 1 2654 ? 222.913 224.151 230.179 1.00 9.15  ? 2654 GLN A CB    1 
ATOM   9414  C  CG    . GLN A 1 2654 ? 224.301 223.672 230.554 1.00 17.75 ? 2654 GLN A CG    1 
ATOM   9415  C  CD    . GLN A 1 2654 ? 225.389 224.456 229.850 1.00 25.21 ? 2654 GLN A CD    1 
ATOM   9416  O  OE1   . GLN A 1 2654 ? 226.579 224.203 230.045 1.00 28.95 ? 2654 GLN A OE1   1 
ATOM   9417  N  NE2   . GLN A 1 2654 ? 224.985 225.416 229.027 1.00 16.11 ? 2654 GLN A NE2   1 
ATOM   9418  N  N     . LEU A 1 2655 ? 222.054 223.250 233.353 1.00 10.75 ? 2655 LEU A N     1 
ATOM   9419  C  CA    . LEU A 1 2655 ? 221.944 223.635 234.752 1.00 10.09 ? 2655 LEU A CA    1 
ATOM   9420  C  C     . LEU A 1 2655 ? 223.132 224.487 235.179 1.00 10.44 ? 2655 LEU A C     1 
ATOM   9421  O  O     . LEU A 1 2655 ? 224.247 224.339 234.667 1.00 8.01  ? 2655 LEU A O     1 
ATOM   9422  C  CB    . LEU A 1 2655 ? 221.848 222.403 235.650 1.00 9.12  ? 2655 LEU A CB    1 
ATOM   9423  C  CG    . LEU A 1 2655 ? 220.757 221.367 235.372 1.00 13.10 ? 2655 LEU A CG    1 
ATOM   9424  C  CD1   . LEU A 1 2655 ? 220.538 220.512 236.604 1.00 10.67 ? 2655 LEU A CD1   1 
ATOM   9425  C  CD2   . LEU A 1 2655 ? 219.452 222.029 234.944 1.00 9.63  ? 2655 LEU A CD2   1 
ATOM   9426  N  N     . GLY A 1 2656 ? 222.880 225.387 236.126 1.00 10.44 ? 2656 GLY A N     1 
ATOM   9427  C  CA    . GLY A 1 2656 ? 223.926 226.241 236.645 1.00 6.20  ? 2656 GLY A CA    1 
ATOM   9428  C  C     . GLY A 1 2656 ? 224.350 227.358 235.725 1.00 7.88  ? 2656 GLY A C     1 
ATOM   9429  O  O     . GLY A 1 2656 ? 225.314 228.063 236.034 1.00 16.52 ? 2656 GLY A O     1 
ATOM   9430  N  N     . LYS A 1 2657 ? 223.657 227.547 234.609 1.00 8.93  ? 2657 LYS A N     1 
ATOM   9431  C  CA    . LYS A 1 2657 ? 224.002 228.555 233.621 1.00 5.71  ? 2657 LYS A CA    1 
ATOM   9432  C  C     . LYS A 1 2657 ? 222.892 229.589 233.522 1.00 3.80  ? 2657 LYS A C     1 
ATOM   9433  O  O     . LYS A 1 2657 ? 221.706 229.247 233.552 1.00 4.75  ? 2657 LYS A O     1 
ATOM   9434  C  CB    . LYS A 1 2657 ? 224.236 227.923 232.247 1.00 7.10  ? 2657 LYS A CB    1 
ATOM   9435  C  CG    . LYS A 1 2657 ? 225.375 226.930 232.197 1.00 7.67  ? 2657 LYS A CG    1 
ATOM   9436  C  CD    . LYS A 1 2657 ? 226.704 227.633 232.375 1.00 14.71 ? 2657 LYS A CD    1 
ATOM   9437  C  CE    . LYS A 1 2657 ? 227.864 226.658 232.333 1.00 20.76 ? 2657 LYS A CE    1 
ATOM   9438  N  NZ    . LYS A 1 2657 ? 228.032 226.075 230.977 1.00 23.83 ? 2657 LYS A NZ    1 
ATOM   9439  N  N     . TRP A 1 2658 ? 223.284 230.851 233.411 1.00 5.58  ? 2658 TRP A N     1 
ATOM   9440  C  CA    . TRP A 1 2658 ? 222.361 231.936 233.117 1.00 1.18  ? 2658 TRP A CA    1 
ATOM   9441  C  C     . TRP A 1 2658 ? 222.366 232.150 231.610 1.00 1.98  ? 2658 TRP A C     1 
ATOM   9442  O  O     . TRP A 1 2658 ? 223.424 232.372 231.017 1.00 6.59  ? 2658 TRP A O     1 
ATOM   9443  C  CB    . TRP A 1 2658 ? 222.761 233.213 233.851 1.00 1.52  ? 2658 TRP A CB    1 
ATOM   9444  C  CG    . TRP A 1 2658 ? 222.127 233.343 235.197 1.00 0.32  ? 2658 TRP A CG    1 
ATOM   9445  C  CD1   . TRP A 1 2658 ? 222.494 232.700 236.337 1.00 0.22  ? 2658 TRP A CD1   1 
ATOM   9446  C  CD2   . TRP A 1 2658 ? 221.000 234.158 235.538 1.00 0.29  ? 2658 TRP A CD2   1 
ATOM   9447  N  NE1   . TRP A 1 2658 ? 221.674 233.069 237.373 1.00 0.50  ? 2658 TRP A NE1   1 
ATOM   9448  C  CE2   . TRP A 1 2658 ? 220.746 233.961 236.908 1.00 0.26  ? 2658 TRP A CE2   1 
ATOM   9449  C  CE3   . TRP A 1 2658 ? 220.184 235.036 234.821 1.00 0.25  ? 2658 TRP A CE3   1 
ATOM   9450  C  CZ2   . TRP A 1 2658 ? 219.713 234.610 237.576 1.00 0.18  ? 2658 TRP A CZ2   1 
ATOM   9451  C  CZ3   . TRP A 1 2658 ? 219.158 235.676 235.482 1.00 0.23  ? 2658 TRP A CZ3   1 
ATOM   9452  C  CH2   . TRP A 1 2658 ? 218.930 235.462 236.847 1.00 0.18  ? 2658 TRP A CH2   1 
ATOM   9453  N  N     . LEU A 1 2659 ? 221.196 232.075 230.994 1.00 1.95  ? 2659 LEU A N     1 
ATOM   9454  C  CA    . LEU A 1 2659 ? 221.086 232.141 229.546 1.00 0.93  ? 2659 LEU A CA    1 
ATOM   9455  C  C     . LEU A 1 2659 ? 220.769 233.576 229.144 1.00 0.55  ? 2659 LEU A C     1 
ATOM   9456  O  O     . LEU A 1 2659 ? 219.809 234.170 229.646 1.00 0.73  ? 2659 LEU A O     1 
ATOM   9457  C  CB    . LEU A 1 2659 ? 220.015 231.170 229.053 1.00 0.55  ? 2659 LEU A CB    1 
ATOM   9458  C  CG    . LEU A 1 2659 ? 219.819 230.902 227.562 1.00 2.72  ? 2659 LEU A CG    1 
ATOM   9459  C  CD1   . LEU A 1 2659 ? 219.234 229.522 227.416 1.00 9.10  ? 2659 LEU A CD1   1 
ATOM   9460  C  CD2   . LEU A 1 2659 ? 218.927 231.904 226.902 1.00 2.40  ? 2659 LEU A CD2   1 
ATOM   9461  N  N     . VAL A 1 2660 ? 221.578 234.129 228.245 1.00 0.68  ? 2660 VAL A N     1 
ATOM   9462  C  CA    . VAL A 1 2660 ? 221.490 235.529 227.847 1.00 0.36  ? 2660 VAL A CA    1 
ATOM   9463  C  C     . VAL A 1 2660 ? 220.879 235.594 226.456 1.00 0.36  ? 2660 VAL A C     1 
ATOM   9464  O  O     . VAL A 1 2660 ? 221.455 235.071 225.495 1.00 0.56  ? 2660 VAL A O     1 
ATOM   9465  C  CB    . VAL A 1 2660 ? 222.868 236.211 227.871 1.00 0.47  ? 2660 VAL A CB    1 
ATOM   9466  C  CG1   . VAL A 1 2660 ? 222.733 237.704 227.631 1.00 0.31  ? 2660 VAL A CG1   1 
ATOM   9467  C  CG2   . VAL A 1 2660 ? 223.574 235.936 229.186 1.00 0.36  ? 2660 VAL A CG2   1 
ATOM   9468  N  N     . LEU A 1 2661 ? 219.719 236.237 226.345 1.00 0.54  ? 2661 LEU A N     1 
ATOM   9469  C  CA    . LEU A 1 2661 ? 219.097 236.489 225.048 1.00 0.33  ? 2661 LEU A CA    1 
ATOM   9470  C  C     . LEU A 1 2661 ? 219.642 237.804 224.510 1.00 0.30  ? 2661 LEU A C     1 
ATOM   9471  O  O     . LEU A 1 2661 ? 219.334 238.875 225.041 1.00 0.26  ? 2661 LEU A O     1 
ATOM   9472  C  CB    . LEU A 1 2661 ? 217.574 236.546 225.145 1.00 0.72  ? 2661 LEU A CB    1 
ATOM   9473  C  CG    . LEU A 1 2661 ? 216.762 235.255 225.259 1.00 0.79  ? 2661 LEU A CG    1 
ATOM   9474  C  CD1   . LEU A 1 2661 ? 216.935 234.640 226.616 1.00 2.69  ? 2661 LEU A CD1   1 
ATOM   9475  C  CD2   . LEU A 1 2661 ? 215.296 235.503 224.977 1.00 1.65  ? 2661 LEU A CD2   1 
ATOM   9476  N  N     . PHE A 1 2662 ? 220.444 237.725 223.456 1.00 0.49  ? 2662 PHE A N     1 
ATOM   9477  C  CA    . PHE A 1 2662 ? 221.015 238.901 222.820 1.00 0.34  ? 2662 PHE A CA    1 
ATOM   9478  C  C     . PHE A 1 2662 ? 220.165 239.275 221.610 1.00 0.47  ? 2662 PHE A C     1 
ATOM   9479  O  O     . PHE A 1 2662 ? 220.075 238.506 220.648 1.00 0.91  ? 2662 PHE A O     1 
ATOM   9480  C  CB    . PHE A 1 2662 ? 222.464 238.647 222.410 1.00 0.44  ? 2662 PHE A CB    1 
ATOM   9481  C  CG    . PHE A 1 2662 ? 223.108 239.810 221.719 1.00 1.06  ? 2662 PHE A CG    1 
ATOM   9482  C  CD1   . PHE A 1 2662 ? 222.818 241.108 222.102 1.00 1.09  ? 2662 PHE A CD1   1 
ATOM   9483  C  CD2   . PHE A 1 2662 ? 224.002 239.605 220.683 1.00 1.03  ? 2662 PHE A CD2   1 
ATOM   9484  C  CE1   . PHE A 1 2662 ? 223.407 242.175 221.467 1.00 0.94  ? 2662 PHE A CE1   1 
ATOM   9485  C  CE2   . PHE A 1 2662 ? 224.596 240.670 220.044 1.00 1.66  ? 2662 PHE A CE2   1 
ATOM   9486  C  CZ    . PHE A 1 2662 ? 224.300 241.957 220.435 1.00 1.73  ? 2662 PHE A CZ    1 
ATOM   9487  N  N     . CYS A 1 2663 ? 219.547 240.451 221.665 1.00 0.52  ? 2663 CYS A N     1 
ATOM   9488  C  CA    . CYS A 1 2663 ? 218.723 240.974 220.582 1.00 0.68  ? 2663 CYS A CA    1 
ATOM   9489  C  C     . CYS A 1 2663 ? 219.472 242.118 219.911 1.00 1.10  ? 2663 CYS A C     1 
ATOM   9490  O  O     . CYS A 1 2663 ? 219.726 243.150 220.539 1.00 0.86  ? 2663 CYS A O     1 
ATOM   9491  C  CB    . CYS A 1 2663 ? 217.365 241.435 221.112 1.00 0.96  ? 2663 CYS A CB    1 
ATOM   9492  S  SG    . CYS A 1 2663 ? 216.556 240.233 222.199 1.00 1.45  ? 2663 CYS A SG    1 
ATOM   9493  N  N     . ASP A 1 2664 ? 219.814 241.934 218.634 1.00 1.35  ? 2664 ASP A N     1 
ATOM   9494  C  CA    . ASP A 1 2664 ? 220.738 242.821 217.935 1.00 1.93  ? 2664 ASP A CA    1 
ATOM   9495  C  C     . ASP A 1 2664 ? 220.079 244.065 217.353 1.00 4.89  ? 2664 ASP A C     1 
ATOM   9496  O  O     . ASP A 1 2664 ? 220.772 245.062 217.121 1.00 5.61  ? 2664 ASP A O     1 
ATOM   9497  C  CB    . ASP A 1 2664 ? 221.435 242.058 216.805 1.00 3.05  ? 2664 ASP A CB    1 
ATOM   9498  C  CG    . ASP A 1 2664 ? 222.699 242.745 216.326 1.00 12.28 ? 2664 ASP A CG    1 
ATOM   9499  O  OD1   . ASP A 1 2664 ? 223.133 243.722 216.970 1.00 13.81 ? 2664 ASP A OD1   1 
ATOM   9500  O  OD2   . ASP A 1 2664 ? 223.260 242.306 215.300 1.00 16.96 ? 2664 ASP A OD2   1 
ATOM   9501  N  N     . GLU A 1 2665 ? 218.778 244.034 217.097 1.00 1.16  ? 2665 GLU A N     1 
ATOM   9502  C  CA    . GLU A 1 2665 ? 218.066 245.145 216.470 1.00 0.85  ? 2665 GLU A CA    1 
ATOM   9503  C  C     . GLU A 1 2665 ? 216.768 245.426 217.213 1.00 1.24  ? 2665 GLU A C     1 
ATOM   9504  O  O     . GLU A 1 2665 ? 215.689 245.526 216.627 1.00 1.39  ? 2665 GLU A O     1 
ATOM   9505  C  CB    . GLU A 1 2665 ? 217.804 244.852 214.997 1.00 1.32  ? 2665 GLU A CB    1 
ATOM   9506  C  CG    . GLU A 1 2665 ? 219.044 244.518 214.179 1.00 1.77  ? 2665 GLU A CG    1 
ATOM   9507  C  CD    . GLU A 1 2665 ? 219.897 245.737 213.870 1.00 3.67  ? 2665 GLU A CD    1 
ATOM   9508  O  OE1   . GLU A 1 2665 ? 219.469 246.867 214.178 1.00 5.49  ? 2665 GLU A OE1   1 
ATOM   9509  O  OE2   . GLU A 1 2665 ? 221.002 245.564 213.315 1.00 7.07  ? 2665 GLU A OE2   1 
ATOM   9510  N  N     . ILE A 1 2666 ? 216.874 245.559 218.538 1.00 0.72  ? 2666 ILE A N     1 
ATOM   9511  C  CA    . ILE A 1 2666 ? 215.713 245.538 219.421 1.00 0.35  ? 2666 ILE A CA    1 
ATOM   9512  C  C     . ILE A 1 2666 ? 214.707 246.648 219.128 1.00 0.32  ? 2666 ILE A C     1 
ATOM   9513  O  O     . ILE A 1 2666 ? 213.560 246.563 219.574 1.00 0.33  ? 2666 ILE A O     1 
ATOM   9514  C  CB    . ILE A 1 2666 ? 216.192 245.589 220.890 1.00 0.31  ? 2666 ILE A CB    1 
ATOM   9515  C  CG1   . ILE A 1 2666 ? 215.121 245.028 221.831 1.00 0.16  ? 2666 ILE A CG1   1 
ATOM   9516  C  CG2   . ILE A 1 2666 ? 216.602 247.002 221.280 1.00 0.17  ? 2666 ILE A CG2   1 
ATOM   9517  C  CD1   . ILE A 1 2666 ? 215.647 244.643 223.192 1.00 0.19  ? 2666 ILE A CD1   1 
ATOM   9518  N  N     . ASN A 1 2667 ? 215.089 247.681 218.381 1.00 0.68  ? 2667 ASN A N     1 
ATOM   9519  C  CA    . ASN A 1 2667 ? 214.185 248.792 218.114 1.00 0.41  ? 2667 ASN A CA    1 
ATOM   9520  C  C     . ASN A 1 2667 ? 213.698 248.840 216.665 1.00 0.51  ? 2667 ASN A C     1 
ATOM   9521  O  O     . ASN A 1 2667 ? 213.050 249.816 216.279 1.00 0.75  ? 2667 ASN A O     1 
ATOM   9522  C  CB    . ASN A 1 2667 ? 214.849 250.115 218.508 1.00 0.22  ? 2667 ASN A CB    1 
ATOM   9523  C  CG    . ASN A 1 2667 ? 216.073 250.425 217.684 1.00 0.63  ? 2667 ASN A CG    1 
ATOM   9524  O  OD1   . ASN A 1 2667 ? 216.749 249.527 217.190 1.00 4.61  ? 2667 ASN A OD1   1 
ATOM   9525  N  ND2   . ASN A 1 2667 ? 216.398 251.704 217.576 1.00 0.36  ? 2667 ASN A ND2   1 
ATOM   9526  N  N     . LEU A 1 2668 ? 214.005 247.824 215.856 1.00 0.58  ? 2668 LEU A N     1 
ATOM   9527  C  CA    . LEU A 1 2668 ? 213.385 247.654 214.541 1.00 0.77  ? 2668 LEU A CA    1 
ATOM   9528  C  C     . LEU A 1 2668 ? 211.948 247.136 214.497 1.00 0.46  ? 2668 LEU A C     1 
ATOM   9529  O  O     . LEU A 1 2668 ? 211.241 247.473 213.540 1.00 0.64  ? 2668 LEU A O     1 
ATOM   9530  C  CB    . LEU A 1 2668 ? 214.229 246.756 213.632 1.00 1.09  ? 2668 LEU A CB    1 
ATOM   9531  C  CG    . LEU A 1 2668 ? 215.546 247.365 213.170 1.00 2.36  ? 2668 LEU A CG    1 
ATOM   9532  C  CD1   . LEU A 1 2668 ? 216.341 246.369 212.354 1.00 3.81  ? 2668 LEU A CD1   1 
ATOM   9533  C  CD2   . LEU A 1 2668 ? 215.232 248.598 212.353 1.00 4.10  ? 2668 LEU A CD2   1 
ATOM   9534  N  N     . PRO A 1 2669 ? 211.479 246.297 215.431 1.00 0.71  ? 2669 PRO A N     1 
ATOM   9535  C  CA    . PRO A 1 2669 ? 210.140 245.714 215.264 1.00 0.73  ? 2669 PRO A CA    1 
ATOM   9536  C  C     . PRO A 1 2669 ? 209.073 246.775 215.035 1.00 0.61  ? 2669 PRO A C     1 
ATOM   9537  O  O     . PRO A 1 2669 ? 209.111 247.857 215.624 1.00 0.88  ? 2669 PRO A O     1 
ATOM   9538  C  CB    . PRO A 1 2669 ? 209.916 244.964 216.578 1.00 0.34  ? 2669 PRO A CB    1 
ATOM   9539  C  CG    . PRO A 1 2669 ? 211.268 244.590 217.002 1.00 0.38  ? 2669 PRO A CG    1 
ATOM   9540  C  CD    . PRO A 1 2669 ? 212.141 245.739 216.625 1.00 0.44  ? 2669 PRO A CD    1 
ATOM   9541  N  N     . ASP A 1 2670 ? 208.134 246.454 214.147 1.00 1.01  ? 2670 ASP A N     1 
ATOM   9542  C  CA    . ASP A 1 2670 ? 207.143 247.424 213.697 1.00 1.61  ? 2670 ASP A CA    1 
ATOM   9543  C  C     . ASP A 1 2670 ? 206.354 247.999 214.863 1.00 2.53  ? 2670 ASP A C     1 
ATOM   9544  O  O     . ASP A 1 2670 ? 205.868 247.268 215.730 1.00 1.75  ? 2670 ASP A O     1 
ATOM   9545  C  CB    . ASP A 1 2670 ? 206.182 246.781 212.695 1.00 1.28  ? 2670 ASP A CB    1 
ATOM   9546  C  CG    . ASP A 1 2670 ? 206.790 246.621 211.317 1.00 7.82  ? 2670 ASP A CG    1 
ATOM   9547  O  OD1   . ASP A 1 2670 ? 206.405 245.669 210.607 1.00 6.86  ? 2670 ASP A OD1   1 
ATOM   9548  O  OD2   . ASP A 1 2670 ? 207.642 247.450 210.938 1.00 11.92 ? 2670 ASP A OD2   1 
ATOM   9549  N  N     . MET A 1 2671 ? 206.232 249.319 214.874 1.00 1.69  ? 2671 MET A N     1 
ATOM   9550  C  CA    . MET A 1 2671 ? 205.341 250.015 215.784 1.00 1.03  ? 2671 MET A CA    1 
ATOM   9551  C  C     . MET A 1 2671 ? 203.973 250.132 215.127 1.00 2.23  ? 2671 MET A C     1 
ATOM   9552  O  O     . MET A 1 2671 ? 203.864 250.620 213.998 1.00 6.83  ? 2671 MET A O     1 
ATOM   9553  C  CB    . MET A 1 2671 ? 205.896 251.400 216.118 1.00 1.81  ? 2671 MET A CB    1 
ATOM   9554  C  CG    . MET A 1 2671 ? 205.104 252.158 217.157 1.00 1.79  ? 2671 MET A CG    1 
ATOM   9555  S  SD    . MET A 1 2671 ? 206.114 253.292 218.126 1.00 20.88 ? 2671 MET A SD    1 
ATOM   9556  C  CE    . MET A 1 2671 ? 207.098 252.148 219.084 1.00 0.98  ? 2671 MET A CE    1 
ATOM   9557  N  N     . ASP A 1 2672 ? 202.936 249.671 215.821 1.00 1.12  ? 2672 ASP A N     1 
ATOM   9558  C  CA    . ASP A 1 2672 ? 201.592 249.754 215.276 1.00 1.26  ? 2672 ASP A CA    1 
ATOM   9559  C  C     . ASP A 1 2672 ? 201.118 251.210 215.265 1.00 1.83  ? 2672 ASP A C     1 
ATOM   9560  O  O     . ASP A 1 2672 ? 201.819 252.128 215.699 1.00 1.38  ? 2672 ASP A O     1 
ATOM   9561  C  CB    . ASP A 1 2672 ? 200.641 248.847 216.056 1.00 1.73  ? 2672 ASP A CB    1 
ATOM   9562  C  CG    . ASP A 1 2672 ? 200.463 249.267 217.511 1.00 1.52  ? 2672 ASP A CG    1 
ATOM   9563  O  OD1   . ASP A 1 2672 ? 201.075 250.260 217.954 1.00 1.77  ? 2672 ASP A OD1   1 
ATOM   9564  O  OD2   . ASP A 1 2672 ? 199.695 248.590 218.220 1.00 3.18  ? 2672 ASP A OD2   1 
ATOM   9565  N  N     . LYS A 1 2673 ? 199.900 251.423 214.763 1.00 2.05  ? 2673 LYS A N     1 
ATOM   9566  C  CA    . LYS A 1 2673 ? 199.369 252.777 214.664 1.00 2.98  ? 2673 LYS A CA    1 
ATOM   9567  C  C     . LYS A 1 2673 ? 199.095 253.402 216.025 1.00 1.78  ? 2673 LYS A C     1 
ATOM   9568  O  O     . LYS A 1 2673 ? 198.846 254.610 216.094 1.00 3.93  ? 2673 LYS A O     1 
ATOM   9569  C  CB    . LYS A 1 2673 ? 198.095 252.787 213.816 1.00 2.26  ? 2673 LYS A CB    1 
ATOM   9570  C  CG    . LYS A 1 2673 ? 196.995 251.886 214.334 1.00 3.16  ? 2673 LYS A CG    1 
ATOM   9571  C  CD    . LYS A 1 2673 ? 195.701 252.082 213.564 1.00 5.38  ? 2673 LYS A CD    1 
ATOM   9572  C  CE    . LYS A 1 2673 ? 195.806 251.562 212.146 1.00 12.42 ? 2673 LYS A CE    1 
ATOM   9573  N  NZ    . LYS A 1 2673 ? 194.486 251.575 211.462 1.00 15.90 ? 2673 LYS A NZ    1 
ATOM   9574  N  N     . TYR A 1 2674 ? 199.139 252.619 217.102 1.00 1.99  ? 2674 TYR A N     1 
ATOM   9575  C  CA    . TYR A 1 2674 ? 198.920 253.120 218.451 1.00 1.19  ? 2674 TYR A CA    1 
ATOM   9576  C  C     . TYR A 1 2674 ? 200.205 253.171 219.270 1.00 1.85  ? 2674 TYR A C     1 
ATOM   9577  O  O     . TYR A 1 2674 ? 200.150 253.153 220.503 1.00 2.17  ? 2674 TYR A O     1 
ATOM   9578  C  CB    . TYR A 1 2674 ? 197.861 252.273 219.153 1.00 1.21  ? 2674 TYR A CB    1 
ATOM   9579  C  CG    . TYR A 1 2674 ? 196.649 252.010 218.292 1.00 1.95  ? 2674 TYR A CG    1 
ATOM   9580  C  CD1   . TYR A 1 2674 ? 195.769 253.035 217.969 1.00 1.88  ? 2674 TYR A CD1   1 
ATOM   9581  C  CD2   . TYR A 1 2674 ? 196.386 250.741 217.797 1.00 1.41  ? 2674 TYR A CD2   1 
ATOM   9582  C  CE1   . TYR A 1 2674 ? 194.662 252.801 217.182 1.00 1.28  ? 2674 TYR A CE1   1 
ATOM   9583  C  CE2   . TYR A 1 2674 ? 195.278 250.499 217.012 1.00 1.87  ? 2674 TYR A CE2   1 
ATOM   9584  C  CZ    . TYR A 1 2674 ? 194.420 251.533 216.707 1.00 1.59  ? 2674 TYR A CZ    1 
ATOM   9585  O  OH    . TYR A 1 2674 ? 193.317 251.296 215.923 1.00 5.23  ? 2674 TYR A OH    1 
ATOM   9586  N  N     . GLY A 1 2675 ? 201.358 253.224 218.609 1.00 2.97  ? 2675 GLY A N     1 
ATOM   9587  C  CA    . GLY A 1 2675 ? 202.619 253.458 219.290 1.00 1.99  ? 2675 GLY A CA    1 
ATOM   9588  C  C     . GLY A 1 2675 ? 203.141 252.315 220.131 1.00 1.45  ? 2675 GLY A C     1 
ATOM   9589  O  O     . GLY A 1 2675 ? 203.876 252.556 221.091 1.00 1.28  ? 2675 GLY A O     1 
ATOM   9590  N  N     . THR A 1 2676 ? 202.802 251.076 219.789 1.00 1.38  ? 2676 THR A N     1 
ATOM   9591  C  CA    . THR A 1 2676 ? 203.192 249.916 220.579 1.00 1.03  ? 2676 THR A CA    1 
ATOM   9592  C  C     . THR A 1 2676 ? 203.949 248.915 219.718 1.00 0.53  ? 2676 THR A C     1 
ATOM   9593  O  O     . THR A 1 2676 ? 203.521 248.596 218.605 1.00 0.53  ? 2676 THR A O     1 
ATOM   9594  C  CB    . THR A 1 2676 ? 201.967 249.240 221.203 1.00 1.10  ? 2676 THR A CB    1 
ATOM   9595  O  OG1   . THR A 1 2676 ? 201.270 250.178 222.031 1.00 1.52  ? 2676 THR A OG1   1 
ATOM   9596  C  CG2   . THR A 1 2676 ? 202.384 248.042 222.045 1.00 0.84  ? 2676 THR A CG2   1 
ATOM   9597  N  N     . GLN A 1 2677 ? 205.074 248.429 220.236 1.00 0.91  ? 2677 GLN A N     1 
ATOM   9598  C  CA    . GLN A 1 2677 ? 205.776 247.283 219.674 1.00 0.43  ? 2677 GLN A CA    1 
ATOM   9599  C  C     . GLN A 1 2677 ? 205.472 246.071 220.547 1.00 0.32  ? 2677 GLN A C     1 
ATOM   9600  O  O     . GLN A 1 2677 ? 205.758 246.085 221.749 1.00 0.91  ? 2677 GLN A O     1 
ATOM   9601  C  CB    . GLN A 1 2677 ? 207.282 247.538 219.605 1.00 0.20  ? 2677 GLN A CB    1 
ATOM   9602  C  CG    . GLN A 1 2677 ? 207.698 248.589 218.592 1.00 0.22  ? 2677 GLN A CG    1 
ATOM   9603  C  CD    . GLN A 1 2677 ? 209.111 249.089 218.822 1.00 0.42  ? 2677 GLN A CD    1 
ATOM   9604  O  OE1   . GLN A 1 2677 ? 209.393 249.745 219.822 1.00 0.59  ? 2677 GLN A OE1   1 
ATOM   9605  N  NE2   . GLN A 1 2677 ? 210.008 248.775 217.896 1.00 0.35  ? 2677 GLN A NE2   1 
ATOM   9606  N  N     . ARG A 1 2678 ? 204.889 245.034 219.944 1.00 0.09  ? 2678 ARG A N     1 
ATOM   9607  C  CA    . ARG A 1 2678 ? 204.412 243.896 220.726 1.00 0.09  ? 2678 ARG A CA    1 
ATOM   9608  C  C     . ARG A 1 2678 ? 205.557 243.178 221.432 1.00 0.12  ? 2678 ARG A C     1 
ATOM   9609  O  O     . ARG A 1 2678 ? 205.438 242.818 222.608 1.00 0.11  ? 2678 ARG A O     1 
ATOM   9610  C  CB    . ARG A 1 2678 ? 203.642 242.925 219.832 1.00 0.19  ? 2678 ARG A CB    1 
ATOM   9611  C  CG    . ARG A 1 2678 ? 203.109 241.709 220.573 1.00 0.28  ? 2678 ARG A CG    1 
ATOM   9612  C  CD    . ARG A 1 2678 ? 202.339 240.776 219.658 1.00 0.60  ? 2678 ARG A CD    1 
ATOM   9613  N  NE    . ARG A 1 2678 ? 201.157 241.407 219.086 1.00 2.15  ? 2678 ARG A NE    1 
ATOM   9614  C  CZ    . ARG A 1 2678 ? 200.360 240.832 218.197 1.00 2.06  ? 2678 ARG A CZ    1 
ATOM   9615  N  NH1   . ARG A 1 2678 ? 200.592 239.610 217.749 1.00 1.71  ? 2678 ARG A NH1   1 
ATOM   9616  N  NH2   . ARG A 1 2678 ? 199.306 241.502 217.741 1.00 3.34  ? 2678 ARG A NH2   1 
ATOM   9617  N  N     . VAL A 1 2679 ? 206.672 242.962 220.734 1.00 0.12  ? 2679 VAL A N     1 
ATOM   9618  C  CA    . VAL A 1 2679 ? 207.788 242.239 221.337 1.00 0.14  ? 2679 VAL A CA    1 
ATOM   9619  C  C     . VAL A 1 2679 ? 208.404 243.050 222.474 1.00 0.05  ? 2679 VAL A C     1 
ATOM   9620  O  O     . VAL A 1 2679 ? 208.845 242.489 223.481 1.00 0.01  ? 2679 VAL A O     1 
ATOM   9621  C  CB    . VAL A 1 2679 ? 208.825 241.851 220.263 1.00 0.16  ? 2679 VAL A CB    1 
ATOM   9622  C  CG1   . VAL A 1 2679 ? 209.563 243.070 219.738 1.00 0.07  ? 2679 VAL A CG1   1 
ATOM   9623  C  CG2   . VAL A 1 2679 ? 209.806 240.826 220.812 1.00 0.04  ? 2679 VAL A CG2   1 
ATOM   9624  N  N     . ILE A 1 2680 ? 208.433 244.378 222.339 1.00 0.03  ? 2680 ILE A N     1 
ATOM   9625  C  CA    . ILE A 1 2680 ? 208.965 245.218 223.407 1.00 0.04  ? 2680 ILE A CA    1 
ATOM   9626  C  C     . ILE A 1 2680 ? 208.091 245.121 224.652 1.00 0.03  ? 2680 ILE A C     1 
ATOM   9627  O  O     . ILE A 1 2680 ? 208.597 245.014 225.774 1.00 0.05  ? 2680 ILE A O     1 
ATOM   9628  C  CB    . ILE A 1 2680 ? 209.115 246.672 222.923 1.00 0.08  ? 2680 ILE A CB    1 
ATOM   9629  C  CG1   . ILE A 1 2680 ? 210.036 246.731 221.703 1.00 0.05  ? 2680 ILE A CG1   1 
ATOM   9630  C  CG2   . ILE A 1 2680 ? 209.652 247.557 224.037 1.00 0.02  ? 2680 ILE A CG2   1 
ATOM   9631  C  CD1   . ILE A 1 2680 ? 211.401 246.149 221.946 1.00 0.07  ? 2680 ILE A CD1   1 
ATOM   9632  N  N     . SER A 1 2681 ? 206.768 245.148 224.474 1.00 0.04  ? 2681 SER A N     1 
ATOM   9633  C  CA    . SER A 1 2681 ? 205.870 244.928 225.602 1.00 0.07  ? 2681 SER A CA    1 
ATOM   9634  C  C     . SER A 1 2681 ? 206.087 243.548 226.206 1.00 0.03  ? 2681 SER A C     1 
ATOM   9635  O  O     . SER A 1 2681 ? 206.020 243.377 227.428 1.00 0.10  ? 2681 SER A O     1 
ATOM   9636  C  CB    . SER A 1 2681 ? 204.415 245.096 225.164 1.00 0.11  ? 2681 SER A CB    1 
ATOM   9637  O  OG    . SER A 1 2681 ? 204.157 246.414 224.723 1.00 0.41  ? 2681 SER A OG    1 
ATOM   9638  N  N     . PHE A 1 2682 ? 206.347 242.553 225.359 1.00 0.04  ? 2682 PHE A N     1 
ATOM   9639  C  CA    . PHE A 1 2682 ? 206.616 241.206 225.846 1.00 0.02  ? 2682 PHE A CA    1 
ATOM   9640  C  C     . PHE A 1 2682 ? 207.902 241.156 226.662 1.00 0.05  ? 2682 PHE A C     1 
ATOM   9641  O  O     . PHE A 1 2682 ? 207.956 240.497 227.708 1.00 0.03  ? 2682 PHE A O     1 
ATOM   9642  C  CB    . PHE A 1 2682 ? 206.676 240.236 224.666 1.00 0.04  ? 2682 PHE A CB    1 
ATOM   9643  C  CG    . PHE A 1 2682 ? 206.764 238.798 225.063 1.00 0.05  ? 2682 PHE A CG    1 
ATOM   9644  C  CD1   . PHE A 1 2682 ? 205.640 238.110 225.480 1.00 0.06  ? 2682 PHE A CD1   1 
ATOM   9645  C  CD2   . PHE A 1 2682 ? 207.967 238.122 225.000 1.00 0.09  ? 2682 PHE A CD2   1 
ATOM   9646  C  CE1   . PHE A 1 2682 ? 205.718 236.782 225.840 1.00 0.08  ? 2682 PHE A CE1   1 
ATOM   9647  C  CE2   . PHE A 1 2682 ? 208.050 236.792 225.359 1.00 0.05  ? 2682 PHE A CE2   1 
ATOM   9648  C  CZ    . PHE A 1 2682 ? 206.925 236.123 225.778 1.00 0.03  ? 2682 PHE A CZ    1 
ATOM   9649  N  N     . ILE A 1 2683 ? 208.933 241.866 226.216 1.00 0.02  ? 2683 ILE A N     1 
ATOM   9650  C  CA    . ILE A 1 2683 ? 210.222 241.872 226.967 1.00 0.03  ? 2683 ILE A CA    1 
ATOM   9651  C  C     . ILE A 1 2683 ? 210.023 242.652 228.277 1.00 0.05  ? 2683 ILE A C     1 
ATOM   9652  O  O     . ILE A 1 2683 ? 210.562 242.211 229.311 1.00 0.01  ? 2683 ILE A O     1 
ATOM   9653  C  CB    . ILE A 1 2683 ? 211.381 242.419 226.113 1.00 0.02  ? 2683 ILE A CB    1 
ATOM   9654  C  CG1   . ILE A 1 2683 ? 211.562 241.602 224.832 1.00 0.02  ? 2683 ILE A CG1   1 
ATOM   9655  C  CG2   . ILE A 1 2683 ? 212.674 242.491 226.925 1.00 0.01  ? 2683 ILE A CG2   1 
ATOM   9656  C  CD1   . ILE A 1 2683 ? 212.596 242.163 223.875 1.00 0.02  ? 2683 ILE A CD1   1 
ATOM   9657  N  N     . ARG A 1 2684 ? 209.260 243.746 228.231 1.00 0.01  ? 2684 ARG A N     1 
ATOM   9658  C  CA    . ARG A 1 2684 ? 209.016 244.568 229.444 1.00 0.03  ? 2684 ARG A CA    1 
ATOM   9659  C  C     . ARG A 1 2684 ? 208.305 243.686 230.478 1.00 0.06  ? 2684 ARG A C     1 
ATOM   9660  O  O     . ARG A 1 2684 ? 208.680 243.745 231.667 1.00 0.06  ? 2684 ARG A O     1 
ATOM   9661  C  CB    . ARG A 1 2684 ? 208.201 245.823 229.110 1.00 0.07  ? 2684 ARG A CB    1 
ATOM   9662  C  CG    . ARG A 1 2684 ? 207.957 246.739 230.301 1.00 0.08  ? 2684 ARG A CG    1 
ATOM   9663  C  CD    . ARG A 1 2684 ? 206.482 247.061 230.464 1.00 0.10  ? 2684 ARG A CD    1 
ATOM   9664  N  NE    . ARG A 1 2684 ? 206.188 247.768 231.715 1.00 2.79  ? 2684 ARG A NE    1 
ATOM   9665  C  CZ    . ARG A 1 2684 ? 204.974 248.123 232.118 1.00 0.38  ? 2684 ARG A CZ    1 
ATOM   9666  N  NH1   . ARG A 1 2684 ? 203.916 247.805 231.396 1.00 0.19  ? 2684 ARG A NH1   1 
ATOM   9667  N  NH2   . ARG A 1 2684 ? 204.826 248.794 233.246 1.00 0.13  ? 2684 ARG A NH2   1 
ATOM   9668  N  N     . GLN A 1 2685 ? 207.338 242.890 230.028 1.00 0.04  ? 2685 GLN A N     1 
ATOM   9669  C  CA    . GLN A 1 2685 ? 206.612 241.972 230.940 1.00 0.05  ? 2685 GLN A CA    1 
ATOM   9670  C  C     . GLN A 1 2685 ? 207.612 240.990 231.569 1.00 0.10  ? 2685 GLN A C     1 
ATOM   9671  O  O     . GLN A 1 2685 ? 207.564 240.818 232.803 1.00 0.25  ? 2685 GLN A O     1 
ATOM   9672  C  CB    . GLN A 1 2685 ? 205.490 241.279 230.165 1.00 0.06  ? 2685 GLN A CB    1 
ATOM   9673  C  CG    . GLN A 1 2685 ? 204.706 240.245 230.967 1.00 0.05  ? 2685 GLN A CG    1 
ATOM   9674  C  CD    . GLN A 1 2685 ? 203.656 239.541 230.136 1.00 0.07  ? 2685 GLN A CD    1 
ATOM   9675  O  OE1   . GLN A 1 2685 ? 203.958 238.907 229.119 1.00 0.19  ? 2685 GLN A OE1   1 
ATOM   9676  N  NE2   . GLN A 1 2685 ? 202.406 239.652 230.558 1.00 0.07  ? 2685 GLN A NE2   1 
ATOM   9677  N  N     . MET A 1 2686 ? 208.496 240.391 230.767 1.00 0.10  ? 2686 MET A N     1 
ATOM   9678  C  CA    . MET A 1 2686 ? 209.404 239.388 231.318 1.00 0.23  ? 2686 MET A CA    1 
ATOM   9679  C  C     . MET A 1 2686 ? 210.420 239.996 232.277 1.00 0.37  ? 2686 MET A C     1 
ATOM   9680  O  O     . MET A 1 2686 ? 210.935 239.294 233.154 1.00 4.68  ? 2686 MET A O     1 
ATOM   9681  C  CB    . MET A 1 2686 ? 210.141 238.635 230.211 1.00 0.31  ? 2686 MET A CB    1 
ATOM   9682  C  CG    . MET A 1 2686 ? 209.276 237.710 229.390 1.00 0.24  ? 2686 MET A CG    1 
ATOM   9683  S  SD    . MET A 1 2686 ? 210.240 236.925 228.091 1.00 11.49 ? 2686 MET A SD    1 
ATOM   9684  C  CE    . MET A 1 2686 ? 210.658 238.330 227.074 1.00 0.07  ? 2686 MET A CE    1 
ATOM   9685  N  N     . VAL A 1 2687 ? 210.732 241.280 232.131 1.00 0.41  ? 2687 VAL A N     1 
ATOM   9686  C  CA    . VAL A 1 2687 ? 211.720 241.888 233.012 1.00 0.79  ? 2687 VAL A CA    1 
ATOM   9687  C  C     . VAL A 1 2687 ? 211.072 242.372 234.302 1.00 0.94  ? 2687 VAL A C     1 
ATOM   9688  O  O     . VAL A 1 2687 ? 211.534 242.041 235.400 1.00 6.75  ? 2687 VAL A O     1 
ATOM   9689  C  CB    . VAL A 1 2687 ? 212.451 243.025 232.277 1.00 2.02  ? 2687 VAL A CB    1 
ATOM   9690  C  CG1   . VAL A 1 2687 ? 213.261 243.842 233.262 1.00 1.68  ? 2687 VAL A CG1   1 
ATOM   9691  C  CG2   . VAL A 1 2687 ? 213.347 242.448 231.190 1.00 0.26  ? 2687 VAL A CG2   1 
ATOM   9692  N  N     . GLU A 1 2688 ? 209.987 243.145 234.178 1.00 0.88  ? 2688 GLU A N     1 
ATOM   9693  C  CA    . GLU A 1 2688 ? 209.328 243.787 235.311 1.00 0.94  ? 2688 GLU A CA    1 
ATOM   9694  C  C     . GLU A 1 2688 ? 208.463 242.813 236.108 1.00 1.00  ? 2688 GLU A C     1 
ATOM   9695  O  O     . GLU A 1 2688 ? 208.444 242.870 237.342 1.00 1.51  ? 2688 GLU A O     1 
ATOM   9696  C  CB    . GLU A 1 2688 ? 208.537 245.001 234.799 1.00 0.97  ? 2688 GLU A CB    1 
ATOM   9697  C  CG    . GLU A 1 2688 ? 207.975 245.944 235.871 1.00 2.66  ? 2688 GLU A CG    1 
ATOM   9698  C  CD    . GLU A 1 2688 ? 206.680 245.492 236.409 1.00 7.23  ? 2688 GLU A CD    1 
ATOM   9699  O  OE1   . GLU A 1 2688 ? 205.976 244.830 235.628 1.00 15.47 ? 2688 GLU A OE1   1 
ATOM   9700  O  OE2   . GLU A 1 2688 ? 206.359 245.796 237.580 1.00 10.50 ? 2688 GLU A OE2   1 
ATOM   9701  N  N     . HIS A 1 2689 ? 207.738 241.916 235.430 1.00 0.40  ? 2689 HIS A N     1 
ATOM   9702  C  CA    . HIS A 1 2689 ? 206.970 240.853 236.079 1.00 0.33  ? 2689 HIS A CA    1 
ATOM   9703  C  C     . HIS A 1 2689 ? 207.720 239.527 236.190 1.00 0.32  ? 2689 HIS A C     1 
ATOM   9704  O  O     . HIS A 1 2689 ? 207.217 238.604 236.838 1.00 0.40  ? 2689 HIS A O     1 
ATOM   9705  C  CB    . HIS A 1 2689 ? 205.644 240.606 235.338 1.00 0.43  ? 2689 HIS A CB    1 
ATOM   9706  C  CG    . HIS A 1 2689 ? 204.713 241.778 235.354 1.00 0.42  ? 2689 HIS A CG    1 
ATOM   9707  N  ND1   . HIS A 1 2689 ? 204.554 242.579 236.463 1.00 0.47  ? 2689 HIS A ND1   1 
ATOM   9708  C  CD2   . HIS A 1 2689 ? 203.923 242.309 234.392 1.00 1.31  ? 2689 HIS A CD2   1 
ATOM   9709  C  CE1   . HIS A 1 2689 ? 203.685 243.532 236.195 1.00 0.85  ? 2689 HIS A CE1   1 
ATOM   9710  N  NE2   . HIS A 1 2689 ? 203.298 243.399 234.940 1.00 2.15  ? 2689 HIS A NE2   1 
ATOM   9711  N  N     . GLY A 1 2690 ? 208.904 239.402 235.596 1.00 0.44  ? 2690 GLY A N     1 
ATOM   9712  C  CA    . GLY A 1 2690 ? 209.638 238.156 235.732 1.00 0.23  ? 2690 GLY A CA    1 
ATOM   9713  C  C     . GLY A 1 2690 ? 209.040 236.965 235.017 1.00 0.12  ? 2690 GLY A C     1 
ATOM   9714  O  O     . GLY A 1 2690 ? 209.338 235.824 235.381 1.00 0.16  ? 2690 GLY A O     1 
ATOM   9715  N  N     . GLY A 1 2691 ? 208.217 237.188 234.000 1.00 0.22  ? 2691 GLY A N     1 
ATOM   9716  C  CA    . GLY A 1 2691 ? 207.622 236.075 233.289 1.00 0.15  ? 2691 GLY A CA    1 
ATOM   9717  C  C     . GLY A 1 2691 ? 206.668 236.537 232.213 1.00 0.06  ? 2691 GLY A C     1 
ATOM   9718  O  O     . GLY A 1 2691 ? 206.683 237.698 231.801 1.00 0.10  ? 2691 GLY A O     1 
ATOM   9719  N  N     . PHE A 1 2692 ? 205.837 235.604 231.758 1.00 0.04  ? 2692 PHE A N     1 
ATOM   9720  C  CA    . PHE A 1 2692 ? 204.861 235.858 230.710 1.00 0.04  ? 2692 PHE A CA    1 
ATOM   9721  C  C     . PHE A 1 2692 ? 203.763 234.811 230.822 1.00 0.03  ? 2692 PHE A C     1 
ATOM   9722  O  O     . PHE A 1 2692 ? 203.828 233.904 231.656 1.00 0.04  ? 2692 PHE A O     1 
ATOM   9723  C  CB    . PHE A 1 2692 ? 205.513 235.837 229.325 1.00 0.06  ? 2692 PHE A CB    1 
ATOM   9724  C  CG    . PHE A 1 2692 ? 206.057 234.496 228.936 1.00 0.06  ? 2692 PHE A CG    1 
ATOM   9725  C  CD1   . PHE A 1 2692 ? 207.310 234.090 229.361 1.00 0.08  ? 2692 PHE A CD1   1 
ATOM   9726  C  CD2   . PHE A 1 2692 ? 205.314 233.640 228.143 1.00 0.06  ? 2692 PHE A CD2   1 
ATOM   9727  C  CE1   . PHE A 1 2692 ? 207.810 232.856 229.001 1.00 0.15  ? 2692 PHE A CE1   1 
ATOM   9728  C  CE2   . PHE A 1 2692 ? 205.806 232.407 227.782 1.00 0.13  ? 2692 PHE A CE2   1 
ATOM   9729  C  CZ    . PHE A 1 2692 ? 207.056 232.016 228.211 1.00 0.09  ? 2692 PHE A CZ    1 
ATOM   9730  N  N     . TYR A 1 2693 ? 202.755 234.939 229.969 1.00 0.05  ? 2693 TYR A N     1 
ATOM   9731  C  CA    . TYR A 1 2693 ? 201.649 233.994 229.916 1.00 0.09  ? 2693 TYR A CA    1 
ATOM   9732  C  C     . TYR A 1 2693 ? 201.838 233.034 228.750 1.00 0.27  ? 2693 TYR A C     1 
ATOM   9733  O  O     . TYR A 1 2693 ? 202.091 233.462 227.621 1.00 0.25  ? 2693 TYR A O     1 
ATOM   9734  C  CB    . TYR A 1 2693 ? 200.308 234.714 229.780 1.00 0.04  ? 2693 TYR A CB    1 
ATOM   9735  C  CG    . TYR A 1 2693 ? 199.747 235.231 231.081 1.00 0.03  ? 2693 TYR A CG    1 
ATOM   9736  C  CD1   . TYR A 1 2693 ? 199.119 234.376 231.976 1.00 0.03  ? 2693 TYR A CD1   1 
ATOM   9737  C  CD2   . TYR A 1 2693 ? 199.837 236.574 231.411 1.00 0.03  ? 2693 TYR A CD2   1 
ATOM   9738  C  CE1   . TYR A 1 2693 ? 198.604 234.845 233.165 1.00 0.07  ? 2693 TYR A CE1   1 
ATOM   9739  C  CE2   . TYR A 1 2693 ? 199.324 237.053 232.597 1.00 0.04  ? 2693 TYR A CE2   1 
ATOM   9740  C  CZ    . TYR A 1 2693 ? 198.709 236.186 233.470 1.00 0.07  ? 2693 TYR A CZ    1 
ATOM   9741  O  OH    . TYR A 1 2693 ? 198.198 236.668 234.653 1.00 0.05  ? 2693 TYR A OH    1 
ATOM   9742  N  N     . ARG A 1 2694 ? 201.709 231.741 229.030 1.00 0.92  ? 2694 ARG A N     1 
ATOM   9743  C  CA    . ARG A 1 2694 ? 201.693 230.718 227.992 1.00 0.88  ? 2694 ARG A CA    1 
ATOM   9744  C  C     . ARG A 1 2694 ? 200.290 230.672 227.402 1.00 1.35  ? 2694 ARG A C     1 
ATOM   9745  O  O     . ARG A 1 2694 ? 199.334 230.293 228.085 1.00 1.85  ? 2694 ARG A O     1 
ATOM   9746  C  CB    . ARG A 1 2694 ? 202.104 229.366 228.571 1.00 1.10  ? 2694 ARG A CB    1 
ATOM   9747  C  CG    . ARG A 1 2694 ? 202.461 228.318 227.529 1.00 2.23  ? 2694 ARG A CG    1 
ATOM   9748  C  CD    . ARG A 1 2694 ? 202.168 226.909 228.028 1.00 2.14  ? 2694 ARG A CD    1 
ATOM   9749  N  NE    . ARG A 1 2694 ? 203.265 226.329 228.789 1.00 2.52  ? 2694 ARG A NE    1 
ATOM   9750  C  CZ    . ARG A 1 2694 ? 203.116 225.633 229.909 1.00 3.14  ? 2694 ARG A CZ    1 
ATOM   9751  N  NH1   . ARG A 1 2694 ? 201.925 225.448 230.454 1.00 1.74  ? 2694 ARG A NH1   1 
ATOM   9752  N  NH2   . ARG A 1 2694 ? 204.187 225.109 230.494 1.00 4.65  ? 2694 ARG A NH2   1 
ATOM   9753  N  N     . THR A 1 2695 ? 200.158 231.064 226.132 1.00 1.62  ? 2695 THR A N     1 
ATOM   9754  C  CA    . THR A 1 2695 ? 198.836 231.253 225.545 1.00 1.62  ? 2695 THR A CA    1 
ATOM   9755  C  C     . THR A 1 2695 ? 198.106 229.945 225.280 1.00 2.58  ? 2695 THR A C     1 
ATOM   9756  O  O     . THR A 1 2695 ? 196.882 229.962 225.107 1.00 4.22  ? 2695 THR A O     1 
ATOM   9757  C  CB    . THR A 1 2695 ? 198.941 232.056 224.244 1.00 2.11  ? 2695 THR A CB    1 
ATOM   9758  O  OG1   . THR A 1 2695 ? 199.778 231.363 223.310 1.00 10.31 ? 2695 THR A OG1   1 
ATOM   9759  C  CG2   . THR A 1 2695 ? 199.525 233.432 224.516 1.00 1.83  ? 2695 THR A CG2   1 
ATOM   9760  N  N     . SER A 1 2696 ? 198.815 228.816 225.236 1.00 3.44  ? 2696 SER A N     1 
ATOM   9761  C  CA    . SER A 1 2696 ? 198.151 227.543 224.969 1.00 3.29  ? 2696 SER A CA    1 
ATOM   9762  C  C     . SER A 1 2696 ? 197.218 227.147 226.108 1.00 3.61  ? 2696 SER A C     1 
ATOM   9763  O  O     . SER A 1 2696 ? 196.117 226.640 225.865 1.00 9.24  ? 2696 SER A O     1 
ATOM   9764  C  CB    . SER A 1 2696 ? 199.189 226.449 224.718 1.00 7.25  ? 2696 SER A CB    1 
ATOM   9765  O  OG    . SER A 1 2696 ? 199.881 226.117 225.907 1.00 9.77  ? 2696 SER A OG    1 
ATOM   9766  N  N     . ASP A 1 2697 ? 197.637 227.362 227.354 1.00 2.21  ? 2697 ASP A N     1 
ATOM   9767  C  CA    . ASP A 1 2697 ? 196.836 226.984 228.512 1.00 2.10  ? 2697 ASP A CA    1 
ATOM   9768  C  C     . ASP A 1 2697 ? 196.510 228.163 229.421 1.00 1.97  ? 2697 ASP A C     1 
ATOM   9769  O  O     . ASP A 1 2697 ? 195.963 227.953 230.509 1.00 2.94  ? 2697 ASP A O     1 
ATOM   9770  C  CB    . ASP A 1 2697 ? 197.543 225.888 229.316 1.00 4.10  ? 2697 ASP A CB    1 
ATOM   9771  C  CG    . ASP A 1 2697 ? 198.910 226.314 229.809 1.00 6.25  ? 2697 ASP A CG    1 
ATOM   9772  O  OD1   . ASP A 1 2697 ? 199.368 227.411 229.430 1.00 4.07  ? 2697 ASP A OD1   1 
ATOM   9773  O  OD2   . ASP A 1 2697 ? 199.527 225.553 230.581 1.00 12.75 ? 2697 ASP A OD2   1 
ATOM   9774  N  N     . GLN A 1 2698 ? 196.838 229.388 229.008 1.00 2.02  ? 2698 GLN A N     1 
ATOM   9775  C  CA    . GLN A 1 2698 ? 196.532 230.594 229.782 1.00 1.39  ? 2698 GLN A CA    1 
ATOM   9776  C  C     . GLN A 1 2698 ? 197.171 230.545 231.168 1.00 1.43  ? 2698 GLN A C     1 
ATOM   9777  O  O     . GLN A 1 2698 ? 196.565 230.939 232.166 1.00 5.75  ? 2698 GLN A O     1 
ATOM   9778  C  CB    . GLN A 1 2698 ? 195.021 230.807 229.892 1.00 1.20  ? 2698 GLN A CB    1 
ATOM   9779  C  CG    . GLN A 1 2698 ? 194.429 231.697 228.827 1.00 0.33  ? 2698 GLN A CG    1 
ATOM   9780  C  CD    . GLN A 1 2698 ? 194.671 231.186 227.427 1.00 0.74  ? 2698 GLN A CD    1 
ATOM   9781  O  OE1   . GLN A 1 2698 ? 194.289 230.068 227.087 1.00 2.24  ? 2698 GLN A OE1   1 
ATOM   9782  N  NE2   . GLN A 1 2698 ? 195.302 232.008 226.600 1.00 2.37  ? 2698 GLN A NE2   1 
ATOM   9783  N  N     . THR A 1 2699 ? 198.405 230.060 231.230 1.00 1.85  ? 2699 THR A N     1 
ATOM   9784  C  CA    . THR A 1 2699 ? 199.099 229.826 232.489 1.00 0.98  ? 2699 THR A CA    1 
ATOM   9785  C  C     . THR A 1 2699 ? 200.299 230.755 232.589 1.00 0.32  ? 2699 THR A C     1 
ATOM   9786  O  O     . THR A 1 2699 ? 201.046 230.917 231.618 1.00 0.19  ? 2699 THR A O     1 
ATOM   9787  C  CB    . THR A 1 2699 ? 199.545 228.363 232.602 1.00 2.16  ? 2699 THR A CB    1 
ATOM   9788  O  OG1   . THR A 1 2699 ? 198.395 227.524 232.763 1.00 6.33  ? 2699 THR A OG1   1 
ATOM   9789  C  CG2   . THR A 1 2699 ? 200.476 228.165 233.788 1.00 1.71  ? 2699 THR A CG2   1 
ATOM   9790  N  N     . TRP A 1 2700 ? 200.473 231.366 233.756 1.00 0.18  ? 2700 TRP A N     1 
ATOM   9791  C  CA    . TRP A 1 2700 ? 201.634 232.214 233.988 1.00 0.11  ? 2700 TRP A CA    1 
ATOM   9792  C  C     . TRP A 1 2700 ? 202.897 231.367 234.075 1.00 0.13  ? 2700 TRP A C     1 
ATOM   9793  O  O     . TRP A 1 2700 ? 202.932 230.348 234.769 1.00 0.33  ? 2700 TRP A O     1 
ATOM   9794  C  CB    . TRP A 1 2700 ? 201.454 233.031 235.264 1.00 0.07  ? 2700 TRP A CB    1 
ATOM   9795  C  CG    . TRP A 1 2700 ? 202.641 233.876 235.592 1.00 0.06  ? 2700 TRP A CG    1 
ATOM   9796  C  CD1   . TRP A 1 2700 ? 203.601 233.615 236.524 1.00 0.04  ? 2700 TRP A CD1   1 
ATOM   9797  C  CD2   . TRP A 1 2700 ? 203.006 235.117 234.979 1.00 0.04  ? 2700 TRP A CD2   1 
ATOM   9798  N  NE1   . TRP A 1 2700 ? 204.535 234.618 236.534 1.00 0.04  ? 2700 TRP A NE1   1 
ATOM   9799  C  CE2   . TRP A 1 2700 ? 204.194 235.553 235.595 1.00 0.04  ? 2700 TRP A CE2   1 
ATOM   9800  C  CE3   . TRP A 1 2700 ? 202.442 235.903 233.971 1.00 0.02  ? 2700 TRP A CE3   1 
ATOM   9801  C  CZ2   . TRP A 1 2700 ? 204.826 236.742 235.239 1.00 0.08  ? 2700 TRP A CZ2   1 
ATOM   9802  C  CZ3   . TRP A 1 2700 ? 203.071 237.079 233.620 1.00 0.02  ? 2700 TRP A CZ3   1 
ATOM   9803  C  CH2   . TRP A 1 2700 ? 204.249 237.487 234.251 1.00 0.06  ? 2700 TRP A CH2   1 
ATOM   9804  N  N     . VAL A 1 2701 ? 203.937 231.798 233.368 1.00 0.08  ? 2701 VAL A N     1 
ATOM   9805  C  CA    . VAL A 1 2701 ? 205.231 231.130 233.362 1.00 0.21  ? 2701 VAL A CA    1 
ATOM   9806  C  C     . VAL A 1 2701 ? 206.246 232.077 233.982 1.00 0.07  ? 2701 VAL A C     1 
ATOM   9807  O  O     . VAL A 1 2701 ? 206.322 233.247 233.594 1.00 0.08  ? 2701 VAL A O     1 
ATOM   9808  C  CB    . VAL A 1 2701 ? 205.659 230.725 231.939 1.00 0.16  ? 2701 VAL A CB    1 
ATOM   9809  C  CG1   . VAL A 1 2701 ? 207.072 230.170 231.948 1.00 0.13  ? 2701 VAL A CG1   1 
ATOM   9810  C  CG2   . VAL A 1 2701 ? 204.686 229.713 231.359 1.00 0.28  ? 2701 VAL A CG2   1 
ATOM   9811  N  N     . LYS A 1 2702 ? 207.008 231.579 234.946 1.00 0.18  ? 2702 LYS A N     1 
ATOM   9812  C  CA    . LYS A 1 2702 ? 208.036 232.363 235.611 1.00 0.21  ? 2702 LYS A CA    1 
ATOM   9813  C  C     . LYS A 1 2702 ? 209.406 232.030 235.034 1.00 0.29  ? 2702 LYS A C     1 
ATOM   9814  O  O     . LYS A 1 2702 ? 209.759 230.859 234.880 1.00 0.21  ? 2702 LYS A O     1 
ATOM   9815  C  CB    . LYS A 1 2702 ? 208.031 232.108 237.117 1.00 0.36  ? 2702 LYS A CB    1 
ATOM   9816  C  CG    . LYS A 1 2702 ? 209.005 232.973 237.888 1.00 1.67  ? 2702 LYS A CG    1 
ATOM   9817  C  CD    . LYS A 1 2702 ? 208.896 232.735 239.383 1.00 3.22  ? 2702 LYS A CD    1 
ATOM   9818  C  CE    . LYS A 1 2702 ? 209.879 233.598 240.151 1.00 8.16  ? 2702 LYS A CE    1 
ATOM   9819  N  NZ    . LYS A 1 2702 ? 209.786 233.375 241.619 1.00 19.38 ? 2702 LYS A NZ    1 
ATOM   9820  N  N     . LEU A 1 2703 ? 210.170 233.070 234.718 1.00 0.63  ? 2703 LEU A N     1 
ATOM   9821  C  CA    . LEU A 1 2703 ? 211.518 232.896 234.203 1.00 0.28  ? 2703 LEU A CA    1 
ATOM   9822  C  C     . LEU A 1 2703 ? 212.501 232.638 235.336 1.00 0.23  ? 2703 LEU A C     1 
ATOM   9823  O  O     . LEU A 1 2703 ? 212.371 233.175 236.439 1.00 0.94  ? 2703 LEU A O     1 
ATOM   9824  C  CB    . LEU A 1 2703 ? 211.958 234.130 233.417 1.00 0.50  ? 2703 LEU A CB    1 
ATOM   9825  C  CG    . LEU A 1 2703 ? 211.229 234.457 232.117 1.00 0.47  ? 2703 LEU A CG    1 
ATOM   9826  C  CD1   . LEU A 1 2703 ? 211.816 235.713 231.501 1.00 1.86  ? 2703 LEU A CD1   1 
ATOM   9827  C  CD2   . LEU A 1 2703 ? 211.309 233.294 231.141 1.00 0.44  ? 2703 LEU A CD2   1 
ATOM   9828  N  N     . GLU A 1 2704 ? 213.493 231.799 235.053 1.00 0.20  ? 2704 GLU A N     1 
ATOM   9829  C  CA    . GLU A 1 2704 ? 214.584 231.545 235.983 1.00 0.34  ? 2704 GLU A CA    1 
ATOM   9830  C  C     . GLU A 1 2704 ? 215.878 231.439 235.194 1.00 0.39  ? 2704 GLU A C     1 
ATOM   9831  O  O     . GLU A 1 2704 ? 215.934 230.728 234.187 1.00 0.45  ? 2704 GLU A O     1 
ATOM   9832  C  CB    . GLU A 1 2704 ? 214.340 230.269 236.800 1.00 0.97  ? 2704 GLU A CB    1 
ATOM   9833  C  CG    . GLU A 1 2704 ? 215.580 229.722 237.487 1.00 4.59  ? 2704 GLU A CG    1 
ATOM   9834  C  CD    . GLU A 1 2704 ? 215.408 228.292 237.960 1.00 13.76 ? 2704 GLU A CD    1 
ATOM   9835  O  OE1   . GLU A 1 2704 ? 214.527 228.048 238.810 1.00 18.01 ? 2704 GLU A OE1   1 
ATOM   9836  O  OE2   . GLU A 1 2704 ? 216.154 227.412 237.485 1.00 13.85 ? 2704 GLU A OE2   1 
ATOM   9837  N  N     . ARG A 1 2705 ? 216.907 232.158 235.651 1.00 0.36  ? 2705 ARG A N     1 
ATOM   9838  C  CA    . ARG A 1 2705 ? 218.232 232.153 235.023 1.00 0.22  ? 2705 ARG A CA    1 
ATOM   9839  C  C     . ARG A 1 2705 ? 218.171 232.557 233.552 1.00 0.25  ? 2705 ARG A C     1 
ATOM   9840  O  O     . ARG A 1 2705 ? 218.852 231.982 232.702 1.00 0.51  ? 2705 ARG A O     1 
ATOM   9841  C  CB    . ARG A 1 2705 ? 218.920 230.796 235.185 1.00 0.39  ? 2705 ARG A CB    1 
ATOM   9842  C  CG    . ARG A 1 2705 ? 219.263 230.437 236.620 1.00 0.32  ? 2705 ARG A CG    1 
ATOM   9843  C  CD    . ARG A 1 2705 ? 219.890 229.056 236.718 1.00 1.74  ? 2705 ARG A CD    1 
ATOM   9844  N  NE    . ARG A 1 2705 ? 218.982 227.996 236.293 1.00 1.50  ? 2705 ARG A NE    1 
ATOM   9845  C  CZ    . ARG A 1 2705 ? 219.208 227.178 235.276 1.00 2.48  ? 2705 ARG A CZ    1 
ATOM   9846  N  NH1   . ARG A 1 2705 ? 220.297 227.284 234.532 1.00 2.77  ? 2705 ARG A NH1   1 
ATOM   9847  N  NH2   . ARG A 1 2705 ? 218.318 226.232 234.993 1.00 3.85  ? 2705 ARG A NH2   1 
ATOM   9848  N  N     . ILE A 1 2706 ? 217.351 233.559 233.246 1.00 0.18  ? 2706 ILE A N     1 
ATOM   9849  C  CA    . ILE A 1 2706 ? 217.238 234.105 231.899 1.00 0.17  ? 2706 ILE A CA    1 
ATOM   9850  C  C     . ILE A 1 2706 ? 217.336 235.622 231.987 1.00 0.15  ? 2706 ILE A C     1 
ATOM   9851  O  O     . ILE A 1 2706 ? 216.533 236.257 232.679 1.00 0.60  ? 2706 ILE A O     1 
ATOM   9852  C  CB    . ILE A 1 2706 ? 215.928 233.678 231.213 1.00 0.31  ? 2706 ILE A CB    1 
ATOM   9853  C  CG1   . ILE A 1 2706 ? 215.916 232.165 230.978 1.00 0.28  ? 2706 ILE A CG1   1 
ATOM   9854  C  CG2   . ILE A 1 2706 ? 215.721 234.443 229.922 1.00 0.19  ? 2706 ILE A CG2   1 
ATOM   9855  C  CD1   . ILE A 1 2706 ? 214.577 231.616 230.554 1.00 0.43  ? 2706 ILE A CD1   1 
ATOM   9856  N  N     . GLN A 1 2707 ? 218.314 236.198 231.296 1.00 0.26  ? 2707 GLN A N     1 
ATOM   9857  C  CA    . GLN A 1 2707 ? 218.487 237.640 231.228 1.00 0.13  ? 2707 GLN A CA    1 
ATOM   9858  C  C     . GLN A 1 2707 ? 218.528 238.085 229.772 1.00 0.19  ? 2707 GLN A C     1 
ATOM   9859  O  O     . GLN A 1 2707 ? 218.738 237.283 228.859 1.00 0.33  ? 2707 GLN A O     1 
ATOM   9860  C  CB    . GLN A 1 2707 ? 219.760 238.101 231.951 1.00 0.19  ? 2707 GLN A CB    1 
ATOM   9861  C  CG    . GLN A 1 2707 ? 221.015 237.334 231.587 1.00 0.26  ? 2707 GLN A CG    1 
ATOM   9862  C  CD    . GLN A 1 2707 ? 222.182 237.684 232.485 1.00 0.74  ? 2707 GLN A CD    1 
ATOM   9863  O  OE1   . GLN A 1 2707 ? 222.695 236.837 233.214 1.00 6.84  ? 2707 GLN A OE1   1 
ATOM   9864  N  NE2   . GLN A 1 2707 ? 222.610 238.937 232.438 1.00 0.41  ? 2707 GLN A NE2   1 
ATOM   9865  N  N     . PHE A 1 2708 ? 218.329 239.384 229.566 1.00 0.49  ? 2708 PHE A N     1 
ATOM   9866  C  CA    . PHE A 1 2708 ? 218.203 239.958 228.235 1.00 0.10  ? 2708 PHE A CA    1 
ATOM   9867  C  C     . PHE A 1 2708 ? 219.244 241.049 228.024 1.00 0.09  ? 2708 PHE A C     1 
ATOM   9868  O  O     . PHE A 1 2708 ? 219.494 241.865 228.915 1.00 0.14  ? 2708 PHE A O     1 
ATOM   9869  C  CB    . PHE A 1 2708 ? 216.798 240.530 228.020 1.00 0.12  ? 2708 PHE A CB    1 
ATOM   9870  C  CG    . PHE A 1 2708 ? 215.701 239.538 228.267 1.00 0.50  ? 2708 PHE A CG    1 
ATOM   9871  C  CD1   . PHE A 1 2708 ? 215.156 239.387 229.530 1.00 0.50  ? 2708 PHE A CD1   1 
ATOM   9872  C  CD2   . PHE A 1 2708 ? 215.220 238.749 227.237 1.00 0.93  ? 2708 PHE A CD2   1 
ATOM   9873  C  CE1   . PHE A 1 2708 ? 214.152 238.471 229.763 1.00 0.50  ? 2708 PHE A CE1   1 
ATOM   9874  C  CE2   . PHE A 1 2708 ? 214.213 237.832 227.465 1.00 1.02  ? 2708 PHE A CE2   1 
ATOM   9875  C  CZ    . PHE A 1 2708 ? 213.680 237.695 228.728 1.00 0.48  ? 2708 PHE A CZ    1 
ATOM   9876  N  N     . VAL A 1 2709 ? 219.854 241.045 226.845 1.00 0.16  ? 2709 VAL A N     1 
ATOM   9877  C  CA    . VAL A 1 2709 ? 220.742 242.112 226.402 1.00 0.03  ? 2709 VAL A CA    1 
ATOM   9878  C  C     . VAL A 1 2709 ? 220.262 242.574 225.036 1.00 0.08  ? 2709 VAL A C     1 
ATOM   9879  O  O     . VAL A 1 2709 ? 220.009 241.752 224.150 1.00 0.21  ? 2709 VAL A O     1 
ATOM   9880  C  CB    . VAL A 1 2709 ? 222.212 241.657 226.339 1.00 0.07  ? 2709 VAL A CB    1 
ATOM   9881  C  CG1   . VAL A 1 2709 ? 223.066 242.708 225.651 1.00 0.06  ? 2709 VAL A CG1   1 
ATOM   9882  C  CG2   . VAL A 1 2709 ? 222.742 241.380 227.731 1.00 0.08  ? 2709 VAL A CG2   1 
ATOM   9883  N  N     . GLY A 1 2710 ? 220.131 243.885 224.868 1.00 0.11  ? 2710 GLY A N     1 
ATOM   9884  C  CA    . GLY A 1 2710 ? 219.701 244.469 223.614 1.00 0.06  ? 2710 GLY A CA    1 
ATOM   9885  C  C     . GLY A 1 2710 ? 220.830 245.218 222.936 1.00 0.05  ? 2710 GLY A C     1 
ATOM   9886  O  O     . GLY A 1 2710 ? 221.704 245.782 223.594 1.00 0.04  ? 2710 GLY A O     1 
ATOM   9887  N  N     . ALA A 1 2711 ? 220.821 245.194 221.611 1.00 0.27  ? 2711 ALA A N     1 
ATOM   9888  C  CA    . ALA A 1 2711 ? 221.661 246.060 220.800 1.00 0.16  ? 2711 ALA A CA    1 
ATOM   9889  C  C     . ALA A 1 2711 ? 220.772 246.747 219.781 1.00 0.20  ? 2711 ALA A C     1 
ATOM   9890  O  O     . ALA A 1 2711 ? 219.741 246.208 219.378 1.00 0.38  ? 2711 ALA A O     1 
ATOM   9891  C  CB    . ALA A 1 2711 ? 222.785 245.291 220.098 1.00 0.14  ? 2711 ALA A CB    1 
ATOM   9892  N  N     . CYS A 1 2712 ? 221.162 247.951 219.383 1.00 0.27  ? 2712 CYS A N     1 
ATOM   9893  C  CA    . CYS A 1 2712 ? 220.333 248.723 218.472 1.00 0.38  ? 2712 CYS A CA    1 
ATOM   9894  C  C     . CYS A 1 2712 ? 221.137 249.900 217.946 1.00 0.34  ? 2712 CYS A C     1 
ATOM   9895  O  O     . CYS A 1 2712 ? 222.176 250.272 218.497 1.00 0.23  ? 2712 CYS A O     1 
ATOM   9896  C  CB    . CYS A 1 2712 ? 219.056 249.214 219.156 1.00 0.23  ? 2712 CYS A CB    1 
ATOM   9897  S  SG    . CYS A 1 2712 ? 219.340 250.313 220.544 1.00 0.58  ? 2712 CYS A SG    1 
ATOM   9898  N  N     . ASN A 1 2713 ? 220.645 250.467 216.875 1.00 0.90  ? 2713 ASN A N     1 
ATOM   9899  C  CA    . ASN A 1 2713 ? 221.094 251.738 216.343 1.00 0.79  ? 2713 ASN A CA    1 
ATOM   9900  C  C     . ASN A 1 2713 ? 220.297 252.866 216.982 1.00 1.10  ? 2713 ASN A C     1 
ATOM   9901  O  O     . ASN A 1 2713 ? 219.225 252.632 217.548 1.00 1.54  ? 2713 ASN A O     1 
ATOM   9902  C  CB    . ASN A 1 2713 ? 220.936 251.745 214.826 1.00 2.55  ? 2713 ASN A CB    1 
ATOM   9903  C  CG    . ASN A 1 2713 ? 221.888 250.784 214.138 1.00 0.71  ? 2713 ASN A CG    1 
ATOM   9904  O  OD1   . ASN A 1 2713 ? 221.717 250.456 212.966 1.00 1.59  ? 2713 ASN A OD1   1 
ATOM   9905  N  ND2   . ASN A 1 2713 ? 222.901 250.331 214.867 1.00 0.11  ? 2713 ASN A ND2   1 
ATOM   9906  N  N     . PRO A 1 2714 ? 220.800 254.097 216.938 1.00 2.29  ? 2714 PRO A N     1 
ATOM   9907  C  CA    . PRO A 1 2714 ? 220.074 255.221 217.544 1.00 1.34  ? 2714 PRO A CA    1 
ATOM   9908  C  C     . PRO A 1 2714 ? 218.676 255.352 216.969 1.00 1.16  ? 2714 PRO A C     1 
ATOM   9909  O  O     . PRO A 1 2714 ? 218.466 255.127 215.768 1.00 4.89  ? 2714 PRO A O     1 
ATOM   9910  C  CB    . PRO A 1 2714 ? 220.944 256.430 217.183 1.00 2.68  ? 2714 PRO A CB    1 
ATOM   9911  C  CG    . PRO A 1 2714 ? 222.316 255.867 217.113 1.00 2.18  ? 2714 PRO A CG    1 
ATOM   9912  C  CD    . PRO A 1 2714 ? 222.165 254.485 216.535 1.00 1.31  ? 2714 PRO A CD    1 
ATOM   9913  N  N     . PRO A 1 2715 ? 217.693 255.705 217.800 1.00 1.83  ? 2715 PRO A N     1 
ATOM   9914  C  CA    . PRO A 1 2715 ? 216.300 255.739 217.322 1.00 1.46  ? 2715 PRO A CA    1 
ATOM   9915  C  C     . PRO A 1 2715 ? 216.058 256.746 216.214 1.00 2.29  ? 2715 PRO A C     1 
ATOM   9916  O  O     . PRO A 1 2715 ? 215.051 256.629 215.505 1.00 3.69  ? 2715 PRO A O     1 
ATOM   9917  C  CB    . PRO A 1 2715 ? 215.505 256.092 218.587 1.00 1.25  ? 2715 PRO A CB    1 
ATOM   9918  C  CG    . PRO A 1 2715 ? 216.495 256.742 219.491 1.00 0.78  ? 2715 PRO A CG    1 
ATOM   9919  C  CD    . PRO A 1 2715 ? 217.795 256.054 219.226 1.00 1.46  ? 2715 PRO A CD    1 
ATOM   9920  N  N     . THR A 1 2716 ? 216.941 257.728 216.042 1.00 2.84  ? 2716 THR A N     1 
ATOM   9921  C  CA    . THR A 1 2716 ? 216.807 258.688 214.955 1.00 4.62  ? 2716 THR A CA    1 
ATOM   9922  C  C     . THR A 1 2716 ? 217.147 258.096 213.593 1.00 5.42  ? 2716 THR A C     1 
ATOM   9923  O  O     . THR A 1 2716 ? 216.822 258.713 212.574 1.00 10.99 ? 2716 THR A O     1 
ATOM   9924  C  CB    . THR A 1 2716 ? 217.693 259.905 215.226 1.00 6.42  ? 2716 THR A CB    1 
ATOM   9925  O  OG1   . THR A 1 2716 ? 219.052 259.484 215.390 1.00 10.56 ? 2716 THR A OG1   1 
ATOM   9926  C  CG2   . THR A 1 2716 ? 217.235 260.622 216.486 1.00 4.74  ? 2716 THR A CG2   1 
ATOM   9927  N  N     . ASP A 1 2717 ? 217.782 256.928 213.547 1.00 3.42  ? 2717 ASP A N     1 
ATOM   9928  C  CA    . ASP A 1 2717 ? 218.121 256.308 212.277 1.00 4.45  ? 2717 ASP A CA    1 
ATOM   9929  C  C     . ASP A 1 2717 ? 216.863 255.790 211.579 1.00 4.55  ? 2717 ASP A C     1 
ATOM   9930  O  O     . ASP A 1 2717 ? 215.879 255.444 212.236 1.00 3.18  ? 2717 ASP A O     1 
ATOM   9931  C  CB    . ASP A 1 2717 ? 219.110 255.166 212.489 1.00 6.04  ? 2717 ASP A CB    1 
ATOM   9932  C  CG    . ASP A 1 2717 ? 220.425 255.637 213.072 1.00 9.87  ? 2717 ASP A CG    1 
ATOM   9933  O  OD1   . ASP A 1 2717 ? 220.563 256.851 213.326 1.00 7.12  ? 2717 ASP A OD1   1 
ATOM   9934  O  OD2   . ASP A 1 2717 ? 221.324 254.794 213.272 1.00 14.86 ? 2717 ASP A OD2   1 
ATOM   9935  N  N     . PRO A 1 2718 ? 216.867 255.741 210.246 1.00 6.32  ? 2718 PRO A N     1 
ATOM   9936  C  CA    . PRO A 1 2718 ? 215.675 255.280 209.519 1.00 4.62  ? 2718 PRO A CA    1 
ATOM   9937  C  C     . PRO A 1 2718 ? 215.322 253.840 209.865 1.00 2.61  ? 2718 PRO A C     1 
ATOM   9938  O  O     . PRO A 1 2718 ? 216.194 252.979 209.996 1.00 4.55  ? 2718 PRO A O     1 
ATOM   9939  C  CB    . PRO A 1 2718 ? 216.078 255.436 208.049 1.00 4.03  ? 2718 PRO A CB    1 
ATOM   9940  C  CG    . PRO A 1 2718 ? 217.569 255.401 208.064 1.00 4.15  ? 2718 PRO A CG    1 
ATOM   9941  C  CD    . PRO A 1 2718 ? 217.956 256.106 209.324 1.00 3.84  ? 2718 PRO A CD    1 
ATOM   9942  N  N     . GLY A 1 2719 ? 214.022 253.586 210.006 1.00 1.70  ? 2719 GLY A N     1 
ATOM   9943  C  CA    . GLY A 1 2719 ? 213.522 252.293 210.409 1.00 0.78  ? 2719 GLY A CA    1 
ATOM   9944  C  C     . GLY A 1 2719 ? 213.543 252.038 211.901 1.00 1.22  ? 2719 GLY A C     1 
ATOM   9945  O  O     . GLY A 1 2719 ? 212.962 251.045 212.352 1.00 1.40  ? 2719 GLY A O     1 
ATOM   9946  N  N     . ARG A 1 2720 ? 214.183 252.904 212.679 1.00 1.09  ? 2720 ARG A N     1 
ATOM   9947  C  CA    . ARG A 1 2720 ? 214.317 252.716 214.115 1.00 0.94  ? 2720 ARG A CA    1 
ATOM   9948  C  C     . ARG A 1 2720 ? 213.251 253.514 214.851 1.00 1.00  ? 2720 ARG A C     1 
ATOM   9949  O  O     . ARG A 1 2720 ? 212.977 254.669 214.514 1.00 3.84  ? 2720 ARG A O     1 
ATOM   9950  C  CB    . ARG A 1 2720 ? 215.709 253.133 214.595 1.00 1.49  ? 2720 ARG A CB    1 
ATOM   9951  C  CG    . ARG A 1 2720 ? 216.817 252.094 214.418 1.00 0.94  ? 2720 ARG A CG    1 
ATOM   9952  C  CD    . ARG A 1 2720 ? 216.987 251.626 212.990 1.00 2.05  ? 2720 ARG A CD    1 
ATOM   9953  N  NE    . ARG A 1 2720 ? 218.008 250.592 212.875 1.00 5.07  ? 2720 ARG A NE    1 
ATOM   9954  C  CZ    . ARG A 1 2720 ? 218.314 249.965 211.748 1.00 3.75  ? 2720 ARG A CZ    1 
ATOM   9955  N  NH1   . ARG A 1 2720 ? 217.686 250.232 210.617 1.00 4.01  ? 2720 ARG A NH1   1 
ATOM   9956  N  NH2   . ARG A 1 2720 ? 219.269 249.039 211.761 1.00 3.07  ? 2720 ARG A NH2   1 
ATOM   9957  N  N     . LYS A 1 2721 ? 212.646 252.891 215.847 1.00 1.23  ? 2721 LYS A N     1 
ATOM   9958  C  CA    . LYS A 1 2721 ? 211.644 253.551 216.662 1.00 1.74  ? 2721 LYS A CA    1 
ATOM   9959  C  C     . LYS A 1 2721 ? 212.165 253.776 218.076 1.00 0.76  ? 2721 LYS A C     1 
ATOM   9960  O  O     . LYS A 1 2721 ? 212.957 252.979 218.584 1.00 0.41  ? 2721 LYS A O     1 
ATOM   9961  C  CB    . LYS A 1 2721 ? 210.346 252.735 216.727 1.00 1.60  ? 2721 LYS A CB    1 
ATOM   9962  C  CG    . LYS A 1 2721 ? 209.401 252.947 215.553 1.00 2.69  ? 2721 LYS A CG    1 
ATOM   9963  C  CD    . LYS A 1 2721 ? 209.889 252.281 214.280 1.00 2.83  ? 2721 LYS A CD    1 
ATOM   9964  C  CE    . LYS A 1 2721 ? 209.822 250.771 214.375 1.00 1.32  ? 2721 LYS A CE    1 
ATOM   9965  N  NZ    . LYS A 1 2721 ? 210.236 250.126 213.101 1.00 1.09  ? 2721 LYS A NZ    1 
ATOM   9966  N  N     . PRO A 1 2722 ? 211.756 254.863 218.729 1.00 2.49  ? 2722 PRO A N     1 
ATOM   9967  C  CA    . PRO A 1 2722 ? 212.125 255.054 220.136 1.00 0.46  ? 2722 PRO A CA    1 
ATOM   9968  C  C     . PRO A 1 2722 ? 211.537 253.958 221.011 1.00 0.33  ? 2722 PRO A C     1 
ATOM   9969  O  O     . PRO A 1 2722 ? 210.402 253.519 220.816 1.00 0.44  ? 2722 PRO A O     1 
ATOM   9970  C  CB    . PRO A 1 2722 ? 211.537 256.426 220.476 1.00 0.31  ? 2722 PRO A CB    1 
ATOM   9971  C  CG    . PRO A 1 2722 ? 210.461 256.640 219.469 1.00 0.68  ? 2722 PRO A CG    1 
ATOM   9972  C  CD    . PRO A 1 2722 ? 210.940 255.975 218.218 1.00 1.18  ? 2722 PRO A CD    1 
ATOM   9973  N  N     . LEU A 1 2723 ? 212.325 253.518 221.984 1.00 0.35  ? 2723 LEU A N     1 
ATOM   9974  C  CA    . LEU A 1 2723 ? 211.860 252.506 222.917 1.00 0.18  ? 2723 LEU A CA    1 
ATOM   9975  C  C     . LEU A 1 2723 ? 210.892 253.117 223.923 1.00 0.24  ? 2723 LEU A C     1 
ATOM   9976  O  O     . LEU A 1 2723 ? 211.007 254.286 224.301 1.00 0.24  ? 2723 LEU A O     1 
ATOM   9977  C  CB    . LEU A 1 2723 ? 213.045 251.865 223.637 1.00 0.15  ? 2723 LEU A CB    1 
ATOM   9978  C  CG    . LEU A 1 2723 ? 213.872 250.890 222.792 1.00 0.14  ? 2723 LEU A CG    1 
ATOM   9979  C  CD1   . LEU A 1 2723 ? 215.063 250.361 223.573 1.00 0.08  ? 2723 LEU A CD1   1 
ATOM   9980  C  CD2   . LEU A 1 2723 ? 213.005 249.745 222.293 1.00 0.08  ? 2723 LEU A CD2   1 
ATOM   9981  N  N     . SER A 1 2724 ? 209.918 252.313 224.344 1.00 0.41  ? 2724 SER A N     1 
ATOM   9982  C  CA    . SER A 1 2724 ? 208.941 252.763 225.325 1.00 0.40  ? 2724 SER A CA    1 
ATOM   9983  C  C     . SER A 1 2724 ? 209.625 253.133 226.636 1.00 0.35  ? 2724 SER A C     1 
ATOM   9984  O  O     . SER A 1 2724 ? 210.528 252.434 227.103 1.00 0.31  ? 2724 SER A O     1 
ATOM   9985  C  CB    . SER A 1 2724 ? 207.895 251.673 225.562 1.00 0.37  ? 2724 SER A CB    1 
ATOM   9986  O  OG    . SER A 1 2724 ? 207.028 252.009 226.629 1.00 3.17  ? 2724 SER A OG    1 
ATOM   9987  N  N     . HIS A 1 2725 ? 209.165 254.222 227.259 1.00 0.81  ? 2725 HIS A N     1 
ATOM   9988  C  CA    . HIS A 1 2725 ? 209.772 254.687 228.538 1.00 0.46  ? 2725 HIS A CA    1 
ATOM   9989  C  C     . HIS A 1 2725 ? 209.508 253.658 229.646 1.00 0.19  ? 2725 HIS A C     1 
ATOM   9990  O  O     . HIS A 1 2725 ? 210.301 253.594 230.606 1.00 0.12  ? 2725 HIS A O     1 
ATOM   9991  C  CB    . HIS A 1 2725 ? 209.265 256.090 228.891 1.00 1.83  ? 2725 HIS A CB    1 
ATOM   9992  C  CG    . HIS A 1 2725 ? 209.781 257.165 227.998 1.00 2.21  ? 2725 HIS A CG    1 
ATOM   9993  N  ND1   . HIS A 1 2725 ? 209.895 258.478 228.398 1.00 3.69  ? 2725 HIS A ND1   1 
ATOM   9994  C  CD2   . HIS A 1 2725 ? 210.201 257.128 226.728 1.00 3.13  ? 2725 HIS A CD2   1 
ATOM   9995  C  CE1   . HIS A 1 2725 ? 210.376 259.200 227.398 1.00 3.42  ? 2725 HIS A CE1   1 
ATOM   9996  N  NE2   . HIS A 1 2725 ? 210.571 258.398 226.374 1.00 3.89  ? 2725 HIS A NE2   1 
ATOM   9997  N  N     . ARG A 1 2726 ? 208.435 252.874 229.513 1.00 0.16  ? 2726 ARG A N     1 
ATOM   9998  C  CA    . ARG A 1 2726 ? 208.107 251.832 230.522 1.00 0.34  ? 2726 ARG A CA    1 
ATOM   9999  C  C     . ARG A 1 2726 ? 209.090 250.656 230.387 1.00 0.20  ? 2726 ARG A C     1 
ATOM   10000 O  O     . ARG A 1 2726 ? 209.243 249.901 231.367 1.00 0.59  ? 2726 ARG A O     1 
ATOM   10001 C  CB    . ARG A 1 2726 ? 206.646 251.394 230.385 1.00 0.54  ? 2726 ARG A CB    1 
ATOM   10002 C  CG    . ARG A 1 2726 ? 205.686 252.004 231.395 1.00 0.15  ? 2726 ARG A CG    1 
ATOM   10003 C  CD    . ARG A 1 2726 ? 204.289 251.445 231.195 1.00 0.25  ? 2726 ARG A CD    1 
ATOM   10004 N  NE    . ARG A 1 2726 ? 203.455 251.570 232.396 1.00 0.12  ? 2726 ARG A NE    1 
ATOM   10005 C  CZ    . ARG A 1 2726 ? 202.209 251.136 232.483 1.00 0.09  ? 2726 ARG A CZ    1 
ATOM   10006 N  NH1   . ARG A 1 2726 ? 201.617 250.610 231.426 1.00 0.82  ? 2726 ARG A NH1   1 
ATOM   10007 N  NH2   . ARG A 1 2726 ? 201.559 251.226 233.628 1.00 0.07  ? 2726 ARG A NH2   1 
ATOM   10008 N  N     . PHE A 1 2727 ? 209.729 250.511 229.225 1.00 0.13  ? 2727 PHE A N     1 
ATOM   10009 C  CA    . PHE A 1 2727 ? 210.746 249.445 229.031 1.00 0.09  ? 2727 PHE A CA    1 
ATOM   10010 C  C     . PHE A 1 2727 ? 212.120 249.982 229.411 1.00 0.12  ? 2727 PHE A C     1 
ATOM   10011 O  O     . PHE A 1 2727 ? 212.958 249.191 229.882 1.00 0.13  ? 2727 PHE A O     1 
ATOM   10012 C  CB    . PHE A 1 2727 ? 210.715 248.972 227.574 1.00 0.04  ? 2727 PHE A CB    1 
ATOM   10013 C  CG    . PHE A 1 2727 ? 211.897 248.121 227.129 1.00 0.07  ? 2727 PHE A CG    1 
ATOM   10014 C  CD1   . PHE A 1 2727 ? 213.038 248.711 226.599 1.00 0.04  ? 2727 PHE A CD1   1 
ATOM   10015 C  CD2   . PHE A 1 2727 ? 211.857 246.734 227.233 1.00 0.03  ? 2727 PHE A CD2   1 
ATOM   10016 C  CE1   . PHE A 1 2727 ? 214.112 247.934 226.192 1.00 0.04  ? 2727 PHE A CE1   1 
ATOM   10017 C  CE2   . PHE A 1 2727 ? 212.934 245.965 226.822 1.00 0.03  ? 2727 PHE A CE2   1 
ATOM   10018 C  CZ    . PHE A 1 2727 ? 214.056 246.565 226.303 1.00 0.02  ? 2727 PHE A CZ    1 
ATOM   10019 N  N     . LEU A 1 2728 ? 212.342 251.287 229.234 1.00 0.05  ? 2728 LEU A N     1 
ATOM   10020 C  CA    . LEU A 1 2728 ? 213.674 251.832 229.469 1.00 0.08  ? 2728 LEU A CA    1 
ATOM   10021 C  C     . LEU A 1 2728 ? 213.996 251.975 230.952 1.00 0.31  ? 2728 LEU A C     1 
ATOM   10022 O  O     . LEU A 1 2728 ? 215.175 252.003 231.318 1.00 0.43  ? 2728 LEU A O     1 
ATOM   10023 C  CB    . LEU A 1 2728 ? 213.822 253.181 228.763 1.00 0.30  ? 2728 LEU A CB    1 
ATOM   10024 C  CG    . LEU A 1 2728 ? 213.876 253.157 227.233 1.00 0.20  ? 2728 LEU A CG    1 
ATOM   10025 C  CD1   . LEU A 1 2728 ? 214.084 254.548 226.673 1.00 0.37  ? 2728 LEU A CD1   1 
ATOM   10026 C  CD2   . LEU A 1 2728 ? 214.974 252.223 226.754 1.00 0.10  ? 2728 LEU A CD2   1 
ATOM   10027 N  N     . ARG A 1 2729 ? 212.981 252.073 231.820 1.00 0.88  ? 2729 ARG A N     1 
ATOM   10028 C  CA    . ARG A 1 2729 ? 213.259 252.230 233.247 1.00 0.32  ? 2729 ARG A CA    1 
ATOM   10029 C  C     . ARG A 1 2729 ? 213.980 251.018 233.816 1.00 0.45  ? 2729 ARG A C     1 
ATOM   10030 O  O     . ARG A 1 2729 ? 214.663 251.128 234.839 1.00 1.03  ? 2729 ARG A O     1 
ATOM   10031 C  CB    . ARG A 1 2729 ? 211.971 252.488 234.031 1.00 0.64  ? 2729 ARG A CB    1 
ATOM   10032 C  CG    . ARG A 1 2729 ? 210.983 251.334 234.036 1.00 1.34  ? 2729 ARG A CG    1 
ATOM   10033 C  CD    . ARG A 1 2729 ? 209.732 251.706 234.810 1.00 2.24  ? 2729 ARG A CD    1 
ATOM   10034 N  NE    . ARG A 1 2729 ? 209.965 251.903 236.237 1.00 4.86  ? 2729 ARG A NE    1 
ATOM   10035 C  CZ    . ARG A 1 2729 ? 209.971 250.927 237.134 1.00 3.67  ? 2729 ARG A CZ    1 
ATOM   10036 N  NH1   . ARG A 1 2729 ? 209.678 249.684 236.805 1.00 9.72  ? 2729 ARG A NH1   1 
ATOM   10037 N  NH2   . ARG A 1 2729 ? 210.250 251.208 238.402 1.00 6.81  ? 2729 ARG A NH2   1 
ATOM   10038 N  N     . HIS A 1 2730 ? 213.843 249.861 233.176 1.00 0.34  ? 2730 HIS A N     1 
ATOM   10039 C  CA    . HIS A 1 2730 ? 214.509 248.646 233.613 1.00 0.35  ? 2730 HIS A CA    1 
ATOM   10040 C  C     . HIS A 1 2730 ? 215.852 248.422 232.941 1.00 0.38  ? 2730 HIS A C     1 
ATOM   10041 O  O     . HIS A 1 2730 ? 216.636 247.597 233.420 1.00 0.78  ? 2730 HIS A O     1 
ATOM   10042 C  CB    . HIS A 1 2730 ? 213.618 247.433 233.342 1.00 0.26  ? 2730 HIS A CB    1 
ATOM   10043 C  CG    . HIS A 1 2730 ? 212.275 247.527 233.985 1.00 0.80  ? 2730 HIS A CG    1 
ATOM   10044 N  ND1   . HIS A 1 2730 ? 211.159 247.970 233.312 1.00 0.63  ? 2730 HIS A ND1   1 
ATOM   10045 C  CD2   . HIS A 1 2730 ? 211.874 247.251 235.245 1.00 0.75  ? 2730 HIS A CD2   1 
ATOM   10046 C  CE1   . HIS A 1 2730 ? 210.124 247.958 234.130 1.00 0.94  ? 2730 HIS A CE1   1 
ATOM   10047 N  NE2   . HIS A 1 2730 ? 210.532 247.525 235.309 1.00 1.06  ? 2730 HIS A NE2   1 
ATOM   10048 N  N     . VAL A 1 2731 ? 216.136 249.130 231.858 1.00 0.34  ? 2731 VAL A N     1 
ATOM   10049 C  CA    . VAL A 1 2731 ? 217.214 248.784 230.946 1.00 0.27  ? 2731 VAL A CA    1 
ATOM   10050 C  C     . VAL A 1 2731 ? 218.181 249.958 230.860 1.00 0.19  ? 2731 VAL A C     1 
ATOM   10051 O  O     . VAL A 1 2731 ? 217.938 250.926 230.140 1.00 0.78  ? 2731 VAL A O     1 
ATOM   10052 C  CB    . VAL A 1 2731 ? 216.665 248.417 229.555 1.00 0.21  ? 2731 VAL A CB    1 
ATOM   10053 C  CG1   . VAL A 1 2731 ? 217.789 248.042 228.634 1.00 0.14  ? 2731 VAL A CG1   1 
ATOM   10054 C  CG2   . VAL A 1 2731 ? 215.655 247.283 229.664 1.00 0.13  ? 2731 VAL A CG2   1 
ATOM   10055 N  N     . PRO A 1 2732 ? 219.294 249.910 231.591 1.00 0.13  ? 2732 PRO A N     1 
ATOM   10056 C  CA    . PRO A 1 2732 ? 220.349 250.908 231.385 1.00 0.18  ? 2732 PRO A CA    1 
ATOM   10057 C  C     . PRO A 1 2732 ? 220.912 250.834 229.974 1.00 0.13  ? 2732 PRO A C     1 
ATOM   10058 O  O     . PRO A 1 2732 ? 221.018 249.762 229.375 1.00 0.27  ? 2732 PRO A O     1 
ATOM   10059 C  CB    . PRO A 1 2732 ? 221.407 250.531 232.431 1.00 0.18  ? 2732 PRO A CB    1 
ATOM   10060 C  CG    . PRO A 1 2732 ? 221.098 249.126 232.802 1.00 0.25  ? 2732 PRO A CG    1 
ATOM   10061 C  CD    . PRO A 1 2732 ? 219.614 249.009 232.707 1.00 0.28  ? 2732 PRO A CD    1 
ATOM   10062 N  N     . VAL A 1 2733 ? 221.272 251.997 229.442 1.00 0.11  ? 2733 VAL A N     1 
ATOM   10063 C  CA    . VAL A 1 2733 ? 221.748 252.129 228.072 1.00 0.11  ? 2733 VAL A CA    1 
ATOM   10064 C  C     . VAL A 1 2733 ? 223.165 252.679 228.100 1.00 0.12  ? 2733 VAL A C     1 
ATOM   10065 O  O     . VAL A 1 2733 ? 223.432 253.690 228.759 1.00 0.19  ? 2733 VAL A O     1 
ATOM   10066 C  CB    . VAL A 1 2733 ? 220.825 253.033 227.234 1.00 0.10  ? 2733 VAL A CB    1 
ATOM   10067 C  CG1   . VAL A 1 2733 ? 221.423 253.280 225.860 1.00 0.11  ? 2733 VAL A CG1   1 
ATOM   10068 C  CG2   . VAL A 1 2733 ? 219.445 252.417 227.116 1.00 0.10  ? 2733 VAL A CG2   1 
ATOM   10069 N  N     . VAL A 1 2734 ? 224.069 252.007 227.398 1.00 0.16  ? 2734 VAL A N     1 
ATOM   10070 C  CA    . VAL A 1 2734 ? 225.427 252.481 227.181 1.00 0.27  ? 2734 VAL A CA    1 
ATOM   10071 C  C     . VAL A 1 2734 ? 225.568 252.845 225.709 1.00 0.19  ? 2734 VAL A C     1 
ATOM   10072 O  O     . VAL A 1 2734 ? 225.090 252.113 224.834 1.00 0.13  ? 2734 VAL A O     1 
ATOM   10073 C  CB    . VAL A 1 2734 ? 226.479 251.436 227.613 1.00 0.40  ? 2734 VAL A CB    1 
ATOM   10074 C  CG1   . VAL A 1 2734 ? 226.384 250.172 226.771 1.00 2.04  ? 2734 VAL A CG1   1 
ATOM   10075 C  CG2   . VAL A 1 2734 ? 227.876 252.026 227.525 1.00 0.37  ? 2734 VAL A CG2   1 
ATOM   10076 N  N     . TYR A 1 2735 ? 226.182 253.992 225.440 1.00 0.41  ? 2735 TYR A N     1 
ATOM   10077 C  CA    . TYR A 1 2735 ? 226.379 254.465 224.077 1.00 0.36  ? 2735 TYR A CA    1 
ATOM   10078 C  C     . TYR A 1 2735 ? 227.767 254.058 223.597 1.00 0.41  ? 2735 TYR A C     1 
ATOM   10079 O  O     . TYR A 1 2735 ? 228.777 254.458 224.186 1.00 0.89  ? 2735 TYR A O     1 
ATOM   10080 C  CB    . TYR A 1 2735 ? 226.212 255.980 223.995 1.00 0.64  ? 2735 TYR A CB    1 
ATOM   10081 C  CG    . TYR A 1 2735 ? 226.386 256.533 222.599 1.00 1.13  ? 2735 TYR A CG    1 
ATOM   10082 C  CD1   . TYR A 1 2735 ? 225.653 256.027 221.533 1.00 1.22  ? 2735 TYR A CD1   1 
ATOM   10083 C  CD2   . TYR A 1 2735 ? 227.295 257.549 222.345 1.00 0.82  ? 2735 TYR A CD2   1 
ATOM   10084 C  CE1   . TYR A 1 2735 ? 225.811 256.526 220.259 1.00 1.93  ? 2735 TYR A CE1   1 
ATOM   10085 C  CE2   . TYR A 1 2735 ? 227.461 258.055 221.072 1.00 1.86  ? 2735 TYR A CE2   1 
ATOM   10086 C  CZ    . TYR A 1 2735 ? 226.717 257.539 220.033 1.00 5.10  ? 2735 TYR A CZ    1 
ATOM   10087 O  OH    . TYR A 1 2735 ? 226.879 258.042 218.764 1.00 12.45 ? 2735 TYR A OH    1 
ATOM   10088 N  N     . VAL A 1 2736 ? 227.814 253.273 222.531 1.00 0.19  ? 2736 VAL A N     1 
ATOM   10089 C  CA    . VAL A 1 2736 ? 229.065 252.845 221.923 1.00 0.46  ? 2736 VAL A CA    1 
ATOM   10090 C  C     . VAL A 1 2736 ? 229.191 253.580 220.598 1.00 0.37  ? 2736 VAL A C     1 
ATOM   10091 O  O     . VAL A 1 2736 ? 228.468 253.285 219.639 1.00 0.32  ? 2736 VAL A O     1 
ATOM   10092 C  CB    . VAL A 1 2736 ? 229.123 251.324 221.735 1.00 0.59  ? 2736 VAL A CB    1 
ATOM   10093 C  CG1   . VAL A 1 2736 ? 230.434 250.921 221.084 1.00 0.25  ? 2736 VAL A CG1   1 
ATOM   10094 C  CG2   . VAL A 1 2736 ? 228.943 250.619 223.072 1.00 0.47  ? 2736 VAL A CG2   1 
ATOM   10095 N  N     . ASP A 1 2737 ? 230.098 254.545 220.545 1.00 0.49  ? 2737 ASP A N     1 
ATOM   10096 C  CA    . ASP A 1 2737 ? 230.329 255.325 219.343 1.00 1.13  ? 2737 ASP A CA    1 
ATOM   10097 C  C     . ASP A 1 2737 ? 231.405 254.671 218.481 1.00 0.55  ? 2737 ASP A C     1 
ATOM   10098 O  O     . ASP A 1 2737 ? 232.073 253.718 218.885 1.00 0.68  ? 2737 ASP A O     1 
ATOM   10099 C  CB    . ASP A 1 2737 ? 230.729 256.753 219.707 1.00 1.28  ? 2737 ASP A CB    1 
ATOM   10100 C  CG    . ASP A 1 2737 ? 230.453 257.738 218.592 1.00 4.81  ? 2737 ASP A CG    1 
ATOM   10101 O  OD1   . ASP A 1 2737 ? 229.875 257.331 217.562 1.00 3.14  ? 2737 ASP A OD1   1 
ATOM   10102 O  OD2   . ASP A 1 2737 ? 230.816 258.923 218.743 1.00 14.41 ? 2737 ASP A OD2   1 
ATOM   10103 N  N     . TYR A 1 2738 ? 231.560 255.195 217.273 1.00 0.94  ? 2738 TYR A N     1 
ATOM   10104 C  CA    . TYR A 1 2738 ? 232.647 254.757 216.418 1.00 0.77  ? 2738 TYR A CA    1 
ATOM   10105 C  C     . TYR A 1 2738 ? 233.981 255.140 217.052 1.00 1.23  ? 2738 TYR A C     1 
ATOM   10106 O  O     . TYR A 1 2738 ? 234.101 256.226 217.632 1.00 1.46  ? 2738 TYR A O     1 
ATOM   10107 C  CB    . TYR A 1 2738 ? 232.528 255.384 215.028 1.00 0.47  ? 2738 TYR A CB    1 
ATOM   10108 C  CG    . TYR A 1 2738 ? 231.528 254.691 214.139 1.00 0.36  ? 2738 TYR A CG    1 
ATOM   10109 C  CD1   . TYR A 1 2738 ? 231.349 253.318 214.210 1.00 0.41  ? 2738 TYR A CD1   1 
ATOM   10110 C  CD2   . TYR A 1 2738 ? 230.754 255.409 213.238 1.00 0.25  ? 2738 TYR A CD2   1 
ATOM   10111 C  CE1   . TYR A 1 2738 ? 230.433 252.676 213.404 1.00 0.30  ? 2738 TYR A CE1   1 
ATOM   10112 C  CE2   . TYR A 1 2738 ? 229.837 254.777 212.429 1.00 0.32  ? 2738 TYR A CE2   1 
ATOM   10113 C  CZ    . TYR A 1 2738 ? 229.681 253.409 212.515 1.00 0.35  ? 2738 TYR A CZ    1 
ATOM   10114 O  OH    . TYR A 1 2738 ? 228.765 252.771 211.714 1.00 0.30  ? 2738 TYR A OH    1 
ATOM   10115 N  N     . PRO A 1 2739 ? 234.987 254.270 216.991 1.00 1.78  ? 2739 PRO A N     1 
ATOM   10116 C  CA    . PRO A 1 2739 ? 236.321 254.663 217.453 1.00 1.26  ? 2739 PRO A CA    1 
ATOM   10117 C  C     . PRO A 1 2739 ? 236.834 255.856 216.662 1.00 1.91  ? 2739 PRO A C     1 
ATOM   10118 O  O     . PRO A 1 2739 ? 236.595 255.980 215.459 1.00 2.62  ? 2739 PRO A O     1 
ATOM   10119 C  CB    . PRO A 1 2739 ? 237.166 253.410 217.201 1.00 0.72  ? 2739 PRO A CB    1 
ATOM   10120 C  CG    . PRO A 1 2739 ? 236.187 252.289 217.206 1.00 0.67  ? 2739 PRO A CG    1 
ATOM   10121 C  CD    . PRO A 1 2739 ? 234.921 252.846 216.626 1.00 1.26  ? 2739 PRO A CD    1 
ATOM   10122 N  N     . GLY A 1 2740 ? 237.544 256.745 217.356 1.00 1.95  ? 2740 GLY A N     1 
ATOM   10123 C  CA    . GLY A 1 2740 ? 238.079 257.919 216.733 1.00 3.37  ? 2740 GLY A CA    1 
ATOM   10124 C  C     . GLY A 1 2740 ? 239.285 257.600 215.872 1.00 4.68  ? 2740 GLY A C     1 
ATOM   10125 O  O     . GLY A 1 2740 ? 239.739 256.452 215.791 1.00 4.13  ? 2740 GLY A O     1 
ATOM   10126 N  N     . PRO A 1 2741 ? 239.813 258.629 215.203 1.00 4.84  ? 2741 PRO A N     1 
ATOM   10127 C  CA    . PRO A 1 2741 ? 240.983 258.409 214.335 1.00 4.72  ? 2741 PRO A CA    1 
ATOM   10128 C  C     . PRO A 1 2741 ? 242.183 257.837 215.068 1.00 4.97  ? 2741 PRO A C     1 
ATOM   10129 O  O     . PRO A 1 2741 ? 242.909 257.010 214.505 1.00 5.23  ? 2741 PRO A O     1 
ATOM   10130 C  CB    . PRO A 1 2741 ? 241.267 259.812 213.780 1.00 7.78  ? 2741 PRO A CB    1 
ATOM   10131 C  CG    . PRO A 1 2741 ? 239.959 260.530 213.890 1.00 10.02 ? 2741 PRO A CG    1 
ATOM   10132 C  CD    . PRO A 1 2741 ? 239.347 260.023 215.156 1.00 8.66  ? 2741 PRO A CD    1 
ATOM   10133 N  N     . ALA A 1 2742 ? 242.412 258.253 216.317 1.00 4.19  ? 2742 ALA A N     1 
ATOM   10134 C  CA    . ALA A 1 2742 ? 243.536 257.719 217.076 1.00 3.07  ? 2742 ALA A CA    1 
ATOM   10135 C  C     . ALA A 1 2742 ? 243.250 256.306 217.564 1.00 2.35  ? 2742 ALA A C     1 
ATOM   10136 O  O     . ALA A 1 2742 ? 244.153 255.463 217.608 1.00 2.07  ? 2742 ALA A O     1 
ATOM   10137 C  CB    . ALA A 1 2742 ? 243.865 258.640 218.251 1.00 3.19  ? 2742 ALA A CB    1 
ATOM   10138 N  N     . SER A 1 2743 ? 242.002 256.033 217.949 1.00 5.18  ? 2743 SER A N     1 
ATOM   10139 C  CA    . SER A 1 2743 ? 241.633 254.680 218.353 1.00 1.37  ? 2743 SER A CA    1 
ATOM   10140 C  C     . SER A 1 2743 ? 241.732 253.711 217.180 1.00 2.45  ? 2743 SER A C     1 
ATOM   10141 O  O     . SER A 1 2743 ? 242.195 252.578 217.343 1.00 3.20  ? 2743 SER A O     1 
ATOM   10142 C  CB    . SER A 1 2743 ? 240.225 254.682 218.945 1.00 1.91  ? 2743 SER A CB    1 
ATOM   10143 O  OG    . SER A 1 2743 ? 239.861 253.397 219.415 1.00 8.15  ? 2743 SER A OG    1 
ATOM   10144 N  N     . LEU A 1 2744 ? 241.303 254.144 215.992 1.00 2.67  ? 2744 LEU A N     1 
ATOM   10145 C  CA    . LEU A 1 2744 ? 241.429 253.303 214.805 1.00 0.98  ? 2744 LEU A CA    1 
ATOM   10146 C  C     . LEU A 1 2744 ? 242.888 253.025 214.481 1.00 1.51  ? 2744 LEU A C     1 
ATOM   10147 O  O     . LEU A 1 2744 ? 243.244 251.904 214.098 1.00 1.46  ? 2744 LEU A O     1 
ATOM   10148 C  CB    . LEU A 1 2744 ? 240.734 253.967 213.618 1.00 1.28  ? 2744 LEU A CB    1 
ATOM   10149 C  CG    . LEU A 1 2744 ? 239.208 254.019 213.675 1.00 1.37  ? 2744 LEU A CG    1 
ATOM   10150 C  CD1   . LEU A 1 2744 ? 238.657 254.740 212.459 1.00 1.25  ? 2744 LEU A CD1   1 
ATOM   10151 C  CD2   . LEU A 1 2744 ? 238.626 252.622 213.790 1.00 0.90  ? 2744 LEU A CD2   1 
ATOM   10152 N  N     . THR A 1 2745 ? 243.749 254.034 214.627 1.00 1.99  ? 2745 THR A N     1 
ATOM   10153 C  CA    . THR A 1 2745 ? 245.174 253.837 214.388 1.00 1.51  ? 2745 THR A CA    1 
ATOM   10154 C  C     . THR A 1 2745 ? 245.757 252.825 215.364 1.00 3.12  ? 2745 THR A C     1 
ATOM   10155 O  O     . THR A 1 2745 ? 246.608 252.009 214.992 1.00 4.83  ? 2745 THR A O     1 
ATOM   10156 C  CB    . THR A 1 2745 ? 245.909 255.172 214.490 1.00 1.26  ? 2745 THR A CB    1 
ATOM   10157 O  OG1   . THR A 1 2745 ? 245.395 256.076 213.503 1.00 1.84  ? 2745 THR A OG1   1 
ATOM   10158 C  CG2   . THR A 1 2745 ? 247.400 254.990 214.271 1.00 1.07  ? 2745 THR A CG2   1 
ATOM   10159 N  N     . GLN A 1 2746 ? 245.313 252.862 216.620 1.00 4.71  ? 2746 GLN A N     1 
ATOM   10160 C  CA    . GLN A 1 2746 ? 245.798 251.902 217.605 1.00 2.96  ? 2746 GLN A CA    1 
ATOM   10161 C  C     . GLN A 1 2746 ? 245.290 250.494 217.308 1.00 3.12  ? 2746 GLN A C     1 
ATOM   10162 O  O     . GLN A 1 2746 ? 246.043 249.522 217.428 1.00 3.40  ? 2746 GLN A O     1 
ATOM   10163 C  CB    . GLN A 1 2746 ? 245.384 252.344 219.008 1.00 4.09  ? 2746 GLN A CB    1 
ATOM   10164 C  CG    . GLN A 1 2746 ? 245.775 251.380 220.112 1.00 5.67  ? 2746 GLN A CG    1 
ATOM   10165 C  CD    . GLN A 1 2746 ? 247.205 251.582 220.585 1.00 20.27 ? 2746 GLN A CD    1 
ATOM   10166 O  OE1   . GLN A 1 2746 ? 247.936 252.412 220.047 1.00 14.60 ? 2746 GLN A OE1   1 
ATOM   10167 N  NE2   . GLN A 1 2746 ? 247.606 250.821 221.599 1.00 15.29 ? 2746 GLN A NE2   1 
ATOM   10168 N  N     . ILE A 1 2747 ? 244.019 250.364 216.919 1.00 1.60  ? 2747 ILE A N     1 
ATOM   10169 C  CA    . ILE A 1 2747 ? 243.446 249.044 216.664 1.00 1.06  ? 2747 ILE A CA    1 
ATOM   10170 C  C     . ILE A 1 2747 ? 244.115 248.392 215.461 1.00 1.56  ? 2747 ILE A C     1 
ATOM   10171 O  O     . ILE A 1 2747 ? 244.735 247.330 215.569 1.00 1.66  ? 2747 ILE A O     1 
ATOM   10172 C  CB    . ILE A 1 2747 ? 241.924 249.141 216.460 1.00 1.34  ? 2747 ILE A CB    1 
ATOM   10173 C  CG1   . ILE A 1 2747 ? 241.227 249.567 217.755 1.00 2.32  ? 2747 ILE A CG1   1 
ATOM   10174 C  CG2   . ILE A 1 2747 ? 241.364 247.826 215.949 1.00 0.30  ? 2747 ILE A CG2   1 
ATOM   10175 C  CD1   . ILE A 1 2747 ? 239.885 250.212 217.534 1.00 0.72  ? 2747 ILE A CD1   1 
ATOM   10176 N  N     . TYR A 1 2748 ? 243.998 249.024 214.297 1.00 1.16  ? 2748 TYR A N     1 
ATOM   10177 C  CA    . TYR A 1 2748 ? 244.451 248.423 213.054 1.00 0.82  ? 2748 TYR A CA    1 
ATOM   10178 C  C     . TYR A 1 2748 ? 245.929 248.648 212.781 1.00 1.05  ? 2748 TYR A C     1 
ATOM   10179 O  O     . TYR A 1 2748 ? 246.490 247.974 211.913 1.00 3.00  ? 2748 TYR A O     1 
ATOM   10180 C  CB    . TYR A 1 2748 ? 243.592 248.941 211.902 1.00 0.46  ? 2748 TYR A CB    1 
ATOM   10181 C  CG    . TYR A 1 2748 ? 242.145 248.568 212.099 1.00 0.23  ? 2748 TYR A CG    1 
ATOM   10182 C  CD1   . TYR A 1 2748 ? 241.711 247.273 211.865 1.00 0.39  ? 2748 TYR A CD1   1 
ATOM   10183 C  CD2   . TYR A 1 2748 ? 241.223 249.496 212.560 1.00 0.22  ? 2748 TYR A CD2   1 
ATOM   10184 C  CE1   . TYR A 1 2748 ? 240.396 246.916 212.058 1.00 0.26  ? 2748 TYR A CE1   1 
ATOM   10185 C  CE2   . TYR A 1 2748 ? 239.903 249.147 212.759 1.00 0.34  ? 2748 TYR A CE2   1 
ATOM   10186 C  CZ    . TYR A 1 2748 ? 239.496 247.852 212.507 1.00 0.28  ? 2748 TYR A CZ    1 
ATOM   10187 O  OH    . TYR A 1 2748 ? 238.185 247.493 212.697 1.00 0.20  ? 2748 TYR A OH    1 
ATOM   10188 N  N     . GLY A 1 2749 ? 246.575 249.564 213.502 1.00 1.26  ? 2749 GLY A N     1 
ATOM   10189 C  CA    . GLY A 1 2749 ? 248.026 249.574 213.527 1.00 1.27  ? 2749 GLY A CA    1 
ATOM   10190 C  C     . GLY A 1 2749 ? 248.592 248.348 214.211 1.00 2.36  ? 2749 GLY A C     1 
ATOM   10191 O  O     . GLY A 1 2749 ? 249.637 247.832 213.803 1.00 5.51  ? 2749 GLY A O     1 
ATOM   10192 N  N     . THR A 1 2750 ? 247.922 247.871 215.261 1.00 4.53  ? 2750 THR A N     1 
ATOM   10193 C  CA    . THR A 1 2750 ? 248.304 246.611 215.888 1.00 4.30  ? 2750 THR A CA    1 
ATOM   10194 C  C     . THR A 1 2750 ? 248.114 245.445 214.927 1.00 2.86  ? 2750 THR A C     1 
ATOM   10195 O  O     . THR A 1 2750 ? 248.974 244.562 214.826 1.00 6.42  ? 2750 THR A O     1 
ATOM   10196 C  CB    . THR A 1 2750 ? 247.488 246.398 217.165 1.00 2.61  ? 2750 THR A CB    1 
ATOM   10197 O  OG1   . THR A 1 2750 ? 247.788 247.436 218.105 1.00 7.69  ? 2750 THR A OG1   1 
ATOM   10198 C  CG2   . THR A 1 2750 ? 247.801 245.048 217.792 1.00 3.92  ? 2750 THR A CG2   1 
ATOM   10199 N  N     . PHE A 1 2751 ? 246.989 245.428 214.206 1.00 2.23  ? 2751 PHE A N     1 
ATOM   10200 C  CA    . PHE A 1 2751 ? 246.739 244.364 213.240 1.00 3.35  ? 2751 PHE A CA    1 
ATOM   10201 C  C     . PHE A 1 2751 ? 247.739 244.408 212.092 1.00 7.13  ? 2751 PHE A C     1 
ATOM   10202 O  O     . PHE A 1 2751 ? 248.251 243.364 211.668 1.00 7.43  ? 2751 PHE A O     1 
ATOM   10203 C  CB    . PHE A 1 2751 ? 245.310 244.471 212.706 1.00 1.96  ? 2751 PHE A CB    1 
ATOM   10204 C  CG    . PHE A 1 2751 ? 244.274 243.934 213.645 1.00 2.41  ? 2751 PHE A CG    1 
ATOM   10205 C  CD1   . PHE A 1 2751 ? 244.564 242.875 214.487 1.00 3.62  ? 2751 PHE A CD1   1 
ATOM   10206 C  CD2   . PHE A 1 2751 ? 243.009 244.492 213.690 1.00 1.54  ? 2751 PHE A CD2   1 
ATOM   10207 C  CE1   . PHE A 1 2751 ? 243.613 242.381 215.349 1.00 3.50  ? 2751 PHE A CE1   1 
ATOM   10208 C  CE2   . PHE A 1 2751 ? 242.053 244.000 214.553 1.00 1.73  ? 2751 PHE A CE2   1 
ATOM   10209 C  CZ    . PHE A 1 2751 ? 242.355 242.943 215.382 1.00 2.24  ? 2751 PHE A CZ    1 
ATOM   10210 N  N     . ASN A 1 2752 ? 248.028 245.604 211.574 1.00 2.52  ? 2752 ASN A N     1 
ATOM   10211 C  CA    . ASN A 1 2752 ? 248.948 245.720 210.446 1.00 3.41  ? 2752 ASN A CA    1 
ATOM   10212 C  C     . ASN A 1 2752 ? 250.359 245.296 210.835 1.00 6.92  ? 2752 ASN A C     1 
ATOM   10213 O  O     . ASN A 1 2752 ? 251.066 244.671 210.037 1.00 8.66  ? 2752 ASN A O     1 
ATOM   10214 C  CB    . ASN A 1 2752 ? 248.938 247.149 209.903 1.00 3.23  ? 2752 ASN A CB    1 
ATOM   10215 C  CG    . ASN A 1 2752 ? 247.721 247.439 209.048 1.00 1.08  ? 2752 ASN A CG    1 
ATOM   10216 O  OD1   . ASN A 1 2752 ? 246.883 246.568 208.821 1.00 1.71  ? 2752 ASN A OD1   1 
ATOM   10217 N  ND2   . ASN A 1 2752 ? 247.611 248.671 208.579 1.00 2.57  ? 2752 ASN A ND2   1 
ATOM   10218 N  N     . ARG A 1 2753 ? 250.789 245.629 212.054 1.00 7.52  ? 2753 ARG A N     1 
ATOM   10219 C  CA    . ARG A 1 2753 ? 252.101 245.187 212.517 1.00 9.15  ? 2753 ARG A CA    1 
ATOM   10220 C  C     . ARG A 1 2753 ? 252.184 243.666 212.560 1.00 8.92  ? 2753 ARG A C     1 
ATOM   10221 O  O     . ARG A 1 2753 ? 253.208 243.081 212.187 1.00 11.88 ? 2753 ARG A O     1 
ATOM   10222 C  CB    . ARG A 1 2753 ? 252.397 245.776 213.895 1.00 5.61  ? 2753 ARG A CB    1 
ATOM   10223 C  CG    . ARG A 1 2753 ? 252.945 247.191 213.866 1.00 11.94 ? 2753 ARG A CG    1 
ATOM   10224 C  CD    . ARG A 1 2753 ? 253.514 247.591 215.216 1.00 10.73 ? 2753 ARG A CD    1 
ATOM   10225 N  NE    . ARG A 1 2753 ? 252.652 247.178 216.317 1.00 10.98 ? 2753 ARG A NE    1 
ATOM   10226 C  CZ    . ARG A 1 2753 ? 251.668 247.913 216.818 1.00 10.65 ? 2753 ARG A CZ    1 
ATOM   10227 N  NH1   . ARG A 1 2753 ? 251.393 249.115 216.341 1.00 6.72  ? 2753 ARG A NH1   1 
ATOM   10228 N  NH2   . ARG A 1 2753 ? 250.942 247.428 217.820 1.00 7.66  ? 2753 ARG A NH2   1 
ATOM   10229 N  N     . ALA A 1 2754 ? 251.119 243.008 213.019 1.00 4.99  ? 2754 ALA A N     1 
ATOM   10230 C  CA    . ALA A 1 2754 ? 251.114 241.550 213.065 1.00 7.90  ? 2754 ALA A CA    1 
ATOM   10231 C  C     . ALA A 1 2754 ? 251.070 240.947 211.665 1.00 11.07 ? 2754 ALA A C     1 
ATOM   10232 O  O     . ALA A 1 2754 ? 251.782 239.977 211.379 1.00 13.64 ? 2754 ALA A O     1 
ATOM   10233 C  CB    . ALA A 1 2754 ? 249.932 241.062 213.900 1.00 7.03  ? 2754 ALA A CB    1 
ATOM   10234 N  N     . MET A 1 2755 ? 250.239 241.506 210.783 1.00 14.94 ? 2755 MET A N     1 
ATOM   10235 C  CA    . MET A 1 2755 ? 250.076 240.935 209.449 1.00 8.36  ? 2755 MET A CA    1 
ATOM   10236 C  C     . MET A 1 2755 ? 251.284 241.222 208.562 1.00 8.81  ? 2755 MET A C     1 
ATOM   10237 O  O     . MET A 1 2755 ? 251.593 240.439 207.657 1.00 16.92 ? 2755 MET A O     1 
ATOM   10238 C  CB    . MET A 1 2755 ? 248.773 241.451 208.833 1.00 5.82  ? 2755 MET A CB    1 
ATOM   10239 C  CG    . MET A 1 2755 ? 248.650 241.334 207.326 1.00 8.74  ? 2755 MET A CG    1 
ATOM   10240 S  SD    . MET A 1 2755 ? 247.613 242.648 206.659 1.00 14.00 ? 2755 MET A SD    1 
ATOM   10241 C  CE    . MET A 1 2755 ? 248.818 243.925 206.342 1.00 6.15  ? 2755 MET A CE    1 
ATOM   10242 N  N     . LEU A 1 2756 ? 251.992 242.320 208.817 1.00 8.29  ? 2756 LEU A N     1 
ATOM   10243 C  CA    . LEU A 1 2756 ? 253.214 242.594 208.067 1.00 6.53  ? 2756 LEU A CA    1 
ATOM   10244 C  C     . LEU A 1 2756 ? 254.440 241.900 208.646 1.00 11.80 ? 2756 LEU A C     1 
ATOM   10245 O  O     . LEU A 1 2756 ? 255.558 242.212 208.222 1.00 13.50 ? 2756 LEU A O     1 
ATOM   10246 C  CB    . LEU A 1 2756 ? 253.450 244.102 207.975 1.00 6.84  ? 2756 LEU A CB    1 
ATOM   10247 C  CG    . LEU A 1 2756 ? 252.510 244.861 207.034 1.00 9.57  ? 2756 LEU A CG    1 
ATOM   10248 C  CD1   . LEU A 1 2756 ? 253.073 246.219 206.690 1.00 9.10  ? 2756 LEU A CD1   1 
ATOM   10249 C  CD2   . LEU A 1 2756 ? 252.305 244.062 205.760 1.00 9.22  ? 2756 LEU A CD2   1 
ATOM   10250 N  N     . ARG A 1 2757 ? 254.273 240.990 209.609 1.00 15.99 ? 2757 ARG A N     1 
ATOM   10251 C  CA    . ARG A 1 2757 ? 255.372 240.109 209.987 1.00 12.75 ? 2757 ARG A CA    1 
ATOM   10252 C  C     . ARG A 1 2757 ? 255.476 238.901 209.066 1.00 13.07 ? 2757 ARG A C     1 
ATOM   10253 O  O     . ARG A 1 2757 ? 256.467 238.168 209.139 1.00 14.08 ? 2757 ARG A O     1 
ATOM   10254 C  CB    . ARG A 1 2757 ? 255.232 239.643 211.438 1.00 15.33 ? 2757 ARG A CB    1 
ATOM   10255 C  CG    . ARG A 1 2757 ? 255.450 240.732 212.471 1.00 16.27 ? 2757 ARG A CG    1 
ATOM   10256 C  CD    . ARG A 1 2757 ? 255.631 240.152 213.865 1.00 15.47 ? 2757 ARG A CD    1 
ATOM   10257 N  NE    . ARG A 1 2757 ? 254.371 239.781 214.498 1.00 17.47 ? 2757 ARG A NE    1 
ATOM   10258 C  CZ    . ARG A 1 2757 ? 253.641 240.594 215.246 1.00 16.87 ? 2757 ARG A CZ    1 
ATOM   10259 N  NH1   . ARG A 1 2757 ? 254.003 241.848 215.464 1.00 18.66 ? 2757 ARG A NH1   1 
ATOM   10260 N  NH2   . ARG A 1 2757 ? 252.520 240.137 215.796 1.00 16.35 ? 2757 ARG A NH2   1 
ATOM   10261 N  N     . LEU A 1 2758 ? 254.475 238.672 208.212 1.00 13.94 ? 2758 LEU A N     1 
ATOM   10262 C  CA    . LEU A 1 2758 ? 254.586 237.628 207.199 1.00 12.38 ? 2758 LEU A CA    1 
ATOM   10263 C  C     . LEU A 1 2758 ? 255.718 237.933 206.227 1.00 17.81 ? 2758 LEU A C     1 
ATOM   10264 O  O     . LEU A 1 2758 ? 256.496 237.045 205.861 1.00 23.47 ? 2758 LEU A O     1 
ATOM   10265 C  CB    . LEU A 1 2758 ? 253.263 237.475 206.450 1.00 12.05 ? 2758 LEU A CB    1 
ATOM   10266 C  CG    . LEU A 1 2758 ? 252.041 237.010 207.243 1.00 14.46 ? 2758 LEU A CG    1 
ATOM   10267 C  CD1   . LEU A 1 2758 ? 250.814 236.952 206.352 1.00 10.93 ? 2758 LEU A CD1   1 
ATOM   10268 C  CD2   . LEU A 1 2758 ? 252.306 235.652 207.869 1.00 9.94  ? 2758 LEU A CD2   1 
ATOM   10269 N  N     . ILE A 1 2759 ? 255.829 239.189 205.807 1.00 13.68 ? 2759 ILE A N     1 
ATOM   10270 C  CA    . ILE A 1 2759 ? 256.903 239.614 204.917 1.00 13.67 ? 2759 ILE A CA    1 
ATOM   10271 C  C     . ILE A 1 2759 ? 257.830 240.528 205.711 1.00 16.80 ? 2759 ILE A C     1 
ATOM   10272 O  O     . ILE A 1 2759 ? 257.523 241.715 205.886 1.00 22.81 ? 2759 ILE A O     1 
ATOM   10273 C  CB    . ILE A 1 2759 ? 256.356 240.326 203.672 1.00 17.08 ? 2759 ILE A CB    1 
ATOM   10274 C  CG1   . ILE A 1 2759 ? 255.209 239.526 203.049 1.00 16.61 ? 2759 ILE A CG1   1 
ATOM   10275 C  CG2   . ILE A 1 2759 ? 257.461 240.532 202.655 1.00 17.91 ? 2759 ILE A CG2   1 
ATOM   10276 C  CD1   . ILE A 1 2759 ? 255.611 238.167 202.538 1.00 15.71 ? 2759 ILE A CD1   1 
ATOM   10277 N  N     . PRO A 1 2760 ? 258.959 240.021 206.211 1.00 21.10 ? 2760 PRO A N     1 
ATOM   10278 C  CA    . PRO A 1 2760 ? 259.850 240.867 207.022 1.00 16.87 ? 2760 PRO A CA    1 
ATOM   10279 C  C     . PRO A 1 2760 ? 260.365 242.100 206.299 1.00 21.74 ? 2760 PRO A C     1 
ATOM   10280 O  O     . PRO A 1 2760 ? 260.672 243.109 206.948 1.00 24.92 ? 2760 PRO A O     1 
ATOM   10281 C  CB    . PRO A 1 2760 ? 260.990 239.903 207.381 1.00 20.30 ? 2760 PRO A CB    1 
ATOM   10282 C  CG    . PRO A 1 2760 ? 260.331 238.571 207.411 1.00 19.26 ? 2760 PRO A CG    1 
ATOM   10283 C  CD    . PRO A 1 2760 ? 259.336 238.599 206.283 1.00 18.45 ? 2760 PRO A CD    1 
ATOM   10284 N  N     . SER A 1 2761 ? 260.475 242.051 204.973 1.00 16.12 ? 2761 SER A N     1 
ATOM   10285 C  CA    . SER A 1 2761 ? 260.924 243.211 204.214 1.00 16.84 ? 2761 SER A CA    1 
ATOM   10286 C  C     . SER A 1 2761 ? 259.890 244.329 204.165 1.00 16.56 ? 2761 SER A C     1 
ATOM   10287 O  O     . SER A 1 2761 ? 260.216 245.423 203.696 1.00 17.50 ? 2761 SER A O     1 
ATOM   10288 C  CB    . SER A 1 2761 ? 261.298 242.793 202.791 1.00 24.17 ? 2761 SER A CB    1 
ATOM   10289 O  OG    . SER A 1 2761 ? 260.161 242.364 202.066 1.00 26.87 ? 2761 SER A OG    1 
ATOM   10290 N  N     . LEU A 1 2762 ? 258.661 244.086 204.621 1.00 19.10 ? 2762 LEU A N     1 
ATOM   10291 C  CA    . LEU A 1 2762 ? 257.609 245.095 204.592 1.00 14.40 ? 2762 LEU A CA    1 
ATOM   10292 C  C     . LEU A 1 2762 ? 257.234 245.598 205.982 1.00 15.10 ? 2762 LEU A C     1 
ATOM   10293 O  O     . LEU A 1 2762 ? 256.193 246.247 206.132 1.00 16.07 ? 2762 LEU A O     1 
ATOM   10294 C  CB    . LEU A 1 2762 ? 256.370 244.545 203.882 1.00 17.22 ? 2762 LEU A CB    1 
ATOM   10295 C  CG    . LEU A 1 2762 ? 256.500 244.346 202.370 1.00 15.73 ? 2762 LEU A CG    1 
ATOM   10296 C  CD1   . LEU A 1 2762 ? 255.186 243.864 201.779 1.00 13.40 ? 2762 LEU A CD1   1 
ATOM   10297 C  CD2   . LEU A 1 2762 ? 256.963 245.625 201.693 1.00 14.48 ? 2762 LEU A CD2   1 
ATOM   10298 N  N     . ARG A 1 2763 ? 258.054 245.321 206.998 1.00 20.15 ? 2763 ARG A N     1 
ATOM   10299 C  CA    . ARG A 1 2763 ? 257.735 245.749 208.360 1.00 16.82 ? 2763 ARG A CA    1 
ATOM   10300 C  C     . ARG A 1 2763 ? 257.688 247.268 208.473 1.00 14.01 ? 2763 ARG A C     1 
ATOM   10301 O  O     . ARG A 1 2763 ? 256.858 247.818 209.206 1.00 14.55 ? 2763 ARG A O     1 
ATOM   10302 C  CB    . ARG A 1 2763 ? 258.758 245.171 209.338 1.00 18.27 ? 2763 ARG A CB    1 
ATOM   10303 C  CG    . ARG A 1 2763 ? 258.453 245.434 210.805 1.00 25.44 ? 2763 ARG A CG    1 
ATOM   10304 C  CD    . ARG A 1 2763 ? 259.512 244.811 211.706 1.00 26.29 ? 2763 ARG A CD    1 
ATOM   10305 N  NE    . ARG A 1 2763 ? 259.529 243.354 211.623 1.00 26.71 ? 2763 ARG A NE    1 
ATOM   10306 C  CZ    . ARG A 1 2763 ? 258.738 242.558 212.328 1.00 31.13 ? 2763 ARG A CZ    1 
ATOM   10307 N  NH1   . ARG A 1 2763 ? 257.876 243.043 213.207 1.00 32.78 ? 2763 ARG A NH1   1 
ATOM   10308 N  NH2   . ARG A 1 2763 ? 258.824 241.242 212.158 1.00 31.64 ? 2763 ARG A NH2   1 
ATOM   10309 N  N     . THR A 1 2764 ? 258.574 247.961 207.756 1.00 14.07 ? 2764 THR A N     1 
ATOM   10310 C  CA    . THR A 1 2764 ? 258.672 249.413 207.878 1.00 12.63 ? 2764 THR A CA    1 
ATOM   10311 C  C     . THR A 1 2764 ? 257.391 250.110 207.435 1.00 10.52 ? 2764 THR A C     1 
ATOM   10312 O  O     . THR A 1 2764 ? 257.050 251.176 207.961 1.00 17.60 ? 2764 THR A O     1 
ATOM   10313 C  CB    . THR A 1 2764 ? 259.870 249.918 207.068 1.00 19.33 ? 2764 THR A CB    1 
ATOM   10314 O  OG1   . THR A 1 2764 ? 261.071 249.320 207.567 1.00 26.28 ? 2764 THR A OG1   1 
ATOM   10315 C  CG2   . THR A 1 2764 ? 260.001 251.428 207.165 1.00 15.79 ? 2764 THR A CG2   1 
ATOM   10316 N  N     . TYR A 1 2765 ? 256.659 249.526 206.488 1.00 11.45 ? 2765 TYR A N     1 
ATOM   10317 C  CA    . TYR A 1 2765 ? 255.478 250.170 205.930 1.00 10.33 ? 2765 TYR A CA    1 
ATOM   10318 C  C     . TYR A 1 2765 ? 254.211 249.932 206.751 1.00 6.62  ? 2765 TYR A C     1 
ATOM   10319 O  O     . TYR A 1 2765 ? 253.111 250.141 206.228 1.00 6.02  ? 2765 TYR A O     1 
ATOM   10320 C  CB    . TYR A 1 2765 ? 255.262 249.706 204.487 1.00 6.89  ? 2765 TYR A CB    1 
ATOM   10321 C  CG    . TYR A 1 2765 ? 256.442 249.959 203.580 1.00 7.37  ? 2765 TYR A CG    1 
ATOM   10322 C  CD1   . TYR A 1 2765 ? 256.719 251.234 203.113 1.00 8.83  ? 2765 TYR A CD1   1 
ATOM   10323 C  CD2   . TYR A 1 2765 ? 257.276 248.922 203.186 1.00 8.38  ? 2765 TYR A CD2   1 
ATOM   10324 C  CE1   . TYR A 1 2765 ? 257.796 251.474 202.284 1.00 9.18  ? 2765 TYR A CE1   1 
ATOM   10325 C  CE2   . TYR A 1 2765 ? 258.354 249.150 202.357 1.00 8.39  ? 2765 TYR A CE2   1 
ATOM   10326 C  CZ    . TYR A 1 2765 ? 258.608 250.429 201.907 1.00 9.98  ? 2765 TYR A CZ    1 
ATOM   10327 O  OH    . TYR A 1 2765 ? 259.681 250.665 201.080 1.00 19.83 ? 2765 TYR A OH    1 
ATOM   10328 N  N     . ALA A 1 2766 ? 254.332 249.513 208.011 1.00 7.99  ? 2766 ALA A N     1 
ATOM   10329 C  CA    . ALA A 1 2766 ? 253.142 249.256 208.820 1.00 6.13  ? 2766 ALA A CA    1 
ATOM   10330 C  C     . ALA A 1 2766 ? 252.401 250.548 209.146 1.00 5.47  ? 2766 ALA A C     1 
ATOM   10331 O  O     . ALA A 1 2766 ? 251.177 250.627 208.992 1.00 5.77  ? 2766 ALA A O     1 
ATOM   10332 C  CB    . ALA A 1 2766 ? 253.526 248.519 210.102 1.00 5.44  ? 2766 ALA A CB    1 
ATOM   10333 N  N     . GLU A 1 2767 ? 253.124 251.568 209.610 1.00 6.96  ? 2767 GLU A N     1 
ATOM   10334 C  CA    . GLU A 1 2767 ? 252.477 252.832 209.954 1.00 3.66  ? 2767 GLU A CA    1 
ATOM   10335 C  C     . GLU A 1 2767 ? 251.857 253.532 208.750 1.00 3.11  ? 2767 GLU A C     1 
ATOM   10336 O  O     . GLU A 1 2767 ? 250.687 253.941 208.842 1.00 3.53  ? 2767 GLU A O     1 
ATOM   10337 C  CB    . GLU A 1 2767 ? 253.473 253.740 210.685 1.00 8.17  ? 2767 GLU A CB    1 
ATOM   10338 C  CG    . GLU A 1 2767 ? 253.614 253.441 212.164 1.00 12.78 ? 2767 GLU A CG    1 
ATOM   10339 C  CD    . GLU A 1 2767 ? 254.858 254.062 212.766 1.00 28.46 ? 2767 GLU A CD    1 
ATOM   10340 O  OE1   . GLU A 1 2767 ? 255.015 254.000 214.004 1.00 31.81 ? 2767 GLU A OE1   1 
ATOM   10341 O  OE2   . GLU A 1 2767 ? 255.680 254.611 212.004 1.00 23.90 ? 2767 GLU A OE2   1 
ATOM   10342 N  N     . PRO A 1 2768 ? 252.552 253.720 207.619 1.00 6.68  ? 2768 PRO A N     1 
ATOM   10343 C  CA    . PRO A 1 2768 ? 251.880 254.335 206.460 1.00 2.82  ? 2768 PRO A CA    1 
ATOM   10344 C  C     . PRO A 1 2768 ? 250.707 253.525 205.934 1.00 1.84  ? 2768 PRO A C     1 
ATOM   10345 O  O     . PRO A 1 2768 ? 249.737 254.113 205.441 1.00 2.17  ? 2768 PRO A O     1 
ATOM   10346 C  CB    . PRO A 1 2768 ? 253.001 254.448 205.416 1.00 2.41  ? 2768 PRO A CB    1 
ATOM   10347 C  CG    . PRO A 1 2768 ? 254.039 253.493 205.854 1.00 4.35  ? 2768 PRO A CG    1 
ATOM   10348 C  CD    . PRO A 1 2768 ? 253.981 253.482 207.344 1.00 5.04  ? 2768 PRO A CD    1 
ATOM   10349 N  N     . LEU A 1 2769 ? 250.768 252.195 206.015 1.00 2.10  ? 2769 LEU A N     1 
ATOM   10350 C  CA    . LEU A 1 2769 ? 249.641 251.380 205.575 1.00 2.30  ? 2769 LEU A CA    1 
ATOM   10351 C  C     . LEU A 1 2769 ? 248.412 251.629 206.439 1.00 2.67  ? 2769 LEU A C     1 
ATOM   10352 O  O     . LEU A 1 2769 ? 247.294 251.748 205.922 1.00 3.98  ? 2769 LEU A O     1 
ATOM   10353 C  CB    . LEU A 1 2769 ? 250.020 249.899 205.598 1.00 2.87  ? 2769 LEU A CB    1 
ATOM   10354 C  CG    . LEU A 1 2769 ? 248.948 248.925 205.109 1.00 1.65  ? 2769 LEU A CG    1 
ATOM   10355 C  CD1   . LEU A 1 2769 ? 248.787 249.023 203.601 1.00 0.72  ? 2769 LEU A CD1   1 
ATOM   10356 C  CD2   . LEU A 1 2769 ? 249.279 247.506 205.530 1.00 1.71  ? 2769 LEU A CD2   1 
ATOM   10357 N  N     . THR A 1 2770 ? 248.599 251.710 207.758 1.00 2.01  ? 2770 THR A N     1 
ATOM   10358 C  CA    . THR A 1 2770 ? 247.487 252.027 208.648 1.00 1.33  ? 2770 THR A CA    1 
ATOM   10359 C  C     . THR A 1 2770 ? 246.964 253.435 208.397 1.00 1.51  ? 2770 THR A C     1 
ATOM   10360 O  O     . THR A 1 2770 ? 245.748 253.656 208.364 1.00 0.98  ? 2770 THR A O     1 
ATOM   10361 C  CB    . THR A 1 2770 ? 247.917 251.869 210.107 1.00 1.88  ? 2770 THR A CB    1 
ATOM   10362 O  OG1   . THR A 1 2770 ? 248.411 250.542 210.323 1.00 1.76  ? 2770 THR A OG1   1 
ATOM   10363 C  CG2   . THR A 1 2770 ? 246.746 252.126 211.043 1.00 0.71  ? 2770 THR A CG2   1 
ATOM   10364 N  N     . ALA A 1 2771 ? 247.870 254.398 208.214 1.00 1.48  ? 2771 ALA A N     1 
ATOM   10365 C  CA    . ALA A 1 2771 ? 247.454 255.780 207.999 1.00 1.83  ? 2771 ALA A CA    1 
ATOM   10366 C  C     . ALA A 1 2771 ? 246.648 255.922 206.716 1.00 2.31  ? 2771 ALA A C     1 
ATOM   10367 O  O     . ALA A 1 2771 ? 245.632 256.628 206.687 1.00 2.70  ? 2771 ALA A O     1 
ATOM   10368 C  CB    . ALA A 1 2771 ? 248.677 256.696 207.970 1.00 2.56  ? 2771 ALA A CB    1 
ATOM   10369 N  N     . ALA A 1 2772 ? 247.082 255.257 205.644 1.00 1.49  ? 2772 ALA A N     1 
ATOM   10370 C  CA    . ALA A 1 2772 ? 246.313 255.267 204.406 1.00 1.23  ? 2772 ALA A CA    1 
ATOM   10371 C  C     . ALA A 1 2772 ? 244.952 254.611 204.600 1.00 0.56  ? 2772 ALA A C     1 
ATOM   10372 O  O     . ALA A 1 2772 ? 243.943 255.086 204.066 1.00 0.66  ? 2772 ALA A O     1 
ATOM   10373 C  CB    . ALA A 1 2772 ? 247.099 254.568 203.296 1.00 1.02  ? 2772 ALA A CB    1 
ATOM   10374 N  N     . MET A 1 2773 ? 244.907 253.518 205.361 1.00 1.06  ? 2773 MET A N     1 
ATOM   10375 C  CA    . MET A 1 2773 ? 243.641 252.848 205.637 1.00 0.57  ? 2773 MET A CA    1 
ATOM   10376 C  C     . MET A 1 2773 ? 242.676 253.774 206.366 1.00 0.79  ? 2773 MET A C     1 
ATOM   10377 O  O     . MET A 1 2773 ? 241.505 253.893 205.989 1.00 0.66  ? 2773 MET A O     1 
ATOM   10378 C  CB    . MET A 1 2773 ? 243.893 251.590 206.465 1.00 0.58  ? 2773 MET A CB    1 
ATOM   10379 C  CG    . MET A 1 2773 ? 244.167 250.346 205.656 1.00 0.52  ? 2773 MET A CG    1 
ATOM   10380 S  SD    . MET A 1 2773 ? 244.362 248.905 206.715 1.00 7.16  ? 2773 MET A SD    1 
ATOM   10381 C  CE    . MET A 1 2773 ? 244.174 247.589 205.530 1.00 0.64  ? 2773 MET A CE    1 
ATOM   10382 N  N     . VAL A 1 2774 ? 243.158 254.446 207.413 1.00 2.17  ? 2774 VAL A N     1 
ATOM   10383 C  CA    . VAL A 1 2774 ? 242.293 255.320 208.201 1.00 1.02  ? 2774 VAL A CA    1 
ATOM   10384 C  C     . VAL A 1 2774 ? 241.851 256.523 207.378 1.00 0.98  ? 2774 VAL A C     1 
ATOM   10385 O  O     . VAL A 1 2774 ? 240.689 256.939 207.440 1.00 2.20  ? 2774 VAL A O     1 
ATOM   10386 C  CB    . VAL A 1 2774 ? 243.007 255.744 209.498 1.00 1.28  ? 2774 VAL A CB    1 
ATOM   10387 C  CG1   . VAL A 1 2774 ? 242.193 256.786 210.246 1.00 1.91  ? 2774 VAL A CG1   1 
ATOM   10388 C  CG2   . VAL A 1 2774 ? 243.260 254.535 210.383 1.00 0.66  ? 2774 VAL A CG2   1 
ATOM   10389 N  N     . GLU A 1 2775 ? 242.762 257.098 206.591 1.00 0.74  ? 2775 GLU A N     1 
ATOM   10390 C  CA    . GLU A 1 2775 ? 242.418 258.288 205.818 1.00 1.42  ? 2775 GLU A CA    1 
ATOM   10391 C  C     . GLU A 1 2775 ? 241.346 257.985 204.779 1.00 1.82  ? 2775 GLU A C     1 
ATOM   10392 O  O     . GLU A 1 2775 ? 240.347 258.707 204.676 1.00 2.40  ? 2775 GLU A O     1 
ATOM   10393 C  CB    . GLU A 1 2775 ? 243.664 258.867 205.150 1.00 4.37  ? 2775 GLU A CB    1 
ATOM   10394 C  CG    . GLU A 1 2775 ? 243.381 260.154 204.396 1.00 3.60  ? 2775 GLU A CG    1 
ATOM   10395 C  CD    . GLU A 1 2775 ? 244.617 260.757 203.778 1.00 11.78 ? 2775 GLU A CD    1 
ATOM   10396 O  OE1   . GLU A 1 2775 ? 245.704 260.164 203.921 1.00 14.99 ? 2775 GLU A OE1   1 
ATOM   10397 O  OE2   . GLU A 1 2775 ? 244.506 261.832 203.153 1.00 18.48 ? 2775 GLU A OE2   1 
ATOM   10398 N  N     . PHE A 1 2776 ? 241.532 256.921 203.995 1.00 0.71  ? 2776 PHE A N     1 
ATOM   10399 C  CA    . PHE A 1 2776 ? 240.552 256.606 202.963 1.00 0.67  ? 2776 PHE A CA    1 
ATOM   10400 C  C     . PHE A 1 2776 ? 239.222 256.176 203.571 1.00 0.88  ? 2776 PHE A C     1 
ATOM   10401 O  O     . PHE A 1 2776 ? 238.156 256.525 203.049 1.00 1.21  ? 2776 PHE A O     1 
ATOM   10402 C  CB    . PHE A 1 2776 ? 241.080 255.527 202.019 1.00 0.78  ? 2776 PHE A CB    1 
ATOM   10403 C  CG    . PHE A 1 2776 ? 240.157 255.245 200.875 1.00 1.03  ? 2776 PHE A CG    1 
ATOM   10404 C  CD1   . PHE A 1 2776 ? 240.101 256.103 199.790 1.00 2.23  ? 2776 PHE A CD1   1 
ATOM   10405 C  CD2   . PHE A 1 2776 ? 239.313 254.148 200.901 1.00 0.47  ? 2776 PHE A CD2   1 
ATOM   10406 C  CE1   . PHE A 1 2776 ? 239.235 255.860 198.745 1.00 2.64  ? 2776 PHE A CE1   1 
ATOM   10407 C  CE2   . PHE A 1 2776 ? 238.449 253.902 199.859 1.00 0.91  ? 2776 PHE A CE2   1 
ATOM   10408 C  CZ    . PHE A 1 2776 ? 238.409 254.760 198.779 1.00 2.02  ? 2776 PHE A CZ    1 
ATOM   10409 N  N     . TYR A 1 2777 ? 239.263 255.408 204.662 1.00 1.01  ? 2777 TYR A N     1 
ATOM   10410 C  CA    . TYR A 1 2777 ? 238.026 254.989 205.312 1.00 0.78  ? 2777 TYR A CA    1 
ATOM   10411 C  C     . TYR A 1 2777 ? 237.251 256.187 205.846 1.00 0.96  ? 2777 TYR A C     1 
ATOM   10412 O  O     . TYR A 1 2777 ? 236.024 256.254 205.709 1.00 1.17  ? 2777 TYR A O     1 
ATOM   10413 C  CB    . TYR A 1 2777 ? 238.329 254.006 206.440 1.00 0.59  ? 2777 TYR A CB    1 
ATOM   10414 C  CG    . TYR A 1 2777 ? 237.241 253.931 207.483 1.00 0.65  ? 2777 TYR A CG    1 
ATOM   10415 C  CD1   . TYR A 1 2777 ? 236.047 253.275 207.219 1.00 0.71  ? 2777 TYR A CD1   1 
ATOM   10416 C  CD2   . TYR A 1 2777 ? 237.401 254.522 208.728 1.00 0.78  ? 2777 TYR A CD2   1 
ATOM   10417 C  CE1   . TYR A 1 2777 ? 235.048 253.209 208.162 1.00 0.82  ? 2777 TYR A CE1   1 
ATOM   10418 C  CE2   . TYR A 1 2777 ? 236.406 254.457 209.680 1.00 0.64  ? 2777 TYR A CE2   1 
ATOM   10419 C  CZ    . TYR A 1 2777 ? 235.232 253.799 209.391 1.00 0.60  ? 2777 TYR A CZ    1 
ATOM   10420 O  OH    . TYR A 1 2777 ? 234.234 253.731 210.333 1.00 3.45  ? 2777 TYR A OH    1 
ATOM   10421 N  N     . THR A 1 2778 ? 237.949 257.139 206.470 1.00 1.00  ? 2778 THR A N     1 
ATOM   10422 C  CA    . THR A 1 2778 ? 237.285 258.335 206.976 1.00 1.14  ? 2778 THR A CA    1 
ATOM   10423 C  C     . THR A 1 2778 ? 236.713 259.170 205.838 1.00 1.18  ? 2778 THR A C     1 
ATOM   10424 O  O     . THR A 1 2778 ? 235.588 259.674 205.930 1.00 1.51  ? 2778 THR A O     1 
ATOM   10425 C  CB    . THR A 1 2778 ? 238.259 259.166 207.812 1.00 1.00  ? 2778 THR A CB    1 
ATOM   10426 O  OG1   . THR A 1 2778 ? 238.807 258.355 208.856 1.00 1.18  ? 2778 THR A OG1   1 
ATOM   10427 C  CG2   . THR A 1 2778 ? 237.549 260.358 208.430 1.00 4.63  ? 2778 THR A CG2   1 
ATOM   10428 N  N     . MET A 1 2779 ? 237.476 259.323 204.753 1.00 1.58  ? 2779 MET A N     1 
ATOM   10429 C  CA    . MET A 1 2779 ? 236.996 260.090 203.608 1.00 0.97  ? 2779 MET A CA    1 
ATOM   10430 C  C     . MET A 1 2779 ? 235.769 259.442 202.982 1.00 1.68  ? 2779 MET A C     1 
ATOM   10431 O  O     . MET A 1 2779 ? 234.808 260.134 202.628 1.00 3.57  ? 2779 MET A O     1 
ATOM   10432 C  CB    . MET A 1 2779 ? 238.113 260.237 202.576 1.00 0.92  ? 2779 MET A CB    1 
ATOM   10433 C  CG    . MET A 1 2779 ? 239.169 261.258 202.955 1.00 1.84  ? 2779 MET A CG    1 
ATOM   10434 S  SD    . MET A 1 2779 ? 240.729 261.004 202.091 1.00 16.87 ? 2779 MET A SD    1 
ATOM   10435 C  CE    . MET A 1 2779 ? 240.150 260.699 200.428 1.00 5.57  ? 2779 MET A CE    1 
ATOM   10436 N  N     . SER A 1 2780 ? 235.784 258.116 202.836 1.00 1.27  ? 2780 SER A N     1 
ATOM   10437 C  CA    . SER A 1 2780 ? 234.638 257.421 202.260 1.00 1.34  ? 2780 SER A CA    1 
ATOM   10438 C  C     . SER A 1 2780 ? 233.417 257.524 203.162 1.00 1.78  ? 2780 SER A C     1 
ATOM   10439 O  O     . SER A 1 2780 ? 232.292 257.695 202.678 1.00 3.69  ? 2780 SER A O     1 
ATOM   10440 C  CB    . SER A 1 2780 ? 234.990 255.957 201.997 1.00 2.45  ? 2780 SER A CB    1 
ATOM   10441 O  OG    . SER A 1 2780 ? 236.137 255.846 201.176 1.00 3.03  ? 2780 SER A OG    1 
ATOM   10442 N  N     . GLN A 1 2781 ? 233.619 257.420 204.476 1.00 1.89  ? 2781 GLN A N     1 
ATOM   10443 C  CA    . GLN A 1 2781 ? 232.504 257.501 205.410 1.00 1.39  ? 2781 GLN A CA    1 
ATOM   10444 C  C     . GLN A 1 2781 ? 231.865 258.886 205.381 1.00 2.31  ? 2781 GLN A C     1 
ATOM   10445 O  O     . GLN A 1 2781 ? 230.646 259.019 205.528 1.00 3.16  ? 2781 GLN A O     1 
ATOM   10446 C  CB    . GLN A 1 2781 ? 232.981 257.143 206.816 1.00 1.60  ? 2781 GLN A CB    1 
ATOM   10447 C  CG    . GLN A 1 2781 ? 231.884 257.067 207.858 1.00 1.82  ? 2781 GLN A CG    1 
ATOM   10448 C  CD    . GLN A 1 2781 ? 232.413 256.671 209.218 1.00 4.95  ? 2781 GLN A CD    1 
ATOM   10449 O  OE1   . GLN A 1 2781 ? 233.341 257.290 209.738 1.00 10.03 ? 2781 GLN A OE1   1 
ATOM   10450 N  NE2   . GLN A 1 2781 ? 231.828 255.633 209.803 1.00 2.63  ? 2781 GLN A NE2   1 
ATOM   10451 N  N     . GLU A 1 2782 ? 232.676 259.927 205.197 1.00 2.90  ? 2782 GLU A N     1 
ATOM   10452 C  CA    . GLU A 1 2782 ? 232.142 261.275 205.049 1.00 2.51  ? 2782 GLU A CA    1 
ATOM   10453 C  C     . GLU A 1 2782 ? 231.508 261.477 203.680 1.00 4.09  ? 2782 GLU A C     1 
ATOM   10454 O  O     . GLU A 1 2782 ? 230.428 262.068 203.573 1.00 4.75  ? 2782 GLU A O     1 
ATOM   10455 C  CB    . GLU A 1 2782 ? 233.258 262.298 205.297 1.00 2.13  ? 2782 GLU A CB    1 
ATOM   10456 C  CG    . GLU A 1 2782 ? 232.872 263.772 205.145 1.00 9.10  ? 2782 GLU A CG    1 
ATOM   10457 C  CD    . GLU A 1 2782 ? 232.822 264.244 203.704 1.00 17.80 ? 2782 GLU A CD    1 
ATOM   10458 O  OE1   . GLU A 1 2782 ? 233.792 263.991 202.957 1.00 19.20 ? 2782 GLU A OE1   1 
ATOM   10459 O  OE2   . GLU A 1 2782 ? 231.814 264.872 203.319 1.00 21.23 ? 2782 GLU A OE2   1 
ATOM   10460 N  N     . ARG A 1 2783 ? 232.164 260.991 202.623 1.00 3.13  ? 2783 ARG A N     1 
ATOM   10461 C  CA    . ARG A 1 2783 ? 231.692 261.233 201.263 1.00 2.83  ? 2783 ARG A CA    1 
ATOM   10462 C  C     . ARG A 1 2783 ? 230.343 260.572 201.006 1.00 2.92  ? 2783 ARG A C     1 
ATOM   10463 O  O     . ARG A 1 2783 ? 229.462 261.172 200.380 1.00 8.44  ? 2783 ARG A O     1 
ATOM   10464 C  CB    . ARG A 1 2783 ? 232.735 260.739 200.260 1.00 4.03  ? 2783 ARG A CB    1 
ATOM   10465 C  CG    . ARG A 1 2783 ? 232.304 260.783 198.806 1.00 3.38  ? 2783 ARG A CG    1 
ATOM   10466 C  CD    . ARG A 1 2783 ? 232.305 262.188 198.237 1.00 3.05  ? 2783 ARG A CD    1 
ATOM   10467 N  NE    . ARG A 1 2783 ? 232.067 262.194 196.797 1.00 6.69  ? 2783 ARG A NE    1 
ATOM   10468 C  CZ    . ARG A 1 2783 ? 230.912 261.891 196.217 1.00 9.55  ? 2783 ARG A CZ    1 
ATOM   10469 N  NH1   . ARG A 1 2783 ? 229.839 261.578 196.926 1.00 7.95  ? 2783 ARG A NH1   1 
ATOM   10470 N  NH2   . ARG A 1 2783 ? 230.831 261.906 194.890 1.00 8.37  ? 2783 ARG A NH2   1 
ATOM   10471 N  N     . PHE A 1 2784 ? 230.159 259.340 201.473 1.00 2.27  ? 2784 PHE A N     1 
ATOM   10472 C  CA    . PHE A 1 2784 ? 228.943 258.576 201.222 1.00 1.95  ? 2784 PHE A CA    1 
ATOM   10473 C  C     . PHE A 1 2784 ? 228.240 258.303 202.541 1.00 3.06  ? 2784 PHE A C     1 
ATOM   10474 O  O     . PHE A 1 2784 ? 228.838 257.738 203.462 1.00 9.15  ? 2784 PHE A O     1 
ATOM   10475 C  CB    . PHE A 1 2784 ? 229.259 257.270 200.492 1.00 2.12  ? 2784 PHE A CB    1 
ATOM   10476 C  CG    . PHE A 1 2784 ? 230.147 257.450 199.298 1.00 1.70  ? 2784 PHE A CG    1 
ATOM   10477 C  CD1   . PHE A 1 2784 ? 229.681 258.095 198.167 1.00 1.74  ? 2784 PHE A CD1   1 
ATOM   10478 C  CD2   . PHE A 1 2784 ? 231.448 256.983 199.307 1.00 2.60  ? 2784 PHE A CD2   1 
ATOM   10479 C  CE1   . PHE A 1 2784 ? 230.493 258.267 197.068 1.00 2.30  ? 2784 PHE A CE1   1 
ATOM   10480 C  CE2   . PHE A 1 2784 ? 232.265 257.153 198.207 1.00 2.92  ? 2784 PHE A CE2   1 
ATOM   10481 C  CZ    . PHE A 1 2784 ? 231.786 257.791 197.086 1.00 1.90  ? 2784 PHE A CZ    1 
ATOM   10482 N  N     . THR A 1 2785 ? 226.974 258.702 202.628 1.00 2.57  ? 2785 THR A N     1 
ATOM   10483 C  CA    . THR A 1 2785 ? 226.186 258.591 203.845 1.00 2.81  ? 2785 THR A CA    1 
ATOM   10484 C  C     . THR A 1 2785 ? 224.824 257.997 203.514 1.00 3.35  ? 2785 THR A C     1 
ATOM   10485 O  O     . THR A 1 2785 ? 224.465 257.823 202.347 1.00 3.46  ? 2785 THR A O     1 
ATOM   10486 C  CB    . THR A 1 2785 ? 226.017 259.957 204.532 1.00 4.47  ? 2785 THR A CB    1 
ATOM   10487 O  OG1   . THR A 1 2785 ? 225.276 260.836 203.678 1.00 4.49  ? 2785 THR A OG1   1 
ATOM   10488 C  CG2   . THR A 1 2785 ? 227.370 260.580 204.838 1.00 1.83  ? 2785 THR A CG2   1 
ATOM   10489 N  N     . GLN A 1 2786 ? 224.060 257.690 204.565 1.00 4.90  ? 2786 GLN A N     1 
ATOM   10490 C  CA    . GLN A 1 2786 ? 222.731 257.118 204.379 1.00 3.99  ? 2786 GLN A CA    1 
ATOM   10491 C  C     . GLN A 1 2786 ? 221.775 258.080 203.690 1.00 6.05  ? 2786 GLN A C     1 
ATOM   10492 O  O     . GLN A 1 2786 ? 220.728 257.646 203.198 1.00 9.43  ? 2786 GLN A O     1 
ATOM   10493 C  CB    . GLN A 1 2786 ? 222.139 256.687 205.723 1.00 6.59  ? 2786 GLN A CB    1 
ATOM   10494 C  CG    . GLN A 1 2786 ? 222.712 255.400 206.278 1.00 11.57 ? 2786 GLN A CG    1 
ATOM   10495 C  CD    . GLN A 1 2786 ? 221.855 254.816 207.386 1.00 14.26 ? 2786 GLN A CD    1 
ATOM   10496 O  OE1   . GLN A 1 2786 ? 222.262 254.779 208.545 1.00 21.52 ? 2786 GLN A OE1   1 
ATOM   10497 N  NE2   . GLN A 1 2786 ? 220.664 254.350 207.030 1.00 10.89 ? 2786 GLN A NE2   1 
ATOM   10498 N  N     . ASP A 1 2787 ? 222.101 259.374 203.653 1.00 6.27  ? 2787 ASP A N     1 
ATOM   10499 C  CA    . ASP A 1 2787 ? 221.246 260.332 202.962 1.00 5.00  ? 2787 ASP A CA    1 
ATOM   10500 C  C     . ASP A 1 2787 ? 221.195 260.048 201.467 1.00 8.57  ? 2787 ASP A C     1 
ATOM   10501 O  O     . ASP A 1 2787 ? 220.129 260.134 200.848 1.00 7.65  ? 2787 ASP A O     1 
ATOM   10502 C  CB    . ASP A 1 2787 ? 221.735 261.756 203.224 1.00 6.04  ? 2787 ASP A CB    1 
ATOM   10503 C  CG    . ASP A 1 2787 ? 221.826 262.079 204.701 1.00 23.05 ? 2787 ASP A CG    1 
ATOM   10504 O  OD1   . ASP A 1 2787 ? 220.771 262.314 205.328 1.00 21.23 ? 2787 ASP A OD1   1 
ATOM   10505 O  OD2   . ASP A 1 2787 ? 222.954 262.099 205.238 1.00 27.17 ? 2787 ASP A OD2   1 
ATOM   10506 N  N     . THR A 1 2788 ? 222.338 259.707 200.869 1.00 5.74  ? 2788 THR A N     1 
ATOM   10507 C  CA    . THR A 1 2788 ? 222.370 259.414 199.440 1.00 4.40  ? 2788 THR A CA    1 
ATOM   10508 C  C     . THR A 1 2788 ? 221.714 258.070 199.147 1.00 5.41  ? 2788 THR A C     1 
ATOM   10509 O  O     . THR A 1 2788 ? 220.742 257.993 198.388 1.00 5.92  ? 2788 THR A O     1 
ATOM   10510 C  CB    . THR A 1 2788 ? 223.815 259.439 198.931 1.00 6.57  ? 2788 THR A CB    1 
ATOM   10511 O  OG1   . THR A 1 2788 ? 224.276 260.792 198.863 1.00 17.88 ? 2788 THR A OG1   1 
ATOM   10512 C  CG2   . THR A 1 2788 ? 223.899 258.825 197.545 1.00 4.56  ? 2788 THR A CG2   1 
ATOM   10513 N  N     . GLN A 1 2789 ? 222.232 257.000 199.740 1.00 5.59  ? 2789 GLN A N     1 
ATOM   10514 C  CA    . GLN A 1 2789 ? 221.688 255.665 199.554 1.00 5.69  ? 2789 GLN A CA    1 
ATOM   10515 C  C     . GLN A 1 2789 ? 221.547 254.968 200.897 1.00 5.67  ? 2789 GLN A C     1 
ATOM   10516 O  O     . GLN A 1 2789 ? 222.360 255.181 201.801 1.00 6.72  ? 2789 GLN A O     1 
ATOM   10517 C  CB    . GLN A 1 2789 ? 222.578 254.826 198.625 1.00 2.62  ? 2789 GLN A CB    1 
ATOM   10518 C  CG    . GLN A 1 2789 ? 222.725 255.404 197.231 1.00 2.26  ? 2789 GLN A CG    1 
ATOM   10519 C  CD    . GLN A 1 2789 ? 221.495 255.184 196.371 1.00 5.08  ? 2789 GLN A CD    1 
ATOM   10520 O  OE1   . GLN A 1 2789 ? 220.605 254.410 196.719 1.00 5.06  ? 2789 GLN A OE1   1 
ATOM   10521 N  NE2   . GLN A 1 2789 ? 221.437 255.876 195.240 1.00 3.22  ? 2789 GLN A NE2   1 
ATOM   10522 N  N     . PRO A 1 2790 ? 220.524 254.122 201.053 1.00 7.72  ? 2790 PRO A N     1 
ATOM   10523 C  CA    . PRO A 1 2790 ? 220.283 253.484 202.356 1.00 4.22  ? 2790 PRO A CA    1 
ATOM   10524 C  C     . PRO A 1 2790 ? 221.360 252.507 202.783 1.00 3.19  ? 2790 PRO A C     1 
ATOM   10525 O  O     . PRO A 1 2790 ? 221.405 252.157 203.967 1.00 8.61  ? 2790 PRO A O     1 
ATOM   10526 C  CB    . PRO A 1 2790 ? 218.945 252.767 202.146 1.00 4.69  ? 2790 PRO A CB    1 
ATOM   10527 C  CG    . PRO A 1 2790 ? 218.923 252.479 200.690 1.00 8.24  ? 2790 PRO A CG    1 
ATOM   10528 C  CD    . PRO A 1 2790 ? 219.542 253.686 200.046 1.00 4.74  ? 2790 PRO A CD    1 
ATOM   10529 N  N     . HIS A 1 2791 ? 222.207 252.039 201.870 1.00 2.86  ? 2791 HIS A N     1 
ATOM   10530 C  CA    . HIS A 1 2791 ? 223.241 251.065 202.190 1.00 1.66  ? 2791 HIS A CA    1 
ATOM   10531 C  C     . HIS A 1 2791 ? 224.630 251.683 202.251 1.00 1.74  ? 2791 HIS A C     1 
ATOM   10532 O  O     . HIS A 1 2791 ? 225.625 250.952 202.262 1.00 5.42  ? 2791 HIS A O     1 
ATOM   10533 C  CB    . HIS A 1 2791 ? 223.212 249.915 201.179 1.00 1.50  ? 2791 HIS A CB    1 
ATOM   10534 C  CG    . HIS A 1 2791 ? 223.550 250.325 199.782 1.00 1.24  ? 2791 HIS A CG    1 
ATOM   10535 N  ND1   . HIS A 1 2791 ? 222.663 250.995 198.966 1.00 1.74  ? 2791 HIS A ND1   1 
ATOM   10536 C  CD2   . HIS A 1 2791 ? 224.675 250.153 199.050 1.00 0.98  ? 2791 HIS A CD2   1 
ATOM   10537 C  CE1   . HIS A 1 2791 ? 223.230 251.221 197.795 1.00 1.14  ? 2791 HIS A CE1   1 
ATOM   10538 N  NE2   . HIS A 1 2791 ? 224.452 250.720 197.820 1.00 0.53  ? 2791 HIS A NE2   1 
ATOM   10539 N  N     . TYR A 1 2792 ? 224.726 253.012 202.291 1.00 2.23  ? 2792 TYR A N     1 
ATOM   10540 C  CA    . TYR A 1 2792 ? 226.015 253.694 202.397 1.00 2.53  ? 2792 TYR A CA    1 
ATOM   10541 C  C     . TYR A 1 2792 ? 226.386 253.853 203.872 1.00 3.28  ? 2792 TYR A C     1 
ATOM   10542 O  O     . TYR A 1 2792 ? 226.412 254.948 204.434 1.00 5.93  ? 2792 TYR A O     1 
ATOM   10543 C  CB    . TYR A 1 2792 ? 225.966 255.040 201.686 1.00 2.30  ? 2792 TYR A CB    1 
ATOM   10544 C  CG    . TYR A 1 2792 ? 226.032 254.973 200.176 1.00 2.24  ? 2792 TYR A CG    1 
ATOM   10545 C  CD1   . TYR A 1 2792 ? 225.998 253.755 199.506 1.00 1.74  ? 2792 TYR A CD1   1 
ATOM   10546 C  CD2   . TYR A 1 2792 ? 226.122 256.132 199.418 1.00 1.79  ? 2792 TYR A CD2   1 
ATOM   10547 C  CE1   . TYR A 1 2792 ? 226.058 253.697 198.127 1.00 1.03  ? 2792 TYR A CE1   1 
ATOM   10548 C  CE2   . TYR A 1 2792 ? 226.181 256.085 198.043 1.00 2.01  ? 2792 TYR A CE2   1 
ATOM   10549 C  CZ    . TYR A 1 2792 ? 226.150 254.868 197.399 1.00 2.55  ? 2792 TYR A CZ    1 
ATOM   10550 O  OH    . TYR A 1 2792 ? 226.209 254.827 196.028 1.00 2.66  ? 2792 TYR A OH    1 
ATOM   10551 N  N     . ILE A 1 2793 ? 226.668 252.718 204.504 1.00 3.26  ? 2793 ILE A N     1 
ATOM   10552 C  CA    . ILE A 1 2793 ? 227.121 252.673 205.889 1.00 2.38  ? 2793 ILE A CA    1 
ATOM   10553 C  C     . ILE A 1 2793 ? 228.535 252.120 205.885 1.00 2.18  ? 2793 ILE A C     1 
ATOM   10554 O  O     . ILE A 1 2793 ? 228.763 250.974 205.479 1.00 4.14  ? 2793 ILE A O     1 
ATOM   10555 C  CB    . ILE A 1 2793 ? 226.205 251.823 206.782 1.00 4.89  ? 2793 ILE A CB    1 
ATOM   10556 C  CG1   . ILE A 1 2793 ? 224.796 252.412 206.855 1.00 3.34  ? 2793 ILE A CG1   1 
ATOM   10557 C  CG2   . ILE A 1 2793 ? 226.799 251.687 208.176 1.00 5.00  ? 2793 ILE A CG2   1 
ATOM   10558 C  CD1   . ILE A 1 2793 ? 223.877 251.918 205.780 1.00 8.29  ? 2793 ILE A CD1   1 
ATOM   10559 N  N     . TYR A 1 2794 ? 229.483 252.925 206.345 1.00 1.81  ? 2794 TYR A N     1 
ATOM   10560 C  CA    . TYR A 1 2794 ? 230.867 252.507 206.483 1.00 1.05  ? 2794 TYR A CA    1 
ATOM   10561 C  C     . TYR A 1 2794 ? 231.236 252.523 207.958 1.00 1.06  ? 2794 TYR A C     1 
ATOM   10562 O  O     . TYR A 1 2794 ? 230.984 253.509 208.657 1.00 3.28  ? 2794 TYR A O     1 
ATOM   10563 C  CB    . TYR A 1 2794 ? 231.795 253.406 205.667 1.00 1.22  ? 2794 TYR A CB    1 
ATOM   10564 C  CG    . TYR A 1 2794 ? 231.534 253.319 204.181 1.00 2.82  ? 2794 TYR A CG    1 
ATOM   10565 C  CD1   . TYR A 1 2794 ? 232.035 252.265 203.430 1.00 2.51  ? 2794 TYR A CD1   1 
ATOM   10566 C  CD2   . TYR A 1 2794 ? 230.770 254.279 203.533 1.00 1.83  ? 2794 TYR A CD2   1 
ATOM   10567 C  CE1   . TYR A 1 2794 ? 231.794 252.175 202.075 1.00 2.40  ? 2794 TYR A CE1   1 
ATOM   10568 C  CE2   . TYR A 1 2794 ? 230.524 254.199 202.179 1.00 1.46  ? 2794 TYR A CE2   1 
ATOM   10569 C  CZ    . TYR A 1 2794 ? 231.039 253.145 201.454 1.00 4.13  ? 2794 TYR A CZ    1 
ATOM   10570 O  OH    . TYR A 1 2794 ? 230.796 253.062 200.104 1.00 9.18  ? 2794 TYR A OH    1 
ATOM   10571 N  N     . SER A 1 2795 ? 231.817 251.429 208.422 1.00 0.90  ? 2795 SER A N     1 
ATOM   10572 C  CA    . SER A 1 2795 ? 232.100 251.226 209.833 1.00 0.58  ? 2795 SER A CA    1 
ATOM   10573 C  C     . SER A 1 2795 ? 233.463 250.561 209.975 1.00 0.63  ? 2795 SER A C     1 
ATOM   10574 O  O     . SER A 1 2795 ? 234.073 250.196 208.964 1.00 0.79  ? 2795 SER A O     1 
ATOM   10575 C  CB    . SER A 1 2795 ? 230.999 250.376 210.472 1.00 0.51  ? 2795 SER A CB    1 
ATOM   10576 O  OG    . SER A 1 2795 ? 230.944 249.085 209.897 1.00 0.66  ? 2795 SER A OG    1 
ATOM   10577 N  N     . PRO A 1 2796 ? 233.979 250.389 211.197 1.00 0.73  ? 2796 PRO A N     1 
ATOM   10578 C  CA    . PRO A 1 2796 ? 235.209 249.600 211.369 1.00 0.68  ? 2796 PRO A CA    1 
ATOM   10579 C  C     . PRO A 1 2796 ? 235.092 248.163 210.888 1.00 0.28  ? 2796 PRO A C     1 
ATOM   10580 O  O     . PRO A 1 2796 ? 236.114 247.469 210.832 1.00 0.37  ? 2796 PRO A O     1 
ATOM   10581 C  CB    . PRO A 1 2796 ? 235.455 249.665 212.880 1.00 0.29  ? 2796 PRO A CB    1 
ATOM   10582 C  CG    . PRO A 1 2796 ? 234.863 250.961 213.274 1.00 0.37  ? 2796 PRO A CG    1 
ATOM   10583 C  CD    . PRO A 1 2796 ? 233.627 251.106 212.438 1.00 0.25  ? 2796 PRO A CD    1 
ATOM   10584 N  N     . ARG A 1 2797 ? 233.891 247.697 210.545 1.00 0.39  ? 2797 ARG A N     1 
ATOM   10585 C  CA    . ARG A 1 2797 ? 233.753 246.384 209.925 1.00 1.22  ? 2797 ARG A CA    1 
ATOM   10586 C  C     . ARG A 1 2797 ? 234.483 246.334 208.588 1.00 1.60  ? 2797 ARG A C     1 
ATOM   10587 O  O     . ARG A 1 2797 ? 235.109 245.322 208.253 1.00 2.51  ? 2797 ARG A O     1 
ATOM   10588 C  CB    . ARG A 1 2797 ? 232.275 246.043 209.748 1.00 0.68  ? 2797 ARG A CB    1 
ATOM   10589 C  CG    . ARG A 1 2797 ? 231.704 245.230 210.888 1.00 0.83  ? 2797 ARG A CG    1 
ATOM   10590 C  CD    . ARG A 1 2797 ? 230.368 244.616 210.527 1.00 2.20  ? 2797 ARG A CD    1 
ATOM   10591 N  NE    . ARG A 1 2797 ? 229.340 245.623 210.297 1.00 5.06  ? 2797 ARG A NE    1 
ATOM   10592 C  CZ    . ARG A 1 2797 ? 228.267 245.780 211.061 1.00 3.21  ? 2797 ARG A CZ    1 
ATOM   10593 N  NH1   . ARG A 1 2797 ? 228.072 245.036 212.137 1.00 2.92  ? 2797 ARG A NH1   1 
ATOM   10594 N  NH2   . ARG A 1 2797 ? 227.372 246.708 210.739 1.00 0.91  ? 2797 ARG A NH2   1 
ATOM   10595 N  N     . GLU A 1 2798 ? 234.410 247.418 207.813 1.00 1.27  ? 2798 GLU A N     1 
ATOM   10596 C  CA    . GLU A 1 2798 ? 235.185 247.504 206.579 1.00 1.13  ? 2798 GLU A CA    1 
ATOM   10597 C  C     . GLU A 1 2798 ? 236.680 247.508 206.863 1.00 0.72  ? 2798 GLU A C     1 
ATOM   10598 O  O     . GLU A 1 2798 ? 237.462 246.917 206.110 1.00 1.11  ? 2798 GLU A O     1 
ATOM   10599 C  CB    . GLU A 1 2798 ? 234.781 248.752 205.792 1.00 0.98  ? 2798 GLU A CB    1 
ATOM   10600 C  CG    . GLU A 1 2798 ? 233.581 248.545 204.883 1.00 1.42  ? 2798 GLU A CG    1 
ATOM   10601 C  CD    . GLU A 1 2798 ? 232.329 248.162 205.643 1.00 8.90  ? 2798 GLU A CD    1 
ATOM   10602 O  OE1   . GLU A 1 2798 ? 231.804 249.006 206.396 1.00 4.50  ? 2798 GLU A OE1   1 
ATOM   10603 O  OE2   . GLU A 1 2798 ? 231.876 247.007 205.491 1.00 17.30 ? 2798 GLU A OE2   1 
ATOM   10604 N  N     . MET A 1 2799 ? 237.098 248.174 207.942 1.00 1.07  ? 2799 MET A N     1 
ATOM   10605 C  CA    . MET A 1 2799 ? 238.505 248.147 208.329 1.00 0.52  ? 2799 MET A CA    1 
ATOM   10606 C  C     . MET A 1 2799 ? 238.950 246.735 208.694 1.00 0.66  ? 2799 MET A C     1 
ATOM   10607 O  O     . MET A 1 2799 ? 240.055 246.313 208.336 1.00 0.87  ? 2799 MET A O     1 
ATOM   10608 C  CB    . MET A 1 2799 ? 238.746 249.104 209.493 1.00 0.41  ? 2799 MET A CB    1 
ATOM   10609 C  CG    . MET A 1 2799 ? 238.525 250.571 209.162 1.00 1.07  ? 2799 MET A CG    1 
ATOM   10610 S  SD    . MET A 1 2799 ? 239.804 251.260 208.099 1.00 11.93 ? 2799 MET A SD    1 
ATOM   10611 C  CE    . MET A 1 2799 ? 241.259 251.022 209.111 1.00 0.28  ? 2799 MET A CE    1 
ATOM   10612 N  N     . THR A 1 2800 ? 238.104 245.992 209.409 1.00 0.71  ? 2800 THR A N     1 
ATOM   10613 C  CA    . THR A 1 2800 ? 238.433 244.613 209.754 1.00 0.56  ? 2800 THR A CA    1 
ATOM   10614 C  C     . THR A 1 2800 ? 238.525 243.743 208.506 1.00 0.72  ? 2800 THR A C     1 
ATOM   10615 O  O     . THR A 1 2800 ? 239.441 242.924 208.372 1.00 1.15  ? 2800 THR A O     1 
ATOM   10616 C  CB    . THR A 1 2800 ? 237.395 244.058 210.731 1.00 0.84  ? 2800 THR A CB    1 
ATOM   10617 O  OG1   . THR A 1 2800 ? 237.327 244.901 211.885 1.00 0.80  ? 2800 THR A OG1   1 
ATOM   10618 C  CG2   . THR A 1 2800 ? 237.761 242.647 211.163 1.00 1.23  ? 2800 THR A CG2   1 
ATOM   10619 N  N     . ARG A 1 2801 ? 237.583 243.913 207.576 1.00 0.64  ? 2801 ARG A N     1 
ATOM   10620 C  CA    . ARG A 1 2801 ? 237.642 243.176 206.317 1.00 0.58  ? 2801 ARG A CA    1 
ATOM   10621 C  C     . ARG A 1 2801 ? 238.836 243.614 205.479 1.00 0.92  ? 2801 ARG A C     1 
ATOM   10622 O  O     . ARG A 1 2801 ? 239.430 242.803 204.760 1.00 0.98  ? 2801 ARG A O     1 
ATOM   10623 C  CB    . ARG A 1 2801 ? 236.340 243.366 205.540 1.00 0.78  ? 2801 ARG A CB    1 
ATOM   10624 C  CG    . ARG A 1 2801 ? 235.177 242.555 206.079 1.00 6.97  ? 2801 ARG A CG    1 
ATOM   10625 C  CD    . ARG A 1 2801 ? 233.848 243.217 205.770 1.00 9.72  ? 2801 ARG A CD    1 
ATOM   10626 N  NE    . ARG A 1 2801 ? 232.747 242.591 206.495 1.00 19.73 ? 2801 ARG A NE    1 
ATOM   10627 C  CZ    . ARG A 1 2801 ? 231.571 243.163 206.711 1.00 13.53 ? 2801 ARG A CZ    1 
ATOM   10628 N  NH1   . ARG A 1 2801 ? 231.305 244.383 206.273 1.00 11.60 ? 2801 ARG A NH1   1 
ATOM   10629 N  NH2   . ARG A 1 2801 ? 230.638 242.496 207.383 1.00 9.37  ? 2801 ARG A NH2   1 
ATOM   10630 N  N     . TRP A 1 2802 ? 239.198 244.896 205.560 1.00 0.55  ? 2802 TRP A N     1 
ATOM   10631 C  CA    . TRP A 1 2802 ? 240.336 245.410 204.807 1.00 0.44  ? 2802 TRP A CA    1 
ATOM   10632 C  C     . TRP A 1 2802 ? 241.626 244.728 205.237 1.00 0.59  ? 2802 TRP A C     1 
ATOM   10633 O  O     . TRP A 1 2802 ? 242.430 244.301 204.400 1.00 1.08  ? 2802 TRP A O     1 
ATOM   10634 C  CB    . TRP A 1 2802 ? 240.439 246.921 205.010 1.00 0.73  ? 2802 TRP A CB    1 
ATOM   10635 C  CG    . TRP A 1 2802 ? 241.133 247.659 203.916 1.00 0.44  ? 2802 TRP A CG    1 
ATOM   10636 C  CD1   . TRP A 1 2802 ? 241.967 247.142 202.970 1.00 0.29  ? 2802 TRP A CD1   1 
ATOM   10637 C  CD2   . TRP A 1 2802 ? 241.080 249.067 203.677 1.00 0.49  ? 2802 TRP A CD2   1 
ATOM   10638 N  NE1   . TRP A 1 2802 ? 242.422 248.138 202.146 1.00 0.23  ? 2802 TRP A NE1   1 
ATOM   10639 C  CE2   . TRP A 1 2802 ? 241.892 249.331 202.559 1.00 0.35  ? 2802 TRP A CE2   1 
ATOM   10640 C  CE3   . TRP A 1 2802 ? 240.415 250.130 204.295 1.00 0.67  ? 2802 TRP A CE3   1 
ATOM   10641 C  CZ2   . TRP A 1 2802 ? 242.056 250.613 202.047 1.00 0.60  ? 2802 TRP A CZ2   1 
ATOM   10642 C  CZ3   . TRP A 1 2802 ? 240.582 251.400 203.785 1.00 0.42  ? 2802 TRP A CZ3   1 
ATOM   10643 C  CH2   . TRP A 1 2802 ? 241.396 251.632 202.674 1.00 0.39  ? 2802 TRP A CH2   1 
ATOM   10644 N  N     . VAL A 1 2803 ? 241.839 244.618 206.547 1.00 1.25  ? 2803 VAL A N     1 
ATOM   10645 C  CA    . VAL A 1 2803 ? 243.055 243.995 207.059 1.00 1.09  ? 2803 VAL A CA    1 
ATOM   10646 C  C     . VAL A 1 2803 ? 243.033 242.494 206.796 1.00 1.08  ? 2803 VAL A C     1 
ATOM   10647 O  O     . VAL A 1 2803 ? 244.047 241.901 206.411 1.00 2.08  ? 2803 VAL A O     1 
ATOM   10648 C  CB    . VAL A 1 2803 ? 243.217 244.315 208.556 1.00 1.01  ? 2803 VAL A CB    1 
ATOM   10649 C  CG1   . VAL A 1 2803 ? 244.380 243.544 209.144 1.00 1.69  ? 2803 VAL A CG1   1 
ATOM   10650 C  CG2   . VAL A 1 2803 ? 243.406 245.807 208.756 1.00 1.02  ? 2803 VAL A CG2   1 
ATOM   10651 N  N     . ARG A 1 2804 ? 241.875 241.860 206.997 1.00 1.11  ? 2804 ARG A N     1 
ATOM   10652 C  CA    . ARG A 1 2804 ? 241.741 240.437 206.700 1.00 2.61  ? 2804 ARG A CA    1 
ATOM   10653 C  C     . ARG A 1 2804 ? 241.979 240.145 205.224 1.00 3.42  ? 2804 ARG A C     1 
ATOM   10654 O  O     . ARG A 1 2804 ? 242.648 239.165 204.882 1.00 4.62  ? 2804 ARG A O     1 
ATOM   10655 C  CB    . ARG A 1 2804 ? 240.361 239.940 207.133 1.00 3.84  ? 2804 ARG A CB    1 
ATOM   10656 C  CG    . ARG A 1 2804 ? 240.310 238.459 207.473 1.00 10.28 ? 2804 ARG A CG    1 
ATOM   10657 C  CD    . ARG A 1 2804 ? 241.149 238.093 208.684 1.00 10.00 ? 2804 ARG A CD    1 
ATOM   10658 N  NE    . ARG A 1 2804 ? 241.624 236.718 208.594 1.00 17.40 ? 2804 ARG A NE    1 
ATOM   10659 C  CZ    . ARG A 1 2804 ? 242.370 236.114 209.510 1.00 22.76 ? 2804 ARG A CZ    1 
ATOM   10660 N  NH1   . ARG A 1 2804 ? 242.729 236.730 210.624 1.00 14.36 ? 2804 ARG A NH1   1 
ATOM   10661 N  NH2   . ARG A 1 2804 ? 242.762 234.860 209.303 1.00 23.90 ? 2804 ARG A NH2   1 
ATOM   10662 N  N     . GLY A 1 2805 ? 241.439 240.983 204.337 1.00 3.02  ? 2805 GLY A N     1 
ATOM   10663 C  CA    . GLY A 1 2805 ? 241.620 240.753 202.913 1.00 2.22  ? 2805 GLY A CA    1 
ATOM   10664 C  C     . GLY A 1 2805 ? 243.076 240.810 202.494 1.00 2.26  ? 2805 GLY A C     1 
ATOM   10665 O  O     . GLY A 1 2805 ? 243.549 239.967 201.729 1.00 6.16  ? 2805 GLY A O     1 
ATOM   10666 N  N     . ILE A 1 2806 ? 243.807 241.810 202.989 1.00 1.75  ? 2806 ILE A N     1 
ATOM   10667 C  CA    . ILE A 1 2806 ? 245.236 241.898 202.704 1.00 3.46  ? 2806 ILE A CA    1 
ATOM   10668 C  C     . ILE A 1 2806 ? 245.973 240.713 203.311 1.00 4.13  ? 2806 ILE A C     1 
ATOM   10669 O  O     . ILE A 1 2806 ? 246.877 240.139 202.694 1.00 4.01  ? 2806 ILE A O     1 
ATOM   10670 C  CB    . ILE A 1 2806 ? 245.802 243.238 203.206 1.00 0.99  ? 2806 ILE A CB    1 
ATOM   10671 C  CG1   . ILE A 1 2806 ? 245.107 244.407 202.509 1.00 1.07  ? 2806 ILE A CG1   1 
ATOM   10672 C  CG2   . ILE A 1 2806 ? 247.307 243.295 203.006 1.00 0.54  ? 2806 ILE A CG2   1 
ATOM   10673 C  CD1   . ILE A 1 2806 ? 245.707 245.750 202.830 1.00 0.91  ? 2806 ILE A CD1   1 
ATOM   10674 N  N     . PHE A 1 2807 ? 245.596 240.330 204.532 1.00 3.57  ? 2807 PHE A N     1 
ATOM   10675 C  CA    . PHE A 1 2807 ? 246.261 239.226 205.212 1.00 3.64  ? 2807 PHE A CA    1 
ATOM   10676 C  C     . PHE A 1 2807 ? 246.078 237.911 204.462 1.00 5.73  ? 2807 PHE A C     1 
ATOM   10677 O  O     . PHE A 1 2807 ? 247.021 237.120 204.346 1.00 10.08 ? 2807 PHE A O     1 
ATOM   10678 C  CB    . PHE A 1 2807 ? 245.739 239.117 206.644 1.00 3.33  ? 2807 PHE A CB    1 
ATOM   10679 C  CG    . PHE A 1 2807 ? 246.215 237.903 207.370 1.00 10.34 ? 2807 PHE A CG    1 
ATOM   10680 C  CD1   . PHE A 1 2807 ? 247.489 237.857 207.903 1.00 7.46  ? 2807 PHE A CD1   1 
ATOM   10681 C  CD2   . PHE A 1 2807 ? 245.378 236.816 207.549 1.00 12.85 ? 2807 PHE A CD2   1 
ATOM   10682 C  CE1   . PHE A 1 2807 ? 247.930 236.741 208.573 1.00 9.48  ? 2807 PHE A CE1   1 
ATOM   10683 C  CE2   . PHE A 1 2807 ? 245.812 235.703 208.227 1.00 10.92 ? 2807 PHE A CE2   1 
ATOM   10684 C  CZ    . PHE A 1 2807 ? 247.089 235.662 208.739 1.00 9.52  ? 2807 PHE A CZ    1 
ATOM   10685 N  N     . GLU A 1 2808 ? 244.874 237.662 203.943 1.00 5.38  ? 2808 GLU A N     1 
ATOM   10686 C  CA    . GLU A 1 2808 ? 244.635 236.438 203.186 1.00 5.94  ? 2808 GLU A CA    1 
ATOM   10687 C  C     . GLU A 1 2808 ? 245.454 236.399 201.902 1.00 7.65  ? 2808 GLU A C     1 
ATOM   10688 O  O     . GLU A 1 2808 ? 245.881 235.323 201.473 1.00 10.75 ? 2808 GLU A O     1 
ATOM   10689 C  CB    . GLU A 1 2808 ? 243.146 236.296 202.875 1.00 6.04  ? 2808 GLU A CB    1 
ATOM   10690 C  CG    . GLU A 1 2808 ? 242.282 236.152 204.114 1.00 13.32 ? 2808 GLU A CG    1 
ATOM   10691 C  CD    . GLU A 1 2808 ? 240.830 236.494 203.859 1.00 20.36 ? 2808 GLU A CD    1 
ATOM   10692 O  OE1   . GLU A 1 2808 ? 240.486 236.812 202.701 1.00 16.41 ? 2808 GLU A OE1   1 
ATOM   10693 O  OE2   . GLU A 1 2808 ? 240.034 236.453 204.821 1.00 18.38 ? 2808 GLU A OE2   1 
ATOM   10694 N  N     . ALA A 1 2809 ? 245.683 237.555 201.281 1.00 5.47  ? 2809 ALA A N     1 
ATOM   10695 C  CA    . ALA A 1 2809 ? 246.487 237.632 200.071 1.00 3.03  ? 2809 ALA A CA    1 
ATOM   10696 C  C     . ALA A 1 2809 ? 247.984 237.636 200.350 1.00 6.53  ? 2809 ALA A C     1 
ATOM   10697 O  O     . ALA A 1 2809 ? 248.772 237.626 199.397 1.00 16.15 ? 2809 ALA A O     1 
ATOM   10698 C  CB    . ALA A 1 2809 ? 246.112 238.881 199.271 1.00 3.07  ? 2809 ALA A CB    1 
ATOM   10699 N  N     . LEU A 1 2810 ? 248.395 237.659 201.619 1.00 5.89  ? 2810 LEU A N     1 
ATOM   10700 C  CA    . LEU A 1 2810 ? 249.804 237.698 201.974 1.00 4.32  ? 2810 LEU A CA    1 
ATOM   10701 C  C     . LEU A 1 2810 ? 250.318 236.418 202.618 1.00 11.93 ? 2810 LEU A C     1 
ATOM   10702 O  O     . LEU A 1 2810 ? 251.535 236.212 202.643 1.00 17.14 ? 2810 LEU A O     1 
ATOM   10703 C  CB    . LEU A 1 2810 ? 250.080 238.872 202.927 1.00 5.62  ? 2810 LEU A CB    1 
ATOM   10704 C  CG    . LEU A 1 2810 ? 250.243 240.270 202.329 1.00 3.43  ? 2810 LEU A CG    1 
ATOM   10705 C  CD1   . LEU A 1 2810 ? 250.409 241.300 203.430 1.00 4.44  ? 2810 LEU A CD1   1 
ATOM   10706 C  CD2   . LEU A 1 2810 ? 251.421 240.320 201.379 1.00 10.03 ? 2810 LEU A CD2   1 
ATOM   10707 N  N     . ARG A 1 2811 ? 249.434 235.560 203.135 1.00 7.69  ? 2811 ARG A N     1 
ATOM   10708 C  CA    . ARG A 1 2811 ? 249.883 234.338 203.805 1.00 11.54 ? 2811 ARG A CA    1 
ATOM   10709 C  C     . ARG A 1 2811 ? 250.713 233.419 202.918 1.00 13.15 ? 2811 ARG A C     1 
ATOM   10710 O  O     . ARG A 1 2811 ? 251.797 232.995 203.357 1.00 19.48 ? 2811 ARG A O     1 
ATOM   10711 C  CB    . ARG A 1 2811 ? 248.682 233.579 204.375 1.00 12.89 ? 2811 ARG A CB    1 
ATOM   10712 C  CG    . ARG A 1 2811 ? 247.983 234.260 205.515 1.00 15.21 ? 2811 ARG A CG    1 
ATOM   10713 C  CD    . ARG A 1 2811 ? 246.793 233.442 205.968 1.00 19.53 ? 2811 ARG A CD    1 
ATOM   10714 N  NE    . ARG A 1 2811 ? 245.733 233.410 204.970 1.00 19.97 ? 2811 ARG A NE    1 
ATOM   10715 C  CZ    . ARG A 1 2811 ? 244.639 232.669 205.067 1.00 23.44 ? 2811 ARG A CZ    1 
ATOM   10716 N  NH1   . ARG A 1 2811 ? 244.426 231.887 206.112 1.00 20.75 ? 2811 ARG A NH1   1 
ATOM   10717 N  NH2   . ARG A 1 2811 ? 243.733 232.719 204.095 1.00 22.76 ? 2811 ARG A NH2   1 
ATOM   10718 N  N     . PRO A 1 2812 ? 250.292 233.059 201.695 1.00 14.42 ? 2812 PRO A N     1 
ATOM   10719 C  CA    . PRO A 1 2812 ? 251.076 232.084 200.928 1.00 13.78 ? 2812 PRO A CA    1 
ATOM   10720 C  C     . PRO A 1 2812 ? 252.241 232.709 200.176 1.00 11.76 ? 2812 PRO A C     1 
ATOM   10721 O  O     . PRO A 1 2812 ? 252.817 232.075 199.286 1.00 24.61 ? 2812 PRO A O     1 
ATOM   10722 C  CB    . PRO A 1 2812 ? 250.039 231.504 199.965 1.00 15.53 ? 2812 PRO A CB    1 
ATOM   10723 C  CG    . PRO A 1 2812 ? 249.173 232.671 199.669 1.00 14.45 ? 2812 PRO A CG    1 
ATOM   10724 C  CD    . PRO A 1 2812 ? 249.070 233.447 200.962 1.00 8.53  ? 2812 PRO A CD    1 
ATOM   10725 N  N     . LEU A 1 2813 ? 252.598 233.941 200.520 1.00 14.56 ? 2813 LEU A N     1 
ATOM   10726 C  CA    . LEU A 1 2813 ? 253.628 234.685 199.808 1.00 15.89 ? 2813 LEU A CA    1 
ATOM   10727 C  C     . LEU A 1 2813 ? 254.916 234.705 200.616 1.00 22.12 ? 2813 LEU A C     1 
ATOM   10728 O  O     . LEU A 1 2813 ? 254.916 235.096 201.788 1.00 25.20 ? 2813 LEU A O     1 
ATOM   10729 C  CB    . LEU A 1 2813 ? 253.167 236.114 199.520 1.00 15.75 ? 2813 LEU A CB    1 
ATOM   10730 C  CG    . LEU A 1 2813 ? 251.995 236.261 198.549 1.00 12.47 ? 2813 LEU A CG    1 
ATOM   10731 C  CD1   . LEU A 1 2813 ? 251.884 237.696 198.063 1.00 9.15  ? 2813 LEU A CD1   1 
ATOM   10732 C  CD2   . LEU A 1 2813 ? 252.147 235.304 197.382 1.00 14.33 ? 2813 LEU A CD2   1 
ATOM   10733 N  N     . GLU A 1 2814 ? 256.012 234.280 199.987 1.00 21.35 ? 2814 GLU A N     1 
ATOM   10734 C  CA    . GLU A 1 2814 ? 257.312 234.327 200.645 1.00 23.19 ? 2814 GLU A CA    1 
ATOM   10735 C  C     . GLU A 1 2814 ? 257.888 235.736 200.673 1.00 23.40 ? 2814 GLU A C     1 
ATOM   10736 O  O     . GLU A 1 2814 ? 258.587 236.094 201.626 1.00 22.91 ? 2814 GLU A O     1 
ATOM   10737 C  CB    . GLU A 1 2814 ? 258.284 233.358 199.962 1.00 26.39 ? 2814 GLU A CB    1 
ATOM   10738 C  CG    . GLU A 1 2814 ? 258.904 233.855 198.658 1.00 31.73 ? 2814 GLU A CG    1 
ATOM   10739 C  CD    . GLU A 1 2814 ? 257.875 234.158 197.582 1.00 34.28 ? 2814 GLU A CD    1 
ATOM   10740 O  OE1   . GLU A 1 2814 ? 256.778 233.560 197.612 1.00 31.54 ? 2814 GLU A OE1   1 
ATOM   10741 O  OE2   . GLU A 1 2814 ? 258.162 234.999 196.704 1.00 36.80 ? 2814 GLU A OE2   1 
ATOM   10742 N  N     . THR A 1 2815 ? 257.607 236.547 199.653 1.00 20.16 ? 2815 THR A N     1 
ATOM   10743 C  CA    . THR A 1 2815 ? 258.099 237.914 199.609 1.00 20.55 ? 2815 THR A CA    1 
ATOM   10744 C  C     . THR A 1 2815 ? 257.227 238.720 198.660 1.00 16.84 ? 2815 THR A C     1 
ATOM   10745 O  O     . THR A 1 2815 ? 256.518 238.167 197.815 1.00 19.40 ? 2815 THR A O     1 
ATOM   10746 C  CB    . THR A 1 2815 ? 259.568 237.980 199.175 1.00 20.98 ? 2815 THR A CB    1 
ATOM   10747 O  OG1   . THR A 1 2815 ? 260.108 239.264 199.507 1.00 24.35 ? 2815 THR A OG1   1 
ATOM   10748 C  CG2   . THR A 1 2815 ? 259.694 237.758 197.676 1.00 18.47 ? 2815 THR A CG2   1 
ATOM   10749 N  N     . LEU A 1 2816 ? 257.294 240.045 198.812 1.00 14.27 ? 2816 LEU A N     1 
ATOM   10750 C  CA    . LEU A 1 2816 ? 256.491 240.956 198.015 1.00 9.22  ? 2816 LEU A CA    1 
ATOM   10751 C  C     . LEU A 1 2816 ? 257.117 242.337 198.068 1.00 7.64  ? 2816 LEU A C     1 
ATOM   10752 O  O     . LEU A 1 2816 ? 257.495 242.784 199.160 1.00 23.87 ? 2816 LEU A O     1 
ATOM   10753 C  CB    . LEU A 1 2816 ? 255.049 241.015 198.524 1.00 9.64  ? 2816 LEU A CB    1 
ATOM   10754 C  CG    . LEU A 1 2816 ? 253.993 241.628 197.602 1.00 9.29  ? 2816 LEU A CG    1 
ATOM   10755 C  CD1   . LEU A 1 2816 ? 253.684 240.704 196.435 1.00 3.42  ? 2816 LEU A CD1   1 
ATOM   10756 C  CD2   . LEU A 1 2816 ? 252.734 241.941 198.386 1.00 7.77  ? 2816 LEU A CD2   1 
ATOM   10757 N  N     . PRO A 1 2817 ? 257.252 243.030 196.943 1.00 13.47 ? 2817 PRO A N     1 
ATOM   10758 C  CA    . PRO A 1 2817 ? 257.689 244.429 196.986 1.00 10.56 ? 2817 PRO A CA    1 
ATOM   10759 C  C     . PRO A 1 2817 ? 256.587 245.321 197.534 1.00 11.40 ? 2817 PRO A C     1 
ATOM   10760 O  O     . PRO A 1 2817 ? 255.424 244.931 197.645 1.00 17.14 ? 2817 PRO A O     1 
ATOM   10761 C  CB    . PRO A 1 2817 ? 258.009 244.753 195.526 1.00 8.52  ? 2817 PRO A CB    1 
ATOM   10762 C  CG    . PRO A 1 2817 ? 257.197 243.787 194.737 1.00 12.56 ? 2817 PRO A CG    1 
ATOM   10763 C  CD    . PRO A 1 2817 ? 257.076 242.540 195.565 1.00 11.79 ? 2817 PRO A CD    1 
ATOM   10764 N  N     . VAL A 1 2818 ? 256.975 246.546 197.892 1.00 11.28 ? 2818 VAL A N     1 
ATOM   10765 C  CA    . VAL A 1 2818 ? 256.019 247.476 198.483 1.00 10.00 ? 2818 VAL A CA    1 
ATOM   10766 C  C     . VAL A 1 2818 ? 254.938 247.846 197.474 1.00 8.00  ? 2818 VAL A C     1 
ATOM   10767 O  O     . VAL A 1 2818 ? 253.773 248.049 197.840 1.00 8.75  ? 2818 VAL A O     1 
ATOM   10768 C  CB    . VAL A 1 2818 ? 256.746 248.716 199.039 1.00 9.72  ? 2818 VAL A CB    1 
ATOM   10769 C  CG1   . VAL A 1 2818 ? 257.405 249.517 197.923 1.00 9.76  ? 2818 VAL A CG1   1 
ATOM   10770 C  CG2   . VAL A 1 2818 ? 255.786 249.578 199.846 1.00 6.46  ? 2818 VAL A CG2   1 
ATOM   10771 N  N     . GLU A 1 2819 ? 255.297 247.935 196.192 1.00 9.08  ? 2819 GLU A N     1 
ATOM   10772 C  CA    . GLU A 1 2819 ? 254.297 248.181 195.159 1.00 8.46  ? 2819 GLU A CA    1 
ATOM   10773 C  C     . GLU A 1 2819 ? 253.278 247.050 195.090 1.00 9.98  ? 2819 GLU A C     1 
ATOM   10774 O  O     . GLU A 1 2819 ? 252.102 247.294 194.804 1.00 7.85  ? 2819 GLU A O     1 
ATOM   10775 C  CB    . GLU A 1 2819 ? 254.973 248.380 193.804 1.00 10.65 ? 2819 GLU A CB    1 
ATOM   10776 C  CG    . GLU A 1 2819 ? 255.817 249.643 193.699 1.00 15.92 ? 2819 GLU A CG    1 
ATOM   10777 C  CD    . GLU A 1 2819 ? 257.209 249.477 194.276 1.00 20.29 ? 2819 GLU A CD    1 
ATOM   10778 O  OE1   . GLU A 1 2819 ? 257.551 248.356 194.707 1.00 16.26 ? 2819 GLU A OE1   1 
ATOM   10779 O  OE2   . GLU A 1 2819 ? 257.961 250.473 194.307 1.00 29.54 ? 2819 GLU A OE2   1 
ATOM   10780 N  N     . GLY A 1 2820 ? 253.710 245.813 195.345 1.00 8.19  ? 2820 GLY A N     1 
ATOM   10781 C  CA    . GLY A 1 2820 ? 252.768 244.714 195.441 1.00 4.56  ? 2820 GLY A CA    1 
ATOM   10782 C  C     . GLY A 1 2820 ? 251.833 244.842 196.625 1.00 4.97  ? 2820 GLY A C     1 
ATOM   10783 O  O     . GLY A 1 2820 ? 250.668 244.441 196.548 1.00 5.28  ? 2820 GLY A O     1 
ATOM   10784 N  N     . LEU A 1 2821 ? 252.329 245.386 197.739 1.00 7.61  ? 2821 LEU A N     1 
ATOM   10785 C  CA    . LEU A 1 2821 ? 251.473 245.628 198.897 1.00 3.59  ? 2821 LEU A CA    1 
ATOM   10786 C  C     . LEU A 1 2821 ? 250.402 246.664 198.588 1.00 2.40  ? 2821 LEU A C     1 
ATOM   10787 O  O     . LEU A 1 2821 ? 249.243 246.506 198.985 1.00 2.67  ? 2821 LEU A O     1 
ATOM   10788 C  CB    . LEU A 1 2821 ? 252.319 246.072 200.088 1.00 4.55  ? 2821 LEU A CB    1 
ATOM   10789 C  CG    . LEU A 1 2821 ? 251.556 246.393 201.374 1.00 3.71  ? 2821 LEU A CG    1 
ATOM   10790 C  CD1   . LEU A 1 2821 ? 250.834 245.158 201.893 1.00 1.76  ? 2821 LEU A CD1   1 
ATOM   10791 C  CD2   . LEU A 1 2821 ? 252.489 246.960 202.428 1.00 3.49  ? 2821 LEU A CD2   1 
ATOM   10792 N  N     . ILE A 1 2822 ? 250.771 247.731 197.877 1.00 1.63  ? 2822 ILE A N     1 
ATOM   10793 C  CA    . ILE A 1 2822 ? 249.808 248.782 197.559 1.00 1.64  ? 2822 ILE A CA    1 
ATOM   10794 C  C     . ILE A 1 2822 ? 248.717 248.251 196.641 1.00 2.92  ? 2822 ILE A C     1 
ATOM   10795 O  O     . ILE A 1 2822 ? 247.546 248.632 196.764 1.00 1.85  ? 2822 ILE A O     1 
ATOM   10796 C  CB    . ILE A 1 2822 ? 250.524 249.998 196.944 1.00 3.17  ? 2822 ILE A CB    1 
ATOM   10797 C  CG1   . ILE A 1 2822 ? 251.655 250.472 197.856 1.00 3.54  ? 2822 ILE A CG1   1 
ATOM   10798 C  CG2   . ILE A 1 2822 ? 249.539 251.127 196.693 1.00 5.41  ? 2822 ILE A CG2   1 
ATOM   10799 C  CD1   . ILE A 1 2822 ? 251.230 250.698 199.286 1.00 4.18  ? 2822 ILE A CD1   1 
ATOM   10800 N  N     . ARG A 1 2823 ? 249.079 247.372 195.705 1.00 4.69  ? 2823 ARG A N     1 
ATOM   10801 C  CA    . ARG A 1 2823 ? 248.081 246.815 194.796 1.00 2.23  ? 2823 ARG A CA    1 
ATOM   10802 C  C     . ARG A 1 2823 ? 247.041 246.000 195.553 1.00 1.68  ? 2823 ARG A C     1 
ATOM   10803 O  O     . ARG A 1 2823 ? 245.841 246.103 195.274 1.00 1.75  ? 2823 ARG A O     1 
ATOM   10804 C  CB    . ARG A 1 2823 ? 248.760 245.969 193.720 1.00 4.47  ? 2823 ARG A CB    1 
ATOM   10805 C  CG    . ARG A 1 2823 ? 247.883 245.731 192.509 1.00 3.27  ? 2823 ARG A CG    1 
ATOM   10806 C  CD    . ARG A 1 2823 ? 248.645 245.094 191.363 1.00 3.40  ? 2823 ARG A CD    1 
ATOM   10807 N  NE    . ARG A 1 2823 ? 247.850 245.082 190.141 1.00 11.46 ? 2823 ARG A NE    1 
ATOM   10808 C  CZ    . ARG A 1 2823 ? 247.555 246.156 189.421 1.00 8.59  ? 2823 ARG A CZ    1 
ATOM   10809 N  NH1   . ARG A 1 2823 ? 248.039 247.348 189.726 1.00 6.43  ? 2823 ARG A NH1   1 
ATOM   10810 N  NH2   . ARG A 1 2823 ? 246.759 246.030 188.365 1.00 5.11  ? 2823 ARG A NH2   1 
ATOM   10811 N  N     . ILE A 1 2824 ? 247.480 245.183 196.512 1.00 1.58  ? 2824 ILE A N     1 
ATOM   10812 C  CA    . ILE A 1 2824 ? 246.535 244.465 197.364 1.00 1.43  ? 2824 ILE A CA    1 
ATOM   10813 C  C     . ILE A 1 2824 ? 245.707 245.451 198.176 1.00 1.59  ? 2824 ILE A C     1 
ATOM   10814 O  O     . ILE A 1 2824 ? 244.488 245.295 198.316 1.00 1.58  ? 2824 ILE A O     1 
ATOM   10815 C  CB    . ILE A 1 2824 ? 247.281 243.471 198.276 1.00 1.46  ? 2824 ILE A CB    1 
ATOM   10816 C  CG1   . ILE A 1 2824 ? 248.166 242.541 197.448 1.00 1.50  ? 2824 ILE A CG1   1 
ATOM   10817 C  CG2   . ILE A 1 2824 ? 246.296 242.671 199.114 1.00 1.61  ? 2824 ILE A CG2   1 
ATOM   10818 C  CD1   . ILE A 1 2824 ? 249.032 241.623 198.283 1.00 5.03  ? 2824 ILE A CD1   1 
ATOM   10819 N  N     . TRP A 1 2825 ? 246.357 246.479 198.720 1.00 2.00  ? 2825 TRP A N     1 
ATOM   10820 C  CA    . TRP A 1 2825 ? 245.647 247.497 199.485 1.00 0.67  ? 2825 TRP A CA    1 
ATOM   10821 C  C     . TRP A 1 2825 ? 244.634 248.233 198.618 1.00 1.17  ? 2825 TRP A C     1 
ATOM   10822 O  O     . TRP A 1 2825 ? 243.508 248.502 199.055 1.00 1.50  ? 2825 TRP A O     1 
ATOM   10823 C  CB    . TRP A 1 2825 ? 246.656 248.471 200.094 1.00 0.87  ? 2825 TRP A CB    1 
ATOM   10824 C  CG    . TRP A 1 2825 ? 246.039 249.608 200.829 1.00 0.97  ? 2825 TRP A CG    1 
ATOM   10825 C  CD1   . TRP A 1 2825 ? 245.676 249.633 202.141 1.00 0.41  ? 2825 TRP A CD1   1 
ATOM   10826 C  CD2   . TRP A 1 2825 ? 245.721 250.896 200.298 1.00 1.05  ? 2825 TRP A CD2   1 
ATOM   10827 N  NE1   . TRP A 1 2825 ? 245.146 250.856 202.459 1.00 0.44  ? 2825 TRP A NE1   1 
ATOM   10828 C  CE2   . TRP A 1 2825 ? 245.163 251.651 201.345 1.00 0.41  ? 2825 TRP A CE2   1 
ATOM   10829 C  CE3   . TRP A 1 2825 ? 245.853 251.485 199.037 1.00 1.09  ? 2825 TRP A CE3   1 
ATOM   10830 C  CZ2   . TRP A 1 2825 ? 244.733 252.962 201.172 1.00 0.70  ? 2825 TRP A CZ2   1 
ATOM   10831 C  CZ3   . TRP A 1 2825 ? 245.426 252.786 198.867 1.00 1.41  ? 2825 TRP A CZ3   1 
ATOM   10832 C  CH2   . TRP A 1 2825 ? 244.875 253.510 199.929 1.00 1.87  ? 2825 TRP A CH2   1 
ATOM   10833 N  N     . ALA A 1 2826 ? 245.015 248.574 197.385 1.00 2.50  ? 2826 ALA A N     1 
ATOM   10834 C  CA    . ALA A 1 2826 ? 244.081 249.232 196.479 1.00 1.03  ? 2826 ALA A CA    1 
ATOM   10835 C  C     . ALA A 1 2826 ? 242.969 248.286 196.042 1.00 0.47  ? 2826 ALA A C     1 
ATOM   10836 O  O     . ALA A 1 2826 ? 241.811 248.698 195.918 1.00 0.54  ? 2826 ALA A O     1 
ATOM   10837 C  CB    . ALA A 1 2826 ? 244.828 249.776 195.263 1.00 0.61  ? 2826 ALA A CB    1 
ATOM   10838 N  N     . HIS A 1 2827 ? 243.306 247.020 195.798 1.00 0.59  ? 2827 HIS A N     1 
ATOM   10839 C  CA    . HIS A 1 2827 ? 242.300 246.059 195.363 1.00 0.40  ? 2827 HIS A CA    1 
ATOM   10840 C  C     . HIS A 1 2827 ? 241.231 245.852 196.426 1.00 0.34  ? 2827 HIS A C     1 
ATOM   10841 O  O     . HIS A 1 2827 ? 240.033 245.845 196.119 1.00 0.24  ? 2827 HIS A O     1 
ATOM   10842 C  CB    . HIS A 1 2827 ? 242.964 244.731 195.008 1.00 0.42  ? 2827 HIS A CB    1 
ATOM   10843 C  CG    . HIS A 1 2827 ? 241.993 243.623 194.749 1.00 0.45  ? 2827 HIS A CG    1 
ATOM   10844 N  ND1   . HIS A 1 2827 ? 241.270 243.525 193.582 1.00 0.36  ? 2827 HIS A ND1   1 
ATOM   10845 C  CD2   . HIS A 1 2827 ? 241.627 242.565 195.509 1.00 0.63  ? 2827 HIS A CD2   1 
ATOM   10846 C  CE1   . HIS A 1 2827 ? 240.495 242.458 193.634 1.00 0.40  ? 2827 HIS A CE1   1 
ATOM   10847 N  NE2   . HIS A 1 2827 ? 240.694 241.856 194.794 1.00 0.48  ? 2827 HIS A NE2   1 
ATOM   10848 N  N     . GLU A 1 2828 ? 241.643 245.689 197.684 1.00 0.55  ? 2828 GLU A N     1 
ATOM   10849 C  CA    . GLU A 1 2828 ? 240.678 245.472 198.753 1.00 0.29  ? 2828 GLU A CA    1 
ATOM   10850 C  C     . GLU A 1 2828 ? 239.829 246.711 199.004 1.00 0.24  ? 2828 GLU A C     1 
ATOM   10851 O  O     . GLU A 1 2828 ? 238.656 246.590 199.370 1.00 0.55  ? 2828 GLU A O     1 
ATOM   10852 C  CB    . GLU A 1 2828 ? 241.401 245.038 200.028 1.00 1.48  ? 2828 GLU A CB    1 
ATOM   10853 C  CG    . GLU A 1 2828 ? 242.085 243.688 199.905 1.00 1.56  ? 2828 GLU A CG    1 
ATOM   10854 C  CD    . GLU A 1 2828 ? 241.098 242.541 199.775 1.00 8.45  ? 2828 GLU A CD    1 
ATOM   10855 O  OE1   . GLU A 1 2828 ? 239.913 242.727 200.115 1.00 9.93  ? 2828 GLU A OE1   1 
ATOM   10856 O  OE2   . GLU A 1 2828 ? 241.507 241.454 199.319 1.00 8.28  ? 2828 GLU A OE2   1 
ATOM   10857 N  N     . ALA A 1 2829 ? 240.399 247.902 198.811 1.00 0.31  ? 2829 ALA A N     1 
ATOM   10858 C  CA    . ALA A 1 2829 ? 239.615 249.125 198.937 1.00 0.46  ? 2829 ALA A CA    1 
ATOM   10859 C  C     . ALA A 1 2829 ? 238.500 249.174 197.898 1.00 0.32  ? 2829 ALA A C     1 
ATOM   10860 O  O     . ALA A 1 2829 ? 237.371 249.570 198.208 1.00 0.41  ? 2829 ALA A O     1 
ATOM   10861 C  CB    . ALA A 1 2829 ? 240.524 250.346 198.813 1.00 0.52  ? 2829 ALA A CB    1 
ATOM   10862 N  N     . LEU A 1 2830 ? 238.795 248.772 196.661 1.00 0.34  ? 2830 LEU A N     1 
ATOM   10863 C  CA    . LEU A 1 2830 ? 237.769 248.757 195.622 1.00 0.51  ? 2830 LEU A CA    1 
ATOM   10864 C  C     . LEU A 1 2830 ? 236.664 247.761 195.951 1.00 0.29  ? 2830 LEU A C     1 
ATOM   10865 O  O     . LEU A 1 2830 ? 235.480 248.042 195.741 1.00 0.74  ? 2830 LEU A O     1 
ATOM   10866 C  CB    . LEU A 1 2830 ? 238.398 248.433 194.269 1.00 0.84  ? 2830 LEU A CB    1 
ATOM   10867 C  CG    . LEU A 1 2830 ? 239.335 249.489 193.684 1.00 0.82  ? 2830 LEU A CG    1 
ATOM   10868 C  CD1   . LEU A 1 2830 ? 240.261 248.862 192.657 1.00 0.30  ? 2830 LEU A CD1   1 
ATOM   10869 C  CD2   . LEU A 1 2830 ? 238.544 250.630 193.074 1.00 2.00  ? 2830 LEU A CD2   1 
ATOM   10870 N  N     . ARG A 1 2831 ? 237.034 246.592 196.474 1.00 0.25  ? 2831 ARG A N     1 
ATOM   10871 C  CA    . ARG A 1 2831 ? 236.041 245.577 196.797 1.00 0.34  ? 2831 ARG A CA    1 
ATOM   10872 C  C     . ARG A 1 2831 ? 235.158 245.994 197.965 1.00 0.70  ? 2831 ARG A C     1 
ATOM   10873 O  O     . ARG A 1 2831 ? 233.982 245.619 198.016 1.00 1.75  ? 2831 ARG A O     1 
ATOM   10874 C  CB    . ARG A 1 2831 ? 236.734 244.249 197.096 1.00 0.50  ? 2831 ARG A CB    1 
ATOM   10875 C  CG    . ARG A 1 2831 ? 237.525 243.680 195.927 1.00 0.32  ? 2831 ARG A CG    1 
ATOM   10876 C  CD    . ARG A 1 2831 ? 236.616 243.093 194.848 1.00 0.60  ? 2831 ARG A CD    1 
ATOM   10877 N  NE    . ARG A 1 2831 ? 236.025 244.121 193.998 1.00 0.53  ? 2831 ARG A NE    1 
ATOM   10878 C  CZ    . ARG A 1 2831 ? 236.697 244.861 193.128 1.00 0.39  ? 2831 ARG A CZ    1 
ATOM   10879 N  NH1   . ARG A 1 2831 ? 237.989 244.673 192.909 1.00 0.18  ? 2831 ARG A NH1   1 
ATOM   10880 N  NH2   . ARG A 1 2831 ? 236.060 245.818 192.463 1.00 0.69  ? 2831 ARG A NH2   1 
ATOM   10881 N  N     . LEU A 1 2832 ? 235.696 246.769 198.906 1.00 0.65  ? 2832 LEU A N     1 
ATOM   10882 C  CA    . LEU A 1 2832 ? 234.965 247.141 200.109 1.00 0.61  ? 2832 LEU A CA    1 
ATOM   10883 C  C     . LEU A 1 2832 ? 234.217 248.458 199.987 1.00 0.50  ? 2832 LEU A C     1 
ATOM   10884 O  O     . LEU A 1 2832 ? 233.194 248.635 200.653 1.00 1.68  ? 2832 LEU A O     1 
ATOM   10885 C  CB    . LEU A 1 2832 ? 235.919 247.230 201.301 1.00 1.23  ? 2832 LEU A CB    1 
ATOM   10886 C  CG    . LEU A 1 2832 ? 236.454 245.903 201.836 1.00 0.59  ? 2832 LEU A CG    1 
ATOM   10887 C  CD1   . LEU A 1 2832 ? 237.467 246.171 202.914 1.00 0.45  ? 2832 LEU A CD1   1 
ATOM   10888 C  CD2   . LEU A 1 2832 ? 235.323 245.041 202.363 1.00 1.08  ? 2832 LEU A CD2   1 
ATOM   10889 N  N     . PHE A 1 2833 ? 234.699 249.385 199.165 1.00 0.46  ? 2833 PHE A N     1 
ATOM   10890 C  CA    . PHE A 1 2833 ? 234.111 250.712 199.089 1.00 0.46  ? 2833 PHE A CA    1 
ATOM   10891 C  C     . PHE A 1 2833 ? 233.434 251.013 197.765 1.00 0.55  ? 2833 PHE A C     1 
ATOM   10892 O  O     . PHE A 1 2833 ? 232.450 251.753 197.750 1.00 1.43  ? 2833 PHE A O     1 
ATOM   10893 C  CB    . PHE A 1 2833 ? 235.181 251.781 199.354 1.00 0.46  ? 2833 PHE A CB    1 
ATOM   10894 C  CG    . PHE A 1 2833 ? 235.790 251.701 200.722 1.00 0.27  ? 2833 PHE A CG    1 
ATOM   10895 C  CD1   . PHE A 1 2833 ? 235.190 252.332 201.796 1.00 0.45  ? 2833 PHE A CD1   1 
ATOM   10896 C  CD2   . PHE A 1 2833 ? 236.958 250.995 200.934 1.00 0.29  ? 2833 PHE A CD2   1 
ATOM   10897 C  CE1   . PHE A 1 2833 ? 235.746 252.263 203.054 1.00 0.44  ? 2833 PHE A CE1   1 
ATOM   10898 C  CE2   . PHE A 1 2833 ? 237.518 250.919 202.192 1.00 0.57  ? 2833 PHE A CE2   1 
ATOM   10899 C  CZ    . PHE A 1 2833 ? 236.911 251.556 203.254 1.00 0.53  ? 2833 PHE A CZ    1 
ATOM   10900 N  N     . GLN A 1 2834 ? 233.920 250.452 196.662 1.00 0.61  ? 2834 GLN A N     1 
ATOM   10901 C  CA    . GLN A 1 2834 ? 233.377 250.780 195.351 1.00 0.47  ? 2834 GLN A CA    1 
ATOM   10902 C  C     . GLN A 1 2834 ? 232.267 249.837 194.903 1.00 0.62  ? 2834 GLN A C     1 
ATOM   10903 O  O     . GLN A 1 2834 ? 231.404 250.246 194.120 1.00 1.47  ? 2834 GLN A O     1 
ATOM   10904 C  CB    . GLN A 1 2834 ? 234.499 250.780 194.309 1.00 0.46  ? 2834 GLN A CB    1 
ATOM   10905 C  CG    . GLN A 1 2834 ? 234.198 251.597 193.070 1.00 1.15  ? 2834 GLN A CG    1 
ATOM   10906 C  CD    . GLN A 1 2834 ? 235.223 251.381 191.978 1.00 2.84  ? 2834 GLN A CD    1 
ATOM   10907 O  OE1   . GLN A 1 2834 ? 235.416 250.263 191.508 1.00 5.60  ? 2834 GLN A OE1   1 
ATOM   10908 N  NE2   . GLN A 1 2834 ? 235.887 252.453 191.569 1.00 3.07  ? 2834 GLN A NE2   1 
ATOM   10909 N  N     . ASP A 1 2835 ? 232.256 248.594 195.387 1.00 0.57  ? 2835 ASP A N     1 
ATOM   10910 C  CA    . ASP A 1 2835 ? 231.322 247.597 194.874 1.00 0.63  ? 2835 ASP A CA    1 
ATOM   10911 C  C     . ASP A 1 2835 ? 229.877 247.876 195.263 1.00 0.36  ? 2835 ASP A C     1 
ATOM   10912 O  O     . ASP A 1 2835 ? 228.966 247.355 194.614 1.00 0.43  ? 2835 ASP A O     1 
ATOM   10913 C  CB    . ASP A 1 2835 ? 231.725 246.202 195.350 1.00 0.82  ? 2835 ASP A CB    1 
ATOM   10914 C  CG    . ASP A 1 2835 ? 232.937 245.661 194.617 1.00 1.77  ? 2835 ASP A CG    1 
ATOM   10915 O  OD1   . ASP A 1 2835 ? 233.470 246.369 193.737 1.00 0.72  ? 2835 ASP A OD1   1 
ATOM   10916 O  OD2   . ASP A 1 2835 ? 233.359 244.527 194.919 1.00 3.41  ? 2835 ASP A OD2   1 
ATOM   10917 N  N     . ARG A 1 2836 ? 229.644 248.674 196.301 1.00 0.46  ? 2836 ARG A N     1 
ATOM   10918 C  CA    . ARG A 1 2836 ? 228.293 249.014 196.721 1.00 0.58  ? 2836 ARG A CA    1 
ATOM   10919 C  C     . ARG A 1 2836 ? 227.781 250.304 196.100 1.00 0.65  ? 2836 ARG A C     1 
ATOM   10920 O  O     . ARG A 1 2836 ? 226.601 250.629 196.271 1.00 1.04  ? 2836 ARG A O     1 
ATOM   10921 C  CB    . ARG A 1 2836 ? 228.232 249.137 198.245 1.00 0.62  ? 2836 ARG A CB    1 
ATOM   10922 C  CG    . ARG A 1 2836 ? 228.898 250.394 198.777 1.00 0.59  ? 2836 ARG A CG    1 
ATOM   10923 C  CD    . ARG A 1 2836 ? 228.827 250.448 200.280 1.00 1.65  ? 2836 ARG A CD    1 
ATOM   10924 N  NE    . ARG A 1 2836 ? 229.634 249.400 200.891 1.00 5.70  ? 2836 ARG A NE    1 
ATOM   10925 C  CZ    . ARG A 1 2836 ? 229.597 249.083 202.176 1.00 2.56  ? 2836 ARG A CZ    1 
ATOM   10926 N  NH1   . ARG A 1 2836 ? 228.790 249.707 203.018 1.00 2.28  ? 2836 ARG A NH1   1 
ATOM   10927 N  NH2   . ARG A 1 2836 ? 230.386 248.114 202.629 1.00 4.56  ? 2836 ARG A NH2   1 
ATOM   10928 N  N     . LEU A 1 2837 ? 228.629 251.045 195.393 1.00 0.59  ? 2837 LEU A N     1 
ATOM   10929 C  CA    . LEU A 1 2837 ? 228.239 252.350 194.881 1.00 0.81  ? 2837 LEU A CA    1 
ATOM   10930 C  C     . LEU A 1 2837 ? 227.282 252.208 193.702 1.00 1.86  ? 2837 LEU A C     1 
ATOM   10931 O  O     . LEU A 1 2837 ? 227.380 251.270 192.908 1.00 2.97  ? 2837 LEU A O     1 
ATOM   10932 C  CB    . LEU A 1 2837 ? 229.476 253.146 194.481 1.00 1.33  ? 2837 LEU A CB    1 
ATOM   10933 C  CG    . LEU A 1 2837 ? 230.421 253.453 195.646 1.00 1.31  ? 2837 LEU A CG    1 
ATOM   10934 C  CD1   . LEU A 1 2837 ? 231.638 254.212 195.167 1.00 1.15  ? 2837 LEU A CD1   1 
ATOM   10935 C  CD2   . LEU A 1 2837 ? 229.700 254.225 196.744 1.00 0.92  ? 2837 LEU A CD2   1 
ATOM   10936 N  N     . VAL A 1 2838 ? 226.353 253.153 193.597 1.00 2.64  ? 2838 VAL A N     1 
ATOM   10937 C  CA    . VAL A 1 2838 ? 225.282 253.089 192.609 1.00 2.41  ? 2838 VAL A CA    1 
ATOM   10938 C  C     . VAL A 1 2838 ? 225.648 253.903 191.374 1.00 5.29  ? 2838 VAL A C     1 
ATOM   10939 O  O     . VAL A 1 2838 ? 225.427 253.462 190.242 1.00 10.09 ? 2838 VAL A O     1 
ATOM   10940 C  CB    . VAL A 1 2838 ? 223.954 253.577 193.214 1.00 3.30  ? 2838 VAL A CB    1 
ATOM   10941 C  CG1   . VAL A 1 2838 ? 222.844 253.524 192.180 1.00 3.84  ? 2838 VAL A CG1   1 
ATOM   10942 C  CG2   . VAL A 1 2838 ? 223.597 252.753 194.441 1.00 1.16  ? 2838 VAL A CG2   1 
ATOM   10943 N  N     . GLU A 1 2839 ? 226.204 255.090 191.580 1.00 6.93  ? 2839 GLU A N     1 
ATOM   10944 C  CA    . GLU A 1 2839 ? 226.433 256.041 190.504 1.00 7.66  ? 2839 GLU A CA    1 
ATOM   10945 C  C     . GLU A 1 2839 ? 227.874 255.991 190.010 1.00 6.85  ? 2839 GLU A C     1 
ATOM   10946 O  O     . GLU A 1 2839 ? 228.802 255.688 190.763 1.00 8.03  ? 2839 GLU A O     1 
ATOM   10947 C  CB    . GLU A 1 2839 ? 226.084 257.462 190.957 1.00 7.69  ? 2839 GLU A CB    1 
ATOM   10948 C  CG    . GLU A 1 2839 ? 224.584 257.771 191.090 1.00 9.80  ? 2839 GLU A CG    1 
ATOM   10949 C  CD    . GLU A 1 2839 ? 223.698 257.208 189.974 1.00 20.91 ? 2839 GLU A CD    1 
ATOM   10950 O  OE1   . GLU A 1 2839 ? 224.185 256.937 188.855 1.00 26.12 ? 2839 GLU A OE1   1 
ATOM   10951 O  OE2   . GLU A 1 2839 ? 222.490 257.030 190.227 1.00 25.35 ? 2839 GLU A OE2   1 
ATOM   10952 N  N     . ASP A 1 2840 ? 228.045 256.298 188.721 1.00 13.94 ? 2840 ASP A N     1 
ATOM   10953 C  CA    . ASP A 1 2840 ? 229.375 256.309 188.118 1.00 8.18  ? 2840 ASP A CA    1 
ATOM   10954 C  C     . ASP A 1 2840 ? 230.242 257.426 188.678 1.00 9.13  ? 2840 ASP A C     1 
ATOM   10955 O  O     . ASP A 1 2840 ? 231.467 257.278 188.757 1.00 12.07 ? 2840 ASP A O     1 
ATOM   10956 C  CB    . ASP A 1 2840 ? 229.258 256.441 186.601 1.00 11.47 ? 2840 ASP A CB    1 
ATOM   10957 C  CG    . ASP A 1 2840 ? 229.227 255.097 185.901 1.00 20.09 ? 2840 ASP A CG    1 
ATOM   10958 O  OD1   . ASP A 1 2840 ? 229.560 254.080 186.544 1.00 17.27 ? 2840 ASP A OD1   1 
ATOM   10959 O  OD2   . ASP A 1 2840 ? 228.871 255.058 184.705 1.00 23.24 ? 2840 ASP A OD2   1 
ATOM   10960 N  N     . GLU A 1 2841 ? 229.637 258.556 189.049 1.00 9.19  ? 2841 GLU A N     1 
ATOM   10961 C  CA    . GLU A 1 2841 ? 230.394 259.616 189.704 1.00 9.79  ? 2841 GLU A CA    1 
ATOM   10962 C  C     . GLU A 1 2841 ? 230.955 259.145 191.037 1.00 8.97  ? 2841 GLU A C     1 
ATOM   10963 O  O     . GLU A 1 2841 ? 232.110 259.434 191.372 1.00 9.57  ? 2841 GLU A O     1 
ATOM   10964 C  CB    . GLU A 1 2841 ? 229.506 260.844 189.903 1.00 7.90  ? 2841 GLU A CB    1 
ATOM   10965 C  CG    . GLU A 1 2841 ? 230.211 262.025 190.544 1.00 13.91 ? 2841 GLU A CG    1 
ATOM   10966 C  CD    . GLU A 1 2841 ? 231.311 262.601 189.678 1.00 27.24 ? 2841 GLU A CD    1 
ATOM   10967 O  OE1   . GLU A 1 2841 ? 231.242 262.453 188.439 1.00 22.46 ? 2841 GLU A OE1   1 
ATOM   10968 O  OE2   . GLU A 1 2841 ? 232.249 263.206 190.237 1.00 37.32 ? 2841 GLU A OE2   1 
ATOM   10969 N  N     . GLU A 1 2842 ? 230.150 258.415 191.811 1.00 4.32  ? 2842 GLU A N     1 
ATOM   10970 C  CA    . GLU A 1 2842 ? 230.612 257.905 193.097 1.00 4.32  ? 2842 GLU A CA    1 
ATOM   10971 C  C     . GLU A 1 2842 ? 231.753 256.913 192.915 1.00 3.22  ? 2842 GLU A C     1 
ATOM   10972 O  O     . GLU A 1 2842 ? 232.745 256.955 193.650 1.00 2.69  ? 2842 GLU A O     1 
ATOM   10973 C  CB    . GLU A 1 2842 ? 229.447 257.259 193.843 1.00 3.99  ? 2842 GLU A CB    1 
ATOM   10974 C  CG    . GLU A 1 2842 ? 228.338 258.226 194.200 1.00 3.98  ? 2842 GLU A CG    1 
ATOM   10975 C  CD    . GLU A 1 2842 ? 227.023 257.529 194.477 1.00 9.74  ? 2842 GLU A CD    1 
ATOM   10976 O  OE1   . GLU A 1 2842 ? 226.954 256.296 194.301 1.00 7.12  ? 2842 GLU A OE1   1 
ATOM   10977 O  OE2   . GLU A 1 2842 ? 226.055 258.215 194.865 1.00 12.90 ? 2842 GLU A OE2   1 
ATOM   10978 N  N     . ARG A 1 2843 ? 231.632 256.018 191.932 1.00 5.06  ? 2843 ARG A N     1 
ATOM   10979 C  CA    . ARG A 1 2843 ? 232.698 255.065 191.654 1.00 5.98  ? 2843 ARG A CA    1 
ATOM   10980 C  C     . ARG A 1 2843 ? 233.944 255.760 191.123 1.00 4.00  ? 2843 ARG A C     1 
ATOM   10981 O  O     . ARG A 1 2843 ? 235.066 255.333 191.420 1.00 2.17  ? 2843 ARG A O     1 
ATOM   10982 C  CB    . ARG A 1 2843 ? 232.205 254.004 190.668 1.00 2.69  ? 2843 ARG A CB    1 
ATOM   10983 C  CG    . ARG A 1 2843 ? 230.959 253.273 191.138 1.00 3.32  ? 2843 ARG A CG    1 
ATOM   10984 C  CD    . ARG A 1 2843 ? 230.642 252.062 190.281 1.00 6.01  ? 2843 ARG A CD    1 
ATOM   10985 N  NE    . ARG A 1 2843 ? 229.785 252.405 189.153 1.00 9.23  ? 2843 ARG A NE    1 
ATOM   10986 C  CZ    . ARG A 1 2843 ? 228.491 252.130 189.078 1.00 9.97  ? 2843 ARG A CZ    1 
ATOM   10987 N  NH1   . ARG A 1 2843 ? 227.863 251.491 190.051 1.00 6.63  ? 2843 ARG A NH1   1 
ATOM   10988 N  NH2   . ARG A 1 2843 ? 227.807 252.511 188.002 1.00 12.90 ? 2843 ARG A NH2   1 
ATOM   10989 N  N     . ARG A 1 2844 ? 233.769 256.822 190.335 1.00 5.33  ? 2844 ARG A N     1 
ATOM   10990 C  CA    . ARG A 1 2844 ? 234.916 257.586 189.853 1.00 3.98  ? 2844 ARG A CA    1 
ATOM   10991 C  C     . ARG A 1 2844 ? 235.655 258.257 191.004 1.00 3.14  ? 2844 ARG A C     1 
ATOM   10992 O  O     . ARG A 1 2844 ? 236.890 258.257 191.039 1.00 2.21  ? 2844 ARG A O     1 
ATOM   10993 C  CB    . ARG A 1 2844 ? 234.459 258.621 188.825 1.00 8.32  ? 2844 ARG A CB    1 
ATOM   10994 C  CG    . ARG A 1 2844 ? 235.461 258.881 187.718 1.00 8.96  ? 2844 ARG A CG    1 
ATOM   10995 C  CD    . ARG A 1 2844 ? 234.912 259.860 186.691 1.00 17.66 ? 2844 ARG A CD    1 
ATOM   10996 N  NE    . ARG A 1 2844 ? 233.713 259.354 186.034 1.00 21.25 ? 2844 ARG A NE    1 
ATOM   10997 C  CZ    . ARG A 1 2844 ? 232.495 259.851 186.207 1.00 22.01 ? 2844 ARG A CZ    1 
ATOM   10998 N  NH1   . ARG A 1 2844 ? 232.274 260.875 187.015 1.00 19.64 ? 2844 ARG A NH1   1 
ATOM   10999 N  NH2   . ARG A 1 2844 ? 231.474 259.304 185.556 1.00 16.64 ? 2844 ARG A NH2   1 
ATOM   11000 N  N     . TRP A 1 2845 ? 234.913 258.833 191.953 1.00 4.09  ? 2845 TRP A N     1 
ATOM   11001 C  CA    . TRP A 1 2845 ? 235.545 259.471 193.104 1.00 2.18  ? 2845 TRP A CA    1 
ATOM   11002 C  C     . TRP A 1 2845 ? 236.340 258.465 193.926 1.00 2.96  ? 2845 TRP A C     1 
ATOM   11003 O  O     . TRP A 1 2845 ? 237.472 258.743 194.338 1.00 4.85  ? 2845 TRP A O     1 
ATOM   11004 C  CB    . TRP A 1 2845 ? 234.490 260.154 193.972 1.00 2.06  ? 2845 TRP A CB    1 
ATOM   11005 C  CG    . TRP A 1 2845 ? 235.052 260.846 195.179 1.00 2.62  ? 2845 TRP A CG    1 
ATOM   11006 C  CD1   . TRP A 1 2845 ? 235.385 262.164 195.282 1.00 4.26  ? 2845 TRP A CD1   1 
ATOM   11007 C  CD2   . TRP A 1 2845 ? 235.344 260.259 196.452 1.00 3.19  ? 2845 TRP A CD2   1 
ATOM   11008 N  NE1   . TRP A 1 2845 ? 235.868 262.433 196.537 1.00 3.49  ? 2845 TRP A NE1   1 
ATOM   11009 C  CE2   . TRP A 1 2845 ? 235.852 261.281 197.276 1.00 3.53  ? 2845 TRP A CE2   1 
ATOM   11010 C  CE3   . TRP A 1 2845 ? 235.226 258.968 196.975 1.00 2.48  ? 2845 TRP A CE3   1 
ATOM   11011 C  CZ2   . TRP A 1 2845 ? 236.244 261.052 198.594 1.00 2.80  ? 2845 TRP A CZ2   1 
ATOM   11012 C  CZ3   . TRP A 1 2845 ? 235.617 258.742 198.280 1.00 4.58  ? 2845 TRP A CZ3   1 
ATOM   11013 C  CH2   . TRP A 1 2845 ? 236.117 259.780 199.075 1.00 4.01  ? 2845 TRP A CH2   1 
ATOM   11014 N  N     . THR A 1 2846 ? 235.757 257.291 194.179 1.00 3.33  ? 2846 THR A N     1 
ATOM   11015 C  CA    . THR A 1 2846 ? 236.449 256.268 194.953 1.00 2.44  ? 2846 THR A CA    1 
ATOM   11016 C  C     . THR A 1 2846 ? 237.711 255.803 194.242 1.00 2.69  ? 2846 THR A C     1 
ATOM   11017 O  O     . THR A 1 2846 ? 238.760 255.625 194.870 1.00 3.18  ? 2846 THR A O     1 
ATOM   11018 C  CB    . THR A 1 2846 ? 235.508 255.091 195.215 1.00 3.85  ? 2846 THR A CB    1 
ATOM   11019 O  OG1   . THR A 1 2846 ? 234.418 255.529 196.033 1.00 7.01  ? 2846 THR A OG1   1 
ATOM   11020 C  CG2   . THR A 1 2846 ? 236.236 253.957 195.920 1.00 1.30  ? 2846 THR A CG2   1 
ATOM   11021 N  N     . ASP A 1 2847 ? 237.630 255.614 192.924 1.00 4.00  ? 2847 ASP A N     1 
ATOM   11022 C  CA    . ASP A 1 2847 ? 238.790 255.180 192.158 1.00 4.43  ? 2847 ASP A CA    1 
ATOM   11023 C  C     . ASP A 1 2847 ? 239.908 256.216 192.206 1.00 5.93  ? 2847 ASP A C     1 
ATOM   11024 O  O     . ASP A 1 2847 ? 241.087 255.864 192.324 1.00 6.37  ? 2847 ASP A O     1 
ATOM   11025 C  CB    . ASP A 1 2847 ? 238.374 254.900 190.714 1.00 6.59  ? 2847 ASP A CB    1 
ATOM   11026 C  CG    . ASP A 1 2847 ? 239.333 253.976 190.001 1.00 18.52 ? 2847 ASP A CG    1 
ATOM   11027 O  OD1   . ASP A 1 2847 ? 239.547 252.846 190.486 1.00 16.56 ? 2847 ASP A OD1   1 
ATOM   11028 O  OD2   . ASP A 1 2847 ? 239.875 254.382 188.951 1.00 22.98 ? 2847 ASP A OD2   1 
ATOM   11029 N  N     . GLU A 1 2848 ? 239.556 257.500 192.119 1.00 8.07  ? 2848 GLU A N     1 
ATOM   11030 C  CA    . GLU A 1 2848 ? 240.572 258.547 192.118 1.00 4.66  ? 2848 GLU A CA    1 
ATOM   11031 C  C     . GLU A 1 2848 ? 241.231 258.692 193.485 1.00 6.96  ? 2848 GLU A C     1 
ATOM   11032 O  O     . GLU A 1 2848 ? 242.460 258.783 193.581 1.00 10.45 ? 2848 GLU A O     1 
ATOM   11033 C  CB    . GLU A 1 2848 ? 239.953 259.873 191.679 1.00 5.84  ? 2848 GLU A CB    1 
ATOM   11034 C  CG    . GLU A 1 2848 ? 240.793 261.093 192.013 1.00 17.36 ? 2848 GLU A CG    1 
ATOM   11035 C  CD    . GLU A 1 2848 ? 242.085 261.145 191.219 1.00 23.35 ? 2848 GLU A CD    1 
ATOM   11036 O  OE1   . GLU A 1 2848 ? 243.164 260.997 191.829 1.00 18.97 ? 2848 GLU A OE1   1 
ATOM   11037 O  OE2   . GLU A 1 2848 ? 242.019 261.333 189.987 1.00 21.86 ? 2848 GLU A OE2   1 
ATOM   11038 N  N     . ASN A 1 2849 ? 240.434 258.705 194.554 1.00 7.95  ? 2849 ASN A N     1 
ATOM   11039 C  CA    . ASN A 1 2849 ? 240.974 258.978 195.879 1.00 4.56  ? 2849 ASN A CA    1 
ATOM   11040 C  C     . ASN A 1 2849 ? 241.754 257.802 196.450 1.00 5.60  ? 2849 ASN A C     1 
ATOM   11041 O  O     . ASN A 1 2849 ? 242.544 257.996 197.378 1.00 7.14  ? 2849 ASN A O     1 
ATOM   11042 C  CB    . ASN A 1 2849 ? 239.846 259.385 196.823 1.00 4.52  ? 2849 ASN A CB    1 
ATOM   11043 C  CG    . ASN A 1 2849 ? 239.420 260.827 196.621 1.00 8.87  ? 2849 ASN A CG    1 
ATOM   11044 O  OD1   . ASN A 1 2849 ? 238.480 261.110 195.882 1.00 6.03  ? 2849 ASN A OD1   1 
ATOM   11045 N  ND2   . ASN A 1 2849 ? 240.123 261.748 197.270 1.00 10.33 ? 2849 ASN A ND2   1 
ATOM   11046 N  N     . ILE A 1 2850 ? 241.552 256.593 195.923 1.00 5.01  ? 2850 ILE A N     1 
ATOM   11047 C  CA    . ILE A 1 2850 ? 242.423 255.480 196.285 1.00 3.85  ? 2850 ILE A CA    1 
ATOM   11048 C  C     . ILE A 1 2850 ? 243.849 255.768 195.836 1.00 7.93  ? 2850 ILE A C     1 
ATOM   11049 O  O     . ILE A 1 2850 ? 244.813 255.531 196.575 1.00 9.79  ? 2850 ILE A O     1 
ATOM   11050 C  CB    . ILE A 1 2850 ? 241.886 254.165 195.686 1.00 4.53  ? 2850 ILE A CB    1 
ATOM   11051 C  CG1   . ILE A 1 2850 ? 240.688 253.664 196.490 1.00 3.60  ? 2850 ILE A CG1   1 
ATOM   11052 C  CG2   . ILE A 1 2850 ? 242.962 253.098 195.658 1.00 2.87  ? 2850 ILE A CG2   1 
ATOM   11053 C  CD1   . ILE A 1 2850 ? 240.002 252.470 195.886 1.00 2.17  ? 2850 ILE A CD1   1 
ATOM   11054 N  N     . ASP A 1 2851 ? 244.005 256.297 194.621 1.00 10.15 ? 2851 ASP A N     1 
ATOM   11055 C  CA    . ASP A 1 2851 ? 245.324 256.687 194.137 1.00 9.22  ? 2851 ASP A CA    1 
ATOM   11056 C  C     . ASP A 1 2851 ? 245.894 257.848 194.941 1.00 11.14 ? 2851 ASP A C     1 
ATOM   11057 O  O     . ASP A 1 2851 ? 247.092 257.873 195.243 1.00 15.64 ? 2851 ASP A O     1 
ATOM   11058 C  CB    . ASP A 1 2851 ? 245.247 257.044 192.653 1.00 10.76 ? 2851 ASP A CB    1 
ATOM   11059 C  CG    . ASP A 1 2851 ? 244.789 255.880 191.797 1.00 15.28 ? 2851 ASP A CG    1 
ATOM   11060 O  OD1   . ASP A 1 2851 ? 245.472 254.836 191.790 1.00 19.77 ? 2851 ASP A OD1   1 
ATOM   11061 O  OD2   . ASP A 1 2851 ? 243.738 256.006 191.137 1.00 19.26 ? 2851 ASP A OD2   1 
ATOM   11062 N  N     . THR A 1 2852 ? 245.052 258.823 195.289 1.00 5.86  ? 2852 THR A N     1 
ATOM   11063 C  CA    . THR A 1 2852 ? 245.526 259.988 196.031 1.00 6.66  ? 2852 THR A CA    1 
ATOM   11064 C  C     . THR A 1 2852 ? 246.043 259.596 197.410 1.00 9.92  ? 2852 THR A C     1 
ATOM   11065 O  O     . THR A 1 2852 ? 247.130 260.016 197.821 1.00 11.47 ? 2852 THR A O     1 
ATOM   11066 C  CB    . THR A 1 2852 ? 244.403 261.019 196.157 1.00 7.93  ? 2852 THR A CB    1 
ATOM   11067 O  OG1   . THR A 1 2852 ? 243.981 261.435 194.853 1.00 13.95 ? 2852 THR A OG1   1 
ATOM   11068 C  CG2   . THR A 1 2852 ? 244.876 262.228 196.945 1.00 10.79 ? 2852 THR A CG2   1 
ATOM   11069 N  N     . VAL A 1 2853 ? 245.272 258.786 198.140 1.00 7.29  ? 2853 VAL A N     1 
ATOM   11070 C  CA    . VAL A 1 2853 ? 245.663 258.401 199.491 1.00 5.71  ? 2853 VAL A CA    1 
ATOM   11071 C  C     . VAL A 1 2853 ? 246.936 257.563 199.468 1.00 6.45  ? 2853 VAL A C     1 
ATOM   11072 O  O     . VAL A 1 2853 ? 247.834 257.755 200.295 1.00 12.02 ? 2853 VAL A O     1 
ATOM   11073 C  CB    . VAL A 1 2853 ? 244.505 257.663 200.190 1.00 6.98  ? 2853 VAL A CB    1 
ATOM   11074 C  CG1   . VAL A 1 2853 ? 244.977 257.022 201.481 1.00 3.43  ? 2853 VAL A CG1   1 
ATOM   11075 C  CG2   . VAL A 1 2853 ? 243.355 258.618 200.462 1.00 1.93  ? 2853 VAL A CG2   1 
ATOM   11076 N  N     . ALA A 1 2854 ? 247.037 256.629 198.521 1.00 6.40  ? 2854 ALA A N     1 
ATOM   11077 C  CA    . ALA A 1 2854 ? 248.175 255.714 198.493 1.00 5.62  ? 2854 ALA A CA    1 
ATOM   11078 C  C     . ALA A 1 2854 ? 249.489 256.452 198.267 1.00 10.06 ? 2854 ALA A C     1 
ATOM   11079 O  O     . ALA A 1 2854 ? 250.490 256.165 198.931 1.00 16.97 ? 2854 ALA A O     1 
ATOM   11080 C  CB    . ALA A 1 2854 ? 247.969 254.656 197.411 1.00 4.11  ? 2854 ALA A CB    1 
ATOM   11081 N  N     . LEU A 1 2855 ? 249.512 257.398 197.327 1.00 11.76 ? 2855 LEU A N     1 
ATOM   11082 C  CA    . LEU A 1 2855 ? 250.755 258.110 197.041 1.00 13.78 ? 2855 LEU A CA    1 
ATOM   11083 C  C     . LEU A 1 2855 ? 251.088 259.128 198.122 1.00 14.02 ? 2855 LEU A C     1 
ATOM   11084 O  O     . LEU A 1 2855 ? 252.261 259.470 198.306 1.00 22.49 ? 2855 LEU A O     1 
ATOM   11085 C  CB    . LEU A 1 2855 ? 250.682 258.783 195.669 1.00 16.01 ? 2855 LEU A CB    1 
ATOM   11086 C  CG    . LEU A 1 2855 ? 251.036 257.926 194.447 1.00 19.30 ? 2855 LEU A CG    1 
ATOM   11087 C  CD1   . LEU A 1 2855 ? 252.495 257.502 194.513 1.00 22.86 ? 2855 LEU A CD1   1 
ATOM   11088 C  CD2   . LEU A 1 2855 ? 250.138 256.705 194.311 1.00 13.03 ? 2855 LEU A CD2   1 
ATOM   11089 N  N     . LYS A 1 2856 ? 250.081 259.624 198.840 1.00 7.19  ? 2856 LYS A N     1 
ATOM   11090 C  CA    . LYS A 1 2856 ? 250.351 260.533 199.947 1.00 8.51  ? 2856 LYS A CA    1 
ATOM   11091 C  C     . LYS A 1 2856 ? 251.121 259.830 201.059 1.00 8.44  ? 2856 LYS A C     1 
ATOM   11092 O  O     . LYS A 1 2856 ? 252.040 260.409 201.650 1.00 11.88 ? 2856 LYS A O     1 
ATOM   11093 C  CB    . LYS A 1 2856 ? 249.043 261.121 200.476 1.00 7.08  ? 2856 LYS A CB    1 
ATOM   11094 C  CG    . LYS A 1 2856 ? 249.173 261.822 201.815 1.00 7.57  ? 2856 LYS A CG    1 
ATOM   11095 C  CD    . LYS A 1 2856 ? 247.815 262.205 202.365 1.00 12.06 ? 2856 LYS A CD    1 
ATOM   11096 C  CE    . LYS A 1 2856 ? 247.927 262.736 203.782 1.00 11.30 ? 2856 LYS A CE    1 
ATOM   11097 N  NZ    . LYS A 1 2856 ? 246.604 263.172 204.309 1.00 13.10 ? 2856 LYS A NZ    1 
ATOM   11098 N  N     . HIS A 1 2857 ? 250.766 258.579 201.352 1.00 6.32  ? 2857 HIS A N     1 
ATOM   11099 C  CA    . HIS A 1 2857 ? 251.432 257.821 202.402 1.00 6.34  ? 2857 HIS A CA    1 
ATOM   11100 C  C     . HIS A 1 2857 ? 252.553 256.929 201.889 1.00 8.07  ? 2857 HIS A C     1 
ATOM   11101 O  O     . HIS A 1 2857 ? 253.379 256.479 202.690 1.00 9.73  ? 2857 HIS A O     1 
ATOM   11102 C  CB    . HIS A 1 2857 ? 250.419 256.962 203.166 1.00 4.87  ? 2857 HIS A CB    1 
ATOM   11103 C  CG    . HIS A 1 2857 ? 249.304 257.748 203.776 1.00 6.17  ? 2857 HIS A CG    1 
ATOM   11104 N  ND1   . HIS A 1 2857 ? 249.400 258.331 205.020 1.00 5.93  ? 2857 HIS A ND1   1 
ATOM   11105 C  CD2   . HIS A 1 2857 ? 248.068 258.051 203.314 1.00 7.29  ? 2857 HIS A CD2   1 
ATOM   11106 C  CE1   . HIS A 1 2857 ? 248.273 258.961 205.298 1.00 7.74  ? 2857 HIS A CE1   1 
ATOM   11107 N  NE2   . HIS A 1 2857 ? 247.447 258.804 204.281 1.00 6.52  ? 2857 HIS A NE2   1 
ATOM   11108 N  N     . PHE A 1 2858 ? 252.610 256.662 200.586 1.00 10.23 ? 2858 PHE A N     1 
ATOM   11109 C  CA    . PHE A 1 2858 ? 253.654 255.823 199.998 1.00 9.82  ? 2858 PHE A CA    1 
ATOM   11110 C  C     . PHE A 1 2858 ? 254.296 256.554 198.826 1.00 17.01 ? 2858 PHE A C     1 
ATOM   11111 O  O     . PHE A 1 2858 ? 253.995 256.265 197.661 1.00 23.00 ? 2858 PHE A O     1 
ATOM   11112 C  CB    . PHE A 1 2858 ? 253.093 254.471 199.557 1.00 5.07  ? 2858 PHE A CB    1 
ATOM   11113 C  CG    . PHE A 1 2858 ? 252.712 253.574 200.696 1.00 4.76  ? 2858 PHE A CG    1 
ATOM   11114 C  CD1   . PHE A 1 2858 ? 253.644 252.725 201.268 1.00 3.87  ? 2858 PHE A CD1   1 
ATOM   11115 C  CD2   . PHE A 1 2858 ? 251.423 253.584 201.202 1.00 3.76  ? 2858 PHE A CD2   1 
ATOM   11116 C  CE1   . PHE A 1 2858 ? 253.297 251.903 202.317 1.00 2.98  ? 2858 PHE A CE1   1 
ATOM   11117 C  CE2   . PHE A 1 2858 ? 251.071 252.762 202.250 1.00 1.88  ? 2858 PHE A CE2   1 
ATOM   11118 C  CZ    . PHE A 1 2858 ? 252.008 251.920 202.809 1.00 1.46  ? 2858 PHE A CZ    1 
ATOM   11119 N  N     . PRO A 1 2859 ? 255.172 257.513 199.094 1.00 19.92 ? 2859 PRO A N     1 
ATOM   11120 C  CA    . PRO A 1 2859 ? 255.974 258.111 198.025 1.00 19.71 ? 2859 PRO A CA    1 
ATOM   11121 C  C     . PRO A 1 2859 ? 257.034 257.120 197.555 1.00 20.92 ? 2859 PRO A C     1 
ATOM   11122 O  O     . PRO A 1 2859 ? 257.195 256.035 198.109 1.00 28.90 ? 2859 PRO A O     1 
ATOM   11123 C  CB    . PRO A 1 2859 ? 256.613 259.328 198.697 1.00 18.65 ? 2859 PRO A CB    1 
ATOM   11124 C  CG    . PRO A 1 2859 ? 255.730 259.645 199.835 1.00 14.30 ? 2859 PRO A CG    1 
ATOM   11125 C  CD    . PRO A 1 2859 ? 255.229 258.322 200.325 1.00 18.88 ? 2859 PRO A CD    1 
ATOM   11126 N  N     . ASN A 1 2860 ? 257.766 257.522 196.516 1.00 15.44 ? 2860 ASN A N     1 
ATOM   11127 C  CA    . ASN A 1 2860 ? 258.919 256.768 196.024 1.00 21.10 ? 2860 ASN A CA    1 
ATOM   11128 C  C     . ASN A 1 2860 ? 258.534 255.341 195.640 1.00 22.64 ? 2860 ASN A C     1 
ATOM   11129 O  O     . ASN A 1 2860 ? 259.284 254.393 195.872 1.00 29.23 ? 2860 ASN A O     1 
ATOM   11130 C  CB    . ASN A 1 2860 ? 260.049 256.768 197.054 1.00 19.31 ? 2860 ASN A CB    1 
ATOM   11131 C  CG    . ASN A 1 2860 ? 260.224 258.115 197.723 1.00 25.09 ? 2860 ASN A CG    1 
ATOM   11132 O  OD1   . ASN A 1 2860 ? 260.076 258.240 198.938 1.00 26.61 ? 2860 ASN A OD1   1 
ATOM   11133 N  ND2   . ASN A 1 2860 ? 260.527 259.135 196.930 1.00 22.11 ? 2860 ASN A ND2   1 
ATOM   11134 N  N     . ILE A 1 2861 ? 257.353 255.190 195.047 1.00 19.70 ? 2861 ILE A N     1 
ATOM   11135 C  CA    . ILE A 1 2861 ? 256.882 253.907 194.545 1.00 17.14 ? 2861 ILE A CA    1 
ATOM   11136 C  C     . ILE A 1 2861 ? 256.532 254.077 193.076 1.00 19.63 ? 2861 ILE A C     1 
ATOM   11137 O  O     . ILE A 1 2861 ? 256.219 255.181 192.617 1.00 26.07 ? 2861 ILE A O     1 
ATOM   11138 C  CB    . ILE A 1 2861 ? 255.664 253.377 195.329 1.00 19.49 ? 2861 ILE A CB    1 
ATOM   11139 C  CG1   . ILE A 1 2861 ? 254.480 254.336 195.183 1.00 20.29 ? 2861 ILE A CG1   1 
ATOM   11140 C  CG2   . ILE A 1 2861 ? 256.016 253.173 196.791 1.00 21.44 ? 2861 ILE A CG2   1 
ATOM   11141 C  CD1   . ILE A 1 2861 ? 253.182 253.783 195.720 1.00 24.77 ? 2861 ILE A CD1   1 
ATOM   11142 N  N     . ASP A 1 2862 ? 256.586 252.976 192.334 1.00 20.35 ? 2862 ASP A N     1 
ATOM   11143 C  CA    . ASP A 1 2862 ? 256.273 253.005 190.908 1.00 21.40 ? 2862 ASP A CA    1 
ATOM   11144 C  C     . ASP A 1 2862 ? 254.754 252.958 190.781 1.00 21.09 ? 2862 ASP A C     1 
ATOM   11145 O  O     . ASP A 1 2862 ? 254.132 251.918 191.001 1.00 22.01 ? 2862 ASP A O     1 
ATOM   11146 C  CB    . ASP A 1 2862 ? 256.959 251.850 190.185 1.00 14.26 ? 2862 ASP A CB    1 
ATOM   11147 C  CG    . ASP A 1 2862 ? 256.426 251.620 188.775 1.00 26.37 ? 2862 ASP A CG    1 
ATOM   11148 O  OD1   . ASP A 1 2862 ? 255.762 252.515 188.209 1.00 22.58 ? 2862 ASP A OD1   1 
ATOM   11149 O  OD2   . ASP A 1 2862 ? 256.690 250.533 188.220 1.00 36.54 ? 2862 ASP A OD2   1 
ATOM   11150 N  N     . ARG A 1 2863 ? 254.164 254.096 190.410 1.00 21.47 ? 2863 ARG A N     1 
ATOM   11151 C  CA    . ARG A 1 2863 ? 252.709 254.228 190.377 1.00 20.92 ? 2863 ARG A CA    1 
ATOM   11152 C  C     . ARG A 1 2863 ? 252.070 253.207 189.445 1.00 24.77 ? 2863 ARG A C     1 
ATOM   11153 O  O     . ARG A 1 2863 ? 251.068 252.573 189.793 1.00 23.74 ? 2863 ARG A O     1 
ATOM   11154 C  CB    . ARG A 1 2863 ? 252.332 255.648 189.949 1.00 15.56 ? 2863 ARG A CB    1 
ATOM   11155 C  CG    . ARG A 1 2863 ? 250.843 255.954 189.953 1.00 26.07 ? 2863 ARG A CG    1 
ATOM   11156 C  CD    . ARG A 1 2863 ? 250.605 257.417 189.596 1.00 28.60 ? 2863 ARG A CD    1 
ATOM   11157 N  NE    . ARG A 1 2863 ? 249.192 257.760 189.494 1.00 24.59 ? 2863 ARG A NE    1 
ATOM   11158 C  CZ    . ARG A 1 2863 ? 248.426 258.139 190.509 1.00 26.91 ? 2863 ARG A CZ    1 
ATOM   11159 N  NH1   . ARG A 1 2863 ? 248.908 258.249 191.735 1.00 28.42 ? 2863 ARG A NH1   1 
ATOM   11160 N  NH2   . ARG A 1 2863 ? 247.148 258.426 190.285 1.00 26.67 ? 2863 ARG A NH2   1 
ATOM   11161 N  N     . GLU A 1 2864 ? 252.638 253.034 188.248 1.00 25.23 ? 2864 GLU A N     1 
ATOM   11162 C  CA    . GLU A 1 2864 ? 251.996 252.200 187.237 1.00 20.07 ? 2864 GLU A CA    1 
ATOM   11163 C  C     . GLU A 1 2864 ? 251.931 250.740 187.671 1.00 23.25 ? 2864 GLU A C     1 
ATOM   11164 O  O     . GLU A 1 2864 ? 250.885 250.093 187.539 1.00 26.27 ? 2864 GLU A O     1 
ATOM   11165 C  CB    . GLU A 1 2864 ? 252.729 252.352 185.901 1.00 24.66 ? 2864 GLU A CB    1 
ATOM   11166 C  CG    . GLU A 1 2864 ? 252.282 251.402 184.791 1.00 27.43 ? 2864 GLU A CG    1 
ATOM   11167 C  CD    . GLU A 1 2864 ? 253.057 250.097 184.775 1.00 32.41 ? 2864 GLU A CD    1 
ATOM   11168 O  OE1   . GLU A 1 2864 ? 253.996 249.950 185.586 1.00 30.05 ? 2864 GLU A OE1   1 
ATOM   11169 O  OE2   . GLU A 1 2864 ? 252.730 249.221 183.947 1.00 33.93 ? 2864 GLU A OE2   1 
ATOM   11170 N  N     . LYS A 1 2865 ? 253.031 250.203 188.204 1.00 20.80 ? 2865 LYS A N     1 
ATOM   11171 C  CA    . LYS A 1 2865 ? 253.058 248.797 188.589 1.00 19.49 ? 2865 LYS A CA    1 
ATOM   11172 C  C     . LYS A 1 2865 ? 252.196 248.516 189.812 1.00 21.55 ? 2865 LYS A C     1 
ATOM   11173 O  O     . LYS A 1 2865 ? 251.764 247.371 189.997 1.00 31.54 ? 2865 LYS A O     1 
ATOM   11174 C  CB    . LYS A 1 2865 ? 254.507 248.355 188.832 1.00 18.87 ? 2865 LYS A CB    1 
ATOM   11175 C  CG    . LYS A 1 2865 ? 254.722 246.851 189.028 1.00 26.23 ? 2865 LYS A CG    1 
ATOM   11176 C  CD    . LYS A 1 2865 ? 254.685 246.421 190.490 1.00 20.05 ? 2865 LYS A CD    1 
ATOM   11177 C  CE    . LYS A 1 2865 ? 254.966 244.929 190.622 1.00 25.75 ? 2865 LYS A CE    1 
ATOM   11178 N  NZ    . LYS A 1 2865 ? 254.904 244.461 192.035 1.00 15.30 ? 2865 LYS A NZ    1 
ATOM   11179 N  N     . ALA A 1 2866 ? 251.914 249.523 190.624 1.00 19.24 ? 2866 ALA A N     1 
ATOM   11180 C  CA    . ALA A 1 2866 ? 251.103 249.354 191.820 1.00 15.28 ? 2866 ALA A CA    1 
ATOM   11181 C  C     . ALA A 1 2866 ? 249.652 249.767 191.644 1.00 15.11 ? 2866 ALA A C     1 
ATOM   11182 O  O     . ALA A 1 2866 ? 248.786 249.215 192.325 1.00 17.44 ? 2866 ALA A O     1 
ATOM   11183 C  CB    . ALA A 1 2866 ? 251.704 250.153 192.987 1.00 15.93 ? 2866 ALA A CB    1 
ATOM   11184 N  N     . MET A 1 2867 ? 249.354 250.710 190.750 1.00 19.24 ? 2867 MET A N     1 
ATOM   11185 C  CA    . MET A 1 2867 ? 248.016 251.282 190.681 1.00 11.95 ? 2867 MET A CA    1 
ATOM   11186 C  C     . MET A 1 2867 ? 247.420 251.226 189.277 1.00 14.57 ? 2867 MET A C     1 
ATOM   11187 O  O     . MET A 1 2867 ? 246.553 252.039 188.949 1.00 20.21 ? 2867 MET A O     1 
ATOM   11188 C  CB    . MET A 1 2867 ? 248.033 252.721 191.194 1.00 17.37 ? 2867 MET A CB    1 
ATOM   11189 C  CG    . MET A 1 2867 ? 248.313 252.811 192.685 1.00 19.86 ? 2867 MET A CG    1 
ATOM   11190 S  SD    . MET A 1 2867 ? 247.060 251.974 193.663 1.00 34.54 ? 2867 MET A SD    1 
ATOM   11191 C  CE    . MET A 1 2867 ? 246.329 253.340 194.540 1.00 15.18 ? 2867 MET A CE    1 
ATOM   11192 N  N     . SER A 1 2868 ? 247.863 250.285 188.445 1.00 14.03 ? 2868 SER A N     1 
ATOM   11193 C  CA    . SER A 1 2868 ? 247.255 250.072 187.136 1.00 9.70  ? 2868 SER A CA    1 
ATOM   11194 C  C     . SER A 1 2868 ? 245.768 249.801 187.286 1.00 13.41 ? 2868 SER A C     1 
ATOM   11195 O  O     . SER A 1 2868 ? 245.367 248.852 187.965 1.00 19.18 ? 2868 SER A O     1 
ATOM   11196 C  CB    . SER A 1 2868 ? 247.935 248.900 186.424 1.00 12.26 ? 2868 SER A CB    1 
ATOM   11197 O  OG    . SER A 1 2868 ? 249.297 249.177 186.157 1.00 21.04 ? 2868 SER A OG    1 
ATOM   11198 N  N     . ARG A 1 2869 ? 244.950 250.634 186.640 1.00 15.92 ? 2869 ARG A N     1 
ATOM   11199 C  CA    . ARG A 1 2869 ? 243.517 250.684 186.933 1.00 15.98 ? 2869 ARG A CA    1 
ATOM   11200 C  C     . ARG A 1 2869 ? 242.799 249.343 186.836 1.00 22.65 ? 2869 ARG A C     1 
ATOM   11201 O  O     . ARG A 1 2869 ? 241.961 249.061 187.706 1.00 33.44 ? 2869 ARG A O     1 
ATOM   11202 C  CB    . ARG A 1 2869 ? 242.861 251.748 186.043 1.00 20.51 ? 2869 ARG A CB    1 
ATOM   11203 C  CG    . ARG A 1 2869 ? 243.140 253.201 186.472 1.00 20.09 ? 2869 ARG A CG    1 
ATOM   11204 C  CD    . ARG A 1 2869 ? 242.715 253.484 187.925 1.00 24.96 ? 2869 ARG A CD    1 
ATOM   11205 N  NE    . ARG A 1 2869 ? 243.614 252.934 188.936 1.00 23.05 ? 2869 ARG A NE    1 
ATOM   11206 C  CZ    . ARG A 1 2869 ? 243.392 252.971 190.243 1.00 16.05 ? 2869 ARG A CZ    1 
ATOM   11207 N  NH1   . ARG A 1 2869 ? 242.288 253.499 190.741 1.00 13.66 ? 2869 ARG A NH1   1 
ATOM   11208 N  NH2   . ARG A 1 2869 ? 244.297 252.460 191.069 1.00 14.18 ? 2869 ARG A NH2   1 
ATOM   11209 N  N     . PRO A 1 2870 ? 243.053 248.483 185.844 1.00 18.85 ? 2870 PRO A N     1 
ATOM   11210 C  CA    . PRO A 1 2870 ? 242.448 247.145 185.905 1.00 11.33 ? 2870 PRO A CA    1 
ATOM   11211 C  C     . PRO A 1 2870 ? 243.098 246.283 186.978 1.00 6.55  ? 2870 PRO A C     1 
ATOM   11212 O  O     . PRO A 1 2870 ? 243.970 245.462 186.682 1.00 9.11  ? 2870 PRO A O     1 
ATOM   11213 C  CB    . PRO A 1 2870 ? 242.689 246.585 184.497 1.00 8.10  ? 2870 PRO A CB    1 
ATOM   11214 C  CG    . PRO A 1 2870 ? 243.887 247.311 184.010 1.00 11.67 ? 2870 PRO A CG    1 
ATOM   11215 C  CD    . PRO A 1 2870 ? 243.794 248.690 184.586 1.00 10.93 ? 2870 PRO A CD    1 
ATOM   11216 N  N     . ILE A 1 2871 ? 242.691 246.472 188.231 1.00 4.05  ? 2871 ILE A N     1 
ATOM   11217 C  CA    . ILE A 1 2871 ? 243.221 245.697 189.350 1.00 4.84  ? 2871 ILE A CA    1 
ATOM   11218 C  C     . ILE A 1 2871 ? 242.377 244.437 189.493 1.00 2.22  ? 2871 ILE A C     1 
ATOM   11219 O  O     . ILE A 1 2871 ? 241.227 244.496 189.933 1.00 4.27  ? 2871 ILE A O     1 
ATOM   11220 C  CB    . ILE A 1 2871 ? 243.225 246.503 190.653 1.00 5.10  ? 2871 ILE A CB    1 
ATOM   11221 C  CG1   . ILE A 1 2871 ? 243.746 247.919 190.419 1.00 5.27  ? 2871 ILE A CG1   1 
ATOM   11222 C  CG2   . ILE A 1 2871 ? 244.068 245.795 191.700 1.00 3.67  ? 2871 ILE A CG2   1 
ATOM   11223 C  CD1   . ILE A 1 2871 ? 243.922 248.720 191.683 1.00 5.49  ? 2871 ILE A CD1   1 
ATOM   11224 N  N     . LEU A 1 2872 ? 242.953 243.292 189.138 1.00 2.36  ? 2872 LEU A N     1 
ATOM   11225 C  CA    . LEU A 1 2872 ? 242.252 242.019 189.201 1.00 2.01  ? 2872 LEU A CA    1 
ATOM   11226 C  C     . LEU A 1 2872 ? 243.100 241.014 189.961 1.00 1.27  ? 2872 LEU A C     1 
ATOM   11227 O  O     . LEU A 1 2872 ? 244.302 240.891 189.710 1.00 1.51  ? 2872 LEU A O     1 
ATOM   11228 C  CB    . LEU A 1 2872 ? 241.930 241.489 187.800 1.00 5.09  ? 2872 LEU A CB    1 
ATOM   11229 C  CG    . LEU A 1 2872 ? 241.182 242.456 186.883 1.00 2.90  ? 2872 LEU A CG    1 
ATOM   11230 C  CD1   . LEU A 1 2872 ? 241.191 241.949 185.453 1.00 4.04  ? 2872 LEU A CD1   1 
ATOM   11231 C  CD2   . LEU A 1 2872 ? 239.762 242.669 187.377 1.00 1.44  ? 2872 LEU A CD2   1 
ATOM   11232 N  N     . TYR A 1 2873 ? 242.471 240.302 190.889 1.00 1.68  ? 2873 TYR A N     1 
ATOM   11233 C  CA    . TYR A 1 2873 ? 243.124 239.264 191.667 1.00 1.03  ? 2873 TYR A CA    1 
ATOM   11234 C  C     . TYR A 1 2873 ? 242.322 237.979 191.546 1.00 0.67  ? 2873 TYR A C     1 
ATOM   11235 O  O     . TYR A 1 2873 ? 241.089 238.006 191.544 1.00 0.77  ? 2873 TYR A O     1 
ATOM   11236 C  CB    . TYR A 1 2873 ? 243.257 239.669 193.137 1.00 0.45  ? 2873 TYR A CB    1 
ATOM   11237 C  CG    . TYR A 1 2873 ? 244.463 240.528 193.421 1.00 0.38  ? 2873 TYR A CG    1 
ATOM   11238 C  CD1   . TYR A 1 2873 ? 244.468 241.879 193.105 1.00 0.73  ? 2873 TYR A CD1   1 
ATOM   11239 C  CD2   . TYR A 1 2873 ? 245.597 239.990 194.006 1.00 0.54  ? 2873 TYR A CD2   1 
ATOM   11240 C  CE1   . TYR A 1 2873 ? 245.569 242.667 193.362 1.00 0.48  ? 2873 TYR A CE1   1 
ATOM   11241 C  CE2   . TYR A 1 2873 ? 246.700 240.771 194.269 1.00 0.69  ? 2873 TYR A CE2   1 
ATOM   11242 C  CZ    . TYR A 1 2873 ? 246.682 242.106 193.943 1.00 0.55  ? 2873 TYR A CZ    1 
ATOM   11243 O  OH    . TYR A 1 2873 ? 247.784 242.882 194.205 1.00 2.50  ? 2873 TYR A OH    1 
ATOM   11244 N  N     . SER A 1 2874 ? 243.026 236.858 191.430 1.00 0.65  ? 2874 SER A N     1 
ATOM   11245 C  CA    . SER A 1 2874 ? 242.358 235.577 191.268 1.00 1.33  ? 2874 SER A CA    1 
ATOM   11246 C  C     . SER A 1 2874 ? 243.285 234.463 191.720 1.00 1.80  ? 2874 SER A C     1 
ATOM   11247 O  O     . SER A 1 2874 ? 244.509 234.595 191.675 1.00 2.12  ? 2874 SER A O     1 
ATOM   11248 C  CB    . SER A 1 2874 ? 241.930 235.352 189.811 1.00 0.72  ? 2874 SER A CB    1 
ATOM   11249 O  OG    . SER A 1 2874 ? 241.121 234.198 189.690 1.00 0.81  ? 2874 SER A OG    1 
ATOM   11250 N  N     . ASN A 1 2875 ? 242.678 233.360 192.159 1.00 2.04  ? 2875 ASN A N     1 
ATOM   11251 C  CA    . ASN A 1 2875 ? 243.387 232.112 192.399 1.00 3.24  ? 2875 ASN A CA    1 
ATOM   11252 C  C     . ASN A 1 2875 ? 243.032 231.058 191.357 1.00 7.61  ? 2875 ASN A C     1 
ATOM   11253 O  O     . ASN A 1 2875 ? 243.176 229.860 191.611 1.00 11.21 ? 2875 ASN A O     1 
ATOM   11254 C  CB    . ASN A 1 2875 ? 243.101 231.595 193.810 1.00 2.51  ? 2875 ASN A CB    1 
ATOM   11255 C  CG    . ASN A 1 2875 ? 241.621 231.542 194.124 1.00 4.36  ? 2875 ASN A CG    1 
ATOM   11256 O  OD1   . ASN A 1 2875 ? 240.783 231.819 193.269 1.00 7.37  ? 2875 ASN A OD1   1 
ATOM   11257 N  ND2   . ASN A 1 2875 ? 241.292 231.190 195.360 1.00 6.14  ? 2875 ASN A ND2   1 
ATOM   11258 N  N     . TRP A 1 2876 ? 242.555 231.490 190.188 1.00 2.37  ? 2876 TRP A N     1 
ATOM   11259 C  CA    . TRP A 1 2876 ? 242.135 230.558 189.150 1.00 3.09  ? 2876 TRP A CA    1 
ATOM   11260 C  C     . TRP A 1 2876 ? 243.289 230.118 188.257 1.00 9.05  ? 2876 TRP A C     1 
ATOM   11261 O  O     . TRP A 1 2876 ? 243.258 229.005 187.723 1.00 10.94 ? 2876 TRP A O     1 
ATOM   11262 C  CB    . TRP A 1 2876 ? 241.034 231.188 188.299 1.00 1.85  ? 2876 TRP A CB    1 
ATOM   11263 C  CG    . TRP A 1 2876 ? 239.704 231.229 188.974 1.00 1.78  ? 2876 TRP A CG    1 
ATOM   11264 C  CD1   . TRP A 1 2876 ? 239.332 230.546 190.092 1.00 2.10  ? 2876 TRP A CD1   1 
ATOM   11265 C  CD2   . TRP A 1 2876 ? 238.561 231.984 188.566 1.00 1.03  ? 2876 TRP A CD2   1 
ATOM   11266 N  NE1   . TRP A 1 2876 ? 238.030 230.835 190.411 1.00 0.96  ? 2876 TRP A NE1   1 
ATOM   11267 C  CE2   . TRP A 1 2876 ? 237.531 231.715 189.487 1.00 0.86  ? 2876 TRP A CE2   1 
ATOM   11268 C  CE3   . TRP A 1 2876 ? 238.307 232.866 187.512 1.00 0.85  ? 2876 TRP A CE3   1 
ATOM   11269 C  CZ2   . TRP A 1 2876 ? 236.271 232.293 189.387 1.00 0.95  ? 2876 TRP A CZ2   1 
ATOM   11270 C  CZ3   . TRP A 1 2876 ? 237.055 233.438 187.415 1.00 1.12  ? 2876 TRP A CZ3   1 
ATOM   11271 C  CH2   . TRP A 1 2876 ? 236.051 233.149 188.347 1.00 0.90  ? 2876 TRP A CH2   1 
ATOM   11272 N  N     . LEU A 1 2877 ? 244.300 230.966 188.077 1.00 6.52  ? 2877 LEU A N     1 
ATOM   11273 C  CA    . LEU A 1 2877 ? 245.426 230.655 187.207 1.00 6.01  ? 2877 LEU A CA    1 
ATOM   11274 C  C     . LEU A 1 2877 ? 246.636 230.147 187.972 1.00 13.04 ? 2877 LEU A C     1 
ATOM   11275 O  O     . LEU A 1 2877 ? 247.693 229.932 187.370 1.00 20.47 ? 2877 LEU A O     1 
ATOM   11276 C  CB    . LEU A 1 2877 ? 245.814 231.881 186.377 1.00 6.35  ? 2877 LEU A CB    1 
ATOM   11277 C  CG    . LEU A 1 2877 ? 244.721 232.535 185.527 1.00 8.68  ? 2877 LEU A CG    1 
ATOM   11278 C  CD1   . LEU A 1 2877 ? 245.345 233.340 184.403 1.00 6.16  ? 2877 LEU A CD1   1 
ATOM   11279 C  CD2   . LEU A 1 2877 ? 243.759 231.500 184.972 1.00 4.34  ? 2877 LEU A CD2   1 
ATOM   11280 N  N     . SER A 1 2878 ? 246.510 229.949 189.279 1.00 13.84 ? 2878 SER A N     1 
ATOM   11281 C  CA    . SER A 1 2878 ? 247.610 229.475 190.104 1.00 12.26 ? 2878 SER A CA    1 
ATOM   11282 C  C     . SER A 1 2878 ? 247.032 228.919 191.397 1.00 14.55 ? 2878 SER A C     1 
ATOM   11283 O  O     . SER A 1 2878 ? 245.814 228.886 191.593 1.00 20.09 ? 2878 SER A O     1 
ATOM   11284 C  CB    . SER A 1 2878 ? 248.620 230.592 190.373 1.00 16.80 ? 2878 SER A CB    1 
ATOM   11285 O  OG    . SER A 1 2878 ? 247.982 231.728 190.932 1.00 17.64 ? 2878 SER A OG    1 
ATOM   11286 N  N     . LYS A 1 2879 ? 247.922 228.478 192.284 1.00 13.90 ? 2879 LYS A N     1 
ATOM   11287 C  CA    . LYS A 1 2879 ? 247.496 228.016 193.599 1.00 15.76 ? 2879 LYS A CA    1 
ATOM   11288 C  C     . LYS A 1 2879 ? 247.143 229.177 194.518 1.00 13.48 ? 2879 LYS A C     1 
ATOM   11289 O  O     . LYS A 1 2879 ? 246.310 229.019 195.416 1.00 12.32 ? 2879 LYS A O     1 
ATOM   11290 C  CB    . LYS A 1 2879 ? 248.593 227.167 194.240 1.00 16.12 ? 2879 LYS A CB    1 
ATOM   11291 C  CG    . LYS A 1 2879 ? 249.941 227.861 194.314 1.00 19.66 ? 2879 LYS A CG    1 
ATOM   11292 C  CD    . LYS A 1 2879 ? 250.980 226.996 195.007 1.00 25.77 ? 2879 LYS A CD    1 
ATOM   11293 C  CE    . LYS A 1 2879 ? 252.322 227.704 195.084 1.00 26.28 ? 2879 LYS A CE    1 
ATOM   11294 N  NZ    . LYS A 1 2879 ? 252.801 228.141 193.744 1.00 24.84 ? 2879 LYS A NZ    1 
ATOM   11295 N  N     . ASP A 1 2880 ? 247.751 230.337 194.305 1.00 13.74 ? 2880 ASP A N     1 
ATOM   11296 C  CA    . ASP A 1 2880 ? 247.658 231.465 195.217 1.00 9.21  ? 2880 ASP A CA    1 
ATOM   11297 C  C     . ASP A 1 2880 ? 246.754 232.548 194.647 1.00 6.17  ? 2880 ASP A C     1 
ATOM   11298 O  O     . ASP A 1 2880 ? 246.478 232.602 193.446 1.00 11.37 ? 2880 ASP A O     1 
ATOM   11299 C  CB    . ASP A 1 2880 ? 249.050 232.035 195.503 1.00 9.22  ? 2880 ASP A CB    1 
ATOM   11300 C  CG    . ASP A 1 2880 ? 249.825 231.201 196.494 1.00 16.52 ? 2880 ASP A CG    1 
ATOM   11301 O  OD1   . ASP A 1 2880 ? 249.290 230.167 196.942 1.00 22.54 ? 2880 ASP A OD1   1 
ATOM   11302 O  OD2   . ASP A 1 2880 ? 250.971 231.574 196.820 1.00 18.60 ? 2880 ASP A OD2   1 
ATOM   11303 N  N     . TYR A 1 2881 ? 246.296 233.421 195.541 1.00 3.83  ? 2881 TYR A N     1 
ATOM   11304 C  CA    . TYR A 1 2881 ? 245.464 234.566 195.183 1.00 1.50  ? 2881 TYR A CA    1 
ATOM   11305 C  C     . TYR A 1 2881 ? 246.401 235.713 194.824 1.00 2.41  ? 2881 TYR A C     1 
ATOM   11306 O  O     . TYR A 1 2881 ? 246.781 236.526 195.665 1.00 4.38  ? 2881 TYR A O     1 
ATOM   11307 C  CB    . TYR A 1 2881 ? 244.527 234.916 196.330 1.00 3.10  ? 2881 TYR A CB    1 
ATOM   11308 C  CG    . TYR A 1 2881 ? 243.489 235.965 196.017 1.00 2.19  ? 2881 TYR A CG    1 
ATOM   11309 C  CD1   . TYR A 1 2881 ? 242.410 235.678 195.193 1.00 1.38  ? 2881 TYR A CD1   1 
ATOM   11310 C  CD2   . TYR A 1 2881 ? 243.562 237.233 196.579 1.00 1.00  ? 2881 TYR A CD2   1 
ATOM   11311 C  CE1   . TYR A 1 2881 ? 241.450 236.627 194.914 1.00 0.97  ? 2881 TYR A CE1   1 
ATOM   11312 C  CE2   . TYR A 1 2881 ? 242.605 238.189 196.310 1.00 1.01  ? 2881 TYR A CE2   1 
ATOM   11313 C  CZ    . TYR A 1 2881 ? 241.550 237.880 195.478 1.00 1.10  ? 2881 TYR A CZ    1 
ATOM   11314 O  OH    . TYR A 1 2881 ? 240.594 238.828 195.204 1.00 1.75  ? 2881 TYR A OH    1 
ATOM   11315 N  N     . ILE A 1 2882 ? 246.775 235.769 193.554 1.00 5.18  ? 2882 ILE A N     1 
ATOM   11316 C  CA    . ILE A 1 2882 ? 247.773 236.716 193.058 1.00 3.72  ? 2882 ILE A CA    1 
ATOM   11317 C  C     . ILE A 1 2882 ? 247.128 237.516 191.936 1.00 1.63  ? 2882 ILE A C     1 
ATOM   11318 O  O     . ILE A 1 2882 ? 246.086 237.114 191.391 1.00 2.20  ? 2882 ILE A O     1 
ATOM   11319 C  CB    . ILE A 1 2882 ? 249.059 235.998 192.590 1.00 3.08  ? 2882 ILE A CB    1 
ATOM   11320 C  CG1   . ILE A 1 2882 ? 248.769 235.124 191.369 1.00 3.27  ? 2882 ILE A CG1   1 
ATOM   11321 C  CG2   . ILE A 1 2882 ? 249.661 235.191 193.730 1.00 3.93  ? 2882 ILE A CG2   1 
ATOM   11322 C  CD1   . ILE A 1 2882 ? 250.000 234.504 190.758 1.00 4.70  ? 2882 ILE A CD1   1 
ATOM   11323 N  N     . PRO A 1 2883 ? 247.699 238.670 191.580 1.00 1.71  ? 2883 PRO A N     1 
ATOM   11324 C  CA    . PRO A 1 2883 ? 247.115 239.465 190.493 1.00 1.52  ? 2883 PRO A CA    1 
ATOM   11325 C  C     . PRO A 1 2883 ? 247.108 238.707 189.172 1.00 2.22  ? 2883 PRO A C     1 
ATOM   11326 O  O     . PRO A 1 2883 ? 248.022 237.939 188.862 1.00 3.49  ? 2883 PRO A O     1 
ATOM   11327 C  CB    . PRO A 1 2883 ? 248.027 240.697 190.429 1.00 1.76  ? 2883 PRO A CB    1 
ATOM   11328 C  CG    . PRO A 1 2883 ? 249.307 240.243 191.024 1.00 0.76  ? 2883 PRO A CG    1 
ATOM   11329 C  CD    . PRO A 1 2883 ? 248.907 239.316 192.123 1.00 1.18  ? 2883 PRO A CD    1 
ATOM   11330 N  N     . VAL A 1 2884 ? 246.057 238.939 188.390 1.00 1.84  ? 2884 VAL A N     1 
ATOM   11331 C  CA    . VAL A 1 2884 ? 245.821 238.230 187.137 1.00 2.31  ? 2884 VAL A CA    1 
ATOM   11332 C  C     . VAL A 1 2884 ? 245.624 239.249 186.023 1.00 3.58  ? 2884 VAL A C     1 
ATOM   11333 O  O     . VAL A 1 2884 ? 244.985 240.288 186.225 1.00 1.73  ? 2884 VAL A O     1 
ATOM   11334 C  CB    . VAL A 1 2884 ? 244.605 237.280 187.244 1.00 1.64  ? 2884 VAL A CB    1 
ATOM   11335 C  CG1   . VAL A 1 2884 ? 243.344 238.045 187.622 1.00 0.93  ? 2884 VAL A CG1   1 
ATOM   11336 C  CG2   . VAL A 1 2884 ? 244.399 236.512 185.950 1.00 2.10  ? 2884 VAL A CG2   1 
ATOM   11337 N  N     . ASP A 1 2885 ? 246.196 238.963 184.856 1.00 4.55  ? 2885 ASP A N     1 
ATOM   11338 C  CA    . ASP A 1 2885 ? 245.984 239.811 183.693 1.00 5.75  ? 2885 ASP A CA    1 
ATOM   11339 C  C     . ASP A 1 2885 ? 244.561 239.656 183.170 1.00 5.05  ? 2885 ASP A C     1 
ATOM   11340 O  O     . ASP A 1 2885 ? 243.984 238.565 183.212 1.00 4.48  ? 2885 ASP A O     1 
ATOM   11341 C  CB    . ASP A 1 2885 ? 246.984 239.471 182.590 1.00 5.35  ? 2885 ASP A CB    1 
ATOM   11342 C  CG    . ASP A 1 2885 ? 247.072 240.552 181.532 1.00 16.96 ? 2885 ASP A CG    1 
ATOM   11343 O  OD1   . ASP A 1 2885 ? 246.210 240.576 180.629 1.00 14.32 ? 2885 ASP A OD1   1 
ATOM   11344 O  OD2   . ASP A 1 2885 ? 248.001 241.382 181.609 1.00 22.78 ? 2885 ASP A OD2   1 
ATOM   11345 N  N     . GLN A 1 2886 ? 243.998 240.758 182.672 1.00 3.58  ? 2886 GLN A N     1 
ATOM   11346 C  CA    . GLN A 1 2886 ? 242.617 240.740 182.198 1.00 5.03  ? 2886 GLN A CA    1 
ATOM   11347 C  C     . GLN A 1 2886 ? 242.449 239.807 181.004 1.00 7.46  ? 2886 GLN A C     1 
ATOM   11348 O  O     . GLN A 1 2886 ? 241.484 239.039 180.934 1.00 5.49  ? 2886 GLN A O     1 
ATOM   11349 C  CB    . GLN A 1 2886 ? 242.165 242.156 181.842 1.00 5.43  ? 2886 GLN A CB    1 
ATOM   11350 C  CG    . GLN A 1 2886 ? 240.691 242.257 181.505 1.00 4.69  ? 2886 GLN A CG    1 
ATOM   11351 C  CD    . GLN A 1 2886 ? 240.238 243.681 181.287 1.00 6.65  ? 2886 GLN A CD    1 
ATOM   11352 O  OE1   . GLN A 1 2886 ? 240.733 244.372 180.399 1.00 15.19 ? 2886 GLN A OE1   1 
ATOM   11353 N  NE2   . GLN A 1 2886 ? 239.286 244.130 182.096 1.00 8.56  ? 2886 GLN A NE2   1 
ATOM   11354 N  N     . GLU A 1 2887 ? 243.382 239.862 180.051 1.00 9.46  ? 2887 GLU A N     1 
ATOM   11355 C  CA    . GLU A 1 2887 ? 243.277 239.004 178.874 1.00 7.07  ? 2887 GLU A CA    1 
ATOM   11356 C  C     . GLU A 1 2887 ? 243.511 237.541 179.227 1.00 7.84  ? 2887 GLU A C     1 
ATOM   11357 O  O     . GLU A 1 2887 ? 242.845 236.653 178.685 1.00 7.05  ? 2887 GLU A O     1 
ATOM   11358 C  CB    . GLU A 1 2887 ? 244.255 239.468 177.796 1.00 6.84  ? 2887 GLU A CB    1 
ATOM   11359 C  CG    . GLU A 1 2887 ? 243.937 240.845 177.239 1.00 12.16 ? 2887 GLU A CG    1 
ATOM   11360 C  CD    . GLU A 1 2887 ? 242.455 241.036 176.975 1.00 15.95 ? 2887 GLU A CD    1 
ATOM   11361 O  OE1   . GLU A 1 2887 ? 241.877 240.238 176.205 1.00 19.72 ? 2887 GLU A OE1   1 
ATOM   11362 O  OE2   . GLU A 1 2887 ? 241.869 241.984 177.535 1.00 14.17 ? 2887 GLU A OE2   1 
ATOM   11363 N  N     . GLU A 1 2888 ? 244.454 237.269 180.131 1.00 8.39  ? 2888 GLU A N     1 
ATOM   11364 C  CA    . GLU A 1 2888 ? 244.654 235.899 180.594 1.00 5.62  ? 2888 GLU A CA    1 
ATOM   11365 C  C     . GLU A 1 2888 ? 243.413 235.378 181.304 1.00 5.78  ? 2888 GLU A C     1 
ATOM   11366 O  O     . GLU A 1 2888 ? 243.022 234.220 181.121 1.00 9.21  ? 2888 GLU A O     1 
ATOM   11367 C  CB    . GLU A 1 2888 ? 245.871 235.824 181.517 1.00 5.43  ? 2888 GLU A CB    1 
ATOM   11368 C  CG    . GLU A 1 2888 ? 247.200 236.117 180.836 1.00 12.40 ? 2888 GLU A CG    1 
ATOM   11369 C  CD    . GLU A 1 2888 ? 247.584 235.068 179.812 1.00 25.24 ? 2888 GLU A CD    1 
ATOM   11370 O  OE1   . GLU A 1 2888 ? 247.228 233.886 180.007 1.00 28.15 ? 2888 GLU A OE1   1 
ATOM   11371 O  OE2   . GLU A 1 2888 ? 248.242 235.424 178.811 1.00 28.25 ? 2888 GLU A OE2   1 
ATOM   11372 N  N     . LEU A 1 2889 ? 242.780 236.222 182.122 1.00 5.19  ? 2889 LEU A N     1 
ATOM   11373 C  CA    . LEU A 1 2889 ? 241.552 235.826 182.803 1.00 4.38  ? 2889 LEU A CA    1 
ATOM   11374 C  C     . LEU A 1 2889 ? 240.422 235.581 181.810 1.00 3.89  ? 2889 LEU A C     1 
ATOM   11375 O  O     . LEU A 1 2889 ? 239.620 234.657 181.991 1.00 4.50  ? 2889 LEU A O     1 
ATOM   11376 C  CB    . LEU A 1 2889 ? 241.152 236.894 183.821 1.00 1.90  ? 2889 LEU A CB    1 
ATOM   11377 C  CG    . LEU A 1 2889 ? 239.902 236.623 184.657 1.00 1.12  ? 2889 LEU A CG    1 
ATOM   11378 C  CD1   . LEU A 1 2889 ? 240.188 235.608 185.752 1.00 0.87  ? 2889 LEU A CD1   1 
ATOM   11379 C  CD2   . LEU A 1 2889 ? 239.358 237.913 185.241 1.00 0.78  ? 2889 LEU A CD2   1 
ATOM   11380 N  N     . ARG A 1 2890 ? 240.335 236.405 180.763 1.00 5.94  ? 2890 ARG A N     1 
ATOM   11381 C  CA    . ARG A 1 2890 ? 239.260 236.255 179.787 1.00 4.46  ? 2890 ARG A CA    1 
ATOM   11382 C  C     . ARG A 1 2890 ? 239.345 234.913 179.074 1.00 5.42  ? 2890 ARG A C     1 
ATOM   11383 O  O     . ARG A 1 2890 ? 238.322 234.256 178.850 1.00 8.96  ? 2890 ARG A O     1 
ATOM   11384 C  CB    . ARG A 1 2890 ? 239.307 237.402 178.779 1.00 6.18  ? 2890 ARG A CB    1 
ATOM   11385 C  CG    . ARG A 1 2890 ? 237.999 237.625 178.040 1.00 4.87  ? 2890 ARG A CG    1 
ATOM   11386 C  CD    . ARG A 1 2890 ? 238.187 238.541 176.848 1.00 5.95  ? 2890 ARG A CD    1 
ATOM   11387 N  NE    . ARG A 1 2890 ? 238.859 239.780 177.216 1.00 9.32  ? 2890 ARG A NE    1 
ATOM   11388 C  CZ    . ARG A 1 2890 ? 238.236 240.878 177.624 1.00 11.09 ? 2890 ARG A CZ    1 
ATOM   11389 N  NH1   . ARG A 1 2890 ? 236.919 240.927 177.732 1.00 8.50  ? 2890 ARG A NH1   1 
ATOM   11390 N  NH2   . ARG A 1 2890 ? 238.956 241.951 177.939 1.00 7.02  ? 2890 ARG A NH2   1 
ATOM   11391 N  N     . ASP A 1 2891 ? 240.556 234.489 178.705 1.00 6.73  ? 2891 ASP A N     1 
ATOM   11392 C  CA    . ASP A 1 2891 ? 240.721 233.190 178.062 1.00 4.20  ? 2891 ASP A CA    1 
ATOM   11393 C  C     . ASP A 1 2891 ? 240.315 232.058 178.993 1.00 6.41  ? 2891 ASP A C     1 
ATOM   11394 O  O     . ASP A 1 2891 ? 239.659 231.099 178.567 1.00 12.65 ? 2891 ASP A O     1 
ATOM   11395 C  CB    . ASP A 1 2891 ? 242.167 233.010 177.605 1.00 8.01  ? 2891 ASP A CB    1 
ATOM   11396 C  CG    . ASP A 1 2891 ? 242.586 234.035 176.576 1.00 16.52 ? 2891 ASP A CG    1 
ATOM   11397 O  OD1   . ASP A 1 2891 ? 243.795 234.326 176.485 1.00 23.94 ? 2891 ASP A OD1   1 
ATOM   11398 O  OD2   . ASP A 1 2891 ? 241.706 234.549 175.858 1.00 16.55 ? 2891 ASP A OD2   1 
ATOM   11399 N  N     . TYR A 1 2892 ? 240.699 232.148 180.269 1.00 8.46  ? 2892 TYR A N     1 
ATOM   11400 C  CA    . TYR A 1 2892 ? 240.365 231.094 181.222 1.00 3.53  ? 2892 TYR A CA    1 
ATOM   11401 C  C     . TYR A 1 2892 ? 238.861 230.988 181.429 1.00 2.80  ? 2892 TYR A C     1 
ATOM   11402 O  O     . TYR A 1 2892 ? 238.317 229.882 181.511 1.00 5.23  ? 2892 TYR A O     1 
ATOM   11403 C  CB    . TYR A 1 2892 ? 241.078 231.346 182.548 1.00 5.25  ? 2892 TYR A CB    1 
ATOM   11404 C  CG    . TYR A 1 2892 ? 240.770 230.320 183.612 1.00 3.24  ? 2892 TYR A CG    1 
ATOM   11405 C  CD1   . TYR A 1 2892 ? 241.413 229.092 183.623 1.00 2.29  ? 2892 TYR A CD1   1 
ATOM   11406 C  CD2   . TYR A 1 2892 ? 239.833 230.579 184.604 1.00 1.82  ? 2892 TYR A CD2   1 
ATOM   11407 C  CE1   . TYR A 1 2892 ? 241.130 228.148 184.589 1.00 3.58  ? 2892 TYR A CE1   1 
ATOM   11408 C  CE2   . TYR A 1 2892 ? 239.547 229.646 185.569 1.00 1.53  ? 2892 TYR A CE2   1 
ATOM   11409 C  CZ    . TYR A 1 2892 ? 240.199 228.432 185.561 1.00 4.74  ? 2892 TYR A CZ    1 
ATOM   11410 O  OH    . TYR A 1 2892 ? 239.911 227.499 186.530 1.00 8.49  ? 2892 TYR A OH    1 
ATOM   11411 N  N     . VAL A 1 2893 ? 238.169 232.126 181.521 1.00 2.70  ? 2893 VAL A N     1 
ATOM   11412 C  CA    . VAL A 1 2893 ? 236.728 232.099 181.748 1.00 3.72  ? 2893 VAL A CA    1 
ATOM   11413 C  C     . VAL A 1 2893 ? 236.007 231.545 180.525 1.00 3.51  ? 2893 VAL A C     1 
ATOM   11414 O  O     . VAL A 1 2893 ? 235.023 230.806 180.650 1.00 3.92  ? 2893 VAL A O     1 
ATOM   11415 C  CB    . VAL A 1 2893 ? 236.217 233.500 182.137 1.00 4.08  ? 2893 VAL A CB    1 
ATOM   11416 C  CG1   . VAL A 1 2893 ? 234.696 233.518 182.215 1.00 2.54  ? 2893 VAL A CG1   1 
ATOM   11417 C  CG2   . VAL A 1 2893 ? 236.812 233.927 183.464 1.00 2.21  ? 2893 VAL A CG2   1 
ATOM   11418 N  N     . LYS A 1 2894 ? 236.487 231.876 179.322 1.00 5.68  ? 2894 LYS A N     1 
ATOM   11419 C  CA    . LYS A 1 2894 ? 235.918 231.284 178.114 1.00 3.92  ? 2894 LYS A CA    1 
ATOM   11420 C  C     . LYS A 1 2894 ? 236.119 229.775 178.092 1.00 4.19  ? 2894 LYS A C     1 
ATOM   11421 O  O     . LYS A 1 2894 ? 235.209 229.026 177.721 1.00 6.16  ? 2894 LYS A O     1 
ATOM   11422 C  CB    . LYS A 1 2894 ? 236.527 231.915 176.861 1.00 8.34  ? 2894 LYS A CB    1 
ATOM   11423 C  CG    . LYS A 1 2894 ? 236.152 233.363 176.642 1.00 11.13 ? 2894 LYS A CG    1 
ATOM   11424 C  CD    . LYS A 1 2894 ? 236.762 233.911 175.368 1.00 20.64 ? 2894 LYS A CD    1 
ATOM   11425 C  CE    . LYS A 1 2894 ? 236.396 235.374 175.169 1.00 18.30 ? 2894 LYS A CE    1 
ATOM   11426 N  NZ    . LYS A 1 2894 ? 236.995 235.935 173.929 1.00 23.26 ? 2894 LYS A NZ    1 
ATOM   11427 N  N     . ALA A 1 2895 ? 237.306 229.310 178.487 1.00 5.07  ? 2895 ALA A N     1 
ATOM   11428 C  CA    . ALA A 1 2895 ? 237.556 227.875 178.536 1.00 3.35  ? 2895 ALA A CA    1 
ATOM   11429 C  C     . ALA A 1 2895 ? 236.645 227.189 179.545 1.00 4.47  ? 2895 ALA A C     1 
ATOM   11430 O  O     . ALA A 1 2895 ? 236.124 226.098 179.281 1.00 5.21  ? 2895 ALA A O     1 
ATOM   11431 C  CB    . ALA A 1 2895 ? 239.024 227.611 178.870 1.00 2.22  ? 2895 ALA A CB    1 
ATOM   11432 N  N     . ARG A 1 2896 ? 236.438 227.811 180.708 1.00 4.73  ? 2896 ARG A N     1 
ATOM   11433 C  CA    . ARG A 1 2896 ? 235.580 227.207 181.721 1.00 3.61  ? 2896 ARG A CA    1 
ATOM   11434 C  C     . ARG A 1 2896 ? 234.107 227.341 181.362 1.00 2.97  ? 2896 ARG A C     1 
ATOM   11435 O  O     . ARG A 1 2896 ? 233.307 226.467 181.712 1.00 5.62  ? 2896 ARG A O     1 
ATOM   11436 C  CB    . ARG A 1 2896 ? 235.857 227.831 183.091 1.00 2.94  ? 2896 ARG A CB    1 
ATOM   11437 C  CG    . ARG A 1 2896 ? 237.269 227.596 183.608 1.00 1.87  ? 2896 ARG A CG    1 
ATOM   11438 C  CD    . ARG A 1 2896 ? 237.693 226.145 183.444 1.00 4.82  ? 2896 ARG A CD    1 
ATOM   11439 N  NE    . ARG A 1 2896 ? 236.896 225.232 184.252 1.00 4.41  ? 2896 ARG A NE    1 
ATOM   11440 C  CZ    . ARG A 1 2896 ? 236.815 223.924 184.039 1.00 4.12  ? 2896 ARG A CZ    1 
ATOM   11441 N  NH1   . ARG A 1 2896 ? 237.442 223.348 183.027 1.00 3.49  ? 2896 ARG A NH1   1 
ATOM   11442 N  NH2   . ARG A 1 2896 ? 236.081 223.177 184.860 1.00 4.01  ? 2896 ARG A NH2   1 
ATOM   11443 N  N     . LEU A 1 2897 ? 233.728 228.420 180.672 1.00 2.15  ? 2897 LEU A N     1 
ATOM   11444 C  CA    . LEU A 1 2897 ? 232.343 228.567 180.237 1.00 3.03  ? 2897 LEU A CA    1 
ATOM   11445 C  C     . LEU A 1 2897 ? 231.960 227.497 179.227 1.00 3.24  ? 2897 LEU A C     1 
ATOM   11446 O  O     . LEU A 1 2897 ? 230.806 227.054 179.199 1.00 3.90  ? 2897 LEU A O     1 
ATOM   11447 C  CB    . LEU A 1 2897 ? 232.118 229.961 179.645 1.00 1.87  ? 2897 LEU A CB    1 
ATOM   11448 C  CG    . LEU A 1 2897 ? 231.715 231.065 180.623 1.00 2.03  ? 2897 LEU A CG    1 
ATOM   11449 C  CD1   . LEU A 1 2897 ? 231.643 232.403 179.912 1.00 2.11  ? 2897 LEU A CD1   1 
ATOM   11450 C  CD2   . LEU A 1 2897 ? 230.393 230.741 181.302 1.00 0.84  ? 2897 LEU A CD2   1 
ATOM   11451 N  N     . LYS A 1 2898 ? 232.911 227.070 178.393 1.00 4.10  ? 2898 LYS A N     1 
ATOM   11452 C  CA    . LYS A 1 2898 ? 232.655 225.988 177.450 1.00 4.57  ? 2898 LYS A CA    1 
ATOM   11453 C  C     . LYS A 1 2898 ? 232.263 224.709 178.180 1.00 8.33  ? 2898 LYS A C     1 
ATOM   11454 O  O     . LYS A 1 2898 ? 231.305 224.027 177.797 1.00 14.08 ? 2898 LYS A O     1 
ATOM   11455 C  CB    . LYS A 1 2898 ? 233.892 225.760 176.583 1.00 6.09  ? 2898 LYS A CB    1 
ATOM   11456 C  CG    . LYS A 1 2898 ? 233.713 224.727 175.489 1.00 10.37 ? 2898 LYS A CG    1 
ATOM   11457 C  CD    . LYS A 1 2898 ? 234.962 224.627 174.630 1.00 17.10 ? 2898 LYS A CD    1 
ATOM   11458 C  CE    . LYS A 1 2898 ? 234.800 223.590 173.534 1.00 24.01 ? 2898 LYS A CE    1 
ATOM   11459 N  NZ    . LYS A 1 2898 ? 236.019 223.486 172.692 1.00 24.87 ? 2898 LYS A NZ    1 
ATOM   11460 N  N     . VAL A 1 2899 ? 232.995 224.370 179.241 1.00 4.20  ? 2899 VAL A N     1 
ATOM   11461 C  CA    . VAL A 1 2899 ? 232.654 223.197 180.039 1.00 3.07  ? 2899 VAL A CA    1 
ATOM   11462 C  C     . VAL A 1 2899 ? 231.336 223.414 180.773 1.00 4.37  ? 2899 VAL A C     1 
ATOM   11463 O  O     . VAL A 1 2899 ? 230.533 222.486 180.925 1.00 7.35  ? 2899 VAL A O     1 
ATOM   11464 C  CB    . VAL A 1 2899 ? 233.804 222.869 181.008 1.00 1.47  ? 2899 VAL A CB    1 
ATOM   11465 C  CG1   . VAL A 1 2899 ? 233.498 221.615 181.793 1.00 1.41  ? 2899 VAL A CG1   1 
ATOM   11466 C  CG2   . VAL A 1 2899 ? 235.109 222.720 180.247 1.00 1.33  ? 2899 VAL A CG2   1 
ATOM   11467 N  N     . PHE A 1 2900 ? 231.093 224.644 181.233 1.00 3.79  ? 2900 PHE A N     1 
ATOM   11468 C  CA    . PHE A 1 2900 ? 229.863 224.947 181.960 1.00 3.10  ? 2900 PHE A CA    1 
ATOM   11469 C  C     . PHE A 1 2900 ? 228.633 224.755 181.079 1.00 4.77  ? 2900 PHE A C     1 
ATOM   11470 O  O     . PHE A 1 2900 ? 227.577 224.327 181.561 1.00 2.74  ? 2900 PHE A O     1 
ATOM   11471 C  CB    . PHE A 1 2900 ? 229.928 226.376 182.503 1.00 1.27  ? 2900 PHE A CB    1 
ATOM   11472 C  CG    . PHE A 1 2900 ? 228.733 226.779 183.315 1.00 0.67  ? 2900 PHE A CG    1 
ATOM   11473 C  CD1   . PHE A 1 2900 ? 228.528 226.256 184.582 1.00 0.52  ? 2900 PHE A CD1   1 
ATOM   11474 C  CD2   . PHE A 1 2900 ? 227.829 227.705 182.826 1.00 0.55  ? 2900 PHE A CD2   1 
ATOM   11475 C  CE1   . PHE A 1 2900 ? 227.435 226.639 185.337 1.00 0.46  ? 2900 PHE A CE1   1 
ATOM   11476 C  CE2   . PHE A 1 2900 ? 226.733 228.089 183.575 1.00 0.46  ? 2900 PHE A CE2   1 
ATOM   11477 C  CZ    . PHE A 1 2900 ? 226.536 227.554 184.833 1.00 0.31  ? 2900 PHE A CZ    1 
ATOM   11478 N  N     . TYR A 1 2901 ? 228.746 225.071 179.787 1.00 4.82  ? 2901 TYR A N     1 
ATOM   11479 C  CA    . TYR A 1 2901 ? 227.620 224.888 178.876 1.00 6.00  ? 2901 TYR A CA    1 
ATOM   11480 C  C     . TYR A 1 2901 ? 227.252 223.416 178.736 1.00 7.68  ? 2901 TYR A C     1 
ATOM   11481 O  O     . TYR A 1 2901 ? 226.067 223.070 178.665 1.00 9.84  ? 2901 TYR A O     1 
ATOM   11482 C  CB    . TYR A 1 2901 ? 227.946 225.483 177.507 1.00 6.18  ? 2901 TYR A CB    1 
ATOM   11483 C  CG    . TYR A 1 2901 ? 228.228 226.966 177.523 1.00 6.46  ? 2901 TYR A CG    1 
ATOM   11484 C  CD1   . TYR A 1 2901 ? 227.628 227.800 178.458 1.00 5.01  ? 2901 TYR A CD1   1 
ATOM   11485 C  CD2   . TYR A 1 2901 ? 229.095 227.534 176.600 1.00 4.07  ? 2901 TYR A CD2   1 
ATOM   11486 C  CE1   . TYR A 1 2901 ? 227.886 229.154 178.473 1.00 3.96  ? 2901 TYR A CE1   1 
ATOM   11487 C  CE2   . TYR A 1 2901 ? 229.360 228.886 176.608 1.00 2.32  ? 2901 TYR A CE2   1 
ATOM   11488 C  CZ    . TYR A 1 2901 ? 228.753 229.693 177.545 1.00 3.36  ? 2901 TYR A CZ    1 
ATOM   11489 O  OH    . TYR A 1 2901 ? 229.017 231.043 177.553 1.00 6.57  ? 2901 TYR A OH    1 
ATOM   11490 N  N     . GLU A 1 2902 ? 228.252 222.536 178.697 1.00 8.23  ? 2902 GLU A N     1 
ATOM   11491 C  CA    . GLU A 1 2902 ? 228.032 221.114 178.464 1.00 7.77  ? 2902 GLU A CA    1 
ATOM   11492 C  C     . GLU A 1 2902 ? 227.648 220.341 179.720 1.00 8.41  ? 2902 GLU A C     1 
ATOM   11493 O  O     . GLU A 1 2902 ? 227.234 219.184 179.606 1.00 19.54 ? 2902 GLU A O     1 
ATOM   11494 C  CB    . GLU A 1 2902 ? 229.288 220.494 177.853 1.00 8.90  ? 2902 GLU A CB    1 
ATOM   11495 C  CG    . GLU A 1 2902 ? 229.596 220.987 176.449 1.00 15.35 ? 2902 GLU A CG    1 
ATOM   11496 C  CD    . GLU A 1 2902 ? 230.854 220.370 175.875 1.00 26.23 ? 2902 GLU A CD    1 
ATOM   11497 O  OE1   . GLU A 1 2902 ? 231.558 219.652 176.616 1.00 26.80 ? 2902 GLU A OE1   1 
ATOM   11498 O  OE2   . GLU A 1 2902 ? 231.138 220.598 174.681 1.00 32.32 ? 2902 GLU A OE2   1 
ATOM   11499 N  N     . GLU A 1 2903 ? 227.769 220.933 180.904 1.00 7.57  ? 2903 GLU A N     1 
ATOM   11500 C  CA    . GLU A 1 2903 ? 227.491 220.220 182.144 1.00 7.10  ? 2903 GLU A CA    1 
ATOM   11501 C  C     . GLU A 1 2903 ? 226.315 220.773 182.932 1.00 11.52 ? 2903 GLU A C     1 
ATOM   11502 O  O     . GLU A 1 2903 ? 225.536 219.994 183.486 1.00 19.72 ? 2903 GLU A O     1 
ATOM   11503 C  CB    . GLU A 1 2903 ? 228.732 220.213 183.045 1.00 6.96  ? 2903 GLU A CB    1 
ATOM   11504 C  CG    . GLU A 1 2903 ? 229.869 219.348 182.535 1.00 11.03 ? 2903 GLU A CG    1 
ATOM   11505 C  CD    . GLU A 1 2903 ? 231.075 219.371 183.451 1.00 21.10 ? 2903 GLU A CD    1 
ATOM   11506 O  OE1   . GLU A 1 2903 ? 230.925 219.757 184.631 1.00 27.01 ? 2903 GLU A OE1   1 
ATOM   11507 O  OE2   . GLU A 1 2903 ? 232.176 218.989 183.000 1.00 22.54 ? 2903 GLU A OE2   1 
ATOM   11508 N  N     . GLU A 1 2904 ? 226.160 222.094 183.012 1.00 10.81 ? 2904 GLU A N     1 
ATOM   11509 C  CA    . GLU A 1 2904 ? 225.164 222.694 183.888 1.00 7.79  ? 2904 GLU A CA    1 
ATOM   11510 C  C     . GLU A 1 2904 ? 224.079 223.445 183.128 1.00 10.76 ? 2904 GLU A C     1 
ATOM   11511 O  O     . GLU A 1 2904 ? 222.894 223.132 183.270 1.00 17.36 ? 2904 GLU A O     1 
ATOM   11512 C  CB    . GLU A 1 2904 ? 225.852 223.635 184.883 1.00 4.71  ? 2904 GLU A CB    1 
ATOM   11513 C  CG    . GLU A 1 2904 ? 226.743 222.934 185.885 1.00 9.11  ? 2904 GLU A CG    1 
ATOM   11514 C  CD    . GLU A 1 2904 ? 225.965 222.049 186.835 1.00 17.62 ? 2904 GLU A CD    1 
ATOM   11515 O  OE1   . GLU A 1 2904 ? 225.026 222.555 187.485 1.00 14.58 ? 2904 GLU A OE1   1 
ATOM   11516 O  OE2   . GLU A 1 2904 ? 226.292 220.849 186.932 1.00 17.80 ? 2904 GLU A OE2   1 
ATOM   11517 N  N     . LEU A 1 2905 ? 224.451 224.432 182.316 1.00 8.19  ? 2905 LEU A N     1 
ATOM   11518 C  CA    . LEU A 1 2905 ? 223.472 225.323 181.705 1.00 7.34  ? 2905 LEU A CA    1 
ATOM   11519 C  C     . LEU A 1 2905 ? 223.959 225.693 180.313 1.00 6.14  ? 2905 LEU A C     1 
ATOM   11520 O  O     . LEU A 1 2905 ? 224.957 226.405 180.174 1.00 10.61 ? 2905 LEU A O     1 
ATOM   11521 C  CB    . LEU A 1 2905 ? 223.264 226.570 182.558 1.00 7.53  ? 2905 LEU A CB    1 
ATOM   11522 C  CG    . LEU A 1 2905 ? 221.874 227.202 182.542 1.00 5.81  ? 2905 LEU A CG    1 
ATOM   11523 C  CD1   . LEU A 1 2905 ? 220.809 226.157 182.820 1.00 5.55  ? 2905 LEU A CD1   1 
ATOM   11524 C  CD2   . LEU A 1 2905 ? 221.802 228.338 183.548 1.00 7.26  ? 2905 LEU A CD2   1 
ATOM   11525 N  N     . ASP A 1 2906 ? 223.250 225.227 179.290 1.00 8.45  ? 2906 ASP A N     1 
ATOM   11526 C  CA    . ASP A 1 2906 ? 223.609 225.547 177.908 1.00 9.37  ? 2906 ASP A CA    1 
ATOM   11527 C  C     . ASP A 1 2906 ? 222.933 226.850 177.475 1.00 8.99  ? 2906 ASP A C     1 
ATOM   11528 O  O     . ASP A 1 2906 ? 222.088 226.895 176.584 1.00 12.10 ? 2906 ASP A O     1 
ATOM   11529 C  CB    . ASP A 1 2906 ? 223.251 224.391 176.983 1.00 11.40 ? 2906 ASP A CB    1 
ATOM   11530 C  CG    . ASP A 1 2906 ? 223.732 224.616 175.566 1.00 18.42 ? 2906 ASP A CG    1 
ATOM   11531 O  OD1   . ASP A 1 2906 ? 224.951 224.497 175.326 1.00 21.28 ? 2906 ASP A OD1   1 
ATOM   11532 O  OD2   . ASP A 1 2906 ? 222.894 224.909 174.688 1.00 29.58 ? 2906 ASP A OD2   1 
ATOM   11533 N  N     . VAL A 1 2907 ? 223.322 227.923 178.148 1.00 7.72  ? 2907 VAL A N     1 
ATOM   11534 C  CA    . VAL A 1 2907 ? 222.915 229.277 177.800 1.00 6.53  ? 2907 VAL A CA    1 
ATOM   11535 C  C     . VAL A 1 2907 ? 224.171 230.077 177.482 1.00 6.75  ? 2907 VAL A C     1 
ATOM   11536 O  O     . VAL A 1 2907 ? 224.888 230.512 178.383 1.00 12.62 ? 2907 VAL A O     1 
ATOM   11537 C  CB    . VAL A 1 2907 ? 222.108 229.937 178.934 1.00 6.93  ? 2907 VAL A CB    1 
ATOM   11538 C  CG1   . VAL A 1 2907 ? 221.582 231.287 178.489 1.00 5.05  ? 2907 VAL A CG1   1 
ATOM   11539 C  CG2   . VAL A 1 2907 ? 220.964 229.033 179.377 1.00 7.86  ? 2907 VAL A CG2   1 
ATOM   11540 N  N     . PRO A 1 2908 ? 224.479 230.279 176.202 1.00 5.73  ? 2908 PRO A N     1 
ATOM   11541 C  CA    . PRO A 1 2908 ? 225.704 231.007 175.844 1.00 6.26  ? 2908 PRO A CA    1 
ATOM   11542 C  C     . PRO A 1 2908 ? 225.691 232.430 176.382 1.00 7.59  ? 2908 PRO A C     1 
ATOM   11543 O  O     . PRO A 1 2908 ? 224.657 233.100 176.401 1.00 13.71 ? 2908 PRO A O     1 
ATOM   11544 C  CB    . PRO A 1 2908 ? 225.695 230.985 174.311 1.00 8.70  ? 2908 PRO A CB    1 
ATOM   11545 C  CG    . PRO A 1 2908 ? 224.814 229.831 173.952 1.00 5.91  ? 2908 PRO A CG    1 
ATOM   11546 C  CD    . PRO A 1 2908 ? 223.760 229.794 175.013 1.00 5.95  ? 2908 PRO A CD    1 
ATOM   11547 N  N     . LEU A 1 2909 ? 226.861 232.889 176.814 1.00 5.71  ? 2909 LEU A N     1 
ATOM   11548 C  CA    . LEU A 1 2909 ? 227.023 234.217 177.387 1.00 2.59  ? 2909 LEU A CA    1 
ATOM   11549 C  C     . LEU A 1 2909 ? 228.107 234.972 176.636 1.00 2.82  ? 2909 LEU A C     1 
ATOM   11550 O  O     . LEU A 1 2909 ? 229.145 234.404 176.287 1.00 4.60  ? 2909 LEU A O     1 
ATOM   11551 C  CB    . LEU A 1 2909 ? 227.387 234.146 178.875 1.00 2.95  ? 2909 LEU A CB    1 
ATOM   11552 C  CG    . LEU A 1 2909 ? 226.450 233.364 179.794 1.00 4.26  ? 2909 LEU A CG    1 
ATOM   11553 C  CD1   . LEU A 1 2909 ? 227.135 233.078 181.117 1.00 3.12  ? 2909 LEU A CD1   1 
ATOM   11554 C  CD2   . LEU A 1 2909 ? 225.158 234.130 180.010 1.00 2.59  ? 2909 LEU A CD2   1 
ATOM   11555 N  N     . VAL A 1 2910 ? 227.859 236.252 176.392 1.00 2.97  ? 2910 VAL A N     1 
ATOM   11556 C  CA    . VAL A 1 2910 ? 228.859 237.142 175.815 1.00 3.76  ? 2910 VAL A CA    1 
ATOM   11557 C  C     . VAL A 1 2910 ? 229.699 237.706 176.950 1.00 3.14  ? 2910 VAL A C     1 
ATOM   11558 O  O     . VAL A 1 2910 ? 229.162 238.244 177.924 1.00 7.32  ? 2910 VAL A O     1 
ATOM   11559 C  CB    . VAL A 1 2910 ? 228.195 238.267 175.004 1.00 4.82  ? 2910 VAL A CB    1 
ATOM   11560 C  CG1   . VAL A 1 2910 ? 229.244 239.244 174.496 1.00 3.32  ? 2910 VAL A CG1   1 
ATOM   11561 C  CG2   . VAL A 1 2910 ? 227.391 237.689 173.852 1.00 3.04  ? 2910 VAL A CG2   1 
ATOM   11562 N  N     . LEU A 1 2911 ? 231.016 237.575 176.833 1.00 2.11  ? 2911 LEU A N     1 
ATOM   11563 C  CA    . LEU A 1 2911 ? 231.930 237.971 177.898 1.00 2.68  ? 2911 LEU A CA    1 
ATOM   11564 C  C     . LEU A 1 2911 ? 232.410 239.395 177.648 1.00 4.73  ? 2911 LEU A C     1 
ATOM   11565 O  O     . LEU A 1 2911 ? 233.149 239.649 176.693 1.00 18.36 ? 2911 LEU A O     1 
ATOM   11566 C  CB    . LEU A 1 2911 ? 233.113 237.014 177.981 1.00 5.07  ? 2911 LEU A CB    1 
ATOM   11567 C  CG    . LEU A 1 2911 ? 232.906 235.747 178.807 1.00 5.58  ? 2911 LEU A CG    1 
ATOM   11568 C  CD1   . LEU A 1 2911 ? 234.227 235.042 179.014 1.00 6.88  ? 2911 LEU A CD1   1 
ATOM   11569 C  CD2   . LEU A 1 2911 ? 232.254 236.063 180.132 1.00 4.77  ? 2911 LEU A CD2   1 
ATOM   11570 N  N     . PHE A 1 2912 ? 231.993 240.320 178.502 1.00 1.49  ? 2912 PHE A N     1 
ATOM   11571 C  CA    . PHE A 1 2912 ? 232.531 241.669 178.512 1.00 2.14  ? 2912 PHE A CA    1 
ATOM   11572 C  C     . PHE A 1 2912 ? 233.261 241.921 179.826 1.00 3.23  ? 2912 PHE A C     1 
ATOM   11573 O  O     . PHE A 1 2912 ? 233.263 241.089 180.736 1.00 3.01  ? 2912 PHE A O     1 
ATOM   11574 C  CB    . PHE A 1 2912 ? 231.428 242.711 178.265 1.00 1.87  ? 2912 PHE A CB    1 
ATOM   11575 C  CG    . PHE A 1 2912 ? 230.257 242.615 179.200 1.00 1.74  ? 2912 PHE A CG    1 
ATOM   11576 C  CD1   . PHE A 1 2912 ? 229.208 241.756 178.929 1.00 1.42  ? 2912 PHE A CD1   1 
ATOM   11577 C  CD2   . PHE A 1 2912 ? 230.182 243.417 180.324 1.00 2.20  ? 2912 PHE A CD2   1 
ATOM   11578 C  CE1   . PHE A 1 2912 ? 228.119 241.680 179.772 1.00 0.76  ? 2912 PHE A CE1   1 
ATOM   11579 C  CE2   . PHE A 1 2912 ? 229.094 243.343 181.172 1.00 1.62  ? 2912 PHE A CE2   1 
ATOM   11580 C  CZ    . PHE A 1 2912 ? 228.064 242.474 180.894 1.00 1.24  ? 2912 PHE A CZ    1 
ATOM   11581 N  N     . ASN A 1 2913 ? 233.899 243.092 179.906 1.00 3.24  ? 2913 ASN A N     1 
ATOM   11582 C  CA    . ASN A 1 2913 ? 234.849 243.357 180.983 1.00 1.33  ? 2913 ASN A CA    1 
ATOM   11583 C  C     . ASN A 1 2913 ? 234.181 243.338 182.353 1.00 3.80  ? 2913 ASN A C     1 
ATOM   11584 O  O     . ASN A 1 2913 ? 234.756 242.830 183.321 1.00 2.94  ? 2913 ASN A O     1 
ATOM   11585 C  CB    . ASN A 1 2913 ? 235.550 244.692 180.744 1.00 1.80  ? 2913 ASN A CB    1 
ATOM   11586 C  CG    . ASN A 1 2913 ? 236.658 244.591 179.717 1.00 2.43  ? 2913 ASN A CG    1 
ATOM   11587 O  OD1   . ASN A 1 2913 ? 236.986 243.503 179.247 1.00 3.95  ? 2913 ASN A OD1   1 
ATOM   11588 N  ND2   . ASN A 1 2913 ? 237.241 245.727 179.360 1.00 1.82  ? 2913 ASN A ND2   1 
ATOM   11589 N  N     . GLU A 1 2914 ? 232.973 243.895 182.460 1.00 4.32  ? 2914 GLU A N     1 
ATOM   11590 C  CA    . GLU A 1 2914 ? 232.296 243.932 183.754 1.00 2.79  ? 2914 GLU A CA    1 
ATOM   11591 C  C     . GLU A 1 2914 ? 231.964 242.535 184.263 1.00 2.81  ? 2914 GLU A C     1 
ATOM   11592 O  O     . GLU A 1 2914 ? 231.936 242.316 185.478 1.00 5.94  ? 2914 GLU A O     1 
ATOM   11593 C  CB    . GLU A 1 2914 ? 231.030 244.781 183.666 1.00 4.14  ? 2914 GLU A CB    1 
ATOM   11594 C  CG    . GLU A 1 2914 ? 231.282 246.271 183.591 1.00 10.22 ? 2914 GLU A CG    1 
ATOM   11595 C  CD    . GLU A 1 2914 ? 230.188 247.011 182.847 1.00 19.05 ? 2914 GLU A CD    1 
ATOM   11596 O  OE1   . GLU A 1 2914 ? 228.998 246.799 183.162 1.00 9.62  ? 2914 GLU A OE1   1 
ATOM   11597 O  OE2   . GLU A 1 2914 ? 230.520 247.807 181.942 1.00 15.51 ? 2914 GLU A OE2   1 
ATOM   11598 N  N     . VAL A 1 2915 ? 231.708 241.585 183.361 1.00 2.31  ? 2915 VAL A N     1 
ATOM   11599 C  CA    . VAL A 1 2915 ? 231.432 240.214 183.786 1.00 1.41  ? 2915 VAL A CA    1 
ATOM   11600 C  C     . VAL A 1 2915 ? 232.655 239.610 184.463 1.00 0.93  ? 2915 VAL A C     1 
ATOM   11601 O  O     . VAL A 1 2915 ? 232.545 238.943 185.498 1.00 2.16  ? 2915 VAL A O     1 
ATOM   11602 C  CB    . VAL A 1 2915 ? 230.966 239.359 182.591 1.00 1.80  ? 2915 VAL A CB    1 
ATOM   11603 C  CG1   . VAL A 1 2915 ? 231.106 237.883 182.908 1.00 2.46  ? 2915 VAL A CG1   1 
ATOM   11604 C  CG2   . VAL A 1 2915 ? 229.534 239.678 182.241 1.00 1.05  ? 2915 VAL A CG2   1 
ATOM   11605 N  N     . LEU A 1 2916 ? 233.842 239.842 183.895 1.00 1.00  ? 2916 LEU A N     1 
ATOM   11606 C  CA    . LEU A 1 2916 ? 235.066 239.299 184.474 1.00 0.86  ? 2916 LEU A CA    1 
ATOM   11607 C  C     . LEU A 1 2916 ? 235.302 239.838 185.878 1.00 0.98  ? 2916 LEU A C     1 
ATOM   11608 O  O     . LEU A 1 2916 ? 235.722 239.099 186.775 1.00 0.81  ? 2916 LEU A O     1 
ATOM   11609 C  CB    . LEU A 1 2916 ? 236.258 239.615 183.572 1.00 0.88  ? 2916 LEU A CB    1 
ATOM   11610 C  CG    . LEU A 1 2916 ? 236.226 239.043 182.158 1.00 1.60  ? 2916 LEU A CG    1 
ATOM   11611 C  CD1   . LEU A 1 2916 ? 237.447 239.495 181.378 1.00 4.21  ? 2916 LEU A CD1   1 
ATOM   11612 C  CD2   . LEU A 1 2916 ? 236.140 237.527 182.192 1.00 1.97  ? 2916 LEU A CD2   1 
ATOM   11613 N  N     . ASP A 1 2917 ? 235.054 241.131 186.084 1.00 1.22  ? 2917 ASP A N     1 
ATOM   11614 C  CA    . ASP A 1 2917 ? 235.163 241.692 187.425 1.00 1.18  ? 2917 ASP A CA    1 
ATOM   11615 C  C     . ASP A 1 2917 ? 234.084 241.117 188.338 1.00 0.74  ? 2917 ASP A C     1 
ATOM   11616 O  O     . ASP A 1 2917 ? 234.348 240.805 189.504 1.00 0.26  ? 2917 ASP A O     1 
ATOM   11617 C  CB    . ASP A 1 2917 ? 235.081 243.221 187.355 1.00 1.73  ? 2917 ASP A CB    1 
ATOM   11618 C  CG    . ASP A 1 2917 ? 235.406 243.901 188.683 1.00 9.27  ? 2917 ASP A CG    1 
ATOM   11619 O  OD1   . ASP A 1 2917 ? 235.672 243.209 189.686 1.00 8.27  ? 2917 ASP A OD1   1 
ATOM   11620 O  OD2   . ASP A 1 2917 ? 235.405 245.150 188.718 1.00 12.56 ? 2917 ASP A OD2   1 
ATOM   11621 N  N     . HIS A 1 2918 ? 232.867 240.943 187.813 1.00 0.61  ? 2918 HIS A N     1 
ATOM   11622 C  CA    . HIS A 1 2918 ? 231.767 240.439 188.631 1.00 1.08  ? 2918 HIS A CA    1 
ATOM   11623 C  C     . HIS A 1 2918 ? 232.004 239.002 189.083 1.00 0.41  ? 2918 HIS A C     1 
ATOM   11624 O  O     . HIS A 1 2918 ? 231.757 238.668 190.247 1.00 0.23  ? 2918 HIS A O     1 
ATOM   11625 C  CB    . HIS A 1 2918 ? 230.447 240.544 187.868 1.00 0.67  ? 2918 HIS A CB    1 
ATOM   11626 C  CG    . HIS A 1 2918 ? 229.945 241.945 187.724 1.00 1.32  ? 2918 HIS A CG    1 
ATOM   11627 N  ND1   . HIS A 1 2918 ? 228.902 242.278 186.888 1.00 3.03  ? 2918 HIS A ND1   1 
ATOM   11628 C  CD2   . HIS A 1 2918 ? 230.347 243.099 188.303 1.00 2.50  ? 2918 HIS A CD2   1 
ATOM   11629 C  CE1   . HIS A 1 2918 ? 228.679 243.577 186.964 1.00 1.78  ? 2918 HIS A CE1   1 
ATOM   11630 N  NE2   . HIS A 1 2918 ? 229.542 244.100 187.816 1.00 3.07  ? 2918 HIS A NE2   1 
ATOM   11631 N  N     . VAL A 1 2919 ? 232.473 238.137 188.182 1.00 0.43  ? 2919 VAL A N     1 
ATOM   11632 C  CA    . VAL A 1 2919 ? 232.688 236.744 188.564 1.00 0.66  ? 2919 VAL A CA    1 
ATOM   11633 C  C     . VAL A 1 2919 ? 233.792 236.639 189.606 1.00 0.26  ? 2919 VAL A C     1 
ATOM   11634 O  O     . VAL A 1 2919 ? 233.736 235.778 190.491 1.00 0.22  ? 2919 VAL A O     1 
ATOM   11635 C  CB    . VAL A 1 2919 ? 232.970 235.864 187.328 1.00 0.43  ? 2919 VAL A CB    1 
ATOM   11636 C  CG1   . VAL A 1 2919 ? 231.796 235.909 186.369 1.00 0.38  ? 2919 VAL A CG1   1 
ATOM   11637 C  CG2   . VAL A 1 2919 ? 234.252 236.282 186.630 1.00 0.70  ? 2919 VAL A CG2   1 
ATOM   11638 N  N     . LEU A 1 2920 ? 234.805 237.504 189.529 1.00 0.26  ? 2920 LEU A N     1 
ATOM   11639 C  CA    . LEU A 1 2920 ? 235.843 237.522 190.554 1.00 0.21  ? 2920 LEU A CA    1 
ATOM   11640 C  C     . LEU A 1 2920 ? 235.280 237.956 191.904 1.00 0.28  ? 2920 LEU A C     1 
ATOM   11641 O  O     . LEU A 1 2920 ? 235.663 237.411 192.944 1.00 0.43  ? 2920 LEU A O     1 
ATOM   11642 C  CB    . LEU A 1 2920 ? 236.988 238.437 190.123 1.00 0.18  ? 2920 LEU A CB    1 
ATOM   11643 C  CG    . LEU A 1 2920 ? 237.904 237.902 189.019 1.00 0.35  ? 2920 LEU A CG    1 
ATOM   11644 C  CD1   . LEU A 1 2920 ? 239.066 238.845 188.781 1.00 0.37  ? 2920 LEU A CD1   1 
ATOM   11645 C  CD2   . LEU A 1 2920 ? 238.403 236.504 189.346 1.00 0.33  ? 2920 LEU A CD2   1 
ATOM   11646 N  N     . ARG A 1 2921 ? 234.374 238.937 191.908 1.00 0.19  ? 2921 ARG A N     1 
ATOM   11647 C  CA    . ARG A 1 2921 ? 233.758 239.379 193.155 1.00 0.21  ? 2921 ARG A CA    1 
ATOM   11648 C  C     . ARG A 1 2921 ? 232.892 238.287 193.768 1.00 0.28  ? 2921 ARG A C     1 
ATOM   11649 O  O     . ARG A 1 2921 ? 232.894 238.103 194.991 1.00 0.50  ? 2921 ARG A O     1 
ATOM   11650 C  CB    . ARG A 1 2921 ? 232.931 240.643 192.919 1.00 0.64  ? 2921 ARG A CB    1 
ATOM   11651 C  CG    . ARG A 1 2921 ? 233.724 241.831 192.418 1.00 0.58  ? 2921 ARG A CG    1 
ATOM   11652 C  CD    . ARG A 1 2921 ? 232.799 242.947 191.976 1.00 1.63  ? 2921 ARG A CD    1 
ATOM   11653 N  NE    . ARG A 1 2921 ? 233.514 244.012 191.283 1.00 2.53  ? 2921 ARG A NE    1 
ATOM   11654 C  CZ    . ARG A 1 2921 ? 232.954 245.135 190.860 1.00 1.94  ? 2921 ARG A CZ    1 
ATOM   11655 N  NH1   . ARG A 1 2921 ? 231.667 245.380 191.048 1.00 1.66  ? 2921 ARG A NH1   1 
ATOM   11656 N  NH2   . ARG A 1 2921 ? 233.704 246.042 190.240 1.00 2.44  ? 2921 ARG A NH2   1 
ATOM   11657 N  N     . ILE A 1 2922 ? 232.135 237.563 192.943 1.00 0.28  ? 2922 ILE A N     1 
ATOM   11658 C  CA    . ILE A 1 2922 ? 231.322 236.463 193.453 1.00 0.22  ? 2922 ILE A CA    1 
ATOM   11659 C  C     . ILE A 1 2922 ? 232.212 235.334 193.962 1.00 0.35  ? 2922 ILE A C     1 
ATOM   11660 O  O     . ILE A 1 2922 ? 231.901 234.688 194.969 1.00 0.58  ? 2922 ILE A O     1 
ATOM   11661 C  CB    . ILE A 1 2922 ? 230.344 235.978 192.366 1.00 0.17  ? 2922 ILE A CB    1 
ATOM   11662 C  CG1   . ILE A 1 2922 ? 229.392 237.107 191.964 1.00 0.15  ? 2922 ILE A CG1   1 
ATOM   11663 C  CG2   . ILE A 1 2922 ? 229.562 234.763 192.841 1.00 0.10  ? 2922 ILE A CG2   1 
ATOM   11664 C  CD1   . ILE A 1 2922 ? 228.530 236.783 190.769 1.00 0.30  ? 2922 ILE A CD1   1 
ATOM   11665 N  N     . ASP A 1 2923 ? 233.336 235.090 193.286 1.00 0.29  ? 2923 ASP A N     1 
ATOM   11666 C  CA    . ASP A 1 2923 ? 234.244 234.027 193.701 1.00 0.57  ? 2923 ASP A CA    1 
ATOM   11667 C  C     . ASP A 1 2923 ? 234.830 234.303 195.079 1.00 0.89  ? 2923 ASP A C     1 
ATOM   11668 O  O     . ASP A 1 2923 ? 235.058 233.375 195.862 1.00 2.29  ? 2923 ASP A O     1 
ATOM   11669 C  CB    . ASP A 1 2923 ? 235.354 233.859 192.664 1.00 0.57  ? 2923 ASP A CB    1 
ATOM   11670 C  CG    . ASP A 1 2923 ? 236.309 232.738 193.009 1.00 2.02  ? 2923 ASP A CG    1 
ATOM   11671 O  OD1   . ASP A 1 2923 ? 235.891 231.567 192.957 1.00 2.55  ? 2923 ASP A OD1   1 
ATOM   11672 O  OD2   . ASP A 1 2923 ? 237.477 233.026 193.335 1.00 7.67  ? 2923 ASP A OD2   1 
ATOM   11673 N  N     . ARG A 1 2924 ? 235.084 235.576 195.391 1.00 0.95  ? 2924 ARG A N     1 
ATOM   11674 C  CA    . ARG A 1 2924 ? 235.631 235.934 196.697 1.00 0.98  ? 2924 ARG A CA    1 
ATOM   11675 C  C     . ARG A 1 2924 ? 234.670 235.572 197.824 1.00 0.80  ? 2924 ARG A C     1 
ATOM   11676 O  O     . ARG A 1 2924 ? 235.081 235.030 198.856 1.00 3.18  ? 2924 ARG A O     1 
ATOM   11677 C  CB    . ARG A 1 2924 ? 235.957 237.424 196.725 1.00 0.70  ? 2924 ARG A CB    1 
ATOM   11678 C  CG    . ARG A 1 2924 ? 237.211 237.792 195.970 1.00 1.16  ? 2924 ARG A CG    1 
ATOM   11679 C  CD    . ARG A 1 2924 ? 237.440 239.289 195.973 1.00 1.72  ? 2924 ARG A CD    1 
ATOM   11680 N  NE    . ARG A 1 2924 ? 237.193 239.887 197.278 1.00 3.85  ? 2924 ARG A NE    1 
ATOM   11681 C  CZ    . ARG A 1 2924 ? 238.116 240.494 198.010 1.00 2.76  ? 2924 ARG A CZ    1 
ATOM   11682 N  NH1   . ARG A 1 2924 ? 239.381 240.542 197.626 1.00 2.37  ? 2924 ARG A NH1   1 
ATOM   11683 N  NH2   . ARG A 1 2924 ? 237.763 241.061 199.159 1.00 4.01  ? 2924 ARG A NH2   1 
ATOM   11684 N  N     . ILE A 1 2925 ? 233.382 235.863 197.640 1.00 0.90  ? 2925 ILE A N     1 
ATOM   11685 C  CA    . ILE A 1 2925 ? 232.408 235.653 198.707 1.00 1.27  ? 2925 ILE A CA    1 
ATOM   11686 C  C     . ILE A 1 2925 ? 232.162 234.165 198.940 1.00 0.87  ? 2925 ILE A C     1 
ATOM   11687 O  O     . ILE A 1 2925 ? 232.004 233.724 200.082 1.00 1.29  ? 2925 ILE A O     1 
ATOM   11688 C  CB    . ILE A 1 2925 ? 231.107 236.412 198.391 1.00 1.55  ? 2925 ILE A CB    1 
ATOM   11689 C  CG1   . ILE A 1 2925 ? 231.428 237.858 198.011 1.00 1.24  ? 2925 ILE A CG1   1 
ATOM   11690 C  CG2   . ILE A 1 2925 ? 230.162 236.376 199.573 1.00 0.29  ? 2925 ILE A CG2   1 
ATOM   11691 C  CD1   . ILE A 1 2925 ? 232.283 238.584 199.022 1.00 0.81  ? 2925 ILE A CD1   1 
ATOM   11692 N  N     . PHE A 1 2926 ? 232.125 233.368 197.869 1.00 1.69  ? 2926 PHE A N     1 
ATOM   11693 C  CA    . PHE A 1 2926 ? 231.962 231.926 198.017 1.00 1.22  ? 2926 PHE A CA    1 
ATOM   11694 C  C     . PHE A 1 2926 ? 233.132 231.255 198.723 1.00 2.33  ? 2926 PHE A C     1 
ATOM   11695 O  O     . PHE A 1 2926 ? 232.989 230.107 199.153 1.00 6.50  ? 2926 PHE A O     1 
ATOM   11696 C  CB    . PHE A 1 2926 ? 231.750 231.258 196.656 1.00 0.85  ? 2926 PHE A CB    1 
ATOM   11697 C  CG    . PHE A 1 2926 ? 230.416 231.544 196.036 1.00 0.57  ? 2926 PHE A CG    1 
ATOM   11698 C  CD1   . PHE A 1 2926 ? 229.386 232.083 196.787 1.00 0.38  ? 2926 PHE A CD1   1 
ATOM   11699 C  CD2   . PHE A 1 2926 ? 230.180 231.242 194.706 1.00 0.10  ? 2926 PHE A CD2   1 
ATOM   11700 C  CE1   . PHE A 1 2926 ? 228.156 232.330 196.219 1.00 0.33  ? 2926 PHE A CE1   1 
ATOM   11701 C  CE2   . PHE A 1 2926 ? 228.953 231.488 194.134 1.00 0.08  ? 2926 PHE A CE2   1 
ATOM   11702 C  CZ    . PHE A 1 2926 ? 227.939 232.030 194.891 1.00 0.13  ? 2926 PHE A CZ    1 
ATOM   11703 N  N     . ARG A 1 2927 ? 234.276 231.926 198.847 1.00 2.66  ? 2927 ARG A N     1 
ATOM   11704 C  CA    . ARG A 1 2927 ? 235.437 231.364 199.523 1.00 2.84  ? 2927 ARG A CA    1 
ATOM   11705 C  C     . ARG A 1 2927 ? 235.591 231.880 200.948 1.00 3.01  ? 2927 ARG A C     1 
ATOM   11706 O  O     . ARG A 1 2927 ? 236.615 231.616 201.584 1.00 6.76  ? 2927 ARG A O     1 
ATOM   11707 C  CB    . ARG A 1 2927 ? 236.704 231.649 198.712 1.00 3.53  ? 2927 ARG A CB    1 
ATOM   11708 C  CG    . ARG A 1 2927 ? 236.695 231.020 197.330 1.00 3.69  ? 2927 ARG A CG    1 
ATOM   11709 C  CD    . ARG A 1 2927 ? 238.015 231.224 196.608 1.00 4.17  ? 2927 ARG A CD    1 
ATOM   11710 N  NE    . ARG A 1 2927 ? 238.128 232.558 196.027 1.00 5.50  ? 2927 ARG A NE    1 
ATOM   11711 C  CZ    . ARG A 1 2927 ? 238.955 233.496 196.462 1.00 10.36 ? 2927 ARG A CZ    1 
ATOM   11712 N  NH1   . ARG A 1 2927 ? 239.764 233.282 197.488 1.00 8.89  ? 2927 ARG A NH1   1 
ATOM   11713 N  NH2   . ARG A 1 2927 ? 238.974 234.678 195.854 1.00 4.80  ? 2927 ARG A NH2   1 
ATOM   11714 N  N     . GLN A 1 2928 ? 234.597 232.603 201.465 1.00 3.77  ? 2928 GLN A N     1 
ATOM   11715 C  CA    . GLN A 1 2928 ? 234.589 233.103 202.829 1.00 3.28  ? 2928 GLN A CA    1 
ATOM   11716 C  C     . GLN A 1 2928 ? 233.513 232.397 203.646 1.00 1.99  ? 2928 GLN A C     1 
ATOM   11717 O  O     . GLN A 1 2928 ? 232.448 232.063 203.118 1.00 2.13  ? 2928 GLN A O     1 
ATOM   11718 C  CB    . GLN A 1 2928 ? 234.331 234.615 202.871 1.00 3.21  ? 2928 GLN A CB    1 
ATOM   11719 C  CG    . GLN A 1 2928 ? 235.507 235.479 202.447 1.00 4.56  ? 2928 GLN A CG    1 
ATOM   11720 C  CD    . GLN A 1 2928 ? 236.792 235.123 203.169 1.00 12.72 ? 2928 GLN A CD    1 
ATOM   11721 O  OE1   . GLN A 1 2928 ? 236.948 235.406 204.356 1.00 15.37 ? 2928 GLN A OE1   1 
ATOM   11722 N  NE2   . GLN A 1 2928 ? 237.722 234.508 202.451 1.00 11.04 ? 2928 GLN A NE2   1 
ATOM   11723 N  N     . PRO A 1 2929 ? 233.764 232.140 204.930 1.00 4.13  ? 2929 PRO A N     1 
ATOM   11724 C  CA    . PRO A 1 2929 ? 232.709 231.578 205.784 1.00 2.05  ? 2929 PRO A CA    1 
ATOM   11725 C  C     . PRO A 1 2929 ? 231.552 232.551 205.949 1.00 1.87  ? 2929 PRO A C     1 
ATOM   11726 O  O     . PRO A 1 2929 ? 231.741 233.764 206.053 1.00 3.28  ? 2929 PRO A O     1 
ATOM   11727 C  CB    . PRO A 1 2929 ? 233.429 231.327 207.115 1.00 3.38  ? 2929 PRO A CB    1 
ATOM   11728 C  CG    . PRO A 1 2929 ? 234.577 232.281 207.102 1.00 3.57  ? 2929 PRO A CG    1 
ATOM   11729 C  CD    . PRO A 1 2929 ? 235.021 232.345 205.669 1.00 4.51  ? 2929 PRO A CD    1 
ATOM   11730 N  N     . GLN A 1 2930 ? 230.340 231.994 205.991 1.00 2.74  ? 2930 GLN A N     1 
ATOM   11731 C  CA    . GLN A 1 2930 ? 229.103 232.780 205.974 1.00 2.29  ? 2930 GLN A CA    1 
ATOM   11732 C  C     . GLN A 1 2930 ? 229.122 233.804 204.844 1.00 1.64  ? 2930 GLN A C     1 
ATOM   11733 O  O     . GLN A 1 2930 ? 228.735 234.961 205.014 1.00 2.52  ? 2930 GLN A O     1 
ATOM   11734 C  CB    . GLN A 1 2930 ? 228.848 233.457 207.321 1.00 1.77  ? 2930 GLN A CB    1 
ATOM   11735 C  CG    . GLN A 1 2930 ? 228.002 232.631 208.268 1.00 4.30  ? 2930 GLN A CG    1 
ATOM   11736 C  CD    . GLN A 1 2930 ? 227.688 233.358 209.560 1.00 5.68  ? 2930 GLN A CD    1 
ATOM   11737 O  OE1   . GLN A 1 2930 ? 226.525 233.583 209.893 1.00 4.57  ? 2930 GLN A OE1   1 
ATOM   11738 N  NE2   . GLN A 1 2930 ? 228.727 233.727 210.297 1.00 3.84  ? 2930 GLN A NE2   1 
ATOM   11739 N  N     . GLY A 1 2931 ? 229.573 233.369 203.672 1.00 1.10  ? 2931 GLY A N     1 
ATOM   11740 C  CA    . GLY A 1 2931 ? 229.706 234.274 202.554 1.00 0.60  ? 2931 GLY A CA    1 
ATOM   11741 C  C     . GLY A 1 2931 ? 228.391 234.459 201.835 1.00 0.25  ? 2931 GLY A C     1 
ATOM   11742 O  O     . GLY A 1 2931 ? 227.987 233.624 201.024 1.00 0.14  ? 2931 GLY A O     1 
ATOM   11743 N  N     . HIS A 1 2932 ? 227.721 235.566 202.125 1.00 0.30  ? 2932 HIS A N     1 
ATOM   11744 C  CA    . HIS A 1 2932 ? 226.410 235.867 201.579 1.00 0.09  ? 2932 HIS A CA    1 
ATOM   11745 C  C     . HIS A 1 2932 ? 226.498 237.049 200.624 1.00 0.06  ? 2932 HIS A C     1 
ATOM   11746 O  O     . HIS A 1 2932 ? 227.258 237.995 200.838 1.00 0.19  ? 2932 HIS A O     1 
ATOM   11747 C  CB    . HIS A 1 2932 ? 225.414 236.159 202.699 1.00 0.22  ? 2932 HIS A CB    1 
ATOM   11748 C  CG    . HIS A 1 2932 ? 225.282 235.050 203.693 1.00 0.34  ? 2932 HIS A CG    1 
ATOM   11749 N  ND1   . HIS A 1 2932 ? 225.294 233.720 203.328 1.00 0.17  ? 2932 HIS A ND1   1 
ATOM   11750 C  CD2   . HIS A 1 2932 ? 225.157 235.069 205.039 1.00 0.49  ? 2932 HIS A CD2   1 
ATOM   11751 C  CE1   . HIS A 1 2932 ? 225.168 232.970 204.406 1.00 0.15  ? 2932 HIS A CE1   1 
ATOM   11752 N  NE2   . HIS A 1 2932 ? 225.083 233.763 205.458 1.00 0.33  ? 2932 HIS A NE2   1 
ATOM   11753 N  N     . LEU A 1 2933 ? 225.707 236.982 199.562 1.00 0.14  ? 2933 LEU A N     1 
ATOM   11754 C  CA    . LEU A 1 2933 ? 225.765 237.944 198.475 1.00 0.13  ? 2933 LEU A CA    1 
ATOM   11755 C  C     . LEU A 1 2933 ? 224.421 238.633 198.315 1.00 0.09  ? 2933 LEU A C     1 
ATOM   11756 O  O     . LEU A 1 2933 ? 223.372 237.987 198.360 1.00 0.14  ? 2933 LEU A O     1 
ATOM   11757 C  CB    . LEU A 1 2933 ? 226.153 237.259 197.165 1.00 0.12  ? 2933 LEU A CB    1 
ATOM   11758 C  CG    . LEU A 1 2933 ? 227.644 237.198 196.858 1.00 1.59  ? 2933 LEU A CG    1 
ATOM   11759 C  CD1   . LEU A 1 2933 ? 227.889 236.375 195.614 1.00 1.94  ? 2933 LEU A CD1   1 
ATOM   11760 C  CD2   . LEU A 1 2933 ? 228.191 238.598 196.691 1.00 1.92  ? 2933 LEU A CD2   1 
ATOM   11761 N  N     . LEU A 1 2934 ? 224.464 239.945 198.127 1.00 0.15  ? 2934 LEU A N     1 
ATOM   11762 C  CA    . LEU A 1 2934 ? 223.293 240.745 197.778 1.00 0.12  ? 2934 LEU A CA    1 
ATOM   11763 C  C     . LEU A 1 2934 ? 223.592 241.379 196.421 1.00 0.09  ? 2934 LEU A C     1 
ATOM   11764 O  O     . LEU A 1 2934 ? 224.211 242.442 196.339 1.00 0.08  ? 2934 LEU A O     1 
ATOM   11765 C  CB    . LEU A 1 2934 ? 222.985 241.792 198.850 1.00 0.18  ? 2934 LEU A CB    1 
ATOM   11766 C  CG    . LEU A 1 2934 ? 221.814 242.732 198.555 1.00 0.26  ? 2934 LEU A CG    1 
ATOM   11767 C  CD1   . LEU A 1 2934 ? 220.562 241.940 198.218 1.00 0.35  ? 2934 LEU A CD1   1 
ATOM   11768 C  CD2   . LEU A 1 2934 ? 221.563 243.668 199.725 1.00 0.72  ? 2934 LEU A CD2   1 
ATOM   11769 N  N     . LEU A 1 2935 ? 223.159 240.714 195.358 1.00 0.19  ? 2935 LEU A N     1 
ATOM   11770 C  CA    . LEU A 1 2935 ? 223.370 241.187 193.997 1.00 0.16  ? 2935 LEU A CA    1 
ATOM   11771 C  C     . LEU A 1 2935 ? 222.189 242.054 193.582 1.00 0.14  ? 2935 LEU A C     1 
ATOM   11772 O  O     . LEU A 1 2935 ? 221.057 241.570 193.503 1.00 0.41  ? 2935 LEU A O     1 
ATOM   11773 C  CB    . LEU A 1 2935 ? 223.534 240.009 193.038 1.00 0.34  ? 2935 LEU A CB    1 
ATOM   11774 C  CG    . LEU A 1 2935 ? 224.721 239.075 193.270 1.00 0.24  ? 2935 LEU A CG    1 
ATOM   11775 C  CD1   . LEU A 1 2935 ? 224.979 238.234 192.034 1.00 0.13  ? 2935 LEU A CD1   1 
ATOM   11776 C  CD2   . LEU A 1 2935 ? 225.966 239.852 193.665 1.00 0.30  ? 2935 LEU A CD2   1 
ATOM   11777 N  N     . ILE A 1 2936 ? 222.448 243.329 193.315 1.00 0.21  ? 2936 ILE A N     1 
ATOM   11778 C  CA    . ILE A 1 2936 ? 221.406 244.284 192.959 1.00 0.40  ? 2936 ILE A CA    1 
ATOM   11779 C  C     . ILE A 1 2936 ? 221.642 244.734 191.525 1.00 0.58  ? 2936 ILE A C     1 
ATOM   11780 O  O     . ILE A 1 2936 ? 222.730 245.213 191.186 1.00 0.74  ? 2936 ILE A O     1 
ATOM   11781 C  CB    . ILE A 1 2936 ? 221.373 245.479 193.920 1.00 0.80  ? 2936 ILE A CB    1 
ATOM   11782 C  CG1   . ILE A 1 2936 ? 221.226 244.988 195.363 1.00 0.55  ? 2936 ILE A CG1   1 
ATOM   11783 C  CG2   . ILE A 1 2936 ? 220.240 246.426 193.556 1.00 0.77  ? 2936 ILE A CG2   1 
ATOM   11784 C  CD1   . ILE A 1 2936 ? 221.195 246.092 196.384 1.00 0.84  ? 2936 ILE A CD1   1 
ATOM   11785 N  N     . GLY A 1 2937 ? 220.625 244.582 190.690 1.00 0.80  ? 2937 GLY A N     1 
ATOM   11786 C  CA    . GLY A 1 2937 ? 220.731 244.985 189.301 1.00 0.91  ? 2937 GLY A CA    1 
ATOM   11787 C  C     . GLY A 1 2937 ? 219.442 244.691 188.570 1.00 1.71  ? 2937 GLY A C     1 
ATOM   11788 O  O     . GLY A 1 2937 ? 218.534 244.039 189.095 1.00 5.37  ? 2937 GLY A O     1 
ATOM   11789 N  N     . VAL A 1 2938 ? 219.381 245.190 187.336 1.00 1.77  ? 2938 VAL A N     1 
ATOM   11790 C  CA    . VAL A 1 2938 ? 218.202 244.992 186.507 1.00 1.54  ? 2938 VAL A CA    1 
ATOM   11791 C  C     . VAL A 1 2938 ? 218.068 243.512 186.147 1.00 0.98  ? 2938 VAL A C     1 
ATOM   11792 O  O     . VAL A 1 2938 ? 219.059 242.780 186.041 1.00 1.86  ? 2938 VAL A O     1 
ATOM   11793 C  CB    . VAL A 1 2938 ? 218.294 245.873 185.248 1.00 1.66  ? 2938 VAL A CB    1 
ATOM   11794 C  CG1   . VAL A 1 2938 ? 217.024 245.781 184.412 1.00 1.88  ? 2938 VAL A CG1   1 
ATOM   11795 C  CG2   . VAL A 1 2938 ? 218.577 247.315 185.635 1.00 2.53  ? 2938 VAL A CG2   1 
ATOM   11796 N  N     . SER A 1 2939 ? 216.826 243.066 185.978 1.00 0.92  ? 2939 SER A N     1 
ATOM   11797 C  CA    . SER A 1 2939 ? 216.573 241.693 185.569 1.00 0.80  ? 2939 SER A CA    1 
ATOM   11798 C  C     . SER A 1 2939 ? 217.150 241.435 184.185 1.00 0.83  ? 2939 SER A C     1 
ATOM   11799 O  O     . SER A 1 2939 ? 217.160 242.317 183.323 1.00 1.95  ? 2939 SER A O     1 
ATOM   11800 C  CB    . SER A 1 2939 ? 215.074 241.403 185.575 1.00 2.39  ? 2939 SER A CB    1 
ATOM   11801 O  OG    . SER A 1 2939 ? 214.540 241.499 186.881 1.00 10.30 ? 2939 SER A OG    1 
ATOM   11802 N  N     . GLY A 1 2940 ? 217.642 240.218 183.977 1.00 0.76  ? 2940 GLY A N     1 
ATOM   11803 C  CA    . GLY A 1 2940 ? 218.232 239.862 182.704 1.00 0.73  ? 2940 GLY A CA    1 
ATOM   11804 C  C     . GLY A 1 2940 ? 219.655 240.320 182.512 1.00 0.96  ? 2940 GLY A C     1 
ATOM   11805 O  O     . GLY A 1 2940 ? 220.161 240.274 181.387 1.00 3.28  ? 2940 GLY A O     1 
ATOM   11806 N  N     . ALA A 1 2941 ? 220.320 240.764 183.574 1.00 0.80  ? 2941 ALA A N     1 
ATOM   11807 C  CA    . ALA A 1 2941 ? 221.705 241.197 183.503 1.00 0.59  ? 2941 ALA A CA    1 
ATOM   11808 C  C     . ALA A 1 2941 ? 222.689 240.079 183.811 1.00 1.06  ? 2941 ALA A C     1 
ATOM   11809 O  O     . ALA A 1 2941 ? 223.901 240.314 183.789 1.00 2.03  ? 2941 ALA A O     1 
ATOM   11810 C  CB    . ALA A 1 2941 ? 221.938 242.371 184.458 1.00 0.58  ? 2941 ALA A CB    1 
ATOM   11811 N  N     . GLY A 1 2942 ? 222.203 238.874 184.093 1.00 0.60  ? 2942 GLY A N     1 
ATOM   11812 C  CA    . GLY A 1 2942 ? 223.073 237.748 184.348 1.00 0.80  ? 2942 GLY A CA    1 
ATOM   11813 C  C     . GLY A 1 2942 ? 223.431 237.502 185.795 1.00 0.26  ? 2942 GLY A C     1 
ATOM   11814 O  O     . GLY A 1 2942 ? 224.377 236.754 186.057 1.00 0.40  ? 2942 GLY A O     1 
ATOM   11815 N  N     . LYS A 1 2943 ? 222.709 238.105 186.743 1.00 0.36  ? 2943 LYS A N     1 
ATOM   11816 C  CA    . LYS A 1 2943 ? 223.047 237.929 188.153 1.00 0.42  ? 2943 LYS A CA    1 
ATOM   11817 C  C     . LYS A 1 2943 ? 222.924 236.469 188.573 1.00 0.39  ? 2943 LYS A C     1 
ATOM   11818 O  O     . LYS A 1 2943 ? 223.812 235.925 189.235 1.00 0.27  ? 2943 LYS A O     1 
ATOM   11819 C  CB    . LYS A 1 2943 ? 222.154 238.815 189.023 1.00 0.26  ? 2943 LYS A CB    1 
ATOM   11820 C  CG    . LYS A 1 2943 ? 222.412 240.302 188.871 1.00 0.36  ? 2943 LYS A CG    1 
ATOM   11821 C  CD    . LYS A 1 2943 ? 221.581 241.117 189.852 1.00 0.32  ? 2943 LYS A CD    1 
ATOM   11822 C  CE    . LYS A 1 2943 ? 220.098 240.822 189.705 1.00 0.49  ? 2943 LYS A CE    1 
ATOM   11823 N  NZ    . LYS A 1 2943 ? 219.609 241.062 188.321 1.00 0.51  ? 2943 LYS A NZ    1 
ATOM   11824 N  N     . THR A 1 2944 ? 221.828 235.814 188.186 1.00 0.26  ? 2944 THR A N     1 
ATOM   11825 C  CA    . THR A 1 2944 ? 221.650 234.413 188.548 1.00 0.24  ? 2944 THR A CA    1 
ATOM   11826 C  C     . THR A 1 2944 ? 222.616 233.518 187.783 1.00 0.39  ? 2944 THR A C     1 
ATOM   11827 O  O     . THR A 1 2944 ? 223.212 232.602 188.363 1.00 0.35  ? 2944 THR A O     1 
ATOM   11828 C  CB    . THR A 1 2944 ? 220.208 233.978 188.294 1.00 0.45  ? 2944 THR A CB    1 
ATOM   11829 O  OG1   . THR A 1 2944 ? 219.312 234.931 188.876 1.00 0.65  ? 2944 THR A OG1   1 
ATOM   11830 C  CG2   . THR A 1 2944 ? 219.949 232.614 188.902 1.00 0.54  ? 2944 THR A CG2   1 
ATOM   11831 N  N     . THR A 1 2945 ? 222.782 233.765 186.483 1.00 0.42  ? 2945 THR A N     1 
ATOM   11832 C  CA    . THR A 1 2945 ? 223.625 232.902 185.663 1.00 0.21  ? 2945 THR A CA    1 
ATOM   11833 C  C     . THR A 1 2945 ? 225.080 232.965 186.108 1.00 0.19  ? 2945 THR A C     1 
ATOM   11834 O  O     . THR A 1 2945 ? 225.750 231.932 186.207 1.00 1.10  ? 2945 THR A O     1 
ATOM   11835 C  CB    . THR A 1 2945 ? 223.497 233.291 184.189 1.00 0.24  ? 2945 THR A CB    1 
ATOM   11836 O  OG1   . THR A 1 2945 ? 222.119 233.261 183.805 1.00 0.48  ? 2945 THR A OG1   1 
ATOM   11837 C  CG2   . THR A 1 2945 ? 224.279 232.328 183.317 1.00 0.12  ? 2945 THR A CG2   1 
ATOM   11838 N  N     . LEU A 1 2946 ? 225.586 234.168 186.384 1.00 0.14  ? 2946 LEU A N     1 
ATOM   11839 C  CA    . LEU A 1 2946 ? 226.959 234.292 186.853 1.00 0.12  ? 2946 LEU A CA    1 
ATOM   11840 C  C     . LEU A 1 2946 ? 227.137 233.632 188.213 1.00 0.09  ? 2946 LEU A C     1 
ATOM   11841 O  O     . LEU A 1 2946 ? 228.169 233.003 188.472 1.00 0.10  ? 2946 LEU A O     1 
ATOM   11842 C  CB    . LEU A 1 2946 ? 227.367 235.763 186.905 1.00 0.17  ? 2946 LEU A CB    1 
ATOM   11843 C  CG    . LEU A 1 2946 ? 227.593 236.440 185.553 1.00 0.16  ? 2946 LEU A CG    1 
ATOM   11844 C  CD1   . LEU A 1 2946 ? 228.240 237.799 185.740 1.00 0.23  ? 2946 LEU A CD1   1 
ATOM   11845 C  CD2   . LEU A 1 2946 ? 228.432 235.564 184.636 1.00 0.14  ? 2946 LEU A CD2   1 
ATOM   11846 N  N     . SER A 1 2947 ? 226.140 233.760 189.090 1.00 0.10  ? 2947 SER A N     1 
ATOM   11847 C  CA    . SER A 1 2947 ? 226.219 233.116 190.396 1.00 0.09  ? 2947 SER A CA    1 
ATOM   11848 C  C     . SER A 1 2947 ? 226.290 231.600 190.262 1.00 0.08  ? 2947 SER A C     1 
ATOM   11849 O  O     . SER A 1 2947 ? 227.079 230.948 190.954 1.00 0.07  ? 2947 SER A O     1 
ATOM   11850 C  CB    . SER A 1 2947 ? 225.024 233.526 191.257 1.00 0.10  ? 2947 SER A CB    1 
ATOM   11851 O  OG    . SER A 1 2947 ? 225.003 234.923 191.464 1.00 1.07  ? 2947 SER A OG    1 
ATOM   11852 N  N     . ARG A 1 2948 ? 225.475 231.023 189.377 1.00 0.09  ? 2948 ARG A N     1 
ATOM   11853 C  CA    . ARG A 1 2948 ? 225.536 229.582 189.154 1.00 0.12  ? 2948 ARG A CA    1 
ATOM   11854 C  C     . ARG A 1 2948 ? 226.868 229.175 188.540 1.00 0.10  ? 2948 ARG A C     1 
ATOM   11855 O  O     . ARG A 1 2948 ? 227.426 228.128 188.889 1.00 0.16  ? 2948 ARG A O     1 
ATOM   11856 C  CB    . ARG A 1 2948 ? 224.371 229.136 188.270 1.00 0.13  ? 2948 ARG A CB    1 
ATOM   11857 C  CG    . ARG A 1 2948 ? 223.011 229.360 188.896 1.00 0.78  ? 2948 ARG A CG    1 
ATOM   11858 C  CD    . ARG A 1 2948 ? 221.883 229.148 187.903 1.00 2.35  ? 2948 ARG A CD    1 
ATOM   11859 N  NE    . ARG A 1 2948 ? 221.742 227.751 187.515 1.00 4.41  ? 2948 ARG A NE    1 
ATOM   11860 C  CZ    . ARG A 1 2948 ? 220.719 227.268 186.823 1.00 6.08  ? 2948 ARG A CZ    1 
ATOM   11861 N  NH1   . ARG A 1 2948 ? 219.725 228.045 186.429 1.00 5.63  ? 2948 ARG A NH1   1 
ATOM   11862 N  NH2   . ARG A 1 2948 ? 220.691 225.973 186.522 1.00 5.53  ? 2948 ARG A NH2   1 
ATOM   11863 N  N     . PHE A 1 2949 ? 227.390 229.984 187.619 1.00 0.09  ? 2949 PHE A N     1 
ATOM   11864 C  CA    . PHE A 1 2949 ? 228.657 229.663 186.975 1.00 0.10  ? 2949 PHE A CA    1 
ATOM   11865 C  C     . PHE A 1 2949 ? 229.813 229.701 187.968 1.00 0.11  ? 2949 PHE A C     1 
ATOM   11866 O  O     . PHE A 1 2949 ? 230.684 228.825 187.948 1.00 0.19  ? 2949 PHE A O     1 
ATOM   11867 C  CB    . PHE A 1 2949 ? 228.899 230.624 185.811 1.00 0.08  ? 2949 PHE A CB    1 
ATOM   11868 C  CG    . PHE A 1 2949 ? 230.305 230.613 185.292 1.00 0.06  ? 2949 PHE A CG    1 
ATOM   11869 C  CD1   . PHE A 1 2949 ? 230.823 229.485 184.680 1.00 0.10  ? 2949 PHE A CD1   1 
ATOM   11870 C  CD2   . PHE A 1 2949 ? 231.106 231.734 185.405 1.00 0.07  ? 2949 PHE A CD2   1 
ATOM   11871 C  CE1   . PHE A 1 2949 ? 232.110 229.471 184.197 1.00 0.12  ? 2949 PHE A CE1   1 
ATOM   11872 C  CE2   . PHE A 1 2949 ? 232.400 231.728 184.923 1.00 0.16  ? 2949 PHE A CE2   1 
ATOM   11873 C  CZ    . PHE A 1 2949 ? 232.901 230.596 184.313 1.00 0.25  ? 2949 PHE A CZ    1 
ATOM   11874 N  N     . VAL A 1 2950 ? 229.846 230.715 188.833 1.00 0.12  ? 2950 VAL A N     1 
ATOM   11875 C  CA    . VAL A 1 2950 ? 230.889 230.783 189.851 1.00 0.13  ? 2950 VAL A CA    1 
ATOM   11876 C  C     . VAL A 1 2950 ? 230.687 229.690 190.895 1.00 0.08  ? 2950 VAL A C     1 
ATOM   11877 O  O     . VAL A 1 2950 ? 231.655 229.115 191.406 1.00 0.24  ? 2950 VAL A O     1 
ATOM   11878 C  CB    . VAL A 1 2950 ? 230.927 232.188 190.482 1.00 0.14  ? 2950 VAL A CB    1 
ATOM   11879 C  CG1   . VAL A 1 2950 ? 231.926 232.236 191.622 1.00 0.19  ? 2950 VAL A CG1   1 
ATOM   11880 C  CG2   . VAL A 1 2950 ? 231.284 233.222 189.432 1.00 0.09  ? 2950 VAL A CG2   1 
ATOM   11881 N  N     . ALA A 1 2951 ? 229.432 229.382 191.223 1.00 0.05  ? 2951 ALA A N     1 
ATOM   11882 C  CA    . ALA A 1 2951 ? 229.153 228.298 192.160 1.00 0.16  ? 2951 ALA A CA    1 
ATOM   11883 C  C     . ALA A 1 2951 ? 229.638 226.962 191.616 1.00 0.66  ? 2951 ALA A C     1 
ATOM   11884 O  O     . ALA A 1 2951 ? 230.124 226.114 192.373 1.00 1.10  ? 2951 ALA A O     1 
ATOM   11885 C  CB    . ALA A 1 2951 ? 227.659 228.240 192.471 1.00 0.15  ? 2951 ALA A CB    1 
ATOM   11886 N  N     . TRP A 1 2952 ? 229.506 226.753 190.305 1.00 0.51  ? 2952 TRP A N     1 
ATOM   11887 C  CA    . TRP A 1 2952 ? 230.003 225.526 189.695 1.00 0.39  ? 2952 TRP A CA    1 
ATOM   11888 C  C     . TRP A 1 2952 ? 231.526 225.499 189.651 1.00 0.68  ? 2952 TRP A C     1 
ATOM   11889 O  O     . TRP A 1 2952 ? 232.127 224.420 189.693 1.00 1.37  ? 2952 TRP A O     1 
ATOM   11890 C  CB    . TRP A 1 2952 ? 229.408 225.372 188.294 1.00 0.46  ? 2952 TRP A CB    1 
ATOM   11891 C  CG    . TRP A 1 2952 ? 230.102 224.379 187.413 1.00 1.07  ? 2952 TRP A CG    1 
ATOM   11892 C  CD1   . TRP A 1 2952 ? 229.855 223.042 187.336 1.00 1.04  ? 2952 TRP A CD1   1 
ATOM   11893 C  CD2   . TRP A 1 2952 ? 231.144 224.648 186.469 1.00 0.70  ? 2952 TRP A CD2   1 
ATOM   11894 N  NE1   . TRP A 1 2952 ? 230.683 222.461 186.410 1.00 0.95  ? 2952 TRP A NE1   1 
ATOM   11895 C  CE2   . TRP A 1 2952 ? 231.484 223.425 185.863 1.00 0.76  ? 2952 TRP A CE2   1 
ATOM   11896 C  CE3   . TRP A 1 2952 ? 231.826 225.806 186.082 1.00 0.70  ? 2952 TRP A CE3   1 
ATOM   11897 C  CZ2   . TRP A 1 2952 ? 232.475 223.324 184.890 1.00 1.67  ? 2952 TRP A CZ2   1 
ATOM   11898 C  CZ3   . TRP A 1 2952 ? 232.810 225.704 185.118 1.00 1.17  ? 2952 TRP A CZ3   1 
ATOM   11899 C  CH2   . TRP A 1 2952 ? 233.125 224.473 184.533 1.00 1.71  ? 2952 TRP A CH2   1 
ATOM   11900 N  N     . MET A 1 2953 ? 232.163 226.671 189.580 1.00 0.65  ? 2953 MET A N     1 
ATOM   11901 C  CA    . MET A 1 2953 ? 233.621 226.728 189.578 1.00 0.73  ? 2953 MET A CA    1 
ATOM   11902 C  C     . MET A 1 2953 ? 234.205 226.460 190.958 1.00 1.70  ? 2953 MET A C     1 
ATOM   11903 O  O     . MET A 1 2953 ? 235.342 225.991 191.070 1.00 6.84  ? 2953 MET A O     1 
ATOM   11904 C  CB    . MET A 1 2953 ? 234.096 228.088 189.071 1.00 1.83  ? 2953 MET A CB    1 
ATOM   11905 C  CG    . MET A 1 2953 ? 233.963 228.286 187.572 1.00 2.13  ? 2953 MET A CG    1 
ATOM   11906 S  SD    . MET A 1 2953 ? 234.633 229.875 187.067 1.00 24.58 ? 2953 MET A SD    1 
ATOM   11907 C  CE    . MET A 1 2953 ? 236.384 229.501 187.034 1.00 2.47  ? 2953 MET A CE    1 
ATOM   11908 N  N     . ASN A 1 2954 ? 233.459 226.762 192.017 1.00 2.17  ? 2954 ASN A N     1 
ATOM   11909 C  CA    . ASN A 1 2954 ? 233.930 226.585 193.383 1.00 1.86  ? 2954 ASN A CA    1 
ATOM   11910 C  C     . ASN A 1 2954 ? 233.416 225.301 194.020 1.00 3.38  ? 2954 ASN A C     1 
ATOM   11911 O  O     . ASN A 1 2954 ? 233.620 225.094 195.220 1.00 9.62  ? 2954 ASN A O     1 
ATOM   11912 C  CB    . ASN A 1 2954 ? 233.532 227.791 194.233 1.00 1.39  ? 2954 ASN A CB    1 
ATOM   11913 C  CG    . ASN A 1 2954 ? 234.362 229.016 193.924 1.00 2.82  ? 2954 ASN A CG    1 
ATOM   11914 O  OD1   . ASN A 1 2954 ? 235.563 229.045 194.181 1.00 6.79  ? 2954 ASN A OD1   1 
ATOM   11915 N  ND2   . ASN A 1 2954 ? 233.728 230.032 193.358 1.00 3.26  ? 2954 ASN A ND2   1 
ATOM   11916 N  N     . GLY A 1 2955 ? 232.757 224.437 193.251 1.00 1.98  ? 2955 GLY A N     1 
ATOM   11917 C  CA    . GLY A 1 2955 ? 232.235 223.198 193.780 1.00 0.64  ? 2955 GLY A CA    1 
ATOM   11918 C  C     . GLY A 1 2955 ? 230.976 223.330 194.601 1.00 0.90  ? 2955 GLY A C     1 
ATOM   11919 O  O     . GLY A 1 2955 ? 230.613 222.382 195.308 1.00 2.26  ? 2955 GLY A O     1 
ATOM   11920 N  N     . LEU A 1 2956 ? 230.297 224.469 194.535 1.00 2.17  ? 2956 LEU A N     1 
ATOM   11921 C  CA    . LEU A 1 2956 ? 229.085 224.699 195.306 1.00 0.60  ? 2956 LEU A CA    1 
ATOM   11922 C  C     . LEU A 1 2956 ? 227.874 224.223 194.518 1.00 1.12  ? 2956 LEU A C     1 
ATOM   11923 O  O     . LEU A 1 2956 ? 227.730 224.542 193.334 1.00 4.07  ? 2956 LEU A O     1 
ATOM   11924 C  CB    . LEU A 1 2956 ? 228.930 226.182 195.653 1.00 0.84  ? 2956 LEU A CB    1 
ATOM   11925 C  CG    . LEU A 1 2956 ? 229.632 226.755 196.888 1.00 0.72  ? 2956 LEU A CG    1 
ATOM   11926 C  CD1   . LEU A 1 2956 ? 231.131 226.520 196.853 1.00 1.39  ? 2956 LEU A CD1   1 
ATOM   11927 C  CD2   . LEU A 1 2956 ? 229.324 228.240 197.031 1.00 0.22  ? 2956 LEU A CD2   1 
ATOM   11928 N  N     . SER A 1 2957 ? 227.012 223.456 195.173 1.00 1.00  ? 2957 SER A N     1 
ATOM   11929 C  CA    . SER A 1 2957 ? 225.741 223.081 194.578 1.00 0.68  ? 2957 SER A CA    1 
ATOM   11930 C  C     . SER A 1 2957 ? 224.794 224.271 194.595 1.00 0.78  ? 2957 SER A C     1 
ATOM   11931 O  O     . SER A 1 2957 ? 224.767 225.049 195.552 1.00 0.97  ? 2957 SER A O     1 
ATOM   11932 C  CB    . SER A 1 2957 ? 225.125 221.902 195.327 1.00 2.06  ? 2957 SER A CB    1 
ATOM   11933 O  OG    . SER A 1 2957 ? 225.988 220.780 195.300 1.00 13.59 ? 2957 SER A OG    1 
ATOM   11934 N  N     . VAL A 1 2958 ? 224.023 224.419 193.528 1.00 2.21  ? 2958 VAL A N     1 
ATOM   11935 C  CA    . VAL A 1 2958 ? 223.074 225.515 193.400 1.00 1.22  ? 2958 VAL A CA    1 
ATOM   11936 C  C     . VAL A 1 2958 ? 221.709 225.009 193.836 1.00 1.15  ? 2958 VAL A C     1 
ATOM   11937 O  O     . VAL A 1 2958 ? 221.197 224.026 193.291 1.00 1.62  ? 2958 VAL A O     1 
ATOM   11938 C  CB    . VAL A 1 2958 ? 223.027 226.060 191.965 1.00 0.74  ? 2958 VAL A CB    1 
ATOM   11939 C  CG1   . VAL A 1 2958 ? 221.806 226.942 191.779 1.00 0.73  ? 2958 VAL A CG1   1 
ATOM   11940 C  CG2   . VAL A 1 2958 ? 224.294 226.828 191.649 1.00 0.64  ? 2958 VAL A CG2   1 
ATOM   11941 N  N     . TYR A 1 2959 ? 221.122 225.671 194.827 1.00 1.51  ? 2959 TYR A N     1 
ATOM   11942 C  CA    . TYR A 1 2959 ? 219.757 225.403 195.250 1.00 0.87  ? 2959 TYR A CA    1 
ATOM   11943 C  C     . TYR A 1 2959 ? 218.902 226.629 194.972 1.00 0.81  ? 2959 TYR A C     1 
ATOM   11944 O  O     . TYR A 1 2959 ? 219.233 227.736 195.408 1.00 1.00  ? 2959 TYR A O     1 
ATOM   11945 C  CB    . TYR A 1 2959 ? 219.682 225.038 196.734 1.00 0.80  ? 2959 TYR A CB    1 
ATOM   11946 C  CG    . TYR A 1 2959 ? 218.332 224.496 197.143 1.00 2.04  ? 2959 TYR A CG    1 
ATOM   11947 C  CD1   . TYR A 1 2959 ? 217.275 225.352 197.429 1.00 2.10  ? 2959 TYR A CD1   1 
ATOM   11948 C  CD2   . TYR A 1 2959 ? 218.109 223.129 197.234 1.00 2.06  ? 2959 TYR A CD2   1 
ATOM   11949 C  CE1   . TYR A 1 2959 ? 216.041 224.864 197.793 1.00 2.67  ? 2959 TYR A CE1   1 
ATOM   11950 C  CE2   . TYR A 1 2959 ? 216.878 222.633 197.602 1.00 3.13  ? 2959 TYR A CE2   1 
ATOM   11951 C  CZ    . TYR A 1 2959 ? 215.846 223.505 197.881 1.00 5.14  ? 2959 TYR A CZ    1 
ATOM   11952 O  OH    . TYR A 1 2959 ? 214.615 223.017 198.248 1.00 7.36  ? 2959 TYR A OH    1 
ATOM   11953 N  N     . GLN A 1 2960 ? 217.809 226.425 194.248 1.00 0.65  ? 2960 GLN A N     1 
ATOM   11954 C  CA    . GLN A 1 2960 ? 216.805 227.452 194.025 1.00 1.59  ? 2960 GLN A CA    1 
ATOM   11955 C  C     . GLN A 1 2960 ? 215.447 226.892 194.410 1.00 2.67  ? 2960 GLN A C     1 
ATOM   11956 O  O     . GLN A 1 2960 ? 215.101 225.769 194.030 1.00 7.48  ? 2960 GLN A O     1 
ATOM   11957 C  CB    . GLN A 1 2960 ? 216.792 227.922 192.562 1.00 1.23  ? 2960 GLN A CB    1 
ATOM   11958 C  CG    . GLN A 1 2960 ? 218.100 228.533 192.094 1.00 1.60  ? 2960 GLN A CG    1 
ATOM   11959 C  CD    . GLN A 1 2960 ? 218.058 228.965 190.642 1.00 4.05  ? 2960 GLN A CD    1 
ATOM   11960 O  OE1   . GLN A 1 2960 ? 217.287 229.847 190.265 1.00 4.46  ? 2960 GLN A OE1   1 
ATOM   11961 N  NE2   . GLN A 1 2960 ? 218.891 228.345 189.817 1.00 7.36  ? 2960 GLN A NE2   1 
ATOM   11962 N  N     . ILE A 1 2961 ? 214.685 227.665 195.182 1.00 1.82  ? 2961 ILE A N     1 
ATOM   11963 C  CA    . ILE A 1 2961 ? 213.343 227.236 195.551 1.00 3.17  ? 2961 ILE A CA    1 
ATOM   11964 C  C     . ILE A 1 2961 ? 212.443 227.305 194.326 1.00 6.95  ? 2961 ILE A C     1 
ATOM   11965 O  O     . ILE A 1 2961 ? 212.545 228.226 193.504 1.00 8.20  ? 2961 ILE A O     1 
ATOM   11966 C  CB    . ILE A 1 2961 ? 212.807 228.067 196.727 1.00 2.31  ? 2961 ILE A CB    1 
ATOM   11967 C  CG1   . ILE A 1 2961 ? 212.380 229.467 196.287 1.00 3.30  ? 2961 ILE A CG1   1 
ATOM   11968 C  CG2   . ILE A 1 2961 ? 213.828 228.128 197.847 1.00 5.17  ? 2961 ILE A CG2   1 
ATOM   11969 C  CD1   . ILE A 1 2961 ? 211.712 230.261 197.382 1.00 6.55  ? 2961 ILE A CD1   1 
ATOM   11970 N  N     . LYS A 1 2962 ? 211.584 226.299 194.175 1.00 9.74  ? 2962 LYS A N     1 
ATOM   11971 C  CA    . LYS A 1 2962 ? 210.795 226.126 192.959 1.00 6.00  ? 2962 LYS A CA    1 
ATOM   11972 C  C     . LYS A 1 2962 ? 209.390 226.675 193.206 1.00 7.85  ? 2962 LYS A C     1 
ATOM   11973 O  O     . LYS A 1 2962 ? 208.420 225.945 193.424 1.00 7.96  ? 2962 LYS A O     1 
ATOM   11974 C  CB    . LYS A 1 2962 ? 210.775 224.660 192.557 1.00 8.61  ? 2962 LYS A CB    1 
ATOM   11975 C  CG    . LYS A 1 2962 ? 212.162 224.115 192.265 1.00 12.72 ? 2962 LYS A CG    1 
ATOM   11976 C  CD    . LYS A 1 2962 ? 212.768 224.710 191.010 1.00 20.05 ? 2962 LYS A CD    1 
ATOM   11977 C  CE    . LYS A 1 2962 ? 214.160 224.148 190.764 1.00 13.94 ? 2962 LYS A CE    1 
ATOM   11978 N  NZ    . LYS A 1 2962 ? 214.136 222.705 190.410 1.00 18.64 ? 2962 LYS A NZ    1 
ATOM   11979 N  N     . VAL A 1 2963 ? 209.297 228.005 193.175 1.00 6.45  ? 2963 VAL A N     1 
ATOM   11980 C  CA    . VAL A 1 2963 ? 208.039 228.658 193.513 1.00 7.88  ? 2963 VAL A CA    1 
ATOM   11981 C  C     . VAL A 1 2963 ? 207.005 228.428 192.418 1.00 10.38 ? 2963 VAL A C     1 
ATOM   11982 O  O     . VAL A 1 2963 ? 207.318 228.133 191.258 1.00 6.99  ? 2963 VAL A O     1 
ATOM   11983 C  CB    . VAL A 1 2963 ? 208.237 230.160 193.772 1.00 7.60  ? 2963 VAL A CB    1 
ATOM   11984 C  CG1   . VAL A 1 2963 ? 209.156 230.378 194.947 1.00 8.34  ? 2963 VAL A CG1   1 
ATOM   11985 C  CG2   . VAL A 1 2963 ? 208.791 230.839 192.531 1.00 12.73 ? 2963 VAL A CG2   1 
ATOM   11986 N  N     . HIS A 1 2964 ? 205.745 228.567 192.811 1.00 10.48 ? 2964 HIS A N     1 
ATOM   11987 C  CA    . HIS A 1 2964 ? 204.612 228.503 191.908 1.00 9.07  ? 2964 HIS A CA    1 
ATOM   11988 C  C     . HIS A 1 2964 ? 203.485 229.309 192.540 1.00 11.30 ? 2964 HIS A C     1 
ATOM   11989 O  O     . HIS A 1 2964 ? 203.659 229.931 193.591 1.00 13.95 ? 2964 HIS A O     1 
ATOM   11990 C  CB    . HIS A 1 2964 ? 204.220 227.050 191.616 1.00 9.12  ? 2964 HIS A CB    1 
ATOM   11991 C  CG    . HIS A 1 2964 ? 204.074 226.201 192.840 1.00 9.95  ? 2964 HIS A CG    1 
ATOM   11992 N  ND1   . HIS A 1 2964 ? 202.877 226.049 193.505 1.00 11.45 ? 2964 HIS A ND1   1 
ATOM   11993 C  CD2   . HIS A 1 2964 ? 204.976 225.446 193.511 1.00 8.34  ? 2964 HIS A CD2   1 
ATOM   11994 C  CE1   . HIS A 1 2964 ? 203.050 225.244 194.538 1.00 8.64  ? 2964 HIS A CE1   1 
ATOM   11995 N  NE2   . HIS A 1 2964 ? 204.313 224.864 194.563 1.00 8.94  ? 2964 HIS A NE2   1 
ATOM   11996 N  N     . ARG A 1 2965 ? 202.323 229.307 191.886 1.00 14.19 ? 2965 ARG A N     1 
ATOM   11997 C  CA    . ARG A 1 2965 ? 201.210 230.107 192.383 1.00 16.14 ? 2965 ARG A CA    1 
ATOM   11998 C  C     . ARG A 1 2965 ? 200.713 229.632 193.742 1.00 11.40 ? 2965 ARG A C     1 
ATOM   11999 O  O     . ARG A 1 2965 ? 200.143 230.426 194.495 1.00 12.28 ? 2965 ARG A O     1 
ATOM   12000 C  CB    . ARG A 1 2965 ? 200.057 230.093 191.382 1.00 15.84 ? 2965 ARG A CB    1 
ATOM   12001 C  CG    . ARG A 1 2965 ? 199.608 228.702 190.972 1.00 19.25 ? 2965 ARG A CG    1 
ATOM   12002 C  CD    . ARG A 1 2965 ? 198.456 228.793 189.995 1.00 25.91 ? 2965 ARG A CD    1 
ATOM   12003 N  NE    . ARG A 1 2965 ? 197.367 229.586 190.551 1.00 21.13 ? 2965 ARG A NE    1 
ATOM   12004 C  CZ    . ARG A 1 2965 ? 196.937 230.728 190.035 1.00 25.01 ? 2965 ARG A CZ    1 
ATOM   12005 N  NH1   . ARG A 1 2965 ? 197.485 231.243 188.945 1.00 24.37 ? 2965 ARG A NH1   1 
ATOM   12006 N  NH2   . ARG A 1 2965 ? 195.941 231.376 190.631 1.00 22.57 ? 2965 ARG A NH2   1 
ATOM   12007 N  N     . LYS A 1 2966 ? 200.919 228.358 194.074 1.00 11.96 ? 2966 LYS A N     1 
ATOM   12008 C  CA    . LYS A 1 2966 ? 200.457 227.790 195.334 1.00 13.29 ? 2966 LYS A CA    1 
ATOM   12009 C  C     . LYS A 1 2966 ? 201.587 227.578 196.335 1.00 13.92 ? 2966 LYS A C     1 
ATOM   12010 O  O     . LYS A 1 2966 ? 201.399 226.860 197.323 1.00 15.53 ? 2966 LYS A O     1 
ATOM   12011 C  CB    . LYS A 1 2966 ? 199.727 226.471 195.080 1.00 11.67 ? 2966 LYS A CB    1 
ATOM   12012 C  CG    . LYS A 1 2966 ? 198.482 226.554 194.188 1.00 14.13 ? 2966 LYS A CG    1 
ATOM   12013 C  CD    . LYS A 1 2966 ? 197.289 227.250 194.852 1.00 14.24 ? 2966 LYS A CD    1 
ATOM   12014 C  CE    . LYS A 1 2966 ? 197.214 228.739 194.531 1.00 22.43 ? 2966 LYS A CE    1 
ATOM   12015 N  NZ    . LYS A 1 2966 ? 195.986 229.364 195.100 1.00 26.74 ? 2966 LYS A NZ    1 
ATOM   12016 N  N     . TYR A 1 2967 ? 202.754 228.172 196.102 1.00 14.54 ? 2967 TYR A N     1 
ATOM   12017 C  CA    . TYR A 1 2967 ? 203.878 228.023 197.019 1.00 7.91  ? 2967 TYR A CA    1 
ATOM   12018 C  C     . TYR A 1 2967 ? 203.662 228.900 198.248 1.00 9.41  ? 2967 TYR A C     1 
ATOM   12019 O  O     . TYR A 1 2967 ? 203.489 230.116 198.133 1.00 9.78  ? 2967 TYR A O     1 
ATOM   12020 C  CB    . TYR A 1 2967 ? 205.175 228.399 196.307 1.00 6.96  ? 2967 TYR A CB    1 
ATOM   12021 C  CG    . TYR A 1 2967 ? 206.443 228.032 197.039 1.00 6.30  ? 2967 TYR A CG    1 
ATOM   12022 C  CD1   . TYR A 1 2967 ? 207.009 228.896 197.968 1.00 3.67  ? 2967 TYR A CD1   1 
ATOM   12023 C  CD2   . TYR A 1 2967 ? 207.091 226.832 196.780 1.00 4.79  ? 2967 TYR A CD2   1 
ATOM   12024 C  CE1   . TYR A 1 2967 ? 208.176 228.568 198.627 1.00 4.12  ? 2967 TYR A CE1   1 
ATOM   12025 C  CE2   . TYR A 1 2967 ? 208.257 226.495 197.433 1.00 4.61  ? 2967 TYR A CE2   1 
ATOM   12026 C  CZ    . TYR A 1 2967 ? 208.795 227.366 198.356 1.00 3.05  ? 2967 TYR A CZ    1 
ATOM   12027 O  OH    . TYR A 1 2967 ? 209.956 227.028 199.004 1.00 2.28  ? 2967 TYR A OH    1 
ATOM   12028 N  N     . THR A 1 2968 ? 203.670 228.283 199.428 1.00 11.71 ? 2968 THR A N     1 
ATOM   12029 C  CA    . THR A 1 2968 ? 203.303 228.959 200.665 1.00 12.46 ? 2968 THR A CA    1 
ATOM   12030 C  C     . THR A 1 2968 ? 204.462 228.932 201.656 1.00 7.81  ? 2968 THR A C     1 
ATOM   12031 O  O     . THR A 1 2968 ? 205.576 228.504 201.338 1.00 5.40  ? 2968 THR A O     1 
ATOM   12032 C  CB    . THR A 1 2968 ? 202.051 228.328 201.287 1.00 12.70 ? 2968 THR A CB    1 
ATOM   12033 O  OG1   . THR A 1 2968 ? 202.388 227.051 201.839 1.00 15.79 ? 2968 THR A OG1   1 
ATOM   12034 C  CG2   . THR A 1 2968 ? 200.956 228.164 200.249 1.00 9.53  ? 2968 THR A CG2   1 
ATOM   12035 N  N     . GLY A 1 2969 ? 204.180 229.406 202.872 1.00 10.22 ? 2969 GLY A N     1 
ATOM   12036 C  CA    . GLY A 1 2969 ? 205.226 229.552 203.871 1.00 5.06  ? 2969 GLY A CA    1 
ATOM   12037 C  C     . GLY A 1 2969 ? 205.794 228.230 204.349 1.00 8.75  ? 2969 GLY A C     1 
ATOM   12038 O  O     . GLY A 1 2969 ? 207.003 228.105 204.558 1.00 14.85 ? 2969 GLY A O     1 
ATOM   12039 N  N     . GLU A 1 2970 ? 204.934 227.228 204.546 1.00 9.14  ? 2970 GLU A N     1 
ATOM   12040 C  CA    . GLU A 1 2970 ? 205.431 225.931 204.992 1.00 7.41  ? 2970 GLU A CA    1 
ATOM   12041 C  C     . GLU A 1 2970 ? 206.124 225.182 203.860 1.00 8.50  ? 2970 GLU A C     1 
ATOM   12042 O  O     . GLU A 1 2970 ? 206.915 224.264 204.107 1.00 9.51  ? 2970 GLU A O     1 
ATOM   12043 C  CB    . GLU A 1 2970 ? 204.303 225.100 205.612 1.00 8.53  ? 2970 GLU A CB    1 
ATOM   12044 C  CG    . GLU A 1 2970 ? 203.227 224.608 204.667 1.00 14.23 ? 2970 GLU A CG    1 
ATOM   12045 C  CD    . GLU A 1 2970 ? 202.131 225.634 204.438 1.00 24.13 ? 2970 GLU A CD    1 
ATOM   12046 O  OE1   . GLU A 1 2970 ? 202.338 226.824 204.760 1.00 18.74 ? 2970 GLU A OE1   1 
ATOM   12047 O  OE2   . GLU A 1 2970 ? 201.052 225.246 203.941 1.00 26.04 ? 2970 GLU A OE2   1 
ATOM   12048 N  N     . ASP A 1 2971 ? 205.840 225.552 202.608 1.00 10.01 ? 2971 ASP A N     1 
ATOM   12049 C  CA    . ASP A 1 2971 ? 206.670 225.079 201.504 1.00 8.49  ? 2971 ASP A CA    1 
ATOM   12050 C  C     . ASP A 1 2971 ? 208.076 225.658 201.592 1.00 4.90  ? 2971 ASP A C     1 
ATOM   12051 O  O     . ASP A 1 2971 ? 209.062 224.962 201.325 1.00 5.63  ? 2971 ASP A O     1 
ATOM   12052 C  CB    . ASP A 1 2971 ? 206.031 225.434 200.162 1.00 7.13  ? 2971 ASP A CB    1 
ATOM   12053 C  CG    . ASP A 1 2971 ? 204.651 224.841 200.001 1.00 14.11 ? 2971 ASP A CG    1 
ATOM   12054 O  OD1   . ASP A 1 2971 ? 203.770 225.146 200.830 1.00 20.29 ? 2971 ASP A OD1   1 
ATOM   12055 O  OD2   . ASP A 1 2971 ? 204.450 224.066 199.043 1.00 19.08 ? 2971 ASP A OD2   1 
ATOM   12056 N  N     . PHE A 1 2972 ? 208.183 226.937 201.955 1.00 3.81  ? 2972 PHE A N     1 
ATOM   12057 C  CA    . PHE A 1 2972 ? 209.493 227.553 202.129 1.00 2.66  ? 2972 PHE A CA    1 
ATOM   12058 C  C     . PHE A 1 2972 ? 210.224 226.958 203.325 1.00 2.95  ? 2972 PHE A C     1 
ATOM   12059 O  O     . PHE A 1 2972 ? 211.447 226.784 203.286 1.00 1.97  ? 2972 PHE A O     1 
ATOM   12060 C  CB    . PHE A 1 2972 ? 209.340 229.066 202.278 1.00 3.15  ? 2972 PHE A CB    1 
ATOM   12061 C  CG    . PHE A 1 2972 ? 210.641 229.813 202.270 1.00 3.16  ? 2972 PHE A CG    1 
ATOM   12062 C  CD1   . PHE A 1 2972 ? 211.442 229.825 201.141 1.00 2.89  ? 2972 PHE A CD1   1 
ATOM   12063 C  CD2   . PHE A 1 2972 ? 211.061 230.516 203.386 1.00 2.47  ? 2972 PHE A CD2   1 
ATOM   12064 C  CE1   . PHE A 1 2972 ? 212.639 230.514 201.130 1.00 2.33  ? 2972 PHE A CE1   1 
ATOM   12065 C  CE2   . PHE A 1 2972 ? 212.254 231.204 203.379 1.00 1.98  ? 2972 PHE A CE2   1 
ATOM   12066 C  CZ    . PHE A 1 2972 ? 213.044 231.203 202.249 1.00 1.83  ? 2972 PHE A CZ    1 
ATOM   12067 N  N     . ASP A 1 2973 ? 209.492 226.644 204.398 1.00 4.80  ? 2973 ASP A N     1 
ATOM   12068 C  CA    . ASP A 1 2973 ? 210.113 226.034 205.568 1.00 3.06  ? 2973 ASP A CA    1 
ATOM   12069 C  C     . ASP A 1 2973 ? 210.657 224.648 205.251 1.00 2.19  ? 2973 ASP A C     1 
ATOM   12070 O  O     . ASP A 1 2973 ? 211.761 224.294 205.682 1.00 1.86  ? 2973 ASP A O     1 
ATOM   12071 C  CB    . ASP A 1 2973 ? 209.109 225.969 206.718 1.00 4.72  ? 2973 ASP A CB    1 
ATOM   12072 C  CG    . ASP A 1 2973 ? 209.017 227.269 207.488 1.00 11.09 ? 2973 ASP A CG    1 
ATOM   12073 O  OD1   . ASP A 1 2973 ? 209.718 228.231 207.115 1.00 16.70 ? 2973 ASP A OD1   1 
ATOM   12074 O  OD2   . ASP A 1 2973 ? 208.247 227.331 208.467 1.00 12.80 ? 2973 ASP A OD2   1 
ATOM   12075 N  N     . GLU A 1 2974 ? 209.895 223.845 204.506 1.00 2.57  ? 2974 GLU A N     1 
ATOM   12076 C  CA    . GLU A 1 2974 ? 210.388 222.535 204.097 1.00 4.55  ? 2974 GLU A CA    1 
ATOM   12077 C  C     . GLU A 1 2974 ? 211.583 222.665 203.163 1.00 5.37  ? 2974 GLU A C     1 
ATOM   12078 O  O     . GLU A 1 2974 ? 212.533 221.878 203.246 1.00 3.23  ? 2974 GLU A O     1 
ATOM   12079 C  CB    . GLU A 1 2974 ? 209.265 221.730 203.444 1.00 4.00  ? 2974 GLU A CB    1 
ATOM   12080 C  CG    . GLU A 1 2974 ? 209.673 220.327 203.020 1.00 10.34 ? 2974 GLU A CG    1 
ATOM   12081 C  CD    . GLU A 1 2974 ? 210.038 219.433 204.192 1.00 20.29 ? 2974 GLU A CD    1 
ATOM   12082 O  OE1   . GLU A 1 2974 ? 209.545 219.673 205.314 1.00 18.86 ? 2974 GLU A OE1   1 
ATOM   12083 O  OE2   . GLU A 1 2974 ? 210.830 218.488 203.991 1.00 22.19 ? 2974 GLU A OE2   1 
ATOM   12084 N  N     . ASP A 1 2975 ? 211.553 223.654 202.266 1.00 3.29  ? 2975 ASP A N     1 
ATOM   12085 C  CA    . ASP A 1 2975 ? 212.705 223.906 201.408 1.00 2.52  ? 2975 ASP A CA    1 
ATOM   12086 C  C     . ASP A 1 2975 ? 213.913 224.345 202.226 1.00 1.89  ? 2975 ASP A C     1 
ATOM   12087 O  O     . ASP A 1 2975 ? 215.046 223.949 201.935 1.00 2.80  ? 2975 ASP A O     1 
ATOM   12088 C  CB    . ASP A 1 2975 ? 212.355 224.954 200.353 1.00 2.75  ? 2975 ASP A CB    1 
ATOM   12089 C  CG    . ASP A 1 2975 ? 211.691 224.351 199.134 1.00 8.35  ? 2975 ASP A CG    1 
ATOM   12090 O  OD1   . ASP A 1 2975 ? 211.741 223.114 198.979 1.00 15.00 ? 2975 ASP A OD1   1 
ATOM   12091 O  OD2   . ASP A 1 2975 ? 211.111 225.111 198.331 1.00 8.17  ? 2975 ASP A OD2   1 
ATOM   12092 N  N     . LEU A 1 2976 ? 213.689 225.163 203.258 1.00 1.69  ? 2976 LEU A N     1 
ATOM   12093 C  CA    . LEU A 1 2976 ? 214.781 225.554 204.145 1.00 1.05  ? 2976 LEU A CA    1 
ATOM   12094 C  C     . LEU A 1 2976 ? 215.368 224.348 204.864 1.00 1.17  ? 2976 LEU A C     1 
ATOM   12095 O  O     . LEU A 1 2976 ? 216.588 224.246 205.026 1.00 1.52  ? 2976 LEU A O     1 
ATOM   12096 C  CB    . LEU A 1 2976 ? 214.299 226.590 205.158 1.00 1.22  ? 2976 LEU A CB    1 
ATOM   12097 C  CG    . LEU A 1 2976 ? 214.183 228.039 204.690 1.00 1.10  ? 2976 LEU A CG    1 
ATOM   12098 C  CD1   . LEU A 1 2976 ? 213.695 228.912 205.833 1.00 2.23  ? 2976 LEU A CD1   1 
ATOM   12099 C  CD2   . LEU A 1 2976 ? 215.511 228.540 204.152 1.00 1.12  ? 2976 LEU A CD2   1 
ATOM   12100 N  N     . ARG A 1 2977 ? 214.512 223.425 205.308 1.00 1.69  ? 2977 ARG A N     1 
ATOM   12101 C  CA    . ARG A 1 2977 ? 214.999 222.225 205.980 1.00 0.85  ? 2977 ARG A CA    1 
ATOM   12102 C  C     . ARG A 1 2977 ? 215.859 221.385 205.050 1.00 1.03  ? 2977 ARG A C     1 
ATOM   12103 O  O     . ARG A 1 2977 ? 216.871 220.818 205.476 1.00 2.03  ? 2977 ARG A O     1 
ATOM   12104 C  CB    . ARG A 1 2977 ? 213.824 221.402 206.509 1.00 1.62  ? 2977 ARG A CB    1 
ATOM   12105 C  CG    . ARG A 1 2977 ? 213.179 221.960 207.760 1.00 1.15  ? 2977 ARG A CG    1 
ATOM   12106 C  CD    . ARG A 1 2977 ? 211.907 221.206 208.112 1.00 2.50  ? 2977 ARG A CD    1 
ATOM   12107 N  NE    . ARG A 1 2977 ? 210.951 222.064 208.795 1.00 4.86  ? 2977 ARG A NE    1 
ATOM   12108 C  CZ    . ARG A 1 2977 ? 209.752 222.375 208.325 1.00 2.25  ? 2977 ARG A CZ    1 
ATOM   12109 N  NH1   . ARG A 1 2977 ? 209.309 221.882 207.181 1.00 1.33  ? 2977 ARG A NH1   1 
ATOM   12110 N  NH2   . ARG A 1 2977 ? 208.978 223.202 209.022 1.00 3.86  ? 2977 ARG A NH2   1 
ATOM   12111 N  N     . THR A 1 2978 ? 215.473 221.290 203.778 1.00 1.23  ? 2978 THR A N     1 
ATOM   12112 C  CA    . THR A 1 2978 ? 216.243 220.501 202.823 1.00 1.54  ? 2978 THR A CA    1 
ATOM   12113 C  C     . THR A 1 2978 ? 217.646 221.066 202.636 1.00 1.39  ? 2978 THR A C     1 
ATOM   12114 O  O     . THR A 1 2978 ? 218.629 220.318 202.634 1.00 1.51  ? 2978 THR A O     1 
ATOM   12115 C  CB    . THR A 1 2978 ? 215.504 220.433 201.486 1.00 1.99  ? 2978 THR A CB    1 
ATOM   12116 O  OG1   . THR A 1 2978 ? 214.293 219.686 201.647 1.00 6.14  ? 2978 THR A OG1   1 
ATOM   12117 C  CG2   . THR A 1 2978 ? 216.364 219.767 200.424 1.00 1.72  ? 2978 THR A CG2   1 
ATOM   12118 N  N     . VAL A 1 2979 ? 217.760 222.388 202.493 1.00 1.00  ? 2979 VAL A N     1 
ATOM   12119 C  CA    . VAL A 1 2979 ? 219.067 223.004 202.284 1.00 0.92  ? 2979 VAL A CA    1 
ATOM   12120 C  C     . VAL A 1 2979 ? 219.919 222.900 203.541 1.00 1.18  ? 2979 VAL A C     1 
ATOM   12121 O  O     . VAL A 1 2979 ? 221.128 222.654 203.470 1.00 2.28  ? 2979 VAL A O     1 
ATOM   12122 C  CB    . VAL A 1 2979 ? 218.905 224.467 201.833 1.00 1.34  ? 2979 VAL A CB    1 
ATOM   12123 C  CG1   . VAL A 1 2979 ? 220.232 225.026 201.354 1.00 1.51  ? 2979 VAL A CG1   1 
ATOM   12124 C  CG2   . VAL A 1 2979 ? 217.877 224.562 200.739 1.00 2.40  ? 2979 VAL A CG2   1 
ATOM   12125 N  N     . LEU A 1 2980 ? 219.308 223.096 204.711 1.00 1.41  ? 2980 LEU A N     1 
ATOM   12126 C  CA    . LEU A 1 2980 ? 220.068 223.044 205.956 1.00 0.77  ? 2980 LEU A CA    1 
ATOM   12127 C  C     . LEU A 1 2980 ? 220.572 221.636 206.245 1.00 0.71  ? 2980 LEU A C     1 
ATOM   12128 O  O     . LEU A 1 2980 ? 221.694 221.465 206.731 1.00 1.55  ? 2980 LEU A O     1 
ATOM   12129 C  CB    . LEU A 1 2980 ? 219.217 223.570 207.111 1.00 1.29  ? 2980 LEU A CB    1 
ATOM   12130 C  CG    . LEU A 1 2980 ? 218.941 225.074 207.079 1.00 0.48  ? 2980 LEU A CG    1 
ATOM   12131 C  CD1   . LEU A 1 2980 ? 218.215 225.515 208.333 1.00 2.31  ? 2980 LEU A CD1   1 
ATOM   12132 C  CD2   . LEU A 1 2980 ? 220.226 225.857 206.902 1.00 0.36  ? 2980 LEU A CD2   1 
ATOM   12133 N  N     . ARG A 1 2981 ? 219.761 220.614 205.960 1.00 1.55  ? 2981 ARG A N     1 
ATOM   12134 C  CA    . ARG A 1 2981 ? 220.216 219.240 206.153 1.00 1.46  ? 2981 ARG A CA    1 
ATOM   12135 C  C     . ARG A 1 2981 ? 221.410 218.926 205.263 1.00 1.56  ? 2981 ARG A C     1 
ATOM   12136 O  O     . ARG A 1 2981 ? 222.371 218.286 205.703 1.00 2.09  ? 2981 ARG A O     1 
ATOM   12137 C  CB    . ARG A 1 2981 ? 219.082 218.254 205.875 1.00 2.02  ? 2981 ARG A CB    1 
ATOM   12138 C  CG    . ARG A 1 2981 ? 217.962 218.253 206.889 1.00 2.35  ? 2981 ARG A CG    1 
ATOM   12139 C  CD    . ARG A 1 2981 ? 216.781 217.442 206.372 1.00 2.83  ? 2981 ARG A CD    1 
ATOM   12140 N  NE    . ARG A 1 2981 ? 215.635 217.447 207.274 1.00 3.16  ? 2981 ARG A NE    1 
ATOM   12141 C  CZ    . ARG A 1 2981 ? 215.606 216.865 208.465 1.00 5.86  ? 2981 ARG A CZ    1 
ATOM   12142 N  NH1   . ARG A 1 2981 ? 216.652 216.213 208.945 1.00 6.48  ? 2981 ARG A NH1   1 
ATOM   12143 N  NH2   . ARG A 1 2981 ? 214.494 216.933 209.192 1.00 4.80  ? 2981 ARG A NH2   1 
ATOM   12144 N  N     . ARG A 1 2982 ? 221.367 219.366 204.006 1.00 1.16  ? 2982 ARG A N     1 
ATOM   12145 C  CA    . ARG A 1 2982 ? 222.460 219.071 203.086 1.00 1.33  ? 2982 ARG A CA    1 
ATOM   12146 C  C     . ARG A 1 2982 ? 223.743 219.786 203.494 1.00 1.66  ? 2982 ARG A C     1 
ATOM   12147 O  O     . ARG A 1 2982 ? 224.827 219.192 203.461 1.00 4.54  ? 2982 ARG A O     1 
ATOM   12148 C  CB    . ARG A 1 2982 ? 222.058 219.444 201.662 1.00 1.76  ? 2982 ARG A CB    1 
ATOM   12149 C  CG    . ARG A 1 2982 ? 220.956 218.579 201.081 1.00 1.43  ? 2982 ARG A CG    1 
ATOM   12150 C  CD    . ARG A 1 2982 ? 220.435 219.154 199.781 1.00 1.65  ? 2982 ARG A CD    1 
ATOM   12151 N  NE    . ARG A 1 2982 ? 221.492 219.296 198.789 1.00 3.40  ? 2982 ARG A NE    1 
ATOM   12152 C  CZ    . ARG A 1 2982 ? 221.335 219.862 197.601 1.00 3.23  ? 2982 ARG A CZ    1 
ATOM   12153 N  NH1   . ARG A 1 2982 ? 220.172 220.362 197.222 1.00 2.15  ? 2982 ARG A NH1   1 
ATOM   12154 N  NH2   . ARG A 1 2982 ? 222.372 219.931 196.773 1.00 3.15  ? 2982 ARG A NH2   1 
ATOM   12155 N  N     . SER A 1 2983 ? 223.646 221.053 203.889 1.00 1.19  ? 2983 SER A N     1 
ATOM   12156 C  CA    . SER A 1 2983 ? 224.828 221.820 204.257 1.00 1.04  ? 2983 SER A CA    1 
ATOM   12157 C  C     . SER A 1 2983 ? 225.226 221.647 205.716 1.00 1.85  ? 2983 SER A C     1 
ATOM   12158 O  O     . SER A 1 2983 ? 226.395 221.864 206.052 1.00 1.63  ? 2983 SER A O     1 
ATOM   12159 C  CB    . SER A 1 2983 ? 224.609 223.308 203.961 1.00 0.77  ? 2983 SER A CB    1 
ATOM   12160 O  OG    . SER A 1 2983 ? 223.825 223.925 204.962 1.00 2.42  ? 2983 SER A OG    1 
ATOM   12161 N  N     . GLY A 1 2984 ? 224.296 221.261 206.584 1.00 1.24  ? 2984 GLY A N     1 
ATOM   12162 C  CA    . GLY A 1 2984 ? 224.609 221.102 207.987 1.00 0.78  ? 2984 GLY A CA    1 
ATOM   12163 C  C     . GLY A 1 2984 ? 224.968 219.686 208.387 1.00 2.04  ? 2984 GLY A C     1 
ATOM   12164 O  O     . GLY A 1 2984 ? 225.748 219.481 209.320 1.00 2.82  ? 2984 GLY A O     1 
ATOM   12165 N  N     . CYS A 1 2985 ? 224.413 218.697 207.691 1.00 2.01  ? 2985 CYS A N     1 
ATOM   12166 C  CA    . CYS A 1 2985 ? 224.637 217.294 208.019 1.00 3.51  ? 2985 CYS A CA    1 
ATOM   12167 C  C     . CYS A 1 2985 ? 225.517 216.568 207.018 1.00 3.62  ? 2985 CYS A C     1 
ATOM   12168 O  O     . CYS A 1 2985 ? 226.342 215.744 207.416 1.00 5.24  ? 2985 CYS A O     1 
ATOM   12169 C  CB    . CYS A 1 2985 ? 223.299 216.556 208.137 1.00 2.14  ? 2985 CYS A CB    1 
ATOM   12170 S  SG    . CYS A 1 2985 ? 222.142 217.279 209.316 1.00 12.57 ? 2985 CYS A SG    1 
ATOM   12171 N  N     . LYS A 1 2986 ? 225.366 216.849 205.726 1.00 2.93  ? 2986 LYS A N     1 
ATOM   12172 C  CA    . LYS A 1 2986 ? 226.107 216.159 204.679 1.00 2.53  ? 2986 LYS A CA    1 
ATOM   12173 C  C     . LYS A 1 2986 ? 227.364 216.904 204.248 1.00 2.60  ? 2986 LYS A C     1 
ATOM   12174 O  O     . LYS A 1 2986 ? 228.051 216.448 203.328 1.00 7.21  ? 2986 LYS A O     1 
ATOM   12175 C  CB    . LYS A 1 2986 ? 225.203 215.915 203.470 1.00 2.16  ? 2986 LYS A CB    1 
ATOM   12176 C  CG    . LYS A 1 2986 ? 224.007 215.032 203.765 1.00 4.39  ? 2986 LYS A CG    1 
ATOM   12177 C  CD    . LYS A 1 2986 ? 224.462 213.615 204.077 1.00 9.22  ? 2986 LYS A CD    1 
ATOM   12178 C  CE    . LYS A 1 2986 ? 223.287 212.684 204.299 1.00 10.89 ? 2986 LYS A CE    1 
ATOM   12179 N  NZ    . LYS A 1 2986 ? 223.753 211.312 204.645 1.00 15.28 ? 2986 LYS A NZ    1 
ATOM   12180 N  N     . ASN A 1 2987 ? 227.677 218.033 204.886 1.00 2.29  ? 2987 ASN A N     1 
ATOM   12181 C  CA    . ASN A 1 2987 ? 228.886 218.805 204.594 1.00 1.55  ? 2987 ASN A CA    1 
ATOM   12182 C  C     . ASN A 1 2987 ? 228.945 219.231 203.126 1.00 1.87  ? 2987 ASN A C     1 
ATOM   12183 O  O     . ASN A 1 2987 ? 230.010 219.247 202.507 1.00 1.95  ? 2987 ASN A O     1 
ATOM   12184 C  CB    . ASN A 1 2987 ? 230.141 218.021 204.985 1.00 1.58  ? 2987 ASN A CB    1 
ATOM   12185 C  CG    . ASN A 1 2987 ? 231.338 218.914 205.208 1.00 2.85  ? 2987 ASN A CG    1 
ATOM   12186 O  OD1   . ASN A 1 2987 ? 231.270 219.890 205.953 1.00 5.37  ? 2987 ASN A OD1   1 
ATOM   12187 N  ND2   . ASN A 1 2987 ? 232.449 218.582 204.566 1.00 1.57  ? 2987 ASN A ND2   1 
ATOM   12188 N  N     . GLU A 1 2988 ? 227.795 219.592 202.569 1.00 1.46  ? 2988 GLU A N     1 
ATOM   12189 C  CA    . GLU A 1 2988 ? 227.686 219.956 201.163 1.00 1.57  ? 2988 GLU A CA    1 
ATOM   12190 C  C     . GLU A 1 2988 ? 227.692 221.473 201.027 1.00 2.26  ? 2988 GLU A C     1 
ATOM   12191 O  O     . GLU A 1 2988 ? 226.827 222.153 201.589 1.00 2.94  ? 2988 GLU A O     1 
ATOM   12192 C  CB    . GLU A 1 2988 ? 226.419 219.366 200.549 1.00 2.11  ? 2988 GLU A CB    1 
ATOM   12193 C  CG    . GLU A 1 2988 ? 226.209 219.738 199.095 1.00 3.39  ? 2988 GLU A CG    1 
ATOM   12194 C  CD    . GLU A 1 2988 ? 224.907 219.205 198.538 1.00 7.99  ? 2988 GLU A CD    1 
ATOM   12195 O  OE1   . GLU A 1 2988 ? 224.146 218.571 199.299 1.00 10.74 ? 2988 GLU A OE1   1 
ATOM   12196 O  OE2   . GLU A 1 2988 ? 224.643 219.420 197.339 1.00 10.20 ? 2988 GLU A OE2   1 
ATOM   12197 N  N     . LYS A 1 2989 ? 228.660 221.998 200.280 1.00 1.95  ? 2989 LYS A N     1 
ATOM   12198 C  CA    . LYS A 1 2989 ? 228.712 223.427 200.000 1.00 1.05  ? 2989 LYS A CA    1 
ATOM   12199 C  C     . LYS A 1 2989 ? 227.603 223.791 199.020 1.00 0.72  ? 2989 LYS A C     1 
ATOM   12200 O  O     . LYS A 1 2989 ? 227.529 223.235 197.920 1.00 1.04  ? 2989 LYS A O     1 
ATOM   12201 C  CB    . LYS A 1 2989 ? 230.080 223.807 199.440 1.00 2.46  ? 2989 LYS A CB    1 
ATOM   12202 C  CG    . LYS A 1 2989 ? 231.216 223.653 200.439 1.00 3.18  ? 2989 LYS A CG    1 
ATOM   12203 C  CD    . LYS A 1 2989 ? 232.526 224.196 199.896 1.00 3.90  ? 2989 LYS A CD    1 
ATOM   12204 C  CE    . LYS A 1 2989 ? 233.119 223.282 198.842 1.00 12.56 ? 2989 LYS A CE    1 
ATOM   12205 N  NZ    . LYS A 1 2989 ? 234.455 223.756 198.391 1.00 24.52 ? 2989 LYS A NZ    1 
ATOM   12206 N  N     . ILE A 1 2990 ? 226.739 224.722 199.418 1.00 1.75  ? 2990 ILE A N     1 
ATOM   12207 C  CA    . ILE A 1 2990 ? 225.524 225.036 198.679 1.00 0.49  ? 2990 ILE A CA    1 
ATOM   12208 C  C     . ILE A 1 2990 ? 225.443 226.539 198.462 1.00 0.47  ? 2990 ILE A C     1 
ATOM   12209 O  O     . ILE A 1 2990 ? 225.622 227.320 199.404 1.00 0.41  ? 2990 ILE A O     1 
ATOM   12210 C  CB    . ILE A 1 2990 ? 224.268 224.530 199.416 1.00 0.62  ? 2990 ILE A CB    1 
ATOM   12211 C  CG1   . ILE A 1 2990 ? 224.211 223.002 199.378 1.00 1.35  ? 2990 ILE A CG1   1 
ATOM   12212 C  CG2   . ILE A 1 2990 ? 223.006 225.133 198.813 1.00 0.57  ? 2990 ILE A CG2   1 
ATOM   12213 C  CD1   . ILE A 1 2990 ? 222.958 222.427 199.974 1.00 1.18  ? 2990 ILE A CD1   1 
ATOM   12214 N  N     . ALA A 1 2991 ? 225.174 226.942 197.223 1.00 0.66  ? 2991 ALA A N     1 
ATOM   12215 C  CA    . ALA A 1 2991 ? 224.847 228.326 196.891 1.00 0.46  ? 2991 ALA A CA    1 
ATOM   12216 C  C     . ALA A 1 2991 ? 223.328 228.423 196.800 1.00 0.71  ? 2991 ALA A C     1 
ATOM   12217 O  O     . ALA A 1 2991 ? 222.726 228.017 195.803 1.00 0.75  ? 2991 ALA A O     1 
ATOM   12218 C  CB    . ALA A 1 2991 ? 225.518 228.759 195.593 1.00 0.26  ? 2991 ALA A CB    1 
ATOM   12219 N  N     . PHE A 1 2992 ? 222.710 228.954 197.849 1.00 0.47  ? 2992 PHE A N     1 
ATOM   12220 C  CA    . PHE A 1 2992 ? 221.260 229.110 197.914 1.00 0.56  ? 2992 PHE A CA    1 
ATOM   12221 C  C     . PHE A 1 2992 ? 220.909 230.430 197.240 1.00 0.98  ? 2992 PHE A C     1 
ATOM   12222 O  O     . PHE A 1 2992 ? 220.936 231.491 197.867 1.00 2.31  ? 2992 PHE A O     1 
ATOM   12223 C  CB    . PHE A 1 2992 ? 220.785 229.050 199.364 1.00 0.87  ? 2992 PHE A CB    1 
ATOM   12224 C  CG    . PHE A 1 2992 ? 219.300 229.210 199.531 1.00 1.14  ? 2992 PHE A CG    1 
ATOM   12225 C  CD1   . PHE A 1 2992 ? 218.428 228.855 198.518 1.00 1.79  ? 2992 PHE A CD1   1 
ATOM   12226 C  CD2   . PHE A 1 2992 ? 218.779 229.710 200.711 1.00 2.15  ? 2992 PHE A CD2   1 
ATOM   12227 C  CE1   . PHE A 1 2992 ? 217.069 229.008 198.673 1.00 6.02  ? 2992 PHE A CE1   1 
ATOM   12228 C  CE2   . PHE A 1 2992 ? 217.418 229.861 200.875 1.00 2.83  ? 2992 PHE A CE2   1 
ATOM   12229 C  CZ    . PHE A 1 2992 ? 216.561 229.510 199.857 1.00 5.61  ? 2992 PHE A CZ    1 
ATOM   12230 N  N     . ILE A 1 2993 ? 220.575 230.363 195.957 1.00 1.21  ? 2993 ILE A N     1 
ATOM   12231 C  CA    . ILE A 1 2993 ? 220.297 231.548 195.155 1.00 0.79  ? 2993 ILE A CA    1 
ATOM   12232 C  C     . ILE A 1 2993 ? 218.796 231.796 195.167 1.00 1.08  ? 2993 ILE A C     1 
ATOM   12233 O  O     . ILE A 1 2993 ? 218.012 230.945 194.732 1.00 2.78  ? 2993 ILE A O     1 
ATOM   12234 C  CB    . ILE A 1 2993 ? 220.820 231.385 193.721 1.00 0.63  ? 2993 ILE A CB    1 
ATOM   12235 C  CG1   . ILE A 1 2993 ? 222.289 230.957 193.745 1.00 0.20  ? 2993 ILE A CG1   1 
ATOM   12236 C  CG2   . ILE A 1 2993 ? 220.637 232.678 192.937 1.00 0.46  ? 2993 ILE A CG2   1 
ATOM   12237 C  CD1   . ILE A 1 2993 ? 222.890 230.747 192.379 1.00 0.23  ? 2993 ILE A CD1   1 
ATOM   12238 N  N     . MET A 1 2994 ? 218.394 232.960 195.663 1.00 1.62  ? 2994 MET A N     1 
ATOM   12239 C  CA    . MET A 1 2994 ? 216.989 233.301 195.814 1.00 3.06  ? 2994 MET A CA    1 
ATOM   12240 C  C     . MET A 1 2994 ? 216.765 234.753 195.418 1.00 1.95  ? 2994 MET A C     1 
ATOM   12241 O  O     . MET A 1 2994 ? 217.490 235.647 195.860 1.00 3.00  ? 2994 MET A O     1 
ATOM   12242 C  CB    . MET A 1 2994 ? 216.525 233.034 197.254 1.00 5.53  ? 2994 MET A CB    1 
ATOM   12243 C  CG    . MET A 1 2994 ? 215.059 233.305 197.516 1.00 15.46 ? 2994 MET A CG    1 
ATOM   12244 S  SD    . MET A 1 2994 ? 214.591 232.930 199.218 1.00 38.27 ? 2994 MET A SD    1 
ATOM   12245 C  CE    . MET A 1 2994 ? 215.378 234.257 200.115 1.00 18.23 ? 2994 MET A CE    1 
ATOM   12246 N  N     . ASP A 1 2995 ? 215.765 234.974 194.574 1.00 3.10  ? 2995 ASP A N     1 
ATOM   12247 C  CA    . ASP A 1 2995 ? 215.438 236.295 194.062 1.00 7.54  ? 2995 ASP A CA    1 
ATOM   12248 C  C     . ASP A 1 2995 ? 214.390 236.974 194.936 1.00 4.79  ? 2995 ASP A C     1 
ATOM   12249 O  O     . ASP A 1 2995 ? 213.734 236.342 195.768 1.00 5.59  ? 2995 ASP A O     1 
ATOM   12250 C  CB    . ASP A 1 2995 ? 214.936 236.205 192.620 1.00 4.47  ? 2995 ASP A CB    1 
ATOM   12251 C  CG    . ASP A 1 2995 ? 215.121 237.499 191.854 1.00 6.70  ? 2995 ASP A CG    1 
ATOM   12252 O  OD1   . ASP A 1 2995 ? 216.232 237.735 191.339 1.00 10.19 ? 2995 ASP A OD1   1 
ATOM   12253 O  OD2   . ASP A 1 2995 ? 214.154 238.285 191.769 1.00 14.33 ? 2995 ASP A OD2   1 
ATOM   12254 N  N     . GLU A 1 2996 ? 214.241 238.285 194.733 1.00 9.20  ? 2996 GLU A N     1 
ATOM   12255 C  CA    . GLU A 1 2996 ? 213.193 239.030 195.423 1.00 10.14 ? 2996 GLU A CA    1 
ATOM   12256 C  C     . GLU A 1 2996 ? 211.809 238.531 195.024 1.00 6.65  ? 2996 GLU A C     1 
ATOM   12257 O  O     . GLU A 1 2996 ? 210.878 238.546 195.836 1.00 5.40  ? 2996 GLU A O     1 
ATOM   12258 C  CB    . GLU A 1 2996 ? 213.331 240.528 195.139 1.00 8.82  ? 2996 GLU A CB    1 
ATOM   12259 C  CG    . GLU A 1 2996 ? 213.106 240.913 193.684 1.00 9.39  ? 2996 GLU A CG    1 
ATOM   12260 C  CD    . GLU A 1 2996 ? 213.305 242.394 193.414 1.00 14.11 ? 2996 GLU A CD    1 
ATOM   12261 O  OE1   . GLU A 1 2996 ? 213.640 243.140 194.357 1.00 14.69 ? 2996 GLU A OE1   1 
ATOM   12262 O  OE2   . GLU A 1 2996 ? 213.137 242.810 192.253 1.00 9.34  ? 2996 GLU A OE2   1 
ATOM   12263 N  N     . SER A 1 2997 ? 211.657 238.084 193.776 1.00 7.48  ? 2997 SER A N     1 
ATOM   12264 C  CA    . SER A 1 2997 ? 210.373 237.558 193.326 1.00 9.61  ? 2997 SER A CA    1 
ATOM   12265 C  C     . SER A 1 2997 ? 210.016 236.269 194.055 1.00 8.91  ? 2997 SER A C     1 
ATOM   12266 O  O     . SER A 1 2997 ? 208.834 235.930 194.190 1.00 13.56 ? 2997 SER A O     1 
ATOM   12267 C  CB    . SER A 1 2997 ? 210.398 237.338 191.815 1.00 10.12 ? 2997 SER A CB    1 
ATOM   12268 O  OG    . SER A 1 2997 ? 211.551 236.614 191.429 1.00 12.39 ? 2997 SER A OG    1 
ATOM   12269 N  N     . ASN A 1 2998 ? 211.022 235.532 194.529 1.00 10.43 ? 2998 ASN A N     1 
ATOM   12270 C  CA    . ASN A 1 2998 ? 210.765 234.332 195.315 1.00 10.80 ? 2998 ASN A CA    1 
ATOM   12271 C  C     . ASN A 1 2998 ? 210.104 234.649 196.650 1.00 10.04 ? 2998 ASN A C     1 
ATOM   12272 O  O     . ASN A 1 2998 ? 209.499 233.760 197.256 1.00 15.54 ? 2998 ASN A O     1 
ATOM   12273 C  CB    . ASN A 1 2998 ? 212.067 233.568 195.559 1.00 7.15  ? 2998 ASN A CB    1 
ATOM   12274 C  CG    . ASN A 1 2998 ? 212.611 232.924 194.305 1.00 8.54  ? 2998 ASN A CG    1 
ATOM   12275 O  OD1   . ASN A 1 2998 ? 212.012 233.015 193.235 1.00 13.14 ? 2998 ASN A OD1   1 
ATOM   12276 N  ND2   . ASN A 1 2998 ? 213.758 232.272 194.428 1.00 10.16 ? 2998 ASN A ND2   1 
ATOM   12277 N  N     . VAL A 1 2999 ? 210.205 235.890 197.117 1.00 7.34  ? 2999 VAL A N     1 
ATOM   12278 C  CA    . VAL A 1 2999 ? 209.607 236.287 198.384 1.00 8.87  ? 2999 VAL A CA    1 
ATOM   12279 C  C     . VAL A 1 2999 ? 208.118 236.521 198.164 1.00 12.87 ? 2999 VAL A C     1 
ATOM   12280 O  O     . VAL A 1 2999 ? 207.695 237.626 197.807 1.00 13.95 ? 2999 VAL A O     1 
ATOM   12281 C  CB    . VAL A 1 2999 ? 210.294 237.540 198.958 1.00 8.10  ? 2999 VAL A CB    1 
ATOM   12282 C  CG1   . VAL A 1 2999 ? 209.608 237.996 200.238 1.00 9.88  ? 2999 VAL A CG1   1 
ATOM   12283 C  CG2   . VAL A 1 2999 ? 211.772 237.275 199.196 1.00 4.93  ? 2999 VAL A CG2   1 
ATOM   12284 N  N     . LEU A 1 3000 ? 207.317 235.474 198.361 1.00 14.90 ? 3000 LEU A N     1 
ATOM   12285 C  CA    . LEU A 1 3000 ? 205.875 235.588 198.190 1.00 13.87 ? 3000 LEU A CA    1 
ATOM   12286 C  C     . LEU A 1 3000 ? 205.178 236.069 199.452 1.00 15.62 ? 3000 LEU A C     1 
ATOM   12287 O  O     . LEU A 1 3000 ? 203.979 236.367 199.408 1.00 18.59 ? 3000 LEU A O     1 
ATOM   12288 C  CB    . LEU A 1 3000 ? 205.289 234.245 197.753 1.00 12.73 ? 3000 LEU A CB    1 
ATOM   12289 C  CG    . LEU A 1 3000 ? 206.018 233.531 196.617 1.00 12.94 ? 3000 LEU A CG    1 
ATOM   12290 C  CD1   . LEU A 1 3000 ? 205.261 232.288 196.187 1.00 10.96 ? 3000 LEU A CD1   1 
ATOM   12291 C  CD2   . LEU A 1 3000 ? 206.207 234.471 195.436 1.00 15.79 ? 3000 LEU A CD2   1 
ATOM   12292 N  N     . ASP A 1 3001 ? 205.900 236.155 200.565 1.00 11.81 ? 3001 ASP A N     1 
ATOM   12293 C  CA    . ASP A 1 3001 ? 205.337 236.588 201.832 1.00 12.60 ? 3001 ASP A CA    1 
ATOM   12294 C  C     . ASP A 1 3001 ? 206.457 237.158 202.690 1.00 15.10 ? 3001 ASP A C     1 
ATOM   12295 O  O     . ASP A 1 3001 ? 207.616 236.753 202.572 1.00 21.20 ? 3001 ASP A O     1 
ATOM   12296 C  CB    . ASP A 1 3001 ? 204.627 235.425 202.548 1.00 15.64 ? 3001 ASP A CB    1 
ATOM   12297 C  CG    . ASP A 1 3001 ? 204.347 235.714 204.010 1.00 21.96 ? 3001 ASP A CG    1 
ATOM   12298 O  OD1   . ASP A 1 3001 ? 204.023 236.874 204.344 1.00 25.55 ? 3001 ASP A OD1   1 
ATOM   12299 O  OD2   . ASP A 1 3001 ? 204.448 234.775 204.827 1.00 24.87 ? 3001 ASP A OD2   1 
ATOM   12300 N  N     . SER A 1 3002 ? 206.096 238.107 203.557 1.00 18.10 ? 3002 SER A N     1 
ATOM   12301 C  CA    . SER A 1 3002 ? 207.075 238.709 204.454 1.00 16.16 ? 3002 SER A CA    1 
ATOM   12302 C  C     . SER A 1 3002 ? 207.678 237.697 205.417 1.00 17.13 ? 3002 SER A C     1 
ATOM   12303 O  O     . SER A 1 3002 ? 208.786 237.916 205.916 1.00 20.17 ? 3002 SER A O     1 
ATOM   12304 C  CB    . SER A 1 3002 ? 206.435 239.853 205.239 1.00 19.14 ? 3002 SER A CB    1 
ATOM   12305 O  OG    . SER A 1 3002 ? 205.417 239.370 206.097 1.00 29.47 ? 3002 SER A OG    1 
ATOM   12306 N  N     . GLY A 1 3003 ? 206.974 236.597 205.694 1.00 11.81 ? 3003 GLY A N     1 
ATOM   12307 C  CA    . GLY A 1 3003 ? 207.511 235.580 206.578 1.00 7.77  ? 3003 GLY A CA    1 
ATOM   12308 C  C     . GLY A 1 3003 ? 208.696 234.837 206.005 1.00 10.48 ? 3003 GLY A C     1 
ATOM   12309 O  O     . GLY A 1 3003 ? 209.449 234.216 206.762 1.00 11.12 ? 3003 GLY A O     1 
ATOM   12310 N  N     . PHE A 1 3004 ? 208.874 234.881 204.682 1.00 10.84 ? 3004 PHE A N     1 
ATOM   12311 C  CA    . PHE A 1 3004 ? 210.038 234.252 204.070 1.00 7.47  ? 3004 PHE A CA    1 
ATOM   12312 C  C     . PHE A 1 3004 ? 211.327 234.891 204.568 1.00 4.35  ? 3004 PHE A C     1 
ATOM   12313 O  O     . PHE A 1 3004 ? 212.282 234.193 204.926 1.00 4.45  ? 3004 PHE A O     1 
ATOM   12314 C  CB    . PHE A 1 3004 ? 209.961 234.360 202.545 1.00 7.34  ? 3004 PHE A CB    1 
ATOM   12315 C  CG    . PHE A 1 3004 ? 208.996 233.402 201.899 1.00 6.24  ? 3004 PHE A CG    1 
ATOM   12316 C  CD1   . PHE A 1 3004 ? 207.827 233.023 202.536 1.00 6.20  ? 3004 PHE A CD1   1 
ATOM   12317 C  CD2   . PHE A 1 3004 ? 209.254 232.900 200.637 1.00 7.09  ? 3004 PHE A CD2   1 
ATOM   12318 C  CE1   . PHE A 1 3004 ? 206.942 232.156 201.933 1.00 5.07  ? 3004 PHE A CE1   1 
ATOM   12319 C  CE2   . PHE A 1 3004 ? 208.373 232.031 200.029 1.00 7.75  ? 3004 PHE A CE2   1 
ATOM   12320 C  CZ    . PHE A 1 3004 ? 207.215 231.659 200.679 1.00 6.76  ? 3004 PHE A CZ    1 
ATOM   12321 N  N     . LEU A 1 3005 ? 211.365 236.223 204.610 1.00 6.70  ? 3005 LEU A N     1 
ATOM   12322 C  CA    . LEU A 1 3005 ? 212.577 236.944 204.973 1.00 5.94  ? 3005 LEU A CA    1 
ATOM   12323 C  C     . LEU A 1 3005 ? 212.846 236.947 206.469 1.00 5.24  ? 3005 LEU A C     1 
ATOM   12324 O  O     . LEU A 1 3005 ? 214.003 237.111 206.873 1.00 8.10  ? 3005 LEU A O     1 
ATOM   12325 C  CB    . LEU A 1 3005 ? 212.503 238.380 204.463 1.00 5.88  ? 3005 LEU A CB    1 
ATOM   12326 C  CG    . LEU A 1 3005 ? 212.573 238.487 202.943 1.00 12.60 ? 3005 LEU A CG    1 
ATOM   12327 C  CD1   . LEU A 1 3005 ? 212.592 239.934 202.537 1.00 12.15 ? 3005 LEU A CD1   1 
ATOM   12328 C  CD2   . LEU A 1 3005 ? 213.798 237.759 202.412 1.00 5.80  ? 3005 LEU A CD2   1 
ATOM   12329 N  N     . GLU A 1 3006 ? 211.815 236.784 207.298 1.00 4.73  ? 3006 GLU A N     1 
ATOM   12330 C  CA    . GLU A 1 3006 ? 212.045 236.649 208.731 1.00 6.72  ? 3006 GLU A CA    1 
ATOM   12331 C  C     . GLU A 1 3006 ? 212.841 235.385 209.028 1.00 5.91  ? 3006 GLU A C     1 
ATOM   12332 O  O     . GLU A 1 3006 ? 213.652 235.358 209.961 1.00 8.03  ? 3006 GLU A O     1 
ATOM   12333 C  CB    . GLU A 1 3006 ? 210.707 236.659 209.472 1.00 8.24  ? 3006 GLU A CB    1 
ATOM   12334 C  CG    . GLU A 1 3006 ? 210.793 236.759 210.988 1.00 6.07  ? 3006 GLU A CG    1 
ATOM   12335 C  CD    . GLU A 1 3006 ? 211.020 235.418 211.661 1.00 24.78 ? 3006 GLU A CD    1 
ATOM   12336 O  OE1   . GLU A 1 3006 ? 210.590 234.389 211.100 1.00 18.48 ? 3006 GLU A OE1   1 
ATOM   12337 O  OE2   . GLU A 1 3006 ? 211.622 235.397 212.754 1.00 26.61 ? 3006 GLU A OE2   1 
ATOM   12338 N  N     . ARG A 1 3007 ? 212.634 234.336 208.231 1.00 4.00  ? 3007 ARG A N     1 
ATOM   12339 C  CA    . ARG A 1 3007 ? 213.448 233.133 208.355 1.00 3.46  ? 3007 ARG A CA    1 
ATOM   12340 C  C     . ARG A 1 3007 ? 214.859 233.363 207.829 1.00 3.59  ? 3007 ARG A C     1 
ATOM   12341 O  O     . ARG A 1 3007 ? 215.838 232.933 208.450 1.00 5.27  ? 3007 ARG A O     1 
ATOM   12342 C  CB    . ARG A 1 3007 ? 212.787 231.972 207.613 1.00 2.81  ? 3007 ARG A CB    1 
ATOM   12343 C  CG    . ARG A 1 3007 ? 211.404 231.601 208.109 1.00 1.85  ? 3007 ARG A CG    1 
ATOM   12344 C  CD    . ARG A 1 3007 ? 211.483 230.727 209.345 1.00 7.31  ? 3007 ARG A CD    1 
ATOM   12345 N  NE    . ARG A 1 3007 ? 210.294 229.901 209.501 1.00 14.00 ? 3007 ARG A NE    1 
ATOM   12346 C  CZ    . ARG A 1 3007 ? 210.075 229.084 210.523 1.00 11.31 ? 3007 ARG A CZ    1 
ATOM   12347 N  NH1   . ARG A 1 3007 ? 210.943 228.969 211.512 1.00 7.42  ? 3007 ARG A NH1   1 
ATOM   12348 N  NH2   . ARG A 1 3007 ? 208.957 228.367 210.552 1.00 16.18 ? 3007 ARG A NH2   1 
ATOM   12349 N  N     . MET A 1 3008 ? 214.984 234.036 206.681 1.00 1.87  ? 3008 MET A N     1 
ATOM   12350 C  CA    . MET A 1 3008 ? 216.303 234.292 206.112 1.00 2.38  ? 3008 MET A CA    1 
ATOM   12351 C  C     . MET A 1 3008 ? 217.102 235.276 206.951 1.00 2.33  ? 3008 MET A C     1 
ATOM   12352 O  O     . MET A 1 3008 ? 218.330 235.165 207.028 1.00 4.47  ? 3008 MET A O     1 
ATOM   12353 C  CB    . MET A 1 3008 ? 216.175 234.801 204.677 1.00 2.68  ? 3008 MET A CB    1 
ATOM   12354 C  CG    . MET A 1 3008 ? 215.317 233.926 203.789 1.00 5.01  ? 3008 MET A CG    1 
ATOM   12355 S  SD    . MET A 1 3008 ? 216.176 232.412 203.319 1.00 22.10 ? 3008 MET A SD    1 
ATOM   12356 C  CE    . MET A 1 3008 ? 217.786 233.057 202.875 1.00 6.55  ? 3008 MET A CE    1 
ATOM   12357 N  N     . ASN A 1 3009 ? 216.431 236.238 207.588 1.00 2.86  ? 3009 ASN A N     1 
ATOM   12358 C  CA    . ASN A 1 3009 ? 217.134 237.188 208.441 1.00 2.15  ? 3009 ASN A CA    1 
ATOM   12359 C  C     . ASN A 1 3009 ? 217.846 236.474 209.583 1.00 1.92  ? 3009 ASN A C     1 
ATOM   12360 O  O     . ASN A 1 3009 ? 218.966 236.841 209.954 1.00 1.97  ? 3009 ASN A O     1 
ATOM   12361 C  CB    . ASN A 1 3009 ? 216.155 238.228 208.983 1.00 2.13  ? 3009 ASN A CB    1 
ATOM   12362 C  CG    . ASN A 1 3009 ? 216.852 239.419 209.597 1.00 3.11  ? 3009 ASN A CG    1 
ATOM   12363 O  OD1   . ASN A 1 3009 ? 217.509 240.193 208.903 1.00 4.27  ? 3009 ASN A OD1   1 
ATOM   12364 N  ND2   . ASN A 1 3009 ? 216.715 239.573 210.907 1.00 1.15  ? 3009 ASN A ND2   1 
ATOM   12365 N  N     . THR A 1 3010 ? 217.208 235.453 210.154 1.00 2.77  ? 3010 THR A N     1 
ATOM   12366 C  CA    . THR A 1 3010 ? 217.862 234.656 211.187 1.00 3.22  ? 3010 THR A CA    1 
ATOM   12367 C  C     . THR A 1 3010 ? 218.948 233.769 210.592 1.00 2.34  ? 3010 THR A C     1 
ATOM   12368 O  O     . THR A 1 3010 ? 220.031 233.632 211.171 1.00 1.68  ? 3010 THR A O     1 
ATOM   12369 C  CB    . THR A 1 3010 ? 216.827 233.812 211.930 1.00 3.99  ? 3010 THR A CB    1 
ATOM   12370 O  OG1   . THR A 1 3010 ? 215.668 234.608 212.201 1.00 11.29 ? 3010 THR A OG1   1 
ATOM   12371 C  CG2   . THR A 1 3010 ? 217.398 233.298 213.237 1.00 2.67  ? 3010 THR A CG2   1 
ATOM   12372 N  N     . LEU A 1 3011 ? 218.673 233.164 209.435 1.00 2.78  ? 3011 LEU A N     1 
ATOM   12373 C  CA    . LEU A 1 3011 ? 219.625 232.243 208.822 1.00 1.54  ? 3011 LEU A CA    1 
ATOM   12374 C  C     . LEU A 1 3011 ? 220.905 232.956 208.402 1.00 1.90  ? 3011 LEU A C     1 
ATOM   12375 O  O     . LEU A 1 3011 ? 222.005 232.420 208.574 1.00 2.03  ? 3011 LEU A O     1 
ATOM   12376 C  CB    . LEU A 1 3011 ? 218.978 231.548 207.625 1.00 1.57  ? 3011 LEU A CB    1 
ATOM   12377 C  CG    . LEU A 1 3011 ? 219.848 230.556 206.851 1.00 1.25  ? 3011 LEU A CG    1 
ATOM   12378 C  CD1   . LEU A 1 3011 ? 220.428 229.507 207.786 1.00 0.98  ? 3011 LEU A CD1   1 
ATOM   12379 C  CD2   . LEU A 1 3011 ? 219.046 229.904 205.741 1.00 0.88  ? 3011 LEU A CD2   1 
ATOM   12380 N  N     . LEU A 1 3012 ? 220.780 234.162 207.842 1.00 1.33  ? 3012 LEU A N     1 
ATOM   12381 C  CA    . LEU A 1 3012 ? 221.956 234.891 207.377 1.00 0.91  ? 3012 LEU A CA    1 
ATOM   12382 C  C     . LEU A 1 3012 ? 222.871 235.268 208.534 1.00 1.37  ? 3012 LEU A C     1 
ATOM   12383 O  O     . LEU A 1 3012 ? 224.098 235.248 208.394 1.00 1.39  ? 3012 LEU A O     1 
ATOM   12384 C  CB    . LEU A 1 3012 ? 221.529 236.141 206.612 1.00 2.15  ? 3012 LEU A CB    1 
ATOM   12385 C  CG    . LEU A 1 3012 ? 220.852 235.954 205.254 1.00 0.94  ? 3012 LEU A CG    1 
ATOM   12386 C  CD1   . LEU A 1 3012 ? 220.172 237.243 204.832 1.00 2.24  ? 3012 LEU A CD1   1 
ATOM   12387 C  CD2   . LEU A 1 3012 ? 221.850 235.500 204.210 1.00 0.25  ? 3012 LEU A CD2   1 
ATOM   12388 N  N     . ALA A 1 3013 ? 222.295 235.622 209.680 1.00 3.23  ? 3013 ALA A N     1 
ATOM   12389 C  CA    . ALA A 1 3013 ? 223.081 236.120 210.802 1.00 2.44  ? 3013 ALA A CA    1 
ATOM   12390 C  C     . ALA A 1 3013 ? 223.615 235.005 211.696 1.00 2.85  ? 3013 ALA A C     1 
ATOM   12391 O  O     . ALA A 1 3013 ? 224.781 235.046 212.097 1.00 6.24  ? 3013 ALA A O     1 
ATOM   12392 C  CB    . ALA A 1 3013 ? 222.243 237.093 211.630 1.00 2.27  ? 3013 ALA A CB    1 
ATOM   12393 N  N     . ASN A 1 3014 ? 222.790 234.009 212.018 1.00 3.71  ? 3014 ASN A N     1 
ATOM   12394 C  CA    . ASN A 1 3014 ? 223.160 232.995 212.993 1.00 5.15  ? 3014 ASN A CA    1 
ATOM   12395 C  C     . ASN A 1 3014 ? 223.414 231.621 212.392 1.00 4.98  ? 3014 ASN A C     1 
ATOM   12396 O  O     . ASN A 1 3014 ? 223.894 230.736 213.108 1.00 6.75  ? 3014 ASN A O     1 
ATOM   12397 C  CB    . ASN A 1 3014 ? 222.074 232.874 214.072 1.00 2.85  ? 3014 ASN A CB    1 
ATOM   12398 C  CG    . ASN A 1 3014 ? 221.747 234.203 214.718 1.00 7.45  ? 3014 ASN A CG    1 
ATOM   12399 O  OD1   . ASN A 1 3014 ? 222.606 234.833 215.334 1.00 8.24  ? 3014 ASN A OD1   1 
ATOM   12400 N  ND2   . ASN A 1 3014 ? 220.500 234.641 214.577 1.00 4.76  ? 3014 ASN A ND2   1 
ATOM   12401 N  N     . GLY A 1 3015 ? 223.108 231.412 211.115 1.00 4.10  ? 3015 GLY A N     1 
ATOM   12402 C  CA    . GLY A 1 3015 ? 223.255 230.092 210.538 1.00 2.08  ? 3015 GLY A CA    1 
ATOM   12403 C  C     . GLY A 1 3015 ? 222.285 229.070 211.078 1.00 2.55  ? 3015 GLY A C     1 
ATOM   12404 O  O     . GLY A 1 3015 ? 222.527 227.869 210.950 1.00 4.85  ? 3015 GLY A O     1 
ATOM   12405 N  N     . GLU A 1 3016 ? 221.191 229.517 211.685 1.00 2.91  ? 3016 GLU A N     1 
ATOM   12406 C  CA    . GLU A 1 3016 ? 220.230 228.622 212.311 1.00 2.78  ? 3016 GLU A CA    1 
ATOM   12407 C  C     . GLU A 1 3016 ? 218.899 229.343 212.420 1.00 3.31  ? 3016 GLU A C     1 
ATOM   12408 O  O     . GLU A 1 3016 ? 218.849 230.573 212.480 1.00 5.45  ? 3016 GLU A O     1 
ATOM   12409 C  CB    . GLU A 1 3016 ? 220.712 228.171 213.695 1.00 5.24  ? 3016 GLU A CB    1 
ATOM   12410 C  CG    . GLU A 1 3016 ? 220.800 229.301 214.702 1.00 8.44  ? 3016 GLU A CG    1 
ATOM   12411 C  CD    . GLU A 1 3016 ? 221.341 228.857 216.044 1.00 15.96 ? 3016 GLU A CD    1 
ATOM   12412 O  OE1   . GLU A 1 3016 ? 221.674 227.663 216.190 1.00 29.21 ? 3016 GLU A OE1   1 
ATOM   12413 O  OE2   . GLU A 1 3016 ? 221.437 229.705 216.954 1.00 19.54 ? 3016 GLU A OE2   1 
ATOM   12414 N  N     . VAL A 1 3017 ? 217.822 228.567 212.429 1.00 3.11  ? 3017 VAL A N     1 
ATOM   12415 C  CA    . VAL A 1 3017 ? 216.472 229.072 212.631 1.00 3.09  ? 3017 VAL A CA    1 
ATOM   12416 C  C     . VAL A 1 3017 ? 215.901 228.352 213.846 1.00 6.82  ? 3017 VAL A C     1 
ATOM   12417 O  O     . VAL A 1 3017 ? 215.680 227.139 213.795 1.00 12.45 ? 3017 VAL A O     1 
ATOM   12418 C  CB    . VAL A 1 3017 ? 215.578 228.860 211.397 1.00 4.87  ? 3017 VAL A CB    1 
ATOM   12419 C  CG1   . VAL A 1 3017 ? 214.223 229.512 211.609 1.00 8.51  ? 3017 VAL A CG1   1 
ATOM   12420 C  CG2   . VAL A 1 3017 ? 216.255 229.408 210.152 1.00 1.22  ? 3017 VAL A CG2   1 
ATOM   12421 N  N     . PRO A 1 3018 ? 215.655 229.051 214.962 1.00 9.88  ? 3018 PRO A N     1 
ATOM   12422 C  CA    . PRO A 1 3018 ? 215.312 228.344 216.211 1.00 8.56  ? 3018 PRO A CA    1 
ATOM   12423 C  C     . PRO A 1 3018 ? 214.097 227.436 216.112 1.00 6.45  ? 3018 PRO A C     1 
ATOM   12424 O  O     . PRO A 1 3018 ? 214.097 226.354 216.710 1.00 8.96  ? 3018 PRO A O     1 
ATOM   12425 C  CB    . PRO A 1 3018 ? 215.080 229.490 217.212 1.00 8.29  ? 3018 PRO A CB    1 
ATOM   12426 C  CG    . PRO A 1 3018 ? 215.014 230.751 216.390 1.00 9.59  ? 3018 PRO A CG    1 
ATOM   12427 C  CD    . PRO A 1 3018 ? 215.820 230.498 215.165 1.00 8.40  ? 3018 PRO A CD    1 
ATOM   12428 N  N     . GLY A 1 3019 ? 213.060 227.835 215.378 1.00 3.39  ? 3019 GLY A N     1 
ATOM   12429 C  CA    . GLY A 1 3019 ? 211.850 227.043 215.285 1.00 6.63  ? 3019 GLY A CA    1 
ATOM   12430 C  C     . GLY A 1 3019 ? 211.645 226.261 214.007 1.00 8.29  ? 3019 GLY A C     1 
ATOM   12431 O  O     . GLY A 1 3019 ? 210.545 225.736 213.794 1.00 11.85 ? 3019 GLY A O     1 
ATOM   12432 N  N     . LEU A 1 3020 ? 212.656 226.156 213.142 1.00 3.44  ? 3020 LEU A N     1 
ATOM   12433 C  CA    . LEU A 1 3020 ? 212.459 225.501 211.853 1.00 3.15  ? 3020 LEU A CA    1 
ATOM   12434 C  C     . LEU A 1 3020 ? 212.305 223.992 212.014 1.00 2.70  ? 3020 LEU A C     1 
ATOM   12435 O  O     . LEU A 1 3020 ? 211.435 223.377 211.388 1.00 3.29  ? 3020 LEU A O     1 
ATOM   12436 C  CB    . LEU A 1 3020 ? 213.621 225.829 210.917 1.00 4.66  ? 3020 LEU A CB    1 
ATOM   12437 C  CG    . LEU A 1 3020 ? 213.429 225.424 209.456 1.00 1.94  ? 3020 LEU A CG    1 
ATOM   12438 C  CD1   . LEU A 1 3020 ? 212.243 226.148 208.844 1.00 2.39  ? 3020 LEU A CD1   1 
ATOM   12439 C  CD2   . LEU A 1 3020 ? 214.684 225.695 208.667 1.00 1.15  ? 3020 LEU A CD2   1 
ATOM   12440 N  N     . PHE A 1 3021 ? 213.138 223.379 212.848 1.00 4.14  ? 3021 PHE A N     1 
ATOM   12441 C  CA    . PHE A 1 3021 ? 213.093 221.943 213.096 1.00 2.37  ? 3021 PHE A CA    1 
ATOM   12442 C  C     . PHE A 1 3021 ? 212.323 221.699 214.389 1.00 3.63  ? 3021 PHE A C     1 
ATOM   12443 O  O     . PHE A 1 3021 ? 212.795 222.049 215.475 1.00 4.33  ? 3021 PHE A O     1 
ATOM   12444 C  CB    . PHE A 1 3021 ? 214.502 221.361 213.178 1.00 1.12  ? 3021 PHE A CB    1 
ATOM   12445 C  CG    . PHE A 1 3021 ? 215.253 221.400 211.879 1.00 1.56  ? 3021 PHE A CG    1 
ATOM   12446 C  CD1   . PHE A 1 3021 ? 215.160 220.352 210.980 1.00 1.24  ? 3021 PHE A CD1   1 
ATOM   12447 C  CD2   . PHE A 1 3021 ? 216.060 222.481 211.562 1.00 1.01  ? 3021 PHE A CD2   1 
ATOM   12448 C  CE1   . PHE A 1 3021 ? 215.854 220.381 209.787 1.00 0.81  ? 3021 PHE A CE1   1 
ATOM   12449 C  CE2   . PHE A 1 3021 ? 216.755 222.516 210.371 1.00 1.04  ? 3021 PHE A CE2   1 
ATOM   12450 C  CZ    . PHE A 1 3021 ? 216.652 221.466 209.482 1.00 0.90  ? 3021 PHE A CZ    1 
ATOM   12451 N  N     . GLU A 1 3022 ? 211.141 221.098 214.273 1.00 4.21  ? 3022 GLU A N     1 
ATOM   12452 C  CA    . GLU A 1 3022 ? 210.300 220.825 215.429 1.00 5.48  ? 3022 GLU A CA    1 
ATOM   12453 C  C     . GLU A 1 3022 ? 209.684 219.441 215.307 1.00 5.43  ? 3022 GLU A C     1 
ATOM   12454 O  O     . GLU A 1 3022 ? 209.448 218.953 214.199 1.00 7.94  ? 3022 GLU A O     1 
ATOM   12455 C  CB    . GLU A 1 3022 ? 209.190 221.874 215.580 1.00 4.39  ? 3022 GLU A CB    1 
ATOM   12456 C  CG    . GLU A 1 3022 ? 209.642 223.170 216.221 1.00 7.22  ? 3022 GLU A CG    1 
ATOM   12457 C  CD    . GLU A 1 3022 ? 208.525 224.186 216.325 1.00 19.34 ? 3022 GLU A CD    1 
ATOM   12458 O  OE1   . GLU A 1 3022 ? 208.804 225.395 216.187 1.00 19.78 ? 3022 GLU A OE1   1 
ATOM   12459 O  OE2   . GLU A 1 3022 ? 207.365 223.779 216.546 1.00 21.30 ? 3022 GLU A OE2   1 
ATOM   12460 N  N     . GLY A 1 3023 ? 209.420 218.822 216.452 1.00 4.63  ? 3023 GLY A N     1 
ATOM   12461 C  CA    . GLY A 1 3023 ? 208.759 217.525 216.451 1.00 2.80  ? 3023 GLY A CA    1 
ATOM   12462 C  C     . GLY A 1 3023 ? 209.631 216.453 215.833 1.00 3.61  ? 3023 GLY A C     1 
ATOM   12463 O  O     . GLY A 1 3023 ? 210.799 216.279 216.199 1.00 6.17  ? 3023 GLY A O     1 
ATOM   12464 N  N     . ASP A 1 3024 ? 209.055 215.712 214.884 1.00 8.16  ? 3024 ASP A N     1 
ATOM   12465 C  CA    . ASP A 1 3024 ? 209.789 214.634 214.229 1.00 4.39  ? 3024 ASP A CA    1 
ATOM   12466 C  C     . ASP A 1 3024 ? 210.928 215.167 213.371 1.00 3.64  ? 3024 ASP A C     1 
ATOM   12467 O  O     . ASP A 1 3024 ? 211.930 214.470 213.177 1.00 5.05  ? 3024 ASP A O     1 
ATOM   12468 C  CB    . ASP A 1 3024 ? 208.838 213.791 213.383 1.00 6.04  ? 3024 ASP A CB    1 
ATOM   12469 C  CG    . ASP A 1 3024 ? 207.939 212.906 214.223 1.00 11.17 ? 3024 ASP A CG    1 
ATOM   12470 O  OD1   . ASP A 1 3024 ? 208.261 212.687 215.409 1.00 20.87 ? 3024 ASP A OD1   1 
ATOM   12471 O  OD2   . ASP A 1 3024 ? 206.911 212.433 213.701 1.00 15.40 ? 3024 ASP A OD2   1 
ATOM   12472 N  N     . GLU A 1 3025 ? 210.792 216.388 212.850 1.00 3.67  ? 3025 GLU A N     1 
ATOM   12473 C  CA    . GLU A 1 3025 ? 211.865 216.975 212.055 1.00 3.97  ? 3025 GLU A CA    1 
ATOM   12474 C  C     . GLU A 1 3025 ? 213.125 217.169 212.888 1.00 4.84  ? 3025 GLU A C     1 
ATOM   12475 O  O     . GLU A 1 3025 ? 214.238 216.923 212.410 1.00 7.58  ? 3025 GLU A O     1 
ATOM   12476 C  CB    . GLU A 1 3025 ? 211.408 218.304 211.454 1.00 3.60  ? 3025 GLU A CB    1 
ATOM   12477 C  CG    . GLU A 1 3025 ? 210.291 218.178 210.428 1.00 4.93  ? 3025 GLU A CG    1 
ATOM   12478 C  CD    . GLU A 1 3025 ? 210.729 217.458 209.168 1.00 15.70 ? 3025 GLU A CD    1 
ATOM   12479 O  OE1   . GLU A 1 3025 ? 211.913 217.572 208.794 1.00 16.10 ? 3025 GLU A OE1   1 
ATOM   12480 O  OE2   . GLU A 1 3025 ? 209.884 216.777 208.551 1.00 22.29 ? 3025 GLU A OE2   1 
ATOM   12481 N  N     . TYR A 1 3026 ? 212.972 217.616 214.138 1.00 2.96  ? 3026 TYR A N     1 
ATOM   12482 C  CA    . TYR A 1 3026 ? 214.131 217.765 215.010 1.00 2.85  ? 3026 TYR A CA    1 
ATOM   12483 C  C     . TYR A 1 3026 ? 214.744 216.415 215.353 1.00 2.96  ? 3026 TYR A C     1 
ATOM   12484 O  O     . TYR A 1 3026 ? 215.971 216.281 215.407 1.00 3.07  ? 3026 TYR A O     1 
ATOM   12485 C  CB    . TYR A 1 3026 ? 213.749 218.521 216.282 1.00 2.99  ? 3026 TYR A CB    1 
ATOM   12486 C  CG    . TYR A 1 3026 ? 214.944 218.966 217.092 1.00 2.66  ? 3026 TYR A CG    1 
ATOM   12487 C  CD1   . TYR A 1 3026 ? 215.630 220.129 216.769 1.00 1.69  ? 3026 TYR A CD1   1 
ATOM   12488 C  CD2   . TYR A 1 3026 ? 215.391 218.222 218.176 1.00 1.36  ? 3026 TYR A CD2   1 
ATOM   12489 C  CE1   . TYR A 1 3026 ? 216.723 220.540 217.502 1.00 3.09  ? 3026 TYR A CE1   1 
ATOM   12490 C  CE2   . TYR A 1 3026 ? 216.483 218.624 218.916 1.00 1.57  ? 3026 TYR A CE2   1 
ATOM   12491 C  CZ    . TYR A 1 3026 ? 217.146 219.785 218.575 1.00 4.42  ? 3026 TYR A CZ    1 
ATOM   12492 O  OH    . TYR A 1 3026 ? 218.235 220.193 219.309 1.00 5.81  ? 3026 TYR A OH    1 
ATOM   12493 N  N     . ALA A 1 3027 ? 213.905 215.407 215.603 1.00 3.29  ? 3027 ALA A N     1 
ATOM   12494 C  CA    . ALA A 1 3027 ? 214.417 214.080 215.924 1.00 3.70  ? 3027 ALA A CA    1 
ATOM   12495 C  C     . ALA A 1 3027 ? 215.195 213.490 214.754 1.00 2.75  ? 3027 ALA A C     1 
ATOM   12496 O  O     . ALA A 1 3027 ? 216.257 212.886 214.946 1.00 2.16  ? 3027 ALA A O     1 
ATOM   12497 C  CB    . ALA A 1 3027 ? 213.268 213.158 216.329 1.00 2.40  ? 3027 ALA A CB    1 
ATOM   12498 N  N     . THR A 1 3028 ? 214.675 213.646 213.535 1.00 3.25  ? 3028 THR A N     1 
ATOM   12499 C  CA    . THR A 1 3028 ? 215.401 213.185 212.356 1.00 4.12  ? 3028 THR A CA    1 
ATOM   12500 C  C     . THR A 1 3028 ? 216.692 213.972 212.166 1.00 5.04  ? 3028 THR A C     1 
ATOM   12501 O  O     . THR A 1 3028 ? 217.726 213.403 211.795 1.00 4.77  ? 3028 THR A O     1 
ATOM   12502 C  CB    . THR A 1 3028 ? 214.509 213.294 211.118 1.00 5.72  ? 3028 THR A CB    1 
ATOM   12503 O  OG1   . THR A 1 3028 ? 213.342 212.485 211.298 1.00 9.59  ? 3028 THR A OG1   1 
ATOM   12504 C  CG2   . THR A 1 3028 ? 215.246 212.827 209.878 1.00 6.72  ? 3028 THR A CG2   1 
ATOM   12505 N  N     . LEU A 1 3029 ? 216.653 215.280 212.427 1.00 2.70  ? 3029 LEU A N     1 
ATOM   12506 C  CA    . LEU A 1 3029 ? 217.854 216.100 212.315 1.00 2.32  ? 3029 LEU A CA    1 
ATOM   12507 C  C     . LEU A 1 3029 ? 218.937 215.633 213.279 1.00 2.93  ? 3029 LEU A C     1 
ATOM   12508 O  O     . LEU A 1 3029 ? 220.117 215.579 212.915 1.00 6.79  ? 3029 LEU A O     1 
ATOM   12509 C  CB    . LEU A 1 3029 ? 217.513 217.568 212.567 1.00 3.57  ? 3029 LEU A CB    1 
ATOM   12510 C  CG    . LEU A 1 3029 ? 218.684 218.552 212.528 1.00 1.93  ? 3029 LEU A CG    1 
ATOM   12511 C  CD1   . LEU A 1 3029 ? 219.277 218.617 211.136 1.00 1.43  ? 3029 LEU A CD1   1 
ATOM   12512 C  CD2   . LEU A 1 3029 ? 218.253 219.932 212.995 1.00 1.12  ? 3029 LEU A CD2   1 
ATOM   12513 N  N     . MET A 1 3030 ? 218.556 215.289 214.510 1.00 3.38  ? 3030 MET A N     1 
ATOM   12514 C  CA    . MET A 1 3030 ? 219.535 214.818 215.483 1.00 2.92  ? 3030 MET A CA    1 
ATOM   12515 C  C     . MET A 1 3030 ? 220.174 213.506 215.050 1.00 3.62  ? 3030 MET A C     1 
ATOM   12516 O  O     . MET A 1 3030 ? 221.375 213.304 215.257 1.00 7.34  ? 3030 MET A O     1 
ATOM   12517 C  CB    . MET A 1 3030 ? 218.884 214.667 216.857 1.00 2.81  ? 3030 MET A CB    1 
ATOM   12518 C  CG    . MET A 1 3030 ? 218.461 215.975 217.528 1.00 3.98  ? 3030 MET A CG    1 
ATOM   12519 S  SD    . MET A 1 3030 ? 219.798 217.079 218.048 1.00 15.31 ? 3030 MET A SD    1 
ATOM   12520 C  CE    . MET A 1 3030 ? 220.158 218.019 216.565 1.00 2.16  ? 3030 MET A CE    1 
ATOM   12521 N  N     . THR A 1 3031 ? 219.391 212.603 214.460 1.00 2.94  ? 3031 THR A N     1 
ATOM   12522 C  CA    . THR A 1 3031 ? 219.952 211.362 213.936 1.00 3.51  ? 3031 THR A CA    1 
ATOM   12523 C  C     . THR A 1 3031 ? 220.950 211.640 212.818 1.00 6.20  ? 3031 THR A C     1 
ATOM   12524 O  O     . THR A 1 3031 ? 222.019 211.023 212.764 1.00 7.51  ? 3031 THR A O     1 
ATOM   12525 C  CB    . THR A 1 3031 ? 218.832 210.451 213.436 1.00 5.53  ? 3031 THR A CB    1 
ATOM   12526 O  OG1   . THR A 1 3031 ? 217.901 210.210 214.497 1.00 5.82  ? 3031 THR A OG1   1 
ATOM   12527 C  CG2   . THR A 1 3031 ? 219.395 209.126 212.948 1.00 4.00  ? 3031 THR A CG2   1 
ATOM   12528 N  N     . GLN A 1 3032 ? 220.616 212.566 211.921 1.00 5.03  ? 3032 GLN A N     1 
ATOM   12529 C  CA    . GLN A 1 3032 ? 221.502 212.869 210.801 1.00 3.62  ? 3032 GLN A CA    1 
ATOM   12530 C  C     . GLN A 1 3032 ? 222.744 213.620 211.264 1.00 5.48  ? 3032 GLN A C     1 
ATOM   12531 O  O     . GLN A 1 3032 ? 223.839 213.406 210.730 1.00 6.07  ? 3032 GLN A O     1 
ATOM   12532 C  CB    . GLN A 1 3032 ? 220.737 213.670 209.748 1.00 5.29  ? 3032 GLN A CB    1 
ATOM   12533 C  CG    . GLN A 1 3032 ? 219.629 212.872 209.089 1.00 4.70  ? 3032 GLN A CG    1 
ATOM   12534 C  CD    . GLN A 1 3032 ? 218.850 213.673 208.068 1.00 7.48  ? 3032 GLN A CD    1 
ATOM   12535 O  OE1   . GLN A 1 3032 ? 219.084 214.866 207.884 1.00 11.01 ? 3032 GLN A OE1   1 
ATOM   12536 N  NE2   . GLN A 1 3032 ? 217.912 213.017 207.400 1.00 12.81 ? 3032 GLN A NE2   1 
ATOM   12537 N  N     . CYS A 1 3033 ? 222.596 214.506 212.251 1.00 6.16  ? 3033 CYS A N     1 
ATOM   12538 C  CA    . CYS A 1 3033 ? 223.752 215.221 212.782 1.00 4.22  ? 3033 CYS A CA    1 
ATOM   12539 C  C     . CYS A 1 3033 ? 224.721 214.272 213.472 1.00 5.17  ? 3033 CYS A C     1 
ATOM   12540 O  O     . CYS A 1 3033 ? 225.942 214.424 213.354 1.00 6.13  ? 3033 CYS A O     1 
ATOM   12541 C  CB    . CYS A 1 3033 ? 223.297 216.320 213.742 1.00 4.37  ? 3033 CYS A CB    1 
ATOM   12542 S  SG    . CYS A 1 3033 ? 222.440 217.690 212.948 1.00 17.02 ? 3033 CYS A SG    1 
ATOM   12543 N  N     . LYS A 1 3034 ? 224.196 213.292 214.213 1.00 5.74  ? 3034 LYS A N     1 
ATOM   12544 C  CA    . LYS A 1 3034 ? 225.061 212.304 214.847 1.00 5.93  ? 3034 LYS A CA    1 
ATOM   12545 C  C     . LYS A 1 3034 ? 225.810 211.487 213.803 1.00 7.33  ? 3034 LYS A C     1 
ATOM   12546 O  O     . LYS A 1 3034 ? 227.007 211.214 213.958 1.00 7.27  ? 3034 LYS A O     1 
ATOM   12547 C  CB    . LYS A 1 3034 ? 224.239 211.397 215.761 1.00 9.36  ? 3034 LYS A CB    1 
ATOM   12548 C  CG    . LYS A 1 3034 ? 225.063 210.372 216.514 1.00 8.39  ? 3034 LYS A CG    1 
ATOM   12549 C  CD    . LYS A 1 3034 ? 224.207 209.579 217.480 1.00 9.94  ? 3034 LYS A CD    1 
ATOM   12550 C  CE    . LYS A 1 3034 ? 225.002 208.456 218.124 1.00 19.05 ? 3034 LYS A CE    1 
ATOM   12551 N  NZ    . LYS A 1 3034 ? 226.083 208.984 219.002 1.00 21.67 ? 3034 LYS A NZ    1 
ATOM   12552 N  N     . GLU A 1 3035 ? 225.123 211.087 212.731 1.00 6.24  ? 3035 GLU A N     1 
ATOM   12553 C  CA    . GLU A 1 3035 ? 225.793 210.409 211.626 1.00 6.59  ? 3035 GLU A CA    1 
ATOM   12554 C  C     . GLU A 1 3035 ? 226.793 211.327 210.934 1.00 8.72  ? 3035 GLU A C     1 
ATOM   12555 O  O     . GLU A 1 3035 ? 227.900 210.899 210.586 1.00 11.20 ? 3035 GLU A O     1 
ATOM   12556 C  CB    . GLU A 1 3035 ? 224.760 209.894 210.623 1.00 5.76  ? 3035 GLU A CB    1 
ATOM   12557 C  CG    . GLU A 1 3035 ? 225.357 209.104 209.471 1.00 10.25 ? 3035 GLU A CG    1 
ATOM   12558 C  CD    . GLU A 1 3035 ? 224.306 208.563 208.522 1.00 24.45 ? 3035 GLU A CD    1 
ATOM   12559 O  OE1   . GLU A 1 3035 ? 223.107 208.823 208.752 1.00 28.48 ? 3035 GLU A OE1   1 
ATOM   12560 O  OE2   . GLU A 1 3035 ? 224.680 207.879 207.548 1.00 27.51 ? 3035 GLU A OE2   1 
ATOM   12561 N  N     . GLY A 1 3036 ? 226.419 212.588 210.719 1.00 7.47  ? 3036 GLY A N     1 
ATOM   12562 C  CA    . GLY A 1 3036 ? 227.310 213.507 210.031 1.00 5.94  ? 3036 GLY A CA    1 
ATOM   12563 C  C     . GLY A 1 3036 ? 228.560 213.829 210.825 1.00 7.19  ? 3036 GLY A C     1 
ATOM   12564 O  O     . GLY A 1 3036 ? 229.659 213.897 210.270 1.00 13.83 ? 3036 GLY A O     1 
ATOM   12565 N  N     . ALA A 1 3037 ? 228.411 214.041 212.134 1.00 5.92  ? 3037 ALA A N     1 
ATOM   12566 C  CA    . ALA A 1 3037 ? 229.568 214.346 212.967 1.00 5.74  ? 3037 ALA A CA    1 
ATOM   12567 C  C     . ALA A 1 3037 ? 230.489 213.141 213.114 1.00 13.48 ? 3037 ALA A C     1 
ATOM   12568 O  O     . ALA A 1 3037 ? 231.703 213.310 213.272 1.00 17.40 ? 3037 ALA A O     1 
ATOM   12569 C  CB    . ALA A 1 3037 ? 229.112 214.843 214.338 1.00 5.90  ? 3037 ALA A CB    1 
ATOM   12570 N  N     . GLN A 1 3038 ? 229.935 211.927 213.070 1.00 14.70 ? 3038 GLN A N     1 
ATOM   12571 C  CA    . GLN A 1 3038 ? 230.764 210.727 213.144 1.00 16.40 ? 3038 GLN A CA    1 
ATOM   12572 C  C     . GLN A 1 3038 ? 231.707 210.630 211.950 1.00 17.77 ? 3038 GLN A C     1 
ATOM   12573 O  O     . GLN A 1 3038 ? 232.878 210.266 212.105 1.00 18.09 ? 3038 GLN A O     1 
ATOM   12574 C  CB    . GLN A 1 3038 ? 229.880 209.484 213.231 1.00 15.46 ? 3038 GLN A CB    1 
ATOM   12575 C  CG    . GLN A 1 3038 ? 230.646 208.184 213.382 1.00 22.91 ? 3038 GLN A CG    1 
ATOM   12576 C  CD    . GLN A 1 3038 ? 231.463 208.132 214.655 1.00 28.61 ? 3038 GLN A CD    1 
ATOM   12577 O  OE1   . GLN A 1 3038 ? 232.685 208.275 214.628 1.00 27.50 ? 3038 GLN A OE1   1 
ATOM   12578 N  NE2   . GLN A 1 3038 ? 230.789 207.926 215.781 1.00 26.02 ? 3038 GLN A NE2   1 
ATOM   12579 N  N     . LYS A 1 3039 ? 231.215 210.959 210.754 1.00 15.60 ? 3039 LYS A N     1 
ATOM   12580 C  CA    . LYS A 1 3039 ? 232.057 210.935 209.565 1.00 14.70 ? 3039 LYS A CA    1 
ATOM   12581 C  C     . LYS A 1 3039 ? 233.181 211.960 209.633 1.00 21.81 ? 3039 LYS A C     1 
ATOM   12582 O  O     . LYS A 1 3039 ? 234.159 211.841 208.885 1.00 24.63 ? 3039 LYS A O     1 
ATOM   12583 C  CB    . LYS A 1 3039 ? 231.203 211.178 208.319 1.00 10.35 ? 3039 LYS A CB    1 
ATOM   12584 C  CG    . LYS A 1 3039 ? 230.404 209.964 207.876 1.00 17.12 ? 3039 LYS A CG    1 
ATOM   12585 C  CD    . LYS A 1 3039 ? 229.285 210.338 206.913 1.00 17.28 ? 3039 LYS A CD    1 
ATOM   12586 C  CE    . LYS A 1 3039 ? 229.743 211.351 205.874 1.00 18.39 ? 3039 LYS A CE    1 
ATOM   12587 N  NZ    . LYS A 1 3039 ? 230.853 210.831 205.029 1.00 20.14 ? 3039 LYS A NZ    1 
ATOM   12588 N  N     . GLU A 1 3040 ? 233.061 212.959 210.502 1.00 21.53 ? 3040 GLU A N     1 
ATOM   12589 C  CA    . GLU A 1 3040 ? 234.088 213.971 210.699 1.00 18.29 ? 3040 GLU A CA    1 
ATOM   12590 C  C     . GLU A 1 3040 ? 235.047 213.616 211.829 1.00 22.70 ? 3040 GLU A C     1 
ATOM   12591 O  O     . GLU A 1 3040 ? 236.028 214.335 212.045 1.00 28.77 ? 3040 GLU A O     1 
ATOM   12592 C  CB    . GLU A 1 3040 ? 233.426 215.327 210.969 1.00 17.58 ? 3040 GLU A CB    1 
ATOM   12593 C  CG    . GLU A 1 3040 ? 234.311 216.540 210.738 1.00 20.10 ? 3040 GLU A CG    1 
ATOM   12594 C  CD    . GLU A 1 3040 ? 233.511 217.826 210.631 1.00 21.45 ? 3040 GLU A CD    1 
ATOM   12595 O  OE1   . GLU A 1 3040 ? 233.588 218.658 211.561 1.00 12.20 ? 3040 GLU A OE1   1 
ATOM   12596 O  OE2   . GLU A 1 3040 ? 232.800 217.999 209.620 1.00 18.60 ? 3040 GLU A OE2   1 
ATOM   12597 N  N     . GLY A 1 3041 ? 234.793 212.524 212.545 1.00 19.72 ? 3041 GLY A N     1 
ATOM   12598 C  CA    . GLY A 1 3041 ? 235.654 212.106 213.631 1.00 18.53 ? 3041 GLY A CA    1 
ATOM   12599 C  C     . GLY A 1 3041 ? 235.404 212.783 214.960 1.00 21.98 ? 3041 GLY A C     1 
ATOM   12600 O  O     . GLY A 1 3041 ? 236.226 212.641 215.871 1.00 29.32 ? 3041 GLY A O     1 
ATOM   12601 N  N     . LEU A 1 3042 ? 234.302 213.512 215.104 1.00 21.94 ? 3042 LEU A N     1 
ATOM   12602 C  CA    . LEU A 1 3042 ? 233.994 214.196 216.351 1.00 23.17 ? 3042 LEU A CA    1 
ATOM   12603 C  C     . LEU A 1 3042 ? 233.170 213.299 217.262 1.00 27.34 ? 3042 LEU A C     1 
ATOM   12604 O  O     . LEU A 1 3042 ? 232.317 212.536 216.800 1.00 27.83 ? 3042 LEU A O     1 
ATOM   12605 C  CB    . LEU A 1 3042 ? 233.242 215.501 216.085 1.00 14.56 ? 3042 LEU A CB    1 
ATOM   12606 C  CG    . LEU A 1 3042 ? 233.841 216.421 215.022 1.00 17.17 ? 3042 LEU A CG    1 
ATOM   12607 C  CD1   . LEU A 1 3042 ? 233.095 217.743 214.991 1.00 23.93 ? 3042 LEU A CD1   1 
ATOM   12608 C  CD2   . LEU A 1 3042 ? 235.320 216.647 215.278 1.00 17.91 ? 3042 LEU A CD2   1 
ATOM   12609 N  N     . MET A 1 3043 ? 233.435 213.394 218.564 1.00 24.05 ? 3043 MET A N     1 
ATOM   12610 C  CA    . MET A 1 3043 ? 232.720 212.608 219.569 1.00 23.20 ? 3043 MET A CA    1 
ATOM   12611 C  C     . MET A 1 3043 ? 231.592 213.466 220.127 1.00 24.34 ? 3043 MET A C     1 
ATOM   12612 O  O     . MET A 1 3043 ? 231.772 214.229 221.075 1.00 28.59 ? 3043 MET A O     1 
ATOM   12613 C  CB    . MET A 1 3043 ? 233.673 212.144 220.661 1.00 25.87 ? 3043 MET A CB    1 
ATOM   12614 C  CG    . MET A 1 3043 ? 234.720 211.149 220.185 1.00 28.08 ? 3043 MET A CG    1 
ATOM   12615 S  SD    . MET A 1 3043 ? 235.790 210.571 221.514 1.00 57.69 ? 3043 MET A SD    1 
ATOM   12616 C  CE    . MET A 1 3043 ? 236.819 212.014 221.771 1.00 32.14 ? 3043 MET A CE    1 
ATOM   12617 N  N     . LEU A 1 3044 ? 230.409 213.340 219.530 1.00 18.45 ? 3044 LEU A N     1 
ATOM   12618 C  CA    . LEU A 1 3044 ? 229.244 214.120 219.929 1.00 14.78 ? 3044 LEU A CA    1 
ATOM   12619 C  C     . LEU A 1 3044 ? 228.049 213.197 220.113 1.00 15.77 ? 3044 LEU A C     1 
ATOM   12620 O  O     . LEU A 1 3044 ? 227.744 212.388 219.232 1.00 13.46 ? 3044 LEU A O     1 
ATOM   12621 C  CB    . LEU A 1 3044 ? 228.918 215.198 218.893 1.00 12.26 ? 3044 LEU A CB    1 
ATOM   12622 C  CG    . LEU A 1 3044 ? 229.964 216.290 218.679 1.00 13.32 ? 3044 LEU A CG    1 
ATOM   12623 C  CD1   . LEU A 1 3044 ? 229.524 217.236 217.577 1.00 11.04 ? 3044 LEU A CD1   1 
ATOM   12624 C  CD2   . LEU A 1 3044 ? 230.227 217.050 219.968 1.00 10.54 ? 3044 LEU A CD2   1 
ATOM   12625 N  N     . ASP A 1 3045 ? 227.379 213.320 221.257 1.00 19.20 ? 3045 ASP A N     1 
ATOM   12626 C  CA    . ASP A 1 3045 ? 226.185 212.531 221.529 1.00 20.49 ? 3045 ASP A CA    1 
ATOM   12627 C  C     . ASP A 1 3045 ? 225.056 213.412 222.047 1.00 17.37 ? 3045 ASP A C     1 
ATOM   12628 O  O     . ASP A 1 3045 ? 223.876 213.099 221.851 1.00 23.35 ? 3045 ASP A O     1 
ATOM   12629 C  CB    . ASP A 1 3045 ? 226.497 211.420 222.534 1.00 25.38 ? 3045 ASP A CB    1 
ATOM   12630 C  CG    . ASP A 1 3045 ? 225.300 210.535 222.812 1.00 33.09 ? 3045 ASP A CG    1 
ATOM   12631 O  OD1   . ASP A 1 3045 ? 224.802 209.893 221.865 1.00 23.80 ? 3045 ASP A OD1   1 
ATOM   12632 O  OD2   . ASP A 1 3045 ? 224.855 210.487 223.978 1.00 36.01 ? 3045 ASP A OD2   1 
ATOM   12633 N  N     . SER A 1 3046 ? 225.407 214.513 222.705 1.00 14.58 ? 3046 SER A N     1 
ATOM   12634 C  CA    . SER A 1 3046 ? 224.404 215.426 223.236 1.00 7.63  ? 3046 SER A CA    1 
ATOM   12635 C  C     . SER A 1 3046 ? 223.678 216.144 222.106 1.00 10.95 ? 3046 SER A C     1 
ATOM   12636 O  O     . SER A 1 3046 ? 224.284 216.533 221.107 1.00 13.78 ? 3046 SER A O     1 
ATOM   12637 C  CB    . SER A 1 3046 ? 225.058 216.441 224.172 1.00 8.85  ? 3046 SER A CB    1 
ATOM   12638 O  OG    . SER A 1 3046 ? 224.179 217.512 224.463 1.00 13.00 ? 3046 SER A OG    1 
ATOM   12639 N  N     . HIS A 1 3047 ? 222.365 216.318 222.272 1.00 11.77 ? 3047 HIS A N     1 
ATOM   12640 C  CA    . HIS A 1 3047 ? 221.582 217.029 221.266 1.00 7.48  ? 3047 HIS A CA    1 
ATOM   12641 C  C     . HIS A 1 3047 ? 222.036 218.477 221.135 1.00 8.45  ? 3047 HIS A C     1 
ATOM   12642 O  O     . HIS A 1 3047 ? 222.121 219.011 220.023 1.00 13.17 ? 3047 HIS A O     1 
ATOM   12643 C  CB    . HIS A 1 3047 ? 220.095 216.963 221.606 1.00 4.57  ? 3047 HIS A CB    1 
ATOM   12644 C  CG    . HIS A 1 3047 ? 219.436 215.687 221.187 1.00 10.36 ? 3047 HIS A CG    1 
ATOM   12645 N  ND1   . HIS A 1 3047 ? 218.070 215.512 221.219 1.00 10.48 ? 3047 HIS A ND1   1 
ATOM   12646 C  CD2   . HIS A 1 3047 ? 219.954 214.523 220.731 1.00 10.91 ? 3047 HIS A CD2   1 
ATOM   12647 C  CE1   . HIS A 1 3047 ? 217.775 214.295 220.798 1.00 9.99  ? 3047 HIS A CE1   1 
ATOM   12648 N  NE2   . HIS A 1 3047 ? 218.901 213.674 220.495 1.00 10.21 ? 3047 HIS A NE2   1 
ATOM   12649 N  N     . GLU A 1 3048 ? 222.321 219.133 222.262 1.00 10.08 ? 3048 GLU A N     1 
ATOM   12650 C  CA    . GLU A 1 3048 ? 222.820 220.503 222.217 1.00 5.58  ? 3048 GLU A CA    1 
ATOM   12651 C  C     . GLU A 1 3048 ? 224.166 220.572 221.509 1.00 6.52  ? 3048 GLU A C     1 
ATOM   12652 O  O     . GLU A 1 3048 ? 224.404 221.473 220.697 1.00 7.01  ? 3048 GLU A O     1 
ATOM   12653 C  CB    . GLU A 1 3048 ? 222.927 221.073 223.632 1.00 6.41  ? 3048 GLU A CB    1 
ATOM   12654 C  CG    . GLU A 1 3048 ? 221.601 221.435 224.294 1.00 14.98 ? 3048 GLU A CG    1 
ATOM   12655 C  CD    . GLU A 1 3048 ? 220.670 220.249 224.479 1.00 19.88 ? 3048 GLU A CD    1 
ATOM   12656 O  OE1   . GLU A 1 3048 ? 220.962 219.382 225.328 1.00 19.68 ? 3048 GLU A OE1   1 
ATOM   12657 O  OE2   . GLU A 1 3048 ? 219.638 220.191 223.777 1.00 15.38 ? 3048 GLU A OE2   1 
ATOM   12658 N  N     . GLU A 1 3049 ? 225.059 219.625 221.806 1.00 7.57  ? 3049 GLU A N     1 
ATOM   12659 C  CA    . GLU A 1 3049 ? 226.347 219.580 221.123 1.00 5.57  ? 3049 GLU A CA    1 
ATOM   12660 C  C     . GLU A 1 3049 ? 226.175 219.295 219.637 1.00 6.09  ? 3049 GLU A C     1 
ATOM   12661 O  O     . GLU A 1 3049 ? 226.892 219.860 218.802 1.00 7.23  ? 3049 GLU A O     1 
ATOM   12662 C  CB    . GLU A 1 3049 ? 227.246 218.530 221.769 1.00 7.38  ? 3049 GLU A CB    1 
ATOM   12663 C  CG    . GLU A 1 3049 ? 228.082 219.053 222.916 1.00 10.88 ? 3049 GLU A CG    1 
ATOM   12664 C  CD    . GLU A 1 3049 ? 228.646 217.939 223.772 1.00 21.87 ? 3049 GLU A CD    1 
ATOM   12665 O  OE1   . GLU A 1 3049 ? 228.453 217.978 225.005 1.00 22.15 ? 3049 GLU A OE1   1 
ATOM   12666 O  OE2   . GLU A 1 3049 ? 229.284 217.025 223.208 1.00 23.07 ? 3049 GLU A OE2   1 
ATOM   12667 N  N     . LEU A 1 3050 ? 225.236 218.413 219.290 1.00 7.10  ? 3050 LEU A N     1 
ATOM   12668 C  CA    . LEU A 1 3050 ? 224.970 218.127 217.885 1.00 4.02  ? 3050 LEU A CA    1 
ATOM   12669 C  C     . LEU A 1 3050 ? 224.431 219.352 217.160 1.00 2.64  ? 3050 LEU A C     1 
ATOM   12670 O  O     . LEU A 1 3050 ? 224.805 219.618 216.014 1.00 3.51  ? 3050 LEU A O     1 
ATOM   12671 C  CB    . LEU A 1 3050 ? 223.993 216.958 217.762 1.00 6.02  ? 3050 LEU A CB    1 
ATOM   12672 C  CG    . LEU A 1 3050 ? 224.550 215.562 218.038 1.00 9.19  ? 3050 LEU A CG    1 
ATOM   12673 C  CD1   . LEU A 1 3050 ? 223.443 214.528 217.961 1.00 8.33  ? 3050 LEU A CD1   1 
ATOM   12674 C  CD2   . LEU A 1 3050 ? 225.669 215.227 217.070 1.00 7.14  ? 3050 LEU A CD2   1 
ATOM   12675 N  N     . TYR A 1 3051 ? 223.548 220.110 217.814 1.00 2.77  ? 3051 TYR A N     1 
ATOM   12676 C  CA    . TYR A 1 3051 ? 222.951 221.273 217.166 1.00 1.46  ? 3051 TYR A CA    1 
ATOM   12677 C  C     . TYR A 1 3051 ? 223.978 222.379 216.949 1.00 2.46  ? 3051 TYR A C     1 
ATOM   12678 O  O     . TYR A 1 3051 ? 223.928 223.084 215.935 1.00 2.71  ? 3051 TYR A O     1 
ATOM   12679 C  CB    . TYR A 1 3051 ? 221.766 221.782 217.987 1.00 1.34  ? 3051 TYR A CB    1 
ATOM   12680 C  CG    . TYR A 1 3051 ? 220.878 222.740 217.228 1.00 3.02  ? 3051 TYR A CG    1 
ATOM   12681 C  CD1   . TYR A 1 3051 ? 219.893 222.272 216.370 1.00 3.33  ? 3051 TYR A CD1   1 
ATOM   12682 C  CD2   . TYR A 1 3051 ? 221.027 224.114 217.366 1.00 4.53  ? 3051 TYR A CD2   1 
ATOM   12683 C  CE1   . TYR A 1 3051 ? 219.083 223.143 215.668 1.00 3.53  ? 3051 TYR A CE1   1 
ATOM   12684 C  CE2   . TYR A 1 3051 ? 220.221 224.991 216.671 1.00 3.98  ? 3051 TYR A CE2   1 
ATOM   12685 C  CZ    . TYR A 1 3051 ? 219.252 224.502 215.825 1.00 5.03  ? 3051 TYR A CZ    1 
ATOM   12686 O  OH    . TYR A 1 3051 ? 218.447 225.376 215.133 1.00 11.76 ? 3051 TYR A OH    1 
ATOM   12687 N  N     . LYS A 1 3052 ? 224.907 222.556 217.892 1.00 2.85  ? 3052 LYS A N     1 
ATOM   12688 C  CA    . LYS A 1 3052 ? 225.969 223.542 217.700 1.00 1.60  ? 3052 LYS A CA    1 
ATOM   12689 C  C     . LYS A 1 3052 ? 226.870 223.166 216.530 1.00 1.85  ? 3052 LYS A C     1 
ATOM   12690 O  O     . LYS A 1 3052 ? 227.261 224.031 215.737 1.00 2.35  ? 3052 LYS A O     1 
ATOM   12691 C  CB    . LYS A 1 3052 ? 226.793 223.697 218.978 1.00 3.43  ? 3052 LYS A CB    1 
ATOM   12692 C  CG    . LYS A 1 3052 ? 226.037 224.294 220.148 1.00 3.81  ? 3052 LYS A CG    1 
ATOM   12693 C  CD    . LYS A 1 3052 ? 226.931 224.425 221.369 1.00 6.27  ? 3052 LYS A CD    1 
ATOM   12694 C  CE    . LYS A 1 3052 ? 226.207 225.107 222.518 1.00 15.88 ? 3052 LYS A CE    1 
ATOM   12695 N  NZ    . LYS A 1 3052 ? 225.090 224.281 223.051 1.00 19.39 ? 3052 LYS A NZ    1 
ATOM   12696 N  N     . TRP A 1 3053 ? 227.220 221.884 216.413 1.00 1.97  ? 3053 TRP A N     1 
ATOM   12697 C  CA    . TRP A 1 3053 ? 228.019 221.439 215.276 1.00 0.93  ? 3053 TRP A CA    1 
ATOM   12698 C  C     . TRP A 1 3053 ? 227.256 221.619 213.972 1.00 1.28  ? 3053 TRP A C     1 
ATOM   12699 O  O     . TRP A 1 3053 ? 227.836 222.006 212.951 1.00 1.13  ? 3053 TRP A O     1 
ATOM   12700 C  CB    . TRP A 1 3053 ? 228.429 219.979 215.464 1.00 0.94  ? 3053 TRP A CB    1 
ATOM   12701 C  CG    . TRP A 1 3053 ? 229.028 219.360 214.241 1.00 1.43  ? 3053 TRP A CG    1 
ATOM   12702 C  CD1   . TRP A 1 3053 ? 230.334 219.402 213.861 1.00 1.27  ? 3053 TRP A CD1   1 
ATOM   12703 C  CD2   . TRP A 1 3053 ? 228.341 218.609 213.232 1.00 1.37  ? 3053 TRP A CD2   1 
ATOM   12704 N  NE1   . TRP A 1 3053 ? 230.507 218.722 212.683 1.00 2.93  ? 3053 TRP A NE1   1 
ATOM   12705 C  CE2   . TRP A 1 3053 ? 229.298 218.226 212.274 1.00 1.74  ? 3053 TRP A CE2   1 
ATOM   12706 C  CE3   . TRP A 1 3053 ? 227.010 218.225 213.047 1.00 1.34  ? 3053 TRP A CE3   1 
ATOM   12707 C  CZ2   . TRP A 1 3053 ? 228.968 217.478 211.148 1.00 1.70  ? 3053 TRP A CZ2   1 
ATOM   12708 C  CZ3   . TRP A 1 3053 ? 226.685 217.484 211.930 1.00 2.37  ? 3053 TRP A CZ3   1 
ATOM   12709 C  CH2   . TRP A 1 3053 ? 227.659 217.118 210.994 1.00 2.62  ? 3053 TRP A CH2   1 
ATOM   12710 N  N     . PHE A 1 3054 ? 225.952 221.342 213.992 1.00 0.90  ? 3054 PHE A N     1 
ATOM   12711 C  CA    . PHE A 1 3054 ? 225.115 221.543 212.814 1.00 0.88  ? 3054 PHE A CA    1 
ATOM   12712 C  C     . PHE A 1 3054 ? 225.069 223.012 212.411 1.00 0.79  ? 3054 PHE A C     1 
ATOM   12713 O  O     . PHE A 1 3054 ? 225.107 223.338 211.218 1.00 0.85  ? 3054 PHE A O     1 
ATOM   12714 C  CB    . PHE A 1 3054 ? 223.714 220.996 213.096 1.00 0.57  ? 3054 PHE A CB    1 
ATOM   12715 C  CG    . PHE A 1 3054 ? 222.678 221.389 212.087 1.00 0.38  ? 3054 PHE A CG    1 
ATOM   12716 C  CD1   . PHE A 1 3054 ? 222.579 220.720 210.880 1.00 0.75  ? 3054 PHE A CD1   1 
ATOM   12717 C  CD2   . PHE A 1 3054 ? 221.766 222.390 212.369 1.00 0.65  ? 3054 PHE A CD2   1 
ATOM   12718 C  CE1   . PHE A 1 3054 ? 221.614 221.069 209.959 1.00 0.40  ? 3054 PHE A CE1   1 
ATOM   12719 C  CE2   . PHE A 1 3054 ? 220.796 222.741 211.451 1.00 0.54  ? 3054 PHE A CE2   1 
ATOM   12720 C  CZ    . PHE A 1 3054 ? 220.721 222.079 210.245 1.00 0.39  ? 3054 PHE A CZ    1 
ATOM   12721 N  N     . THR A 1 3055 ? 224.988 223.913 213.389 1.00 0.69  ? 3055 THR A N     1 
ATOM   12722 C  CA    . THR A 1 3055 ? 225.032 225.341 213.092 1.00 0.96  ? 3055 THR A CA    1 
ATOM   12723 C  C     . THR A 1 3055 ? 226.380 225.740 212.504 1.00 0.79  ? 3055 THR A C     1 
ATOM   12724 O  O     . THR A 1 3055 ? 226.445 226.532 211.557 1.00 0.80  ? 3055 THR A O     1 
ATOM   12725 C  CB    . THR A 1 3055 ? 224.740 226.148 214.358 1.00 1.78  ? 3055 THR A CB    1 
ATOM   12726 O  OG1   . THR A 1 3055 ? 223.467 225.761 214.886 1.00 4.51  ? 3055 THR A OG1   1 
ATOM   12727 C  CG2   . THR A 1 3055 ? 224.726 227.636 214.055 1.00 1.59  ? 3055 THR A CG2   1 
ATOM   12728 N  N     . SER A 1 3056 ? 227.469 225.198 213.051 1.00 0.78  ? 3056 SER A N     1 
ATOM   12729 C  CA    . SER A 1 3056 ? 228.797 225.539 212.555 1.00 0.90  ? 3056 SER A CA    1 
ATOM   12730 C  C     . SER A 1 3056 ? 228.999 225.046 211.127 1.00 0.69  ? 3056 SER A C     1 
ATOM   12731 O  O     . SER A 1 3056 ? 229.726 225.668 210.344 1.00 0.62  ? 3056 SER A O     1 
ATOM   12732 C  CB    . SER A 1 3056 ? 229.867 224.968 213.487 1.00 0.93  ? 3056 SER A CB    1 
ATOM   12733 O  OG    . SER A 1 3056 ? 229.842 223.553 213.496 1.00 1.62  ? 3056 SER A OG    1 
ATOM   12734 N  N     . GLN A 1 3057 ? 228.374 223.921 210.774 1.00 0.75  ? 3057 GLN A N     1 
ATOM   12735 C  CA    . GLN A 1 3057 ? 228.458 223.429 209.402 1.00 0.68  ? 3057 GLN A CA    1 
ATOM   12736 C  C     . GLN A 1 3057 ? 227.673 224.316 208.445 1.00 0.62  ? 3057 GLN A C     1 
ATOM   12737 O  O     . GLN A 1 3057 ? 228.139 224.603 207.337 1.00 1.32  ? 3057 GLN A O     1 
ATOM   12738 C  CB    . GLN A 1 3057 ? 227.960 221.985 209.332 1.00 1.18  ? 3057 GLN A CB    1 
ATOM   12739 C  CG    . GLN A 1 3057 ? 228.829 220.992 210.084 1.00 0.82  ? 3057 GLN A CG    1 
ATOM   12740 C  CD    . GLN A 1 3057 ? 230.102 220.647 209.338 1.00 2.03  ? 3057 GLN A CD    1 
ATOM   12741 O  OE1   . GLN A 1 3057 ? 231.202 220.897 209.821 1.00 3.27  ? 3057 GLN A OE1   1 
ATOM   12742 N  NE2   . GLN A 1 3057 ? 229.955 220.060 208.159 1.00 3.18  ? 3057 GLN A NE2   1 
ATOM   12743 N  N     . VAL A 1 3058 ? 226.483 224.758 208.855 1.00 0.43  ? 3058 VAL A N     1 
ATOM   12744 C  CA    . VAL A 1 3058 ? 225.692 225.659 208.021 1.00 0.39  ? 3058 VAL A CA    1 
ATOM   12745 C  C     . VAL A 1 3058 ? 226.430 226.974 207.816 1.00 0.65  ? 3058 VAL A C     1 
ATOM   12746 O  O     . VAL A 1 3058 ? 226.393 227.565 206.730 1.00 0.81  ? 3058 VAL A O     1 
ATOM   12747 C  CB    . VAL A 1 3058 ? 224.300 225.879 208.645 1.00 0.41  ? 3058 VAL A CB    1 
ATOM   12748 C  CG1   . VAL A 1 3058 ? 223.563 227.011 207.940 1.00 0.31  ? 3058 VAL A CG1   1 
ATOM   12749 C  CG2   . VAL A 1 3058 ? 223.486 224.599 208.597 1.00 0.53  ? 3058 VAL A CG2   1 
ATOM   12750 N  N     . ILE A 1 3059 ? 227.128 227.441 208.853 1.00 0.59  ? 3059 ILE A N     1 
ATOM   12751 C  CA    . ILE A 1 3059 ? 227.869 228.696 208.762 1.00 0.77  ? 3059 ILE A CA    1 
ATOM   12752 C  C     . ILE A 1 3059 ? 228.953 228.606 207.696 1.00 0.84  ? 3059 ILE A C     1 
ATOM   12753 O  O     . ILE A 1 3059 ? 229.142 229.537 206.904 1.00 1.12  ? 3059 ILE A O     1 
ATOM   12754 C  CB    . ILE A 1 3059 ? 228.446 229.066 210.142 1.00 1.05  ? 3059 ILE A CB    1 
ATOM   12755 C  CG1   . ILE A 1 3059 ? 227.354 229.678 211.023 1.00 0.93  ? 3059 ILE A CG1   1 
ATOM   12756 C  CG2   . ILE A 1 3059 ? 229.641 229.997 210.010 1.00 1.45  ? 3059 ILE A CG2   1 
ATOM   12757 C  CD1   . ILE A 1 3059 ? 227.844 230.150 212.364 1.00 1.11  ? 3059 ILE A CD1   1 
ATOM   12758 N  N     . ARG A 1 3060 ? 229.668 227.486 207.643 1.00 0.86  ? 3060 ARG A N     1 
ATOM   12759 C  CA    . ARG A 1 3060 ? 230.787 227.352 206.721 1.00 1.23  ? 3060 ARG A CA    1 
ATOM   12760 C  C     . ARG A 1 3060 ? 230.386 226.869 205.331 1.00 1.00  ? 3060 ARG A C     1 
ATOM   12761 O  O     . ARG A 1 3060 ? 231.131 227.113 204.376 1.00 1.74  ? 3060 ARG A O     1 
ATOM   12762 C  CB    . ARG A 1 3060 ? 231.838 226.403 207.305 1.00 0.83  ? 3060 ARG A CB    1 
ATOM   12763 C  CG    . ARG A 1 3060 ? 231.358 224.980 207.494 1.00 2.13  ? 3060 ARG A CG    1 
ATOM   12764 C  CD    . ARG A 1 3060 ? 232.409 224.127 208.187 1.00 4.91  ? 3060 ARG A CD    1 
ATOM   12765 N  NE    . ARG A 1 3060 ? 233.640 224.039 207.413 1.00 3.97  ? 3060 ARG A NE    1 
ATOM   12766 C  CZ    . ARG A 1 3060 ? 233.881 223.109 206.499 1.00 4.70  ? 3060 ARG A CZ    1 
ATOM   12767 N  NH1   . ARG A 1 3060 ? 232.996 222.167 206.222 1.00 3.42  ? 3060 ARG A NH1   1 
ATOM   12768 N  NH2   . ARG A 1 3060 ? 235.040 223.126 205.846 1.00 8.50  ? 3060 ARG A NH2   1 
ATOM   12769 N  N     . ASN A 1 3061 ? 229.236 226.213 205.182 1.00 0.66  ? 3061 ASN A N     1 
ATOM   12770 C  CA    . ASN A 1 3061 ? 228.870 225.606 203.909 1.00 0.61  ? 3061 ASN A CA    1 
ATOM   12771 C  C     . ASN A 1 3061 ? 227.752 226.317 203.167 1.00 0.60  ? 3061 ASN A C     1 
ATOM   12772 O  O     . ASN A 1 3061 ? 227.767 226.334 201.935 1.00 1.08  ? 3061 ASN A O     1 
ATOM   12773 C  CB    . ASN A 1 3061 ? 228.463 224.141 204.110 1.00 0.93  ? 3061 ASN A CB    1 
ATOM   12774 C  CG    . ASN A 1 3061 ? 229.636 223.254 204.461 1.00 1.36  ? 3061 ASN A CG    1 
ATOM   12775 O  OD1   . ASN A 1 3061 ? 230.712 223.376 203.882 1.00 5.55  ? 3061 ASN A OD1   1 
ATOM   12776 N  ND2   . ASN A 1 3061 ? 229.428 222.342 205.398 1.00 1.18  ? 3061 ASN A ND2   1 
ATOM   12777 N  N     . LEU A 1 3062 ? 226.785 226.899 203.868 1.00 0.35  ? 3062 LEU A N     1 
ATOM   12778 C  CA    . LEU A 1 3062 ? 225.633 227.496 203.204 1.00 0.19  ? 3062 LEU A CA    1 
ATOM   12779 C  C     . LEU A 1 3062 ? 225.965 228.917 202.765 1.00 0.09  ? 3062 LEU A C     1 
ATOM   12780 O  O     . LEU A 1 3062 ? 226.356 229.755 203.581 1.00 0.43  ? 3062 LEU A O     1 
ATOM   12781 C  CB    . LEU A 1 3062 ? 224.418 227.484 204.127 1.00 0.22  ? 3062 LEU A CB    1 
ATOM   12782 C  CG    . LEU A 1 3062 ? 223.151 228.118 203.552 1.00 0.16  ? 3062 LEU A CG    1 
ATOM   12783 C  CD1   . LEU A 1 3062 ? 222.799 227.496 202.209 1.00 0.20  ? 3062 LEU A CD1   1 
ATOM   12784 C  CD2   . LEU A 1 3062 ? 221.998 227.984 204.524 1.00 0.23  ? 3062 LEU A CD2   1 
ATOM   12785 N  N     . HIS A 1 3063 ? 225.814 229.180 201.470 1.00 0.20  ? 3063 HIS A N     1 
ATOM   12786 C  CA    . HIS A 1 3063 ? 226.000 230.504 200.898 1.00 0.12  ? 3063 HIS A CA    1 
ATOM   12787 C  C     . HIS A 1 3063 ? 224.679 230.955 200.297 1.00 0.09  ? 3063 HIS A C     1 
ATOM   12788 O  O     . HIS A 1 3063 ? 224.081 230.232 199.494 1.00 0.35  ? 3063 HIS A O     1 
ATOM   12789 C  CB    . HIS A 1 3063 ? 227.093 230.499 199.826 1.00 0.10  ? 3063 HIS A CB    1 
ATOM   12790 C  CG    . HIS A 1 3063 ? 228.458 230.185 200.353 1.00 0.10  ? 3063 HIS A CG    1 
ATOM   12791 N  ND1   . HIS A 1 3063 ? 229.352 231.162 200.729 1.00 0.20  ? 3063 HIS A ND1   1 
ATOM   12792 C  CD2   . HIS A 1 3063 ? 229.081 229.002 200.563 1.00 0.17  ? 3063 HIS A CD2   1 
ATOM   12793 C  CE1   . HIS A 1 3063 ? 230.468 230.595 201.151 1.00 0.47  ? 3063 HIS A CE1   1 
ATOM   12794 N  NE2   . HIS A 1 3063 ? 230.328 229.285 201.061 1.00 0.22  ? 3063 HIS A NE2   1 
ATOM   12795 N  N     . VAL A 1 3064 ? 224.224 232.139 200.685 1.00 0.11  ? 3064 VAL A N     1 
ATOM   12796 C  CA    . VAL A 1 3064 ? 222.963 232.687 200.206 1.00 0.19  ? 3064 VAL A CA    1 
ATOM   12797 C  C     . VAL A 1 3064 ? 223.280 233.827 199.253 1.00 0.08  ? 3064 VAL A C     1 
ATOM   12798 O  O     . VAL A 1 3064 ? 224.024 234.751 199.602 1.00 0.07  ? 3064 VAL A O     1 
ATOM   12799 C  CB    . VAL A 1 3064 ? 222.071 233.159 201.363 1.00 0.27  ? 3064 VAL A CB    1 
ATOM   12800 C  CG1   . VAL A 1 3064 ? 220.907 233.984 200.833 1.00 0.05  ? 3064 VAL A CG1   1 
ATOM   12801 C  CG2   . VAL A 1 3064 ? 221.569 231.967 202.158 1.00 0.30  ? 3064 VAL A CG2   1 
ATOM   12802 N  N     . VAL A 1 3065 ? 222.731 233.753 198.047 1.00 0.14  ? 3065 VAL A N     1 
ATOM   12803 C  CA    . VAL A 1 3065 ? 222.835 234.822 197.064 1.00 0.11  ? 3065 VAL A CA    1 
ATOM   12804 C  C     . VAL A 1 3065 ? 221.449 235.423 196.893 1.00 0.08  ? 3065 VAL A C     1 
ATOM   12805 O  O     . VAL A 1 3065 ? 220.516 234.738 196.459 1.00 0.24  ? 3065 VAL A O     1 
ATOM   12806 C  CB    . VAL A 1 3065 ? 223.392 234.316 195.725 1.00 0.10  ? 3065 VAL A CB    1 
ATOM   12807 C  CG1   . VAL A 1 3065 ? 223.512 235.463 194.736 1.00 0.06  ? 3065 VAL A CG1   1 
ATOM   12808 C  CG2   . VAL A 1 3065 ? 224.734 233.636 195.932 1.00 0.05  ? 3065 VAL A CG2   1 
ATOM   12809 N  N     . PHE A 1 3066 ? 221.315 236.696 197.240 1.00 0.04  ? 3066 PHE A N     1 
ATOM   12810 C  CA    . PHE A 1 3066 ? 220.067 237.432 197.093 1.00 0.19  ? 3066 PHE A CA    1 
ATOM   12811 C  C     . PHE A 1 3066 ? 220.178 238.360 195.893 1.00 0.25  ? 3066 PHE A C     1 
ATOM   12812 O  O     . PHE A 1 3066 ? 221.097 239.180 195.823 1.00 0.19  ? 3066 PHE A O     1 
ATOM   12813 C  CB    . PHE A 1 3066 ? 219.742 238.223 198.359 1.00 0.79  ? 3066 PHE A CB    1 
ATOM   12814 C  CG    . PHE A 1 3066 ? 218.274 238.379 198.613 1.00 2.95  ? 3066 PHE A CG    1 
ATOM   12815 C  CD1   . PHE A 1 3066 ? 217.530 237.344 199.150 1.00 3.74  ? 3066 PHE A CD1   1 
ATOM   12816 C  CD2   . PHE A 1 3066 ? 217.632 239.565 198.296 1.00 4.28  ? 3066 PHE A CD2   1 
ATOM   12817 C  CE1   . PHE A 1 3066 ? 216.177 237.495 199.375 1.00 12.11 ? 3066 PHE A CE1   1 
ATOM   12818 C  CE2   . PHE A 1 3066 ? 216.279 239.719 198.519 1.00 8.72  ? 3066 PHE A CE2   1 
ATOM   12819 C  CZ    . PHE A 1 3066 ? 215.549 238.683 199.059 1.00 7.94  ? 3066 PHE A CZ    1 
ATOM   12820 N  N     . THR A 1 3067 ? 219.241 238.230 194.960 1.00 1.10  ? 3067 THR A N     1 
ATOM   12821 C  CA    . THR A 1 3067 ? 219.181 239.075 193.777 1.00 2.12  ? 3067 THR A CA    1 
ATOM   12822 C  C     . THR A 1 3067 ? 217.907 239.907 193.821 1.00 1.85  ? 3067 THR A C     1 
ATOM   12823 O  O     . THR A 1 3067 ? 216.826 239.378 194.089 1.00 4.16  ? 3067 THR A O     1 
ATOM   12824 C  CB    . THR A 1 3067 ? 219.231 238.242 192.495 1.00 1.60  ? 3067 THR A CB    1 
ATOM   12825 O  OG1   . THR A 1 3067 ? 218.198 237.251 192.524 1.00 5.25  ? 3067 THR A OG1   1 
ATOM   12826 C  CG2   . THR A 1 3067 ? 220.578 237.558 192.358 1.00 0.48  ? 3067 THR A CG2   1 
ATOM   12827 N  N     . MET A 1 3068 ? 218.042 241.208 193.574 1.00 2.67  ? 3068 MET A N     1 
ATOM   12828 C  CA    . MET A 1 3068 ? 216.903 242.112 193.592 1.00 4.60  ? 3068 MET A CA    1 
ATOM   12829 C  C     . MET A 1 3068 ? 217.157 243.268 192.634 1.00 2.59  ? 3068 MET A C     1 
ATOM   12830 O  O     . MET A 1 3068 ? 218.303 243.646 192.386 1.00 1.52  ? 3068 MET A O     1 
ATOM   12831 C  CB    . MET A 1 3068 ? 216.632 242.637 195.006 1.00 3.87  ? 3068 MET A CB    1 
ATOM   12832 C  CG    . MET A 1 3068 ? 217.812 243.331 195.655 1.00 3.94  ? 3068 MET A CG    1 
ATOM   12833 S  SD    . MET A 1 3068 ? 217.471 243.814 197.356 1.00 18.13 ? 3068 MET A SD    1 
ATOM   12834 C  CE    . MET A 1 3068 ? 215.857 244.561 197.176 1.00 17.25 ? 3068 MET A CE    1 
ATOM   12835 N  N     . ASN A 1 3069 ? 216.069 243.824 192.099 1.00 7.36  ? 3069 ASN A N     1 
ATOM   12836 C  CA    . ASN A 1 3069 ? 216.175 244.983 191.228 1.00 6.11  ? 3069 ASN A CA    1 
ATOM   12837 C  C     . ASN A 1 3069 ? 216.405 246.256 192.040 1.00 6.69  ? 3069 ASN A C     1 
ATOM   12838 O  O     . ASN A 1 3069 ? 215.986 246.349 193.195 1.00 7.42  ? 3069 ASN A O     1 
ATOM   12839 C  CB    . ASN A 1 3069 ? 214.917 245.142 190.381 1.00 5.86  ? 3069 ASN A CB    1 
ATOM   12840 C  CG    . ASN A 1 3069 ? 214.704 243.990 189.430 1.00 7.55  ? 3069 ASN A CG    1 
ATOM   12841 O  OD1   . ASN A 1 3069 ? 215.490 243.771 188.511 1.00 10.11 ? 3069 ASN A OD1   1 
ATOM   12842 N  ND2   . ASN A 1 3069 ? 213.640 243.239 189.651 1.00 14.76 ? 3069 ASN A ND2   1 
ATOM   12843 N  N     . PRO A 1 3070 ? 217.077 247.248 191.455 1.00 6.56  ? 3070 PRO A N     1 
ATOM   12844 C  CA    . PRO A 1 3070 ? 217.232 248.540 192.137 1.00 7.33  ? 3070 PRO A CA    1 
ATOM   12845 C  C     . PRO A 1 3070 ? 215.902 249.271 192.226 1.00 10.95 ? 3070 PRO A C     1 
ATOM   12846 O  O     . PRO A 1 3070 ? 215.314 249.655 191.213 1.00 16.42 ? 3070 PRO A O     1 
ATOM   12847 C  CB    . PRO A 1 3070 ? 218.233 249.292 191.249 1.00 5.41  ? 3070 PRO A CB    1 
ATOM   12848 C  CG    . PRO A 1 3070 ? 218.879 248.243 190.403 1.00 4.19  ? 3070 PRO A CG    1 
ATOM   12849 C  CD    . PRO A 1 3070 ? 217.838 247.196 190.198 1.00 3.49  ? 3070 PRO A CD    1 
ATOM   12850 N  N     . SER A 1 3071 ? 215.424 249.452 193.453 1.00 13.46 ? 3071 SER A N     1 
ATOM   12851 C  CA    . SER A 1 3071 ? 214.227 250.243 193.724 1.00 14.71 ? 3071 SER A CA    1 
ATOM   12852 C  C     . SER A 1 3071 ? 214.522 251.099 194.944 1.00 18.30 ? 3071 SER A C     1 
ATOM   12853 O  O     . SER A 1 3071 ? 214.771 250.564 196.027 1.00 18.02 ? 3071 SER A O     1 
ATOM   12854 C  CB    . SER A 1 3071 ? 213.007 249.352 193.955 1.00 15.19 ? 3071 SER A CB    1 
ATOM   12855 O  OG    . SER A 1 3071 ? 212.795 248.483 192.857 1.00 18.34 ? 3071 SER A OG    1 
ATOM   12856 N  N     . SER A 1 3072 ? 214.502 252.423 194.768 1.00 24.41 ? 3072 SER A N     1 
ATOM   12857 C  CA    . SER A 1 3072 ? 214.865 253.322 195.859 1.00 20.54 ? 3072 SER A CA    1 
ATOM   12858 C  C     . SER A 1 3072 ? 213.965 253.115 197.071 1.00 19.07 ? 3072 SER A C     1 
ATOM   12859 O  O     . SER A 1 3072 ? 214.447 252.968 198.199 1.00 20.99 ? 3072 SER A O     1 
ATOM   12860 C  CB    . SER A 1 3072 ? 214.804 254.773 195.381 1.00 17.92 ? 3072 SER A CB    1 
ATOM   12861 O  OG    . SER A 1 3072 ? 215.719 254.997 194.323 1.00 22.83 ? 3072 SER A OG    1 
ATOM   12862 N  N     . GLU A 1 3073 ? 212.650 253.093 196.855 1.00 20.80 ? 3073 GLU A N     1 
ATOM   12863 C  CA    . GLU A 1 3073 ? 211.731 252.811 197.952 1.00 22.85 ? 3073 GLU A CA    1 
ATOM   12864 C  C     . GLU A 1 3073 ? 211.890 251.377 198.441 1.00 18.75 ? 3073 GLU A C     1 
ATOM   12865 O  O     . GLU A 1 3073 ? 211.904 251.120 199.651 1.00 24.19 ? 3073 GLU A O     1 
ATOM   12866 C  CB    . GLU A 1 3073 ? 210.291 253.076 197.513 1.00 22.77 ? 3073 GLU A CB    1 
ATOM   12867 C  CG    . GLU A 1 3073 ? 209.253 252.728 198.567 1.00 25.47 ? 3073 GLU A CG    1 
ATOM   12868 C  CD    . GLU A 1 3073 ? 207.834 252.984 198.098 1.00 35.47 ? 3073 GLU A CD    1 
ATOM   12869 O  OE1   . GLU A 1 3073 ? 207.420 252.373 197.090 1.00 33.57 ? 3073 GLU A OE1   1 
ATOM   12870 O  OE2   . GLU A 1 3073 ? 207.133 253.796 198.736 1.00 37.00 ? 3073 GLU A OE2   1 
ATOM   12871 N  N     . GLY A 1 3074 ? 212.015 250.428 197.511 1.00 17.76 ? 3074 GLY A N     1 
ATOM   12872 C  CA    . GLY A 1 3074 ? 212.135 249.034 197.905 1.00 16.30 ? 3074 GLY A CA    1 
ATOM   12873 C  C     . GLY A 1 3074 ? 213.413 248.750 198.674 1.00 17.67 ? 3074 GLY A C     1 
ATOM   12874 O  O     . GLY A 1 3074 ? 213.410 247.995 199.650 1.00 15.23 ? 3074 GLY A O     1 
ATOM   12875 N  N     . LEU A 1 3075 ? 214.524 249.347 198.237 1.00 14.03 ? 3075 LEU A N     1 
ATOM   12876 C  CA    . LEU A 1 3075 ? 215.802 249.101 198.896 1.00 12.97 ? 3075 LEU A CA    1 
ATOM   12877 C  C     . LEU A 1 3075 ? 215.804 249.654 200.316 1.00 17.15 ? 3075 LEU A C     1 
ATOM   12878 O  O     . LEU A 1 3075 ? 216.272 248.993 201.250 1.00 12.77 ? 3075 LEU A O     1 
ATOM   12879 C  CB    . LEU A 1 3075 ? 216.937 249.710 198.075 1.00 15.91 ? 3075 LEU A CB    1 
ATOM   12880 C  CG    . LEU A 1 3075 ? 218.353 249.354 198.516 1.00 15.41 ? 3075 LEU A CG    1 
ATOM   12881 C  CD1   . LEU A 1 3075 ? 218.609 247.878 198.273 1.00 12.36 ? 3075 LEU A CD1   1 
ATOM   12882 C  CD2   . LEU A 1 3075 ? 219.376 250.210 197.795 1.00 12.30 ? 3075 LEU A CD2   1 
ATOM   12883 N  N     . LYS A 1 3076 ? 215.286 250.872 200.500 1.00 17.71 ? 3076 LYS A N     1 
ATOM   12884 C  CA    . LYS A 1 3076 ? 215.199 251.443 201.843 1.00 12.70 ? 3076 LYS A CA    1 
ATOM   12885 C  C     . LYS A 1 3076 ? 214.276 250.624 202.735 1.00 14.33 ? 3076 LYS A C     1 
ATOM   12886 O  O     . LYS A 1 3076 ? 214.590 250.378 203.905 1.00 22.65 ? 3076 LYS A O     1 
ATOM   12887 C  CB    . LYS A 1 3076 ? 214.724 252.896 201.779 1.00 13.57 ? 3076 LYS A CB    1 
ATOM   12888 C  CG    . LYS A 1 3076 ? 215.652 253.831 201.034 1.00 12.15 ? 3076 LYS A CG    1 
ATOM   12889 C  CD    . LYS A 1 3076 ? 215.173 255.268 201.123 1.00 14.01 ? 3076 LYS A CD    1 
ATOM   12890 C  CE    . LYS A 1 3076 ? 216.164 256.221 200.480 1.00 12.56 ? 3076 LYS A CE    1 
ATOM   12891 N  NZ    . LYS A 1 3076 ? 215.712 257.636 200.579 1.00 22.79 ? 3076 LYS A NZ    1 
ATOM   12892 N  N     . ASP A 1 3077 ? 213.130 250.199 202.201 1.00 14.33 ? 3077 ASP A N     1 
ATOM   12893 C  CA    . ASP A 1 3077 ? 212.221 249.368 202.981 1.00 16.16 ? 3077 ASP A CA    1 
ATOM   12894 C  C     . ASP A 1 3077 ? 212.827 247.997 203.257 1.00 13.49 ? 3077 ASP A C     1 
ATOM   12895 O  O     . ASP A 1 3077 ? 212.490 247.353 204.257 1.00 20.06 ? 3077 ASP A O     1 
ATOM   12896 C  CB    . ASP A 1 3077 ? 210.885 249.223 202.254 1.00 19.93 ? 3077 ASP A CB    1 
ATOM   12897 C  CG    . ASP A 1 3077 ? 210.101 250.519 202.214 1.00 27.53 ? 3077 ASP A CG    1 
ATOM   12898 O  OD1   . ASP A 1 3077 ? 210.255 251.339 203.141 1.00 28.62 ? 3077 ASP A OD1   1 
ATOM   12899 O  OD2   . ASP A 1 3077 ? 209.330 250.717 201.252 1.00 29.94 ? 3077 ASP A OD2   1 
ATOM   12900 N  N     . ARG A 1 3078 ? 213.723 247.540 202.382 1.00 15.83 ? 3078 ARG A N     1 
ATOM   12901 C  CA    . ARG A 1 3078 ? 214.255 246.188 202.508 1.00 14.75 ? 3078 ARG A CA    1 
ATOM   12902 C  C     . ARG A 1 3078 ? 215.129 246.061 203.749 1.00 12.27 ? 3078 ARG A C     1 
ATOM   12903 O  O     . ARG A 1 3078 ? 215.243 244.974 204.324 1.00 11.24 ? 3078 ARG A O     1 
ATOM   12904 C  CB    . ARG A 1 3078 ? 215.061 245.829 201.258 1.00 13.69 ? 3078 ARG A CB    1 
ATOM   12905 C  CG    . ARG A 1 3078 ? 215.662 244.446 201.285 1.00 17.44 ? 3078 ARG A CG    1 
ATOM   12906 C  CD    . ARG A 1 3078 ? 214.525 243.444 201.257 1.00 13.60 ? 3078 ARG A CD    1 
ATOM   12907 N  NE    . ARG A 1 3078 ? 213.824 243.547 199.982 1.00 21.12 ? 3078 ARG A NE    1 
ATOM   12908 C  CZ    . ARG A 1 3078 ? 212.651 242.996 199.708 1.00 23.55 ? 3078 ARG A CZ    1 
ATOM   12909 N  NH1   . ARG A 1 3078 ? 211.966 242.335 200.623 1.00 21.31 ? 3078 ARG A NH1   1 
ATOM   12910 N  NH2   . ARG A 1 3078 ? 212.143 243.129 198.485 1.00 24.75 ? 3078 ARG A NH2   1 
ATOM   12911 N  N     . ALA A 1 3079 ? 215.745 247.167 204.176 1.00 8.68  ? 3079 ALA A N     1 
ATOM   12912 C  CA    . ALA A 1 3079 ? 216.658 247.133 205.314 1.00 9.16  ? 3079 ALA A CA    1 
ATOM   12913 C  C     . ALA A 1 3079 ? 215.932 246.765 206.603 1.00 13.20 ? 3079 ALA A C     1 
ATOM   12914 O  O     . ALA A 1 3079 ? 216.455 246.007 207.425 1.00 11.04 ? 3079 ALA A O     1 
ATOM   12915 C  CB    . ALA A 1 3079 ? 217.361 248.483 205.455 1.00 6.27  ? 3079 ALA A CB    1 
ATOM   12916 N  N     . ALA A 1 3080 ? 214.730 247.308 206.809 1.00 10.44 ? 3080 ALA A N     1 
ATOM   12917 C  CA    . ALA A 1 3080 ? 213.992 246.996 208.027 1.00 7.25  ? 3080 ALA A CA    1 
ATOM   12918 C  C     . ALA A 1 3080 ? 213.507 245.551 208.027 1.00 5.58  ? 3080 ALA A C     1 
ATOM   12919 O  O     . ALA A 1 3080 ? 213.570 244.870 209.057 1.00 3.40  ? 3080 ALA A O     1 
ATOM   12920 C  CB    . ALA A 1 3080 ? 212.818 247.960 208.193 1.00 6.25  ? 3080 ALA A CB    1 
ATOM   12921 N  N     . THR A 1 3081 ? 213.011 245.070 206.884 1.00 8.47  ? 3081 THR A N     1 
ATOM   12922 C  CA    . THR A 1 3081 ? 212.491 243.708 206.811 1.00 7.87  ? 3081 THR A CA    1 
ATOM   12923 C  C     . THR A 1 3081 ? 213.595 242.676 207.018 1.00 9.24  ? 3081 THR A C     1 
ATOM   12924 O  O     . THR A 1 3081 ? 213.388 241.670 207.708 1.00 12.92 ? 3081 THR A O     1 
ATOM   12925 C  CB    . THR A 1 3081 ? 211.793 243.489 205.468 1.00 11.81 ? 3081 THR A CB    1 
ATOM   12926 O  OG1   . THR A 1 3081 ? 210.708 244.416 205.339 1.00 11.60 ? 3081 THR A OG1   1 
ATOM   12927 C  CG2   . THR A 1 3081 ? 211.253 242.074 205.363 1.00 9.76  ? 3081 THR A CG2   1 
ATOM   12928 N  N     . SER A 1 3082 ? 214.764 242.893 206.420 1.00 7.94  ? 3082 SER A N     1 
ATOM   12929 C  CA    . SER A 1 3082 ? 215.905 241.992 206.563 1.00 5.98  ? 3082 SER A CA    1 
ATOM   12930 C  C     . SER A 1 3082 ? 217.166 242.814 206.790 1.00 5.12  ? 3082 SER A C     1 
ATOM   12931 O  O     . SER A 1 3082 ? 217.942 243.053 205.857 1.00 8.14  ? 3082 SER A O     1 
ATOM   12932 C  CB    . SER A 1 3082 ? 216.047 241.083 205.341 1.00 7.42  ? 3082 SER A CB    1 
ATOM   12933 O  OG    . SER A 1 3082 ? 217.172 240.232 205.469 1.00 8.23  ? 3082 SER A OG    1 
ATOM   12934 N  N     . PRO A 1 3083 ? 217.399 243.270 208.025 1.00 6.49  ? 3083 PRO A N     1 
ATOM   12935 C  CA    . PRO A 1 3083 ? 218.649 243.996 208.306 1.00 5.67  ? 3083 PRO A CA    1 
ATOM   12936 C  C     . PRO A 1 3083 ? 219.895 243.165 208.074 1.00 2.22  ? 3083 PRO A C     1 
ATOM   12937 O  O     . PRO A 1 3083 ? 220.970 243.730 207.836 1.00 2.11  ? 3083 PRO A O     1 
ATOM   12938 C  CB    . PRO A 1 3083 ? 218.498 244.397 209.782 1.00 3.39  ? 3083 PRO A CB    1 
ATOM   12939 C  CG    . PRO A 1 3083 ? 217.429 243.506 210.320 1.00 2.29  ? 3083 PRO A CG    1 
ATOM   12940 C  CD    . PRO A 1 3083 ? 216.500 243.255 209.188 1.00 2.89  ? 3083 PRO A CD    1 
ATOM   12941 N  N     . ALA A 1 3084 ? 219.788 241.836 208.138 1.00 3.06  ? 3084 ALA A N     1 
ATOM   12942 C  CA    . ALA A 1 3084 ? 220.923 240.976 207.833 1.00 2.95  ? 3084 ALA A CA    1 
ATOM   12943 C  C     . ALA A 1 3084 ? 221.352 241.077 206.375 1.00 3.35  ? 3084 ALA A C     1 
ATOM   12944 O  O     . ALA A 1 3084 ? 222.519 240.818 206.068 1.00 3.45  ? 3084 ALA A O     1 
ATOM   12945 C  CB    . ALA A 1 3084 ? 220.593 239.526 208.183 1.00 2.70  ? 3084 ALA A CB    1 
ATOM   12946 N  N     . LEU A 1 3085 ? 220.439 241.451 205.474 1.00 2.71  ? 3085 LEU A N     1 
ATOM   12947 C  CA    . LEU A 1 3085 ? 220.803 241.603 204.070 1.00 3.26  ? 3085 LEU A CA    1 
ATOM   12948 C  C     . LEU A 1 3085 ? 221.845 242.695 203.868 1.00 4.47  ? 3085 LEU A C     1 
ATOM   12949 O  O     . LEU A 1 3085 ? 222.601 242.656 202.892 1.00 6.58  ? 3085 LEU A O     1 
ATOM   12950 C  CB    . LEU A 1 3085 ? 219.562 241.914 203.231 1.00 4.33  ? 3085 LEU A CB    1 
ATOM   12951 C  CG    . LEU A 1 3085 ? 218.738 240.752 202.675 1.00 3.68  ? 3085 LEU A CG    1 
ATOM   12952 C  CD1   . LEU A 1 3085 ? 217.766 241.262 201.629 1.00 8.32  ? 3085 LEU A CD1   1 
ATOM   12953 C  CD2   . LEU A 1 3085 ? 219.630 239.677 202.092 1.00 3.69  ? 3085 LEU A CD2   1 
ATOM   12954 N  N     . PHE A 1 3086 ? 221.908 243.667 204.774 1.00 3.00  ? 3086 PHE A N     1 
ATOM   12955 C  CA    . PHE A 1 3086 ? 222.773 244.822 204.603 1.00 1.89  ? 3086 PHE A CA    1 
ATOM   12956 C  C     . PHE A 1 3086 ? 223.935 244.868 205.586 1.00 2.91  ? 3086 PHE A C     1 
ATOM   12957 O  O     . PHE A 1 3086 ? 224.800 245.738 205.452 1.00 5.36  ? 3086 PHE A O     1 
ATOM   12958 C  CB    . PHE A 1 3086 ? 221.946 246.107 204.698 1.00 3.00  ? 3086 PHE A CB    1 
ATOM   12959 C  CG    . PHE A 1 3086 ? 220.949 246.255 203.586 1.00 5.98  ? 3086 PHE A CG    1 
ATOM   12960 C  CD1   . PHE A 1 3086 ? 219.689 245.693 203.690 1.00 4.69  ? 3086 PHE A CD1   1 
ATOM   12961 C  CD2   . PHE A 1 3086 ? 221.281 246.936 202.429 1.00 6.35  ? 3086 PHE A CD2   1 
ATOM   12962 C  CE1   . PHE A 1 3086 ? 218.777 245.817 202.667 1.00 6.62  ? 3086 PHE A CE1   1 
ATOM   12963 C  CE2   . PHE A 1 3086 ? 220.369 247.063 201.403 1.00 7.84  ? 3086 PHE A CE2   1 
ATOM   12964 C  CZ    . PHE A 1 3086 ? 219.118 246.504 201.524 1.00 8.60  ? 3086 PHE A CZ    1 
ATOM   12965 N  N     . ASN A 1 3087 ? 223.987 243.961 206.563 1.00 3.96  ? 3087 ASN A N     1 
ATOM   12966 C  CA    . ASN A 1 3087 ? 225.141 243.867 207.443 1.00 3.65  ? 3087 ASN A CA    1 
ATOM   12967 C  C     . ASN A 1 3087 ? 225.757 242.476 207.520 1.00 4.47  ? 3087 ASN A C     1 
ATOM   12968 O  O     . ASN A 1 3087 ? 226.860 242.345 208.061 1.00 6.96  ? 3087 ASN A O     1 
ATOM   12969 C  CB    . ASN A 1 3087 ? 224.787 244.354 208.862 1.00 4.22  ? 3087 ASN A CB    1 
ATOM   12970 C  CG    . ASN A 1 3087 ? 223.696 243.530 209.522 1.00 7.73  ? 3087 ASN A CG    1 
ATOM   12971 O  OD1   . ASN A 1 3087 ? 223.809 242.315 209.660 1.00 12.46 ? 3087 ASN A OD1   1 
ATOM   12972 N  ND2   . ASN A 1 3087 ? 222.636 244.200 209.951 1.00 9.95  ? 3087 ASN A ND2   1 
ATOM   12973 N  N     . ARG A 1 3088 ? 225.091 241.444 206.997 1.00 3.98  ? 3088 ARG A N     1 
ATOM   12974 C  CA    . ARG A 1 3088 ? 225.673 240.113 206.901 1.00 4.45  ? 3088 ARG A CA    1 
ATOM   12975 C  C     . ARG A 1 3088 ? 225.958 239.675 205.473 1.00 4.74  ? 3088 ARG A C     1 
ATOM   12976 O  O     . ARG A 1 3088 ? 226.636 238.659 205.284 1.00 3.53  ? 3088 ARG A O     1 
ATOM   12977 C  CB    . ARG A 1 3088 ? 224.761 239.065 207.563 1.00 5.98  ? 3088 ARG A CB    1 
ATOM   12978 C  CG    . ARG A 1 3088 ? 224.391 239.349 209.008 1.00 3.85  ? 3088 ARG A CG    1 
ATOM   12979 C  CD    . ARG A 1 3088 ? 225.617 239.546 209.880 1.00 6.05  ? 3088 ARG A CD    1 
ATOM   12980 N  NE    . ARG A 1 3088 ? 225.518 238.798 211.128 1.00 12.61 ? 3088 ARG A NE    1 
ATOM   12981 C  CZ    . ARG A 1 3088 ? 224.981 239.273 212.244 1.00 12.50 ? 3088 ARG A CZ    1 
ATOM   12982 N  NH1   . ARG A 1 3088 ? 224.489 240.499 212.310 1.00 9.93  ? 3088 ARG A NH1   1 
ATOM   12983 N  NH2   . ARG A 1 3088 ? 224.936 238.495 213.324 1.00 9.28  ? 3088 ARG A NH2   1 
ATOM   12984 N  N     . CYS A 1 3089 ? 225.469 240.395 204.469 1.00 6.54  ? 3089 CYS A N     1 
ATOM   12985 C  CA    . CYS A 1 3089 ? 225.701 240.061 203.072 1.00 2.10  ? 3089 CYS A CA    1 
ATOM   12986 C  C     . CYS A 1 3089 ? 226.566 241.133 202.425 1.00 1.63  ? 3089 CYS A C     1 
ATOM   12987 O  O     . CYS A 1 3089 ? 226.405 242.324 202.699 1.00 2.61  ? 3089 CYS A O     1 
ATOM   12988 C  CB    . CYS A 1 3089 ? 224.383 239.931 202.305 1.00 0.43  ? 3089 CYS A CB    1 
ATOM   12989 S  SG    . CYS A 1 3089 ? 223.140 238.890 203.093 1.00 7.73  ? 3089 CYS A SG    1 
ATOM   12990 N  N     . VAL A 1 3090 ? 227.484 240.701 201.568 1.00 1.38  ? 3090 VAL A N     1 
ATOM   12991 C  CA    . VAL A 1 3090 ? 228.299 241.628 200.790 1.00 1.58  ? 3090 VAL A CA    1 
ATOM   12992 C  C     . VAL A 1 3090 ? 227.462 242.128 199.621 1.00 0.67  ? 3090 VAL A C     1 
ATOM   12993 O  O     . VAL A 1 3090 ? 226.922 241.334 198.846 1.00 0.90  ? 3090 VAL A O     1 
ATOM   12994 C  CB    . VAL A 1 3090 ? 229.592 240.958 200.304 1.00 1.18  ? 3090 VAL A CB    1 
ATOM   12995 C  CG1   . VAL A 1 3090 ? 230.290 241.831 199.278 1.00 0.67  ? 3090 VAL A CG1   1 
ATOM   12996 C  CG2   . VAL A 1 3090 ? 230.504 240.668 201.479 1.00 0.76  ? 3090 VAL A CG2   1 
ATOM   12997 N  N     . LEU A 1 3091 ? 227.343 243.445 199.499 1.00 0.82  ? 3091 LEU A N     1 
ATOM   12998 C  CA    . LEU A 1 3091 ? 226.493 244.044 198.482 1.00 0.41  ? 3091 LEU A CA    1 
ATOM   12999 C  C     . LEU A 1 3091 ? 227.335 244.416 197.269 1.00 0.50  ? 3091 LEU A C     1 
ATOM   13000 O  O     . LEU A 1 3091 ? 228.359 245.092 197.397 1.00 0.38  ? 3091 LEU A O     1 
ATOM   13001 C  CB    . LEU A 1 3091 ? 225.769 245.271 199.046 1.00 0.50  ? 3091 LEU A CB    1 
ATOM   13002 C  CG    . LEU A 1 3091 ? 224.607 245.909 198.271 1.00 0.63  ? 3091 LEU A CG    1 
ATOM   13003 C  CD1   . LEU A 1 3091 ? 223.798 246.785 199.207 1.00 0.54  ? 3091 LEU A CD1   1 
ATOM   13004 C  CD2   . LEU A 1 3091 ? 225.058 246.722 197.062 1.00 0.32  ? 3091 LEU A CD2   1 
ATOM   13005 N  N     . ASN A 1 3092 ? 226.903 243.959 196.100 1.00 0.58  ? 3092 ASN A N     1 
ATOM   13006 C  CA    . ASN A 1 3092 ? 227.533 244.296 194.828 1.00 0.50  ? 3092 ASN A CA    1 
ATOM   13007 C  C     . ASN A 1 3092 ? 226.472 244.912 193.930 1.00 0.34  ? 3092 ASN A C     1 
ATOM   13008 O  O     . ASN A 1 3092 ? 225.520 244.234 193.529 1.00 0.23  ? 3092 ASN A O     1 
ATOM   13009 C  CB    . ASN A 1 3092 ? 228.162 243.065 194.179 1.00 0.72  ? 3092 ASN A CB    1 
ATOM   13010 C  CG    . ASN A 1 3092 ? 229.289 242.484 195.005 1.00 1.91  ? 3092 ASN A CG    1 
ATOM   13011 O  OD1   . ASN A 1 3092 ? 229.193 241.369 195.509 1.00 13.57 ? 3092 ASN A OD1   1 
ATOM   13012 N  ND2   . ASN A 1 3092 ? 230.369 243.237 195.141 1.00 4.52  ? 3092 ASN A ND2   1 
ATOM   13013 N  N     . TRP A 1 3093 ? 226.629 246.197 193.625 1.00 0.27  ? 3093 TRP A N     1 
ATOM   13014 C  CA    . TRP A 1 3093 ? 225.687 246.911 192.766 1.00 0.45  ? 3093 TRP A CA    1 
ATOM   13015 C  C     . TRP A 1 3093 ? 226.059 246.648 191.315 1.00 0.41  ? 3093 TRP A C     1 
ATOM   13016 O  O     . TRP A 1 3093 ? 226.845 247.376 190.707 1.00 2.46  ? 3093 TRP A O     1 
ATOM   13017 C  CB    . TRP A 1 3093 ? 225.692 248.401 193.073 1.00 0.79  ? 3093 TRP A CB    1 
ATOM   13018 C  CG    . TRP A 1 3093 ? 224.448 249.094 192.622 1.00 1.02  ? 3093 TRP A CG    1 
ATOM   13019 C  CD1   . TRP A 1 3093 ? 224.195 249.593 191.379 1.00 0.62  ? 3093 TRP A CD1   1 
ATOM   13020 C  CD2   . TRP A 1 3093 ? 223.287 249.375 193.410 1.00 1.17  ? 3093 TRP A CD2   1 
ATOM   13021 N  NE1   . TRP A 1 3093 ? 222.949 250.159 191.341 1.00 1.16  ? 3093 TRP A NE1   1 
ATOM   13022 C  CE2   . TRP A 1 3093 ? 222.368 250.040 192.576 1.00 1.43  ? 3093 TRP A CE2   1 
ATOM   13023 C  CE3   . TRP A 1 3093 ? 222.934 249.125 194.739 1.00 1.04  ? 3093 TRP A CE3   1 
ATOM   13024 C  CZ2   . TRP A 1 3093 ? 221.122 250.459 193.027 1.00 1.36  ? 3093 TRP A CZ2   1 
ATOM   13025 C  CZ3   . TRP A 1 3093 ? 221.696 249.541 195.184 1.00 2.18  ? 3093 TRP A CZ3   1 
ATOM   13026 C  CH2   . TRP A 1 3093 ? 220.804 250.201 194.332 1.00 1.89  ? 3093 TRP A CH2   1 
ATOM   13027 N  N     . PHE A 1 3094 ? 225.491 245.585 190.751 1.00 0.37  ? 3094 PHE A N     1 
ATOM   13028 C  CA    . PHE A 1 3094 ? 225.677 245.332 189.329 1.00 0.44  ? 3094 PHE A CA    1 
ATOM   13029 C  C     . PHE A 1 3094 ? 224.899 246.329 188.481 1.00 0.84  ? 3094 PHE A C     1 
ATOM   13030 O  O     . PHE A 1 3094 ? 225.376 246.733 187.414 1.00 2.38  ? 3094 PHE A O     1 
ATOM   13031 C  CB    . PHE A 1 3094 ? 225.273 243.897 188.986 1.00 0.46  ? 3094 PHE A CB    1 
ATOM   13032 C  CG    . PHE A 1 3094 ? 226.202 242.851 189.545 1.00 1.70  ? 3094 PHE A CG    1 
ATOM   13033 C  CD1   . PHE A 1 3094 ? 227.374 243.214 190.196 1.00 1.44  ? 3094 PHE A CD1   1 
ATOM   13034 C  CD2   . PHE A 1 3094 ? 225.909 241.505 189.411 1.00 1.15  ? 3094 PHE A CD2   1 
ATOM   13035 C  CE1   . PHE A 1 3094 ? 228.228 242.254 190.708 1.00 1.02  ? 3094 PHE A CE1   1 
ATOM   13036 C  CE2   . PHE A 1 3094 ? 226.759 240.541 189.916 1.00 1.35  ? 3094 PHE A CE2   1 
ATOM   13037 C  CZ    . PHE A 1 3094 ? 227.919 240.916 190.566 1.00 2.28  ? 3094 PHE A CZ    1 
ATOM   13038 N  N     . GLY A 1 3095 ? 223.721 246.742 188.942 1.00 0.57  ? 3095 GLY A N     1 
ATOM   13039 C  CA    . GLY A 1 3095 ? 222.941 247.744 188.238 1.00 0.68  ? 3095 GLY A CA    1 
ATOM   13040 C  C     . GLY A 1 3095 ? 222.538 247.285 186.853 1.00 1.72  ? 3095 GLY A C     1 
ATOM   13041 O  O     . GLY A 1 3095 ? 222.229 246.111 186.620 1.00 4.03  ? 3095 GLY A O     1 
ATOM   13042 N  N     . ASP A 1 3096 ? 222.535 248.226 185.921 1.00 2.08  ? 3096 ASP A N     1 
ATOM   13043 C  CA    . ASP A 1 3096 ? 222.266 247.958 184.518 1.00 2.05  ? 3096 ASP A CA    1 
ATOM   13044 C  C     . ASP A 1 3096 ? 223.579 247.905 183.747 1.00 1.64  ? 3096 ASP A C     1 
ATOM   13045 O  O     . ASP A 1 3096 ? 224.617 248.378 184.213 1.00 2.68  ? 3096 ASP A O     1 
ATOM   13046 C  CB    . ASP A 1 3096 ? 221.345 249.033 183.933 1.00 2.70  ? 3096 ASP A CB    1 
ATOM   13047 C  CG    . ASP A 1 3096 ? 220.650 248.585 182.663 1.00 6.78  ? 3096 ASP A CG    1 
ATOM   13048 O  OD1   . ASP A 1 3096 ? 221.091 247.590 182.052 1.00 4.09  ? 3096 ASP A OD1   1 
ATOM   13049 O  OD2   . ASP A 1 3096 ? 219.660 249.233 182.271 1.00 10.58 ? 3096 ASP A OD2   1 
ATOM   13050 N  N     . TRP A 1 3097 ? 223.526 247.304 182.560 1.00 1.52  ? 3097 TRP A N     1 
ATOM   13051 C  CA    . TRP A 1 3097 ? 224.695 247.281 181.692 1.00 1.08  ? 3097 TRP A CA    1 
ATOM   13052 C  C     . TRP A 1 3097 ? 225.050 248.698 181.260 1.00 2.29  ? 3097 TRP A C     1 
ATOM   13053 O  O     . TRP A 1 3097 ? 224.180 249.474 180.854 1.00 4.99  ? 3097 TRP A O     1 
ATOM   13054 C  CB    . TRP A 1 3097 ? 224.441 246.404 180.467 1.00 0.74  ? 3097 TRP A CB    1 
ATOM   13055 C  CG    . TRP A 1 3097 ? 224.455 244.935 180.752 1.00 0.53  ? 3097 TRP A CG    1 
ATOM   13056 C  CD1   . TRP A 1 3097 ? 224.512 244.339 181.975 1.00 0.56  ? 3097 TRP A CD1   1 
ATOM   13057 C  CD2   . TRP A 1 3097 ? 224.418 243.874 179.791 1.00 0.58  ? 3097 TRP A CD2   1 
ATOM   13058 N  NE1   . TRP A 1 3097 ? 224.506 242.974 181.838 1.00 0.47  ? 3097 TRP A NE1   1 
ATOM   13059 C  CE2   . TRP A 1 3097 ? 224.449 242.661 180.506 1.00 0.55  ? 3097 TRP A CE2   1 
ATOM   13060 C  CE3   . TRP A 1 3097 ? 224.356 243.831 178.395 1.00 0.48  ? 3097 TRP A CE3   1 
ATOM   13061 C  CZ2   . TRP A 1 3097 ? 224.425 241.420 179.874 1.00 0.87  ? 3097 TRP A CZ2   1 
ATOM   13062 C  CZ3   . TRP A 1 3097 ? 224.331 242.598 177.769 1.00 1.13  ? 3097 TRP A CZ3   1 
ATOM   13063 C  CH2   . TRP A 1 3097 ? 224.367 241.409 178.508 1.00 0.55  ? 3097 TRP A CH2   1 
ATOM   13064 N  N     . SER A 1 3098 ? 226.330 249.032 181.347 1.00 2.09  ? 3098 SER A N     1 
ATOM   13065 C  CA    . SER A 1 3098 ? 226.782 250.364 180.990 1.00 2.47  ? 3098 SER A CA    1 
ATOM   13066 C  C     . SER A 1 3098 ? 226.897 250.505 179.473 1.00 2.63  ? 3098 SER A C     1 
ATOM   13067 O  O     . SER A 1 3098 ? 226.699 249.554 178.713 1.00 2.25  ? 3098 SER A O     1 
ATOM   13068 C  CB    . SER A 1 3098 ? 228.120 250.669 181.659 1.00 2.07  ? 3098 SER A CB    1 
ATOM   13069 O  OG    . SER A 1 3098 ? 229.124 249.775 181.215 1.00 4.16  ? 3098 SER A OG    1 
ATOM   13070 N  N     . THR A 1 3099 ? 227.222 251.722 179.038 1.00 3.04  ? 3099 THR A N     1 
ATOM   13071 C  CA    . THR A 1 3099 ? 227.477 251.955 177.619 1.00 1.63  ? 3099 THR A CA    1 
ATOM   13072 C  C     . THR A 1 3099 ? 228.687 251.157 177.151 1.00 3.04  ? 3099 THR A C     1 
ATOM   13073 O  O     . THR A 1 3099 ? 228.703 250.634 176.031 1.00 4.40  ? 3099 THR A O     1 
ATOM   13074 C  CB    . THR A 1 3099 ? 227.679 253.449 177.363 1.00 2.06  ? 3099 THR A CB    1 
ATOM   13075 O  OG1   . THR A 1 3099 ? 226.479 254.155 177.700 1.00 4.70  ? 3099 THR A OG1   1 
ATOM   13076 C  CG2   . THR A 1 3099 ? 228.012 253.708 175.904 1.00 4.15  ? 3099 THR A CG2   1 
ATOM   13077 N  N     . GLU A 1 3100 ? 229.709 251.048 178.002 1.00 3.75  ? 3100 GLU A N     1 
ATOM   13078 C  CA    . GLU A 1 3100 ? 230.867 250.224 177.676 1.00 5.20  ? 3100 GLU A CA    1 
ATOM   13079 C  C     . GLU A 1 3100 ? 230.478 248.761 177.528 1.00 4.92  ? 3100 GLU A C     1 
ATOM   13080 O  O     . GLU A 1 3100 ? 230.943 248.077 176.609 1.00 5.31  ? 3100 GLU A O     1 
ATOM   13081 C  CB    . GLU A 1 3100 ? 231.938 250.382 178.754 1.00 9.13  ? 3100 GLU A CB    1 
ATOM   13082 C  CG    . GLU A 1 3100 ? 233.222 249.631 178.479 1.00 12.46 ? 3100 GLU A CG    1 
ATOM   13083 C  CD    . GLU A 1 3100 ? 234.260 249.861 179.556 1.00 26.10 ? 3100 GLU A CD    1 
ATOM   13084 O  OE1   . GLU A 1 3100 ? 233.957 250.592 180.523 1.00 26.93 ? 3100 GLU A OE1   1 
ATOM   13085 O  OE2   . GLU A 1 3100 ? 235.377 249.315 179.441 1.00 25.85 ? 3100 GLU A OE2   1 
ATOM   13086 N  N     . ALA A 1 3101 ? 229.630 248.260 178.432 1.00 3.12  ? 3101 ALA A N     1 
ATOM   13087 C  CA    . ALA A 1 3101 ? 229.190 246.873 178.344 1.00 3.44  ? 3101 ALA A CA    1 
ATOM   13088 C  C     . ALA A 1 3101 ? 228.382 246.631 177.078 1.00 3.41  ? 3101 ALA A C     1 
ATOM   13089 O  O     . ALA A 1 3101 ? 228.578 245.620 176.394 1.00 2.50  ? 3101 ALA A O     1 
ATOM   13090 C  CB    . ALA A 1 3101 ? 228.376 246.502 179.582 1.00 2.27  ? 3101 ALA A CB    1 
ATOM   13091 N  N     . LEU A 1 3102 ? 227.477 247.555 176.743 1.00 2.50  ? 3102 LEU A N     1 
ATOM   13092 C  CA    . LEU A 1 3102 ? 226.669 247.412 175.535 1.00 0.70  ? 3102 LEU A CA    1 
ATOM   13093 C  C     . LEU A 1 3102 ? 227.545 247.374 174.289 1.00 1.82  ? 3102 LEU A C     1 
ATOM   13094 O  O     . LEU A 1 3102 ? 227.321 246.564 173.383 1.00 2.80  ? 3102 LEU A O     1 
ATOM   13095 C  CB    . LEU A 1 3102 ? 225.656 248.553 175.446 1.00 0.73  ? 3102 LEU A CB    1 
ATOM   13096 C  CG    . LEU A 1 3102 ? 224.501 248.568 176.446 1.00 0.83  ? 3102 LEU A CG    1 
ATOM   13097 C  CD1   . LEU A 1 3102 ? 223.713 249.857 176.326 1.00 0.59  ? 3102 LEU A CD1   1 
ATOM   13098 C  CD2   . LEU A 1 3102 ? 223.593 247.370 176.233 1.00 0.13  ? 3102 LEU A CD2   1 
ATOM   13099 N  N     . TYR A 1 3103 ? 228.551 248.248 174.227 1.00 1.48  ? 3103 TYR A N     1 
ATOM   13100 C  CA    . TYR A 1 3103 ? 229.435 248.284 173.069 1.00 1.46  ? 3103 TYR A CA    1 
ATOM   13101 C  C     . TYR A 1 3103 ? 230.239 246.997 172.944 1.00 1.85  ? 3103 TYR A C     1 
ATOM   13102 O  O     . TYR A 1 3103 ? 230.404 246.459 171.843 1.00 2.49  ? 3103 TYR A O     1 
ATOM   13103 C  CB    . TYR A 1 3103 ? 230.365 249.496 173.156 1.00 2.27  ? 3103 TYR A CB    1 
ATOM   13104 C  CG    . TYR A 1 3103 ? 231.233 249.678 171.934 1.00 2.66  ? 3103 TYR A CG    1 
ATOM   13105 C  CD1   . TYR A 1 3103 ? 230.794 250.426 170.852 1.00 3.16  ? 3103 TYR A CD1   1 
ATOM   13106 C  CD2   . TYR A 1 3103 ? 232.494 249.104 171.866 1.00 2.41  ? 3103 TYR A CD2   1 
ATOM   13107 C  CE1   . TYR A 1 3103 ? 231.584 250.590 169.734 1.00 5.30  ? 3103 TYR A CE1   1 
ATOM   13108 C  CE2   . TYR A 1 3103 ? 233.290 249.263 170.753 1.00 3.82  ? 3103 TYR A CE2   1 
ATOM   13109 C  CZ    . TYR A 1 3103 ? 232.832 250.008 169.691 1.00 7.88  ? 3103 TYR A CZ    1 
ATOM   13110 O  OH    . TYR A 1 3103 ? 233.626 250.167 168.582 1.00 16.23 ? 3103 TYR A OH    1 
ATOM   13111 N  N     . GLN A 1 3104 ? 230.760 246.492 174.063 1.00 3.86  ? 3104 GLN A N     1 
ATOM   13112 C  CA    . GLN A 1 3104 ? 231.561 245.274 174.018 1.00 2.61  ? 3104 GLN A CA    1 
ATOM   13113 C  C     . GLN A 1 3104 ? 230.708 244.073 173.635 1.00 1.55  ? 3104 GLN A C     1 
ATOM   13114 O  O     . GLN A 1 3104 ? 231.144 243.212 172.863 1.00 2.66  ? 3104 GLN A O     1 
ATOM   13115 C  CB    . GLN A 1 3104 ? 232.254 245.056 175.363 1.00 2.82  ? 3104 GLN A CB    1 
ATOM   13116 C  CG    . GLN A 1 3104 ? 233.305 246.107 175.674 1.00 3.42  ? 3104 GLN A CG    1 
ATOM   13117 C  CD    . GLN A 1 3104 ? 233.974 245.898 177.017 1.00 10.19 ? 3104 GLN A CD    1 
ATOM   13118 O  OE1   . GLN A 1 3104 ? 233.617 244.993 177.769 1.00 11.50 ? 3104 GLN A OE1   1 
ATOM   13119 N  NE2   . GLN A 1 3104 ? 234.950 246.742 177.328 1.00 6.58  ? 3104 GLN A NE2   1 
ATOM   13120 N  N     . VAL A 1 3105 ? 229.485 244.002 174.160 1.00 1.28  ? 3105 VAL A N     1 
ATOM   13121 C  CA    . VAL A 1 3105 ? 228.572 242.931 173.767 1.00 1.37  ? 3105 VAL A CA    1 
ATOM   13122 C  C     . VAL A 1 3105 ? 228.249 243.035 172.283 1.00 2.05  ? 3105 VAL A C     1 
ATOM   13123 O  O     . VAL A 1 3105 ? 228.272 242.039 171.552 1.00 6.58  ? 3105 VAL A O     1 
ATOM   13124 C  CB    . VAL A 1 3105 ? 227.295 242.967 174.625 1.00 1.47  ? 3105 VAL A CB    1 
ATOM   13125 C  CG1   . VAL A 1 3105 ? 226.260 242.003 174.074 1.00 1.13  ? 3105 VAL A CG1   1 
ATOM   13126 C  CG2   . VAL A 1 3105 ? 227.615 242.627 176.058 1.00 1.29  ? 3105 VAL A CG2   1 
ATOM   13127 N  N     . GLY A 1 3106 ? 227.954 244.248 171.816 1.00 1.64  ? 3106 GLY A N     1 
ATOM   13128 C  CA    . GLY A 1 3106 ? 227.634 244.430 170.411 1.00 2.08  ? 3106 GLY A CA    1 
ATOM   13129 C  C     . GLY A 1 3106 ? 228.795 244.096 169.495 1.00 1.98  ? 3106 GLY A C     1 
ATOM   13130 O  O     . GLY A 1 3106 ? 228.628 243.402 168.491 1.00 5.64  ? 3106 GLY A O     1 
ATOM   13131 N  N     . LYS A 1 3107 ? 229.990 244.587 169.828 1.00 1.64  ? 3107 LYS A N     1 
ATOM   13132 C  CA    . LYS A 1 3107 ? 231.149 244.321 168.982 1.00 3.09  ? 3107 LYS A CA    1 
ATOM   13133 C  C     . LYS A 1 3107 ? 231.511 242.843 168.990 1.00 5.26  ? 3107 LYS A C     1 
ATOM   13134 O  O     . LYS A 1 3107 ? 231.857 242.272 167.950 1.00 11.53 ? 3107 LYS A O     1 
ATOM   13135 C  CB    . LYS A 1 3107 ? 232.340 245.172 169.426 1.00 3.23  ? 3107 LYS A CB    1 
ATOM   13136 C  CG    . LYS A 1 3107 ? 233.581 244.989 168.566 1.00 8.74  ? 3107 LYS A CG    1 
ATOM   13137 C  CD    . LYS A 1 3107 ? 234.697 245.949 168.962 1.00 14.98 ? 3107 LYS A CD    1 
ATOM   13138 C  CE    . LYS A 1 3107 ? 235.338 245.546 170.281 1.00 17.04 ? 3107 LYS A CE    1 
ATOM   13139 N  NZ    . LYS A 1 3107 ? 236.504 246.404 170.621 1.00 23.24 ? 3107 LYS A NZ    1 
ATOM   13140 N  N     . GLU A 1 3108 ? 231.437 242.203 170.159 1.00 7.40  ? 3108 GLU A N     1 
ATOM   13141 C  CA    . GLU A 1 3108 ? 231.755 240.784 170.244 1.00 10.33 ? 3108 GLU A CA    1 
ATOM   13142 C  C     . GLU A 1 3108 ? 230.720 239.936 169.512 1.00 8.53  ? 3108 GLU A C     1 
ATOM   13143 O  O     . GLU A 1 3108 ? 231.073 238.971 168.828 1.00 12.19 ? 3108 GLU A O     1 
ATOM   13144 C  CB    . GLU A 1 3108 ? 231.860 240.360 171.710 1.00 10.86 ? 3108 GLU A CB    1 
ATOM   13145 C  CG    . GLU A 1 3108 ? 232.194 238.891 171.923 1.00 14.71 ? 3108 GLU A CG    1 
ATOM   13146 C  CD    . GLU A 1 3108 ? 233.605 238.527 171.495 1.00 23.13 ? 3108 GLU A CD    1 
ATOM   13147 O  OE1   . GLU A 1 3108 ? 234.361 239.424 171.063 1.00 22.23 ? 3108 GLU A OE1   1 
ATOM   13148 O  OE2   . GLU A 1 3108 ? 233.957 237.333 171.586 1.00 25.35 ? 3108 GLU A OE2   1 
ATOM   13149 N  N     . PHE A 1 3109 ? 229.439 240.287 169.641 1.00 6.20  ? 3109 PHE A N     1 
ATOM   13150 C  CA    . PHE A 1 3109 ? 228.383 239.467 169.059 1.00 6.04  ? 3109 PHE A CA    1 
ATOM   13151 C  C     . PHE A 1 3109 ? 228.296 239.645 167.547 1.00 5.79  ? 3109 PHE A C     1 
ATOM   13152 O  O     . PHE A 1 3109 ? 227.824 238.742 166.847 1.00 9.91  ? 3109 PHE A O     1 
ATOM   13153 C  CB    . PHE A 1 3109 ? 227.046 239.797 169.725 1.00 4.43  ? 3109 PHE A CB    1 
ATOM   13154 C  CG    . PHE A 1 3109 ? 225.940 238.836 169.394 1.00 5.25  ? 3109 PHE A CG    1 
ATOM   13155 C  CD1   . PHE A 1 3109 ? 225.135 239.032 168.286 1.00 3.33  ? 3109 PHE A CD1   1 
ATOM   13156 C  CD2   . PHE A 1 3109 ? 225.706 237.732 170.201 1.00 2.86  ? 3109 PHE A CD2   1 
ATOM   13157 C  CE1   . PHE A 1 3109 ? 224.120 238.147 167.985 1.00 1.29  ? 3109 PHE A CE1   1 
ATOM   13158 C  CE2   . PHE A 1 3109 ? 224.692 236.843 169.904 1.00 1.63  ? 3109 PHE A CE2   1 
ATOM   13159 C  CZ    . PHE A 1 3109 ? 223.897 237.053 168.795 1.00 3.41  ? 3109 PHE A CZ    1 
ATOM   13160 N  N     . THR A 1 3110 ? 228.744 240.785 167.024 1.00 6.94  ? 3110 THR A N     1 
ATOM   13161 C  CA    . THR A 1 3110 ? 228.690 241.062 165.595 1.00 7.77  ? 3110 THR A CA    1 
ATOM   13162 C  C     . THR A 1 3110 ? 229.996 240.741 164.878 1.00 9.36  ? 3110 THR A C     1 
ATOM   13163 O  O     . THR A 1 3110 ? 230.215 241.229 163.766 1.00 11.55 ? 3110 THR A O     1 
ATOM   13164 C  CB    . THR A 1 3110 ? 228.314 242.526 165.349 1.00 6.05  ? 3110 THR A CB    1 
ATOM   13165 O  OG1   . THR A 1 3110 ? 229.256 243.383 166.007 1.00 9.26  ? 3110 THR A OG1   1 
ATOM   13166 C  CG2   . THR A 1 3110 ? 226.922 242.812 165.887 1.00 3.79  ? 3110 THR A CG2   1 
ATOM   13167 N  N     . SER A 1 3111 ? 230.876 239.949 165.492 1.00 12.13 ? 3111 SER A N     1 
ATOM   13168 C  CA    . SER A 1 3111 ? 232.113 239.563 164.822 1.00 9.04  ? 3111 SER A CA    1 
ATOM   13169 C  C     . SER A 1 3111 ? 231.827 238.702 163.596 1.00 10.50 ? 3111 SER A C     1 
ATOM   13170 O  O     . SER A 1 3111 ? 232.467 238.858 162.550 1.00 12.30 ? 3111 SER A O     1 
ATOM   13171 C  CB    . SER A 1 3111 ? 233.031 238.832 165.800 1.00 14.08 ? 3111 SER A CB    1 
ATOM   13172 O  OG    . SER A 1 3111 ? 233.306 239.635 166.934 1.00 21.74 ? 3111 SER A OG    1 
ATOM   13173 N  N     . LYS A 1 3112 ? 230.865 237.782 163.713 1.00 12.82 ? 3112 LYS A N     1 
ATOM   13174 C  CA    . LYS A 1 3112 ? 230.467 236.964 162.570 1.00 10.95 ? 3112 LYS A CA    1 
ATOM   13175 C  C     . LYS A 1 3112 ? 229.875 237.813 161.453 1.00 10.93 ? 3112 LYS A C     1 
ATOM   13176 O  O     . LYS A 1 3112 ? 229.924 237.422 160.283 1.00 10.79 ? 3112 LYS A O     1 
ATOM   13177 C  CB    . LYS A 1 3112 ? 229.457 235.908 163.017 1.00 18.44 ? 3112 LYS A CB    1 
ATOM   13178 C  CG    . LYS A 1 3112 ? 228.289 236.486 163.800 1.00 17.53 ? 3112 LYS A CG    1 
ATOM   13179 C  CD    . LYS A 1 3112 ? 227.395 235.403 164.382 1.00 23.25 ? 3112 LYS A CD    1 
ATOM   13180 C  CE    . LYS A 1 3112 ? 226.294 236.010 165.242 1.00 20.63 ? 3112 LYS A CE    1 
ATOM   13181 N  NZ    . LYS A 1 3112 ? 225.417 234.978 165.854 1.00 16.50 ? 3112 LYS A NZ    1 
ATOM   13182 N  N     . MET A 1 3113 ? 229.305 238.960 161.804 1.00 16.55 ? 3113 MET A N     1 
ATOM   13183 C  CA    . MET A 1 3113 ? 228.697 239.855 160.831 1.00 10.00 ? 3113 MET A CA    1 
ATOM   13184 C  C     . MET A 1 3113 ? 229.750 240.384 159.862 1.00 12.93 ? 3113 MET A C     1 
ATOM   13185 O  O     . MET A 1 3113 ? 230.903 240.619 160.231 1.00 15.33 ? 3113 MET A O     1 
ATOM   13186 C  CB    . MET A 1 3113 ? 228.032 241.016 161.569 1.00 10.42 ? 3113 MET A CB    1 
ATOM   13187 C  CG    . MET A 1 3113 ? 226.724 240.667 162.258 1.00 8.02  ? 3113 MET A CG    1 
ATOM   13188 S  SD    . MET A 1 3113 ? 225.779 242.142 162.672 1.00 26.88 ? 3113 MET A SD    1 
ATOM   13189 C  CE    . MET A 1 3113 ? 224.407 242.016 161.558 1.00 2.51  ? 3113 MET A CE    1 
ATOM   13190 N  N     . ASP A 1 3114 ? 229.344 240.566 158.605 1.00 16.03 ? 3114 ASP A N     1 
ATOM   13191 C  CA    . ASP A 1 3114 ? 230.215 241.141 157.584 1.00 13.07 ? 3114 ASP A CA    1 
ATOM   13192 C  C     . ASP A 1 3114 ? 229.872 242.622 157.452 1.00 14.48 ? 3114 ASP A C     1 
ATOM   13193 O  O     . ASP A 1 3114 ? 229.187 243.056 156.525 1.00 21.37 ? 3114 ASP A O     1 
ATOM   13194 C  CB    . ASP A 1 3114 ? 230.071 240.395 156.261 1.00 16.90 ? 3114 ASP A CB    1 
ATOM   13195 C  CG    . ASP A 1 3114 ? 230.920 240.996 155.160 1.00 27.93 ? 3114 ASP A CG    1 
ATOM   13196 O  OD1   . ASP A 1 3114 ? 232.137 241.174 155.376 1.00 34.89 ? 3114 ASP A OD1   1 
ATOM   13197 O  OD2   . ASP A 1 3114 ? 230.373 241.290 154.075 1.00 35.12 ? 3114 ASP A OD2   1 
ATOM   13198 N  N     . LEU A 1 3115 ? 230.364 243.408 158.410 1.00 16.47 ? 3115 LEU A N     1 
ATOM   13199 C  CA    . LEU A 1 3115 ? 230.073 244.831 158.491 1.00 10.54 ? 3115 LEU A CA    1 
ATOM   13200 C  C     . LEU A 1 3115 ? 231.222 245.694 157.987 1.00 13.60 ? 3115 LEU A C     1 
ATOM   13201 O  O     . LEU A 1 3115 ? 231.322 246.866 158.366 1.00 19.51 ? 3115 LEU A O     1 
ATOM   13202 C  CB    . LEU A 1 3115 ? 229.724 245.214 159.929 1.00 9.19  ? 3115 LEU A CB    1 
ATOM   13203 C  CG    . LEU A 1 3115 ? 228.566 244.440 160.557 1.00 12.35 ? 3115 LEU A CG    1 
ATOM   13204 C  CD1   . LEU A 1 3115 ? 228.323 244.900 161.985 1.00 8.49  ? 3115 LEU A CD1   1 
ATOM   13205 C  CD2   . LEU A 1 3115 ? 227.306 244.583 159.717 1.00 10.25 ? 3115 LEU A CD2   1 
ATOM   13206 N  N     . GLU A 1 3116 ? 232.085 245.146 157.141 1.00 16.88 ? 3116 GLU A N     1 
ATOM   13207 C  CA    . GLU A 1 3116 ? 233.253 245.868 156.654 1.00 17.74 ? 3116 GLU A CA    1 
ATOM   13208 C  C     . GLU A 1 3116 ? 232.883 246.651 155.400 1.00 19.30 ? 3116 GLU A C     1 
ATOM   13209 O  O     . GLU A 1 3116 ? 232.511 246.064 154.379 1.00 25.53 ? 3116 GLU A O     1 
ATOM   13210 C  CB    . GLU A 1 3116 ? 234.404 244.904 156.372 1.00 16.44 ? 3116 GLU A CB    1 
ATOM   13211 C  CG    . GLU A 1 3116 ? 234.998 244.239 157.614 1.00 22.28 ? 3116 GLU A CG    1 
ATOM   13212 C  CD    . GLU A 1 3116 ? 235.673 245.209 158.577 1.00 27.94 ? 3116 GLU A CD    1 
ATOM   13213 O  OE1   . GLU A 1 3116 ? 236.160 244.747 159.630 1.00 26.68 ? 3116 GLU A OE1   1 
ATOM   13214 O  OE2   . GLU A 1 3116 ? 235.749 246.421 158.282 1.00 26.06 ? 3116 GLU A OE2   1 
ATOM   13215 N  N     . LYS A 1 3117 ? 232.972 247.977 155.485 1.00 20.71 ? 3117 LYS A N     1 
ATOM   13216 C  CA    . LYS A 1 3117 ? 232.740 248.868 154.349 1.00 19.46 ? 3117 LYS A CA    1 
ATOM   13217 C  C     . LYS A 1 3117 ? 233.948 249.786 154.237 1.00 21.75 ? 3117 LYS A C     1 
ATOM   13218 O  O     . LYS A 1 3117 ? 233.994 250.851 154.868 1.00 20.14 ? 3117 LYS A O     1 
ATOM   13219 C  CB    . LYS A 1 3117 ? 231.443 249.661 154.511 1.00 17.46 ? 3117 LYS A CB    1 
ATOM   13220 C  CG    . LYS A 1 3117 ? 231.089 250.502 153.296 1.00 18.18 ? 3117 LYS A CG    1 
ATOM   13221 C  CD    . LYS A 1 3117 ? 229.640 250.966 153.318 1.00 15.71 ? 3117 LYS A CD    1 
ATOM   13222 C  CE    . LYS A 1 3117 ? 229.373 251.908 154.474 1.00 18.64 ? 3117 LYS A CE    1 
ATOM   13223 N  NZ    . LYS A 1 3117 ? 227.963 252.379 154.499 1.00 20.88 ? 3117 LYS A NZ    1 
ATOM   13224 N  N     . PRO A 1 3118 ? 234.956 249.399 153.449 1.00 22.86 ? 3118 PRO A N     1 
ATOM   13225 C  CA    . PRO A 1 3118 ? 236.163 250.235 153.339 1.00 21.71 ? 3118 PRO A CA    1 
ATOM   13226 C  C     . PRO A 1 3118 ? 235.897 251.623 152.786 1.00 24.46 ? 3118 PRO A C     1 
ATOM   13227 O  O     . PRO A 1 3118 ? 236.671 252.547 153.059 1.00 26.25 ? 3118 PRO A O     1 
ATOM   13228 C  CB    . PRO A 1 3118 ? 237.066 249.418 152.402 1.00 18.17 ? 3118 PRO A CB    1 
ATOM   13229 C  CG    . PRO A 1 3118 ? 236.125 248.534 151.647 1.00 20.35 ? 3118 PRO A CG    1 
ATOM   13230 C  CD    . PRO A 1 3118 ? 235.049 248.185 152.626 1.00 21.76 ? 3118 PRO A CD    1 
ATOM   13231 N  N     . ASN A 1 3119 ? 234.824 251.799 152.018 1.00 22.53 ? 3119 ASN A N     1 
ATOM   13232 C  CA    . ASN A 1 3119 ? 234.495 253.089 151.426 1.00 17.70 ? 3119 ASN A CA    1 
ATOM   13233 C  C     . ASN A 1 3119 ? 233.677 253.981 152.351 1.00 23.34 ? 3119 ASN A C     1 
ATOM   13234 O  O     . ASN A 1 3119 ? 233.268 255.066 151.926 1.00 28.02 ? 3119 ASN A O     1 
ATOM   13235 C  CB    . ASN A 1 3119 ? 233.743 252.882 150.109 1.00 20.75 ? 3119 ASN A CB    1 
ATOM   13236 C  CG    . ASN A 1 3119 ? 232.459 252.094 150.286 1.00 24.98 ? 3119 ASN A CG    1 
ATOM   13237 O  OD1   . ASN A 1 3119 ? 231.491 252.580 150.871 1.00 24.39 ? 3119 ASN A OD1   1 
ATOM   13238 N  ND2   . ASN A 1 3119 ? 232.446 250.868 149.777 1.00 27.87 ? 3119 ASN A ND2   1 
ATOM   13239 N  N     . TYR A 1 3120 ? 233.418 253.551 153.584 1.00 23.23 ? 3120 TYR A N     1 
ATOM   13240 C  CA    . TYR A 1 3120 ? 232.638 254.352 154.518 1.00 16.54 ? 3120 TYR A CA    1 
ATOM   13241 C  C     . TYR A 1 3120 ? 233.343 255.670 154.817 1.00 16.24 ? 3120 TYR A C     1 
ATOM   13242 O  O     . TYR A 1 3120 ? 234.562 255.716 154.995 1.00 19.84 ? 3120 TYR A O     1 
ATOM   13243 C  CB    . TYR A 1 3120 ? 232.408 253.560 155.808 1.00 16.95 ? 3120 TYR A CB    1 
ATOM   13244 C  CG    . TYR A 1 3120 ? 231.848 254.358 156.965 1.00 13.70 ? 3120 TYR A CG    1 
ATOM   13245 C  CD1   . TYR A 1 3120 ? 230.498 254.664 157.031 1.00 11.16 ? 3120 TYR A CD1   1 
ATOM   13246 C  CD2   . TYR A 1 3120 ? 232.665 254.781 158.004 1.00 12.07 ? 3120 TYR A CD2   1 
ATOM   13247 C  CE1   . TYR A 1 3120 ? 229.977 255.380 158.088 1.00 12.19 ? 3120 TYR A CE1   1 
ATOM   13248 C  CE2   . TYR A 1 3120 ? 232.155 255.502 159.066 1.00 10.68 ? 3120 TYR A CE2   1 
ATOM   13249 C  CZ    . TYR A 1 3120 ? 230.810 255.798 159.104 1.00 13.96 ? 3120 TYR A CZ    1 
ATOM   13250 O  OH    . TYR A 1 3120 ? 230.294 256.514 160.159 1.00 14.77 ? 3120 TYR A OH    1 
ATOM   13251 N  N     . ILE A 1 3121 ? 232.566 256.751 154.862 1.00 14.53 ? 3121 ILE A N     1 
ATOM   13252 C  CA    . ILE A 1 3121 ? 233.081 258.082 155.169 1.00 15.15 ? 3121 ILE A CA    1 
ATOM   13253 C  C     . ILE A 1 3121 ? 232.647 258.454 156.578 1.00 14.57 ? 3121 ILE A C     1 
ATOM   13254 O  O     . ILE A 1 3121 ? 231.456 258.394 156.905 1.00 18.57 ? 3121 ILE A O     1 
ATOM   13255 C  CB    . ILE A 1 3121 ? 232.590 259.137 154.160 1.00 18.07 ? 3121 ILE A CB    1 
ATOM   13256 C  CG1   . ILE A 1 3121 ? 233.083 258.843 152.742 1.00 17.67 ? 3121 ILE A CG1   1 
ATOM   13257 C  CG2   . ILE A 1 3121 ? 233.031 260.528 154.587 1.00 17.61 ? 3121 ILE A CG2   1 
ATOM   13258 C  CD1   . ILE A 1 3121 ? 232.162 257.951 151.941 1.00 16.02 ? 3121 ILE A CD1   1 
ATOM   13259 N  N     . VAL A 1 3122 ? 233.608 258.842 157.410 1.00 15.33 ? 3122 VAL A N     1 
ATOM   13260 C  CA    . VAL A 1 3122 ? 233.305 259.294 158.765 1.00 12.86 ? 3122 VAL A CA    1 
ATOM   13261 C  C     . VAL A 1 3122 ? 232.728 260.700 158.692 1.00 17.35 ? 3122 VAL A C     1 
ATOM   13262 O  O     . VAL A 1 3122 ? 233.374 261.605 158.142 1.00 24.16 ? 3122 VAL A O     1 
ATOM   13263 C  CB    . VAL A 1 3122 ? 234.548 259.251 159.663 1.00 15.55 ? 3122 VAL A CB    1 
ATOM   13264 C  CG1   . VAL A 1 3122 ? 234.227 259.819 161.034 1.00 18.60 ? 3122 VAL A CG1   1 
ATOM   13265 C  CG2   . VAL A 1 3122 ? 235.065 257.833 159.779 1.00 11.59 ? 3122 VAL A CG2   1 
ATOM   13266 N  N     . PRO A 1 3123 ? 231.531 260.932 159.223 1.00 15.22 ? 3123 PRO A N     1 
ATOM   13267 C  CA    . PRO A 1 3123 ? 230.963 262.282 159.197 1.00 16.28 ? 3123 PRO A CA    1 
ATOM   13268 C  C     . PRO A 1 3123 ? 231.744 263.232 160.091 1.00 22.45 ? 3123 PRO A C     1 
ATOM   13269 O  O     . PRO A 1 3123 ? 232.411 262.820 161.042 1.00 28.63 ? 3123 PRO A O     1 
ATOM   13270 C  CB    . PRO A 1 3123 ? 229.537 262.076 159.720 1.00 19.11 ? 3123 PRO A CB    1 
ATOM   13271 C  CG    . PRO A 1 3123 ? 229.628 260.844 160.554 1.00 15.17 ? 3123 PRO A CG    1 
ATOM   13272 C  CD    . PRO A 1 3123 ? 230.626 259.964 159.863 1.00 16.16 ? 3123 PRO A CD    1 
ATOM   13273 N  N     . ASP A 1 3124 ? 231.658 264.523 159.767 1.00 24.03 ? 3124 ASP A N     1 
ATOM   13274 C  CA    . ASP A 1 3124 ? 232.298 265.542 160.592 1.00 26.05 ? 3124 ASP A CA    1 
ATOM   13275 C  C     . ASP A 1 3124 ? 231.728 265.536 162.003 1.00 30.85 ? 3124 ASP A C     1 
ATOM   13276 O  O     . ASP A 1 3124 ? 232.468 265.606 162.990 1.00 34.66 ? 3124 ASP A O     1 
ATOM   13277 C  CB    . ASP A 1 3124 ? 232.137 266.917 159.944 1.00 24.93 ? 3124 ASP A CB    1 
ATOM   13278 C  CG    . ASP A 1 3124 ? 232.707 266.971 158.541 1.00 33.43 ? 3124 ASP A CG    1 
ATOM   13279 O  OD1   . ASP A 1 3124 ? 233.923 266.732 158.383 1.00 32.17 ? 3124 ASP A OD1   1 
ATOM   13280 O  OD2   . ASP A 1 3124 ? 231.940 267.251 157.595 1.00 34.30 ? 3124 ASP A OD2   1 
ATOM   13281 N  N     . TYR A 1 3125 ? 230.404 265.454 162.118 1.00 28.01 ? 3125 TYR A N     1 
ATOM   13282 C  CA    . TYR A 1 3125 ? 229.740 265.326 163.413 1.00 27.39 ? 3125 TYR A CA    1 
ATOM   13283 C  C     . TYR A 1 3125 ? 229.281 263.880 163.555 1.00 31.86 ? 3125 TYR A C     1 
ATOM   13284 O  O     . TYR A 1 3125 ? 228.277 263.473 162.965 1.00 27.84 ? 3125 TYR A O     1 
ATOM   13285 C  CB    . TYR A 1 3125 ? 228.581 266.310 163.534 1.00 27.23 ? 3125 TYR A CB    1 
ATOM   13286 C  CG    . TYR A 1 3125 ? 227.689 266.079 164.737 1.00 31.00 ? 3125 TYR A CG    1 
ATOM   13287 C  CD1   . TYR A 1 3125 ? 227.992 266.644 165.969 1.00 27.78 ? 3125 TYR A CD1   1 
ATOM   13288 C  CD2   . TYR A 1 3125 ? 226.529 265.317 164.635 1.00 37.24 ? 3125 TYR A CD2   1 
ATOM   13289 C  CE1   . TYR A 1 3125 ? 227.179 266.441 167.069 1.00 30.49 ? 3125 TYR A CE1   1 
ATOM   13290 C  CE2   . TYR A 1 3125 ? 225.711 265.108 165.729 1.00 30.85 ? 3125 TYR A CE2   1 
ATOM   13291 C  CZ    . TYR A 1 3125 ? 226.040 265.674 166.943 1.00 35.26 ? 3125 TYR A CZ    1 
ATOM   13292 O  OH    . TYR A 1 3125 ? 225.228 265.472 168.034 1.00 39.89 ? 3125 TYR A OH    1 
ATOM   13293 N  N     . MET A 1 3126 ? 230.028 263.101 164.322 1.00 35.18 ? 3126 MET A N     1 
ATOM   13294 C  CA    . MET A 1 3126 ? 229.730 261.693 164.566 1.00 22.21 ? 3126 MET A CA    1 
ATOM   13295 C  C     . MET A 1 3126 ? 228.852 261.563 165.804 1.00 22.09 ? 3126 MET A C     1 
ATOM   13296 O  O     . MET A 1 3126 ? 229.246 262.024 166.883 1.00 19.50 ? 3126 MET A O     1 
ATOM   13297 C  CB    . MET A 1 3126 ? 231.017 260.902 164.756 1.00 19.20 ? 3126 MET A CB    1 
ATOM   13298 C  CG    . MET A 1 3126 ? 230.842 259.394 164.862 1.00 19.54 ? 3126 MET A CG    1 
ATOM   13299 S  SD    . MET A 1 3126 ? 230.241 258.610 163.356 1.00 42.38 ? 3126 MET A SD    1 
ATOM   13300 C  CE    . MET A 1 3126 ? 229.506 257.125 164.028 1.00 11.72 ? 3126 MET A CE    1 
ATOM   13301 N  N     . PRO A 1 3127 ? 227.668 260.959 165.696 1.00 22.31 ? 3127 PRO A N     1 
ATOM   13302 C  CA    . PRO A 1 3127 ? 226.779 260.819 166.862 1.00 14.59 ? 3127 PRO A CA    1 
ATOM   13303 C  C     . PRO A 1 3127 ? 227.289 259.775 167.851 1.00 19.05 ? 3127 PRO A C     1 
ATOM   13304 O  O     . PRO A 1 3127 ? 226.731 258.685 168.000 1.00 18.54 ? 3127 PRO A O     1 
ATOM   13305 C  CB    . PRO A 1 3127 ? 225.448 260.422 166.209 1.00 13.73 ? 3127 PRO A CB    1 
ATOM   13306 C  CG    . PRO A 1 3127 ? 225.850 259.672 164.990 1.00 13.63 ? 3127 PRO A CG    1 
ATOM   13307 C  CD    . PRO A 1 3127 ? 227.109 260.325 164.488 1.00 14.96 ? 3127 PRO A CD    1 
ATOM   13308 N  N     . VAL A 1 3128 ? 228.372 260.121 168.547 1.00 18.68 ? 3128 VAL A N     1 
ATOM   13309 C  CA    . VAL A 1 3128 ? 229.065 259.164 169.400 1.00 18.76 ? 3128 VAL A CA    1 
ATOM   13310 C  C     . VAL A 1 3128 ? 228.306 258.993 170.709 1.00 19.53 ? 3128 VAL A C     1 
ATOM   13311 O  O     . VAL A 1 3128 ? 227.961 259.973 171.383 1.00 17.89 ? 3128 VAL A O     1 
ATOM   13312 C  CB    . VAL A 1 3128 ? 230.507 259.626 169.654 1.00 21.65 ? 3128 VAL A CB    1 
ATOM   13313 C  CG1   . VAL A 1 3128 ? 231.200 258.690 170.619 1.00 16.14 ? 3128 VAL A CG1   1 
ATOM   13314 C  CG2   . VAL A 1 3128 ? 231.274 259.717 168.346 1.00 23.30 ? 3128 VAL A CG2   1 
ATOM   13315 N  N     . VAL A 1 3129 ? 228.043 257.740 171.077 1.00 16.84 ? 3129 VAL A N     1 
ATOM   13316 C  CA    . VAL A 1 3129 ? 227.434 257.431 172.363 1.00 9.45  ? 3129 VAL A CA    1 
ATOM   13317 C  C     . VAL A 1 3129 ? 228.371 256.668 173.289 1.00 10.52 ? 3129 VAL A C     1 
ATOM   13318 O  O     . VAL A 1 3129 ? 228.134 256.655 174.508 1.00 10.75 ? 3129 VAL A O     1 
ATOM   13319 C  CB    . VAL A 1 3129 ? 226.115 256.650 172.182 1.00 13.45 ? 3129 VAL A CB    1 
ATOM   13320 C  CG1   . VAL A 1 3129 ? 225.110 257.483 171.406 1.00 10.12 ? 3129 VAL A CG1   1 
ATOM   13321 C  CG2   . VAL A 1 3129 ? 226.365 255.325 171.493 1.00 6.56  ? 3129 VAL A CG2   1 
ATOM   13322 N  N     . TYR A 1 3130 ? 229.420 256.040 172.768 1.00 14.27 ? 3130 TYR A N     1 
ATOM   13323 C  CA    . TYR A 1 3130 ? 230.431 255.359 173.569 1.00 7.86  ? 3130 TYR A CA    1 
ATOM   13324 C  C     . TYR A 1 3130 ? 231.640 256.279 173.689 1.00 15.58 ? 3130 TYR A C     1 
ATOM   13325 O  O     . TYR A 1 3130 ? 232.279 256.609 172.685 1.00 17.60 ? 3130 TYR A O     1 
ATOM   13326 C  CB    . TYR A 1 3130 ? 230.806 254.026 172.927 1.00 7.83  ? 3130 TYR A CB    1 
ATOM   13327 C  CG    . TYR A 1 3130 ? 231.887 253.254 173.648 1.00 8.02  ? 3130 TYR A CG    1 
ATOM   13328 C  CD1   . TYR A 1 3130 ? 231.934 253.202 175.035 1.00 6.55  ? 3130 TYR A CD1   1 
ATOM   13329 C  CD2   . TYR A 1 3130 ? 232.863 252.576 172.934 1.00 5.96  ? 3130 TYR A CD2   1 
ATOM   13330 C  CE1   . TYR A 1 3130 ? 232.927 252.495 175.687 1.00 8.43  ? 3130 TYR A CE1   1 
ATOM   13331 C  CE2   . TYR A 1 3130 ? 233.855 251.869 173.575 1.00 9.53  ? 3130 TYR A CE2   1 
ATOM   13332 C  CZ    . TYR A 1 3130 ? 233.885 251.831 174.949 1.00 11.58 ? 3130 TYR A CZ    1 
ATOM   13333 O  OH    . TYR A 1 3130 ? 234.879 251.122 175.583 1.00 17.42 ? 3130 TYR A OH    1 
ATOM   13334 N  N     . ASP A 1 3131 ? 231.962 256.680 174.924 1.00 18.82 ? 3131 ASP A N     1 
ATOM   13335 C  CA    . ASP A 1 3131 ? 232.999 257.684 175.136 1.00 17.14 ? 3131 ASP A CA    1 
ATOM   13336 C  C     . ASP A 1 3131 ? 234.355 257.238 174.602 1.00 17.84 ? 3131 ASP A C     1 
ATOM   13337 O  O     . ASP A 1 3131 ? 235.141 258.072 174.137 1.00 25.06 ? 3131 ASP A O     1 
ATOM   13338 C  CB    . ASP A 1 3131 ? 233.108 258.025 176.621 1.00 17.34 ? 3131 ASP A CB    1 
ATOM   13339 C  CG    . ASP A 1 3131 ? 231.899 258.776 177.140 1.00 29.35 ? 3131 ASP A CG    1 
ATOM   13340 O  OD1   . ASP A 1 3131 ? 231.265 259.507 176.351 1.00 29.04 ? 3131 ASP A OD1   1 
ATOM   13341 O  OD2   . ASP A 1 3131 ? 231.585 258.641 178.342 1.00 30.56 ? 3131 ASP A OD2   1 
ATOM   13342 N  N     . LYS A 1 3132 ? 234.649 255.941 174.646 1.00 11.57 ? 3132 LYS A N     1 
ATOM   13343 C  CA    . LYS A 1 3132 ? 235.929 255.432 174.174 1.00 15.48 ? 3132 LYS A CA    1 
ATOM   13344 C  C     . LYS A 1 3132 ? 235.854 254.857 172.766 1.00 15.22 ? 3132 LYS A C     1 
ATOM   13345 O  O     . LYS A 1 3132 ? 236.706 254.041 172.396 1.00 17.53 ? 3132 LYS A O     1 
ATOM   13346 C  CB    . LYS A 1 3132 ? 236.479 254.383 175.139 1.00 14.46 ? 3132 LYS A CB    1 
ATOM   13347 C  CG    . LYS A 1 3132 ? 236.867 254.940 176.496 1.00 16.00 ? 3132 LYS A CG    1 
ATOM   13348 C  CD    . LYS A 1 3132 ? 237.560 253.886 177.343 1.00 19.22 ? 3132 LYS A CD    1 
ATOM   13349 C  CE    . LYS A 1 3132 ? 236.584 252.847 177.864 1.00 23.98 ? 3132 LYS A CE    1 
ATOM   13350 N  NZ    . LYS A 1 3132 ? 237.254 251.884 178.781 1.00 28.86 ? 3132 LYS A NZ    1 
ATOM   13351 N  N     . LEU A 1 3133 ? 234.861 255.248 171.979 1.00 16.63 ? 3133 LEU A N     1 
ATOM   13352 C  CA    . LEU A 1 3133 ? 234.829 254.888 170.569 1.00 13.94 ? 3133 LEU A CA    1 
ATOM   13353 C  C     . LEU A 1 3133 ? 236.008 255.546 169.860 1.00 15.53 ? 3133 LEU A C     1 
ATOM   13354 O  O     . LEU A 1 3133 ? 236.225 256.755 170.032 1.00 24.70 ? 3133 LEU A O     1 
ATOM   13355 C  CB    . LEU A 1 3133 ? 233.509 255.320 169.936 1.00 12.74 ? 3133 LEU A CB    1 
ATOM   13356 C  CG    . LEU A 1 3133 ? 233.274 254.954 168.467 1.00 14.68 ? 3133 LEU A CG    1 
ATOM   13357 C  CD1   . LEU A 1 3133 ? 233.198 253.447 168.294 1.00 8.00  ? 3133 LEU A CD1   1 
ATOM   13358 C  CD2   . LEU A 1 3133 ? 232.016 255.619 167.940 1.00 14.93 ? 3133 LEU A CD2   1 
ATOM   13359 N  N     . PRO A 1 3134 ? 236.796 254.801 169.077 1.00 14.50 ? 3134 PRO A N     1 
ATOM   13360 C  CA    . PRO A 1 3134 ? 238.000 255.382 168.463 1.00 17.62 ? 3134 PRO A CA    1 
ATOM   13361 C  C     . PRO A 1 3134 ? 237.729 256.600 167.593 1.00 24.94 ? 3134 PRO A C     1 
ATOM   13362 O  O     . PRO A 1 3134 ? 236.707 256.672 166.903 1.00 28.76 ? 3134 PRO A O     1 
ATOM   13363 C  CB    . PRO A 1 3134 ? 238.545 254.211 167.641 1.00 16.35 ? 3134 PRO A CB    1 
ATOM   13364 C  CG    . PRO A 1 3134 ? 238.209 253.033 168.494 1.00 11.93 ? 3134 PRO A CG    1 
ATOM   13365 C  CD    . PRO A 1 3134 ? 236.803 253.330 168.982 1.00 12.32 ? 3134 PRO A CD    1 
ATOM   13366 N  N     . GLN A 1 3135 ? 238.652 257.566 167.634 1.00 24.15 ? 3135 GLN A N     1 
ATOM   13367 C  CA    . GLN A 1 3135 ? 238.431 258.858 166.986 1.00 20.90 ? 3135 GLN A CA    1 
ATOM   13368 C  C     . GLN A 1 3135 ? 238.175 258.746 165.487 1.00 24.98 ? 3135 GLN A C     1 
ATOM   13369 O  O     . GLN A 1 3135 ? 237.300 259.471 164.984 1.00 34.41 ? 3135 GLN A O     1 
ATOM   13370 C  CB    . GLN A 1 3135 ? 239.608 259.794 167.284 1.00 28.82 ? 3135 GLN A CB    1 
ATOM   13371 C  CG    . GLN A 1 3135 ? 239.822 260.094 168.760 1.00 30.92 ? 3135 GLN A CG    1 
ATOM   13372 C  CD    . GLN A 1 3135 ? 238.606 260.721 169.410 1.00 36.49 ? 3135 GLN A CD    1 
ATOM   13373 O  OE1   . GLN A 1 3135 ? 238.115 261.758 168.965 1.00 31.66 ? 3135 GLN A OE1   1 
ATOM   13374 N  NE2   . GLN A 1 3135 ? 238.116 260.095 170.475 1.00 36.83 ? 3135 GLN A NE2   1 
ATOM   13375 N  N     . PRO A 1 3136 ? 238.924 257.960 164.713 1.00 23.02 ? 3136 PRO A N     1 
ATOM   13376 C  CA    . PRO A 1 3136 ? 238.481 257.619 163.355 1.00 17.82 ? 3136 PRO A CA    1 
ATOM   13377 C  C     . PRO A 1 3136 ? 237.695 256.320 163.345 1.00 23.86 ? 3136 PRO A C     1 
ATOM   13378 O  O     . PRO A 1 3136 ? 238.259 255.257 163.043 1.00 26.08 ? 3136 PRO A O     1 
ATOM   13379 C  CB    . PRO A 1 3136 ? 239.799 257.484 162.582 1.00 17.89 ? 3136 PRO A CB    1 
ATOM   13380 C  CG    . PRO A 1 3136 ? 240.802 257.062 163.615 1.00 22.41 ? 3136 PRO A CG    1 
ATOM   13381 C  CD    . PRO A 1 3136 ? 240.260 257.398 164.990 1.00 22.13 ? 3136 PRO A CD    1 
ATOM   13382 N  N     . PRO A 1 3137 ? 236.404 256.346 163.683 1.00 20.54 ? 3137 PRO A N     1 
ATOM   13383 C  CA    . PRO A 1 3137 ? 235.656 255.088 163.774 1.00 18.78 ? 3137 PRO A CA    1 
ATOM   13384 C  C     . PRO A 1 3137 ? 235.557 254.410 162.416 1.00 16.63 ? 3137 PRO A C     1 
ATOM   13385 O  O     . PRO A 1 3137 ? 235.485 255.066 161.376 1.00 21.88 ? 3137 PRO A O     1 
ATOM   13386 C  CB    . PRO A 1 3137 ? 234.281 255.531 164.280 1.00 17.21 ? 3137 PRO A CB    1 
ATOM   13387 C  CG    . PRO A 1 3137 ? 234.127 256.899 163.740 1.00 20.42 ? 3137 PRO A CG    1 
ATOM   13388 C  CD    . PRO A 1 3137 ? 235.504 257.512 163.713 1.00 20.73 ? 3137 PRO A CD    1 
ATOM   13389 N  N     . SER A 1 3138 ? 235.565 253.081 162.434 1.00 16.22 ? 3138 SER A N     1 
ATOM   13390 C  CA    . SER A 1 3138 ? 235.328 252.308 161.228 1.00 12.00 ? 3138 SER A CA    1 
ATOM   13391 C  C     . SER A 1 3138 ? 233.827 252.096 161.049 1.00 11.70 ? 3138 SER A C     1 
ATOM   13392 O  O     . SER A 1 3138 ? 233.016 252.471 161.899 1.00 12.77 ? 3138 SER A O     1 
ATOM   13393 C  CB    . SER A 1 3138 ? 236.079 250.980 161.286 1.00 13.81 ? 3138 SER A CB    1 
ATOM   13394 O  OG    . SER A 1 3138 ? 235.524 250.125 162.269 1.00 16.35 ? 3138 SER A OG    1 
ATOM   13395 N  N     . HIS A 1 3139 ? 233.449 251.490 159.921 1.00 15.81 ? 3139 HIS A N     1 
ATOM   13396 C  CA    . HIS A 1 3139 ? 232.033 251.245 159.663 1.00 8.51  ? 3139 HIS A CA    1 
ATOM   13397 C  C     . HIS A 1 3139 ? 231.442 250.285 160.689 1.00 8.22  ? 3139 HIS A C     1 
ATOM   13398 O  O     . HIS A 1 3139 ? 230.317 250.485 161.159 1.00 9.81  ? 3139 HIS A O     1 
ATOM   13399 C  CB    . HIS A 1 3139 ? 231.840 250.706 158.246 1.00 10.10 ? 3139 HIS A CB    1 
ATOM   13400 C  CG    . HIS A 1 3139 ? 230.422 250.350 157.927 1.00 14.43 ? 3139 HIS A CG    1 
ATOM   13401 N  ND1   . HIS A 1 3139 ? 230.004 249.052 157.737 1.00 10.29 ? 3139 HIS A ND1   1 
ATOM   13402 C  CD2   . HIS A 1 3139 ? 229.321 251.126 157.784 1.00 7.89  ? 3139 HIS A CD2   1 
ATOM   13403 C  CE1   . HIS A 1 3139 ? 228.708 249.042 157.478 1.00 10.97 ? 3139 HIS A CE1   1 
ATOM   13404 N  NE2   . HIS A 1 3139 ? 228.270 250.288 157.501 1.00 10.84 ? 3139 HIS A NE2   1 
ATOM   13405 N  N     . ARG A 1 3140 ? 232.186 249.235 161.043 1.00 10.43 ? 3140 ARG A N     1 
ATOM   13406 C  CA    . ARG A 1 3140 ? 231.735 248.327 162.093 1.00 6.38  ? 3140 ARG A CA    1 
ATOM   13407 C  C     . ARG A 1 3140 ? 231.635 249.042 163.433 1.00 5.06  ? 3140 ARG A C     1 
ATOM   13408 O  O     . ARG A 1 3140 ? 230.688 248.822 164.196 1.00 6.83  ? 3140 ARG A O     1 
ATOM   13409 C  CB    . ARG A 1 3140 ? 232.682 247.131 162.187 1.00 7.13  ? 3140 ARG A CB    1 
ATOM   13410 C  CG    . ARG A 1 3140 ? 232.228 246.045 163.141 1.00 6.84  ? 3140 ARG A CG    1 
ATOM   13411 C  CD    . ARG A 1 3140 ? 233.314 245.004 163.329 1.00 3.91  ? 3140 ARG A CD    1 
ATOM   13412 N  NE    . ARG A 1 3140 ? 233.484 244.172 162.142 1.00 7.09  ? 3140 ARG A NE    1 
ATOM   13413 C  CZ    . ARG A 1 3140 ? 232.663 243.193 161.790 1.00 10.20 ? 3140 ARG A CZ    1 
ATOM   13414 N  NH1   . ARG A 1 3140 ? 231.606 242.877 162.521 1.00 9.52  ? 3140 ARG A NH1   1 
ATOM   13415 N  NH2   . ARG A 1 3140 ? 232.907 242.514 160.673 1.00 12.95 ? 3140 ARG A NH2   1 
ATOM   13416 N  N     . GLU A 1 3141 ? 232.607 249.903 163.733 1.00 10.99 ? 3141 GLU A N     1 
ATOM   13417 C  CA    . GLU A 1 3141 ? 232.564 250.682 164.966 1.00 9.43  ? 3141 GLU A CA    1 
ATOM   13418 C  C     . GLU A 1 3141 ? 231.353 251.604 164.994 1.00 7.17  ? 3141 GLU A C     1 
ATOM   13419 O  O     . GLU A 1 3141 ? 230.733 251.797 166.045 1.00 6.59  ? 3141 GLU A O     1 
ATOM   13420 C  CB    . GLU A 1 3141 ? 233.857 251.479 165.108 1.00 8.42  ? 3141 GLU A CB    1 
ATOM   13421 C  CG    . GLU A 1 3141 ? 235.041 250.651 165.560 1.00 11.07 ? 3141 GLU A CG    1 
ATOM   13422 C  CD    . GLU A 1 3141 ? 236.362 251.317 165.240 1.00 24.11 ? 3141 GLU A CD    1 
ATOM   13423 O  OE1   . GLU A 1 3141 ? 236.736 252.262 165.954 1.00 22.37 ? 3141 GLU A OE1   1 
ATOM   13424 O  OE2   . GLU A 1 3141 ? 237.037 250.882 164.285 1.00 25.16 ? 3141 GLU A OE2   1 
ATOM   13425 N  N     . ALA A 1 3142 ? 231.009 252.193 163.847 1.00 7.60  ? 3142 ALA A N     1 
ATOM   13426 C  CA    . ALA A 1 3142 ? 229.819 253.031 163.770 1.00 6.16  ? 3142 ALA A CA    1 
ATOM   13427 C  C     . ALA A 1 3142 ? 228.548 252.208 163.945 1.00 5.58  ? 3142 ALA A C     1 
ATOM   13428 O  O     . ALA A 1 3142 ? 227.595 252.662 164.591 1.00 7.38  ? 3142 ALA A O     1 
ATOM   13429 C  CB    . ALA A 1 3142 ? 229.795 253.787 162.443 1.00 5.29  ? 3142 ALA A CB    1 
ATOM   13430 N  N     . ILE A 1 3143 ? 228.512 251.000 163.375 1.00 3.28  ? 3143 ILE A N     1 
ATOM   13431 C  CA    . ILE A 1 3143 ? 227.322 250.157 163.478 1.00 2.69  ? 3143 ILE A CA    1 
ATOM   13432 C  C     . ILE A 1 3143 ? 227.060 249.776 164.928 1.00 4.17  ? 3143 ILE A C     1 
ATOM   13433 O  O     . ILE A 1 3143 ? 225.937 249.907 165.430 1.00 6.59  ? 3143 ILE A O     1 
ATOM   13434 C  CB    . ILE A 1 3143 ? 227.470 248.908 162.590 1.00 3.18  ? 3143 ILE A CB    1 
ATOM   13435 C  CG1   . ILE A 1 3143 ? 227.298 249.269 161.114 1.00 2.97  ? 3143 ILE A CG1   1 
ATOM   13436 C  CG2   . ILE A 1 3143 ? 226.460 247.845 162.996 1.00 3.18  ? 3143 ILE A CG2   1 
ATOM   13437 C  CD1   . ILE A 1 3143 ? 225.867 249.522 160.715 1.00 2.15  ? 3143 ILE A CD1   1 
ATOM   13438 N  N     . VAL A 1 3144 ? 228.093 249.299 165.625 1.00 5.58  ? 3144 VAL A N     1 
ATOM   13439 C  CA    . VAL A 1 3144 ? 227.932 248.919 167.024 1.00 2.55  ? 3144 VAL A CA    1 
ATOM   13440 C  C     . VAL A 1 3144 ? 227.593 250.139 167.867 1.00 2.32  ? 3144 VAL A C     1 
ATOM   13441 O  O     . VAL A 1 3144 ? 226.779 250.063 168.796 1.00 3.32  ? 3144 VAL A O     1 
ATOM   13442 C  CB    . VAL A 1 3144 ? 229.198 248.204 167.533 1.00 3.30  ? 3144 VAL A CB    1 
ATOM   13443 C  CG1   . VAL A 1 3144 ? 229.069 247.874 169.008 1.00 1.67  ? 3144 VAL A CG1   1 
ATOM   13444 C  CG2   . VAL A 1 3144 ? 229.452 246.942 166.725 1.00 2.52  ? 3144 VAL A CG2   1 
ATOM   13445 N  N     . ASN A 1 3145 ? 228.193 251.287 167.545 1.00 3.49  ? 3145 ASN A N     1 
ATOM   13446 C  CA    . ASN A 1 3145 ? 227.844 252.526 168.230 1.00 3.08  ? 3145 ASN A CA    1 
ATOM   13447 C  C     . ASN A 1 3145 ? 226.374 252.864 168.029 1.00 2.42  ? 3145 ASN A C     1 
ATOM   13448 O  O     . ASN A 1 3145 ? 225.697 253.312 168.961 1.00 2.60  ? 3145 ASN A O     1 
ATOM   13449 C  CB    . ASN A 1 3145 ? 228.733 253.664 167.727 1.00 3.09  ? 3145 ASN A CB    1 
ATOM   13450 C  CG    . ASN A 1 3145 ? 228.635 254.905 168.585 1.00 7.59  ? 3145 ASN A CG    1 
ATOM   13451 O  OD1   . ASN A 1 3145 ? 228.994 254.890 169.761 1.00 14.25 ? 3145 ASN A OD1   1 
ATOM   13452 N  ND2   . ASN A 1 3145 ? 228.144 255.990 168.002 1.00 9.44  ? 3145 ASN A ND2   1 
ATOM   13453 N  N     . SER A 1 3146 ? 225.860 252.657 166.814 1.00 2.60  ? 3146 SER A N     1 
ATOM   13454 C  CA    . SER A 1 3146 ? 224.441 252.877 166.557 1.00 1.88  ? 3146 SER A CA    1 
ATOM   13455 C  C     . SER A 1 3146 ? 223.580 251.868 167.305 1.00 1.27  ? 3146 SER A C     1 
ATOM   13456 O  O     . SER A 1 3146 ? 222.483 252.203 167.766 1.00 0.60  ? 3146 SER A O     1 
ATOM   13457 C  CB    . SER A 1 3146 ? 224.164 252.811 165.055 1.00 3.24  ? 3146 SER A CB    1 
ATOM   13458 O  OG    . SER A 1 3146 ? 224.927 253.777 164.355 1.00 7.96  ? 3146 SER A OG    1 
ATOM   13459 N  N     . CYS A 1 3147 ? 224.055 250.626 167.426 1.00 2.91  ? 3147 CYS A N     1 
ATOM   13460 C  CA    . CYS A 1 3147 ? 223.322 249.624 168.192 1.00 0.74  ? 3147 CYS A CA    1 
ATOM   13461 C  C     . CYS A 1 3147 ? 223.213 250.024 169.657 1.00 0.51  ? 3147 CYS A C     1 
ATOM   13462 O  O     . CYS A 1 3147 ? 222.175 249.809 170.292 1.00 0.45  ? 3147 CYS A O     1 
ATOM   13463 C  CB    . CYS A 1 3147 ? 223.993 248.258 168.056 1.00 0.71  ? 3147 CYS A CB    1 
ATOM   13464 S  SG    . CYS A 1 3147 ? 223.892 247.517 166.412 1.00 4.88  ? 3147 CYS A SG    1 
ATOM   13465 N  N     . VAL A 1 3148 ? 224.280 250.599 170.214 1.00 0.53  ? 3148 VAL A N     1 
ATOM   13466 C  CA    . VAL A 1 3148 ? 224.225 251.090 171.587 1.00 0.44  ? 3148 VAL A CA    1 
ATOM   13467 C  C     . VAL A 1 3148 ? 223.231 252.236 171.698 1.00 0.35  ? 3148 VAL A C     1 
ATOM   13468 O  O     . VAL A 1 3148 ? 222.462 252.318 172.664 1.00 0.37  ? 3148 VAL A O     1 
ATOM   13469 C  CB    . VAL A 1 3148 ? 225.630 251.508 172.067 1.00 0.67  ? 3148 VAL A CB    1 
ATOM   13470 C  CG1   . VAL A 1 3148 ? 225.564 252.085 173.471 1.00 0.96  ? 3148 VAL A CG1   1 
ATOM   13471 C  CG2   . VAL A 1 3148 ? 226.577 250.329 172.020 1.00 0.46  ? 3148 VAL A CG2   1 
ATOM   13472 N  N     . PHE A 1 3149 ? 223.220 253.132 170.708 1.00 0.45  ? 3149 PHE A N     1 
ATOM   13473 C  CA    . PHE A 1 3149 ? 222.324 254.281 170.748 1.00 0.34  ? 3149 PHE A CA    1 
ATOM   13474 C  C     . PHE A 1 3149 ? 220.863 253.848 170.765 1.00 0.43  ? 3149 PHE A C     1 
ATOM   13475 O  O     . PHE A 1 3149 ? 220.041 254.444 171.471 1.00 0.49  ? 3149 PHE A O     1 
ATOM   13476 C  CB    . PHE A 1 3149 ? 222.587 255.200 169.555 1.00 0.57  ? 3149 PHE A CB    1 
ATOM   13477 C  CG    . PHE A 1 3149 ? 221.554 256.278 169.385 1.00 0.80  ? 3149 PHE A CG    1 
ATOM   13478 C  CD1   . PHE A 1 3149 ? 221.640 257.454 170.108 1.00 0.49  ? 3149 PHE A CD1   1 
ATOM   13479 C  CD2   . PHE A 1 3149 ? 220.493 256.114 168.508 1.00 0.77  ? 3149 PHE A CD2   1 
ATOM   13480 C  CE1   . PHE A 1 3149 ? 220.692 258.446 169.960 1.00 0.71  ? 3149 PHE A CE1   1 
ATOM   13481 C  CE2   . PHE A 1 3149 ? 219.541 257.102 168.361 1.00 0.55  ? 3149 PHE A CE2   1 
ATOM   13482 C  CZ    . PHE A 1 3149 ? 219.641 258.270 169.086 1.00 0.72  ? 3149 PHE A CZ    1 
ATOM   13483 N  N     . VAL A 1 3150 ? 220.520 252.822 169.984 1.00 0.38  ? 3150 VAL A N     1 
ATOM   13484 C  CA    . VAL A 1 3150 ? 219.127 252.388 169.887 1.00 0.27  ? 3150 VAL A CA    1 
ATOM   13485 C  C     . VAL A 1 3150 ? 218.621 251.909 171.240 1.00 0.45  ? 3150 VAL A C     1 
ATOM   13486 O  O     . VAL A 1 3150 ? 217.500 252.236 171.651 1.00 1.31  ? 3150 VAL A O     1 
ATOM   13487 C  CB    . VAL A 1 3150 ? 218.983 251.300 168.807 1.00 0.24  ? 3150 VAL A CB    1 
ATOM   13488 C  CG1   . VAL A 1 3150 ? 217.609 250.668 168.871 1.00 0.14  ? 3150 VAL A CG1   1 
ATOM   13489 C  CG2   . VAL A 1 3150 ? 219.239 251.882 167.428 1.00 0.19  ? 3150 VAL A CG2   1 
ATOM   13490 N  N     . HIS A 1 3151 ? 219.438 251.133 171.955 1.00 0.51  ? 3151 HIS A N     1 
ATOM   13491 C  CA    . HIS A 1 3151 ? 219.039 250.643 173.270 1.00 0.19  ? 3151 HIS A CA    1 
ATOM   13492 C  C     . HIS A 1 3151 ? 218.810 251.789 174.246 1.00 0.72  ? 3151 HIS A C     1 
ATOM   13493 O  O     . HIS A 1 3151 ? 217.838 251.781 175.008 1.00 0.87  ? 3151 HIS A O     1 
ATOM   13494 C  CB    . HIS A 1 3151 ? 220.099 249.683 173.811 1.00 0.21  ? 3151 HIS A CB    1 
ATOM   13495 C  CG    . HIS A 1 3151 ? 219.742 249.075 175.131 1.00 0.09  ? 3151 HIS A CG    1 
ATOM   13496 N  ND1   . HIS A 1 3151 ? 218.868 248.018 175.254 1.00 0.06  ? 3151 HIS A ND1   1 
ATOM   13497 C  CD2   . HIS A 1 3151 ? 220.145 249.377 176.387 1.00 0.08  ? 3151 HIS A CD2   1 
ATOM   13498 C  CE1   . HIS A 1 3151 ? 218.745 247.696 176.527 1.00 0.10  ? 3151 HIS A CE1   1 
ATOM   13499 N  NE2   . HIS A 1 3151 ? 219.509 248.507 177.237 1.00 0.24  ? 3151 HIS A NE2   1 
ATOM   13500 N  N     . GLN A 1 3152 ? 219.694 252.788 174.235 1.00 0.80  ? 3152 GLN A N     1 
ATOM   13501 C  CA    . GLN A 1 3152 ? 219.552 253.924 175.135 1.00 1.08  ? 3152 GLN A CA    1 
ATOM   13502 C  C     . GLN A 1 3152 ? 218.351 254.793 174.787 1.00 1.54  ? 3152 GLN A C     1 
ATOM   13503 O  O     . GLN A 1 3152 ? 217.859 255.522 175.654 1.00 2.85  ? 3152 GLN A O     1 
ATOM   13504 C  CB    . GLN A 1 3152 ? 220.832 254.760 175.121 1.00 1.38  ? 3152 GLN A CB    1 
ATOM   13505 C  CG    . GLN A 1 3152 ? 222.093 253.936 175.290 1.00 3.76  ? 3152 GLN A CG    1 
ATOM   13506 C  CD    . GLN A 1 3152 ? 223.220 254.706 175.942 1.00 5.55  ? 3152 GLN A CD    1 
ATOM   13507 O  OE1   . GLN A 1 3152 ? 223.852 254.226 176.883 1.00 7.24  ? 3152 GLN A OE1   1 
ATOM   13508 N  NE2   . GLN A 1 3152 ? 223.485 255.905 175.441 1.00 6.54  ? 3152 GLN A NE2   1 
ATOM   13509 N  N     . THR A 1 3153 ? 217.873 254.731 173.544 1.00 1.16  ? 3153 THR A N     1 
ATOM   13510 C  CA    . THR A 1 3153 ? 216.691 255.495 173.163 1.00 1.34  ? 3153 THR A CA    1 
ATOM   13511 C  C     . THR A 1 3153 ? 215.441 254.981 173.872 1.00 1.56  ? 3153 THR A C     1 
ATOM   13512 O  O     . THR A 1 3153 ? 214.562 255.775 174.228 1.00 2.67  ? 3153 THR A O     1 
ATOM   13513 C  CB    . THR A 1 3153 ? 216.516 255.450 171.641 1.00 1.01  ? 3153 THR A CB    1 
ATOM   13514 O  OG1   . THR A 1 3153 ? 217.559 256.210 171.021 1.00 1.35  ? 3153 THR A OG1   1 
ATOM   13515 C  CG2   . THR A 1 3153 ? 215.181 256.032 171.227 1.00 4.69  ? 3153 THR A CG2   1 
ATOM   13516 N  N     . LEU A 1 3154 ? 215.354 253.670 174.105 1.00 1.05  ? 3154 LEU A N     1 
ATOM   13517 C  CA    . LEU A 1 3154 ? 214.195 253.120 174.800 1.00 1.37  ? 3154 LEU A CA    1 
ATOM   13518 C  C     . LEU A 1 3154 ? 214.108 253.617 176.235 1.00 2.31  ? 3154 LEU A C     1 
ATOM   13519 O  O     . LEU A 1 3154 ? 213.004 253.790 176.764 1.00 4.71  ? 3154 LEU A O     1 
ATOM   13520 C  CB    . LEU A 1 3154 ? 214.224 251.591 174.765 1.00 0.88  ? 3154 LEU A CB    1 
ATOM   13521 C  CG    . LEU A 1 3154 ? 213.657 250.915 173.515 1.00 0.32  ? 3154 LEU A CG    1 
ATOM   13522 C  CD1   . LEU A 1 3154 ? 212.173 251.222 173.372 1.00 0.51  ? 3154 LEU A CD1   1 
ATOM   13523 C  CD2   . LEU A 1 3154 ? 214.409 251.284 172.249 1.00 0.19  ? 3154 LEU A CD2   1 
ATOM   13524 N  N     . HIS A 1 3155 ? 215.252 253.838 176.887 1.00 2.10  ? 3155 HIS A N     1 
ATOM   13525 C  CA    . HIS A 1 3155 ? 215.231 254.444 178.214 1.00 2.51  ? 3155 HIS A CA    1 
ATOM   13526 C  C     . HIS A 1 3155 ? 214.685 255.863 178.160 1.00 3.85  ? 3155 HIS A C     1 
ATOM   13527 O  O     . HIS A 1 3155 ? 213.886 256.263 179.013 1.00 9.38  ? 3155 HIS A O     1 
ATOM   13528 C  CB    . HIS A 1 3155 ? 216.631 254.423 178.823 1.00 2.34  ? 3155 HIS A CB    1 
ATOM   13529 C  CG    . HIS A 1 3155 ? 217.087 253.061 179.236 1.00 2.41  ? 3155 HIS A CG    1 
ATOM   13530 N  ND1   . HIS A 1 3155 ? 218.164 252.429 178.654 1.00 3.06  ? 3155 HIS A ND1   1 
ATOM   13531 C  CD2   . HIS A 1 3155 ? 216.610 252.207 180.171 1.00 2.78  ? 3155 HIS A CD2   1 
ATOM   13532 C  CE1   . HIS A 1 3155 ? 218.333 251.246 179.214 1.00 4.16  ? 3155 HIS A CE1   1 
ATOM   13533 N  NE2   . HIS A 1 3155 ? 217.403 251.086 180.138 1.00 5.66  ? 3155 HIS A NE2   1 
ATOM   13534 N  N     . GLN A 1 3156 ? 215.105 256.639 177.159 1.00 4.89  ? 3156 GLN A N     1 
ATOM   13535 C  CA    . GLN A 1 3156 ? 214.520 257.960 176.952 1.00 6.76  ? 3156 GLN A CA    1 
ATOM   13536 C  C     . GLN A 1 3156 ? 213.040 257.849 176.613 1.00 7.89  ? 3156 GLN A C     1 
ATOM   13537 O  O     . GLN A 1 3156 ? 212.224 258.647 177.089 1.00 12.57 ? 3156 GLN A O     1 
ATOM   13538 C  CB    . GLN A 1 3156 ? 215.269 258.701 175.843 1.00 6.61  ? 3156 GLN A CB    1 
ATOM   13539 C  CG    . GLN A 1 3156 ? 216.799 258.764 175.971 1.00 6.76  ? 3156 GLN A CG    1 
ATOM   13540 C  CD    . GLN A 1 3156 ? 217.317 259.469 177.228 1.00 20.87 ? 3156 GLN A CD    1 
ATOM   13541 O  OE1   . GLN A 1 3156 ? 216.711 259.425 178.299 1.00 15.97 ? 3156 GLN A OE1   1 
ATOM   13542 N  NE2   . GLN A 1 3156 ? 218.461 260.126 177.085 1.00 23.60 ? 3156 GLN A NE2   1 
ATOM   13543 N  N     . ALA A 1 3157 ? 212.679 256.863 175.790 1.00 8.49  ? 3157 ALA A N     1 
ATOM   13544 C  CA    . ALA A 1 3157 ? 211.285 256.682 175.404 1.00 7.96  ? 3157 ALA A CA    1 
ATOM   13545 C  C     . ALA A 1 3157 ? 210.414 256.332 176.603 1.00 8.77  ? 3157 ALA A C     1 
ATOM   13546 O  O     . ALA A 1 3157 ? 209.304 256.857 176.744 1.00 9.76  ? 3157 ALA A O     1 
ATOM   13547 C  CB    . ALA A 1 3157 ? 211.180 255.601 174.327 1.00 3.53  ? 3157 ALA A CB    1 
ATOM   13548 N  N     . ASN A 1 3158 ? 210.894 255.445 177.479 1.00 8.74  ? 3158 ASN A N     1 
ATOM   13549 C  CA    . ASN A 1 3158 ? 210.127 255.113 178.675 1.00 6.76  ? 3158 ASN A CA    1 
ATOM   13550 C  C     . ASN A 1 3158 ? 209.962 256.326 179.579 1.00 10.20 ? 3158 ASN A C     1 
ATOM   13551 O  O     . ASN A 1 3158 ? 208.899 256.524 180.175 1.00 13.59 ? 3158 ASN A O     1 
ATOM   13552 C  CB    . ASN A 1 3158 ? 210.791 253.967 179.437 1.00 5.30  ? 3158 ASN A CB    1 
ATOM   13553 C  CG    . ASN A 1 3158 ? 210.398 252.605 178.903 1.00 4.90  ? 3158 ASN A CG    1 
ATOM   13554 O  OD1   . ASN A 1 3158 ? 209.719 252.497 177.886 1.00 5.80  ? 3158 ASN A OD1   1 
ATOM   13555 N  ND2   . ASN A 1 3158 ? 210.810 251.556 179.605 1.00 4.01  ? 3158 ASN A ND2   1 
ATOM   13556 N  N     . ALA A 1 3159 ? 211.008 257.150 179.690 1.00 14.92 ? 3159 ALA A N     1 
ATOM   13557 C  CA    . ALA A 1 3159 ? 210.940 258.331 180.544 1.00 10.26 ? 3159 ALA A CA    1 
ATOM   13558 C  C     . ALA A 1 3159 ? 209.872 259.305 180.062 1.00 11.93 ? 3159 ALA A C     1 
ATOM   13559 O  O     . ALA A 1 3159 ? 209.154 259.900 180.873 1.00 20.24 ? 3159 ALA A O     1 
ATOM   13560 C  CB    . ALA A 1 3159 ? 212.306 259.013 180.600 1.00 9.65  ? 3159 ALA A CB    1 
ATOM   13561 N  N     . ARG A 1 3160 ? 209.755 259.486 178.744 1.00 13.16 ? 3160 ARG A N     1 
ATOM   13562 C  CA    . ARG A 1 3160 ? 208.752 260.402 178.208 1.00 13.82 ? 3160 ARG A CA    1 
ATOM   13563 C  C     . ARG A 1 3160 ? 207.337 259.921 178.504 1.00 18.41 ? 3160 ARG A C     1 
ATOM   13564 O  O     . ARG A 1 3160 ? 206.471 260.717 178.883 1.00 29.79 ? 3160 ARG A O     1 
ATOM   13565 C  CB    . ARG A 1 3160 ? 208.957 260.588 176.706 1.00 16.52 ? 3160 ARG A CB    1 
ATOM   13566 C  CG    . ARG A 1 3160 ? 210.010 261.629 176.360 1.00 22.74 ? 3160 ARG A CG    1 
ATOM   13567 C  CD    . ARG A 1 3160 ? 210.086 261.890 174.863 1.00 26.00 ? 3160 ARG A CD    1 
ATOM   13568 N  NE    . ARG A 1 3160 ? 208.774 262.082 174.258 1.00 22.17 ? 3160 ARG A NE    1 
ATOM   13569 C  CZ    . ARG A 1 3160 ? 208.312 261.375 173.236 1.00 29.63 ? 3160 ARG A CZ    1 
ATOM   13570 N  NH1   . ARG A 1 3160 ? 209.028 260.411 172.682 1.00 28.48 ? 3160 ARG A NH1   1 
ATOM   13571 N  NH2   . ARG A 1 3160 ? 207.101 261.646 172.753 1.00 29.11 ? 3160 ARG A NH2   1 
ATOM   13572 N  N     . LEU A 1 3161 ? 207.072 258.624 178.332 1.00 11.73 ? 3161 LEU A N     1 
ATOM   13573 C  CA    . LEU A 1 3161 ? 205.740 258.114 178.646 1.00 13.32 ? 3161 LEU A CA    1 
ATOM   13574 C  C     . LEU A 1 3161 ? 205.489 258.101 180.148 1.00 16.01 ? 3161 LEU A C     1 
ATOM   13575 O  O     . LEU A 1 3161 ? 204.365 258.355 180.595 1.00 18.29 ? 3161 LEU A O     1 
ATOM   13576 C  CB    . LEU A 1 3161 ? 205.540 256.720 178.054 1.00 9.56  ? 3161 LEU A CB    1 
ATOM   13577 C  CG    . LEU A 1 3161 ? 205.196 256.617 176.564 1.00 12.87 ? 3161 LEU A CG    1 
ATOM   13578 C  CD1   . LEU A 1 3161 ? 206.373 256.960 175.669 1.00 14.14 ? 3161 LEU A CD1   1 
ATOM   13579 C  CD2   . LEU A 1 3161 ? 204.659 255.230 176.242 1.00 10.13 ? 3161 LEU A CD2   1 
ATOM   13580 N  N     . ALA A 1 3162 ? 206.519 257.804 180.945 1.00 14.73 ? 3162 ALA A N     1 
ATOM   13581 C  CA    . ALA A 1 3162 ? 206.355 257.821 182.393 1.00 14.62 ? 3162 ALA A CA    1 
ATOM   13582 C  C     . ALA A 1 3162 ? 206.042 259.225 182.897 1.00 23.17 ? 3162 ALA A C     1 
ATOM   13583 O  O     . ALA A 1 3162 ? 205.177 259.400 183.764 1.00 26.41 ? 3162 ALA A O     1 
ATOM   13584 C  CB    . ALA A 1 3162 ? 207.608 257.271 183.072 1.00 13.75 ? 3162 ALA A CB    1 
ATOM   13585 N  N     . LYS A 1 3163 ? 206.724 260.238 182.358 1.00 22.29 ? 3163 LYS A N     1 
ATOM   13586 C  CA    . LYS A 1 3163 ? 206.478 261.612 182.779 1.00 20.36 ? 3163 LYS A CA    1 
ATOM   13587 C  C     . LYS A 1 3163 ? 205.094 262.106 182.373 1.00 20.32 ? 3163 LYS A C     1 
ATOM   13588 O  O     . LYS A 1 3163 ? 204.589 263.055 182.980 1.00 33.45 ? 3163 LYS A O     1 
ATOM   13589 C  CB    . LYS A 1 3163 ? 207.558 262.538 182.213 1.00 22.27 ? 3163 LYS A CB    1 
ATOM   13590 C  CG    . LYS A 1 3163 ? 207.270 263.062 180.816 1.00 23.28 ? 3163 LYS A CG    1 
ATOM   13591 C  CD    . LYS A 1 3163 ? 208.486 263.749 180.219 1.00 24.66 ? 3163 LYS A CD    1 
ATOM   13592 C  CE    . LYS A 1 3163 ? 208.231 264.162 178.778 1.00 26.49 ? 3163 LYS A CE    1 
ATOM   13593 N  NZ    . LYS A 1 3163 ? 207.027 265.031 178.653 1.00 27.22 ? 3163 LYS A NZ    1 
ATOM   13594 N  N     . ARG A 1 3164 ? 204.472 261.487 181.370 1.00 17.17 ? 3164 ARG A N     1 
ATOM   13595 C  CA    . ARG A 1 3164 ? 203.109 261.811 180.971 1.00 19.08 ? 3164 ARG A CA    1 
ATOM   13596 C  C     . ARG A 1 3164 ? 202.079 260.896 181.617 1.00 19.53 ? 3164 ARG A C     1 
ATOM   13597 O  O     . ARG A 1 3164 ? 200.901 260.954 181.256 1.00 17.95 ? 3164 ARG A O     1 
ATOM   13598 C  CB    . ARG A 1 3164 ? 202.967 261.746 179.448 1.00 16.31 ? 3164 ARG A CB    1 
ATOM   13599 C  CG    . ARG A 1 3164 ? 203.951 262.606 178.680 1.00 24.93 ? 3164 ARG A CG    1 
ATOM   13600 C  CD    . ARG A 1 3164 ? 203.529 262.740 177.224 1.00 28.02 ? 3164 ARG A CD    1 
ATOM   13601 N  NE    . ARG A 1 3164 ? 204.147 261.728 176.375 1.00 34.36 ? 3164 ARG A NE    1 
ATOM   13602 C  CZ    . ARG A 1 3164 ? 205.430 261.701 176.041 1.00 32.44 ? 3164 ARG A CZ    1 
ATOM   13603 N  NH1   . ARG A 1 3164 ? 206.270 262.641 176.442 1.00 28.65 ? 3164 ARG A NH1   1 
ATOM   13604 N  NH2   . ARG A 1 3164 ? 205.882 260.707 175.281 1.00 28.55 ? 3164 ARG A NH2   1 
ATOM   13605 N  N     . GLY A 1 3165 ? 202.495 260.046 182.553 1.00 22.72 ? 3165 GLY A N     1 
ATOM   13606 C  CA    . GLY A 1 3165 ? 201.585 259.112 183.179 1.00 18.89 ? 3165 GLY A CA    1 
ATOM   13607 C  C     . GLY A 1 3165 ? 201.305 257.861 182.382 1.00 21.51 ? 3165 GLY A C     1 
ATOM   13608 O  O     . GLY A 1 3165 ? 200.472 257.050 182.802 1.00 20.86 ? 3165 GLY A O     1 
ATOM   13609 N  N     . GLY A 1 3166 ? 201.969 257.676 181.243 1.00 23.67 ? 3166 GLY A N     1 
ATOM   13610 C  CA    . GLY A 1 3166 ? 201.765 256.481 180.457 1.00 16.23 ? 3166 GLY A CA    1 
ATOM   13611 C  C     . GLY A 1 3166 ? 202.398 255.260 181.100 1.00 16.63 ? 3166 GLY A C     1 
ATOM   13612 O  O     . GLY A 1 3166 ? 203.288 255.354 181.943 1.00 12.52 ? 3166 GLY A O     1 
ATOM   13613 N  N     . ARG A 1 3167 ? 201.918 254.094 180.684 1.00 17.29 ? 3167 ARG A N     1 
ATOM   13614 C  CA    . ARG A 1 3167 ? 202.407 252.831 181.216 1.00 14.43 ? 3167 ARG A CA    1 
ATOM   13615 C  C     . ARG A 1 3167 ? 203.643 252.405 180.436 1.00 12.62 ? 3167 ARG A C     1 
ATOM   13616 O  O     . ARG A 1 3167 ? 203.628 252.376 179.202 1.00 12.34 ? 3167 ARG A O     1 
ATOM   13617 C  CB    . ARG A 1 3167 ? 201.321 251.760 181.126 1.00 17.76 ? 3167 ARG A CB    1 
ATOM   13618 C  CG    . ARG A 1 3167 ? 200.257 251.845 182.211 1.00 22.17 ? 3167 ARG A CG    1 
ATOM   13619 C  CD    . ARG A 1 3167 ? 199.295 253.003 181.958 1.00 27.57 ? 3167 ARG A CD    1 
ATOM   13620 N  NE    . ARG A 1 3167 ? 198.232 253.073 182.952 1.00 30.45 ? 3167 ARG A NE    1 
ATOM   13621 C  CZ    . ARG A 1 3167 ? 197.081 252.423 182.859 1.00 26.46 ? 3167 ARG A CZ    1 
ATOM   13622 N  NH1   . ARG A 1 3167 ? 196.800 251.669 181.810 1.00 23.22 ? 3167 ARG A NH1   1 
ATOM   13623 N  NH2   . ARG A 1 3167 ? 196.189 252.540 183.837 1.00 24.11 ? 3167 ARG A NH2   1 
ATOM   13624 N  N     . THR A 1 3168 ? 204.717 252.085 181.153 1.00 7.96  ? 3168 THR A N     1 
ATOM   13625 C  CA    . THR A 1 3168 ? 205.974 251.699 180.533 1.00 8.86  ? 3168 THR A CA    1 
ATOM   13626 C  C     . THR A 1 3168 ? 206.412 250.341 181.058 1.00 7.26  ? 3168 THR A C     1 
ATOM   13627 O  O     . THR A 1 3168 ? 206.077 249.953 182.180 1.00 8.22  ? 3168 THR A O     1 
ATOM   13628 C  CB    . THR A 1 3168 ? 207.090 252.730 180.791 1.00 6.86  ? 3168 THR A CB    1 
ATOM   13629 O  OG1   . THR A 1 3168 ? 207.383 252.783 182.193 1.00 10.53 ? 3168 THR A OG1   1 
ATOM   13630 C  CG2   . THR A 1 3168 ? 206.663 254.104 180.318 1.00 10.96 ? 3168 THR A CG2   1 
ATOM   13631 N  N     . MET A 1 3169 ? 207.162 249.621 180.230 1.00 6.64  ? 3169 MET A N     1 
ATOM   13632 C  CA    . MET A 1 3169 ? 207.707 248.325 180.595 1.00 4.45  ? 3169 MET A CA    1 
ATOM   13633 C  C     . MET A 1 3169 ? 209.224 248.413 180.663 1.00 3.81  ? 3169 MET A C     1 
ATOM   13634 O  O     . MET A 1 3169 ? 209.853 249.173 179.920 1.00 4.17  ? 3169 MET A O     1 
ATOM   13635 C  CB    . MET A 1 3169 ? 207.275 247.244 179.601 1.00 3.89  ? 3169 MET A CB    1 
ATOM   13636 C  CG    . MET A 1 3169 ? 205.775 247.034 179.594 1.00 4.90  ? 3169 MET A CG    1 
ATOM   13637 S  SD    . MET A 1 3169 ? 205.172 246.217 181.079 1.00 22.67 ? 3169 MET A SD    1 
ATOM   13638 C  CE    . MET A 1 3169 ? 203.434 246.076 180.690 1.00 12.39 ? 3169 MET A CE    1 
ATOM   13639 N  N     . ALA A 1 3170 ? 209.804 247.635 181.573 1.00 3.39  ? 3170 ALA A N     1 
ATOM   13640 C  CA    . ALA A 1 3170 ? 211.230 247.740 181.857 1.00 2.43  ? 3170 ALA A CA    1 
ATOM   13641 C  C     . ALA A 1 3170 ? 212.065 247.390 180.633 1.00 1.35  ? 3170 ALA A C     1 
ATOM   13642 O  O     . ALA A 1 3170 ? 211.767 246.441 179.903 1.00 1.97  ? 3170 ALA A O     1 
ATOM   13643 C  CB    . ALA A 1 3170 ? 211.601 246.824 183.023 1.00 2.36  ? 3170 ALA A CB    1 
ATOM   13644 N  N     . ILE A 1 3171 ? 213.118 248.167 180.412 1.00 0.93  ? 3171 ILE A N     1 
ATOM   13645 C  CA    . ILE A 1 3171 ? 214.096 247.897 179.369 1.00 0.72  ? 3171 ILE A CA    1 
ATOM   13646 C  C     . ILE A 1 3171 ? 215.289 247.217 180.023 1.00 1.09  ? 3171 ILE A C     1 
ATOM   13647 O  O     . ILE A 1 3171 ? 215.896 247.765 180.952 1.00 2.75  ? 3171 ILE A O     1 
ATOM   13648 C  CB    . ILE A 1 3171 ? 214.515 249.182 178.640 1.00 2.12  ? 3171 ILE A CB    1 
ATOM   13649 C  CG1   . ILE A 1 3171 ? 213.290 249.867 178.028 1.00 1.57  ? 3171 ILE A CG1   1 
ATOM   13650 C  CG2   . ILE A 1 3171 ? 215.545 248.874 177.567 1.00 0.77  ? 3171 ILE A CG2   1 
ATOM   13651 C  CD1   . ILE A 1 3171 ? 212.489 248.976 177.109 1.00 0.84  ? 3171 ILE A CD1   1 
ATOM   13652 N  N     . THR A 1 3172 ? 215.621 246.028 179.547 1.00 0.71  ? 3172 THR A N     1 
ATOM   13653 C  CA    . THR A 1 3172 ? 216.605 245.156 180.162 1.00 0.78  ? 3172 THR A CA    1 
ATOM   13654 C  C     . THR A 1 3172 ? 217.693 244.795 179.160 1.00 0.18  ? 3172 THR A C     1 
ATOM   13655 O  O     . THR A 1 3172 ? 217.513 244.966 177.949 1.00 0.15  ? 3172 THR A O     1 
ATOM   13656 C  CB    . THR A 1 3172 ? 215.939 243.873 180.690 1.00 0.53  ? 3172 THR A CB    1 
ATOM   13657 O  OG1   . THR A 1 3172 ? 215.590 243.021 179.594 1.00 0.88  ? 3172 THR A OG1   1 
ATOM   13658 C  CG2   . THR A 1 3172 ? 214.689 244.207 181.485 1.00 1.21  ? 3172 THR A CG2   1 
ATOM   13659 N  N     . PRO A 1 3173 ? 218.848 244.315 179.631 1.00 0.39  ? 3173 PRO A N     1 
ATOM   13660 C  CA    . PRO A 1 3173 ? 219.873 243.834 178.693 1.00 0.27  ? 3173 PRO A CA    1 
ATOM   13661 C  C     . PRO A 1 3173 ? 219.394 242.709 177.793 1.00 0.07  ? 3173 PRO A C     1 
ATOM   13662 O  O     . PRO A 1 3173 ? 219.957 242.524 176.708 1.00 0.05  ? 3173 PRO A O     1 
ATOM   13663 C  CB    . PRO A 1 3173 ? 221.003 243.369 179.621 1.00 0.19  ? 3173 PRO A CB    1 
ATOM   13664 C  CG    . PRO A 1 3173 ? 220.830 244.194 180.840 1.00 0.12  ? 3173 PRO A CG    1 
ATOM   13665 C  CD    . PRO A 1 3173 ? 219.349 244.343 181.016 1.00 0.17  ? 3173 PRO A CD    1 
ATOM   13666 N  N     . ARG A 1 3174 ? 218.380 241.950 178.206 1.00 0.12  ? 3174 ARG A N     1 
ATOM   13667 C  CA    . ARG A 1 3174 ? 217.837 240.915 177.336 1.00 0.20  ? 3174 ARG A CA    1 
ATOM   13668 C  C     . ARG A 1 3174 ? 217.165 241.508 176.104 1.00 0.11  ? 3174 ARG A C     1 
ATOM   13669 O  O     . ARG A 1 3174 ? 217.091 240.847 175.064 1.00 0.09  ? 3174 ARG A O     1 
ATOM   13670 C  CB    . ARG A 1 3174 ? 216.866 240.032 178.114 1.00 0.34  ? 3174 ARG A CB    1 
ATOM   13671 C  CG    . ARG A 1 3174 ? 217.552 239.179 179.162 1.00 0.60  ? 3174 ARG A CG    1 
ATOM   13672 C  CD    . ARG A 1 3174 ? 216.692 238.014 179.592 1.00 0.71  ? 3174 ARG A CD    1 
ATOM   13673 N  NE    . ARG A 1 3174 ? 216.501 237.047 178.520 1.00 0.84  ? 3174 ARG A NE    1 
ATOM   13674 C  CZ    . ARG A 1 3174 ? 215.713 235.986 178.607 1.00 2.53  ? 3174 ARG A CZ    1 
ATOM   13675 N  NH1   . ARG A 1 3174 ? 215.031 235.720 179.708 1.00 1.64  ? 3174 ARG A NH1   1 
ATOM   13676 N  NH2   . ARG A 1 3174 ? 215.606 235.169 177.562 1.00 3.35  ? 3174 ARG A NH2   1 
ATOM   13677 N  N     . HIS A 1 3175 ? 216.669 242.742 176.200 1.00 0.13  ? 3175 HIS A N     1 
ATOM   13678 C  CA    . HIS A 1 3175 ? 216.216 243.448 175.006 1.00 0.06  ? 3175 HIS A CA    1 
ATOM   13679 C  C     . HIS A 1 3175 ? 217.373 243.700 174.048 1.00 0.06  ? 3175 HIS A C     1 
ATOM   13680 O  O     . HIS A 1 3175 ? 217.227 243.543 172.831 1.00 0.10  ? 3175 HIS A O     1 
ATOM   13681 C  CB    . HIS A 1 3175 ? 215.556 244.769 175.393 1.00 0.17  ? 3175 HIS A CB    1 
ATOM   13682 C  CG    . HIS A 1 3175 ? 214.270 244.614 176.140 1.00 0.22  ? 3175 HIS A CG    1 
ATOM   13683 N  ND1   . HIS A 1 3175 ? 214.220 244.270 177.474 1.00 0.34  ? 3175 HIS A ND1   1 
ATOM   13684 C  CD2   . HIS A 1 3175 ? 212.984 244.777 175.746 1.00 0.23  ? 3175 HIS A CD2   1 
ATOM   13685 C  CE1   . HIS A 1 3175 ? 212.960 244.217 177.866 1.00 0.76  ? 3175 HIS A CE1   1 
ATOM   13686 N  NE2   . HIS A 1 3175 ? 212.191 244.520 176.837 1.00 0.64  ? 3175 HIS A NE2   1 
ATOM   13687 N  N     . TYR A 1 3176 ? 218.529 244.105 174.580 1.00 0.05  ? 3176 TYR A N     1 
ATOM   13688 C  CA    . TYR A 1 3176 ? 219.701 244.333 173.742 1.00 0.04  ? 3176 TYR A CA    1 
ATOM   13689 C  C     . TYR A 1 3176 ? 220.191 243.037 173.111 1.00 0.05  ? 3176 TYR A C     1 
ATOM   13690 O  O     . TYR A 1 3176 ? 220.536 243.006 171.925 1.00 0.04  ? 3176 TYR A O     1 
ATOM   13691 C  CB    . TYR A 1 3176 ? 220.811 244.987 174.570 1.00 0.06  ? 3176 TYR A CB    1 
ATOM   13692 C  CG    . TYR A 1 3176 ? 222.008 245.437 173.767 1.00 0.05  ? 3176 TYR A CG    1 
ATOM   13693 C  CD1   . TYR A 1 3176 ? 221.965 246.605 173.022 1.00 0.08  ? 3176 TYR A CD1   1 
ATOM   13694 C  CD2   . TYR A 1 3176 ? 223.187 244.703 173.767 1.00 0.07  ? 3176 TYR A CD2   1 
ATOM   13695 C  CE1   . TYR A 1 3176 ? 223.054 247.026 172.293 1.00 0.14  ? 3176 TYR A CE1   1 
ATOM   13696 C  CE2   . TYR A 1 3176 ? 224.283 245.118 173.039 1.00 0.09  ? 3176 TYR A CE2   1 
ATOM   13697 C  CZ    . TYR A 1 3176 ? 224.210 246.280 172.303 1.00 0.13  ? 3176 TYR A CZ    1 
ATOM   13698 O  OH    . TYR A 1 3176 ? 225.292 246.705 171.573 1.00 0.51  ? 3176 TYR A OH    1 
ATOM   13699 N  N     . LEU A 1 3177 ? 220.236 241.955 173.893 1.00 0.12  ? 3177 LEU A N     1 
ATOM   13700 C  CA    . LEU A 1 3177 ? 220.605 240.658 173.337 1.00 0.09  ? 3177 LEU A CA    1 
ATOM   13701 C  C     . LEU A 1 3177 ? 219.593 240.208 172.297 1.00 0.09  ? 3177 LEU A C     1 
ATOM   13702 O  O     . LEU A 1 3177 ? 219.960 239.624 171.271 1.00 0.13  ? 3177 LEU A O     1 
ATOM   13703 C  CB    . LEU A 1 3177 ? 220.735 239.629 174.458 1.00 0.08  ? 3177 LEU A CB    1 
ATOM   13704 C  CG    . LEU A 1 3177 ? 221.941 239.840 175.371 1.00 0.16  ? 3177 LEU A CG    1 
ATOM   13705 C  CD1   . LEU A 1 3177 ? 221.715 239.184 176.720 1.00 0.29  ? 3177 LEU A CD1   1 
ATOM   13706 C  CD2   . LEU A 1 3177 ? 223.206 239.312 174.715 1.00 0.10  ? 3177 LEU A CD2   1 
ATOM   13707 N  N     . ASP A 1 3178 ? 218.310 240.472 172.546 1.00 0.07  ? 3178 ASP A N     1 
ATOM   13708 C  CA    . ASP A 1 3178 ? 217.290 240.242 171.533 1.00 0.08  ? 3178 ASP A CA    1 
ATOM   13709 C  C     . ASP A 1 3178 ? 217.568 241.064 170.282 1.00 0.12  ? 3178 ASP A C     1 
ATOM   13710 O  O     . ASP A 1 3178 ? 217.430 240.569 169.160 1.00 0.22  ? 3178 ASP A O     1 
ATOM   13711 C  CB    . ASP A 1 3178 ? 215.915 240.581 172.107 1.00 0.23  ? 3178 ASP A CB    1 
ATOM   13712 C  CG    . ASP A 1 3178 ? 214.835 239.655 171.618 1.00 3.95  ? 3178 ASP A CG    1 
ATOM   13713 O  OD1   . ASP A 1 3178 ? 215.009 239.069 170.532 1.00 9.80  ? 3178 ASP A OD1   1 
ATOM   13714 O  OD2   . ASP A 1 3178 ? 213.813 239.507 172.320 1.00 11.55 ? 3178 ASP A OD2   1 
ATOM   13715 N  N     . PHE A 1 3179 ? 217.975 242.321 170.463 1.00 0.09  ? 3179 PHE A N     1 
ATOM   13716 C  CA    . PHE A 1 3179 ? 218.220 243.214 169.334 1.00 0.03  ? 3179 PHE A CA    1 
ATOM   13717 C  C     . PHE A 1 3179 ? 219.360 242.702 168.458 1.00 0.05  ? 3179 PHE A C     1 
ATOM   13718 O  O     . PHE A 1 3179 ? 219.199 242.543 167.245 1.00 0.12  ? 3179 PHE A O     1 
ATOM   13719 C  CB    . PHE A 1 3179 ? 218.514 244.622 169.865 1.00 0.04  ? 3179 PHE A CB    1 
ATOM   13720 C  CG    . PHE A 1 3179 ? 219.022 245.590 168.828 1.00 0.04  ? 3179 PHE A CG    1 
ATOM   13721 C  CD1   . PHE A 1 3179 ? 218.520 245.594 167.540 1.00 0.03  ? 3179 PHE A CD1   1 
ATOM   13722 C  CD2   . PHE A 1 3179 ? 220.000 246.508 169.156 1.00 0.11  ? 3179 PHE A CD2   1 
ATOM   13723 C  CE1   . PHE A 1 3179 ? 218.992 246.486 166.604 1.00 0.13  ? 3179 PHE A CE1   1 
ATOM   13724 C  CE2   . PHE A 1 3179 ? 220.470 247.405 168.221 1.00 0.21  ? 3179 PHE A CE2   1 
ATOM   13725 C  CZ    . PHE A 1 3179 ? 219.965 247.394 166.943 1.00 0.12  ? 3179 PHE A CZ    1 
ATOM   13726 N  N     . ILE A 1 3180 ? 220.520 242.425 169.058 1.00 0.07  ? 3180 ILE A N     1 
ATOM   13727 C  CA    . ILE A 1 3180 ? 221.672 242.028 168.255 1.00 0.13  ? 3180 ILE A CA    1 
ATOM   13728 C  C     . ILE A 1 3180 ? 221.473 240.641 167.664 1.00 0.12  ? 3180 ILE A C     1 
ATOM   13729 O  O     . ILE A 1 3180 ? 221.986 240.343 166.579 1.00 0.16  ? 3180 ILE A O     1 
ATOM   13730 C  CB    . ILE A 1 3180 ? 222.967 242.113 169.083 1.00 0.27  ? 3180 ILE A CB    1 
ATOM   13731 C  CG1   . ILE A 1 3180 ? 222.869 241.232 170.328 1.00 0.28  ? 3180 ILE A CG1   1 
ATOM   13732 C  CG2   . ILE A 1 3180 ? 223.264 243.558 169.455 1.00 0.06  ? 3180 ILE A CG2   1 
ATOM   13733 C  CD1   . ILE A 1 3180 ? 224.039 241.361 171.260 1.00 0.55  ? 3180 ILE A CD1   1 
ATOM   13734 N  N     . ASN A 1 3181 ? 220.736 239.772 168.356 1.00 0.24  ? 3181 ASN A N     1 
ATOM   13735 C  CA    . ASN A 1 3181 ? 220.418 238.461 167.803 1.00 0.61  ? 3181 ASN A CA    1 
ATOM   13736 C  C     . ASN A 1 3181 ? 219.603 238.602 166.522 1.00 0.42  ? 3181 ASN A C     1 
ATOM   13737 O  O     . ASN A 1 3181 ? 219.922 237.987 165.499 1.00 0.89  ? 3181 ASN A O     1 
ATOM   13738 C  CB    . ASN A 1 3181 ? 219.663 237.627 168.841 1.00 1.50  ? 3181 ASN A CB    1 
ATOM   13739 C  CG    . ASN A 1 3181 ? 219.477 236.184 168.419 1.00 6.20  ? 3181 ASN A CG    1 
ATOM   13740 O  OD1   . ASN A 1 3181 ? 219.885 235.780 167.332 1.00 13.03 ? 3181 ASN A OD1   1 
ATOM   13741 N  ND2   . ASN A 1 3181 ? 218.840 235.399 169.280 1.00 11.22 ? 3181 ASN A ND2   1 
ATOM   13742 N  N     . HIS A 1 3182 ? 218.559 239.432 166.558 1.00 0.20  ? 3182 HIS A N     1 
ATOM   13743 C  CA    . HIS A 1 3182 ? 217.763 239.677 165.361 1.00 0.26  ? 3182 HIS A CA    1 
ATOM   13744 C  C     . HIS A 1 3182 ? 218.595 240.342 164.273 1.00 0.51  ? 3182 HIS A C     1 
ATOM   13745 O  O     . HIS A 1 3182 ? 218.400 240.072 163.083 1.00 2.11  ? 3182 HIS A O     1 
ATOM   13746 C  CB    . HIS A 1 3182 ? 216.547 240.538 165.707 1.00 0.24  ? 3182 HIS A CB    1 
ATOM   13747 C  CG    . HIS A 1 3182 ? 215.431 239.779 166.351 1.00 0.47  ? 3182 HIS A CG    1 
ATOM   13748 N  ND1   . HIS A 1 3182 ? 214.662 240.305 167.364 1.00 0.28  ? 3182 HIS A ND1   1 
ATOM   13749 C  CD2   . HIS A 1 3182 ? 214.939 238.540 166.109 1.00 0.73  ? 3182 HIS A CD2   1 
ATOM   13750 C  CE1   . HIS A 1 3182 ? 213.757 239.419 167.733 1.00 0.43  ? 3182 HIS A CE1   1 
ATOM   13751 N  NE2   . HIS A 1 3182 ? 213.901 238.340 166.986 1.00 0.69  ? 3182 HIS A NE2   1 
ATOM   13752 N  N     . TYR A 1 3183 ? 219.523 241.217 164.661 1.00 0.18  ? 3183 TYR A N     1 
ATOM   13753 C  CA    . TYR A 1 3183 ? 220.359 241.897 163.677 1.00 0.42  ? 3183 TYR A CA    1 
ATOM   13754 C  C     . TYR A 1 3183 ? 221.229 240.903 162.919 1.00 0.88  ? 3183 TYR A C     1 
ATOM   13755 O  O     . TYR A 1 3183 ? 221.357 240.983 161.693 1.00 1.89  ? 3183 TYR A O     1 
ATOM   13756 C  CB    . TYR A 1 3183 ? 221.209 242.962 164.369 1.00 0.67  ? 3183 TYR A CB    1 
ATOM   13757 C  CG    . TYR A 1 3183 ? 221.990 243.861 163.433 1.00 0.81  ? 3183 TYR A CG    1 
ATOM   13758 C  CD1   . TYR A 1 3183 ? 221.556 244.098 162.139 1.00 0.96  ? 3183 TYR A CD1   1 
ATOM   13759 C  CD2   . TYR A 1 3183 ? 223.153 244.484 163.858 1.00 1.08  ? 3183 TYR A CD2   1 
ATOM   13760 C  CE1   . TYR A 1 3183 ? 222.269 244.922 161.288 1.00 0.92  ? 3183 TYR A CE1   1 
ATOM   13761 C  CE2   . TYR A 1 3183 ? 223.869 245.309 163.020 1.00 2.33  ? 3183 TYR A CE2   1 
ATOM   13762 C  CZ    . TYR A 1 3183 ? 223.422 245.525 161.736 1.00 1.59  ? 3183 TYR A CZ    1 
ATOM   13763 O  OH    . TYR A 1 3183 ? 224.136 246.347 160.899 1.00 1.92  ? 3183 TYR A OH    1 
ATOM   13764 N  N     . ALA A 1 3184 ? 221.827 239.947 163.632 1.00 1.26  ? 3184 ALA A N     1 
ATOM   13765 C  CA    . ALA A 1 3184 ? 222.654 238.940 162.975 1.00 1.49  ? 3184 ALA A CA    1 
ATOM   13766 C  C     . ALA A 1 3184 ? 221.821 238.049 162.059 1.00 2.00  ? 3184 ALA A C     1 
ATOM   13767 O  O     . ALA A 1 3184 ? 222.232 237.735 160.937 1.00 3.30  ? 3184 ALA A O     1 
ATOM   13768 C  CB    . ALA A 1 3184 ? 223.386 238.102 164.024 1.00 1.85  ? 3184 ALA A CB    1 
ATOM   13769 N  N     . ASN A 1 3185 ? 220.641 237.632 162.526 1.00 1.92  ? 3185 ASN A N     1 
ATOM   13770 C  CA    . ASN A 1 3185 ? 219.805 236.728 161.741 1.00 1.74  ? 3185 ASN A CA    1 
ATOM   13771 C  C     . ASN A 1 3185 ? 219.276 237.410 160.485 1.00 4.64  ? 3185 ASN A C     1 
ATOM   13772 O  O     . ASN A 1 3185 ? 219.356 236.856 159.383 1.00 7.65  ? 3185 ASN A O     1 
ATOM   13773 C  CB    . ASN A 1 3185 ? 218.650 236.209 162.596 1.00 1.88  ? 3185 ASN A CB    1 
ATOM   13774 C  CG    . ASN A 1 3185 ? 219.125 235.498 163.844 1.00 3.20  ? 3185 ASN A CG    1 
ATOM   13775 O  OD1   . ASN A 1 3185 ? 220.321 235.295 164.040 1.00 5.44  ? 3185 ASN A OD1   1 
ATOM   13776 N  ND2   . ASN A 1 3185 ? 218.184 235.119 164.699 1.00 5.55  ? 3185 ASN A ND2   1 
ATOM   13777 N  N     . LEU A 1 3186 ? 218.723 238.616 160.635 1.00 4.45  ? 3186 LEU A N     1 
ATOM   13778 C  CA    . LEU A 1 3186 ? 218.173 239.329 159.487 1.00 3.00  ? 3186 LEU A CA    1 
ATOM   13779 C  C     . LEU A 1 3186 ? 219.256 239.669 158.472 1.00 4.55  ? 3186 LEU A C     1 
ATOM   13780 O  O     . LEU A 1 3186 ? 219.035 239.563 157.260 1.00 9.63  ? 3186 LEU A O     1 
ATOM   13781 C  CB    . LEU A 1 3186 ? 217.456 240.595 159.954 1.00 1.84  ? 3186 LEU A CB    1 
ATOM   13782 C  CG    . LEU A 1 3186 ? 216.139 240.363 160.696 1.00 2.75  ? 3186 LEU A CG    1 
ATOM   13783 C  CD1   . LEU A 1 3186 ? 215.553 241.672 161.190 1.00 1.97  ? 3186 LEU A CD1   1 
ATOM   13784 C  CD2   . LEU A 1 3186 ? 215.152 239.635 159.795 1.00 5.58  ? 3186 LEU A CD2   1 
ATOM   13785 N  N     . PHE A 1 3187 ? 220.430 240.083 158.949 1.00 4.20  ? 3187 PHE A N     1 
ATOM   13786 C  CA    . PHE A 1 3187 ? 221.532 240.419 158.053 1.00 3.66  ? 3187 PHE A CA    1 
ATOM   13787 C  C     . PHE A 1 3187 ? 221.950 239.216 157.220 1.00 5.08  ? 3187 PHE A C     1 
ATOM   13788 O  O     . PHE A 1 3187 ? 222.142 239.324 156.005 1.00 6.03  ? 3187 PHE A O     1 
ATOM   13789 C  CB    . PHE A 1 3187 ? 222.705 240.943 158.872 1.00 3.87  ? 3187 PHE A CB    1 
ATOM   13790 C  CG    . PHE A 1 3187 ? 223.822 241.527 158.059 1.00 4.96  ? 3187 PHE A CG    1 
ATOM   13791 C  CD1   . PHE A 1 3187 ? 223.732 242.812 157.554 1.00 5.75  ? 3187 PHE A CD1   1 
ATOM   13792 C  CD2   . PHE A 1 3187 ? 224.982 240.805 157.835 1.00 6.52  ? 3187 PHE A CD2   1 
ATOM   13793 C  CE1   . PHE A 1 3187 ? 224.764 243.356 156.817 1.00 11.37 ? 3187 PHE A CE1   1 
ATOM   13794 C  CE2   . PHE A 1 3187 ? 226.018 241.344 157.102 1.00 9.18  ? 3187 PHE A CE2   1 
ATOM   13795 C  CZ    . PHE A 1 3187 ? 225.911 242.621 156.594 1.00 8.95  ? 3187 PHE A CZ    1 
ATOM   13796 N  N     . HIS A 1 3188 ? 222.102 238.057 157.863 1.00 7.67  ? 3188 HIS A N     1 
ATOM   13797 C  CA    . HIS A 1 3188 ? 222.424 236.847 157.121 1.00 7.41  ? 3188 HIS A CA    1 
ATOM   13798 C  C     . HIS A 1 3188 ? 221.287 236.453 156.189 1.00 9.63  ? 3188 HIS A C     1 
ATOM   13799 O  O     . HIS A 1 3188 ? 221.523 236.065 155.041 1.00 11.78 ? 3188 HIS A O     1 
ATOM   13800 C  CB    . HIS A 1 3188 ? 222.748 235.709 158.087 1.00 5.43  ? 3188 HIS A CB    1 
ATOM   13801 C  CG    . HIS A 1 3188 ? 222.802 234.363 157.436 1.00 14.51 ? 3188 HIS A CG    1 
ATOM   13802 N  ND1   . HIS A 1 3188 ? 223.799 234.000 156.558 1.00 19.40 ? 3188 HIS A ND1   1 
ATOM   13803 C  CD2   . HIS A 1 3188 ? 221.973 233.296 157.527 1.00 14.72 ? 3188 HIS A CD2   1 
ATOM   13804 C  CE1   . HIS A 1 3188 ? 223.587 232.766 156.139 1.00 20.17 ? 3188 HIS A CE1   1 
ATOM   13805 N  NE2   . HIS A 1 3188 ? 222.485 232.316 156.712 1.00 20.89 ? 3188 HIS A NE2   1 
ATOM   13806 N  N     . GLU A 1 3189 ? 220.044 236.554 156.669 1.00 6.63  ? 3189 GLU A N     1 
ATOM   13807 C  CA    . GLU A 1 3189 ? 218.890 236.190 155.854 1.00 7.17  ? 3189 GLU A CA    1 
ATOM   13808 C  C     . GLU A 1 3189 ? 218.763 237.096 154.636 1.00 11.20 ? 3189 GLU A C     1 
ATOM   13809 O  O     . GLU A 1 3189 ? 218.525 236.626 153.518 1.00 13.74 ? 3189 GLU A O     1 
ATOM   13810 C  CB    . GLU A 1 3189 ? 217.622 236.247 156.706 1.00 9.05  ? 3189 GLU A CB    1 
ATOM   13811 C  CG    . GLU A 1 3189 ? 216.359 235.787 156.007 1.00 13.29 ? 3189 GLU A CG    1 
ATOM   13812 C  CD    . GLU A 1 3189 ? 215.104 236.282 156.700 1.00 16.31 ? 3189 GLU A CD    1 
ATOM   13813 O  OE1   . GLU A 1 3189 ? 214.990 236.093 157.929 1.00 17.40 ? 3189 GLU A OE1   1 
ATOM   13814 O  OE2   . GLU A 1 3189 ? 214.233 236.859 156.017 1.00 15.73 ? 3189 GLU A OE2   1 
ATOM   13815 N  N     . LYS A 1 3190 ? 218.926 238.407 154.831 1.00 9.38  ? 3190 LYS A N     1 
ATOM   13816 C  CA    . LYS A 1 3190 ? 218.772 239.341 153.720 1.00 6.61  ? 3190 LYS A CA    1 
ATOM   13817 C  C     . LYS A 1 3190 ? 219.939 239.245 152.749 1.00 6.84  ? 3190 LYS A C     1 
ATOM   13818 O  O     . LYS A 1 3190 ? 219.750 239.348 151.531 1.00 13.55 ? 3190 LYS A O     1 
ATOM   13819 C  CB    . LYS A 1 3190 ? 218.625 240.765 154.247 1.00 6.40  ? 3190 LYS A CB    1 
ATOM   13820 C  CG    . LYS A 1 3190 ? 217.279 241.039 154.869 1.00 5.63  ? 3190 LYS A CG    1 
ATOM   13821 C  CD    . LYS A 1 3190 ? 216.163 240.846 153.864 1.00 4.72  ? 3190 LYS A CD    1 
ATOM   13822 C  CE    . LYS A 1 3190 ? 214.824 241.200 154.471 1.00 6.68  ? 3190 LYS A CE    1 
ATOM   13823 N  NZ    . LYS A 1 3190 ? 213.780 241.424 153.436 1.00 7.09  ? 3190 LYS A NZ    1 
ATOM   13824 N  N     . ARG A 1 3191 ? 221.155 239.066 153.268 1.00 13.28 ? 3191 ARG A N     1 
ATOM   13825 C  CA    . ARG A 1 3191 ? 222.313 238.891 152.398 1.00 10.43 ? 3191 ARG A CA    1 
ATOM   13826 C  C     . ARG A 1 3191 ? 222.194 237.609 151.584 1.00 9.03  ? 3191 ARG A C     1 
ATOM   13827 O  O     . ARG A 1 3191 ? 222.480 237.601 150.381 1.00 11.23 ? 3191 ARG A O     1 
ATOM   13828 C  CB    . ARG A 1 3191 ? 223.590 238.882 153.237 1.00 10.22 ? 3191 ARG A CB    1 
ATOM   13829 C  CG    . ARG A 1 3191 ? 224.884 238.802 152.453 1.00 16.41 ? 3191 ARG A CG    1 
ATOM   13830 C  CD    . ARG A 1 3191 ? 226.073 238.889 153.399 1.00 23.53 ? 3191 ARG A CD    1 
ATOM   13831 N  NE    . ARG A 1 3191 ? 227.351 238.741 152.715 1.00 34.59 ? 3191 ARG A NE    1 
ATOM   13832 C  CZ    . ARG A 1 3191 ? 228.020 239.743 152.161 1.00 35.19 ? 3191 ARG A CZ    1 
ATOM   13833 N  NH1   . ARG A 1 3191 ? 227.583 240.988 152.232 1.00 27.88 ? 3191 ARG A NH1   1 
ATOM   13834 N  NH2   . ARG A 1 3191 ? 229.165 239.488 151.532 1.00 31.76 ? 3191 ARG A NH2   1 
ATOM   13835 N  N     . SER A 1 3192 ? 221.763 236.520 152.224 1.00 9.39  ? 3192 SER A N     1 
ATOM   13836 C  CA    . SER A 1 3192 ? 221.615 235.247 151.523 1.00 12.50 ? 3192 SER A CA    1 
ATOM   13837 C  C     . SER A 1 3192 ? 220.527 235.320 150.458 1.00 14.80 ? 3192 SER A C     1 
ATOM   13838 O  O     . SER A 1 3192 ? 220.703 234.803 149.349 1.00 15.23 ? 3192 SER A O     1 
ATOM   13839 C  CB    . SER A 1 3192 ? 221.316 234.133 152.524 1.00 11.85 ? 3192 SER A CB    1 
ATOM   13840 O  OG    . SER A 1 3192 ? 221.133 232.890 151.874 1.00 20.87 ? 3192 SER A OG    1 
ATOM   13841 N  N     . GLU A 1 3193 ? 219.392 235.949 150.778 1.00 13.67 ? 3193 GLU A N     1 
ATOM   13842 C  CA    . GLU A 1 3193 ? 218.315 236.072 149.800 1.00 10.33 ? 3193 GLU A CA    1 
ATOM   13843 C  C     . GLU A 1 3193 ? 218.751 236.898 148.597 1.00 13.06 ? 3193 GLU A C     1 
ATOM   13844 O  O     . GLU A 1 3193 ? 218.465 236.538 147.450 1.00 17.88 ? 3193 GLU A O     1 
ATOM   13845 C  CB    . GLU A 1 3193 ? 217.077 236.694 150.448 1.00 8.93  ? 3193 GLU A CB    1 
ATOM   13846 C  CG    . GLU A 1 3193 ? 216.321 235.763 151.376 1.00 15.33 ? 3193 GLU A CG    1 
ATOM   13847 C  CD    . GLU A 1 3193 ? 215.008 236.353 151.853 1.00 29.34 ? 3193 GLU A CD    1 
ATOM   13848 O  OE1   . GLU A 1 3193 ? 214.989 236.962 152.944 1.00 23.88 ? 3193 GLU A OE1   1 
ATOM   13849 O  OE2   . GLU A 1 3193 ? 213.994 236.209 151.137 1.00 34.90 ? 3193 GLU A OE2   1 
ATOM   13850 N  N     . LEU A 1 3194 ? 219.447 238.009 148.841 1.00 12.42 ? 3194 LEU A N     1 
ATOM   13851 C  CA    . LEU A 1 3194 ? 219.857 238.884 147.748 1.00 11.17 ? 3194 LEU A CA    1 
ATOM   13852 C  C     . LEU A 1 3194 ? 220.881 238.205 146.848 1.00 17.03 ? 3194 LEU A C     1 
ATOM   13853 O  O     . LEU A 1 3194 ? 220.780 238.272 145.617 1.00 26.33 ? 3194 LEU A O     1 
ATOM   13854 C  CB    . LEU A 1 3194 ? 220.416 240.190 148.307 1.00 12.21 ? 3194 LEU A CB    1 
ATOM   13855 C  CG    . LEU A 1 3194 ? 220.539 241.345 147.318 1.00 17.77 ? 3194 LEU A CG    1 
ATOM   13856 C  CD1   . LEU A 1 3194 ? 219.198 241.652 146.672 1.00 21.07 ? 3194 LEU A CD1   1 
ATOM   13857 C  CD2   . LEU A 1 3194 ? 221.084 242.561 148.021 1.00 20.73 ? 3194 LEU A CD2   1 
ATOM   13858 N  N     . GLU A 1 3195 ? 221.879 237.552 147.445 1.00 18.65 ? 3195 GLU A N     1 
ATOM   13859 C  CA    . GLU A 1 3195 ? 222.883 236.858 146.644 1.00 16.52 ? 3195 GLU A CA    1 
ATOM   13860 C  C     . GLU A 1 3195 ? 222.264 235.699 145.876 1.00 13.99 ? 3195 GLU A C     1 
ATOM   13861 O  O     . GLU A 1 3195 ? 222.626 235.446 144.721 1.00 16.86 ? 3195 GLU A O     1 
ATOM   13862 C  CB    . GLU A 1 3195 ? 224.023 236.367 147.537 1.00 17.25 ? 3195 GLU A CB    1 
ATOM   13863 C  CG    . GLU A 1 3195 ? 224.851 237.484 148.148 1.00 19.17 ? 3195 GLU A CG    1 
ATOM   13864 C  CD    . GLU A 1 3195 ? 225.959 236.966 149.041 1.00 31.87 ? 3195 GLU A CD    1 
ATOM   13865 O  OE1   . GLU A 1 3195 ? 226.007 235.743 149.283 1.00 31.26 ? 3195 GLU A OE1   1 
ATOM   13866 O  OE2   . GLU A 1 3195 ? 226.781 237.783 149.501 1.00 35.95 ? 3195 GLU A OE2   1 
ATOM   13867 N  N     . GLU A 1 3196 ? 221.335 234.978 146.506 1.00 19.47 ? 3196 GLU A N     1 
ATOM   13868 C  CA    . GLU A 1 3196 ? 220.648 233.891 145.816 1.00 20.05 ? 3196 GLU A CA    1 
ATOM   13869 C  C     . GLU A 1 3196 ? 219.814 234.428 144.660 1.00 18.86 ? 3196 GLU A C     1 
ATOM   13870 O  O     . GLU A 1 3196 ? 219.779 233.830 143.579 1.00 21.00 ? 3196 GLU A O     1 
ATOM   13871 C  CB    . GLU A 1 3196 ? 219.769 233.123 146.804 1.00 16.62 ? 3196 GLU A CB    1 
ATOM   13872 C  CG    . GLU A 1 3196 ? 219.034 231.928 146.224 1.00 18.97 ? 3196 GLU A CG    1 
ATOM   13873 C  CD    . GLU A 1 3196 ? 219.981 230.827 145.773 1.00 34.47 ? 3196 GLU A CD    1 
ATOM   13874 O  OE1   . GLU A 1 3196 ? 221.102 230.743 146.318 1.00 38.53 ? 3196 GLU A OE1   1 
ATOM   13875 O  OE2   . GLU A 1 3196 ? 219.603 230.036 144.887 1.00 34.36 ? 3196 GLU A OE2   1 
ATOM   13876 N  N     . GLN A 1 3197 ? 219.134 235.557 144.874 1.00 17.86 ? 3197 GLN A N     1 
ATOM   13877 C  CA    . GLN A 1 3197 ? 218.373 236.188 143.799 1.00 18.47 ? 3197 GLN A CA    1 
ATOM   13878 C  C     . GLN A 1 3197 ? 219.286 236.643 142.668 1.00 18.95 ? 3197 GLN A C     1 
ATOM   13879 O  O     . GLN A 1 3197 ? 218.971 236.445 141.488 1.00 22.21 ? 3197 GLN A O     1 
ATOM   13880 C  CB    . GLN A 1 3197 ? 217.573 237.369 144.343 1.00 18.90 ? 3197 GLN A CB    1 
ATOM   13881 C  CG    . GLN A 1 3197 ? 216.683 238.035 143.307 1.00 22.53 ? 3197 GLN A CG    1 
ATOM   13882 C  CD    . GLN A 1 3197 ? 215.857 239.165 143.883 1.00 25.43 ? 3197 GLN A CD    1 
ATOM   13883 O  OE1   . GLN A 1 3197 ? 215.967 239.491 145.065 1.00 30.11 ? 3197 GLN A OE1   1 
ATOM   13884 N  NE2   . GLN A 1 3197 ? 215.028 239.778 143.046 1.00 25.35 ? 3197 GLN A NE2   1 
ATOM   13885 N  N     . GLN A 1 3198 ? 220.419 237.258 143.009 1.00 16.16 ? 3198 GLN A N     1 
ATOM   13886 C  CA    . GLN A 1 3198 ? 221.356 237.703 141.983 1.00 16.43 ? 3198 GLN A CA    1 
ATOM   13887 C  C     . GLN A 1 3198 ? 221.933 236.529 141.204 1.00 20.28 ? 3198 GLN A C     1 
ATOM   13888 O  O     . GLN A 1 3198 ? 222.309 236.685 140.037 1.00 23.73 ? 3198 GLN A O     1 
ATOM   13889 C  CB    . GLN A 1 3198 ? 222.475 238.525 142.619 1.00 20.56 ? 3198 GLN A CB    1 
ATOM   13890 C  CG    . GLN A 1 3198 ? 223.227 239.419 141.648 1.00 20.93 ? 3198 GLN A CG    1 
ATOM   13891 C  CD    . GLN A 1 3198 ? 222.301 240.203 140.738 1.00 25.26 ? 3198 GLN A CD    1 
ATOM   13892 O  OE1   . GLN A 1 3198 ? 221.433 240.942 141.200 1.00 28.37 ? 3198 GLN A OE1   1 
ATOM   13893 N  NE2   . GLN A 1 3198 ? 222.483 240.045 139.433 1.00 27.08 ? 3198 GLN A NE2   1 
ATOM   13894 N  N     . MET A 1 3199 ? 222.011 235.353 141.828 1.00 19.78 ? 3199 MET A N     1 
ATOM   13895 C  CA    . MET A 1 3199 ? 222.494 234.170 141.126 1.00 19.97 ? 3199 MET A CA    1 
ATOM   13896 C  C     . MET A 1 3199 ? 221.513 233.749 140.037 1.00 23.90 ? 3199 MET A C     1 
ATOM   13897 O  O     . MET A 1 3199 ? 221.915 233.447 138.908 1.00 31.68 ? 3199 MET A O     1 
ATOM   13898 C  CB    . MET A 1 3199 ? 222.741 233.039 142.130 1.00 21.15 ? 3199 MET A CB    1 
ATOM   13899 C  CG    . MET A 1 3199 ? 223.310 231.731 141.565 1.00 29.19 ? 3199 MET A CG    1 
ATOM   13900 S  SD    . MET A 1 3199 ? 222.198 230.710 140.571 1.00 50.51 ? 3199 MET A SD    1 
ATOM   13901 C  CE    . MET A 1 3199 ? 221.165 229.989 141.844 1.00 27.12 ? 3199 MET A CE    1 
ATOM   13902 N  N     . HIS A 1 3200 ? 220.217 233.721 140.361 1.00 24.53 ? 3200 HIS A N     1 
ATOM   13903 C  CA    . HIS A 1 3200 ? 219.217 233.340 139.370 1.00 24.37 ? 3200 HIS A CA    1 
ATOM   13904 C  C     . HIS A 1 3200 ? 219.153 234.349 138.229 1.00 23.84 ? 3200 HIS A C     1 
ATOM   13905 O  O     . HIS A 1 3200 ? 219.048 233.965 137.058 1.00 27.26 ? 3200 HIS A O     1 
ATOM   13906 C  CB    . HIS A 1 3200 ? 217.844 233.202 140.027 1.00 21.44 ? 3200 HIS A CB    1 
ATOM   13907 C  CG    . HIS A 1 3200 ? 217.723 232.022 140.940 1.00 21.99 ? 3200 HIS A CG    1 
ATOM   13908 N  ND1   . HIS A 1 3200 ? 217.881 232.119 142.304 1.00 28.25 ? 3200 HIS A ND1   1 
ATOM   13909 C  CD2   . HIS A 1 3200 ? 217.470 230.718 140.682 1.00 25.88 ? 3200 HIS A CD2   1 
ATOM   13910 C  CE1   . HIS A 1 3200 ? 217.720 230.927 142.850 1.00 30.19 ? 3200 HIS A CE1   1 
ATOM   13911 N  NE2   . HIS A 1 3200 ? 217.473 230.058 141.886 1.00 26.52 ? 3200 HIS A NE2   1 
ATOM   13912 N  N     . LEU A 1 3201 ? 219.214 235.644 138.551 1.00 15.35 ? 3201 LEU A N     1 
ATOM   13913 C  CA    . LEU A 1 3201 ? 219.126 236.668 137.517 1.00 17.65 ? 3201 LEU A CA    1 
ATOM   13914 C  C     . LEU A 1 3201 ? 220.284 236.560 136.535 1.00 22.59 ? 3201 LEU A C     1 
ATOM   13915 O  O     . LEU A 1 3201 ? 220.096 236.708 135.323 1.00 23.00 ? 3201 LEU A O     1 
ATOM   13916 C  CB    . LEU A 1 3201 ? 219.090 238.058 138.152 1.00 18.86 ? 3201 LEU A CB    1 
ATOM   13917 C  CG    . LEU A 1 3201 ? 217.852 238.424 138.974 1.00 23.30 ? 3201 LEU A CG    1 
ATOM   13918 C  CD1   . LEU A 1 3201 ? 217.877 239.897 139.341 1.00 28.55 ? 3201 LEU A CD1   1 
ATOM   13919 C  CD2   . LEU A 1 3201 ? 216.575 238.079 138.227 1.00 16.24 ? 3201 LEU A CD2   1 
ATOM   13920 N  N     . ASN A 1 3202 ? 221.494 236.310 137.040 1.00 25.64 ? 3202 ASN A N     1 
ATOM   13921 C  CA    . ASN A 1 3202 ? 222.647 236.164 136.158 1.00 21.52 ? 3202 ASN A CA    1 
ATOM   13922 C  C     . ASN A 1 3202 ? 222.516 234.932 135.272 1.00 24.39 ? 3202 ASN A C     1 
ATOM   13923 O  O     . ASN A 1 3202 ? 222.858 234.977 134.085 1.00 25.73 ? 3202 ASN A O     1 
ATOM   13924 C  CB    . ASN A 1 3202 ? 223.928 236.108 136.984 1.00 26.54 ? 3202 ASN A CB    1 
ATOM   13925 C  CG    . ASN A 1 3202 ? 224.392 237.479 137.422 1.00 32.26 ? 3202 ASN A CG    1 
ATOM   13926 O  OD1   . ASN A 1 3202 ? 223.764 238.487 137.097 1.00 24.44 ? 3202 ASN A OD1   1 
ATOM   13927 N  ND2   . ASN A 1 3202 ? 225.491 237.526 138.163 1.00 35.43 ? 3202 ASN A ND2   1 
ATOM   13928 N  N     . VAL A 1 3203 ? 222.034 233.821 135.831 1.00 25.68 ? 3203 VAL A N     1 
ATOM   13929 C  CA    . VAL A 1 3203 ? 221.799 232.632 135.020 1.00 23.21 ? 3203 VAL A CA    1 
ATOM   13930 C  C     . VAL A 1 3203 ? 220.670 232.878 134.028 1.00 27.69 ? 3203 VAL A C     1 
ATOM   13931 O  O     . VAL A 1 3203 ? 220.775 232.523 132.848 1.00 26.84 ? 3203 VAL A O     1 
ATOM   13932 C  CB    . VAL A 1 3203 ? 221.511 231.417 135.920 1.00 17.60 ? 3203 VAL A CB    1 
ATOM   13933 C  CG1   . VAL A 1 3203 ? 220.995 230.252 135.090 1.00 20.96 ? 3203 VAL A CG1   1 
ATOM   13934 C  CG2   . VAL A 1 3203 ? 222.761 231.020 136.684 1.00 23.46 ? 3203 VAL A CG2   1 
ATOM   13935 N  N     . GLY A 1 3204 ? 219.577 233.491 134.485 1.00 25.44 ? 3204 GLY A N     1 
ATOM   13936 C  CA    . GLY A 1 3204 ? 218.467 233.760 133.587 1.00 23.18 ? 3204 GLY A CA    1 
ATOM   13937 C  C     . GLY A 1 3204 ? 218.846 234.692 132.452 1.00 25.55 ? 3204 GLY A C     1 
ATOM   13938 O  O     . GLY A 1 3204 ? 218.431 234.495 131.308 1.00 32.38 ? 3204 GLY A O     1 
ATOM   13939 N  N     . LEU A 1 3205 ? 219.637 235.723 132.754 1.00 22.09 ? 3205 LEU A N     1 
ATOM   13940 C  CA    . LEU A 1 3205 ? 220.085 236.640 131.714 1.00 22.42 ? 3205 LEU A CA    1 
ATOM   13941 C  C     . LEU A 1 3205 ? 220.999 235.945 130.713 1.00 25.80 ? 3205 LEU A C     1 
ATOM   13942 O  O     . LEU A 1 3205 ? 220.900 236.189 129.504 1.00 29.68 ? 3205 LEU A O     1 
ATOM   13943 C  CB    . LEU A 1 3205 ? 220.790 237.842 132.341 1.00 23.26 ? 3205 LEU A CB    1 
ATOM   13944 C  CG    . LEU A 1 3205 ? 219.867 238.898 132.949 1.00 22.66 ? 3205 LEU A CG    1 
ATOM   13945 C  CD1   . LEU A 1 3205 ? 220.663 240.099 133.420 1.00 27.69 ? 3205 LEU A CD1   1 
ATOM   13946 C  CD2   . LEU A 1 3205 ? 218.813 239.312 131.939 1.00 24.30 ? 3205 LEU A CD2   1 
ATOM   13947 N  N     . ARG A 1 3206 ? 221.898 235.079 131.192 1.00 22.18 ? 3206 ARG A N     1 
ATOM   13948 C  CA    . ARG A 1 3206 ? 222.859 234.456 130.289 1.00 23.94 ? 3206 ARG A CA    1 
ATOM   13949 C  C     . ARG A 1 3206 ? 222.194 233.434 129.377 1.00 25.74 ? 3206 ARG A C     1 
ATOM   13950 O  O     . ARG A 1 3206 ? 222.643 233.236 128.243 1.00 31.86 ? 3206 ARG A O     1 
ATOM   13951 C  CB    . ARG A 1 3206 ? 224.005 233.815 131.082 1.00 24.45 ? 3206 ARG A CB    1 
ATOM   13952 C  CG    . ARG A 1 3206 ? 223.685 232.474 131.717 1.00 27.58 ? 3206 ARG A CG    1 
ATOM   13953 C  CD    . ARG A 1 3206 ? 224.887 231.891 132.447 1.00 28.23 ? 3206 ARG A CD    1 
ATOM   13954 N  NE    . ARG A 1 3206 ? 225.214 232.633 133.660 1.00 32.45 ? 3206 ARG A NE    1 
ATOM   13955 C  CZ    . ARG A 1 3206 ? 226.291 233.392 133.810 1.00 33.60 ? 3206 ARG A CZ    1 
ATOM   13956 N  NH1   . ARG A 1 3206 ? 227.172 233.542 132.835 1.00 31.48 ? 3206 ARG A NH1   1 
ATOM   13957 N  NH2   . ARG A 1 3206 ? 226.489 234.016 134.968 1.00 30.85 ? 3206 ARG A NH2   1 
ATOM   13958 N  N     . LYS A 1 3207 ? 221.132 232.772 129.847 1.00 25.75 ? 3207 LYS A N     1 
ATOM   13959 C  CA    . LYS A 1 3207 ? 220.395 231.858 128.979 1.00 27.52 ? 3207 LYS A CA    1 
ATOM   13960 C  C     . LYS A 1 3207 ? 219.692 232.610 127.857 1.00 26.86 ? 3207 LYS A C     1 
ATOM   13961 O  O     . LYS A 1 3207 ? 219.656 232.137 126.715 1.00 27.53 ? 3207 LYS A O     1 
ATOM   13962 C  CB    . LYS A 1 3207 ? 219.393 231.040 129.796 1.00 22.22 ? 3207 LYS A CB    1 
ATOM   13963 C  CG    . LYS A 1 3207 ? 220.023 230.182 130.877 1.00 20.48 ? 3207 LYS A CG    1 
ATOM   13964 C  CD    . LYS A 1 3207 ? 220.892 229.093 130.272 1.00 27.62 ? 3207 LYS A CD    1 
ATOM   13965 C  CE    . LYS A 1 3207 ? 221.393 228.127 131.333 1.00 32.70 ? 3207 LYS A CE    1 
ATOM   13966 N  NZ    . LYS A 1 3207 ? 222.377 228.767 132.248 1.00 33.20 ? 3207 LYS A NZ    1 
ATOM   13967 N  N     . ILE A 1 3208 ? 219.122 233.776 128.163 1.00 24.99 ? 3208 ILE A N     1 
ATOM   13968 C  CA    . ILE A 1 3208 ? 218.488 234.585 127.128 1.00 24.93 ? 3208 ILE A CA    1 
ATOM   13969 C  C     . ILE A 1 3208 ? 219.522 235.064 126.116 1.00 26.58 ? 3208 ILE A C     1 
ATOM   13970 O  O     . ILE A 1 3208 ? 219.292 235.010 124.902 1.00 33.07 ? 3208 ILE A O     1 
ATOM   13971 C  CB    . ILE A 1 3208 ? 217.727 235.763 127.759 1.00 26.35 ? 3208 ILE A CB    1 
ATOM   13972 C  CG1   . ILE A 1 3208 ? 216.612 235.253 128.673 1.00 26.74 ? 3208 ILE A CG1   1 
ATOM   13973 C  CG2   . ILE A 1 3208 ? 217.153 236.664 126.682 1.00 25.21 ? 3208 ILE A CG2   1 
ATOM   13974 C  CD1   . ILE A 1 3208 ? 215.834 236.357 129.343 1.00 22.11 ? 3208 ILE A CD1   1 
ATOM   13975 N  N     . LYS A 1 3209 ? 220.674 235.537 126.596 1.00 25.25 ? 3209 LYS A N     1 
ATOM   13976 C  CA    . LYS A 1 3209 ? 221.720 235.999 125.689 1.00 26.05 ? 3209 LYS A CA    1 
ATOM   13977 C  C     . LYS A 1 3209 ? 222.224 234.865 124.806 1.00 30.20 ? 3209 LYS A C     1 
ATOM   13978 O  O     . LYS A 1 3209 ? 222.462 235.059 123.608 1.00 31.43 ? 3209 LYS A O     1 
ATOM   13979 C  CB    . LYS A 1 3209 ? 222.872 236.613 126.480 1.00 28.52 ? 3209 LYS A CB    1 
ATOM   13980 C  CG    . LYS A 1 3209 ? 223.953 237.237 125.614 1.00 26.05 ? 3209 LYS A CG    1 
ATOM   13981 C  CD    . LYS A 1 3209 ? 224.716 238.311 126.368 1.00 22.40 ? 3209 LYS A CD    1 
ATOM   13982 C  CE    . LYS A 1 3209 ? 223.768 239.337 126.963 1.00 26.52 ? 3209 LYS A CE    1 
ATOM   13983 N  NZ    . LYS A 1 3209 ? 223.044 240.094 125.905 1.00 24.91 ? 3209 LYS A NZ    1 
ATOM   13984 N  N     . GLU A 1 3210 ? 222.396 233.673 125.380 1.00 27.75 ? 3210 GLU A N     1 
ATOM   13985 C  CA    . GLU A 1 3210 ? 222.780 232.517 124.576 1.00 30.59 ? 3210 GLU A CA    1 
ATOM   13986 C  C     . GLU A 1 3210 ? 221.706 232.190 123.547 1.00 32.14 ? 3210 GLU A C     1 
ATOM   13987 O  O     . GLU A 1 3210 ? 222.019 231.829 122.406 1.00 33.57 ? 3210 GLU A O     1 
ATOM   13988 C  CB    . GLU A 1 3210 ? 223.044 231.313 125.480 1.00 24.95 ? 3210 GLU A CB    1 
ATOM   13989 C  CG    . GLU A 1 3210 ? 224.376 231.363 126.207 1.00 32.07 ? 3210 GLU A CG    1 
ATOM   13990 C  CD    . GLU A 1 3210 ? 224.500 230.290 127.271 1.00 38.54 ? 3210 GLU A CD    1 
ATOM   13991 O  OE1   . GLU A 1 3210 ? 223.534 229.521 127.456 1.00 37.14 ? 3210 GLU A OE1   1 
ATOM   13992 O  OE2   . GLU A 1 3210 ? 225.562 230.216 127.921 1.00 34.60 ? 3210 GLU A OE2   1 
ATOM   13993 N  N     . THR A 1 3211 ? 220.434 232.317 123.930 1.00 27.72 ? 3211 THR A N     1 
ATOM   13994 C  CA    . THR A 1 3211 ? 219.338 232.033 123.010 1.00 28.19 ? 3211 THR A CA    1 
ATOM   13995 C  C     . THR A 1 3211 ? 219.371 232.964 121.803 1.00 29.78 ? 3211 THR A C     1 
ATOM   13996 O  O     . THR A 1 3211 ? 219.138 232.531 120.669 1.00 31.89 ? 3211 THR A O     1 
ATOM   13997 C  CB    . THR A 1 3211 ? 218.004 232.148 123.747 1.00 30.59 ? 3211 THR A CB    1 
ATOM   13998 O  OG1   . THR A 1 3211 ? 217.877 231.070 124.685 1.00 33.18 ? 3211 THR A OG1   1 
ATOM   13999 C  CG2   . THR A 1 3211 ? 216.837 232.104 122.771 1.00 25.24 ? 3211 THR A CG2   1 
ATOM   14000 N  N     . VAL A 1 3212 ? 219.667 234.246 122.028 1.00 29.24 ? 3212 VAL A N     1 
ATOM   14001 C  CA    . VAL A 1 3212 ? 219.778 235.191 120.919 1.00 27.50 ? 3212 VAL A CA    1 
ATOM   14002 C  C     . VAL A 1 3212 ? 220.900 234.773 119.976 1.00 33.69 ? 3212 VAL A C     1 
ATOM   14003 O  O     . VAL A 1 3212 ? 220.798 234.933 118.754 1.00 35.42 ? 3212 VAL A O     1 
ATOM   14004 C  CB    . VAL A 1 3212 ? 219.988 236.619 121.456 1.00 25.95 ? 3212 VAL A CB    1 
ATOM   14005 C  CG1   . VAL A 1 3212 ? 220.123 237.610 120.309 1.00 30.02 ? 3212 VAL A CG1   1 
ATOM   14006 C  CG2   . VAL A 1 3212 ? 218.846 237.012 122.371 1.00 28.08 ? 3212 VAL A CG2   1 
ATOM   14007 N  N     . ASP A 1 3213 ? 221.992 234.241 120.530 1.00 31.63 ? 3213 ASP A N     1 
ATOM   14008 C  CA    . ASP A 1 3213 ? 223.075 233.732 119.694 1.00 29.89 ? 3213 ASP A CA    1 
ATOM   14009 C  C     . ASP A 1 3213 ? 222.643 232.497 118.915 1.00 32.26 ? 3213 ASP A C     1 
ATOM   14010 O  O     . ASP A 1 3213 ? 223.017 232.333 117.747 1.00 37.37 ? 3213 ASP A O     1 
ATOM   14011 C  CB    . ASP A 1 3213 ? 224.299 233.421 120.553 1.00 32.50 ? 3213 ASP A CB    1 
ATOM   14012 C  CG    . ASP A 1 3213 ? 224.770 234.617 121.356 1.00 34.19 ? 3213 ASP A CG    1 
ATOM   14013 O  OD1   . ASP A 1 3213 ? 224.824 235.728 120.791 1.00 37.07 ? 3213 ASP A OD1   1 
ATOM   14014 O  OD2   . ASP A 1 3213 ? 225.085 234.445 122.552 1.00 34.32 ? 3213 ASP A OD2   1 
ATOM   14015 N  N     . GLN A 1 3214 ? 221.863 231.610 119.542 1.00 33.33 ? 3214 GLN A N     1 
ATOM   14016 C  CA    . GLN A 1 3214 ? 221.480 230.362 118.891 1.00 30.93 ? 3214 GLN A CA    1 
ATOM   14017 C  C     . GLN A 1 3214 ? 220.643 230.612 117.641 1.00 37.72 ? 3214 GLN A C     1 
ATOM   14018 O  O     . GLN A 1 3214 ? 220.842 229.956 116.612 1.00 37.87 ? 3214 GLN A O     1 
ATOM   14019 C  CB    . GLN A 1 3214 ? 220.718 229.464 119.868 1.00 25.93 ? 3214 GLN A CB    1 
ATOM   14020 C  CG    . GLN A 1 3214 ? 221.517 229.011 121.082 1.00 33.32 ? 3214 GLN A CG    1 
ATOM   14021 C  CD    . GLN A 1 3214 ? 223.004 228.901 120.807 1.00 38.37 ? 3214 GLN A CD    1 
ATOM   14022 O  OE1   . GLN A 1 3214 ? 223.443 228.051 120.032 1.00 36.01 ? 3214 GLN A OE1   1 
ATOM   14023 N  NE2   . GLN A 1 3214 ? 223.788 229.763 121.444 1.00 34.09 ? 3214 GLN A NE2   1 
ATOM   14024 N  N     . VAL A 1 3215 ? 219.691 231.543 117.714 1.00 32.35 ? 3215 VAL A N     1 
ATOM   14025 C  CA    . VAL A 1 3215 ? 218.854 231.814 116.551 1.00 30.46 ? 3215 VAL A CA    1 
ATOM   14026 C  C     . VAL A 1 3215 ? 219.665 232.479 115.445 1.00 35.95 ? 3215 VAL A C     1 
ATOM   14027 O  O     . VAL A 1 3215 ? 219.368 232.299 114.258 1.00 32.66 ? 3215 VAL A O     1 
ATOM   14028 C  CB    . VAL A 1 3215 ? 217.627 232.659 116.946 1.00 32.97 ? 3215 VAL A CB    1 
ATOM   14029 C  CG1   . VAL A 1 3215 ? 216.823 231.944 118.019 1.00 32.50 ? 3215 VAL A CG1   1 
ATOM   14030 C  CG2   . VAL A 1 3215 ? 218.049 234.037 117.426 1.00 26.82 ? 3215 VAL A CG2   1 
ATOM   14031 N  N     . GLU A 1 3216 ? 220.688 233.257 115.805 1.00 32.85 ? 3216 GLU A N     1 
ATOM   14032 C  CA    . GLU A 1 3216 ? 221.523 233.901 114.797 1.00 35.41 ? 3216 GLU A CA    1 
ATOM   14033 C  C     . GLU A 1 3216 ? 222.242 232.864 113.944 1.00 35.93 ? 3216 GLU A C     1 
ATOM   14034 O  O     . GLU A 1 3216 ? 222.281 232.974 112.713 1.00 35.35 ? 3216 GLU A O     1 
ATOM   14035 C  CB    . GLU A 1 3216 ? 222.522 234.841 115.472 1.00 33.78 ? 3216 GLU A CB    1 
ATOM   14036 C  CG    . GLU A 1 3216 ? 223.185 235.835 114.529 1.00 32.57 ? 3216 GLU A CG    1 
ATOM   14037 C  CD    . GLU A 1 3216 ? 224.424 235.273 113.860 1.00 36.57 ? 3216 GLU A CD    1 
ATOM   14038 O  OE1   . GLU A 1 3216 ? 225.344 234.835 114.580 1.00 39.57 ? 3216 GLU A OE1   1 
ATOM   14039 O  OE2   . GLU A 1 3216 ? 224.474 235.268 112.611 1.00 36.63 ? 3216 GLU A OE2   1 
ATOM   14040 N  N     . GLU A 1 3217 ? 222.818 231.840 114.582 1.00 32.78 ? 3217 GLU A N     1 
ATOM   14041 C  CA    . GLU A 1 3217 ? 223.458 230.777 113.815 1.00 34.79 ? 3217 GLU A CA    1 
ATOM   14042 C  C     . GLU A 1 3217 ? 222.428 229.851 113.185 1.00 37.87 ? 3217 GLU A C     1 
ATOM   14043 O  O     . GLU A 1 3217 ? 222.693 229.255 112.135 1.00 39.40 ? 3217 GLU A O     1 
ATOM   14044 C  CB    . GLU A 1 3217 ? 224.426 229.988 114.698 1.00 34.17 ? 3217 GLU A CB    1 
ATOM   14045 C  CG    . GLU A 1 3217 ? 223.764 229.072 115.713 1.00 33.67 ? 3217 GLU A CG    1 
ATOM   14046 C  CD    . GLU A 1 3217 ? 224.769 228.322 116.564 1.00 38.73 ? 3217 GLU A CD    1 
ATOM   14047 O  OE1   . GLU A 1 3217 ? 225.980 228.597 116.436 1.00 40.88 ? 3217 GLU A OE1   1 
ATOM   14048 O  OE2   . GLU A 1 3217 ? 224.349 227.456 117.360 1.00 38.24 ? 3217 GLU A OE2   1 
ATOM   14049 N  N     . LEU A 1 3218 ? 221.255 229.715 113.808 1.00 34.30 ? 3218 LEU A N     1 
ATOM   14050 C  CA    . LEU A 1 3218 ? 220.203 228.895 113.222 1.00 33.27 ? 3218 LEU A CA    1 
ATOM   14051 C  C     . LEU A 1 3218 ? 219.639 229.551 111.968 1.00 36.27 ? 3218 LEU A C     1 
ATOM   14052 O  O     . LEU A 1 3218 ? 219.324 228.863 110.989 1.00 39.60 ? 3218 LEU A O     1 
ATOM   14053 C  CB    . LEU A 1 3218 ? 219.104 228.636 114.253 1.00 29.93 ? 3218 LEU A CB    1 
ATOM   14054 C  CG    . LEU A 1 3218 ? 217.958 227.718 113.836 1.00 32.36 ? 3218 LEU A CG    1 
ATOM   14055 C  CD1   . LEU A 1 3218 ? 218.482 226.328 113.525 1.00 28.59 ? 3218 LEU A CD1   1 
ATOM   14056 C  CD2   . LEU A 1 3218 ? 216.911 227.653 114.938 1.00 32.12 ? 3218 LEU A CD2   1 
ATOM   14057 N  N     . ARG A 1 3219 ? 219.505 230.880 111.977 1.00 34.89 ? 3219 ARG A N     1 
ATOM   14058 C  CA    . ARG A 1 3219 ? 219.179 231.593 110.747 1.00 34.81 ? 3219 ARG A CA    1 
ATOM   14059 C  C     . ARG A 1 3219 ? 220.284 231.425 109.714 1.00 37.68 ? 3219 ARG A C     1 
ATOM   14060 O  O     . ARG A 1 3219 ? 220.012 231.266 108.518 1.00 35.17 ? 3219 ARG A O     1 
ATOM   14061 C  CB    . ARG A 1 3219 ? 218.942 233.075 111.037 1.00 29.77 ? 3219 ARG A CB    1 
ATOM   14062 C  CG    . ARG A 1 3219 ? 217.650 233.376 111.782 1.00 33.07 ? 3219 ARG A CG    1 
ATOM   14063 C  CD    . ARG A 1 3219 ? 217.375 234.873 111.812 1.00 31.62 ? 3219 ARG A CD    1 
ATOM   14064 N  NE    . ARG A 1 3219 ? 218.433 235.609 112.494 1.00 36.45 ? 3219 ARG A NE    1 
ATOM   14065 C  CZ    . ARG A 1 3219 ? 218.249 236.367 113.567 1.00 39.36 ? 3219 ARG A CZ    1 
ATOM   14066 N  NH1   . ARG A 1 3219 ? 217.051 236.518 114.109 1.00 37.42 ? 3219 ARG A NH1   1 
ATOM   14067 N  NH2   . ARG A 1 3219 ? 219.292 236.988 114.110 1.00 36.38 ? 3219 ARG A NH2   1 
ATOM   14068 N  N     . ARG A 1 3220 ? 221.544 231.468 110.156 1.00 33.83 ? 3220 ARG A N     1 
ATOM   14069 C  CA    . ARG A 1 3220 ? 222.654 231.163 109.262 1.00 34.65 ? 3220 ARG A CA    1 
ATOM   14070 C  C     . ARG A 1 3220 ? 222.569 229.725 108.767 1.00 37.44 ? 3220 ARG A C     1 
ATOM   14071 O  O     . ARG A 1 3220 ? 222.815 229.449 107.587 1.00 39.88 ? 3220 ARG A O     1 
ATOM   14072 C  CB    . ARG A 1 3220 ? 223.984 231.417 109.972 1.00 38.82 ? 3220 ARG A CB    1 
ATOM   14073 C  CG    . ARG A 1 3220 ? 225.178 230.719 109.341 1.00 37.74 ? 3220 ARG A CG    1 
ATOM   14074 C  CD    . ARG A 1 3220 ? 226.247 230.395 110.376 1.00 35.03 ? 3220 ARG A CD    1 
ATOM   14075 N  NE    . ARG A 1 3220 ? 225.745 229.536 111.443 1.00 40.50 ? 3220 ARG A NE    1 
ATOM   14076 C  CZ    . ARG A 1 3220 ? 225.526 228.234 111.319 1.00 44.05 ? 3220 ARG A CZ    1 
ATOM   14077 N  NH1   . ARG A 1 3220 ? 225.762 227.597 110.183 1.00 40.96 ? 3220 ARG A NH1   1 
ATOM   14078 N  NH2   . ARG A 1 3220 ? 225.062 227.552 112.363 1.00 39.43 ? 3220 ARG A NH2   1 
ATOM   14079 N  N     . ASP A 1 3221 ? 222.219 228.795 109.658 1.00 38.23 ? 3221 ASP A N     1 
ATOM   14080 C  CA    . ASP A 1 3221 ? 221.982 227.418 109.238 1.00 38.86 ? 3221 ASP A CA    1 
ATOM   14081 C  C     . ASP A 1 3221 ? 220.788 227.335 108.295 1.00 34.83 ? 3221 ASP A C     1 
ATOM   14082 O  O     . ASP A 1 3221 ? 220.805 226.571 107.324 1.00 33.38 ? 3221 ASP A O     1 
ATOM   14083 C  CB    . ASP A 1 3221 ? 221.771 226.525 110.460 1.00 34.98 ? 3221 ASP A CB    1 
ATOM   14084 C  CG    . ASP A 1 3221 ? 221.607 225.063 110.092 1.00 39.15 ? 3221 ASP A CG    1 
ATOM   14085 O  OD1   . ASP A 1 3221 ? 220.489 224.665 109.701 1.00 39.19 ? 3221 ASP A OD1   1 
ATOM   14086 O  OD2   . ASP A 1 3221 ? 222.597 224.309 110.195 1.00 39.69 ? 3221 ASP A OD2   1 
ATOM   14087 N  N     . LEU A 1 3222 ? 219.741 228.119 108.568 1.00 34.15 ? 3222 LEU A N     1 
ATOM   14088 C  CA    . LEU A 1 3222 ? 218.578 228.141 107.683 1.00 37.88 ? 3222 LEU A CA    1 
ATOM   14089 C  C     . LEU A 1 3222 ? 218.962 228.596 106.282 1.00 38.86 ? 3222 LEU A C     1 
ATOM   14090 O  O     . LEU A 1 3222 ? 218.486 228.037 105.286 1.00 38.94 ? 3222 LEU A O     1 
ATOM   14091 C  CB    . LEU A 1 3222 ? 217.493 229.048 108.263 1.00 37.64 ? 3222 LEU A CB    1 
ATOM   14092 C  CG    . LEU A 1 3222 ? 216.250 229.253 107.395 1.00 37.32 ? 3222 LEU A CG    1 
ATOM   14093 C  CD1   . LEU A 1 3222 ? 215.343 228.036 107.452 1.00 34.77 ? 3222 LEU A CD1   1 
ATOM   14094 C  CD2   . LEU A 1 3222 ? 215.499 230.506 107.822 1.00 30.28 ? 3222 LEU A CD2   1 
ATOM   14095 N  N     . ARG A 1 3223 ? 219.815 229.619 106.182 1.00 36.00 ? 3223 ARG A N     1 
ATOM   14096 C  CA    . ARG A 1 3223 ? 220.310 230.037 104.876 1.00 36.01 ? 3223 ARG A CA    1 
ATOM   14097 C  C     . ARG A 1 3223 ? 221.173 228.954 104.243 1.00 36.31 ? 3223 ARG A C     1 
ATOM   14098 O  O     . ARG A 1 3223 ? 221.102 228.721 103.029 1.00 36.81 ? 3223 ARG A O     1 
ATOM   14099 C  CB    . ARG A 1 3223 ? 221.091 231.346 105.003 1.00 36.56 ? 3223 ARG A CB    1 
ATOM   14100 C  CG    . ARG A 1 3223 ? 221.704 231.837 103.700 1.00 34.92 ? 3223 ARG A CG    1 
ATOM   14101 C  CD    . ARG A 1 3223 ? 222.859 232.794 103.953 1.00 39.32 ? 3223 ARG A CD    1 
ATOM   14102 N  NE    . ARG A 1 3223 ? 223.717 232.347 105.044 1.00 39.92 ? 3223 ARG A NE    1 
ATOM   14103 C  CZ    . ARG A 1 3223 ? 224.629 231.390 104.938 1.00 42.35 ? 3223 ARG A CZ    1 
ATOM   14104 N  NH1   . ARG A 1 3223 ? 224.834 230.755 103.796 1.00 37.90 ? 3223 ARG A NH1   1 
ATOM   14105 N  NH2   . ARG A 1 3223 ? 225.354 231.064 106.004 1.00 42.60 ? 3223 ARG A NH2   1 
ATOM   14106 N  N     . ILE A 1 3224 ? 221.998 228.281 105.047 1.00 36.74 ? 3224 ILE A N     1 
ATOM   14107 C  CA    . ILE A 1 3224 ? 222.851 227.216 104.527 1.00 35.60 ? 3224 ILE A CA    1 
ATOM   14108 C  C     . ILE A 1 3224 ? 222.007 226.064 103.997 1.00 37.10 ? 3224 ILE A C     1 
ATOM   14109 O  O     . ILE A 1 3224 ? 222.274 225.523 102.917 1.00 36.97 ? 3224 ILE A O     1 
ATOM   14110 C  CB    . ILE A 1 3224 ? 223.841 226.746 105.610 1.00 37.02 ? 3224 ILE A CB    1 
ATOM   14111 C  CG1   . ILE A 1 3224 ? 225.039 227.695 105.684 1.00 38.08 ? 3224 ILE A CG1   1 
ATOM   14112 C  CG2   . ILE A 1 3224 ? 224.308 225.322 105.340 1.00 33.84 ? 3224 ILE A CG2   1 
ATOM   14113 C  CD1   . ILE A 1 3224 ? 226.063 227.306 106.726 1.00 33.24 ? 3224 ILE A CD1   1 
ATOM   14114 N  N     . LYS A 1 3225 ? 220.969 225.671 104.746 1.00 34.70 ? 3225 LYS A N     1 
ATOM   14115 C  CA    . LYS A 1 3225 ? 220.088 224.604 104.281 1.00 35.38 ? 3225 LYS A CA    1 
ATOM   14116 C  C     . LYS A 1 3225 ? 219.360 224.998 103.005 1.00 38.82 ? 3225 LYS A C     1 
ATOM   14117 O  O     . LYS A 1 3225 ? 219.106 224.144 102.146 1.00 39.53 ? 3225 LYS A O     1 
ATOM   14118 C  CB    . LYS A 1 3225 ? 219.084 224.236 105.375 1.00 36.84 ? 3225 LYS A CB    1 
ATOM   14119 C  CG    . LYS A 1 3225 ? 219.716 223.694 106.647 1.00 36.15 ? 3225 LYS A CG    1 
ATOM   14120 C  CD    . LYS A 1 3225 ? 220.522 222.432 106.381 1.00 35.25 ? 3225 LYS A CD    1 
ATOM   14121 C  CE    . LYS A 1 3225 ? 219.631 221.299 105.903 1.00 34.22 ? 3225 LYS A CE    1 
ATOM   14122 N  NZ    . LYS A 1 3225 ? 218.358 221.229 106.671 1.00 37.89 ? 3225 LYS A NZ    1 
ATOM   14123 N  N     . SER A 1 3226 ? 219.008 226.278 102.863 1.00 37.36 ? 3226 SER A N     1 
ATOM   14124 C  CA    . SER A 1 3226 ? 218.407 226.745 101.617 1.00 35.69 ? 3226 SER A CA    1 
ATOM   14125 C  C     . SER A 1 3226 ? 219.378 226.596 100.454 1.00 38.85 ? 3226 SER A C     1 
ATOM   14126 O  O     . SER A 1 3226 ? 218.980 226.204 99.349  1.00 41.03 ? 3226 SER A O     1 
ATOM   14127 C  CB    . SER A 1 3226 ? 217.959 228.199 101.763 1.00 36.28 ? 3226 SER A CB    1 
ATOM   14128 O  OG    . SER A 1 3226 ? 219.074 229.071 101.840 1.00 39.51 ? 3226 SER A OG    1 
ATOM   14129 N  N     . GLN A 1 3227 ? 220.656 226.908 100.681 1.00 39.53 ? 3227 GLN A N     1 
ATOM   14130 C  CA    . GLN A 1 3227 ? 221.663 226.734 99.638  1.00 38.91 ? 3227 GLN A CA    1 
ATOM   14131 C  C     . GLN A 1 3227 ? 221.815 225.268 99.262  1.00 38.33 ? 3227 GLN A C     1 
ATOM   14132 O  O     . GLN A 1 3227 ? 222.005 224.937 98.085  1.00 39.38 ? 3227 GLN A O     1 
ATOM   14133 C  CB    . GLN A 1 3227 ? 222.999 227.316 100.098 1.00 35.93 ? 3227 GLN A CB    1 
ATOM   14134 C  CG    . GLN A 1 3227 ? 223.941 227.686 98.963  1.00 35.94 ? 3227 GLN A CG    1 
ATOM   14135 C  CD    . GLN A 1 3227 ? 224.861 226.547 98.574  1.00 38.30 ? 3227 GLN A CD    1 
ATOM   14136 O  OE1   . GLN A 1 3227 ? 224.948 225.537 99.270  1.00 39.53 ? 3227 GLN A OE1   1 
ATOM   14137 N  NE2   . GLN A 1 3227 ? 225.557 226.707 97.454  1.00 37.05 ? 3227 GLN A NE2   1 
ATOM   14138 N  N     . GLU A 1 3228 ? 221.745 224.372 100.250 1.00 36.51 ? 3228 GLU A N     1 
ATOM   14139 C  CA    . GLU A 1 3228 ? 221.819 222.943 99.964  1.00 35.92 ? 3228 GLU A CA    1 
ATOM   14140 C  C     . GLU A 1 3228 ? 220.650 222.494 99.097  1.00 37.83 ? 3228 GLU A C     1 
ATOM   14141 O  O     . GLU A 1 3228 ? 220.824 221.683 98.179  1.00 35.03 ? 3228 GLU A O     1 
ATOM   14142 C  CB    . GLU A 1 3228 ? 221.857 222.150 101.270 1.00 33.64 ? 3228 GLU A CB    1 
ATOM   14143 C  CG    . GLU A 1 3228 ? 222.040 220.653 101.086 1.00 36.29 ? 3228 GLU A CG    1 
ATOM   14144 C  CD    . GLU A 1 3228 ? 222.162 219.917 102.406 1.00 38.95 ? 3228 GLU A CD    1 
ATOM   14145 O  OE1   . GLU A 1 3228 ? 222.090 220.574 103.465 1.00 38.12 ? 3228 GLU A OE1   1 
ATOM   14146 O  OE2   . GLU A 1 3228 ? 222.330 218.679 102.384 1.00 39.54 ? 3228 GLU A OE2   1 
ATOM   14147 N  N     . LEU A 1 3229 ? 219.450 223.010 99.374  1.00 39.21 ? 3229 LEU A N     1 
ATOM   14148 C  CA    . LEU A 1 3229 ? 218.291 222.672 98.554  1.00 35.83 ? 3229 LEU A CA    1 
ATOM   14149 C  C     . LEU A 1 3229 ? 218.467 223.152 97.119  1.00 38.90 ? 3229 LEU A C     1 
ATOM   14150 O  O     . LEU A 1 3229 ? 218.113 222.440 96.172  1.00 38.07 ? 3229 LEU A O     1 
ATOM   14151 C  CB    . LEU A 1 3229 ? 217.024 223.267 99.165  1.00 35.68 ? 3229 LEU A CB    1 
ATOM   14152 C  CG    . LEU A 1 3229 ? 216.480 222.539 100.394 1.00 38.17 ? 3229 LEU A CG    1 
ATOM   14153 C  CD1   . LEU A 1 3229 ? 215.264 223.258 100.952 1.00 35.60 ? 3229 LEU A CD1   1 
ATOM   14154 C  CD2   . LEU A 1 3229 ? 216.143 221.107 100.031 1.00 33.67 ? 3229 LEU A CD2   1 
ATOM   14155 N  N     . GLU A 1 3230 ? 219.004 224.361 96.939  1.00 38.22 ? 3230 GLU A N     1 
ATOM   14156 C  CA    . GLU A 1 3230 ? 219.223 224.879 95.593  1.00 36.44 ? 3230 GLU A CA    1 
ATOM   14157 C  C     . GLU A 1 3230 ? 220.222 224.021 94.826  1.00 38.56 ? 3230 GLU A C     1 
ATOM   14158 O  O     . GLU A 1 3230 ? 220.035 223.752 93.635  1.00 38.72 ? 3230 GLU A O     1 
ATOM   14159 C  CB    . GLU A 1 3230 ? 219.701 226.329 95.660  1.00 34.97 ? 3230 GLU A CB    1 
ATOM   14160 C  CG    . GLU A 1 3230 ? 218.689 227.291 96.261  1.00 36.87 ? 3230 GLU A CG    1 
ATOM   14161 C  CD    . GLU A 1 3230 ? 219.341 228.511 96.880  1.00 43.93 ? 3230 GLU A CD    1 
ATOM   14162 O  OE1   . GLU A 1 3230 ? 220.585 228.614 96.827  1.00 42.69 ? 3230 GLU A OE1   1 
ATOM   14163 O  OE2   . GLU A 1 3230 ? 218.611 229.369 97.420  1.00 45.62 ? 3230 GLU A OE2   1 
ATOM   14164 N  N     . VAL A 1 3231 ? 221.293 223.587 95.492  1.00 35.72 ? 3231 VAL A N     1 
ATOM   14165 C  CA    . VAL A 1 3231 ? 222.300 222.761 94.830  1.00 33.47 ? 3231 VAL A CA    1 
ATOM   14166 C  C     . VAL A 1 3231 ? 221.730 221.385 94.503  1.00 38.89 ? 3231 VAL A C     1 
ATOM   14167 O  O     . VAL A 1 3231 ? 221.887 220.879 93.386  1.00 38.94 ? 3231 VAL A O     1 
ATOM   14168 C  CB    . VAL A 1 3231 ? 223.564 222.659 95.702  1.00 36.42 ? 3231 VAL A CB    1 
ATOM   14169 C  CG1   . VAL A 1 3231 ? 224.419 221.477 95.269  1.00 30.61 ? 3231 VAL A CG1   1 
ATOM   14170 C  CG2   . VAL A 1 3231 ? 224.359 223.954 95.637  1.00 33.48 ? 3231 VAL A CG2   1 
ATOM   14171 N  N     . LYS A 1 3232 ? 221.056 220.759 95.473  1.00 36.97 ? 3232 LYS A N     1 
ATOM   14172 C  CA    . LYS A 1 3232 ? 220.508 219.424 95.254  1.00 35.26 ? 3232 LYS A CA    1 
ATOM   14173 C  C     . LYS A 1 3232 ? 219.419 219.434 94.187  1.00 37.70 ? 3232 LYS A C     1 
ATOM   14174 O  O     . LYS A 1 3232 ? 219.371 218.540 93.335  1.00 39.07 ? 3232 LYS A O     1 
ATOM   14175 C  CB    . LYS A 1 3232 ? 219.969 218.853 96.565  1.00 36.72 ? 3232 LYS A CB    1 
ATOM   14176 C  CG    . LYS A 1 3232 ? 221.044 218.501 97.581  1.00 37.19 ? 3232 LYS A CG    1 
ATOM   14177 C  CD    . LYS A 1 3232 ? 222.209 217.773 96.929  1.00 31.53 ? 3232 LYS A CD    1 
ATOM   14178 C  CE    . LYS A 1 3232 ? 223.462 217.859 97.787  1.00 36.71 ? 3232 LYS A CE    1 
ATOM   14179 N  NZ    . LYS A 1 3232 ? 224.659 217.329 97.075  1.00 30.94 ? 3232 LYS A NZ    1 
ATOM   14180 N  N     . ASN A 1 3233 ? 218.530 220.430 94.223  1.00 34.86 ? 3233 ASN A N     1 
ATOM   14181 C  CA    . ASN A 1 3233 ? 217.464 220.502 93.229  1.00 35.56 ? 3233 ASN A CA    1 
ATOM   14182 C  C     . ASN A 1 3233 ? 218.025 220.736 91.831  1.00 38.93 ? 3233 ASN A C     1 
ATOM   14183 O  O     . ASN A 1 3233 ? 217.570 220.116 90.862  1.00 36.89 ? 3233 ASN A O     1 
ATOM   14184 C  CB    . ASN A 1 3233 ? 216.470 221.602 93.601  1.00 34.17 ? 3233 ASN A CB    1 
ATOM   14185 C  CG    . ASN A 1 3233 ? 215.096 221.374 93.002  1.00 37.48 ? 3233 ASN A CG    1 
ATOM   14186 O  OD1   . ASN A 1 3233 ? 214.967 221.023 91.829  1.00 40.13 ? 3233 ASN A OD1   1 
ATOM   14187 N  ND2   . ASN A 1 3233 ? 214.059 221.573 93.808  1.00 35.94 ? 3233 ASN A ND2   1 
ATOM   14188 N  N     . ALA A 1 3234 ? 219.009 221.631 91.706  1.00 38.96 ? 3234 ALA A N     1 
ATOM   14189 C  CA    . ALA A 1 3234 ? 219.611 221.887 90.402  1.00 37.22 ? 3234 ALA A CA    1 
ATOM   14190 C  C     . ALA A 1 3234 ? 220.339 220.657 89.878  1.00 38.81 ? 3234 ALA A C     1 
ATOM   14191 O  O     . ALA A 1 3234 ? 220.242 220.327 88.690  1.00 38.28 ? 3234 ALA A O     1 
ATOM   14192 C  CB    . ALA A 1 3234 ? 220.564 223.080 90.487  1.00 32.01 ? 3234 ALA A CB    1 
ATOM   14193 N  N     . ALA A 1 3235 ? 221.078 219.965 90.749  1.00 37.10 ? 3235 ALA A N     1 
ATOM   14194 C  CA    . ALA A 1 3235 ? 221.788 218.762 90.326  1.00 35.49 ? 3235 ALA A CA    1 
ATOM   14195 C  C     . ALA A 1 3235 ? 220.815 217.667 89.908  1.00 39.47 ? 3235 ALA A C     1 
ATOM   14196 O  O     . ALA A 1 3235 ? 221.045 216.969 88.912  1.00 39.03 ? 3235 ALA A O     1 
ATOM   14197 C  CB    . ALA A 1 3235 ? 222.704 218.269 91.446  1.00 31.49 ? 3235 ALA A CB    1 
ATOM   14198 N  N     . ALA A 1 3236 ? 219.727 217.497 90.659  1.00 38.46 ? 3236 ALA A N     1 
ATOM   14199 C  CA    . ALA A 1 3236 ? 218.731 216.492 90.304  1.00 34.63 ? 3236 ALA A CA    1 
ATOM   14200 C  C     . ALA A 1 3236 ? 218.049 216.828 88.984  1.00 38.19 ? 3236 ALA A C     1 
ATOM   14201 O  O     . ALA A 1 3236 ? 217.807 215.940 88.158  1.00 36.47 ? 3236 ALA A O     1 
ATOM   14202 C  CB    . ALA A 1 3236 ? 217.699 216.355 91.424  1.00 32.78 ? 3236 ALA A CB    1 
ATOM   14203 N  N     . ASN A 1 3237 ? 217.723 218.107 88.770  1.00 35.38 ? 3237 ASN A N     1 
ATOM   14204 C  CA    . ASN A 1 3237 ? 217.082 218.507 87.521  1.00 34.16 ? 3237 ASN A CA    1 
ATOM   14205 C  C     . ASN A 1 3237 ? 218.007 218.292 86.329  1.00 37.49 ? 3237 ASN A C     1 
ATOM   14206 O  O     . ASN A 1 3237 ? 217.573 217.811 85.276  1.00 39.46 ? 3237 ASN A O     1 
ATOM   14207 C  CB    . ASN A 1 3237 ? 216.641 219.968 87.602  1.00 35.34 ? 3237 ASN A CB    1 
ATOM   14208 C  CG    . ASN A 1 3237 ? 215.458 220.168 88.531  1.00 39.86 ? 3237 ASN A CG    1 
ATOM   14209 O  OD1   . ASN A 1 3237 ? 214.896 219.208 89.055  1.00 37.63 ? 3237 ASN A OD1   1 
ATOM   14210 N  ND2   . ASN A 1 3237 ? 215.075 221.423 88.738  1.00 34.19 ? 3237 ASN A ND2   1 
ATOM   14211 N  N     . ASP A 1 3238 ? 219.286 218.649 86.474  1.00 36.20 ? 3238 ASP A N     1 
ATOM   14212 C  CA    . ASP A 1 3238 ? 220.237 218.454 85.383  1.00 36.40 ? 3238 ASP A CA    1 
ATOM   14213 C  C     . ASP A 1 3238 ? 220.432 216.974 85.079  1.00 37.06 ? 3238 ASP A C     1 
ATOM   14214 O  O     . ASP A 1 3238 ? 220.506 216.578 83.911  1.00 37.04 ? 3238 ASP A O     1 
ATOM   14215 C  CB    . ASP A 1 3238 ? 221.573 219.114 85.727  1.00 35.55 ? 3238 ASP A CB    1 
ATOM   14216 C  CG    . ASP A 1 3238 ? 221.461 220.617 85.869  1.00 40.65 ? 3238 ASP A CG    1 
ATOM   14217 O  OD1   . ASP A 1 3238 ? 220.352 221.156 85.664  1.00 40.52 ? 3238 ASP A OD1   1 
ATOM   14218 O  OD2   . ASP A 1 3238 ? 222.482 221.264 86.187  1.00 36.82 ? 3238 ASP A OD2   1 
ATOM   14219 N  N     . LYS A 1 3239 ? 220.521 216.142 86.119  1.00 34.61 ? 3239 LYS A N     1 
ATOM   14220 C  CA    . LYS A 1 3239 ? 220.668 214.706 85.906  1.00 36.31 ? 3239 LYS A CA    1 
ATOM   14221 C  C     . LYS A 1 3239 ? 219.423 214.111 85.261  1.00 38.56 ? 3239 LYS A C     1 
ATOM   14222 O  O     . LYS A 1 3239 ? 219.527 213.233 84.396  1.00 40.17 ? 3239 LYS A O     1 
ATOM   14223 C  CB    . LYS A 1 3239 ? 220.974 214.009 87.232  1.00 36.88 ? 3239 LYS A CB    1 
ATOM   14224 C  CG    . LYS A 1 3239 ? 222.416 214.157 87.689  1.00 36.45 ? 3239 LYS A CG    1 
ATOM   14225 C  CD    . LYS A 1 3239 ? 222.617 213.591 89.086  1.00 35.89 ? 3239 LYS A CD    1 
ATOM   14226 C  CE    . LYS A 1 3239 ? 223.968 213.991 89.654  1.00 34.80 ? 3239 LYS A CE    1 
ATOM   14227 N  NZ    . LYS A 1 3239 ? 224.112 213.595 91.081  1.00 31.91 ? 3239 LYS A NZ    1 
ATOM   14228 N  N     . LEU A 1 3240 ? 218.239 214.571 85.671  1.00 38.25 ? 3240 LEU A N     1 
ATOM   14229 C  CA    . LEU A 1 3240 ? 217.004 214.078 85.068  1.00 35.58 ? 3240 LEU A CA    1 
ATOM   14230 C  C     . LEU A 1 3240 ? 216.888 214.490 83.607  1.00 39.22 ? 3240 LEU A C     1 
ATOM   14231 O  O     . LEU A 1 3240 ? 216.393 213.714 82.783  1.00 39.92 ? 3240 LEU A O     1 
ATOM   14232 C  CB    . LEU A 1 3240 ? 215.797 214.578 85.861  1.00 36.86 ? 3240 LEU A CB    1 
ATOM   14233 C  CG    . LEU A 1 3240 ? 215.235 213.614 86.907  1.00 39.77 ? 3240 LEU A CG    1 
ATOM   14234 C  CD1   . LEU A 1 3240 ? 213.975 214.183 87.541  1.00 32.39 ? 3240 LEU A CD1   1 
ATOM   14235 C  CD2   . LEU A 1 3240 ? 214.962 212.251 86.289  1.00 33.59 ? 3240 LEU A CD2   1 
ATOM   14236 N  N     . LYS A 1 3241 ? 217.335 215.701 83.266  1.00 36.74 ? 3241 LYS A N     1 
ATOM   14237 C  CA    . LYS A 1 3241 ? 217.278 216.174 81.888  1.00 34.93 ? 3241 LYS A CA    1 
ATOM   14238 C  C     . LYS A 1 3241 ? 218.228 215.423 80.964  1.00 35.77 ? 3241 LYS A C     1 
ATOM   14239 O  O     . LYS A 1 3241 ? 218.088 215.535 79.741  1.00 36.38 ? 3241 LYS A O     1 
ATOM   14240 C  CB    . LYS A 1 3241 ? 217.587 217.672 81.835  1.00 33.29 ? 3241 LYS A CB    1 
ATOM   14241 C  CG    . LYS A 1 3241 ? 216.449 218.560 82.309  1.00 32.27 ? 3241 LYS A CG    1 
ATOM   14242 C  CD    . LYS A 1 3241 ? 216.951 219.939 82.698  1.00 35.55 ? 3241 LYS A CD    1 
ATOM   14243 C  CE    . LYS A 1 3241 ? 215.917 220.694 83.519  1.00 32.84 ? 3241 LYS A CE    1 
ATOM   14244 N  NZ    . LYS A 1 3241 ? 216.476 221.947 84.098  1.00 34.41 ? 3241 LYS A NZ    1 
ATOM   14245 N  N     . LYS A 1 3242 ? 219.182 214.674 81.509  1.00 35.94 ? 3242 LYS A N     1 
ATOM   14246 C  CA    . LYS A 1 3242 ? 220.123 213.915 80.693  1.00 37.54 ? 3242 LYS A CA    1 
ATOM   14247 C  C     . LYS A 1 3242 ? 219.417 212.791 79.943  1.00 31.83 ? 3242 LYS A C     1 
ATOM   14248 O  O     . LYS A 1 3242 ? 218.343 212.337 80.342  0.00 28.42 ? 3242 LYS A O     1 
ATOM   14249 C  CB    . LYS A 1 3242 ? 221.245 213.342 81.561  1.00 36.48 ? 3242 LYS A CB    1 
ATOM   14250 C  CG    . LYS A 1 3242 ? 222.213 214.385 82.097  1.00 36.32 ? 3242 LYS A CG    1 
ATOM   14251 C  CD    . LYS A 1 3242 ? 223.197 213.770 83.078  1.00 37.12 ? 3242 LYS A CD    1 
ATOM   14252 C  CE    . LYS A 1 3242 ? 224.120 214.822 83.669  1.00 34.67 ? 3242 LYS A CE    1 
ATOM   14253 N  NZ    . LYS A 1 3242 ? 224.918 214.284 84.805  1.00 34.18 ? 3242 LYS A NZ    1 
ATOM   14254 N  N     . GLU A 1 3449 ? 216.270 206.014 88.287  1.00 35.51 ? 3449 GLU A N     1 
ATOM   14255 C  CA    . GLU A 1 3449 ? 215.953 205.369 89.557  1.00 38.41 ? 3449 GLU A CA    1 
ATOM   14256 C  C     . GLU A 1 3449 ? 216.718 206.020 90.706  1.00 41.25 ? 3449 GLU A C     1 
ATOM   14257 O  O     . GLU A 1 3449 ? 216.144 206.326 91.751  1.00 41.70 ? 3449 GLU A O     1 
ATOM   14258 C  CB    . GLU A 1 3449 ? 216.268 203.875 89.492  1.00 36.95 ? 3449 GLU A CB    1 
ATOM   14259 C  CG    . GLU A 1 3449 ? 215.547 203.142 88.373  1.00 35.67 ? 3449 GLU A CG    1 
ATOM   14260 C  CD    . GLU A 1 3449 ? 215.888 201.666 88.326  1.00 42.81 ? 3449 GLU A CD    1 
ATOM   14261 O  OE1   . GLU A 1 3449 ? 216.718 201.222 89.145  1.00 43.39 ? 3449 GLU A OE1   1 
ATOM   14262 O  OE2   . GLU A 1 3449 ? 215.324 200.951 87.471  1.00 39.68 ? 3449 GLU A OE2   1 
ATOM   14263 N  N     . GLU A 1 3450 ? 218.022 206.225 90.504  1.00 40.55 ? 3450 GLU A N     1 
ATOM   14264 C  CA    . GLU A 1 3450 ? 218.828 206.893 91.521  1.00 39.22 ? 3450 GLU A CA    1 
ATOM   14265 C  C     . GLU A 1 3450 ? 218.424 208.351 91.687  1.00 37.47 ? 3450 GLU A C     1 
ATOM   14266 O  O     . GLU A 1 3450 ? 218.499 208.892 92.796  1.00 40.12 ? 3450 GLU A O     1 
ATOM   14267 C  CB    . GLU A 1 3450 ? 220.312 206.787 91.170  1.00 37.29 ? 3450 GLU A CB    1 
ATOM   14268 C  CG    . GLU A 1 3450 ? 221.247 207.272 92.267  1.00 34.96 ? 3450 GLU A CG    1 
ATOM   14269 C  CD    . GLU A 1 3450 ? 222.672 206.793 92.074  1.00 40.69 ? 3450 GLU A CD    1 
ATOM   14270 O  OE1   . GLU A 1 3450 ? 222.979 206.263 90.986  1.00 40.03 ? 3450 GLU A OE1   1 
ATOM   14271 O  OE2   . GLU A 1 3450 ? 223.483 206.946 93.011  1.00 38.89 ? 3450 GLU A OE2   1 
ATOM   14272 N  N     . TYR A 1 3451 ? 217.995 209.003 90.603  1.00 36.10 ? 3451 TYR A N     1 
ATOM   14273 C  CA    . TYR A 1 3451 ? 217.538 210.385 90.697  1.00 36.43 ? 3451 TYR A CA    1 
ATOM   14274 C  C     . TYR A 1 3451 ? 216.287 210.505 91.556  1.00 37.71 ? 3451 TYR A C     1 
ATOM   14275 O  O     . TYR A 1 3451 ? 216.059 211.551 92.174  1.00 35.77 ? 3451 TYR A O     1 
ATOM   14276 C  CB    . TYR A 1 3451 ? 217.285 210.952 89.300  1.00 37.82 ? 3451 TYR A CB    1 
ATOM   14277 C  CG    . TYR A 1 3451 ? 218.378 210.637 88.302  1.00 39.02 ? 3451 TYR A CG    1 
ATOM   14278 C  CD1   . TYR A 1 3451 ? 219.719 210.802 88.634  1.00 38.15 ? 3451 TYR A CD1   1 
ATOM   14279 C  CD2   . TYR A 1 3451 ? 218.072 210.172 87.031  1.00 37.99 ? 3451 TYR A CD2   1 
ATOM   14280 C  CE1   . TYR A 1 3451 ? 220.719 210.513 87.728  1.00 38.49 ? 3451 TYR A CE1   1 
ATOM   14281 C  CE2   . TYR A 1 3451 ? 219.066 209.881 86.117  1.00 38.48 ? 3451 TYR A CE2   1 
ATOM   14282 C  CZ    . TYR A 1 3451 ? 220.389 210.054 86.471  1.00 42.95 ? 3451 TYR A CZ    1 
ATOM   14283 O  OH    . TYR A 1 3451 ? 221.382 209.766 85.563  1.00 45.01 ? 3451 TYR A OH    1 
ATOM   14284 N  N     . ALA A 1 3452 ? 215.465 209.453 91.602  1.00 40.27 ? 3452 ALA A N     1 
ATOM   14285 C  CA    . ALA A 1 3452 ? 214.307 209.458 92.490  1.00 38.88 ? 3452 ALA A CA    1 
ATOM   14286 C  C     . ALA A 1 3452 ? 214.739 209.503 93.950  1.00 39.33 ? 3452 ALA A C     1 
ATOM   14287 O  O     . ALA A 1 3452 ? 214.086 210.145 94.780  1.00 38.27 ? 3452 ALA A O     1 
ATOM   14288 C  CB    . ALA A 1 3452 ? 213.435 208.232 92.225  1.00 33.51 ? 3452 ALA A CB    1 
ATOM   14289 N  N     . VAL A 1 3453 ? 215.833 208.817 94.285  1.00 35.52 ? 3453 VAL A N     1 
ATOM   14290 C  CA    . VAL A 1 3453 ? 216.380 208.909 95.633  1.00 34.84 ? 3453 VAL A CA    1 
ATOM   14291 C  C     . VAL A 1 3453 ? 216.936 210.306 95.887  1.00 36.93 ? 3453 VAL A C     1 
ATOM   14292 O  O     . VAL A 1 3453 ? 216.801 210.852 96.989  1.00 35.86 ? 3453 VAL A O     1 
ATOM   14293 C  CB    . VAL A 1 3453 ? 217.449 207.823 95.852  1.00 34.12 ? 3453 VAL A CB    1 
ATOM   14294 C  CG1   . VAL A 1 3453 ? 217.977 207.870 97.279  1.00 32.51 ? 3453 VAL A CG1   1 
ATOM   14295 C  CG2   . VAL A 1 3453 ? 216.880 206.449 95.531  1.00 30.75 ? 3453 VAL A CG2   1 
ATOM   14296 N  N     . LEU A 1 3454 ? 217.569 210.904 94.874  1.00 35.34 ? 3454 LEU A N     1 
ATOM   14297 C  CA    . LEU A 1 3454 ? 218.146 212.234 95.040  1.00 36.04 ? 3454 LEU A CA    1 
ATOM   14298 C  C     . LEU A 1 3454 ? 217.072 213.280 95.306  1.00 37.88 ? 3454 LEU A C     1 
ATOM   14299 O  O     . LEU A 1 3454 ? 217.239 214.140 96.180  1.00 37.52 ? 3454 LEU A O     1 
ATOM   14300 C  CB    . LEU A 1 3454 ? 218.963 212.607 93.803  1.00 37.98 ? 3454 LEU A CB    1 
ATOM   14301 C  CG    . LEU A 1 3454 ? 219.954 213.761 93.968  1.00 38.92 ? 3454 LEU A CG    1 
ATOM   14302 C  CD1   . LEU A 1 3454 ? 221.032 213.403 94.981  1.00 32.67 ? 3454 LEU A CD1   1 
ATOM   14303 C  CD2   . LEU A 1 3454 ? 220.572 214.136 92.630  1.00 33.91 ? 3454 LEU A CD2   1 
ATOM   14304 N  N     . ILE A 1 3455 ? 215.963 213.232 94.563  1.00 35.87 ? 3455 ILE A N     1 
ATOM   14305 C  CA    . ILE A 1 3455 ? 214.884 214.183 94.807  1.00 37.04 ? 3455 ILE A CA    1 
ATOM   14306 C  C     . ILE A 1 3455 ? 214.191 213.879 96.129  1.00 36.73 ? 3455 ILE A C     1 
ATOM   14307 O  O     . ILE A 1 3455 ? 213.692 214.790 96.801  1.00 35.72 ? 3455 ILE A O     1 
ATOM   14308 C  CB    . ILE A 1 3455 ? 213.890 214.202 93.629  1.00 36.36 ? 3455 ILE A CB    1 
ATOM   14309 C  CG1   . ILE A 1 3455 ? 213.179 212.856 93.486  1.00 36.94 ? 3455 ILE A CG1   1 
ATOM   14310 C  CG2   . ILE A 1 3455 ? 214.603 214.567 92.337  1.00 28.33 ? 3455 ILE A CG2   1 
ATOM   14311 C  CD1   . ILE A 1 3455 ? 212.022 212.878 92.510  1.00 31.58 ? 3455 ILE A CD1   1 
ATOM   14312 N  N     . SER A 1 3456 ? 214.139 212.602 96.523  1.00 34.64 ? 3456 SER A N     1 
ATOM   14313 C  CA    . SER A 1 3456 ? 213.616 212.259 97.840  1.00 36.57 ? 3456 SER A CA    1 
ATOM   14314 C  C     . SER A 1 3456 ? 214.504 212.821 98.942  1.00 37.44 ? 3456 SER A C     1 
ATOM   14315 O  O     . SER A 1 3456 ? 214.009 213.288 99.974  1.00 36.99 ? 3456 SER A O     1 
ATOM   14316 C  CB    . SER A 1 3456 ? 213.484 210.742 97.975  1.00 32.94 ? 3456 SER A CB    1 
ATOM   14317 O  OG    . SER A 1 3456 ? 214.737 210.146 98.268  1.00 36.85 ? 3456 SER A OG    1 
ATOM   14318 N  N     . GLU A 1 3457 ? 215.824 212.777 98.740  1.00 34.30 ? 3457 GLU A N     1 
ATOM   14319 C  CA    . GLU A 1 3457 ? 216.740 213.383 99.700  1.00 35.11 ? 3457 GLU A CA    1 
ATOM   14320 C  C     . GLU A 1 3457 ? 216.529 214.890 99.782  1.00 37.23 ? 3457 GLU A C     1 
ATOM   14321 O  O     . GLU A 1 3457 ? 216.556 215.469 100.874 1.00 38.82 ? 3457 GLU A O     1 
ATOM   14322 C  CB    . GLU A 1 3457 ? 218.185 213.058 99.320  1.00 30.82 ? 3457 GLU A CB    1 
ATOM   14323 C  CG    . GLU A 1 3457 ? 219.211 213.399 100.391 1.00 31.64 ? 3457 GLU A CG    1 
ATOM   14324 C  CD    . GLU A 1 3457 ? 219.744 214.812 100.258 1.00 41.80 ? 3457 GLU A CD    1 
ATOM   14325 O  OE1   . GLU A 1 3457 ? 219.741 215.348 99.129  1.00 43.62 ? 3457 GLU A OE1   1 
ATOM   14326 O  OE2   . GLU A 1 3457 ? 220.170 215.387 101.282 1.00 41.20 ? 3457 GLU A OE2   1 
ATOM   14327 N  N     . ALA A 1 3458 ? 216.321 215.540 98.635  1.00 35.05 ? 3458 ALA A N     1 
ATOM   14328 C  CA    . ALA A 1 3458 ? 216.034 216.971 98.637  1.00 36.19 ? 3458 ALA A CA    1 
ATOM   14329 C  C     . ALA A 1 3458 ? 214.719 217.266 99.348  1.00 37.76 ? 3458 ALA A C     1 
ATOM   14330 O  O     . ALA A 1 3458 ? 214.616 218.246 100.097 1.00 38.95 ? 3458 ALA A O     1 
ATOM   14331 C  CB    . ALA A 1 3458 ? 216.004 217.503 97.205  1.00 31.95 ? 3458 ALA A CB    1 
ATOM   14332 N  N     . GLN A 1 3459 ? 213.700 216.432 99.122  1.00 37.77 ? 3459 GLN A N     1 
ATOM   14333 C  CA    . GLN A 1 3459 ? 212.423 216.622 99.802  1.00 37.96 ? 3459 GLN A CA    1 
ATOM   14334 C  C     . GLN A 1 3459 ? 212.569 216.442 101.308 1.00 38.14 ? 3459 GLN A C     1 
ATOM   14335 O  O     . GLN A 1 3459 ? 211.938 217.158 102.092 1.00 37.20 ? 3459 GLN A O     1 
ATOM   14336 C  CB    . GLN A 1 3459 ? 211.379 215.659 99.239  1.00 32.77 ? 3459 GLN A CB    1 
ATOM   14337 C  CG    . GLN A 1 3459 ? 209.979 215.868 99.796  1.00 34.91 ? 3459 GLN A CG    1 
ATOM   14338 C  CD    . GLN A 1 3459 ? 208.941 215.009 99.103  1.00 40.82 ? 3459 GLN A CD    1 
ATOM   14339 O  OE1   . GLN A 1 3459 ? 208.702 215.149 97.904  1.00 37.46 ? 3459 GLN A OE1   1 
ATOM   14340 N  NE2   . GLN A 1 3459 ? 208.317 214.112 99.858  1.00 34.15 ? 3459 GLN A NE2   1 
ATOM   14341 N  N     . ALA A 1 3460 ? 213.392 215.477 101.729 1.00 36.07 ? 3460 ALA A N     1 
ATOM   14342 C  CA    . ALA A 1 3460 ? 213.637 215.284 103.156 1.00 35.03 ? 3460 ALA A CA    1 
ATOM   14343 C  C     . ALA A 1 3460 ? 214.302 216.511 103.770 1.00 37.93 ? 3460 ALA A C     1 
ATOM   14344 O  O     . ALA A 1 3460 ? 213.967 216.912 104.890 1.00 38.85 ? 3460 ALA A O     1 
ATOM   14345 C  CB    . ALA A 1 3460 ? 214.493 214.039 103.378 1.00 27.91 ? 3460 ALA A CB    1 
ATOM   14346 N  N     . ILE A 1 3461 ? 215.251 217.115 103.051 1.00 35.07 ? 3461 ILE A N     1 
ATOM   14347 C  CA    . ILE A 1 3461 ? 215.883 218.339 103.532 1.00 34.96 ? 3461 ILE A CA    1 
ATOM   14348 C  C     . ILE A 1 3461 ? 214.872 219.477 103.594 1.00 35.17 ? 3461 ILE A C     1 
ATOM   14349 O  O     . ILE A 1 3461 ? 214.944 220.333 104.486 1.00 36.26 ? 3461 ILE A O     1 
ATOM   14350 C  CB    . ILE A 1 3461 ? 217.092 218.696 102.649 1.00 33.09 ? 3461 ILE A CB    1 
ATOM   14351 C  CG1   . ILE A 1 3461 ? 218.127 217.569 102.684 1.00 35.00 ? 3461 ILE A CG1   1 
ATOM   14352 C  CG2   . ILE A 1 3461 ? 217.730 219.997 103.105 1.00 34.30 ? 3461 ILE A CG2   1 
ATOM   14353 C  CD1   . ILE A 1 3461 ? 218.494 217.117 104.081 1.00 34.60 ? 3461 ILE A CD1   1 
ATOM   14354 N  N     . LYS A 1 3462 ? 213.916 219.510 102.660 1.00 33.51 ? 3462 LYS A N     1 
ATOM   14355 C  CA    . LYS A 1 3462 ? 212.870 220.531 102.704 1.00 34.82 ? 3462 LYS A CA    1 
ATOM   14356 C  C     . LYS A 1 3462 ? 212.086 220.454 104.007 1.00 32.99 ? 3462 LYS A C     1 
ATOM   14357 O  O     . LYS A 1 3462 ? 211.746 221.486 104.597 1.00 32.52 ? 3462 LYS A O     1 
ATOM   14358 C  CB    . LYS A 1 3462 ? 211.933 220.378 101.505 1.00 32.51 ? 3462 LYS A CB    1 
ATOM   14359 C  CG    . LYS A 1 3462 ? 212.541 220.789 100.175 1.00 34.64 ? 3462 LYS A CG    1 
ATOM   14360 C  CD    . LYS A 1 3462 ? 211.465 221.081 99.141  1.00 32.67 ? 3462 LYS A CD    1 
ATOM   14361 C  CE    . LYS A 1 3462 ? 210.703 222.352 99.479  1.00 31.00 ? 3462 LYS A CE    1 
ATOM   14362 N  NZ    . LYS A 1 3462 ? 211.611 223.524 99.610  1.00 30.22 ? 3462 LYS A NZ    1 
ATOM   14363 N  N     . ALA A 1 3463 ? 211.782 219.238 104.467 1.00 34.07 ? 3463 ALA A N     1 
ATOM   14364 C  CA    . ALA A 1 3463 ? 211.146 219.081 105.770 1.00 36.75 ? 3463 ALA A CA    1 
ATOM   14365 C  C     . ALA A 1 3463 ? 212.054 219.577 106.887 1.00 36.87 ? 3463 ALA A C     1 
ATOM   14366 O  O     . ALA A 1 3463 ? 211.587 220.191 107.853 1.00 38.31 ? 3463 ALA A O     1 
ATOM   14367 C  CB    . ALA A 1 3463 ? 210.762 217.619 105.995 1.00 28.57 ? 3463 ALA A CB    1 
ATOM   14368 N  N     . ASP A 1 3464 ? 213.360 219.314 106.775 1.00 32.95 ? 3464 ASP A N     1 
ATOM   14369 C  CA    . ASP A 1 3464 ? 214.305 219.813 107.768 1.00 33.86 ? 3464 ASP A CA    1 
ATOM   14370 C  C     . ASP A 1 3464 ? 214.334 221.336 107.785 1.00 36.45 ? 3464 ASP A C     1 
ATOM   14371 O  O     . ASP A 1 3464 ? 214.370 221.952 108.856 1.00 35.01 ? 3464 ASP A O     1 
ATOM   14372 C  CB    . ASP A 1 3464 ? 215.699 219.252 107.494 1.00 34.00 ? 3464 ASP A CB    1 
ATOM   14373 C  CG    . ASP A 1 3464 ? 216.626 219.382 108.686 1.00 38.62 ? 3464 ASP A CG    1 
ATOM   14374 O  OD1   . ASP A 1 3464 ? 216.138 219.711 109.788 1.00 40.12 ? 3464 ASP A OD1   1 
ATOM   14375 O  OD2   . ASP A 1 3464 ? 217.842 219.154 108.522 1.00 39.00 ? 3464 ASP A OD2   1 
ATOM   14376 N  N     . LEU A 1 3465 ? 214.324 221.962 106.604 1.00 34.46 ? 3465 LEU A N     1 
ATOM   14377 C  CA    . LEU A 1 3465 ? 214.289 223.419 106.540 1.00 31.51 ? 3465 LEU A CA    1 
ATOM   14378 C  C     . LEU A 1 3465 ? 212.987 223.961 107.118 1.00 36.17 ? 3465 LEU A C     1 
ATOM   14379 O  O     . LEU A 1 3465 ? 212.980 225.000 107.786 1.00 36.25 ? 3465 LEU A O     1 
ATOM   14380 C  CB    . LEU A 1 3465 ? 214.479 223.885 105.096 1.00 30.51 ? 3465 LEU A CB    1 
ATOM   14381 C  CG    . LEU A 1 3465 ? 214.626 225.389 104.849 1.00 33.76 ? 3465 LEU A CG    1 
ATOM   14382 C  CD1   . LEU A 1 3465 ? 215.658 225.644 103.765 1.00 33.90 ? 3465 LEU A CD1   1 
ATOM   14383 C  CD2   . LEU A 1 3465 ? 213.295 226.014 104.463 1.00 28.51 ? 3465 LEU A CD2   1 
ATOM   14384 N  N     . ALA A 1 3466 ? 211.872 223.273 106.860 1.00 35.53 ? 3466 ALA A N     1 
ATOM   14385 C  CA    . ALA A 1 3466 ? 210.598 223.682 107.446 1.00 34.57 ? 3466 ALA A CA    1 
ATOM   14386 C  C     . ALA A 1 3466 ? 210.643 223.595 108.967 1.00 35.98 ? 3466 ALA A C     1 
ATOM   14387 O  O     . ALA A 1 3466 ? 210.120 224.474 109.662 1.00 35.66 ? 3466 ALA A O     1 
ATOM   14388 C  CB    . ALA A 1 3466 ? 209.464 222.824 106.890 1.00 27.69 ? 3466 ALA A CB    1 
ATOM   14389 N  N     . ALA A 1 3467 ? 211.259 222.538 109.501 1.00 31.10 ? 3467 ALA A N     1 
ATOM   14390 C  CA    . ALA A 1 3467 ? 211.419 222.430 110.946 1.00 31.38 ? 3467 ALA A CA    1 
ATOM   14391 C  C     . ALA A 1 3467 ? 212.336 223.522 111.482 1.00 33.71 ? 3467 ALA A C     1 
ATOM   14392 O  O     . ALA A 1 3467 ? 212.121 224.035 112.587 1.00 34.50 ? 3467 ALA A O     1 
ATOM   14393 C  CB    . ALA A 1 3467 ? 211.955 221.048 111.314 1.00 28.44 ? 3467 ALA A CB    1 
ATOM   14394 N  N     . VAL A 1 3468 ? 213.371 223.880 110.721 1.00 31.64 ? 3468 VAL A N     1 
ATOM   14395 C  CA    . VAL A 1 3468 ? 214.300 224.916 111.161 1.00 29.36 ? 3468 VAL A CA    1 
ATOM   14396 C  C     . VAL A 1 3468 ? 213.623 226.283 111.159 1.00 30.04 ? 3468 VAL A C     1 
ATOM   14397 O  O     . VAL A 1 3468 ? 213.728 227.045 112.125 1.00 32.08 ? 3468 VAL A O     1 
ATOM   14398 C  CB    . VAL A 1 3468 ? 215.566 224.908 110.285 1.00 33.83 ? 3468 VAL A CB    1 
ATOM   14399 C  CG1   . VAL A 1 3468 ? 216.333 226.211 110.442 1.00 33.70 ? 3468 VAL A CG1   1 
ATOM   14400 C  CG2   . VAL A 1 3468 ? 216.450 223.725 110.646 1.00 32.66 ? 3468 VAL A CG2   1 
ATOM   14401 N  N     . GLU A 1 3469 ? 212.914 226.612 110.073 1.00 32.54 ? 3469 GLU A N     1 
ATOM   14402 C  CA    . GLU A 1 3469 ? 212.308 227.937 109.968 1.00 32.21 ? 3469 GLU A CA    1 
ATOM   14403 C  C     . GLU A 1 3469 ? 211.197 228.122 110.995 1.00 35.23 ? 3469 GLU A C     1 
ATOM   14404 O  O     . GLU A 1 3469 ? 211.028 229.219 111.542 1.00 38.26 ? 3469 GLU A O     1 
ATOM   14405 C  CB    . GLU A 1 3469 ? 211.787 228.179 108.550 1.00 30.24 ? 3469 GLU A CB    1 
ATOM   14406 C  CG    . GLU A 1 3469 ? 210.664 227.256 108.109 1.00 34.59 ? 3469 GLU A CG    1 
ATOM   14407 C  CD    . GLU A 1 3469 ? 210.183 227.559 106.704 1.00 37.95 ? 3469 GLU A CD    1 
ATOM   14408 O  OE1   . GLU A 1 3469 ? 209.653 228.666 106.482 1.00 35.43 ? 3469 GLU A OE1   1 
ATOM   14409 O  OE2   . GLU A 1 3469 ? 210.336 226.687 105.821 1.00 41.41 ? 3469 GLU A OE2   1 
ATOM   14410 N  N     . ALA A 1 3470 ? 210.431 227.064 111.271 1.00 33.04 ? 3470 ALA A N     1 
ATOM   14411 C  CA    . ALA A 1 3470 ? 209.422 227.140 112.321 1.00 34.07 ? 3470 ALA A CA    1 
ATOM   14412 C  C     . ALA A 1 3470 ? 210.068 227.346 113.683 1.00 35.82 ? 3470 ALA A C     1 
ATOM   14413 O  O     . ALA A 1 3470 ? 209.546 228.087 114.524 1.00 35.91 ? 3470 ALA A O     1 
ATOM   14414 C  CB    . ALA A 1 3470 ? 208.561 225.877 112.316 1.00 30.80 ? 3470 ALA A CB    1 
ATOM   14415 N  N     . LYS A 1 3471 ? 211.209 226.694 113.918 1.00 30.83 ? 3471 LYS A N     1 
ATOM   14416 C  CA    . LYS A 1 3471 ? 211.920 226.865 115.179 1.00 28.10 ? 3471 LYS A CA    1 
ATOM   14417 C  C     . LYS A 1 3471 ? 212.470 228.280 115.314 1.00 29.94 ? 3471 LYS A C     1 
ATOM   14418 O  O     . LYS A 1 3471 ? 212.534 228.824 116.423 1.00 30.76 ? 3471 LYS A O     1 
ATOM   14419 C  CB    . LYS A 1 3471 ? 213.041 225.832 115.283 1.00 28.88 ? 3471 LYS A CB    1 
ATOM   14420 C  CG    . LYS A 1 3471 ? 213.803 225.851 116.596 1.00 29.59 ? 3471 LYS A CG    1 
ATOM   14421 C  CD    . LYS A 1 3471 ? 214.975 224.886 116.553 1.00 29.89 ? 3471 LYS A CD    1 
ATOM   14422 C  CE    . LYS A 1 3471 ? 215.017 224.011 117.793 1.00 32.07 ? 3471 LYS A CE    1 
ATOM   14423 N  NZ    . LYS A 1 3471 ? 216.315 223.296 117.925 1.00 33.47 ? 3471 LYS A NZ    1 
ATOM   14424 N  N     . VAL A 1 3472 ? 212.876 228.888 114.198 1.00 33.43 ? 3472 VAL A N     1 
ATOM   14425 C  CA    . VAL A 1 3472 ? 213.369 230.263 114.235 1.00 31.08 ? 3472 VAL A CA    1 
ATOM   14426 C  C     . VAL A 1 3472 ? 212.250 231.216 114.636 1.00 32.88 ? 3472 VAL A C     1 
ATOM   14427 O  O     . VAL A 1 3472 ? 212.428 232.088 115.494 1.00 34.73 ? 3472 VAL A O     1 
ATOM   14428 C  CB    . VAL A 1 3472 ? 213.980 230.652 112.876 1.00 31.29 ? 3472 VAL A CB    1 
ATOM   14429 C  CG1   . VAL A 1 3472 ? 214.056 232.165 112.734 1.00 28.59 ? 3472 VAL A CG1   1 
ATOM   14430 C  CG2   . VAL A 1 3472 ? 215.352 230.033 112.714 1.00 31.88 ? 3472 VAL A CG2   1 
ATOM   14431 N  N     . ASN A 1 3473 ? 211.076 231.060 114.018 1.00 33.02 ? 3473 ASN A N     1 
ATOM   14432 C  CA    . ASN A 1 3473 ? 209.963 231.957 114.308 1.00 30.91 ? 3473 ASN A CA    1 
ATOM   14433 C  C     . ASN A 1 3473 ? 209.465 231.785 115.737 1.00 32.25 ? 3473 ASN A C     1 
ATOM   14434 O  O     . ASN A 1 3473 ? 209.168 232.773 116.419 1.00 34.98 ? 3473 ASN A O     1 
ATOM   14435 C  CB    . ASN A 1 3473 ? 208.828 231.722 113.312 1.00 28.38 ? 3473 ASN A CB    1 
ATOM   14436 C  CG    . ASN A 1 3473 ? 209.256 231.946 111.877 1.00 34.77 ? 3473 ASN A CG    1 
ATOM   14437 O  OD1   . ASN A 1 3473 ? 210.398 232.316 111.609 1.00 35.30 ? 3473 ASN A OD1   1 
ATOM   14438 N  ND2   . ASN A 1 3473 ? 208.339 231.721 110.943 1.00 33.37 ? 3473 ASN A ND2   1 
ATOM   14439 N  N     . ARG A 1 3474 ? 209.360 230.540 116.206 1.00 28.87 ? 3474 ARG A N     1 
ATOM   14440 C  CA    . ARG A 1 3474 ? 208.877 230.306 117.562 1.00 29.61 ? 3474 ARG A CA    1 
ATOM   14441 C  C     . ARG A 1 3474 ? 209.864 230.824 118.601 1.00 31.20 ? 3474 ARG A C     1 
ATOM   14442 O  O     . ARG A 1 3474 ? 209.459 231.414 119.608 1.00 31.62 ? 3474 ARG A O     1 
ATOM   14443 C  CB    . ARG A 1 3474 ? 208.601 228.817 117.774 1.00 29.01 ? 3474 ARG A CB    1 
ATOM   14444 C  CG    . ARG A 1 3474 ? 208.012 228.493 119.135 1.00 27.19 ? 3474 ARG A CG    1 
ATOM   14445 C  CD    . ARG A 1 3474 ? 207.725 227.011 119.286 1.00 28.20 ? 3474 ARG A CD    1 
ATOM   14446 N  NE    . ARG A 1 3474 ? 208.939 226.206 119.248 1.00 34.35 ? 3474 ARG A NE    1 
ATOM   14447 C  CZ    . ARG A 1 3474 ? 208.954 224.882 119.171 1.00 37.36 ? 3474 ARG A CZ    1 
ATOM   14448 N  NH1   . ARG A 1 3474 ? 207.836 224.179 119.128 1.00 35.49 ? 3474 ARG A NH1   1 
ATOM   14449 N  NH2   . ARG A 1 3474 ? 210.123 224.248 119.141 1.00 37.57 ? 3474 ARG A NH2   1 
ATOM   14450 N  N     . SER A 1 3475 ? 211.162 230.613 118.372 1.00 30.53 ? 3475 SER A N     1 
ATOM   14451 C  CA    . SER A 1 3475 ? 212.161 231.097 119.319 1.00 30.76 ? 3475 SER A CA    1 
ATOM   14452 C  C     . SER A 1 3475 ? 212.275 232.615 119.273 1.00 29.04 ? 3475 SER A C     1 
ATOM   14453 O  O     . SER A 1 3475 ? 212.527 233.254 120.301 1.00 33.31 ? 3475 SER A O     1 
ATOM   14454 C  CB    . SER A 1 3475 ? 213.514 230.445 119.035 1.00 32.55 ? 3475 SER A CB    1 
ATOM   14455 O  OG    . SER A 1 3475 ? 214.502 230.920 119.931 1.00 37.43 ? 3475 SER A OG    1 
ATOM   14456 N  N     . THR A 1 3476 ? 212.109 233.208 118.089 1.00 28.62 ? 3476 THR A N     1 
ATOM   14457 C  CA    . THR A 1 3476 ? 212.098 234.663 117.989 1.00 28.99 ? 3476 THR A CA    1 
ATOM   14458 C  C     . THR A 1 3476 ? 210.894 235.251 118.713 1.00 28.57 ? 3476 THR A C     1 
ATOM   14459 O  O     . THR A 1 3476 ? 211.012 236.274 119.398 1.00 34.35 ? 3476 THR A O     1 
ATOM   14460 C  CB    . THR A 1 3476 ? 212.106 235.090 116.521 1.00 28.01 ? 3476 THR A CB    1 
ATOM   14461 O  OG1   . THR A 1 3476 ? 213.230 234.496 115.857 1.00 32.04 ? 3476 THR A OG1   1 
ATOM   14462 C  CG2   . THR A 1 3476 ? 212.199 236.601 116.401 1.00 24.11 ? 3476 THR A CG2   1 
ATOM   14463 N  N     . ALA A 1 3477 ? 209.727 234.619 118.570 1.00 29.02 ? 3477 ALA A N     1 
ATOM   14464 C  CA    . ALA A 1 3477 ? 208.550 235.057 119.313 1.00 33.53 ? 3477 ALA A CA    1 
ATOM   14465 C  C     . ALA A 1 3477 ? 208.744 234.866 120.810 1.00 30.75 ? 3477 ALA A C     1 
ATOM   14466 O  O     . ALA A 1 3477 ? 208.312 235.702 121.614 1.00 28.94 ? 3477 ALA A O     1 
ATOM   14467 C  CB    . ALA A 1 3477 ? 207.311 234.304 118.829 1.00 29.54 ? 3477 ALA A CB    1 
ATOM   14468 N  N     . LEU A 1 3478 ? 209.387 233.763 121.206 1.00 29.50 ? 3478 LEU A N     1 
ATOM   14469 C  CA    . LEU A 1 3478 ? 209.730 233.570 122.610 1.00 26.09 ? 3478 LEU A CA    1 
ATOM   14470 C  C     . LEU A 1 3478 ? 210.665 234.666 123.100 1.00 28.22 ? 3478 LEU A C     1 
ATOM   14471 O  O     . LEU A 1 3478 ? 210.484 235.203 124.197 1.00 29.71 ? 3478 LEU A O     1 
ATOM   14472 C  CB    . LEU A 1 3478 ? 210.367 232.195 122.810 1.00 23.67 ? 3478 LEU A CB    1 
ATOM   14473 C  CG    . LEU A 1 3478 ? 210.845 231.859 124.224 1.00 31.25 ? 3478 LEU A CG    1 
ATOM   14474 C  CD1   . LEU A 1 3478 ? 209.666 231.645 125.156 1.00 26.62 ? 3478 LEU A CD1   1 
ATOM   14475 C  CD2   . LEU A 1 3478 ? 211.752 230.642 124.213 1.00 27.80 ? 3478 LEU A CD2   1 
ATOM   14476 N  N     . LEU A 1 3479 ? 211.670 235.014 122.293 1.00 24.19 ? 3479 LEU A N     1 
ATOM   14477 C  CA    . LEU A 1 3479 ? 212.588 236.083 122.669 1.00 24.98 ? 3479 LEU A CA    1 
ATOM   14478 C  C     . LEU A 1 3479 ? 211.866 237.418 122.780 1.00 27.51 ? 3479 LEU A C     1 
ATOM   14479 O  O     . LEU A 1 3479 ? 212.125 238.198 123.704 1.00 31.82 ? 3479 LEU A O     1 
ATOM   14480 C  CB    . LEU A 1 3479 ? 213.731 236.168 121.659 1.00 27.69 ? 3479 LEU A CB    1 
ATOM   14481 C  CG    . LEU A 1 3479 ? 214.908 235.231 121.922 1.00 26.15 ? 3479 LEU A CG    1 
ATOM   14482 C  CD1   . LEU A 1 3479 ? 215.946 235.343 120.822 1.00 26.01 ? 3479 LEU A CD1   1 
ATOM   14483 C  CD2   . LEU A 1 3479 ? 215.521 235.536 123.277 1.00 28.14 ? 3479 LEU A CD2   1 
ATOM   14484 N  N     . LYS A 1 3480 ? 210.962 237.704 121.841 1.00 28.86 ? 3480 LYS A N     1 
ATOM   14485 C  CA    . LYS A 1 3480 ? 210.168 238.923 121.933 1.00 28.65 ? 3480 LYS A CA    1 
ATOM   14486 C  C     . LYS A 1 3480 ? 209.253 238.886 123.151 1.00 28.42 ? 3480 LYS A C     1 
ATOM   14487 O  O     . LYS A 1 3480 ? 209.060 239.904 123.825 1.00 28.57 ? 3480 LYS A O     1 
ATOM   14488 C  CB    . LYS A 1 3480 ? 209.361 239.121 120.648 1.00 27.94 ? 3480 LYS A CB    1 
ATOM   14489 C  CG    . LYS A 1 3480 ? 208.598 240.437 120.573 1.00 28.66 ? 3480 LYS A CG    1 
ATOM   14490 C  CD    . LYS A 1 3480 ? 207.128 240.264 120.932 1.00 32.26 ? 3480 LYS A CD    1 
ATOM   14491 C  CE    . LYS A 1 3480 ? 206.389 239.471 119.866 1.00 33.17 ? 3480 LYS A CE    1 
ATOM   14492 N  NZ    . LYS A 1 3480 ? 204.949 239.299 120.201 1.00 33.36 ? 3480 LYS A NZ    1 
ATOM   14493 N  N     . SER A 1 3481 ? 208.679 237.716 123.448 1.00 28.06 ? 3481 SER A N     1 
ATOM   14494 C  CA    . SER A 1 3481 ? 207.850 237.577 124.641 1.00 25.71 ? 3481 SER A CA    1 
ATOM   14495 C  C     . SER A 1 3481 ? 208.682 237.664 125.914 1.00 28.74 ? 3481 SER A C     1 
ATOM   14496 O  O     . SER A 1 3481 ? 208.163 238.056 126.966 1.00 28.66 ? 3481 SER A O     1 
ATOM   14497 C  CB    . SER A 1 3481 ? 207.084 236.256 124.593 1.00 26.97 ? 3481 SER A CB    1 
ATOM   14498 O  OG    . SER A 1 3481 ? 206.238 236.114 125.718 1.00 37.75 ? 3481 SER A OG    1 
ATOM   14499 N  N     . LEU A 1 3482 ? 209.960 237.299 125.845 1.00 29.42 ? 3482 LEU A N     1 
ATOM   14500 C  CA    . LEU A 1 3482 ? 210.866 237.385 126.981 1.00 27.33 ? 3482 LEU A CA    1 
ATOM   14501 C  C     . LEU A 1 3482 ? 211.639 238.695 127.019 1.00 30.64 ? 3482 LEU A C     1 
ATOM   14502 O  O     . LEU A 1 3482 ? 212.545 238.841 127.846 1.00 37.28 ? 3482 LEU A O     1 
ATOM   14503 C  CB    . LEU A 1 3482 ? 211.845 236.205 126.968 1.00 23.09 ? 3482 LEU A CB    1 
ATOM   14504 C  CG    . LEU A 1 3482 ? 211.266 234.828 127.295 1.00 24.50 ? 3482 LEU A CG    1 
ATOM   14505 C  CD1   . LEU A 1 3482 ? 212.375 233.803 127.459 1.00 22.60 ? 3482 LEU A CD1   1 
ATOM   14506 C  CD2   . LEU A 1 3482 ? 210.410 234.894 128.547 1.00 25.53 ? 3482 LEU A CD2   1 
ATOM   14507 N  N     . SER A 1 3483 ? 211.314 239.640 126.132 1.00 30.49 ? 3483 SER A N     1 
ATOM   14508 C  CA    . SER A 1 3483 ? 212.002 240.927 126.139 1.00 27.93 ? 3483 SER A CA    1 
ATOM   14509 C  C     . SER A 1 3483 ? 211.744 241.687 127.435 1.00 28.27 ? 3483 SER A C     1 
ATOM   14510 O  O     . SER A 1 3483 ? 212.668 242.271 128.013 1.00 33.80 ? 3483 SER A O     1 
ATOM   14511 C  CB    . SER A 1 3483 ? 211.565 241.759 124.933 1.00 32.76 ? 3483 SER A CB    1 
ATOM   14512 O  OG    . SER A 1 3483 ? 212.153 243.049 124.958 1.00 40.17 ? 3483 SER A OG    1 
ATOM   14513 N  N     . ALA A 1 3484 ? 210.493 241.691 127.905 1.00 30.75 ? 3484 ALA A N     1 
ATOM   14514 C  CA    . ALA A 1 3484 ? 210.172 242.400 129.139 1.00 25.80 ? 3484 ALA A CA    1 
ATOM   14515 C  C     . ALA A 1 3484 ? 210.869 241.772 130.338 1.00 29.95 ? 3484 ALA A C     1 
ATOM   14516 O  O     . ALA A 1 3484 ? 211.419 242.480 131.189 1.00 28.35 ? 3484 ALA A O     1 
ATOM   14517 C  CB    . ALA A 1 3484 ? 208.659 242.427 129.349 1.00 22.60 ? 3484 ALA A CB    1 
ATOM   14518 N  N     . GLU A 1 3485 ? 210.856 240.440 130.424 1.00 32.35 ? 3485 GLU A N     1 
ATOM   14519 C  CA    . GLU A 1 3485 ? 211.526 239.765 131.530 1.00 28.68 ? 3485 GLU A CA    1 
ATOM   14520 C  C     . GLU A 1 3485 ? 213.033 239.987 131.478 1.00 28.89 ? 3485 GLU A C     1 
ATOM   14521 O  O     . GLU A 1 3485 ? 213.674 240.169 132.518 1.00 28.27 ? 3485 GLU A O     1 
ATOM   14522 C  CB    . GLU A 1 3485 ? 211.194 238.274 131.511 1.00 27.57 ? 3485 GLU A CB    1 
ATOM   14523 C  CG    . GLU A 1 3485 ? 209.802 237.950 132.028 1.00 30.69 ? 3485 GLU A CG    1 
ATOM   14524 C  CD    . GLU A 1 3485 ? 208.717 238.209 130.996 1.00 36.35 ? 3485 GLU A CD    1 
ATOM   14525 O  OE1   . GLU A 1 3485 ? 209.055 238.542 129.839 1.00 36.88 ? 3485 GLU A OE1   1 
ATOM   14526 O  OE2   . GLU A 1 3485 ? 207.524 238.087 131.343 1.00 35.18 ? 3485 GLU A OE2   1 
ATOM   14527 N  N     . ARG A 1 3486 ? 213.614 239.978 130.275 1.00 27.05 ? 3486 ARG A N     1 
ATOM   14528 C  CA    . ARG A 1 3486 ? 215.041 240.255 130.148 1.00 29.73 ? 3486 ARG A CA    1 
ATOM   14529 C  C     . ARG A 1 3486 ? 215.366 241.676 130.597 1.00 31.16 ? 3486 ARG A C     1 
ATOM   14530 O  O     . ARG A 1 3486 ? 216.384 241.908 131.258 1.00 32.01 ? 3486 ARG A O     1 
ATOM   14531 C  CB    . ARG A 1 3486 ? 215.496 240.024 128.708 1.00 24.75 ? 3486 ARG A CB    1 
ATOM   14532 C  CG    . ARG A 1 3486 ? 216.999 240.126 128.506 1.00 24.37 ? 3486 ARG A CG    1 
ATOM   14533 C  CD    . ARG A 1 3486 ? 217.360 240.275 127.034 1.00 27.64 ? 3486 ARG A CD    1 
ATOM   14534 N  NE    . ARG A 1 3486 ? 216.513 241.241 126.342 1.00 35.17 ? 3486 ARG A NE    1 
ATOM   14535 C  CZ    . ARG A 1 3486 ? 216.518 242.548 126.568 1.00 31.82 ? 3486 ARG A CZ    1 
ATOM   14536 N  NH1   . ARG A 1 3486 ? 217.339 243.095 127.450 1.00 24.63 ? 3486 ARG A NH1   1 
ATOM   14537 N  NH2   . ARG A 1 3486 ? 215.683 243.327 125.887 1.00 35.25 ? 3486 ARG A NH2   1 
ATOM   14538 N  N     . GLU A 1 3487 ? 214.510 242.639 130.245 1.00 29.51 ? 3487 GLU A N     1 
ATOM   14539 C  CA    . GLU A 1 3487 ? 214.726 244.018 130.673 1.00 28.56 ? 3487 GLU A CA    1 
ATOM   14540 C  C     . GLU A 1 3487 ? 214.598 244.166 132.183 1.00 28.16 ? 3487 GLU A C     1 
ATOM   14541 O  O     . GLU A 1 3487 ? 215.402 244.859 132.814 1.00 29.76 ? 3487 GLU A O     1 
ATOM   14542 C  CB    . GLU A 1 3487 ? 213.741 244.948 129.961 1.00 28.33 ? 3487 GLU A CB    1 
ATOM   14543 C  CG    . GLU A 1 3487 ? 214.028 245.165 128.483 1.00 29.77 ? 3487 GLU A CG    1 
ATOM   14544 C  CD    . GLU A 1 3487 ? 215.199 246.102 128.238 1.00 37.18 ? 3487 GLU A CD    1 
ATOM   14545 O  OE1   . GLU A 1 3487 ? 216.340 245.750 128.605 1.00 35.45 ? 3487 GLU A OE1   1 
ATOM   14546 O  OE2   . GLU A 1 3487 ? 214.976 247.194 127.679 1.00 34.55 ? 3487 GLU A OE2   1 
ATOM   14547 N  N     . ARG A 1 3488 ? 213.586 243.529 132.779 1.00 26.63 ? 3488 ARG A N     1 
ATOM   14548 C  CA    . ARG A 1 3488 ? 213.369 243.656 134.218 1.00 21.04 ? 3488 ARG A CA    1 
ATOM   14549 C  C     . ARG A 1 3488 ? 214.516 243.043 135.011 1.00 26.56 ? 3488 ARG A C     1 
ATOM   14550 O  O     . ARG A 1 3488 ? 214.975 243.625 136.002 1.00 32.49 ? 3488 ARG A O     1 
ATOM   14551 C  CB    . ARG A 1 3488 ? 212.041 243.009 134.604 1.00 22.94 ? 3488 ARG A CB    1 
ATOM   14552 C  CG    . ARG A 1 3488 ? 211.706 243.106 136.081 1.00 23.86 ? 3488 ARG A CG    1 
ATOM   14553 C  CD    . ARG A 1 3488 ? 210.796 241.969 136.518 1.00 24.65 ? 3488 ARG A CD    1 
ATOM   14554 N  NE    . ARG A 1 3488 ? 209.733 241.713 135.554 1.00 30.03 ? 3488 ARG A NE    1 
ATOM   14555 C  CZ    . ARG A 1 3488 ? 209.624 240.604 134.834 1.00 30.94 ? 3488 ARG A CZ    1 
ATOM   14556 N  NH1   . ARG A 1 3488 ? 210.504 239.621 134.940 1.00 30.97 ? 3488 ARG A NH1   1 
ATOM   14557 N  NH2   . ARG A 1 3488 ? 208.608 240.480 133.985 1.00 34.12 ? 3488 ARG A NH2   1 
ATOM   14558 N  N     . TRP A 1 3489 ? 214.993 241.870 134.591 1.00 24.23 ? 3489 TRP A N     1 
ATOM   14559 C  CA    . TRP A 1 3489 ? 216.091 241.224 135.299 1.00 24.49 ? 3489 TRP A CA    1 
ATOM   14560 C  C     . TRP A 1 3489 ? 217.384 242.018 135.180 1.00 31.24 ? 3489 TRP A C     1 
ATOM   14561 O  O     . TRP A 1 3489 ? 218.204 242.007 136.105 1.00 34.34 ? 3489 TRP A O     1 
ATOM   14562 C  CB    . TRP A 1 3489 ? 216.286 239.803 134.775 1.00 24.23 ? 3489 TRP A CB    1 
ATOM   14563 C  CG    . TRP A 1 3489 ? 215.082 238.933 134.955 1.00 23.77 ? 3489 TRP A CG    1 
ATOM   14564 C  CD1   . TRP A 1 3489 ? 214.070 239.109 135.853 1.00 22.72 ? 3489 TRP A CD1   1 
ATOM   14565 C  CD2   . TRP A 1 3489 ? 214.763 237.748 134.220 1.00 24.72 ? 3489 TRP A CD2   1 
ATOM   14566 N  NE1   . TRP A 1 3489 ? 213.141 238.106 135.722 1.00 25.11 ? 3489 TRP A NE1   1 
ATOM   14567 C  CE2   . TRP A 1 3489 ? 213.544 237.257 134.725 1.00 25.46 ? 3489 TRP A CE2   1 
ATOM   14568 C  CE3   . TRP A 1 3489 ? 215.391 237.054 133.181 1.00 22.02 ? 3489 TRP A CE3   1 
ATOM   14569 C  CZ2   . TRP A 1 3489 ? 212.939 236.107 134.227 1.00 22.95 ? 3489 TRP A CZ2   1 
ATOM   14570 C  CZ3   . TRP A 1 3489 ? 214.792 235.913 132.691 1.00 25.96 ? 3489 TRP A CZ3   1 
ATOM   14571 C  CH2   . TRP A 1 3489 ? 213.580 235.448 133.213 1.00 31.56 ? 3489 TRP A CH2   1 
ATOM   14572 N  N     . GLU A 1 3490 ? 217.589 242.703 134.053 1.00 27.80 ? 3490 GLU A N     1 
ATOM   14573 C  CA    . GLU A 1 3490 ? 218.784 243.527 133.895 1.00 28.05 ? 3490 GLU A CA    1 
ATOM   14574 C  C     . GLU A 1 3490 ? 218.769 244.715 134.848 1.00 29.33 ? 3490 GLU A C     1 
ATOM   14575 O  O     . GLU A 1 3490 ? 219.810 245.073 135.415 1.00 30.74 ? 3490 GLU A O     1 
ATOM   14576 C  CB    . GLU A 1 3490 ? 218.908 244.000 132.447 1.00 23.57 ? 3490 GLU A CB    1 
ATOM   14577 C  CG    . GLU A 1 3490 ? 219.407 242.931 131.493 1.00 28.75 ? 3490 GLU A CG    1 
ATOM   14578 C  CD    . GLU A 1 3490 ? 219.150 243.281 130.041 1.00 37.07 ? 3490 GLU A CD    1 
ATOM   14579 O  OE1   . GLU A 1 3490 ? 218.565 244.353 129.781 1.00 37.36 ? 3490 GLU A OE1   1 
ATOM   14580 O  OE2   . GLU A 1 3490 ? 219.526 242.480 129.159 1.00 32.44 ? 3490 GLU A OE2   1 
ATOM   14581 N  N     . LYS A 1 3491 ? 217.606 245.344 135.028 1.00 27.27 ? 3491 LYS A N     1 
ATOM   14582 C  CA    . LYS A 1 3491 ? 217.512 246.501 135.915 1.00 27.73 ? 3491 LYS A CA    1 
ATOM   14583 C  C     . LYS A 1 3491 ? 217.836 246.123 137.355 1.00 27.59 ? 3491 LYS A C     1 
ATOM   14584 O  O     . LYS A 1 3491 ? 218.587 246.827 138.038 1.00 32.90 ? 3491 LYS A O     1 
ATOM   14585 C  CB    . LYS A 1 3491 ? 216.116 247.119 135.824 1.00 30.51 ? 3491 LYS A CB    1 
ATOM   14586 C  CG    . LYS A 1 3491 ? 215.718 247.594 134.435 1.00 29.85 ? 3491 LYS A CG    1 
ATOM   14587 C  CD    . LYS A 1 3491 ? 216.768 248.519 133.841 1.00 30.69 ? 3491 LYS A CD    1 
ATOM   14588 C  CE    . LYS A 1 3491 ? 216.410 248.913 132.415 1.00 30.56 ? 3491 LYS A CE    1 
ATOM   14589 N  NZ    . LYS A 1 3491 ? 216.272 247.727 131.525 1.00 31.24 ? 3491 LYS A NZ    1 
ATOM   14590 N  N     . THR A 1 3492 ? 217.280 245.007 137.834 1.00 29.66 ? 3492 THR A N     1 
ATOM   14591 C  CA    . THR A 1 3492 ? 217.537 244.583 139.208 1.00 28.07 ? 3492 THR A CA    1 
ATOM   14592 C  C     . THR A 1 3492 ? 218.998 244.202 139.404 1.00 28.98 ? 3492 THR A C     1 
ATOM   14593 O  O     . THR A 1 3492 ? 219.582 244.481 140.459 1.00 32.25 ? 3492 THR A O     1 
ATOM   14594 C  CB    . THR A 1 3492 ? 216.619 243.417 139.579 1.00 26.20 ? 3492 THR A CB    1 
ATOM   14595 O  OG1   . THR A 1 3492 ? 215.253 243.821 139.432 1.00 32.22 ? 3492 THR A OG1   1 
ATOM   14596 C  CG2   . THR A 1 3492 ? 216.854 242.990 141.019 1.00 22.73 ? 3492 THR A CG2   1 
ATOM   14597 N  N     . SER A 1 3493 ? 219.608 243.567 138.399 1.00 28.13 ? 3493 SER A N     1 
ATOM   14598 C  CA    . SER A 1 3493 ? 221.013 243.186 138.505 1.00 28.03 ? 3493 SER A CA    1 
ATOM   14599 C  C     . SER A 1 3493 ? 221.902 244.406 138.700 1.00 34.05 ? 3493 SER A C     1 
ATOM   14600 O  O     . SER A 1 3493 ? 222.894 244.350 139.435 1.00 36.26 ? 3493 SER A O     1 
ATOM   14601 C  CB    . SER A 1 3493 ? 221.439 242.404 137.265 1.00 25.99 ? 3493 SER A CB    1 
ATOM   14602 O  OG    . SER A 1 3493 ? 222.822 242.103 137.303 1.00 29.50 ? 3493 SER A OG    1 
ATOM   14603 N  N     . GLU A 1 3494 ? 221.570 245.519 138.039 1.00 28.79 ? 3494 GLU A N     1 
ATOM   14604 C  CA    . GLU A 1 3494 ? 222.318 246.752 138.254 1.00 30.53 ? 3494 GLU A CA    1 
ATOM   14605 C  C     . GLU A 1 3494 ? 222.144 247.262 139.680 1.00 33.58 ? 3494 GLU A C     1 
ATOM   14606 O  O     . GLU A 1 3494 ? 223.112 247.702 140.310 1.00 34.47 ? 3494 GLU A O     1 
ATOM   14607 C  CB    . GLU A 1 3494 ? 221.881 247.814 137.246 1.00 29.47 ? 3494 GLU A CB    1 
ATOM   14608 C  CG    . GLU A 1 3494 ? 222.463 249.206 137.486 1.00 31.72 ? 3494 GLU A CG    1 
ATOM   14609 C  CD    . GLU A 1 3494 ? 223.962 249.279 137.255 1.00 38.78 ? 3494 GLU A CD    1 
ATOM   14610 O  OE1   . GLU A 1 3494 ? 224.730 248.697 138.051 1.00 40.53 ? 3494 GLU A OE1   1 
ATOM   14611 O  OE2   . GLU A 1 3494 ? 224.378 249.923 136.269 1.00 38.89 ? 3494 GLU A OE2   1 
ATOM   14612 N  N     . THR A 1 3495 ? 220.924 247.200 140.207 1.00 29.65 ? 3495 THR A N     1 
ATOM   14613 C  CA    . THR A 1 3495 ? 220.635 247.648 141.569 1.00 30.46 ? 3495 THR A CA    1 
ATOM   14614 C  C     . THR A 1 3495 ? 221.126 246.680 142.634 1.00 27.70 ? 3495 THR A C     1 
ATOM   14615 O  O     . THR A 1 3495 ? 220.796 246.878 143.810 1.00 28.72 ? 3495 THR A O     1 
ATOM   14616 C  CB    . THR A 1 3495 ? 219.133 247.878 141.744 1.00 29.03 ? 3495 THR A CB    1 
ATOM   14617 O  OG1   . THR A 1 3495 ? 218.456 246.615 141.787 1.00 26.50 ? 3495 THR A OG1   1 
ATOM   14618 C  CG2   . THR A 1 3495 ? 218.585 248.708 140.595 1.00 23.62 ? 3495 THR A CG2   1 
ATOM   14619 N  N     . PHE A 1 3496 ? 221.883 245.646 142.260 1.00 26.75 ? 3496 PHE A N     1 
ATOM   14620 C  CA    . PHE A 1 3496 ? 222.405 244.710 143.250 1.00 21.44 ? 3496 PHE A CA    1 
ATOM   14621 C  C     . PHE A 1 3496 ? 223.341 245.402 144.229 1.00 24.49 ? 3496 PHE A C     1 
ATOM   14622 O  O     . PHE A 1 3496 ? 223.280 245.154 145.439 1.00 29.80 ? 3496 PHE A O     1 
ATOM   14623 C  CB    . PHE A 1 3496 ? 223.126 243.560 142.552 1.00 21.65 ? 3496 PHE A CB    1 
ATOM   14624 C  CG    . PHE A 1 3496 ? 223.724 242.562 143.496 1.00 22.53 ? 3496 PHE A CG    1 
ATOM   14625 C  CD1   . PHE A 1 3496 ? 222.960 241.999 144.506 1.00 25.19 ? 3496 PHE A CD1   1 
ATOM   14626 C  CD2   . PHE A 1 3496 ? 225.057 242.204 143.392 1.00 23.14 ? 3496 PHE A CD2   1 
ATOM   14627 C  CE1   . PHE A 1 3496 ? 223.513 241.086 145.380 1.00 26.34 ? 3496 PHE A CE1   1 
ATOM   14628 C  CE2   . PHE A 1 3496 ? 225.611 241.294 144.264 1.00 21.22 ? 3496 PHE A CE2   1 
ATOM   14629 C  CZ    . PHE A 1 3496 ? 224.840 240.734 145.259 1.00 21.00 ? 3496 PHE A CZ    1 
ATOM   14630 N  N     . LYS A 1 3497 ? 224.223 246.271 143.725 1.00 24.90 ? 3497 LYS A N     1 
ATOM   14631 C  CA    . LYS A 1 3497 ? 225.201 246.923 144.592 1.00 25.50 ? 3497 LYS A CA    1 
ATOM   14632 C  C     . LYS A 1 3497 ? 224.526 247.838 145.606 1.00 21.05 ? 3497 LYS A C     1 
ATOM   14633 O  O     . LYS A 1 3497 ? 224.924 247.871 146.777 1.00 22.07 ? 3497 LYS A O     1 
ATOM   14634 C  CB    . LYS A 1 3497 ? 226.208 247.704 143.751 1.00 26.09 ? 3497 LYS A CB    1 
ATOM   14635 C  CG    . LYS A 1 3497 ? 226.870 246.884 142.657 1.00 31.26 ? 3497 LYS A CG    1 
ATOM   14636 C  CD    . LYS A 1 3497 ? 227.984 247.665 141.981 1.00 32.18 ? 3497 LYS A CD    1 
ATOM   14637 C  CE    . LYS A 1 3497 ? 229.035 248.103 142.987 1.00 35.32 ? 3497 LYS A CE    1 
ATOM   14638 N  NZ    . LYS A 1 3497 ? 229.585 246.949 143.750 1.00 35.53 ? 3497 LYS A NZ    1 
ATOM   14639 N  N     . ASN A 1 3498 ? 223.509 248.588 145.175 1.00 20.68 ? 3498 ASN A N     1 
ATOM   14640 C  CA    . ASN A 1 3498 ? 222.831 249.508 146.084 1.00 20.09 ? 3498 ASN A CA    1 
ATOM   14641 C  C     . ASN A 1 3498 ? 222.176 248.759 147.238 1.00 23.07 ? 3498 ASN A C     1 
ATOM   14642 O  O     . ASN A 1 3498 ? 222.276 249.178 148.397 1.00 19.93 ? 3498 ASN A O     1 
ATOM   14643 C  CB    . ASN A 1 3498 ? 221.797 250.329 145.314 1.00 20.30 ? 3498 ASN A CB    1 
ATOM   14644 C  CG    . ASN A 1 3498 ? 221.205 251.460 146.139 1.00 26.38 ? 3498 ASN A CG    1 
ATOM   14645 O  OD1   . ASN A 1 3498 ? 221.539 251.639 147.309 1.00 36.95 ? 3498 ASN A OD1   1 
ATOM   14646 N  ND2   . ASN A 1 3498 ? 220.316 252.230 145.525 1.00 27.08 ? 3498 ASN A ND2   1 
ATOM   14647 N  N     . GLN A 1 3499 ? 221.505 247.644 146.940 1.00 20.11 ? 3499 GLN A N     1 
ATOM   14648 C  CA    . GLN A 1 3499 ? 220.861 246.871 147.997 1.00 18.43 ? 3499 GLN A CA    1 
ATOM   14649 C  C     . GLN A 1 3499 ? 221.888 246.269 148.950 1.00 20.49 ? 3499 GLN A C     1 
ATOM   14650 O  O     . GLN A 1 3499 ? 221.675 246.246 150.168 1.00 23.21 ? 3499 GLN A O     1 
ATOM   14651 C  CB    . GLN A 1 3499 ? 219.976 245.785 147.391 1.00 18.55 ? 3499 GLN A CB    1 
ATOM   14652 C  CG    . GLN A 1 3499 ? 218.931 246.305 146.428 1.00 23.34 ? 3499 GLN A CG    1 
ATOM   14653 C  CD    . GLN A 1 3499 ? 218.040 245.205 145.891 1.00 24.81 ? 3499 GLN A CD    1 
ATOM   14654 O  OE1   . GLN A 1 3499 ? 218.051 244.909 144.697 1.00 29.63 ? 3499 GLN A OE1   1 
ATOM   14655 N  NE2   . GLN A 1 3499 ? 217.261 244.592 146.775 1.00 28.66 ? 3499 GLN A NE2   1 
ATOM   14656 N  N     . MET A 1 3500 ? 223.011 245.777 148.416 1.00 17.12 ? 3500 MET A N     1 
ATOM   14657 C  CA    . MET A 1 3500 ? 224.092 245.299 149.275 1.00 16.29 ? 3500 MET A CA    1 
ATOM   14658 C  C     . MET A 1 3500 ? 224.621 246.399 150.185 1.00 16.97 ? 3500 MET A C     1 
ATOM   14659 O  O     . MET A 1 3500 ? 225.100 246.113 151.287 1.00 21.36 ? 3500 MET A O     1 
ATOM   14660 C  CB    . MET A 1 3500 ? 225.233 244.731 148.429 1.00 18.27 ? 3500 MET A CB    1 
ATOM   14661 C  CG    . MET A 1 3500 ? 224.898 243.474 147.645 1.00 22.65 ? 3500 MET A CG    1 
ATOM   14662 S  SD    . MET A 1 3500 ? 224.431 242.100 148.710 1.00 31.34 ? 3500 MET A SD    1 
ATOM   14663 C  CE    . MET A 1 3500 ? 226.000 241.736 149.491 1.00 26.36 ? 3500 MET A CE    1 
ATOM   14664 N  N     . SER A 1 3501 ? 224.543 247.655 149.750 1.00 14.85 ? 3501 SER A N     1 
ATOM   14665 C  CA    . SER A 1 3501 ? 225.076 248.775 150.510 1.00 12.80 ? 3501 SER A CA    1 
ATOM   14666 C  C     . SER A 1 3501 ? 224.131 249.283 151.591 1.00 11.71 ? 3501 SER A C     1 
ATOM   14667 O  O     . SER A 1 3501 ? 224.546 250.113 152.408 1.00 23.94 ? 3501 SER A O     1 
ATOM   14668 C  CB    . SER A 1 3501 ? 225.431 249.930 149.568 1.00 17.13 ? 3501 SER A CB    1 
ATOM   14669 O  OG    . SER A 1 3501 ? 224.266 250.556 149.060 1.00 26.70 ? 3501 SER A OG    1 
ATOM   14670 N  N     . THR A 1 3502 ? 222.883 248.818 151.627 1.00 9.75  ? 3502 THR A N     1 
ATOM   14671 C  CA    . THR A 1 3502 ? 221.925 249.275 152.623 1.00 10.23 ? 3502 THR A CA    1 
ATOM   14672 C  C     . THR A 1 3502 ? 221.427 248.168 153.541 1.00 9.97  ? 3502 THR A C     1 
ATOM   14673 O  O     . THR A 1 3502 ? 220.659 248.456 154.464 1.00 11.49 ? 3502 THR A O     1 
ATOM   14674 C  CB    . THR A 1 3502 ? 220.716 249.943 151.949 1.00 11.86 ? 3502 THR A CB    1 
ATOM   14675 O  OG1   . THR A 1 3502 ? 220.208 249.095 150.913 1.00 12.07 ? 3502 THR A OG1   1 
ATOM   14676 C  CG2   . THR A 1 3502 ? 221.105 251.292 151.358 1.00 11.29 ? 3502 THR A CG2   1 
ATOM   14677 N  N     . ILE A 1 3503 ? 221.834 246.915 153.318 1.00 7.97  ? 3503 ILE A N     1 
ATOM   14678 C  CA    . ILE A 1 3503 ? 221.377 245.822 154.172 1.00 8.20  ? 3503 ILE A CA    1 
ATOM   14679 C  C     . ILE A 1 3503 ? 221.848 246.031 155.605 1.00 5.74  ? 3503 ILE A C     1 
ATOM   14680 O  O     . ILE A 1 3503 ? 221.108 245.773 156.561 1.00 8.52  ? 3503 ILE A O     1 
ATOM   14681 C  CB    . ILE A 1 3503 ? 221.844 244.467 153.605 1.00 11.20 ? 3503 ILE A CB    1 
ATOM   14682 C  CG1   . ILE A 1 3503 ? 220.980 244.061 152.413 1.00 9.74  ? 3503 ILE A CG1   1 
ATOM   14683 C  CG2   . ILE A 1 3503 ? 221.788 243.383 154.671 1.00 7.57  ? 3503 ILE A CG2   1 
ATOM   14684 C  CD1   . ILE A 1 3503 ? 221.409 242.765 151.765 1.00 16.09 ? 3503 ILE A CD1   1 
ATOM   14685 N  N     . ALA A 1 3504 ? 223.080 246.521 155.775 1.00 4.84  ? 3504 ALA A N     1 
ATOM   14686 C  CA    . ALA A 1 3504 ? 223.610 246.752 157.114 1.00 4.75  ? 3504 ALA A CA    1 
ATOM   14687 C  C     . ALA A 1 3504 ? 222.742 247.732 157.893 1.00 3.18  ? 3504 ALA A C     1 
ATOM   14688 O  O     . ALA A 1 3504 ? 222.475 247.527 159.081 1.00 2.73  ? 3504 ALA A O     1 
ATOM   14689 C  CB    . ALA A 1 3504 ? 225.048 247.256 157.028 1.00 3.31  ? 3504 ALA A CB    1 
ATOM   14690 N  N     . GLY A 1 3505 ? 222.293 248.802 157.241 1.00 4.17  ? 3505 GLY A N     1 
ATOM   14691 C  CA    . GLY A 1 3505 ? 221.410 249.759 157.877 1.00 3.66  ? 3505 GLY A CA    1 
ATOM   14692 C  C     . GLY A 1 3505 ? 219.961 249.321 157.937 1.00 2.55  ? 3505 GLY A C     1 
ATOM   14693 O  O     . GLY A 1 3505 ? 219.277 249.562 158.937 1.00 2.02  ? 3505 GLY A O     1 
ATOM   14694 N  N     . ASP A 1 3506 ? 219.475 248.684 156.869 1.00 2.36  ? 3506 ASP A N     1 
ATOM   14695 C  CA    . ASP A 1 3506 ? 218.079 248.254 156.834 1.00 2.70  ? 3506 ASP A CA    1 
ATOM   14696 C  C     . ASP A 1 3506 ? 217.795 247.194 157.888 1.00 1.95  ? 3506 ASP A C     1 
ATOM   14697 O  O     . ASP A 1 3506 ? 216.769 247.250 158.575 1.00 0.80  ? 3506 ASP A O     1 
ATOM   14698 C  CB    . ASP A 1 3506 ? 217.724 247.730 155.443 1.00 4.46  ? 3506 ASP A CB    1 
ATOM   14699 C  CG    . ASP A 1 3506 ? 217.453 248.843 154.453 1.00 11.51 ? 3506 ASP A CG    1 
ATOM   14700 O  OD1   . ASP A 1 3506 ? 217.248 249.993 154.889 1.00 13.23 ? 3506 ASP A OD1   1 
ATOM   14701 O  OD2   . ASP A 1 3506 ? 217.453 248.568 153.234 1.00 15.22 ? 3506 ASP A OD2   1 
ATOM   14702 N  N     . CYS A 1 3507 ? 218.694 246.217 158.031 1.00 3.24  ? 3507 CYS A N     1 
ATOM   14703 C  CA    . CYS A 1 3507 ? 218.491 245.165 159.017 1.00 1.52  ? 3507 CYS A CA    1 
ATOM   14704 C  C     . CYS A 1 3507 ? 218.627 245.693 160.440 1.00 1.85  ? 3507 CYS A C     1 
ATOM   14705 O  O     . CYS A 1 3507 ? 217.944 245.207 161.345 1.00 1.56  ? 3507 CYS A O     1 
ATOM   14706 C  CB    . CYS A 1 3507 ? 219.472 244.019 158.770 1.00 2.29  ? 3507 CYS A CB    1 
ATOM   14707 S  SG    . CYS A 1 3507 ? 219.143 243.087 157.263 1.00 6.53  ? 3507 CYS A SG    1 
ATOM   14708 N  N     . LEU A 1 3508 ? 219.498 246.683 160.653 1.00 1.10  ? 3508 LEU A N     1 
ATOM   14709 C  CA    . LEU A 1 3508 ? 219.636 247.283 161.975 1.00 0.59  ? 3508 LEU A CA    1 
ATOM   14710 C  C     . LEU A 1 3508 ? 218.330 247.926 162.424 1.00 0.54  ? 3508 LEU A C     1 
ATOM   14711 O  O     . LEU A 1 3508 ? 217.894 247.742 163.567 1.00 0.52  ? 3508 LEU A O     1 
ATOM   14712 C  CB    . LEU A 1 3508 ? 220.769 248.310 161.957 1.00 1.21  ? 3508 LEU A CB    1 
ATOM   14713 C  CG    . LEU A 1 3508 ? 221.447 248.712 163.268 1.00 0.78  ? 3508 LEU A CG    1 
ATOM   14714 C  CD1   . LEU A 1 3508 ? 222.831 249.252 162.972 1.00 1.11  ? 3508 LEU A CD1   1 
ATOM   14715 C  CD2   . LEU A 1 3508 ? 220.631 249.744 164.032 1.00 0.50  ? 3508 LEU A CD2   1 
ATOM   14716 N  N     . LEU A 1 3509 ? 217.690 248.685 161.534 1.00 0.54  ? 3509 LEU A N     1 
ATOM   14717 C  CA    . LEU A 1 3509 ? 216.406 249.298 161.864 1.00 0.34  ? 3509 LEU A CA    1 
ATOM   14718 C  C     . LEU A 1 3509 ? 215.323 248.244 162.054 1.00 0.34  ? 3509 LEU A C     1 
ATOM   14719 O  O     . LEU A 1 3509 ? 214.516 248.334 162.987 1.00 0.12  ? 3509 LEU A O     1 
ATOM   14720 C  CB    . LEU A 1 3509 ? 216.001 250.283 160.770 1.00 0.57  ? 3509 LEU A CB    1 
ATOM   14721 C  CG    . LEU A 1 3509 ? 216.890 251.507 160.565 1.00 1.28  ? 3509 LEU A CG    1 
ATOM   14722 C  CD1   . LEU A 1 3509 ? 216.455 252.274 159.326 1.00 1.03  ? 3509 LEU A CD1   1 
ATOM   14723 C  CD2   . LEU A 1 3509 ? 216.858 252.399 161.789 1.00 0.67  ? 3509 LEU A CD2   1 
ATOM   14724 N  N     . SER A 1 3510 ? 215.291 247.242 161.176 1.00 0.86  ? 3510 SER A N     1 
ATOM   14725 C  CA    . SER A 1 3510 ? 214.279 246.195 161.270 1.00 0.32  ? 3510 SER A CA    1 
ATOM   14726 C  C     . SER A 1 3510 ? 214.443 245.376 162.543 1.00 0.28  ? 3510 SER A C     1 
ATOM   14727 O  O     . SER A 1 3510 ? 213.457 245.067 163.220 1.00 0.25  ? 3510 SER A O     1 
ATOM   14728 C  CB    . SER A 1 3510 ? 214.349 245.296 160.038 1.00 0.57  ? 3510 SER A CB    1 
ATOM   14729 O  OG    . SER A 1 3510 ? 214.234 246.057 158.851 1.00 2.09  ? 3510 SER A OG    1 
ATOM   14730 N  N     . ALA A 1 3511 ? 215.682 245.021 162.883 1.00 0.67  ? 3511 ALA A N     1 
ATOM   14731 C  CA    . ALA A 1 3511 ? 215.926 244.238 164.091 1.00 0.21  ? 3511 ALA A CA    1 
ATOM   14732 C  C     . ALA A 1 3511 ? 215.536 245.014 165.340 1.00 0.15  ? 3511 ALA A C     1 
ATOM   14733 O  O     . ALA A 1 3511 ? 214.966 244.447 166.278 1.00 0.61  ? 3511 ALA A O     1 
ATOM   14734 C  CB    . ALA A 1 3511 ? 217.391 243.818 164.155 1.00 0.22  ? 3511 ALA A CB    1 
ATOM   14735 N  N     . ALA A 1 3512 ? 215.840 246.313 165.372 1.00 0.17  ? 3512 ALA A N     1 
ATOM   14736 C  CA    . ALA A 1 3512 ? 215.478 247.132 166.523 1.00 0.05  ? 3512 ALA A CA    1 
ATOM   14737 C  C     . ALA A 1 3512 ? 213.969 247.205 166.691 1.00 0.08  ? 3512 ALA A C     1 
ATOM   14738 O  O     . ALA A 1 3512 ? 213.460 247.191 167.818 1.00 0.10  ? 3512 ALA A O     1 
ATOM   14739 C  CB    . ALA A 1 3512 ? 216.074 248.531 166.380 1.00 0.06  ? 3512 ALA A CB    1 
ATOM   14740 N  N     . PHE A 1 3513 ? 213.234 247.287 165.581 1.00 0.10  ? 3513 PHE A N     1 
ATOM   14741 C  CA    . PHE A 1 3513 ? 211.780 247.345 165.654 1.00 0.12  ? 3513 PHE A CA    1 
ATOM   14742 C  C     . PHE A 1 3513 ? 211.199 246.060 166.233 1.00 0.11  ? 3513 PHE A C     1 
ATOM   14743 O  O     . PHE A 1 3513 ? 210.254 246.105 167.027 1.00 0.14  ? 3513 PHE A O     1 
ATOM   14744 C  CB    . PHE A 1 3513 ? 211.203 247.632 164.267 1.00 0.10  ? 3513 PHE A CB    1 
ATOM   14745 C  CG    . PHE A 1 3513 ? 209.789 248.122 164.291 1.00 0.19  ? 3513 PHE A CG    1 
ATOM   14746 C  CD1   . PHE A 1 3513 ? 209.516 249.474 164.392 1.00 0.37  ? 3513 PHE A CD1   1 
ATOM   14747 C  CD2   . PHE A 1 3513 ? 208.733 247.235 164.208 1.00 0.27  ? 3513 PHE A CD2   1 
ATOM   14748 C  CE1   . PHE A 1 3513 ? 208.216 249.929 164.419 1.00 0.48  ? 3513 PHE A CE1   1 
ATOM   14749 C  CE2   . PHE A 1 3513 ? 207.433 247.688 164.234 1.00 0.46  ? 3513 PHE A CE2   1 
ATOM   14750 C  CZ    . PHE A 1 3513 ? 207.176 249.036 164.337 1.00 0.59  ? 3513 PHE A CZ    1 
ATOM   14751 N  N     . ILE A 1 3514 ? 211.750 244.908 165.849 1.00 0.13  ? 3514 ILE A N     1 
ATOM   14752 C  CA    . ILE A 1 3514 ? 211.257 243.636 166.368 1.00 0.25  ? 3514 ILE A CA    1 
ATOM   14753 C  C     . ILE A 1 3514 ? 211.548 243.497 167.857 1.00 0.22  ? 3514 ILE A C     1 
ATOM   14754 O  O     . ILE A 1 3514 ? 210.740 242.936 168.606 1.00 0.46  ? 3514 ILE A O     1 
ATOM   14755 C  CB    . ILE A 1 3514 ? 211.858 242.466 165.566 1.00 0.52  ? 3514 ILE A CB    1 
ATOM   14756 C  CG1   . ILE A 1 3514 ? 211.538 242.622 164.081 1.00 0.45  ? 3514 ILE A CG1   1 
ATOM   14757 C  CG2   . ILE A 1 3514 ? 211.332 241.137 166.078 1.00 0.72  ? 3514 ILE A CG2   1 
ATOM   14758 C  CD1   . ILE A 1 3514 ? 210.062 242.687 163.792 1.00 0.89  ? 3514 ILE A CD1   1 
ATOM   14759 N  N     . ALA A 1 3515 ? 212.687 244.006 168.318 1.00 0.12  ? 3515 ALA A N     1 
ATOM   14760 C  CA    . ALA A 1 3515 ? 213.107 243.804 169.698 1.00 0.14  ? 3515 ALA A CA    1 
ATOM   14761 C  C     . ALA A 1 3515 ? 212.511 244.802 170.680 1.00 0.08  ? 3515 ALA A C     1 
ATOM   14762 O  O     . ALA A 1 3515 ? 212.388 244.480 171.865 1.00 0.07  ? 3515 ALA A O     1 
ATOM   14763 C  CB    . ALA A 1 3515 ? 214.633 243.856 169.796 1.00 0.14  ? 3515 ALA A CB    1 
ATOM   14764 N  N     . TYR A 1 3516 ? 212.136 245.989 170.233 1.00 0.15  ? 3516 TYR A N     1 
ATOM   14765 C  CA    . TYR A 1 3516 ? 211.747 247.024 171.186 1.00 0.11  ? 3516 TYR A CA    1 
ATOM   14766 C  C     . TYR A 1 3516 ? 210.344 247.570 170.976 1.00 0.09  ? 3516 TYR A C     1 
ATOM   14767 O  O     . TYR A 1 3516 ? 209.684 247.922 171.954 1.00 0.73  ? 3516 TYR A O     1 
ATOM   14768 C  CB    . TYR A 1 3516 ? 212.739 248.191 171.135 1.00 0.06  ? 3516 TYR A CB    1 
ATOM   14769 C  CG    . TYR A 1 3516 ? 214.150 247.856 171.541 1.00 0.03  ? 3516 TYR A CG    1 
ATOM   14770 C  CD1   . TYR A 1 3516 ? 214.475 247.645 172.871 1.00 0.05  ? 3516 TYR A CD1   1 
ATOM   14771 C  CD2   . TYR A 1 3516 ? 215.164 247.781 170.600 1.00 0.03  ? 3516 TYR A CD2   1 
ATOM   14772 C  CE1   . TYR A 1 3516 ? 215.768 247.360 173.249 1.00 0.04  ? 3516 TYR A CE1   1 
ATOM   14773 C  CE2   . TYR A 1 3516 ? 216.459 247.493 170.972 1.00 0.03  ? 3516 TYR A CE2   1 
ATOM   14774 C  CZ    . TYR A 1 3516 ? 216.754 247.281 172.297 1.00 0.03  ? 3516 TYR A CZ    1 
ATOM   14775 O  OH    . TYR A 1 3516 ? 218.038 246.990 172.676 1.00 0.04  ? 3516 TYR A OH    1 
ATOM   14776 N  N     . ALA A 1 3517 ? 209.873 247.652 169.735 1.00 0.11  ? 3517 ALA A N     1 
ATOM   14777 C  CA    . ALA A 1 3517 ? 208.689 248.441 169.422 1.00 0.25  ? 3517 ALA A CA    1 
ATOM   14778 C  C     . ALA A 1 3517 ? 207.376 247.753 169.770 1.00 0.15  ? 3517 ALA A C     1 
ATOM   14779 O  O     . ALA A 1 3517 ? 206.325 248.388 169.662 1.00 0.89  ? 3517 ALA A O     1 
ATOM   14780 C  CB    . ALA A 1 3517 ? 208.688 248.809 167.936 1.00 0.21  ? 3517 ALA A CB    1 
ATOM   14781 N  N     . GLY A 1 3518 ? 207.409 246.490 170.192 1.00 0.21  ? 3518 GLY A N     1 
ATOM   14782 C  CA    . GLY A 1 3518 ? 206.181 245.715 170.279 1.00 0.18  ? 3518 GLY A CA    1 
ATOM   14783 C  C     . GLY A 1 3518 ? 205.180 246.262 171.277 1.00 0.23  ? 3518 GLY A C     1 
ATOM   14784 O  O     . GLY A 1 3518 ? 203.975 246.270 171.017 1.00 0.29  ? 3518 GLY A O     1 
ATOM   14785 N  N     . TYR A 1 3519 ? 205.658 246.724 172.433 1.00 0.44  ? 3519 TYR A N     1 
ATOM   14786 C  CA    . TYR A 1 3519 ? 204.740 247.168 173.475 1.00 0.30  ? 3519 TYR A CA    1 
ATOM   14787 C  C     . TYR A 1 3519 ? 204.080 248.499 173.140 1.00 0.40  ? 3519 TYR A C     1 
ATOM   14788 O  O     . TYR A 1 3519 ? 202.984 248.785 173.633 1.00 1.11  ? 3519 TYR A O     1 
ATOM   14789 C  CB    . TYR A 1 3519 ? 205.465 247.267 174.817 1.00 0.63  ? 3519 TYR A CB    1 
ATOM   14790 C  CG    . TYR A 1 3519 ? 204.543 247.658 175.942 1.00 1.45  ? 3519 TYR A CG    1 
ATOM   14791 C  CD1   . TYR A 1 3519 ? 203.606 246.763 176.431 1.00 1.19  ? 3519 TYR A CD1   1 
ATOM   14792 C  CD2   . TYR A 1 3519 ? 204.591 248.929 176.498 1.00 1.96  ? 3519 TYR A CD2   1 
ATOM   14793 C  CE1   . TYR A 1 3519 ? 202.749 247.115 177.447 1.00 4.22  ? 3519 TYR A CE1   1 
ATOM   14794 C  CE2   . TYR A 1 3519 ? 203.739 249.290 177.518 1.00 2.82  ? 3519 TYR A CE2   1 
ATOM   14795 C  CZ    . TYR A 1 3519 ? 202.819 248.377 177.989 1.00 4.38  ? 3519 TYR A CZ    1 
ATOM   14796 O  OH    . TYR A 1 3519 ? 201.964 248.725 179.007 1.00 9.23  ? 3519 TYR A OH    1 
ATOM   14797 N  N     . PHE A 1 3520 ? 204.714 249.318 172.309 1.00 0.46  ? 3520 PHE A N     1 
ATOM   14798 C  CA    . PHE A 1 3520 ? 204.248 250.679 172.106 1.00 1.24  ? 3520 PHE A CA    1 
ATOM   14799 C  C     . PHE A 1 3520 ? 203.156 250.746 171.039 1.00 1.72  ? 3520 PHE A C     1 
ATOM   14800 O  O     . PHE A 1 3520 ? 202.957 249.820 170.250 1.00 1.33  ? 3520 PHE A O     1 
ATOM   14801 C  CB    . PHE A 1 3520 ? 205.422 251.580 171.730 1.00 1.12  ? 3520 PHE A CB    1 
ATOM   14802 C  CG    . PHE A 1 3520 ? 206.551 251.529 172.712 1.00 1.16  ? 3520 PHE A CG    1 
ATOM   14803 C  CD1   . PHE A 1 3520 ? 206.478 252.225 173.907 1.00 1.18  ? 3520 PHE A CD1   1 
ATOM   14804 C  CD2   . PHE A 1 3520 ? 207.679 250.768 172.453 1.00 0.57  ? 3520 PHE A CD2   1 
ATOM   14805 C  CE1   . PHE A 1 3520 ? 207.512 252.172 174.816 1.00 2.68  ? 3520 PHE A CE1   1 
ATOM   14806 C  CE2   . PHE A 1 3520 ? 208.712 250.710 173.360 1.00 1.56  ? 3520 PHE A CE2   1 
ATOM   14807 C  CZ    . PHE A 1 3520 ? 208.631 251.415 174.542 1.00 3.40  ? 3520 PHE A CZ    1 
ATOM   14808 N  N     . ASP A 1 3521 ? 202.438 251.867 171.033 1.00 2.65  ? 3521 ASP A N     1 
ATOM   14809 C  CA    . ASP A 1 3521 ? 201.374 252.095 170.067 1.00 1.85  ? 3521 ASP A CA    1 
ATOM   14810 C  C     . ASP A 1 3521 ? 201.953 252.658 168.770 1.00 1.44  ? 3521 ASP A C     1 
ATOM   14811 O  O     . ASP A 1 3521 ? 203.166 252.819 168.618 1.00 2.01  ? 3521 ASP A O     1 
ATOM   14812 C  CB    . ASP A 1 3521 ? 200.301 253.007 170.662 1.00 1.96  ? 3521 ASP A CB    1 
ATOM   14813 C  CG    . ASP A 1 3521 ? 200.843 254.361 171.097 1.00 7.00  ? 3521 ASP A CG    1 
ATOM   14814 O  OD1   . ASP A 1 3521 ? 202.037 254.644 170.876 1.00 10.23 ? 3521 ASP A OD1   1 
ATOM   14815 O  OD2   . ASP A 1 3521 ? 200.063 255.151 171.667 1.00 8.66  ? 3521 ASP A OD2   1 
ATOM   14816 N  N     . GLN A 1 3522 ? 201.066 252.976 167.823 1.00 2.02  ? 3522 GLN A N     1 
ATOM   14817 C  CA    . GLN A 1 3522 ? 201.505 253.360 166.485 1.00 1.95  ? 3522 GLN A CA    1 
ATOM   14818 C  C     . GLN A 1 3522 ? 202.371 254.616 166.509 1.00 3.15  ? 3522 GLN A C     1 
ATOM   14819 O  O     . GLN A 1 3522 ? 203.412 254.671 165.844 1.00 2.40  ? 3522 GLN A O     1 
ATOM   14820 C  CB    . GLN A 1 3522 ? 200.296 253.568 165.573 1.00 1.75  ? 3522 GLN A CB    1 
ATOM   14821 C  CG    . GLN A 1 3522 ? 200.631 254.272 164.267 1.00 3.08  ? 3522 GLN A CG    1 
ATOM   14822 C  CD    . GLN A 1 3522 ? 199.538 254.141 163.228 1.00 6.32  ? 3522 GLN A CD    1 
ATOM   14823 O  OE1   . GLN A 1 3522 ? 198.371 253.950 163.561 1.00 10.65 ? 3522 GLN A OE1   1 
ATOM   14824 N  NE2   . GLN A 1 3522 ? 199.913 254.243 161.961 1.00 11.54 ? 3522 GLN A NE2   1 
ATOM   14825 N  N     . GLN A 1 3523 ? 201.959 255.633 167.268 1.00 3.87  ? 3523 GLN A N     1 
ATOM   14826 C  CA    . GLN A 1 3523 ? 202.710 256.885 167.300 1.00 4.00  ? 3523 GLN A CA    1 
ATOM   14827 C  C     . GLN A 1 3523 ? 204.096 256.688 167.904 1.00 5.54  ? 3523 GLN A C     1 
ATOM   14828 O  O     . GLN A 1 3523 ? 205.086 257.223 167.390 1.00 6.71  ? 3523 GLN A O     1 
ATOM   14829 C  CB    . GLN A 1 3523 ? 201.933 257.944 168.079 1.00 6.14  ? 3523 GLN A CB    1 
ATOM   14830 C  CG    . GLN A 1 3523 ? 202.602 259.313 168.131 1.00 7.12  ? 3523 GLN A CG    1 
ATOM   14831 C  CD    . GLN A 1 3523 ? 202.727 259.963 166.764 1.00 18.38 ? 3523 GLN A CD    1 
ATOM   14832 O  OE1   . GLN A 1 3523 ? 203.673 259.702 166.021 1.00 20.83 ? 3523 GLN A OE1   1 
ATOM   14833 N  NE2   . GLN A 1 3523 ? 201.768 260.817 166.427 1.00 13.06 ? 3523 GLN A NE2   1 
ATOM   14834 N  N     . MET A 1 3524 ? 204.187 255.925 168.992 1.00 3.40  ? 3524 MET A N     1 
ATOM   14835 C  CA    . MET A 1 3524 ? 205.472 255.743 169.657 1.00 2.60  ? 3524 MET A CA    1 
ATOM   14836 C  C     . MET A 1 3524 ? 206.395 254.845 168.841 1.00 3.85  ? 3524 MET A C     1 
ATOM   14837 O  O     . MET A 1 3524 ? 207.615 255.042 168.834 1.00 5.02  ? 3524 MET A O     1 
ATOM   14838 C  CB    . MET A 1 3524 ? 205.262 255.176 171.059 1.00 3.49  ? 3524 MET A CB    1 
ATOM   14839 C  CG    . MET A 1 3524 ? 206.520 255.158 171.900 1.00 5.94  ? 3524 MET A CG    1 
ATOM   14840 S  SD    . MET A 1 3524 ? 207.126 256.828 172.199 1.00 27.38 ? 3524 MET A SD    1 
ATOM   14841 C  CE    . MET A 1 3524 ? 208.856 256.633 171.794 1.00 9.90  ? 3524 MET A CE    1 
ATOM   14842 N  N     . ARG A 1 3525 ? 205.832 253.850 168.150 1.00 2.31  ? 3525 ARG A N     1 
ATOM   14843 C  CA    . ARG A 1 3525 ? 206.638 253.014 167.264 1.00 1.79  ? 3525 ARG A CA    1 
ATOM   14844 C  C     . ARG A 1 3525 ? 207.265 253.847 166.156 1.00 3.02  ? 3525 ARG A C     1 
ATOM   14845 O  O     . ARG A 1 3525 ? 208.442 253.673 165.820 1.00 6.40  ? 3525 ARG A O     1 
ATOM   14846 C  CB    . ARG A 1 3525 ? 205.781 251.895 166.669 1.00 1.57  ? 3525 ARG A CB    1 
ATOM   14847 C  CG    . ARG A 1 3525 ? 205.363 250.817 167.651 1.00 0.93  ? 3525 ARG A CG    1 
ATOM   14848 C  CD    . ARG A 1 3525 ? 204.668 249.675 166.934 1.00 0.46  ? 3525 ARG A CD    1 
ATOM   14849 N  NE    . ARG A 1 3525 ? 204.255 248.615 167.846 1.00 0.38  ? 3525 ARG A NE    1 
ATOM   14850 C  CZ    . ARG A 1 3525 ? 203.667 247.490 167.465 1.00 0.32  ? 3525 ARG A CZ    1 
ATOM   14851 N  NH1   . ARG A 1 3525 ? 203.426 247.236 166.190 1.00 0.34  ? 3525 ARG A NH1   1 
ATOM   14852 N  NH2   . ARG A 1 3525 ? 203.315 246.598 168.383 1.00 0.25  ? 3525 ARG A NH2   1 
ATOM   14853 N  N     . GLN A 1 3526 ? 206.486 254.759 165.571 1.00 3.59  ? 3526 GLN A N     1 
ATOM   14854 C  CA    . GLN A 1 3526 ? 207.004 255.609 164.505 1.00 2.95  ? 3526 GLN A CA    1 
ATOM   14855 C  C     . GLN A 1 3526 ? 208.068 256.566 165.032 1.00 3.46  ? 3526 GLN A C     1 
ATOM   14856 O  O     . GLN A 1 3526 ? 209.064 256.834 164.349 1.00 2.84  ? 3526 GLN A O     1 
ATOM   14857 C  CB    . GLN A 1 3526 ? 205.856 256.378 163.851 1.00 3.87  ? 3526 GLN A CB    1 
ATOM   14858 C  CG    . GLN A 1 3526 ? 206.247 257.182 162.625 1.00 2.16  ? 3526 GLN A CG    1 
ATOM   14859 C  CD    . GLN A 1 3526 ? 207.044 256.369 161.629 1.00 3.08  ? 3526 GLN A CD    1 
ATOM   14860 O  OE1   . GLN A 1 3526 ? 206.599 255.320 161.170 1.00 8.04  ? 3526 GLN A OE1   1 
ATOM   14861 N  NE2   . GLN A 1 3526 ? 208.225 256.857 161.277 1.00 5.69  ? 3526 GLN A NE2   1 
ATOM   14862 N  N     . ASN A 1 3527 ? 207.872 257.091 166.244 1.00 2.95  ? 3527 ASN A N     1 
ATOM   14863 C  CA    . ASN A 1 3527 ? 208.863 257.982 166.839 1.00 1.71  ? 3527 ASN A CA    1 
ATOM   14864 C  C     . ASN A 1 3527 ? 210.189 257.268 167.063 1.00 2.24  ? 3527 ASN A C     1 
ATOM   14865 O  O     . ASN A 1 3527 ? 211.257 257.840 166.823 1.00 2.65  ? 3527 ASN A O     1 
ATOM   14866 C  CB    . ASN A 1 3527 ? 208.338 258.557 168.156 1.00 3.82  ? 3527 ASN A CB    1 
ATOM   14867 C  CG    . ASN A 1 3527 ? 207.150 259.477 167.961 1.00 9.33  ? 3527 ASN A CG    1 
ATOM   14868 O  OD1   . ASN A 1 3527 ? 206.965 260.055 166.889 1.00 14.91 ? 3527 ASN A OD1   1 
ATOM   14869 N  ND2   . ASN A 1 3527 ? 206.342 259.628 169.002 1.00 10.18 ? 3527 ASN A ND2   1 
ATOM   14870 N  N     . LEU A 1 3528 ? 210.143 256.023 167.543 1.00 1.78  ? 3528 LEU A N     1 
ATOM   14871 C  CA    . LEU A 1 3528 ? 211.371 255.262 167.749 1.00 0.90  ? 3528 LEU A CA    1 
ATOM   14872 C  C     . LEU A 1 3528 ? 212.091 255.007 166.433 1.00 0.54  ? 3528 LEU A C     1 
ATOM   14873 O  O     . LEU A 1 3528 ? 213.318 255.133 166.354 1.00 0.65  ? 3528 LEU A O     1 
ATOM   14874 C  CB    . LEU A 1 3528 ? 211.062 253.941 168.453 1.00 0.63  ? 3528 LEU A CB    1 
ATOM   14875 C  CG    . LEU A 1 3528 ? 210.712 254.021 169.938 1.00 0.76  ? 3528 LEU A CG    1 
ATOM   14876 C  CD1   . LEU A 1 3528 ? 210.111 252.715 170.415 1.00 0.96  ? 3528 LEU A CD1   1 
ATOM   14877 C  CD2   . LEU A 1 3528 ? 211.942 254.374 170.755 1.00 0.86  ? 3528 LEU A CD2   1 
ATOM   14878 N  N     . PHE A 1 3529 ? 211.345 254.643 165.390 1.00 1.28  ? 3529 PHE A N     1 
ATOM   14879 C  CA    . PHE A 1 3529 ? 211.963 254.350 164.101 1.00 1.13  ? 3529 PHE A CA    1 
ATOM   14880 C  C     . PHE A 1 3529 ? 212.565 255.604 163.477 1.00 1.82  ? 3529 PHE A C     1 
ATOM   14881 O  O     . PHE A 1 3529 ? 213.641 255.546 162.875 1.00 2.09  ? 3529 PHE A O     1 
ATOM   14882 C  CB    . PHE A 1 3529 ? 210.934 253.712 163.168 1.00 0.93  ? 3529 PHE A CB    1 
ATOM   14883 C  CG    . PHE A 1 3529 ? 211.539 252.904 162.058 1.00 1.76  ? 3529 PHE A CG    1 
ATOM   14884 C  CD1   . PHE A 1 3529 ? 211.875 253.495 160.854 1.00 0.84  ? 3529 PHE A CD1   1 
ATOM   14885 C  CD2   . PHE A 1 3529 ? 211.771 251.547 162.222 1.00 0.58  ? 3529 PHE A CD2   1 
ATOM   14886 C  CE1   . PHE A 1 3529 ? 212.431 252.751 159.836 1.00 0.38  ? 3529 PHE A CE1   1 
ATOM   14887 C  CE2   . PHE A 1 3529 ? 212.327 250.800 161.207 1.00 0.35  ? 3529 PHE A CE2   1 
ATOM   14888 C  CZ    . PHE A 1 3529 ? 212.658 251.402 160.013 1.00 0.46  ? 3529 PHE A CZ    1 
ATOM   14889 N  N     . THR A 1 3530 ? 211.883 256.744 163.609 1.00 2.13  ? 3530 THR A N     1 
ATOM   14890 C  CA    . THR A 1 3530 ? 212.426 257.997 163.090 1.00 2.59  ? 3530 THR A CA    1 
ATOM   14891 C  C     . THR A 1 3530 ? 213.683 258.409 163.847 1.00 2.03  ? 3530 THR A C     1 
ATOM   14892 O  O     . THR A 1 3530 ? 214.645 258.901 163.245 1.00 3.98  ? 3530 THR A O     1 
ATOM   14893 C  CB    . THR A 1 3530 ? 211.362 259.095 163.155 1.00 2.19  ? 3530 THR A CB    1 
ATOM   14894 O  OG1   . THR A 1 3530 ? 210.294 258.776 162.255 1.00 2.19  ? 3530 THR A OG1   1 
ATOM   14895 C  CG2   . THR A 1 3530 ? 211.949 260.444 162.766 1.00 2.73  ? 3530 THR A CG2   1 
ATOM   14896 N  N     . THR A 1 3531 ? 213.696 258.213 165.168 1.00 1.63  ? 3531 THR A N     1 
ATOM   14897 C  CA    . THR A 1 3531 ? 214.884 258.532 165.955 1.00 0.89  ? 3531 THR A CA    1 
ATOM   14898 C  C     . THR A 1 3531 ? 216.069 257.660 165.554 1.00 1.67  ? 3531 THR A C     1 
ATOM   14899 O  O     . THR A 1 3531 ? 217.192 258.157 165.417 1.00 2.72  ? 3531 THR A O     1 
ATOM   14900 C  CB    . THR A 1 3531 ? 214.582 258.373 167.445 1.00 1.70  ? 3531 THR A CB    1 
ATOM   14901 O  OG1   . THR A 1 3531 ? 213.424 259.142 167.784 1.00 3.12  ? 3531 THR A OG1   1 
ATOM   14902 C  CG2   . THR A 1 3531 ? 215.760 258.843 168.284 1.00 1.46  ? 3531 THR A CG2   1 
ATOM   14903 N  N     . TRP A 1 3532 ? 215.840 256.357 165.369 1.00 2.03  ? 3532 TRP A N     1 
ATOM   14904 C  CA    . TRP A 1 3532 ? 216.913 255.478 164.912 1.00 1.13  ? 3532 TRP A CA    1 
ATOM   14905 C  C     . TRP A 1 3532 ? 217.348 255.831 163.498 1.00 1.33  ? 3532 TRP A C     1 
ATOM   14906 O  O     . TRP A 1 3532 ? 218.547 255.864 163.200 1.00 2.95  ? 3532 TRP A O     1 
ATOM   14907 C  CB    . TRP A 1 3532 ? 216.469 254.016 164.970 1.00 0.35  ? 3532 TRP A CB    1 
ATOM   14908 C  CG    . TRP A 1 3532 ? 215.940 253.573 166.286 1.00 0.19  ? 3532 TRP A CG    1 
ATOM   14909 C  CD1   . TRP A 1 3532 ? 216.300 254.036 167.516 1.00 0.24  ? 3532 TRP A CD1   1 
ATOM   14910 C  CD2   . TRP A 1 3532 ? 214.949 252.568 166.510 1.00 0.20  ? 3532 TRP A CD2   1 
ATOM   14911 N  NE1   . TRP A 1 3532 ? 215.592 253.384 168.491 1.00 0.16  ? 3532 TRP A NE1   1 
ATOM   14912 C  CE2   . TRP A 1 3532 ? 214.753 252.477 167.900 1.00 0.11  ? 3532 TRP A CE2   1 
ATOM   14913 C  CE3   . TRP A 1 3532 ? 214.203 251.738 165.669 1.00 0.15  ? 3532 TRP A CE3   1 
ATOM   14914 C  CZ2   . TRP A 1 3532 ? 213.851 251.588 168.468 1.00 0.14  ? 3532 TRP A CZ2   1 
ATOM   14915 C  CZ3   . TRP A 1 3532 ? 213.307 250.858 166.233 1.00 0.08  ? 3532 TRP A CZ3   1 
ATOM   14916 C  CH2   . TRP A 1 3532 ? 213.138 250.787 167.620 1.00 0.11  ? 3532 TRP A CH2   1 
ATOM   14917 N  N     . SER A 1 3533 ? 216.381 256.093 162.613 1.00 1.98  ? 3533 SER A N     1 
ATOM   14918 C  CA    . SER A 1 3533 ? 216.708 256.435 161.232 1.00 2.31  ? 3533 SER A CA    1 
ATOM   14919 C  C     . SER A 1 3533 ? 217.502 257.730 161.162 1.00 3.53  ? 3533 SER A C     1 
ATOM   14920 O  O     . SER A 1 3533 ? 218.452 257.843 160.377 1.00 3.08  ? 3533 SER A O     1 
ATOM   14921 C  CB    . SER A 1 3533 ? 215.427 256.543 160.405 1.00 1.92  ? 3533 SER A CB    1 
ATOM   14922 O  OG    . SER A 1 3533 ? 214.749 255.300 160.356 1.00 3.30  ? 3533 SER A OG    1 
ATOM   14923 N  N     . HIS A 1 3534 ? 217.129 258.721 161.974 1.00 2.73  ? 3534 HIS A N     1 
ATOM   14924 C  CA    . HIS A 1 3534 ? 217.888 259.965 162.021 1.00 4.26  ? 3534 HIS A CA    1 
ATOM   14925 C  C     . HIS A 1 3534 ? 219.321 259.721 162.473 1.00 4.20  ? 3534 HIS A C     1 
ATOM   14926 O  O     . HIS A 1 3534 ? 220.263 260.271 161.895 1.00 4.84  ? 3534 HIS A O     1 
ATOM   14927 C  CB    . HIS A 1 3534 ? 217.205 260.967 162.950 1.00 4.33  ? 3534 HIS A CB    1 
ATOM   14928 C  CG    . HIS A 1 3534 ? 216.032 261.662 162.335 1.00 10.93 ? 3534 HIS A CG    1 
ATOM   14929 N  ND1   . HIS A 1 3534 ? 215.790 261.659 160.978 1.00 10.53 ? 3534 HIS A ND1   1 
ATOM   14930 C  CD2   . HIS A 1 3534 ? 215.036 262.391 162.892 1.00 9.94  ? 3534 HIS A CD2   1 
ATOM   14931 C  CE1   . HIS A 1 3534 ? 214.693 262.351 160.728 1.00 12.56 ? 3534 HIS A CE1   1 
ATOM   14932 N  NE2   . HIS A 1 3534 ? 214.217 262.807 161.872 1.00 11.20 ? 3534 HIS A NE2   1 
ATOM   14933 N  N     . HIS A 1 3535 ? 219.503 258.883 163.497 1.00 3.86  ? 3535 HIS A N     1 
ATOM   14934 C  CA    . HIS A 1 3535 ? 220.840 258.620 164.014 1.00 2.26  ? 3535 HIS A CA    1 
ATOM   14935 C  C     . HIS A 1 3535 ? 221.719 257.944 162.969 1.00 3.44  ? 3535 HIS A C     1 
ATOM   14936 O  O     . HIS A 1 3535 ? 222.911 258.252 162.859 1.00 9.11  ? 3535 HIS A O     1 
ATOM   14937 C  CB    . HIS A 1 3535 ? 220.754 257.764 165.272 1.00 1.13  ? 3535 HIS A CB    1 
ATOM   14938 C  CG    . HIS A 1 3535 ? 222.072 257.547 165.947 1.00 2.04  ? 3535 HIS A CG    1 
ATOM   14939 N  ND1   . HIS A 1 3535 ? 222.896 256.485 165.645 1.00 2.83  ? 3535 HIS A ND1   1 
ATOM   14940 C  CD2   . HIS A 1 3535 ? 222.711 258.259 166.905 1.00 1.88  ? 3535 HIS A CD2   1 
ATOM   14941 C  CE1   . HIS A 1 3535 ? 223.985 256.551 166.388 1.00 3.50  ? 3535 HIS A CE1   1 
ATOM   14942 N  NE2   . HIS A 1 3535 ? 223.897 257.618 167.160 1.00 3.71  ? 3535 HIS A NE2   1 
ATOM   14943 N  N     . LEU A 1 3536 ? 221.151 257.010 162.206 1.00 2.52  ? 3536 LEU A N     1 
ATOM   14944 C  CA    . LEU A 1 3536 ? 221.917 256.359 161.149 1.00 3.59  ? 3536 LEU A CA    1 
ATOM   14945 C  C     . LEU A 1 3536 ? 222.361 257.367 160.097 1.00 5.53  ? 3536 LEU A C     1 
ATOM   14946 O  O     . LEU A 1 3536 ? 223.462 257.252 159.544 1.00 8.45  ? 3536 LEU A O     1 
ATOM   14947 C  CB    . LEU A 1 3536 ? 221.089 255.244 160.513 1.00 5.53  ? 3536 LEU A CB    1 
ATOM   14948 C  CG    . LEU A 1 3536 ? 220.780 254.019 161.378 1.00 3.38  ? 3536 LEU A CG    1 
ATOM   14949 C  CD1   . LEU A 1 3536 ? 220.311 252.865 160.513 1.00 4.29  ? 3536 LEU A CD1   1 
ATOM   14950 C  CD2   . LEU A 1 3536 ? 221.986 253.614 162.206 1.00 3.74  ? 3536 LEU A CD2   1 
ATOM   14951 N  N     . GLN A 1 3537 ? 221.515 258.356 159.801 1.00 6.62  ? 3537 GLN A N     1 
ATOM   14952 C  CA    . GLN A 1 3537 ? 221.886 259.393 158.844 1.00 6.65  ? 3537 GLN A CA    1 
ATOM   14953 C  C     . GLN A 1 3537 ? 223.074 260.210 159.336 1.00 7.92  ? 3537 GLN A C     1 
ATOM   14954 O  O     . GLN A 1 3537 ? 224.001 260.494 158.570 1.00 10.58 ? 3537 GLN A O     1 
ATOM   14955 C  CB    . GLN A 1 3537 ? 220.687 260.298 158.559 1.00 8.35  ? 3537 GLN A CB    1 
ATOM   14956 C  CG    . GLN A 1 3537 ? 219.552 259.610 157.825 1.00 10.68 ? 3537 GLN A CG    1 
ATOM   14957 C  CD    . GLN A 1 3537 ? 218.367 260.525 157.578 1.00 20.10 ? 3537 GLN A CD    1 
ATOM   14958 O  OE1   . GLN A 1 3537 ? 218.354 261.674 158.017 1.00 18.54 ? 3537 GLN A OE1   1 
ATOM   14959 N  NE2   . GLN A 1 3537 ? 217.366 260.018 156.866 1.00 19.79 ? 3537 GLN A NE2   1 
ATOM   14960 N  N     . GLN A 1 3538 ? 223.070 260.595 160.615 1.00 5.14  ? 3538 GLN A N     1 
ATOM   14961 C  CA    . GLN A 1 3538 ? 224.200 261.342 161.156 1.00 5.70  ? 3538 GLN A CA    1 
ATOM   14962 C  C     . GLN A 1 3538 ? 225.460 260.498 161.254 1.00 10.73 ? 3538 GLN A C     1 
ATOM   14963 O  O     . GLN A 1 3538 ? 226.557 261.059 161.346 1.00 21.73 ? 3538 GLN A O     1 
ATOM   14964 C  CB    . GLN A 1 3538 ? 223.862 261.921 162.532 1.00 10.15 ? 3538 GLN A CB    1 
ATOM   14965 C  CG    . GLN A 1 3538 ? 222.416 262.321 162.712 1.00 5.22  ? 3538 GLN A CG    1 
ATOM   14966 C  CD    . GLN A 1 3538 ? 222.203 263.200 163.926 1.00 21.45 ? 3538 GLN A CD    1 
ATOM   14967 O  OE1   . GLN A 1 3538 ? 223.087 263.339 164.770 1.00 26.19 ? 3538 GLN A OE1   1 
ATOM   14968 N  NE2   . GLN A 1 3538 ? 221.022 263.802 164.021 1.00 23.05 ? 3538 GLN A NE2   1 
ATOM   14969 N  N     . ALA A 1 3539 ? 225.335 259.173 161.240 1.00 9.73  ? 3539 ALA A N     1 
ATOM   14970 C  CA    . ALA A 1 3539 ? 226.477 258.275 161.296 1.00 8.29  ? 3539 ALA A CA    1 
ATOM   14971 C  C     . ALA A 1 3539 ? 226.913 257.790 159.920 1.00 9.44  ? 3539 ALA A C     1 
ATOM   14972 O  O     . ALA A 1 3539 ? 227.820 256.957 159.829 1.00 19.13 ? 3539 ALA A O     1 
ATOM   14973 C  CB    . ALA A 1 3539 ? 226.166 257.081 162.196 1.00 5.39  ? 3539 ALA A CB    1 
ATOM   14974 N  N     . ASN A 1 3540 ? 226.284 258.288 158.853 1.00 6.53  ? 3540 ASN A N     1 
ATOM   14975 C  CA    . ASN A 1 3540 ? 226.572 257.873 157.478 1.00 8.42  ? 3540 ASN A CA    1 
ATOM   14976 C  C     . ASN A 1 3540 ? 226.347 256.378 157.272 1.00 8.75  ? 3540 ASN A C     1 
ATOM   14977 O  O     . ASN A 1 3540 ? 227.037 255.739 156.474 1.00 15.63 ? 3540 ASN A O     1 
ATOM   14978 C  CB    . ASN A 1 3540 ? 227.996 258.254 157.059 1.00 10.62 ? 3540 ASN A CB    1 
ATOM   14979 C  CG    . ASN A 1 3540 ? 228.141 259.731 156.767 1.00 14.34 ? 3540 ASN A CG    1 
ATOM   14980 O  OD1   . ASN A 1 3540 ? 227.358 260.551 157.242 1.00 15.66 ? 3540 ASN A OD1   1 
ATOM   14981 N  ND2   . ASN A 1 3540 ? 229.155 260.079 155.983 1.00 17.14 ? 3540 ASN A ND2   1 
ATOM   14982 N  N     . ILE A 1 3541 ? 225.379 255.805 157.982 1.00 8.56  ? 3541 ILE A N     1 
ATOM   14983 C  CA    . ILE A 1 3541 ? 224.990 254.415 157.787 1.00 7.92  ? 3541 ILE A CA    1 
ATOM   14984 C  C     . ILE A 1 3541 ? 223.901 254.379 156.722 1.00 8.90  ? 3541 ILE A C     1 
ATOM   14985 O  O     . ILE A 1 3541 ? 222.860 255.029 156.865 1.00 12.01 ? 3541 ILE A O     1 
ATOM   14986 C  CB    . ILE A 1 3541 ? 224.504 253.775 159.097 1.00 6.41  ? 3541 ILE A CB    1 
ATOM   14987 C  CG1   . ILE A 1 3541 ? 225.529 253.993 160.212 1.00 7.78  ? 3541 ILE A CG1   1 
ATOM   14988 C  CG2   . ILE A 1 3541 ? 224.219 252.294 158.890 1.00 4.81  ? 3541 ILE A CG2   1 
ATOM   14989 C  CD1   . ILE A 1 3541 ? 226.727 253.078 160.137 1.00 7.61  ? 3541 ILE A CD1   1 
ATOM   14990 N  N     . GLN A 1 3542 ? 224.137 253.620 155.659 1.00 9.88  ? 3542 GLN A N     1 
ATOM   14991 C  CA    . GLN A 1 3542 ? 223.239 253.623 154.513 1.00 10.19 ? 3542 GLN A CA    1 
ATOM   14992 C  C     . GLN A 1 3542 ? 222.024 252.742 154.777 1.00 8.50  ? 3542 GLN A C     1 
ATOM   14993 O  O     . GLN A 1 3542 ? 222.159 251.591 155.204 1.00 10.32 ? 3542 GLN A O     1 
ATOM   14994 C  CB    . GLN A 1 3542 ? 223.976 253.146 153.264 1.00 10.83 ? 3542 GLN A CB    1 
ATOM   14995 C  CG    . GLN A 1 3542 ? 225.093 254.071 152.823 1.00 13.19 ? 3542 GLN A CG    1 
ATOM   14996 C  CD    . GLN A 1 3542 ? 224.588 255.444 152.439 1.00 24.83 ? 3542 GLN A CD    1 
ATOM   14997 O  OE1   . GLN A 1 3542 ? 224.821 256.423 153.145 1.00 31.49 ? 3542 GLN A OE1   1 
ATOM   14998 N  NE2   . GLN A 1 3542 ? 223.886 255.524 151.314 1.00 22.40 ? 3542 GLN A NE2   1 
ATOM   14999 N  N     . PHE A 1 3543 ? 220.839 253.291 154.521 1.00 7.59  ? 3543 PHE A N     1 
ATOM   15000 C  CA    . PHE A 1 3543 ? 219.594 252.544 154.618 1.00 6.38  ? 3543 PHE A CA    1 
ATOM   15001 C  C     . PHE A 1 3543 ? 218.581 253.176 153.674 1.00 10.25 ? 3543 PHE A C     1 
ATOM   15002 O  O     . PHE A 1 3543 ? 218.577 254.393 153.472 1.00 12.79 ? 3543 PHE A O     1 
ATOM   15003 C  CB    . PHE A 1 3543 ? 219.047 252.525 156.050 1.00 4.66  ? 3543 PHE A CB    1 
ATOM   15004 C  CG    . PHE A 1 3543 ? 218.631 253.876 156.559 1.00 6.23  ? 3543 PHE A CG    1 
ATOM   15005 C  CD1   . PHE A 1 3543 ? 219.563 254.744 157.105 1.00 6.62  ? 3543 PHE A CD1   1 
ATOM   15006 C  CD2   . PHE A 1 3543 ? 217.309 254.275 156.501 1.00 5.92  ? 3543 PHE A CD2   1 
ATOM   15007 C  CE1   . PHE A 1 3543 ? 219.183 255.983 157.572 1.00 6.60  ? 3543 PHE A CE1   1 
ATOM   15008 C  CE2   . PHE A 1 3543 ? 216.923 255.512 156.971 1.00 6.25  ? 3543 PHE A CE2   1 
ATOM   15009 C  CZ    . PHE A 1 3543 ? 217.860 256.368 157.506 1.00 4.96  ? 3543 PHE A CZ    1 
ATOM   15010 N  N     . ARG A 1 3544 ? 217.724 252.340 153.100 1.00 10.63 ? 3544 ARG A N     1 
ATOM   15011 C  CA    . ARG A 1 3544 ? 216.683 252.826 152.206 1.00 11.14 ? 3544 ARG A CA    1 
ATOM   15012 C  C     . ARG A 1 3544 ? 215.509 253.381 153.001 1.00 12.44 ? 3544 ARG A C     1 
ATOM   15013 O  O     . ARG A 1 3544 ? 215.185 252.891 154.087 1.00 15.76 ? 3544 ARG A O     1 
ATOM   15014 C  CB    . ARG A 1 3544 ? 216.219 251.711 151.271 1.00 10.85 ? 3544 ARG A CB    1 
ATOM   15015 C  CG    . ARG A 1 3544 ? 217.325 251.196 150.364 1.00 13.05 ? 3544 ARG A CG    1 
ATOM   15016 C  CD    . ARG A 1 3544 ? 217.002 249.834 149.786 1.00 15.30 ? 3544 ARG A CD    1 
ATOM   15017 N  NE    . ARG A 1 3544 ? 216.246 249.004 150.715 1.00 17.04 ? 3544 ARG A NE    1 
ATOM   15018 C  CZ    . ARG A 1 3544 ? 215.850 247.767 150.453 1.00 18.71 ? 3544 ARG A CZ    1 
ATOM   15019 N  NH1   . ARG A 1 3544 ? 216.139 247.176 149.305 1.00 19.07 ? 3544 ARG A NH1   1 
ATOM   15020 N  NH2   . ARG A 1 3544 ? 215.144 247.107 151.366 1.00 16.05 ? 3544 ARG A NH2   1 
ATOM   15021 N  N     . THR A 1 3545 ? 214.877 254.424 152.457 1.00 18.20 ? 3545 THR A N     1 
ATOM   15022 C  CA    . THR A 1 3545 ? 213.764 255.100 153.116 1.00 18.51 ? 3545 THR A CA    1 
ATOM   15023 C  C     . THR A 1 3545 ? 212.458 254.948 152.345 1.00 21.39 ? 3545 THR A C     1 
ATOM   15024 O  O     . THR A 1 3545 ? 211.497 255.674 152.614 1.00 21.52 ? 3545 THR A O     1 
ATOM   15025 C  CB    . THR A 1 3545 ? 214.079 256.584 153.320 1.00 21.65 ? 3545 THR A CB    1 
ATOM   15026 O  OG1   . THR A 1 3545 ? 214.279 257.210 152.046 1.00 28.13 ? 3545 THR A OG1   1 
ATOM   15027 C  CG2   . THR A 1 3545 ? 215.331 256.752 154.156 1.00 14.83 ? 3545 THR A CG2   1 
ATOM   15028 N  N     . ASP A 1 3546 ? 212.398 254.018 151.394 1.00 22.68 ? 3546 ASP A N     1 
ATOM   15029 C  CA    . ASP A 1 3546 ? 211.216 253.829 150.560 1.00 24.85 ? 3546 ASP A CA    1 
ATOM   15030 C  C     . ASP A 1 3546 ? 210.395 252.636 151.033 1.00 28.31 ? 3546 ASP A C     1 
ATOM   15031 O  O     . ASP A 1 3546 ? 209.184 252.761 151.235 1.00 26.10 ? 3546 ASP A O     1 
ATOM   15032 C  CB    . ASP A 1 3546 ? 211.626 253.669 149.094 1.00 19.70 ? 3546 ASP A CB    1 
ATOM   15033 C  CG    . ASP A 1 3546 ? 212.754 252.676 148.914 1.00 27.83 ? 3546 ASP A CG    1 
ATOM   15034 O  OD1   . ASP A 1 3546 ? 213.212 252.112 149.929 1.00 30.61 ? 3546 ASP A OD1   1 
ATOM   15035 O  OD2   . ASP A 1 3546 ? 213.183 252.458 147.762 1.00 31.88 ? 3546 ASP A OD2   1 
ATOM   15036 N  N     . ILE A 1 3547 ? 211.023 251.472 151.213 1.00 23.04 ? 3547 ILE A N     1 
ATOM   15037 C  CA    . ILE A 1 3547 ? 210.278 250.272 151.567 1.00 21.38 ? 3547 ILE A CA    1 
ATOM   15038 C  C     . ILE A 1 3547 ? 209.795 250.364 153.007 1.00 23.16 ? 3547 ILE A C     1 
ATOM   15039 O  O     . ILE A 1 3547 ? 210.530 250.780 153.910 1.00 21.01 ? 3547 ILE A O     1 
ATOM   15040 C  CB    . ILE A 1 3547 ? 211.146 249.022 151.329 1.00 26.73 ? 3547 ILE A CB    1 
ATOM   15041 C  CG1   . ILE A 1 3547 ? 210.355 247.747 151.638 1.00 18.53 ? 3547 ILE A CG1   1 
ATOM   15042 C  CG2   . ILE A 1 3547 ? 212.439 249.089 152.135 1.00 19.57 ? 3547 ILE A CG2   1 
ATOM   15043 C  CD1   . ILE A 1 3547 ? 211.071 246.481 151.245 1.00 12.99 ? 3547 ILE A CD1   1 
ATOM   15044 N  N     . ALA A 1 3548 ? 208.536 249.996 153.218 1.00 20.50 ? 3548 ALA A N     1 
ATOM   15045 C  CA    . ALA A 1 3548 ? 207.962 249.964 154.551 1.00 13.80 ? 3548 ALA A CA    1 
ATOM   15046 C  C     . ALA A 1 3548 ? 208.538 248.799 155.350 1.00 12.65 ? 3548 ALA A C     1 
ATOM   15047 O  O     . ALA A 1 3548 ? 209.026 247.811 154.793 1.00 11.91 ? 3548 ALA A O     1 
ATOM   15048 C  CB    . ALA A 1 3548 ? 206.441 249.855 154.478 1.00 15.99 ? 3548 ALA A CB    1 
ATOM   15049 N  N     . ARG A 1 3549 ? 208.475 248.924 156.676 1.00 9.77  ? 3549 ARG A N     1 
ATOM   15050 C  CA    . ARG A 1 3549 ? 209.052 247.899 157.538 1.00 6.62  ? 3549 ARG A CA    1 
ATOM   15051 C  C     . ARG A 1 3549 ? 208.281 246.587 157.429 1.00 6.03  ? 3549 ARG A C     1 
ATOM   15052 O  O     . ARG A 1 3549 ? 208.868 245.504 157.530 1.00 12.27 ? 3549 ARG A O     1 
ATOM   15053 C  CB    . ARG A 1 3549 ? 209.097 248.386 158.987 1.00 6.60  ? 3549 ARG A CB    1 
ATOM   15054 C  CG    . ARG A 1 3549 ? 207.856 249.125 159.447 1.00 11.22 ? 3549 ARG A CG    1 
ATOM   15055 C  CD    . ARG A 1 3549 ? 208.173 250.121 160.551 1.00 2.62  ? 3549 ARG A CD    1 
ATOM   15056 N  NE    . ARG A 1 3549 ? 206.991 250.888 160.922 1.00 3.05  ? 3549 ARG A NE    1 
ATOM   15057 C  CZ    . ARG A 1 3549 ? 206.982 251.887 161.793 1.00 3.56  ? 3549 ARG A CZ    1 
ATOM   15058 N  NH1   . ARG A 1 3549 ? 208.095 252.317 162.362 1.00 13.03 ? 3549 ARG A NH1   1 
ATOM   15059 N  NH2   . ARG A 1 3549 ? 205.830 252.475 162.093 1.00 2.93  ? 3549 ARG A NH2   1 
ATOM   15060 N  N     . THR A 1 3550 ? 206.963 246.661 157.227 1.00 7.01  ? 3550 THR A N     1 
ATOM   15061 C  CA    . THR A 1 3550 ? 206.173 245.445 157.057 1.00 7.28  ? 3550 THR A CA    1 
ATOM   15062 C  C     . THR A 1 3550 ? 206.548 244.702 155.783 1.00 9.38  ? 3550 THR A C     1 
ATOM   15063 O  O     . THR A 1 3550 ? 206.582 243.466 155.774 1.00 7.93  ? 3550 THR A O     1 
ATOM   15064 C  CB    . THR A 1 3550 ? 204.679 245.771 157.054 1.00 6.34  ? 3550 THR A CB    1 
ATOM   15065 O  OG1   . THR A 1 3550 ? 204.395 246.739 156.036 1.00 16.31 ? 3550 THR A OG1   1 
ATOM   15066 C  CG2   . THR A 1 3550 ? 204.249 246.312 158.401 1.00 4.15  ? 3550 THR A CG2   1 
ATOM   15067 N  N     . GLU A 1 3551 ? 206.817 245.428 154.700 1.00 12.71 ? 3551 GLU A N     1 
ATOM   15068 C  CA    . GLU A 1 3551 ? 207.184 244.784 153.443 1.00 9.96  ? 3551 GLU A CA    1 
ATOM   15069 C  C     . GLU A 1 3551 ? 208.581 244.184 153.489 1.00 8.50  ? 3551 GLU A C     1 
ATOM   15070 O  O     . GLU A 1 3551 ? 208.839 243.171 152.830 1.00 10.91 ? 3551 GLU A O     1 
ATOM   15071 C  CB    . GLU A 1 3551 ? 207.084 245.784 152.292 1.00 11.15 ? 3551 GLU A CB    1 
ATOM   15072 C  CG    . GLU A 1 3551 ? 205.775 246.543 152.251 1.00 12.21 ? 3551 GLU A CG    1 
ATOM   15073 C  CD    . GLU A 1 3551 ? 204.585 245.628 152.061 1.00 21.62 ? 3551 GLU A CD    1 
ATOM   15074 O  OE1   . GLU A 1 3551 ? 204.336 245.205 150.913 1.00 19.38 ? 3551 GLU A OE1   1 
ATOM   15075 O  OE2   . GLU A 1 3551 ? 203.898 245.330 153.063 1.00 26.57 ? 3551 GLU A OE2   1 
ATOM   15076 N  N     . TYR A 1 3552 ? 209.493 244.788 154.248 1.00 8.49  ? 3552 TYR A N     1 
ATOM   15077 C  CA    . TYR A 1 3552 ? 210.866 244.311 154.318 1.00 6.92  ? 3552 TYR A CA    1 
ATOM   15078 C  C     . TYR A 1 3552 ? 211.039 243.127 155.263 1.00 5.14  ? 3552 TYR A C     1 
ATOM   15079 O  O     . TYR A 1 3552 ? 212.028 242.399 155.140 1.00 5.97  ? 3552 TYR A O     1 
ATOM   15080 C  CB    . TYR A 1 3552 ? 211.790 245.460 154.739 1.00 6.53  ? 3552 TYR A CB    1 
ATOM   15081 C  CG    . TYR A 1 3552 ? 213.263 245.125 154.760 1.00 7.11  ? 3552 TYR A CG    1 
ATOM   15082 C  CD1   . TYR A 1 3552 ? 214.016 245.162 153.594 1.00 5.80  ? 3552 TYR A CD1   1 
ATOM   15083 C  CD2   . TYR A 1 3552 ? 213.912 244.809 155.946 1.00 5.28  ? 3552 TYR A CD2   1 
ATOM   15084 C  CE1   . TYR A 1 3552 ? 215.360 244.869 153.603 1.00 6.56  ? 3552 TYR A CE1   1 
ATOM   15085 C  CE2   . TYR A 1 3552 ? 215.261 244.518 155.965 1.00 5.43  ? 3552 TYR A CE2   1 
ATOM   15086 C  CZ    . TYR A 1 3552 ? 215.981 244.550 154.789 1.00 8.84  ? 3552 TYR A CZ    1 
ATOM   15087 O  OH    . TYR A 1 3552 ? 217.323 244.261 154.793 1.00 6.54  ? 3552 TYR A OH    1 
ATOM   15088 N  N     . LEU A 1 3553 ? 210.101 242.906 156.180 1.00 5.84  ? 3553 LEU A N     1 
ATOM   15089 C  CA    . LEU A 1 3553 ? 210.206 241.829 157.154 1.00 4.80  ? 3553 LEU A CA    1 
ATOM   15090 C  C     . LEU A 1 3553 ? 209.206 240.707 156.926 1.00 4.07  ? 3553 LEU A C     1 
ATOM   15091 O  O     . LEU A 1 3553 ? 209.133 239.785 157.744 1.00 4.04  ? 3553 LEU A O     1 
ATOM   15092 C  CB    . LEU A 1 3553 ? 210.045 242.383 158.573 1.00 3.01  ? 3553 LEU A CB    1 
ATOM   15093 C  CG    . LEU A 1 3553 ? 211.201 243.255 159.052 1.00 4.39  ? 3553 LEU A CG    1 
ATOM   15094 C  CD1   . LEU A 1 3553 ? 210.903 243.845 160.419 1.00 2.44  ? 3553 LEU A CD1   1 
ATOM   15095 C  CD2   . LEU A 1 3553 ? 212.472 242.425 159.086 1.00 3.38  ? 3553 LEU A CD2   1 
ATOM   15096 N  N     . SER A 1 3554 ? 208.436 240.755 155.845 1.00 6.22  ? 3554 SER A N     1 
ATOM   15097 C  CA    . SER A 1 3554 ? 207.504 239.686 155.521 1.00 6.31  ? 3554 SER A CA    1 
ATOM   15098 C  C     . SER A 1 3554 ? 207.261 239.695 154.022 1.00 5.53  ? 3554 SER A C     1 
ATOM   15099 O  O     . SER A 1 3554 ? 207.375 240.734 153.368 1.00 9.24  ? 3554 SER A O     1 
ATOM   15100 C  CB    . SER A 1 3554 ? 206.183 239.832 156.285 1.00 3.54  ? 3554 SER A CB    1 
ATOM   15101 O  OG    . SER A 1 3554 ? 205.392 240.871 155.743 1.00 7.62  ? 3554 SER A OG    1 
ATOM   15102 N  N     . ASN A 1 3555 ? 206.936 238.527 153.483 1.00 7.33  ? 3555 ASN A N     1 
ATOM   15103 C  CA    . ASN A 1 3555 ? 206.619 238.389 152.070 1.00 7.11  ? 3555 ASN A CA    1 
ATOM   15104 C  C     . ASN A 1 3555 ? 205.110 238.458 151.858 1.00 6.73  ? 3555 ASN A C     1 
ATOM   15105 O  O     . ASN A 1 3555 ? 204.317 238.351 152.795 1.00 9.07  ? 3555 ASN A O     1 
ATOM   15106 C  CB    . ASN A 1 3555 ? 207.188 237.081 151.512 1.00 6.29  ? 3555 ASN A CB    1 
ATOM   15107 C  CG    . ASN A 1 3555 ? 206.827 235.877 152.354 1.00 9.46  ? 3555 ASN A CG    1 
ATOM   15108 O  OD1   . ASN A 1 3555 ? 205.685 235.422 152.346 1.00 13.45 ? 3555 ASN A OD1   1 
ATOM   15109 N  ND2   . ASN A 1 3555 ? 207.801 235.349 153.083 1.00 11.32 ? 3555 ASN A ND2   1 
ATOM   15110 N  N     . ALA A 1 3556 ? 204.720 238.651 150.597 1.00 7.96  ? 3556 ALA A N     1 
ATOM   15111 C  CA    . ALA A 1 3556 ? 203.302 238.714 150.262 1.00 7.39  ? 3556 ALA A CA    1 
ATOM   15112 C  C     . ALA A 1 3556 ? 202.605 237.380 150.505 1.00 8.32  ? 3556 ALA A C     1 
ATOM   15113 O  O     . ALA A 1 3556 ? 201.421 237.358 150.858 1.00 13.72 ? 3556 ALA A O     1 
ATOM   15114 C  CB    . ALA A 1 3556 ? 203.124 239.149 148.810 1.00 8.77  ? 3556 ALA A CB    1 
ATOM   15115 N  N     . ASP A 1 3557 ? 203.317 236.267 150.319 1.00 7.69  ? 3557 ASP A N     1 
ATOM   15116 C  CA    . ASP A 1 3557 ? 202.723 234.959 150.567 1.00 8.14  ? 3557 ASP A CA    1 
ATOM   15117 C  C     . ASP A 1 3557 ? 202.345 234.792 152.033 1.00 11.75 ? 3557 ASP A C     1 
ATOM   15118 O  O     . ASP A 1 3557 ? 201.272 234.266 152.351 1.00 10.99 ? 3557 ASP A O     1 
ATOM   15119 C  CB    . ASP A 1 3557 ? 203.689 233.856 150.136 1.00 8.71  ? 3557 ASP A CB    1 
ATOM   15120 C  CG    . ASP A 1 3557 ? 203.825 233.760 148.631 1.00 18.04 ? 3557 ASP A CG    1 
ATOM   15121 O  OD1   . ASP A 1 3557 ? 202.837 234.038 147.926 1.00 20.73 ? 3557 ASP A OD1   1 
ATOM   15122 O  OD2   . ASP A 1 3557 ? 204.925 233.408 148.154 1.00 24.65 ? 3557 ASP A OD2   1 
ATOM   15123 N  N     . GLU A 1 3558 ? 203.218 235.229 152.941 1.00 6.61  ? 3558 GLU A N     1 
ATOM   15124 C  CA    . GLU A 1 3558 ? 202.923 235.103 154.365 1.00 8.27  ? 3558 GLU A CA    1 
ATOM   15125 C  C     . GLU A 1 3558 ? 201.790 236.031 154.780 1.00 7.00  ? 3558 GLU A C     1 
ATOM   15126 O  O     . GLU A 1 3558 ? 200.956 235.665 155.616 1.00 5.82  ? 3558 GLU A O     1 
ATOM   15127 C  CB    . GLU A 1 3558 ? 204.179 235.384 155.185 1.00 9.08  ? 3558 GLU A CB    1 
ATOM   15128 C  CG    . GLU A 1 3558 ? 204.078 234.929 156.620 1.00 12.59 ? 3558 GLU A CG    1 
ATOM   15129 C  CD    . GLU A 1 3558 ? 205.414 234.939 157.331 1.00 23.28 ? 3558 GLU A CD    1 
ATOM   15130 O  OE1   . GLU A 1 3558 ? 206.331 235.653 156.871 1.00 19.86 ? 3558 GLU A OE1   1 
ATOM   15131 O  OE2   . GLU A 1 3558 ? 205.544 234.231 158.352 1.00 23.18 ? 3558 GLU A OE2   1 
ATOM   15132 N  N     . ARG A 1 3559 ? 201.746 237.237 154.213 1.00 7.36  ? 3559 ARG A N     1 
ATOM   15133 C  CA    . ARG A 1 3559 ? 200.662 238.161 154.526 1.00 5.65  ? 3559 ARG A CA    1 
ATOM   15134 C  C     . ARG A 1 3559 ? 199.322 237.633 154.030 1.00 6.32  ? 3559 ARG A C     1 
ATOM   15135 O  O     . ARG A 1 3559 ? 198.291 237.851 154.677 1.00 6.20  ? 3559 ARG A O     1 
ATOM   15136 C  CB    . ARG A 1 3559 ? 200.958 239.535 153.929 1.00 4.93  ? 3559 ARG A CB    1 
ATOM   15137 C  CG    . ARG A 1 3559 ? 202.113 240.253 154.604 1.00 4.91  ? 3559 ARG A CG    1 
ATOM   15138 C  CD    . ARG A 1 3559 ? 202.302 241.660 154.067 1.00 5.87  ? 3559 ARG A CD    1 
ATOM   15139 N  NE    . ARG A 1 3559 ? 202.574 241.671 152.635 1.00 8.35  ? 3559 ARG A NE    1 
ATOM   15140 C  CZ    . ARG A 1 3559 ? 203.737 242.010 152.096 1.00 9.09  ? 3559 ARG A CZ    1 
ATOM   15141 N  NH1   . ARG A 1 3559 ? 204.775 242.344 152.845 1.00 8.20  ? 3559 ARG A NH1   1 
ATOM   15142 N  NH2   . ARG A 1 3559 ? 203.863 242.008 150.773 1.00 10.16 ? 3559 ARG A NH2   1 
ATOM   15143 N  N     . LEU A 1 3560 ? 199.319 236.939 152.889 1.00 8.84  ? 3560 LEU A N     1 
ATOM   15144 C  CA    . LEU A 1 3560 ? 198.091 236.331 152.389 1.00 7.34  ? 3560 LEU A CA    1 
ATOM   15145 C  C     . LEU A 1 3560 ? 197.562 235.280 153.354 1.00 6.84  ? 3560 LEU A C     1 
ATOM   15146 O  O     . LEU A 1 3560 ? 196.355 235.208 153.607 1.00 10.63 ? 3560 LEU A O     1 
ATOM   15147 C  CB    . LEU A 1 3560 ? 198.338 235.721 151.010 1.00 11.81 ? 3560 LEU A CB    1 
ATOM   15148 C  CG    . LEU A 1 3560 ? 197.116 235.382 150.156 1.00 11.48 ? 3560 LEU A CG    1 
ATOM   15149 C  CD1   . LEU A 1 3560 ? 196.363 236.641 149.780 1.00 6.76  ? 3560 LEU A CD1   1 
ATOM   15150 C  CD2   . LEU A 1 3560 ? 197.534 234.613 148.916 1.00 16.65 ? 3560 LEU A CD2   1 
ATOM   15151 N  N     . ARG A 1 3561 ? 198.453 234.447 153.901 1.00 7.20  ? 3561 ARG A N     1 
ATOM   15152 C  CA    . ARG A 1 3561 ? 198.026 233.447 154.874 1.00 6.08  ? 3561 ARG A CA    1 
ATOM   15153 C  C     . ARG A 1 3561 ? 197.591 234.100 156.180 1.00 7.98  ? 3561 ARG A C     1 
ATOM   15154 O  O     . ARG A 1 3561 ? 196.645 233.637 156.826 1.00 10.14 ? 3561 ARG A O     1 
ATOM   15155 C  CB    . ARG A 1 3561 ? 199.149 232.440 155.122 1.00 8.03  ? 3561 ARG A CB    1 
ATOM   15156 C  CG    . ARG A 1 3561 ? 198.858 231.450 156.237 1.00 11.42 ? 3561 ARG A CG    1 
ATOM   15157 C  CD    . ARG A 1 3561 ? 199.990 230.453 156.414 1.00 15.34 ? 3561 ARG A CD    1 
ATOM   15158 N  NE    . ARG A 1 3561 ? 200.952 230.903 157.413 1.00 21.94 ? 3561 ARG A NE    1 
ATOM   15159 C  CZ    . ARG A 1 3561 ? 202.033 231.617 157.140 1.00 18.48 ? 3561 ARG A CZ    1 
ATOM   15160 N  NH1   . ARG A 1 3561 ? 202.340 231.961 155.902 1.00 18.53 ? 3561 ARG A NH1   1 
ATOM   15161 N  NH2   . ARG A 1 3561 ? 202.829 231.994 158.138 1.00 16.97 ? 3561 ARG A NH2   1 
ATOM   15162 N  N     . TRP A 1 3562 ? 198.266 235.181 156.582 1.00 7.73  ? 3562 TRP A N     1 
ATOM   15163 C  CA    . TRP A 1 3562 ? 197.890 235.879 157.807 1.00 5.92  ? 3562 TRP A CA    1 
ATOM   15164 C  C     . TRP A 1 3562 ? 196.462 236.400 157.724 1.00 6.99  ? 3562 TRP A C     1 
ATOM   15165 O  O     . TRP A 1 3562 ? 195.715 236.342 158.706 1.00 10.89 ? 3562 TRP A O     1 
ATOM   15166 C  CB    . TRP A 1 3562 ? 198.865 237.023 158.084 1.00 4.82  ? 3562 TRP A CB    1 
ATOM   15167 C  CG    . TRP A 1 3562 ? 200.200 236.576 158.581 1.00 3.37  ? 3562 TRP A CG    1 
ATOM   15168 C  CD1   . TRP A 1 3562 ? 200.520 235.346 159.077 1.00 3.72  ? 3562 TRP A CD1   1 
ATOM   15169 C  CD2   . TRP A 1 3562 ? 201.400 237.354 158.634 1.00 4.19  ? 3562 TRP A CD2   1 
ATOM   15170 N  NE1   . TRP A 1 3562 ? 201.845 235.310 159.432 1.00 4.59  ? 3562 TRP A NE1   1 
ATOM   15171 C  CE2   . TRP A 1 3562 ? 202.407 236.531 159.172 1.00 4.22  ? 3562 TRP A CE2   1 
ATOM   15172 C  CE3   . TRP A 1 3562 ? 201.721 238.667 158.277 1.00 3.11  ? 3562 TRP A CE3   1 
ATOM   15173 C  CZ2   . TRP A 1 3562 ? 203.712 236.979 159.365 1.00 2.30  ? 3562 TRP A CZ2   1 
ATOM   15174 C  CZ3   . TRP A 1 3562 ? 203.016 239.107 158.465 1.00 1.76  ? 3562 TRP A CZ3   1 
ATOM   15175 C  CH2   . TRP A 1 3562 ? 203.997 238.266 159.002 1.00 2.15  ? 3562 TRP A CH2   1 
ATOM   15176 N  N     . GLN A 1 3563 ? 196.066 236.909 156.557 1.00 8.43  ? 3563 GLN A N     1 
ATOM   15177 C  CA    . GLN A 1 3563 ? 194.686 237.342 156.369 1.00 6.83  ? 3563 GLN A CA    1 
ATOM   15178 C  C     . GLN A 1 3563 ? 193.718 236.175 156.518 1.00 6.47  ? 3563 GLN A C     1 
ATOM   15179 O  O     . GLN A 1 3563 ? 192.652 236.317 157.128 1.00 5.75  ? 3563 GLN A O     1 
ATOM   15180 C  CB    . GLN A 1 3563 ? 194.525 237.999 155.000 1.00 6.14  ? 3563 GLN A CB    1 
ATOM   15181 C  CG    . GLN A 1 3563 ? 194.604 239.511 155.027 1.00 12.68 ? 3563 GLN A CG    1 
ATOM   15182 C  CD    . GLN A 1 3563 ? 194.713 240.111 153.641 1.00 23.09 ? 3563 GLN A CD    1 
ATOM   15183 O  OE1   . GLN A 1 3563 ? 194.195 239.557 152.670 1.00 26.17 ? 3563 GLN A OE1   1 
ATOM   15184 N  NE2   . GLN A 1 3563 ? 195.392 241.249 153.541 1.00 25.82 ? 3563 GLN A NE2   1 
ATOM   15185 N  N     . ALA A 1 3564 ? 194.074 235.011 155.967 1.00 8.83  ? 3564 ALA A N     1 
ATOM   15186 C  CA    . ALA A 1 3564 ? 193.223 233.835 156.103 1.00 5.97  ? 3564 ALA A CA    1 
ATOM   15187 C  C     . ALA A 1 3564 ? 193.090 233.403 157.558 1.00 10.06 ? 3564 ALA A C     1 
ATOM   15188 O  O     . ALA A 1 3564 ? 192.082 232.797 157.937 1.00 13.24 ? 3564 ALA A O     1 
ATOM   15189 C  CB    . ALA A 1 3564 ? 193.773 232.690 155.256 1.00 4.41  ? 3564 ALA A CB    1 
ATOM   15190 N  N     . SER A 1 3565 ? 194.088 233.706 158.385 1.00 8.79  ? 3565 SER A N     1 
ATOM   15191 C  CA    . SER A 1 3565 ? 194.044 233.425 159.811 1.00 5.06  ? 3565 SER A CA    1 
ATOM   15192 C  C     . SER A 1 3565 ? 193.336 234.515 160.605 1.00 6.25  ? 3565 SER A C     1 
ATOM   15193 O  O     . SER A 1 3565 ? 193.501 234.574 161.830 1.00 9.36  ? 3565 SER A O     1 
ATOM   15194 C  CB    . SER A 1 3565 ? 195.460 233.217 160.352 1.00 8.86  ? 3565 SER A CB    1 
ATOM   15195 O  OG    . SER A 1 3565 ? 196.053 232.060 159.795 1.00 9.84  ? 3565 SER A OG    1 
ATOM   15196 N  N     . SER A 1 3566 ? 192.568 235.369 159.926 1.00 8.76  ? 3566 SER A N     1 
ATOM   15197 C  CA    . SER A 1 3566 ? 191.770 236.433 160.538 1.00 4.98  ? 3566 SER A CA    1 
ATOM   15198 C  C     . SER A 1 3566 ? 192.630 237.512 161.192 1.00 6.96  ? 3566 SER A C     1 
ATOM   15199 O  O     . SER A 1 3566 ? 192.213 238.133 162.170 1.00 12.94 ? 3566 SER A O     1 
ATOM   15200 C  CB    . SER A 1 3566 ? 190.765 235.873 161.552 1.00 7.34  ? 3566 SER A CB    1 
ATOM   15201 O  OG    . SER A 1 3566 ? 191.416 235.358 162.701 1.00 14.32 ? 3566 SER A OG    1 
ATOM   15202 N  N     . LEU A 1 3567 ? 193.826 237.750 160.666 1.00 5.84  ? 3567 LEU A N     1 
ATOM   15203 C  CA    . LEU A 1 3567 ? 194.611 238.890 161.126 1.00 5.35  ? 3567 LEU A CA    1 
ATOM   15204 C  C     . LEU A 1 3567 ? 194.078 240.170 160.492 1.00 8.28  ? 3567 LEU A C     1 
ATOM   15205 O  O     . LEU A 1 3567 ? 193.928 240.229 159.268 1.00 8.53  ? 3567 LEU A O     1 
ATOM   15206 C  CB    . LEU A 1 3567 ? 196.086 238.718 160.785 1.00 5.45  ? 3567 LEU A CB    1 
ATOM   15207 C  CG    . LEU A 1 3567 ? 197.007 239.821 161.314 1.00 3.99  ? 3567 LEU A CG    1 
ATOM   15208 C  CD1   . LEU A 1 3567 ? 197.316 239.608 162.788 1.00 3.37  ? 3567 LEU A CD1   1 
ATOM   15209 C  CD2   . LEU A 1 3567 ? 198.284 239.909 160.497 1.00 2.03  ? 3567 LEU A CD2   1 
ATOM   15210 N  N     . PRO A 1 3568 ? 193.778 241.201 161.282 1.00 5.04  ? 3568 PRO A N     1 
ATOM   15211 C  CA    . PRO A 1 3568 ? 193.236 242.438 160.710 1.00 4.15  ? 3568 PRO A CA    1 
ATOM   15212 C  C     . PRO A 1 3568 ? 194.182 243.057 159.691 1.00 7.98  ? 3568 PRO A C     1 
ATOM   15213 O  O     . PRO A 1 3568 ? 195.404 243.022 159.845 1.00 8.30  ? 3568 PRO A O     1 
ATOM   15214 C  CB    . PRO A 1 3568 ? 193.061 243.342 161.933 1.00 4.56  ? 3568 PRO A CB    1 
ATOM   15215 C  CG    . PRO A 1 3568 ? 192.921 242.400 163.075 1.00 4.72  ? 3568 PRO A CG    1 
ATOM   15216 C  CD    . PRO A 1 3568 ? 193.810 241.240 162.753 1.00 6.30  ? 3568 PRO A CD    1 
ATOM   15217 N  N     . ALA A 1 3569 ? 193.596 243.628 158.637 1.00 6.34  ? 3569 ALA A N     1 
ATOM   15218 C  CA    . ALA A 1 3569 ? 194.361 244.270 157.567 1.00 6.81  ? 3569 ALA A CA    1 
ATOM   15219 C  C     . ALA A 1 3569 ? 194.804 245.645 158.054 1.00 16.22 ? 3569 ALA A C     1 
ATOM   15220 O  O     . ALA A 1 3569 ? 194.223 246.682 157.725 1.00 23.37 ? 3569 ALA A O     1 
ATOM   15221 C  CB    . ALA A 1 3569 ? 193.537 244.357 156.290 1.00 9.26  ? 3569 ALA A CB    1 
ATOM   15222 N  N     . ASP A 1 3570 ? 195.863 245.641 158.861 1.00 10.40 ? 3570 ASP A N     1 
ATOM   15223 C  CA    . ASP A 1 3570 ? 196.373 246.847 159.493 1.00 6.54  ? 3570 ASP A CA    1 
ATOM   15224 C  C     . ASP A 1 3570 ? 197.886 246.731 159.596 1.00 5.75  ? 3570 ASP A C     1 
ATOM   15225 O  O     . ASP A 1 3570 ? 198.415 245.643 159.834 1.00 7.94  ? 3570 ASP A O     1 
ATOM   15226 C  CB    . ASP A 1 3570 ? 195.744 247.041 160.877 1.00 5.77  ? 3570 ASP A CB    1 
ATOM   15227 C  CG    . ASP A 1 3570 ? 196.280 248.255 161.597 1.00 8.40  ? 3570 ASP A CG    1 
ATOM   15228 O  OD1   . ASP A 1 3570 ? 196.349 249.334 160.974 1.00 14.26 ? 3570 ASP A OD1   1 
ATOM   15229 O  OD2   . ASP A 1 3570 ? 196.629 248.129 162.787 1.00 8.12  ? 3570 ASP A OD2   1 
ATOM   15230 N  N     . ASP A 1 3571 ? 198.579 247.858 159.412 1.00 3.97  ? 3571 ASP A N     1 
ATOM   15231 C  CA    . ASP A 1 3571 ? 200.038 247.838 159.427 1.00 5.34  ? 3571 ASP A CA    1 
ATOM   15232 C  C     . ASP A 1 3571 ? 200.579 247.437 160.794 1.00 3.73  ? 3571 ASP A C     1 
ATOM   15233 O  O     . ASP A 1 3571 ? 201.516 246.638 160.886 1.00 2.13  ? 3571 ASP A O     1 
ATOM   15234 C  CB    . ASP A 1 3571 ? 200.589 249.199 159.009 1.00 7.53  ? 3571 ASP A CB    1 
ATOM   15235 C  CG    . ASP A 1 3571 ? 200.737 249.328 157.509 1.00 14.52 ? 3571 ASP A CG    1 
ATOM   15236 O  OD1   . ASP A 1 3571 ? 200.396 248.364 156.793 1.00 10.68 ? 3571 ASP A OD1   1 
ATOM   15237 O  OD2   . ASP A 1 3571 ? 201.201 250.390 157.043 1.00 22.06 ? 3571 ASP A OD2   1 
ATOM   15238 N  N     . LEU A 1 3572 ? 200.002 247.981 161.867 1.00 3.63  ? 3572 LEU A N     1 
ATOM   15239 C  CA    . LEU A 1 3572 ? 200.445 247.605 163.206 1.00 2.53  ? 3572 LEU A CA    1 
ATOM   15240 C  C     . LEU A 1 3572 ? 200.151 246.135 163.489 1.00 1.91  ? 3572 LEU A C     1 
ATOM   15241 O  O     . LEU A 1 3572 ? 200.952 245.448 164.132 1.00 1.12  ? 3572 LEU A O     1 
ATOM   15242 C  CB    . LEU A 1 3572 ? 199.799 248.520 164.250 1.00 1.02  ? 3572 LEU A CB    1 
ATOM   15243 C  CG    . LEU A 1 3572 ? 200.262 248.421 165.708 1.00 1.27  ? 3572 LEU A CG    1 
ATOM   15244 C  CD1   . LEU A 1 3572 ? 200.087 249.751 166.404 1.00 1.25  ? 3572 LEU A CD1   1 
ATOM   15245 C  CD2   . LEU A 1 3572 ? 199.485 247.350 166.464 1.00 0.77  ? 3572 LEU A CD2   1 
ATOM   15246 N  N     . CYS A 1 3573 ? 199.006 245.637 163.019 1.00 1.82  ? 3573 CYS A N     1 
ATOM   15247 C  CA    . CYS A 1 3573 ? 198.712 244.215 163.158 1.00 1.94  ? 3573 CYS A CA    1 
ATOM   15248 C  C     . CYS A 1 3573 ? 199.691 243.367 162.353 1.00 1.20  ? 3573 CYS A C     1 
ATOM   15249 O  O     . CYS A 1 3573 ? 200.103 242.292 162.802 1.00 0.78  ? 3573 CYS A O     1 
ATOM   15250 C  CB    . CYS A 1 3573 ? 197.271 243.934 162.736 1.00 2.78  ? 3573 CYS A CB    1 
ATOM   15251 S  SG    . CYS A 1 3573 ? 196.037 244.507 163.924 1.00 14.26 ? 3573 CYS A SG    1 
ATOM   15252 N  N     . THR A 1 3574 ? 200.067 243.831 161.158 1.00 1.99  ? 3574 THR A N     1 
ATOM   15253 C  CA    . THR A 1 3574 ? 201.077 243.127 160.374 1.00 0.96  ? 3574 THR A CA    1 
ATOM   15254 C  C     . THR A 1 3574 ? 202.435 243.159 161.069 1.00 0.62  ? 3574 THR A C     1 
ATOM   15255 O  O     . THR A 1 3574 ? 203.171 242.166 161.052 1.00 1.00  ? 3574 THR A O     1 
ATOM   15256 C  CB    . THR A 1 3574 ? 201.170 243.736 158.975 1.00 0.77  ? 3574 THR A CB    1 
ATOM   15257 O  OG1   . THR A 1 3574 ? 199.878 243.707 158.358 1.00 7.14  ? 3574 THR A OG1   1 
ATOM   15258 C  CG2   . THR A 1 3574 ? 202.144 242.952 158.113 1.00 0.53  ? 3574 THR A CG2   1 
ATOM   15259 N  N     . GLU A 1 3575 ? 202.782 244.290 161.685 1.00 0.59  ? 3575 GLU A N     1 
ATOM   15260 C  CA    . GLU A 1 3575 ? 204.012 244.366 162.466 1.00 0.74  ? 3575 GLU A CA    1 
ATOM   15261 C  C     . GLU A 1 3575 ? 203.993 243.373 163.619 1.00 0.53  ? 3575 GLU A C     1 
ATOM   15262 O  O     . GLU A 1 3575 ? 205.013 242.744 163.927 1.00 0.54  ? 3575 GLU A O     1 
ATOM   15263 C  CB    . GLU A 1 3575 ? 204.215 245.786 162.993 1.00 0.77  ? 3575 GLU A CB    1 
ATOM   15264 C  CG    . GLU A 1 3575 ? 204.578 246.808 161.935 1.00 1.09  ? 3575 GLU A CG    1 
ATOM   15265 C  CD    . GLU A 1 3575 ? 204.505 248.236 162.446 1.00 3.16  ? 3575 GLU A CD    1 
ATOM   15266 O  OE1   . GLU A 1 3575 ? 204.087 248.440 163.604 1.00 3.90  ? 3575 GLU A OE1   1 
ATOM   15267 O  OE2   . GLU A 1 3575 ? 204.877 249.156 161.689 1.00 9.29  ? 3575 GLU A OE2   1 
ATOM   15268 N  N     . ASN A 1 3576 ? 202.843 243.229 164.278 1.00 0.43  ? 3576 ASN A N     1 
ATOM   15269 C  CA    . ASN A 1 3576 ? 202.718 242.267 165.367 1.00 0.33  ? 3576 ASN A CA    1 
ATOM   15270 C  C     . ASN A 1 3576 ? 202.897 240.838 164.872 1.00 0.36  ? 3576 ASN A C     1 
ATOM   15271 O  O     . ASN A 1 3576 ? 203.536 240.019 165.540 1.00 0.39  ? 3576 ASN A O     1 
ATOM   15272 C  CB    . ASN A 1 3576 ? 201.365 242.438 166.054 1.00 0.42  ? 3576 ASN A CB    1 
ATOM   15273 C  CG    . ASN A 1 3576 ? 201.274 243.725 166.841 1.00 0.26  ? 3576 ASN A CG    1 
ATOM   15274 O  OD1   . ASN A 1 3576 ? 202.208 244.518 166.855 1.00 0.67  ? 3576 ASN A OD1   1 
ATOM   15275 N  ND2   . ASN A 1 3576 ? 200.149 243.935 167.509 1.00 0.21  ? 3576 ASN A ND2   1 
ATOM   15276 N  N     . ALA A 1 3577 ? 202.338 240.521 163.701 1.00 0.37  ? 3577 ALA A N     1 
ATOM   15277 C  CA    . ALA A 1 3577 ? 202.492 239.184 163.140 1.00 0.29  ? 3577 ALA A CA    1 
ATOM   15278 C  C     . ALA A 1 3577 ? 203.956 238.865 162.863 1.00 0.46  ? 3577 ALA A C     1 
ATOM   15279 O  O     . ALA A 1 3577 ? 204.410 237.742 163.109 1.00 0.59  ? 3577 ALA A O     1 
ATOM   15280 C  CB    . ALA A 1 3577 ? 201.663 239.055 161.864 1.00 0.57  ? 3577 ALA A CB    1 
ATOM   15281 N  N     . ILE A 1 3578 ? 204.707 239.841 162.348 1.00 0.45  ? 3578 ILE A N     1 
ATOM   15282 C  CA    . ILE A 1 3578 ? 206.138 239.649 162.125 1.00 0.49  ? 3578 ILE A CA    1 
ATOM   15283 C  C     . ILE A 1 3578 ? 206.848 239.369 163.443 1.00 0.43  ? 3578 ILE A C     1 
ATOM   15284 O  O     . ILE A 1 3578 ? 207.727 238.501 163.520 1.00 0.50  ? 3578 ILE A O     1 
ATOM   15285 C  CB    . ILE A 1 3578 ? 206.729 240.877 161.409 1.00 0.79  ? 3578 ILE A CB    1 
ATOM   15286 C  CG1   . ILE A 1 3578 ? 206.046 241.082 160.058 1.00 0.56  ? 3578 ILE A CG1   1 
ATOM   15287 C  CG2   . ILE A 1 3578 ? 208.233 240.729 161.251 1.00 0.72  ? 3578 ILE A CG2   1 
ATOM   15288 C  CD1   . ILE A 1 3578 ? 206.481 242.327 159.333 1.00 1.22  ? 3578 ILE A CD1   1 
ATOM   15289 N  N     . MET A 1 3579 ? 206.481 240.099 164.496 1.00 0.31  ? 3579 MET A N     1 
ATOM   15290 C  CA    . MET A 1 3579 ? 207.044 239.846 165.817 1.00 0.24  ? 3579 MET A CA    1 
ATOM   15291 C  C     . MET A 1 3579 ? 206.686 238.457 166.324 1.00 0.24  ? 3579 MET A C     1 
ATOM   15292 O  O     . MET A 1 3579 ? 207.521 237.790 166.946 1.00 0.39  ? 3579 MET A O     1 
ATOM   15293 C  CB    . MET A 1 3579 ? 206.557 240.912 166.793 1.00 0.28  ? 3579 MET A CB    1 
ATOM   15294 C  CG    . MET A 1 3579 ? 207.059 242.298 166.473 1.00 0.25  ? 3579 MET A CG    1 
ATOM   15295 S  SD    . MET A 1 3579 ? 206.337 243.555 167.534 1.00 4.08  ? 3579 MET A SD    1 
ATOM   15296 C  CE    . MET A 1 3579 ? 206.945 245.045 166.751 1.00 0.36  ? 3579 MET A CE    1 
ATOM   15297 N  N     . LEU A 1 3580 ? 205.463 238.002 166.066 1.00 0.32  ? 3580 LEU A N     1 
ATOM   15298 C  CA    . LEU A 1 3580 ? 205.017 236.674 166.466 1.00 0.21  ? 3580 LEU A CA    1 
ATOM   15299 C  C     . LEU A 1 3580 ? 205.669 235.562 165.660 1.00 0.26  ? 3580 LEU A C     1 
ATOM   15300 O  O     . LEU A 1 3580 ? 205.492 234.388 166.000 1.00 1.01  ? 3580 LEU A O     1 
ATOM   15301 C  CB    . LEU A 1 3580 ? 203.494 236.575 166.349 1.00 0.31  ? 3580 LEU A CB    1 
ATOM   15302 C  CG    . LEU A 1 3580 ? 202.693 237.461 167.305 1.00 0.26  ? 3580 LEU A CG    1 
ATOM   15303 C  CD1   . LEU A 1 3580 ? 201.216 237.444 166.955 1.00 0.39  ? 3580 LEU A CD1   1 
ATOM   15304 C  CD2   . LEU A 1 3580 ? 202.910 237.024 168.741 1.00 0.20  ? 3580 LEU A CD2   1 
ATOM   15305 N  N     . LYS A 1 3581 ? 206.405 235.896 164.608 1.00 0.41  ? 3581 LYS A N     1 
ATOM   15306 C  CA    . LYS A 1 3581 ? 207.117 234.918 163.797 1.00 0.55  ? 3581 LYS A CA    1 
ATOM   15307 C  C     . LYS A 1 3581 ? 208.624 234.954 163.999 1.00 1.38  ? 3581 LYS A C     1 
ATOM   15308 O  O     . LYS A 1 3581 ? 209.260 233.899 164.019 1.00 5.00  ? 3581 LYS A O     1 
ATOM   15309 C  CB    . LYS A 1 3581 ? 206.790 235.142 162.312 1.00 0.85  ? 3581 LYS A CB    1 
ATOM   15310 C  CG    . LYS A 1 3581 ? 207.600 234.293 161.353 1.00 6.85  ? 3581 LYS A CG    1 
ATOM   15311 C  CD    . LYS A 1 3581 ? 207.994 235.086 160.119 1.00 13.46 ? 3581 LYS A CD    1 
ATOM   15312 C  CE    . LYS A 1 3581 ? 208.695 234.203 159.099 1.00 15.79 ? 3581 LYS A CE    1 
ATOM   15313 N  NZ    . LYS A 1 3581 ? 209.186 234.979 157.928 1.00 10.24 ? 3581 LYS A NZ    1 
ATOM   15314 N  N     . ARG A 1 3582 ? 209.210 236.139 164.170 1.00 1.84  ? 3582 ARG A N     1 
ATOM   15315 C  CA    . ARG A 1 3582 ? 210.657 236.297 164.281 1.00 2.32  ? 3582 ARG A CA    1 
ATOM   15316 C  C     . ARG A 1 3582 ? 211.124 236.490 165.720 1.00 1.10  ? 3582 ARG A C     1 
ATOM   15317 O  O     . ARG A 1 3582 ? 212.253 236.936 165.941 1.00 2.91  ? 3582 ARG A O     1 
ATOM   15318 C  CB    . ARG A 1 3582 ? 211.138 237.470 163.427 1.00 1.28  ? 3582 ARG A CB    1 
ATOM   15319 C  CG    . ARG A 1 3582 ? 210.848 237.358 161.949 1.00 1.41  ? 3582 ARG A CG    1 
ATOM   15320 C  CD    . ARG A 1 3582 ? 211.269 238.634 161.236 1.00 2.05  ? 3582 ARG A CD    1 
ATOM   15321 N  NE    . ARG A 1 3582 ? 211.105 238.566 159.789 1.00 7.44  ? 3582 ARG A NE    1 
ATOM   15322 C  CZ    . ARG A 1 3582 ? 211.773 237.747 158.987 1.00 5.77  ? 3582 ARG A CZ    1 
ATOM   15323 N  NH1   . ARG A 1 3582 ? 212.698 236.923 159.450 1.00 6.10  ? 3582 ARG A NH1   1 
ATOM   15324 N  NH2   . ARG A 1 3582 ? 211.512 237.763 157.683 1.00 4.92  ? 3582 ARG A NH2   1 
ATOM   15325 N  N     . PHE A 1 3583 ? 210.283 236.175 166.699 1.00 0.50  ? 3583 PHE A N     1 
ATOM   15326 C  CA    . PHE A 1 3583 ? 210.638 236.413 168.092 1.00 0.82  ? 3583 PHE A CA    1 
ATOM   15327 C  C     . PHE A 1 3583 ? 211.806 235.531 168.517 1.00 0.71  ? 3583 PHE A C     1 
ATOM   15328 O  O     . PHE A 1 3583 ? 211.961 234.402 168.042 1.00 1.00  ? 3583 PHE A O     1 
ATOM   15329 C  CB    . PHE A 1 3583 ? 209.438 236.149 169.002 1.00 0.31  ? 3583 PHE A CB    1 
ATOM   15330 C  CG    . PHE A 1 3583 ? 208.968 234.725 168.980 1.00 0.47  ? 3583 PHE A CG    1 
ATOM   15331 C  CD1   . PHE A 1 3583 ? 209.482 233.792 169.868 1.00 0.44  ? 3583 PHE A CD1   1 
ATOM   15332 C  CD2   . PHE A 1 3583 ? 208.016 234.311 168.063 1.00 0.41  ? 3583 PHE A CD2   1 
ATOM   15333 C  CE1   . PHE A 1 3583 ? 209.059 232.486 169.841 1.00 0.26  ? 3583 PHE A CE1   1 
ATOM   15334 C  CE2   . PHE A 1 3583 ? 207.585 233.006 168.036 1.00 0.41  ? 3583 PHE A CE2   1 
ATOM   15335 C  CZ    . PHE A 1 3583 ? 208.108 232.092 168.924 1.00 0.41  ? 3583 PHE A CZ    1 
ATOM   15336 N  N     . ASN A 1 3584 ? 212.632 236.057 169.416 1.00 1.16  ? 3584 ASN A N     1 
ATOM   15337 C  CA    . ASN A 1 3584 ? 213.624 235.252 170.117 1.00 2.34  ? 3584 ASN A CA    1 
ATOM   15338 C  C     . ASN A 1 3584 ? 213.126 234.880 171.509 1.00 1.67  ? 3584 ASN A C     1 
ATOM   15339 O  O     . ASN A 1 3584 ? 213.010 233.696 171.837 1.00 12.04 ? 3584 ASN A O     1 
ATOM   15340 C  CB    . ASN A 1 3584 ? 214.962 235.996 170.200 1.00 2.18  ? 3584 ASN A CB    1 
ATOM   15341 C  CG    . ASN A 1 3584 ? 215.587 236.219 168.842 1.00 4.13  ? 3584 ASN A CG    1 
ATOM   15342 O  OD1   . ASN A 1 3584 ? 215.478 235.379 167.949 1.00 11.52 ? 3584 ASN A OD1   1 
ATOM   15343 N  ND2   . ASN A 1 3584 ? 216.251 237.355 168.675 1.00 1.60  ? 3584 ASN A ND2   1 
ATOM   15344 N  N     . ARG A 1 3585 ? 212.819 235.877 172.329 1.00 0.67  ? 3585 ARG A N     1 
ATOM   15345 C  CA    . ARG A 1 3585 ? 212.088 235.635 173.560 1.00 0.56  ? 3585 ARG A CA    1 
ATOM   15346 C  C     . ARG A 1 3585 ? 210.632 235.335 173.235 1.00 0.33  ? 3585 ARG A C     1 
ATOM   15347 O  O     . ARG A 1 3585 ? 210.085 235.820 172.242 1.00 1.09  ? 3585 ARG A O     1 
ATOM   15348 C  CB    . ARG A 1 3585 ? 212.185 236.838 174.498 1.00 0.76  ? 3585 ARG A CB    1 
ATOM   15349 C  CG    . ARG A 1 3585 ? 213.566 237.058 175.092 1.00 0.92  ? 3585 ARG A CG    1 
ATOM   15350 C  CD    . ARG A 1 3585 ? 213.593 238.318 175.934 1.00 1.15  ? 3585 ARG A CD    1 
ATOM   15351 N  NE    . ARG A 1 3585 ? 213.305 239.506 175.142 1.00 0.36  ? 3585 ARG A NE    1 
ATOM   15352 C  CZ    . ARG A 1 3585 ? 213.205 240.732 175.636 1.00 0.22  ? 3585 ARG A CZ    1 
ATOM   15353 N  NH1   . ARG A 1 3585 ? 213.332 240.967 176.930 1.00 0.49  ? 3585 ARG A NH1   1 
ATOM   15354 N  NH2   . ARG A 1 3585 ? 212.962 241.746 174.812 1.00 0.36  ? 3585 ARG A NH2   1 
ATOM   15355 N  N     . TYR A 1 3586 ? 210.008 234.520 174.076 1.00 0.22  ? 3586 TYR A N     1 
ATOM   15356 C  CA    . TYR A 1 3586 ? 208.648 234.089 173.799 1.00 0.20  ? 3586 TYR A CA    1 
ATOM   15357 C  C     . TYR A 1 3586 ? 207.690 235.272 173.890 1.00 0.15  ? 3586 TYR A C     1 
ATOM   15358 O  O     . TYR A 1 3586 ? 207.844 236.134 174.761 1.00 0.16  ? 3586 TYR A O     1 
ATOM   15359 C  CB    . TYR A 1 3586 ? 208.228 232.980 174.765 1.00 0.14  ? 3586 TYR A CB    1 
ATOM   15360 C  CG    . TYR A 1 3586 ? 208.934 231.669 174.512 1.00 0.16  ? 3586 TYR A CG    1 
ATOM   15361 C  CD1   . TYR A 1 3586 ? 208.704 230.950 173.349 1.00 0.15  ? 3586 TYR A CD1   1 
ATOM   15362 C  CD2   . TYR A 1 3586 ? 209.829 231.147 175.439 1.00 0.34  ? 3586 TYR A CD2   1 
ATOM   15363 C  CE1   . TYR A 1 3586 ? 209.344 229.751 173.114 1.00 0.21  ? 3586 TYR A CE1   1 
ATOM   15364 C  CE2   . TYR A 1 3586 ? 210.473 229.949 175.212 1.00 0.28  ? 3586 TYR A CE2   1 
ATOM   15365 C  CZ    . TYR A 1 3586 ? 210.225 229.255 174.047 1.00 0.26  ? 3586 TYR A CZ    1 
ATOM   15366 O  OH    . TYR A 1 3586 ? 210.864 228.060 173.814 1.00 0.33  ? 3586 TYR A OH    1 
ATOM   15367 N  N     . PRO A 1 3587 ? 206.697 235.348 173.007 1.00 0.26  ? 3587 PRO A N     1 
ATOM   15368 C  CA    . PRO A 1 3587 ? 205.844 236.539 172.952 1.00 0.15  ? 3587 PRO A CA    1 
ATOM   15369 C  C     . PRO A 1 3587 ? 204.812 236.581 174.067 1.00 0.11  ? 3587 PRO A C     1 
ATOM   15370 O  O     . PRO A 1 3587 ? 204.170 235.581 174.395 1.00 0.10  ? 3587 PRO A O     1 
ATOM   15371 C  CB    . PRO A 1 3587 ? 205.158 236.415 171.583 1.00 0.12  ? 3587 PRO A CB    1 
ATOM   15372 C  CG    . PRO A 1 3587 ? 205.937 235.367 170.842 1.00 0.18  ? 3587 PRO A CG    1 
ATOM   15373 C  CD    . PRO A 1 3587 ? 206.418 234.433 171.894 1.00 0.09  ? 3587 PRO A CD    1 
ATOM   15374 N  N     . LEU A 1 3588 ? 204.660 237.764 174.653 1.00 0.17  ? 3588 LEU A N     1 
ATOM   15375 C  CA    . LEU A 1 3588 ? 203.529 238.080 175.514 1.00 0.16  ? 3588 LEU A CA    1 
ATOM   15376 C  C     . LEU A 1 3588 ? 202.578 238.961 174.716 1.00 0.11  ? 3588 LEU A C     1 
ATOM   15377 O  O     . LEU A 1 3588 ? 202.954 240.055 174.283 1.00 0.09  ? 3588 LEU A O     1 
ATOM   15378 C  CB    . LEU A 1 3588 ? 203.986 238.780 176.795 1.00 0.17  ? 3588 LEU A CB    1 
ATOM   15379 C  CG    . LEU A 1 3588 ? 203.042 238.760 178.003 1.00 0.21  ? 3588 LEU A CG    1 
ATOM   15380 C  CD1   . LEU A 1 3588 ? 203.816 239.036 179.280 1.00 0.26  ? 3588 LEU A CD1   1 
ATOM   15381 C  CD2   . LEU A 1 3588 ? 201.897 239.758 177.854 1.00 0.12  ? 3588 LEU A CD2   1 
ATOM   15382 N  N     . ILE A 1 3589 ? 201.352 238.487 174.521 1.00 0.21  ? 3589 ILE A N     1 
ATOM   15383 C  CA    . ILE A 1 3589 ? 200.383 239.140 173.650 1.00 0.30  ? 3589 ILE A CA    1 
ATOM   15384 C  C     . ILE A 1 3589 ? 199.403 239.937 174.496 1.00 0.27  ? 3589 ILE A C     1 
ATOM   15385 O  O     . ILE A 1 3589 ? 198.821 239.410 175.451 1.00 0.40  ? 3589 ILE A O     1 
ATOM   15386 C  CB    . ILE A 1 3589 ? 199.645 238.114 172.774 1.00 0.30  ? 3589 ILE A CB    1 
ATOM   15387 C  CG1   . ILE A 1 3589 ? 200.631 237.384 171.863 1.00 0.23  ? 3589 ILE A CG1   1 
ATOM   15388 C  CG2   . ILE A 1 3589 ? 198.555 238.791 171.965 1.00 0.37  ? 3589 ILE A CG2   1 
ATOM   15389 C  CD1   . ILE A 1 3589 ? 200.059 236.145 171.219 1.00 2.94  ? 3589 ILE A CD1   1 
ATOM   15390 N  N     . ILE A 1 3590 ? 199.226 241.205 174.150 1.00 0.38  ? 3590 ILE A N     1 
ATOM   15391 C  CA    . ILE A 1 3590 ? 198.232 242.070 174.772 1.00 0.77  ? 3590 ILE A CA    1 
ATOM   15392 C  C     . ILE A 1 3590 ? 197.193 242.387 173.704 1.00 1.48  ? 3590 ILE A C     1 
ATOM   15393 O  O     . ILE A 1 3590 ? 197.445 243.181 172.793 1.00 1.67  ? 3590 ILE A O     1 
ATOM   15394 C  CB    . ILE A 1 3590 ? 198.858 243.346 175.346 1.00 0.61  ? 3590 ILE A CB    1 
ATOM   15395 C  CG1   . ILE A 1 3590 ? 199.934 242.995 176.374 1.00 0.43  ? 3590 ILE A CG1   1 
ATOM   15396 C  CG2   . ILE A 1 3590 ? 197.788 244.231 175.959 1.00 1.80  ? 3590 ILE A CG2   1 
ATOM   15397 C  CD1   . ILE A 1 3590 ? 200.693 244.184 176.893 1.00 0.41  ? 3590 ILE A CD1   1 
ATOM   15398 N  N     . ASP A 1 3591 ? 196.022 241.762 173.804 1.00 1.68  ? 3591 ASP A N     1 
ATOM   15399 C  CA    . ASP A 1 3591 ? 194.929 242.006 172.865 1.00 3.20  ? 3591 ASP A CA    1 
ATOM   15400 C  C     . ASP A 1 3591 ? 193.608 242.059 173.617 1.00 3.31  ? 3591 ASP A C     1 
ATOM   15401 O  O     . ASP A 1 3591 ? 192.989 241.024 173.889 1.00 4.03  ? 3591 ASP A O     1 
ATOM   15402 C  CB    . ASP A 1 3591 ? 194.879 240.940 171.772 1.00 3.82  ? 3591 ASP A CB    1 
ATOM   15403 C  CG    . ASP A 1 3591 ? 193.944 241.317 170.641 1.00 8.52  ? 3591 ASP A CG    1 
ATOM   15404 O  OD1   . ASP A 1 3591 ? 193.546 242.499 170.570 1.00 10.22 ? 3591 ASP A OD1   1 
ATOM   15405 O  OD2   . ASP A 1 3591 ? 193.596 240.436 169.831 1.00 12.06 ? 3591 ASP A OD2   1 
ATOM   15406 N  N     . PRO A 1 3592 ? 193.147 243.259 173.972 1.00 3.19  ? 3592 PRO A N     1 
ATOM   15407 C  CA    . PRO A 1 3592 ? 191.826 243.370 174.610 1.00 4.75  ? 3592 PRO A CA    1 
ATOM   15408 C  C     . PRO A 1 3592 ? 190.685 242.876 173.735 1.00 6.01  ? 3592 PRO A C     1 
ATOM   15409 O  O     . PRO A 1 3592 ? 189.714 242.318 174.257 1.00 7.90  ? 3592 PRO A O     1 
ATOM   15410 C  CB    . PRO A 1 3592 ? 191.702 244.871 174.910 1.00 1.94  ? 3592 PRO A CB    1 
ATOM   15411 C  CG    . PRO A 1 3592 ? 192.713 245.536 174.042 1.00 3.70  ? 3592 PRO A CG    1 
ATOM   15412 C  CD    . PRO A 1 3592 ? 193.823 244.559 173.845 1.00 3.69  ? 3592 PRO A CD    1 
ATOM   15413 N  N     . SER A 1 3593 ? 190.776 243.060 172.417 1.00 6.03  ? 3593 SER A N     1 
ATOM   15414 C  CA    . SER A 1 3593 ? 189.681 242.659 171.539 1.00 9.42  ? 3593 SER A CA    1 
ATOM   15415 C  C     . SER A 1 3593 ? 189.640 241.146 171.348 1.00 10.19 ? 3593 SER A C     1 
ATOM   15416 O  O     . SER A 1 3593 ? 188.555 240.556 171.275 1.00 13.39 ? 3593 SER A O     1 
ATOM   15417 C  CB    . SER A 1 3593 ? 189.807 243.367 170.196 1.00 10.86 ? 3593 SER A CB    1 
ATOM   15418 O  OG    . SER A 1 3593 ? 190.801 242.751 169.396 1.00 10.22 ? 3593 SER A OG    1 
ATOM   15419 N  N     . GLY A 1 3594 ? 190.802 240.504 171.248 1.00 11.32 ? 3594 GLY A N     1 
ATOM   15420 C  CA    . GLY A 1 3594 ? 190.877 239.062 171.173 1.00 6.74  ? 3594 GLY A CA    1 
ATOM   15421 C  C     . GLY A 1 3594 ? 191.144 238.470 169.804 1.00 8.89  ? 3594 GLY A C     1 
ATOM   15422 O  O     . GLY A 1 3594 ? 191.135 237.239 169.678 1.00 11.12 ? 3594 GLY A O     1 
ATOM   15423 N  N     . GLN A 1 3595 ? 191.379 239.288 168.772 1.00 12.82 ? 3595 GLN A N     1 
ATOM   15424 C  CA    . GLN A 1 3595 ? 191.709 238.719 167.467 1.00 8.79  ? 3595 GLN A CA    1 
ATOM   15425 C  C     . GLN A 1 3595 ? 193.088 238.075 167.457 1.00 6.60  ? 3595 GLN A C     1 
ATOM   15426 O  O     . GLN A 1 3595 ? 193.311 237.114 166.715 1.00 8.68  ? 3595 GLN A O     1 
ATOM   15427 C  CB    . GLN A 1 3595 ? 191.626 239.773 166.356 1.00 11.35 ? 3595 GLN A CB    1 
ATOM   15428 C  CG    . GLN A 1 3595 ? 190.218 240.198 165.971 1.00 11.12 ? 3595 GLN A CG    1 
ATOM   15429 C  CD    . GLN A 1 3595 ? 189.526 241.006 167.036 1.00 20.16 ? 3595 GLN A CD    1 
ATOM   15430 O  OE1   . GLN A 1 3595 ? 189.985 242.081 167.419 1.00 27.60 ? 3595 GLN A OE1   1 
ATOM   15431 N  NE2   . GLN A 1 3595 ? 188.436 240.465 167.559 1.00 21.28 ? 3595 GLN A NE2   1 
ATOM   15432 N  N     . ALA A 1 3596 ? 194.027 238.595 168.251 1.00 7.64  ? 3596 ALA A N     1 
ATOM   15433 C  CA    . ALA A 1 3596 ? 195.357 237.998 168.303 1.00 4.09  ? 3596 ALA A CA    1 
ATOM   15434 C  C     . ALA A 1 3596 ? 195.299 236.570 168.827 1.00 4.17  ? 3596 ALA A C     1 
ATOM   15435 O  O     . ALA A 1 3596 ? 196.000 235.686 168.320 1.00 5.03  ? 3596 ALA A O     1 
ATOM   15436 C  CB    . ALA A 1 3596 ? 196.285 238.847 169.167 1.00 2.17  ? 3596 ALA A CB    1 
ATOM   15437 N  N     . THR A 1 3597 ? 194.472 236.328 169.845 1.00 5.65  ? 3597 THR A N     1 
ATOM   15438 C  CA    . THR A 1 3597 ? 194.280 234.969 170.339 1.00 6.72  ? 3597 THR A CA    1 
ATOM   15439 C  C     . THR A 1 3597 ? 193.741 234.064 169.242 1.00 7.31  ? 3597 THR A C     1 
ATOM   15440 O  O     . THR A 1 3597 ? 194.221 232.941 169.062 1.00 10.67 ? 3597 THR A O     1 
ATOM   15441 C  CB    . THR A 1 3597 ? 193.335 234.977 171.541 1.00 10.94 ? 3597 THR A CB    1 
ATOM   15442 O  OG1   . THR A 1 3597 ? 193.895 235.780 172.586 1.00 15.51 ? 3597 THR A OG1   1 
ATOM   15443 C  CG2   . THR A 1 3597 ? 193.107 233.566 172.058 1.00 11.43 ? 3597 THR A CG2   1 
ATOM   15444 N  N     . GLU A 1 3598 ? 192.749 234.544 168.490 1.00 8.07  ? 3598 GLU A N     1 
ATOM   15445 C  CA    . GLU A 1 3598 ? 192.228 233.769 167.371 1.00 6.12  ? 3598 GLU A CA    1 
ATOM   15446 C  C     . GLU A 1 3598 ? 193.285 233.570 166.293 1.00 7.43  ? 3598 GLU A C     1 
ATOM   15447 O  O     . GLU A 1 3598 ? 193.446 232.464 165.768 1.00 10.30 ? 3598 GLU A O     1 
ATOM   15448 C  CB    . GLU A 1 3598 ? 190.985 234.454 166.798 1.00 7.69  ? 3598 GLU A CB    1 
ATOM   15449 C  CG    . GLU A 1 3598 ? 190.123 233.578 165.896 1.00 14.84 ? 3598 GLU A CG    1 
ATOM   15450 C  CD    . GLU A 1 3598 ? 190.015 232.138 166.370 1.00 25.95 ? 3598 GLU A CD    1 
ATOM   15451 O  OE1   . GLU A 1 3598 ? 189.816 231.907 167.581 1.00 21.35 ? 3598 GLU A OE1   1 
ATOM   15452 O  OE2   . GLU A 1 3598 ? 190.129 231.230 165.520 1.00 22.59 ? 3598 GLU A OE2   1 
ATOM   15453 N  N     . PHE A 1 3599 ? 194.041 234.625 165.978 1.00 7.27  ? 3599 PHE A N     1 
ATOM   15454 C  CA    . PHE A 1 3599 ? 195.065 234.534 164.939 1.00 4.25  ? 3599 PHE A CA    1 
ATOM   15455 C  C     . PHE A 1 3599 ? 196.124 233.498 165.293 1.00 5.18  ? 3599 PHE A C     1 
ATOM   15456 O  O     . PHE A 1 3599 ? 196.572 232.738 164.426 1.00 5.79  ? 3599 PHE A O     1 
ATOM   15457 C  CB    . PHE A 1 3599 ? 195.702 235.908 164.721 1.00 4.26  ? 3599 PHE A CB    1 
ATOM   15458 C  CG    . PHE A 1 3599 ? 196.970 235.875 163.920 1.00 4.30  ? 3599 PHE A CG    1 
ATOM   15459 C  CD1   . PHE A 1 3599 ? 196.933 235.724 162.545 1.00 4.12  ? 3599 PHE A CD1   1 
ATOM   15460 C  CD2   . PHE A 1 3599 ? 198.201 236.003 164.545 1.00 2.21  ? 3599 PHE A CD2   1 
ATOM   15461 C  CE1   . PHE A 1 3599 ? 198.103 235.696 161.808 1.00 4.70  ? 3599 PHE A CE1   1 
ATOM   15462 C  CE2   . PHE A 1 3599 ? 199.370 235.976 163.815 1.00 1.12  ? 3599 PHE A CE2   1 
ATOM   15463 C  CZ    . PHE A 1 3599 ? 199.322 235.824 162.447 1.00 2.26  ? 3599 PHE A CZ    1 
ATOM   15464 N  N     . ILE A 1 3600 ? 196.541 233.456 166.559 1.00 4.40  ? 3600 ILE A N     1 
ATOM   15465 C  CA    . ILE A 1 3600 ? 197.527 232.471 166.986 1.00 4.31  ? 3600 ILE A CA    1 
ATOM   15466 C  C     . ILE A 1 3600 ? 196.968 231.059 166.848 1.00 6.18  ? 3600 ILE A C     1 
ATOM   15467 O  O     . ILE A 1 3600 ? 197.676 230.135 166.433 1.00 7.71  ? 3600 ILE A O     1 
ATOM   15468 C  CB    . ILE A 1 3600 ? 197.987 232.772 168.425 1.00 5.52  ? 3600 ILE A CB    1 
ATOM   15469 C  CG1   . ILE A 1 3600 ? 198.857 234.028 168.442 1.00 4.45  ? 3600 ILE A CG1   1 
ATOM   15470 C  CG2   . ILE A 1 3600 ? 198.754 231.599 169.007 1.00 2.21  ? 3600 ILE A CG2   1 
ATOM   15471 C  CD1   . ILE A 1 3600 ? 200.072 233.938 167.547 1.00 2.37  ? 3600 ILE A CD1   1 
ATOM   15472 N  N     . MET A 1 3601 ? 195.694 230.866 167.200 1.00 7.60  ? 3601 MET A N     1 
ATOM   15473 C  CA    . MET A 1 3601 ? 195.089 229.545 167.066 1.00 5.84  ? 3601 MET A CA    1 
ATOM   15474 C  C     . MET A 1 3601 ? 194.851 229.169 165.607 1.00 7.28  ? 3601 MET A C     1 
ATOM   15475 O  O     . MET A 1 3601 ? 194.986 227.996 165.243 1.00 14.88 ? 3601 MET A O     1 
ATOM   15476 C  CB    . MET A 1 3601 ? 193.794 229.471 167.872 1.00 5.98  ? 3601 MET A CB    1 
ATOM   15477 C  CG    . MET A 1 3601 ? 193.966 229.877 169.321 1.00 7.84  ? 3601 MET A CG    1 
ATOM   15478 S  SD    . MET A 1 3601 ? 194.873 228.636 170.270 1.00 21.30 ? 3601 MET A SD    1 
ATOM   15479 C  CE    . MET A 1 3601 ? 193.716 227.272 170.245 1.00 7.04  ? 3601 MET A CE    1 
ATOM   15480 N  N     . ASN A 1 3602 ? 194.491 230.136 164.754 1.00 9.78  ? 3602 ASN A N     1 
ATOM   15481 C  CA    . ASN A 1 3602 ? 194.376 229.828 163.332 1.00 6.64  ? 3602 ASN A CA    1 
ATOM   15482 C  C     . ASN A 1 3602 ? 195.727 229.436 162.745 1.00 7.14  ? 3602 ASN A C     1 
ATOM   15483 O  O     . ASN A 1 3602 ? 195.815 228.504 161.940 1.00 9.89  ? 3602 ASN A O     1 
ATOM   15484 C  CB    . ASN A 1 3602 ? 193.796 231.010 162.549 1.00 7.54  ? 3602 ASN A CB    1 
ATOM   15485 C  CG    . ASN A 1 3602 ? 192.378 231.359 162.953 1.00 12.53 ? 3602 ASN A CG    1 
ATOM   15486 O  OD1   . ASN A 1 3602 ? 192.118 232.437 163.487 1.00 19.00 ? 3602 ASN A OD1   1 
ATOM   15487 N  ND2   . ASN A 1 3602 ? 191.451 230.453 162.692 1.00 12.34 ? 3602 ASN A ND2   1 
ATOM   15488 N  N     . GLU A 1 3603 ? 196.791 230.134 163.147 1.00 7.68  ? 3603 GLU A N     1 
ATOM   15489 C  CA    . GLU A 1 3603 ? 198.097 229.919 162.535 1.00 7.25  ? 3603 GLU A CA    1 
ATOM   15490 C  C     . GLU A 1 3603 ? 198.711 228.587 162.947 1.00 7.55  ? 3603 GLU A C     1 
ATOM   15491 O  O     . GLU A 1 3603 ? 199.639 228.108 162.284 1.00 6.66  ? 3603 GLU A O     1 
ATOM   15492 C  CB    . GLU A 1 3603 ? 199.042 231.062 162.908 1.00 5.28  ? 3603 GLU A CB    1 
ATOM   15493 C  CG    . GLU A 1 3603 ? 198.993 232.243 161.962 1.00 3.68  ? 3603 GLU A CG    1 
ATOM   15494 C  CD    . GLU A 1 3603 ? 199.509 231.915 160.578 1.00 12.75 ? 3603 GLU A CD    1 
ATOM   15495 O  OE1   . GLU A 1 3603 ? 200.623 231.362 160.469 1.00 11.51 ? 3603 GLU A OE1   1 
ATOM   15496 O  OE2   . GLU A 1 3603 ? 198.794 232.203 159.596 1.00 15.42 ? 3603 GLU A OE2   1 
ATOM   15497 N  N     . TYR A 1 3604 ? 198.218 227.972 164.022 1.00 9.16  ? 3604 TYR A N     1 
ATOM   15498 C  CA    . TYR A 1 3604 ? 198.865 226.794 164.585 1.00 6.54  ? 3604 TYR A CA    1 
ATOM   15499 C  C     . TYR A 1 3604 ? 197.929 225.596 164.737 1.00 10.80 ? 3604 TYR A C     1 
ATOM   15500 O  O     . TYR A 1 3604 ? 198.201 224.717 165.561 1.00 13.95 ? 3604 TYR A O     1 
ATOM   15501 C  CB    . TYR A 1 3604 ? 199.502 227.139 165.933 1.00 6.79  ? 3604 TYR A CB    1 
ATOM   15502 C  CG    . TYR A 1 3604 ? 200.761 227.975 165.831 1.00 7.51  ? 3604 TYR A CG    1 
ATOM   15503 C  CD1   . TYR A 1 3604 ? 200.696 229.359 165.744 1.00 6.48  ? 3604 TYR A CD1   1 
ATOM   15504 C  CD2   . TYR A 1 3604 ? 202.013 227.379 165.818 1.00 6.05  ? 3604 TYR A CD2   1 
ATOM   15505 C  CE1   . TYR A 1 3604 ? 201.843 230.125 165.650 1.00 4.60  ? 3604 TYR A CE1   1 
ATOM   15506 C  CE2   . TYR A 1 3604 ? 203.163 228.134 165.726 1.00 6.12  ? 3604 TYR A CE2   1 
ATOM   15507 C  CZ    . TYR A 1 3604 ? 203.074 229.506 165.642 1.00 5.23  ? 3604 TYR A CZ    1 
ATOM   15508 O  OH    . TYR A 1 3604 ? 204.221 230.257 165.548 1.00 8.84  ? 3604 TYR A OH    1 
ATOM   15509 N  N     . LYS A 1 3605 ? 196.837 225.526 163.967 1.00 14.46 ? 3605 LYS A N     1 
ATOM   15510 C  CA    . LYS A 1 3605 ? 196.032 224.305 163.990 1.00 11.31 ? 3605 LYS A CA    1 
ATOM   15511 C  C     . LYS A 1 3605 ? 196.809 223.110 163.453 1.00 14.07 ? 3605 LYS A C     1 
ATOM   15512 O  O     . LYS A 1 3605 ? 196.738 222.014 164.022 1.00 22.45 ? 3605 LYS A O     1 
ATOM   15513 C  CB    . LYS A 1 3605 ? 194.729 224.459 163.205 1.00 10.48 ? 3605 LYS A CB    1 
ATOM   15514 C  CG    . LYS A 1 3605 ? 193.713 225.429 163.757 1.00 15.58 ? 3605 LYS A CG    1 
ATOM   15515 C  CD    . LYS A 1 3605 ? 192.480 225.428 162.860 1.00 21.10 ? 3605 LYS A CD    1 
ATOM   15516 C  CE    . LYS A 1 3605 ? 191.374 226.309 163.403 1.00 20.67 ? 3605 LYS A CE    1 
ATOM   15517 N  NZ    . LYS A 1 3605 ? 191.756 227.734 163.383 1.00 17.24 ? 3605 LYS A NZ    1 
ATOM   15518 N  N     . ASP A 1 3606 ? 197.549 223.294 162.355 1.00 10.48 ? 3606 ASP A N     1 
ATOM   15519 C  CA    . ASP A 1 3606 ? 198.260 222.169 161.761 1.00 14.66 ? 3606 ASP A CA    1 
ATOM   15520 C  C     . ASP A 1 3606 ? 199.304 221.588 162.702 1.00 15.64 ? 3606 ASP A C     1 
ATOM   15521 O  O     . ASP A 1 3606 ? 199.672 220.418 162.555 1.00 22.34 ? 3606 ASP A O     1 
ATOM   15522 C  CB    . ASP A 1 3606 ? 198.921 222.586 160.443 1.00 21.52 ? 3606 ASP A CB    1 
ATOM   15523 C  CG    . ASP A 1 3606 ? 199.894 223.740 160.608 1.00 25.50 ? 3606 ASP A CG    1 
ATOM   15524 O  OD1   . ASP A 1 3606 ? 200.033 224.256 161.737 1.00 17.37 ? 3606 ASP A OD1   1 
ATOM   15525 O  OD2   . ASP A 1 3606 ? 200.527 224.126 159.604 1.00 28.83 ? 3606 ASP A OD2   1 
ATOM   15526 N  N     . ARG A 1 3607 ? 199.776 222.374 163.664 1.00 17.84 ? 3607 ARG A N     1 
ATOM   15527 C  CA    . ARG A 1 3607 ? 200.730 221.916 164.662 1.00 9.91  ? 3607 ARG A CA    1 
ATOM   15528 C  C     . ARG A 1 3607 ? 200.067 221.583 165.993 1.00 13.24 ? 3607 ARG A C     1 
ATOM   15529 O  O     . ARG A 1 3607 ? 200.769 221.348 166.980 1.00 17.11 ? 3607 ARG A O     1 
ATOM   15530 C  CB    . ARG A 1 3607 ? 201.824 222.966 164.856 1.00 10.32 ? 3607 ARG A CB    1 
ATOM   15531 C  CG    . ARG A 1 3607 ? 202.899 222.921 163.781 1.00 9.95  ? 3607 ARG A CG    1 
ATOM   15532 C  CD    . ARG A 1 3607 ? 203.803 224.138 163.823 1.00 15.08 ? 3607 ARG A CD    1 
ATOM   15533 N  NE    . ARG A 1 3607 ? 203.221 225.301 163.166 1.00 21.26 ? 3607 ARG A NE    1 
ATOM   15534 C  CZ    . ARG A 1 3607 ? 203.873 226.433 162.936 1.00 20.02 ? 3607 ARG A CZ    1 
ATOM   15535 N  NH1   . ARG A 1 3607 ? 205.141 226.584 163.282 1.00 18.42 ? 3607 ARG A NH1   1 
ATOM   15536 N  NH2   . ARG A 1 3607 ? 203.236 227.441 162.346 1.00 11.78 ? 3607 ARG A NH2   1 
ATOM   15537 N  N     . LYS A 1 3608 ? 198.732 221.559 166.036 1.00 13.34 ? 3608 LYS A N     1 
ATOM   15538 C  CA    . LYS A 1 3608 ? 197.963 221.125 167.203 1.00 10.22 ? 3608 LYS A CA    1 
ATOM   15539 C  C     . LYS A 1 3608 ? 198.284 221.976 168.435 1.00 8.73  ? 3608 LYS A C     1 
ATOM   15540 O  O     . LYS A 1 3608 ? 198.820 221.497 169.435 1.00 18.00 ? 3608 LYS A O     1 
ATOM   15541 C  CB    . LYS A 1 3608 ? 198.188 219.635 167.486 1.00 17.19 ? 3608 LYS A CB    1 
ATOM   15542 C  CG    . LYS A 1 3608 ? 197.695 218.712 166.382 1.00 19.56 ? 3608 LYS A CG    1 
ATOM   15543 C  CD    . LYS A 1 3608 ? 197.884 217.246 166.751 1.00 21.36 ? 3608 LYS A CD    1 
ATOM   15544 C  CE    . LYS A 1 3608 ? 199.353 216.854 166.747 1.00 29.20 ? 3608 LYS A CE    1 
ATOM   15545 N  NZ    . LYS A 1 3608 ? 199.940 216.915 165.381 1.00 29.45 ? 3608 LYS A NZ    1 
ATOM   15546 N  N     . ILE A 1 3609 ? 197.938 223.256 168.345 1.00 8.26  ? 3609 ILE A N     1 
ATOM   15547 C  CA    . ILE A 1 3609 ? 198.123 224.177 169.460 1.00 5.65  ? 3609 ILE A CA    1 
ATOM   15548 C  C     . ILE A 1 3609 ? 196.997 223.983 170.465 1.00 5.85  ? 3609 ILE A C     1 
ATOM   15549 O  O     . ILE A 1 3609 ? 195.844 223.733 170.097 1.00 7.80  ? 3609 ILE A O     1 
ATOM   15550 C  CB    . ILE A 1 3609 ? 198.191 225.632 168.958 1.00 5.33  ? 3609 ILE A CB    1 
ATOM   15551 C  CG1   . ILE A 1 3609 ? 198.465 226.592 170.119 1.00 3.57  ? 3609 ILE A CG1   1 
ATOM   15552 C  CG2   . ILE A 1 3609 ? 196.909 226.018 168.229 1.00 5.13  ? 3609 ILE A CG2   1 
ATOM   15553 C  CD1   . ILE A 1 3609 ? 198.821 227.989 169.686 1.00 4.20  ? 3609 ILE A CD1   1 
ATOM   15554 N  N     . THR A 1 3610 ? 197.332 224.087 171.747 1.00 7.68  ? 3610 THR A N     1 
ATOM   15555 C  CA    . THR A 1 3610 ? 196.380 223.931 172.836 1.00 5.15  ? 3610 THR A CA    1 
ATOM   15556 C  C     . THR A 1 3610 ? 196.237 225.253 173.577 1.00 5.54  ? 3610 THR A C     1 
ATOM   15557 O  O     . THR A 1 3610 ? 197.239 225.884 173.928 1.00 9.14  ? 3610 THR A O     1 
ATOM   15558 C  CB    . THR A 1 3610 ? 196.829 222.832 173.803 1.00 4.31  ? 3610 THR A CB    1 
ATOM   15559 O  OG1   . THR A 1 3610 ? 196.927 221.586 173.102 1.00 7.50  ? 3610 THR A OG1   1 
ATOM   15560 C  CG2   . THR A 1 3610 ? 195.846 222.685 174.950 1.00 7.59  ? 3610 THR A CG2   1 
ATOM   15561 N  N     . ARG A 1 3611 ? 194.996 225.674 173.802 1.00 5.12  ? 3611 ARG A N     1 
ATOM   15562 C  CA    . ARG A 1 3611 ? 194.716 226.848 174.614 1.00 3.91  ? 3611 ARG A CA    1 
ATOM   15563 C  C     . ARG A 1 3611 ? 194.571 226.427 176.069 1.00 5.36  ? 3611 ARG A C     1 
ATOM   15564 O  O     . ARG A 1 3611 ? 193.879 225.449 176.374 1.00 15.64 ? 3611 ARG A O     1 
ATOM   15565 C  CB    . ARG A 1 3611 ? 193.441 227.555 174.150 1.00 4.69  ? 3611 ARG A CB    1 
ATOM   15566 C  CG    . ARG A 1 3611 ? 193.170 228.851 174.898 1.00 7.98  ? 3611 ARG A CG    1 
ATOM   15567 C  CD    . ARG A 1 3611 ? 191.894 229.546 174.449 1.00 14.10 ? 3611 ARG A CD    1 
ATOM   15568 N  NE    . ARG A 1 3611 ? 191.919 230.002 173.065 1.00 20.32 ? 3611 ARG A NE    1 
ATOM   15569 C  CZ    . ARG A 1 3611 ? 191.152 229.505 172.105 1.00 20.45 ? 3611 ARG A CZ    1 
ATOM   15570 N  NH1   . ARG A 1 3611 ? 190.320 228.504 172.335 1.00 23.34 ? 3611 ARG A NH1   1 
ATOM   15571 N  NH2   . ARG A 1 3611 ? 191.218 230.029 170.887 1.00 18.50 ? 3611 ARG A NH2   1 
ATOM   15572 N  N     . THR A 1 3612 ? 195.221 227.161 176.965 1.00 3.27  ? 3612 THR A N     1 
ATOM   15573 C  CA    . THR A 1 3612 ? 195.091 226.934 178.395 1.00 5.51  ? 3612 THR A CA    1 
ATOM   15574 C  C     . THR A 1 3612 ? 195.266 228.267 179.109 1.00 2.89  ? 3612 THR A C     1 
ATOM   15575 O  O     . THR A 1 3612 ? 195.429 229.315 178.479 1.00 3.10  ? 3612 THR A O     1 
ATOM   15576 C  CB    . THR A 1 3612 ? 196.097 225.884 178.892 1.00 7.11  ? 3612 THR A CB    1 
ATOM   15577 O  OG1   . THR A 1 3612 ? 195.835 225.582 180.268 1.00 9.32  ? 3612 THR A OG1   1 
ATOM   15578 C  CG2   . THR A 1 3612 ? 197.518 226.389 178.750 1.00 3.12  ? 3612 THR A CG2   1 
ATOM   15579 N  N     . SER A 1 3613 ? 195.226 228.225 180.435 1.00 3.14  ? 3613 SER A N     1 
ATOM   15580 C  CA    . SER A 1 3613 ? 195.339 229.427 181.245 1.00 3.47  ? 3613 SER A CA    1 
ATOM   15581 C  C     . SER A 1 3613 ? 196.152 229.123 182.492 1.00 4.65  ? 3613 SER A C     1 
ATOM   15582 O  O     . SER A 1 3613 ? 196.214 227.978 182.947 1.00 6.49  ? 3613 SER A O     1 
ATOM   15583 C  CB    . SER A 1 3613 ? 193.960 229.972 181.635 1.00 3.23  ? 3613 SER A CB    1 
ATOM   15584 O  OG    . SER A 1 3613 ? 194.054 230.872 182.723 1.00 6.20  ? 3613 SER A OG    1 
ATOM   15585 N  N     . PHE A 1 3614 ? 196.776 230.165 183.044 1.00 4.31  ? 3614 PHE A N     1 
ATOM   15586 C  CA    . PHE A 1 3614 ? 197.509 230.018 184.295 1.00 3.81  ? 3614 PHE A CA    1 
ATOM   15587 C  C     . PHE A 1 3614 ? 196.594 229.633 185.448 1.00 6.38  ? 3614 PHE A C     1 
ATOM   15588 O  O     . PHE A 1 3614 ? 197.070 229.080 186.446 1.00 11.38 ? 3614 PHE A O     1 
ATOM   15589 C  CB    . PHE A 1 3614 ? 198.244 231.312 184.639 1.00 3.77  ? 3614 PHE A CB    1 
ATOM   15590 C  CG    . PHE A 1 3614 ? 199.458 231.569 183.799 1.00 3.72  ? 3614 PHE A CG    1 
ATOM   15591 C  CD1   . PHE A 1 3614 ? 200.617 230.839 183.995 1.00 3.73  ? 3614 PHE A CD1   1 
ATOM   15592 C  CD2   . PHE A 1 3614 ? 199.450 232.560 182.831 1.00 2.08  ? 3614 PHE A CD2   1 
ATOM   15593 C  CE1   . PHE A 1 3614 ? 201.738 231.076 183.229 1.00 2.67  ? 3614 PHE A CE1   1 
ATOM   15594 C  CE2   . PHE A 1 3614 ? 200.572 232.805 182.062 1.00 1.98  ? 3614 PHE A CE2   1 
ATOM   15595 C  CZ    . PHE A 1 3614 ? 201.717 232.060 182.260 1.00 2.11  ? 3614 PHE A CZ    1 
ATOM   15596 N  N     . LEU A 1 3615 ? 195.299 229.921 185.337 1.00 8.68  ? 3615 LEU A N     1 
ATOM   15597 C  CA    . LEU A 1 3615 ? 194.337 229.629 186.387 1.00 8.26  ? 3615 LEU A CA    1 
ATOM   15598 C  C     . LEU A 1 3615 ? 193.718 228.245 186.263 1.00 9.07  ? 3615 LEU A C     1 
ATOM   15599 O  O     . LEU A 1 3615 ? 193.114 227.767 187.229 1.00 14.47 ? 3615 LEU A O     1 
ATOM   15600 C  CB    . LEU A 1 3615 ? 193.231 230.688 186.377 1.00 6.87  ? 3615 LEU A CB    1 
ATOM   15601 C  CG    . LEU A 1 3615 ? 193.743 232.124 186.498 1.00 9.46  ? 3615 LEU A CG    1 
ATOM   15602 C  CD1   . LEU A 1 3615 ? 192.674 233.115 186.087 1.00 6.64  ? 3615 LEU A CD1   1 
ATOM   15603 C  CD2   . LEU A 1 3615 ? 194.236 232.410 187.906 1.00 8.03  ? 3615 LEU A CD2   1 
ATOM   15604 N  N     . ASP A 1 3616 ? 193.849 227.595 185.112 1.00 7.58  ? 3616 ASP A N     1 
ATOM   15605 C  CA    . ASP A 1 3616 ? 193.290 226.264 184.932 1.00 8.73  ? 3616 ASP A CA    1 
ATOM   15606 C  C     . ASP A 1 3616 ? 194.041 225.247 185.784 1.00 16.33 ? 3616 ASP A C     1 
ATOM   15607 O  O     . ASP A 1 3616 ? 195.227 225.408 186.086 1.00 17.42 ? 3616 ASP A O     1 
ATOM   15608 C  CB    . ASP A 1 3616 ? 193.343 225.857 183.460 1.00 9.89  ? 3616 ASP A CB    1 
ATOM   15609 C  CG    . ASP A 1 3616 ? 192.361 226.630 182.603 1.00 17.71 ? 3616 ASP A CG    1 
ATOM   15610 O  OD1   . ASP A 1 3616 ? 191.783 227.619 183.103 1.00 21.75 ? 3616 ASP A OD1   1 
ATOM   15611 O  OD2   . ASP A 1 3616 ? 192.165 226.252 181.429 1.00 21.50 ? 3616 ASP A OD2   1 
ATOM   15612 N  N     . ASP A 1 3617 ? 193.329 224.194 186.187 1.00 19.37 ? 3617 ASP A N     1 
ATOM   15613 C  CA    . ASP A 1 3617 ? 193.948 223.148 186.991 1.00 16.10 ? 3617 ASP A CA    1 
ATOM   15614 C  C     . ASP A 1 3617 ? 194.880 222.266 186.175 1.00 13.80 ? 3617 ASP A C     1 
ATOM   15615 O  O     . ASP A 1 3617 ? 195.793 221.658 186.741 1.00 15.45 ? 3617 ASP A O     1 
ATOM   15616 C  CB    . ASP A 1 3617 ? 192.875 222.289 187.660 1.00 19.03 ? 3617 ASP A CB    1 
ATOM   15617 C  CG    . ASP A 1 3617 ? 193.452 221.322 188.675 1.00 30.97 ? 3617 ASP A CG    1 
ATOM   15618 O  OD1   . ASP A 1 3617 ? 193.691 221.738 189.828 1.00 35.45 ? 3617 ASP A OD1   1 
ATOM   15619 O  OD2   . ASP A 1 3617 ? 193.671 220.144 188.318 1.00 29.90 ? 3617 ASP A OD2   1 
ATOM   15620 N  N     . ALA A 1 3618 ? 194.678 222.190 184.862 1.00 18.20 ? 3618 ALA A N     1 
ATOM   15621 C  CA    . ALA A 1 3618 ? 195.469 221.329 183.995 1.00 15.18 ? 3618 ALA A CA    1 
ATOM   15622 C  C     . ALA A 1 3618 ? 196.656 222.047 183.374 1.00 15.11 ? 3618 ALA A C     1 
ATOM   15623 O  O     . ALA A 1 3618 ? 197.314 221.483 182.494 1.00 19.03 ? 3618 ALA A O     1 
ATOM   15624 C  CB    . ALA A 1 3618 ? 194.584 220.738 182.897 1.00 11.50 ? 3618 ALA A CB    1 
ATOM   15625 N  N     . PHE A 1 3619 ? 196.949 223.277 183.809 1.00 13.07 ? 3619 PHE A N     1 
ATOM   15626 C  CA    . PHE A 1 3619 ? 198.002 224.057 183.170 1.00 8.08  ? 3619 PHE A CA    1 
ATOM   15627 C  C     . PHE A 1 3619 ? 199.357 223.371 183.285 1.00 8.27  ? 3619 PHE A C     1 
ATOM   15628 O  O     . PHE A 1 3619 ? 200.121 223.330 182.313 1.00 11.84 ? 3619 PHE A O     1 
ATOM   15629 C  CB    . PHE A 1 3619 ? 198.067 225.460 183.773 1.00 8.08  ? 3619 PHE A CB    1 
ATOM   15630 C  CG    . PHE A 1 3619 ? 199.348 226.181 183.477 1.00 7.86  ? 3619 PHE A CG    1 
ATOM   15631 C  CD1   . PHE A 1 3619 ? 199.602 226.669 182.205 1.00 5.54  ? 3619 PHE A CD1   1 
ATOM   15632 C  CD2   . PHE A 1 3619 ? 200.303 226.360 184.461 1.00 5.18  ? 3619 PHE A CD2   1 
ATOM   15633 C  CE1   . PHE A 1 3619 ? 200.783 227.325 181.922 1.00 3.71  ? 3619 PHE A CE1   1 
ATOM   15634 C  CE2   . PHE A 1 3619 ? 201.485 227.017 184.183 1.00 7.24  ? 3619 PHE A CE2   1 
ATOM   15635 C  CZ    . PHE A 1 3619 ? 201.725 227.499 182.912 1.00 7.06  ? 3619 PHE A CZ    1 
ATOM   15636 N  N     . ARG A 1 3620 ? 199.680 222.836 184.464 1.00 7.68  ? 3620 ARG A N     1 
ATOM   15637 C  CA    . ARG A 1 3620 ? 200.957 222.150 184.633 1.00 7.02  ? 3620 ARG A CA    1 
ATOM   15638 C  C     . ARG A 1 3620 ? 201.036 220.912 183.749 1.00 8.06  ? 3620 ARG A C     1 
ATOM   15639 O  O     . ARG A 1 3620 ? 202.073 220.649 183.128 1.00 9.55  ? 3620 ARG A O     1 
ATOM   15640 C  CB    . ARG A 1 3620 ? 201.166 221.778 186.100 1.00 12.58 ? 3620 ARG A CB    1 
ATOM   15641 C  CG    . ARG A 1 3620 ? 201.330 222.968 187.024 1.00 14.27 ? 3620 ARG A CG    1 
ATOM   15642 C  CD    . ARG A 1 3620 ? 201.482 222.522 188.464 1.00 22.69 ? 3620 ARG A CD    1 
ATOM   15643 N  NE    . ARG A 1 3620 ? 202.706 221.757 188.658 1.00 30.30 ? 3620 ARG A NE    1 
ATOM   15644 C  CZ    . ARG A 1 3620 ? 203.884 222.294 188.946 1.00 25.05 ? 3620 ARG A CZ    1 
ATOM   15645 N  NH1   . ARG A 1 3620 ? 204.024 223.597 189.121 1.00 16.10 ? 3620 ARG A NH1   1 
ATOM   15646 N  NH2   . ARG A 1 3620 ? 204.945 221.503 189.070 1.00 21.82 ? 3620 ARG A NH2   1 
ATOM   15647 N  N     . LYS A 1 3621 ? 199.951 220.136 183.683 1.00 9.42  ? 3621 LYS A N     1 
ATOM   15648 C  CA    . LYS A 1 3621 ? 199.918 218.983 182.790 1.00 6.78  ? 3621 LYS A CA    1 
ATOM   15649 C  C     . LYS A 1 3621 ? 200.009 219.409 181.330 1.00 7.98  ? 3621 LYS A C     1 
ATOM   15650 O  O     . LYS A 1 3621 ? 200.734 218.790 180.543 1.00 11.77 ? 3621 LYS A O     1 
ATOM   15651 C  CB    . LYS A 1 3621 ? 198.646 218.171 183.028 1.00 10.94 ? 3621 LYS A CB    1 
ATOM   15652 C  CG    . LYS A 1 3621 ? 198.550 216.915 182.179 1.00 12.90 ? 3621 LYS A CG    1 
ATOM   15653 C  CD    . LYS A 1 3621 ? 197.324 216.092 182.536 1.00 24.77 ? 3621 LYS A CD    1 
ATOM   15654 C  CE    . LYS A 1 3621 ? 197.152 214.919 181.588 1.00 27.02 ? 3621 LYS A CE    1 
ATOM   15655 N  NZ    . LYS A 1 3621 ? 198.259 213.933 181.724 1.00 26.65 ? 3621 LYS A NZ    1 
ATOM   15656 N  N     . ASN A 1 3622 ? 199.274 220.457 180.951 1.00 6.52  ? 3622 ASN A N     1 
ATOM   15657 C  CA    . ASN A 1 3622 ? 199.323 220.937 179.573 1.00 6.96  ? 3622 ASN A CA    1 
ATOM   15658 C  C     . ASN A 1 3622 ? 200.711 221.456 179.221 1.00 4.90  ? 3622 ASN A C     1 
ATOM   15659 O  O     . ASN A 1 3622 ? 201.230 221.175 178.134 1.00 4.63  ? 3622 ASN A O     1 
ATOM   15660 C  CB    . ASN A 1 3622 ? 198.271 222.025 179.365 1.00 8.19  ? 3622 ASN A CB    1 
ATOM   15661 C  CG    . ASN A 1 3622 ? 196.857 221.491 179.463 1.00 12.36 ? 3622 ASN A CG    1 
ATOM   15662 O  OD1   . ASN A 1 3622 ? 196.636 220.282 179.439 1.00 15.64 ? 3622 ASN A OD1   1 
ATOM   15663 N  ND2   . ASN A 1 3622 ? 195.892 222.391 179.595 1.00 11.48 ? 3622 ASN A ND2   1 
ATOM   15664 N  N     . LEU A 1 3623 ? 201.326 222.212 180.132 1.00 4.07  ? 3623 LEU A N     1 
ATOM   15665 C  CA    . LEU A 1 3623 ? 202.677 222.713 179.898 1.00 2.71  ? 3623 LEU A CA    1 
ATOM   15666 C  C     . LEU A 1 3623 ? 203.678 221.572 179.772 1.00 4.78  ? 3623 LEU A C     1 
ATOM   15667 O  O     . LEU A 1 3623 ? 204.550 221.597 178.898 1.00 4.20  ? 3623 LEU A O     1 
ATOM   15668 C  CB    . LEU A 1 3623 ? 203.080 223.656 181.025 1.00 2.66  ? 3623 LEU A CB    1 
ATOM   15669 C  CG    . LEU A 1 3623 ? 204.541 224.105 181.027 1.00 3.49  ? 3623 LEU A CG    1 
ATOM   15670 C  CD1   . LEU A 1 3623 ? 204.876 224.910 179.773 1.00 3.34  ? 3623 LEU A CD1   1 
ATOM   15671 C  CD2   . LEU A 1 3623 ? 204.845 224.878 182.290 1.00 0.63  ? 3623 LEU A CD2   1 
ATOM   15672 N  N     . GLU A 1 3624 ? 203.569 220.565 180.642 1.00 7.05  ? 3624 GLU A N     1 
ATOM   15673 C  CA    . GLU A 1 3624 ? 204.462 219.414 180.560 1.00 6.87  ? 3624 GLU A CA    1 
ATOM   15674 C  C     . GLU A 1 3624 ? 204.278 218.665 179.246 1.00 5.91  ? 3624 GLU A C     1 
ATOM   15675 O  O     . GLU A 1 3624 ? 205.257 218.235 178.627 1.00 8.12  ? 3624 GLU A O     1 
ATOM   15676 C  CB    . GLU A 1 3624 ? 204.219 218.484 181.748 1.00 9.27  ? 3624 GLU A CB    1 
ATOM   15677 C  CG    . GLU A 1 3624 ? 205.114 217.261 181.777 1.00 14.99 ? 3624 GLU A CG    1 
ATOM   15678 C  CD    . GLU A 1 3624 ? 204.675 216.246 182.813 1.00 23.86 ? 3624 GLU A CD    1 
ATOM   15679 O  OE1   . GLU A 1 3624 ? 204.975 216.448 184.009 1.00 25.18 ? 3624 GLU A OE1   1 
ATOM   15680 O  OE2   . GLU A 1 3624 ? 204.027 215.250 182.433 1.00 18.92 ? 3624 GLU A OE2   1 
ATOM   15681 N  N     . SER A 1 3625 ? 203.029 218.495 178.812 1.00 7.18  ? 3625 SER A N     1 
ATOM   15682 C  CA    . SER A 1 3625 ? 202.763 217.798 177.558 1.00 5.72  ? 3625 SER A CA    1 
ATOM   15683 C  C     . SER A 1 3625 ? 203.304 218.573 176.362 1.00 6.05  ? 3625 SER A C     1 
ATOM   15684 O  O     . SER A 1 3625 ? 203.896 217.985 175.451 1.00 6.84  ? 3625 SER A O     1 
ATOM   15685 C  CB    . SER A 1 3625 ? 201.263 217.555 177.409 1.00 6.08  ? 3625 SER A CB    1 
ATOM   15686 O  OG    . SER A 1 3625 ? 200.968 216.911 176.185 1.00 14.65 ? 3625 SER A OG    1 
ATOM   15687 N  N     . ALA A 1 3626 ? 203.106 219.894 176.346 1.00 4.92  ? 3626 ALA A N     1 
ATOM   15688 C  CA    . ALA A 1 3626 ? 203.596 220.700 175.234 1.00 2.82  ? 3626 ALA A CA    1 
ATOM   15689 C  C     . ALA A 1 3626 ? 205.118 220.679 175.162 1.00 4.25  ? 3626 ALA A C     1 
ATOM   15690 O  O     . ALA A 1 3626 ? 205.694 220.595 174.072 1.00 3.55  ? 3626 ALA A O     1 
ATOM   15691 C  CB    . ALA A 1 3626 ? 203.081 222.133 175.359 1.00 1.82  ? 3626 ALA A CB    1 
ATOM   15692 N  N     . LEU A 1 3627 ? 205.786 220.763 176.315 1.00 3.24  ? 3627 LEU A N     1 
ATOM   15693 C  CA    . LEU A 1 3627 ? 207.244 220.701 176.334 1.00 1.91  ? 3627 LEU A CA    1 
ATOM   15694 C  C     . LEU A 1 3627 ? 207.745 219.335 175.878 1.00 5.45  ? 3627 LEU A C     1 
ATOM   15695 O  O     . LEU A 1 3627 ? 208.736 219.244 175.147 1.00 4.35  ? 3627 LEU A O     1 
ATOM   15696 C  CB    . LEU A 1 3627 ? 207.762 221.015 177.737 1.00 2.40  ? 3627 LEU A CB    1 
ATOM   15697 C  CG    . LEU A 1 3627 ? 207.607 222.444 178.257 1.00 1.79  ? 3627 LEU A CG    1 
ATOM   15698 C  CD1   . LEU A 1 3627 ? 207.656 222.449 179.778 1.00 2.81  ? 3627 LEU A CD1   1 
ATOM   15699 C  CD2   . LEU A 1 3627 ? 208.671 223.354 177.683 1.00 0.36  ? 3627 LEU A CD2   1 
ATOM   15700 N  N     . ARG A 1 3628 ? 207.070 218.263 176.300 1.00 4.92  ? 3628 ARG A N     1 
ATOM   15701 C  CA    . ARG A 1 3628 ? 207.541 216.917 175.994 1.00 4.58  ? 3628 ARG A CA    1 
ATOM   15702 C  C     . ARG A 1 3628 ? 207.338 216.573 174.525 1.00 4.36  ? 3628 ARG A C     1 
ATOM   15703 O  O     . ARG A 1 3628 ? 208.235 216.022 173.875 1.00 10.19 ? 3628 ARG A O     1 
ATOM   15704 C  CB    . ARG A 1 3628 ? 206.833 215.903 176.895 1.00 7.00  ? 3628 ARG A CB    1 
ATOM   15705 C  CG    . ARG A 1 3628 ? 207.175 214.455 176.598 1.00 6.56  ? 3628 ARG A CG    1 
ATOM   15706 C  CD    . ARG A 1 3628 ? 206.515 213.511 177.588 1.00 7.93  ? 3628 ARG A CD    1 
ATOM   15707 N  NE    . ARG A 1 3628 ? 207.191 213.537 178.879 1.00 15.20 ? 3628 ARG A NE    1 
ATOM   15708 C  CZ    . ARG A 1 3628 ? 206.669 214.038 179.989 1.00 9.34  ? 3628 ARG A CZ    1 
ATOM   15709 N  NH1   . ARG A 1 3628 ? 205.439 214.522 180.017 1.00 10.62 ? 3628 ARG A NH1   1 
ATOM   15710 N  NH2   . ARG A 1 3628 ? 207.399 214.053 181.101 1.00 10.21 ? 3628 ARG A NH2   1 
ATOM   15711 N  N     . PHE A 1 3629 ? 206.169 216.890 173.977 1.00 4.86  ? 3629 PHE A N     1 
ATOM   15712 C  CA    . PHE A 1 3629 ? 205.843 216.542 172.601 1.00 4.81  ? 3629 PHE A CA    1 
ATOM   15713 C  C     . PHE A 1 3629 ? 206.176 217.645 171.607 1.00 6.26  ? 3629 PHE A C     1 
ATOM   15714 O  O     . PHE A 1 3629 ? 206.042 217.428 170.399 1.00 10.45 ? 3629 PHE A O     1 
ATOM   15715 C  CB    . PHE A 1 3629 ? 204.361 216.176 172.491 1.00 5.62  ? 3629 PHE A CB    1 
ATOM   15716 C  CG    . PHE A 1 3629 ? 203.943 215.084 173.425 1.00 8.04  ? 3629 PHE A CG    1 
ATOM   15717 C  CD1   . PHE A 1 3629 ? 204.691 213.922 173.528 1.00 9.53  ? 3629 PHE A CD1   1 
ATOM   15718 C  CD2   . PHE A 1 3629 ? 202.814 215.221 174.213 1.00 5.85  ? 3629 PHE A CD2   1 
ATOM   15719 C  CE1   . PHE A 1 3629 ? 204.315 212.915 174.395 1.00 10.82 ? 3629 PHE A CE1   1 
ATOM   15720 C  CE2   . PHE A 1 3629 ? 202.434 214.215 175.080 1.00 12.50 ? 3629 PHE A CE2   1 
ATOM   15721 C  CZ    . PHE A 1 3629 ? 203.187 213.061 175.171 1.00 8.70  ? 3629 PHE A CZ    1 
ATOM   15722 N  N     . GLY A 1 3630 ? 206.615 218.808 172.076 1.00 5.80  ? 3630 GLY A N     1 
ATOM   15723 C  CA    . GLY A 1 3630 ? 206.922 219.913 171.187 1.00 5.29  ? 3630 GLY A CA    1 
ATOM   15724 C  C     . GLY A 1 3630 ? 205.725 220.504 170.477 1.00 6.50  ? 3630 GLY A C     1 
ATOM   15725 O  O     . GLY A 1 3630 ? 205.807 220.805 169.279 1.00 8.41  ? 3630 GLY A O     1 
ATOM   15726 N  N     . ASN A 1 3631 ? 204.627 220.674 171.174 1.00 4.32  ? 3631 ASN A N     1 
ATOM   15727 C  CA    . ASN A 1 3631 ? 203.472 221.294 170.556 1.00 4.82  ? 3631 ASN A CA    1 
ATOM   15728 C  C     . ASN A 1 3631 ? 203.352 222.753 170.981 1.00 4.45  ? 3631 ASN A C     1 
ATOM   15729 O  O     . ASN A 1 3631 ? 203.734 223.112 172.099 1.00 3.21  ? 3631 ASN A O     1 
ATOM   15730 C  CB    . ASN A 1 3631 ? 202.188 220.551 170.933 1.00 7.21  ? 3631 ASN A CB    1 
ATOM   15731 C  CG    . ASN A 1 3631 ? 202.265 219.067 170.637 1.00 8.46  ? 3631 ASN A CG    1 
ATOM   15732 O  OD1   . ASN A 1 3631 ? 202.010 218.236 171.507 1.00 9.83  ? 3631 ASN A OD1   1 
ATOM   15733 N  ND2   . ASN A 1 3631 ? 202.619 218.725 169.405 1.00 9.10  ? 3631 ASN A ND2   1 
ATOM   15734 N  N     . PRO A 1 3632 ? 202.846 223.615 170.103 1.00 6.10  ? 3632 PRO A N     1 
ATOM   15735 C  CA    . PRO A 1 3632 ? 202.597 225.005 170.501 1.00 2.57  ? 3632 PRO A CA    1 
ATOM   15736 C  C     . PRO A 1 3632 ? 201.555 225.085 171.605 1.00 2.11  ? 3632 PRO A C     1 
ATOM   15737 O  O     . PRO A 1 3632 ? 200.572 224.340 171.616 1.00 6.47  ? 3632 PRO A O     1 
ATOM   15738 C  CB    . PRO A 1 3632 ? 202.105 225.664 169.207 1.00 3.12  ? 3632 PRO A CB    1 
ATOM   15739 C  CG    . PRO A 1 3632 ? 201.667 224.539 168.339 1.00 3.81  ? 3632 PRO A CG    1 
ATOM   15740 C  CD    . PRO A 1 3632 ? 202.538 223.381 168.686 1.00 5.45  ? 3632 PRO A CD    1 
ATOM   15741 N  N     . LEU A 1 3633 ? 201.779 226.003 172.541 1.00 1.12  ? 3633 LEU A N     1 
ATOM   15742 C  CA    . LEU A 1 3633 ? 200.884 226.205 173.671 1.00 1.14  ? 3633 LEU A CA    1 
ATOM   15743 C  C     . LEU A 1 3633 ? 200.560 227.684 173.792 1.00 0.97  ? 3633 LEU A C     1 
ATOM   15744 O  O     . LEU A 1 3633 ? 201.463 228.525 173.763 1.00 1.24  ? 3633 LEU A O     1 
ATOM   15745 C  CB    . LEU A 1 3633 ? 201.509 225.687 174.970 1.00 1.55  ? 3633 LEU A CB    1 
ATOM   15746 C  CG    . LEU A 1 3633 ? 200.620 225.683 176.216 1.00 1.37  ? 3633 LEU A CG    1 
ATOM   15747 C  CD1   . LEU A 1 3633 ? 199.456 224.724 176.050 1.00 2.39  ? 3633 LEU A CD1   1 
ATOM   15748 C  CD2   . LEU A 1 3633 ? 201.432 225.334 177.448 1.00 1.24  ? 3633 LEU A CD2   1 
ATOM   15749 N  N     . LEU A 1 3634 ? 199.276 227.998 173.921 1.00 1.16  ? 3634 LEU A N     1 
ATOM   15750 C  CA    . LEU A 1 3634 ? 198.813 229.359 174.163 1.00 0.93  ? 3634 LEU A CA    1 
ATOM   15751 C  C     . LEU A 1 3634 ? 198.246 229.424 175.575 1.00 1.53  ? 3634 LEU A C     1 
ATOM   15752 O  O     . LEU A 1 3634 ? 197.284 228.718 175.894 1.00 3.05  ? 3634 LEU A O     1 
ATOM   15753 C  CB    . LEU A 1 3634 ? 197.759 229.775 173.138 1.00 1.41  ? 3634 LEU A CB    1 
ATOM   15754 C  CG    . LEU A 1 3634 ? 197.034 231.090 173.428 1.00 2.16  ? 3634 LEU A CG    1 
ATOM   15755 C  CD1   . LEU A 1 3634 ? 198.010 232.257 173.468 1.00 0.70  ? 3634 LEU A CD1   1 
ATOM   15756 C  CD2   . LEU A 1 3634 ? 195.941 231.336 172.408 1.00 4.36  ? 3634 LEU A CD2   1 
ATOM   15757 N  N     . VAL A 1 3635 ? 198.838 230.269 176.412 1.00 0.77  ? 3635 VAL A N     1 
ATOM   15758 C  CA    . VAL A 1 3635 ? 198.455 230.372 177.815 1.00 1.37  ? 3635 VAL A CA    1 
ATOM   15759 C  C     . VAL A 1 3635 ? 197.890 231.768 178.040 1.00 1.07  ? 3635 VAL A C     1 
ATOM   15760 O  O     . VAL A 1 3635 ? 198.573 232.769 177.792 1.00 1.17  ? 3635 VAL A O     1 
ATOM   15761 C  CB    . VAL A 1 3635 ? 199.644 230.098 178.747 1.00 2.11  ? 3635 VAL A CB    1 
ATOM   15762 C  CG1   . VAL A 1 3635 ? 199.229 230.270 180.193 1.00 1.57  ? 3635 VAL A CG1   1 
ATOM   15763 C  CG2   . VAL A 1 3635 ? 200.224 228.720 178.495 1.00 1.49  ? 3635 VAL A CG2   1 
ATOM   15764 N  N     . GLN A 1 3636 ? 196.654 231.836 178.513 1.00 1.52  ? 3636 GLN A N     1 
ATOM   15765 C  CA    . GLN A 1 3636 ? 195.972 233.099 178.745 1.00 2.01  ? 3636 GLN A CA    1 
ATOM   15766 C  C     . GLN A 1 3636 ? 196.081 233.511 180.208 1.00 2.53  ? 3636 GLN A C     1 
ATOM   15767 O  O     . GLN A 1 3636 ? 196.577 232.768 181.059 1.00 5.37  ? 3636 GLN A O     1 
ATOM   15768 C  CB    . GLN A 1 3636 ? 194.502 233.003 178.324 1.00 3.76  ? 3636 GLN A CB    1 
ATOM   15769 C  CG    . GLN A 1 3636 ? 194.300 232.614 176.870 1.00 6.47  ? 3636 GLN A CG    1 
ATOM   15770 C  CD    . GLN A 1 3636 ? 192.840 232.598 176.465 1.00 13.12 ? 3636 GLN A CD    1 
ATOM   15771 O  OE1   . GLN A 1 3636 ? 192.435 233.296 175.537 1.00 16.82 ? 3636 GLN A OE1   1 
ATOM   15772 N  NE2   . GLN A 1 3636 ? 192.041 231.804 177.165 1.00 15.98 ? 3636 GLN A NE2   1 
ATOM   15773 N  N     . ASP A 1 3637 ? 195.610 234.729 180.486 1.00 3.11  ? 3637 ASP A N     1 
ATOM   15774 C  CA    . ASP A 1 3637 ? 195.589 235.296 181.835 1.00 5.61  ? 3637 ASP A CA    1 
ATOM   15775 C  C     . ASP A 1 3637 ? 196.999 235.391 182.419 1.00 5.52  ? 3637 ASP A C     1 
ATOM   15776 O  O     . ASP A 1 3637 ? 197.273 234.931 183.528 1.00 9.80  ? 3637 ASP A O     1 
ATOM   15777 C  CB    . ASP A 1 3637 ? 194.661 234.493 182.754 1.00 5.78  ? 3637 ASP A CB    1 
ATOM   15778 C  CG    . ASP A 1 3637 ? 193.288 234.271 182.144 1.00 8.82  ? 3637 ASP A CG    1 
ATOM   15779 O  OD1   . ASP A 1 3637 ? 192.593 235.266 181.853 1.00 12.68 ? 3637 ASP A OD1   1 
ATOM   15780 O  OD2   . ASP A 1 3637 ? 192.902 233.101 181.950 1.00 11.12 ? 3637 ASP A OD2   1 
ATOM   15781 N  N     . VAL A 1 3638 ? 197.899 236.016 181.657 1.00 4.02  ? 3638 VAL A N     1 
ATOM   15782 C  CA    . VAL A 1 3638 ? 199.286 236.159 182.084 1.00 3.11  ? 3638 VAL A CA    1 
ATOM   15783 C  C     . VAL A 1 3638 ? 199.440 237.143 183.235 1.00 2.74  ? 3638 VAL A C     1 
ATOM   15784 O  O     . VAL A 1 3638 ? 200.520 237.228 183.828 1.00 4.92  ? 3638 VAL A O     1 
ATOM   15785 C  CB    . VAL A 1 3638 ? 200.162 236.558 180.875 1.00 1.79  ? 3638 VAL A CB    1 
ATOM   15786 C  CG1   . VAL A 1 3638 ? 199.935 238.008 180.493 1.00 2.15  ? 3638 VAL A CG1   1 
ATOM   15787 C  CG2   . VAL A 1 3638 ? 201.638 236.270 181.144 1.00 1.61  ? 3638 VAL A CG2   1 
ATOM   15788 N  N     . GLU A 1 3639 ? 198.381 237.882 183.576 1.00 3.62  ? 3639 GLU A N     1 
ATOM   15789 C  CA    . GLU A 1 3639 ? 198.390 238.681 184.796 1.00 6.21  ? 3639 GLU A CA    1 
ATOM   15790 C  C     . GLU A 1 3639 ? 198.516 237.811 186.039 1.00 5.77  ? 3639 GLU A C     1 
ATOM   15791 O  O     . GLU A 1 3639 ? 198.944 238.301 187.089 1.00 8.89  ? 3639 GLU A O     1 
ATOM   15792 C  CB    . GLU A 1 3639 ? 197.121 239.532 184.881 1.00 3.50  ? 3639 GLU A CB    1 
ATOM   15793 C  CG    . GLU A 1 3639 ? 195.824 238.762 184.657 1.00 6.24  ? 3639 GLU A CG    1 
ATOM   15794 C  CD    . GLU A 1 3639 ? 195.445 238.632 183.190 1.00 11.10 ? 3639 GLU A CD    1 
ATOM   15795 O  OE1   . GLU A 1 3639 ? 196.350 238.564 182.335 1.00 6.55  ? 3639 GLU A OE1   1 
ATOM   15796 O  OE2   . GLU A 1 3639 ? 194.234 238.595 182.894 1.00 17.44 ? 3639 GLU A OE2   1 
ATOM   15797 N  N     . SER A 1 3640 ? 198.148 236.536 185.940 1.00 3.31  ? 3640 SER A N     1 
ATOM   15798 C  CA    . SER A 1 3640 ? 198.327 235.549 187.000 1.00 4.92  ? 3640 SER A CA    1 
ATOM   15799 C  C     . SER A 1 3640 ? 199.506 234.632 186.706 1.00 5.38  ? 3640 SER A C     1 
ATOM   15800 O  O     . SER A 1 3640 ? 199.435 233.422 186.930 1.00 6.10  ? 3640 SER A O     1 
ATOM   15801 C  CB    . SER A 1 3640 ? 197.050 234.738 187.193 1.00 5.50  ? 3640 SER A CB    1 
ATOM   15802 O  OG    . SER A 1 3640 ? 195.978 235.572 187.596 1.00 12.01 ? 3640 SER A OG    1 
ATOM   15803 N  N     . TYR A 1 3641 ? 200.593 235.203 186.186 1.00 4.37  ? 3641 TYR A N     1 
ATOM   15804 C  CA    . TYR A 1 3641 ? 201.724 234.422 185.695 1.00 2.29  ? 3641 TYR A CA    1 
ATOM   15805 C  C     . TYR A 1 3641 ? 202.257 233.470 186.760 1.00 5.43  ? 3641 TYR A C     1 
ATOM   15806 O  O     . TYR A 1 3641 ? 202.485 233.860 187.909 1.00 8.00  ? 3641 TYR A O     1 
ATOM   15807 C  CB    . TYR A 1 3641 ? 202.833 235.364 185.228 1.00 2.27  ? 3641 TYR A CB    1 
ATOM   15808 C  CG    . TYR A 1 3641 ? 204.146 234.679 184.931 1.00 1.92  ? 3641 TYR A CG    1 
ATOM   15809 C  CD1   . TYR A 1 3641 ? 204.339 233.991 183.742 1.00 1.25  ? 3641 TYR A CD1   1 
ATOM   15810 C  CD2   . TYR A 1 3641 ? 205.194 234.723 185.841 1.00 0.80  ? 3641 TYR A CD2   1 
ATOM   15811 C  CE1   . TYR A 1 3641 ? 205.535 233.365 183.468 1.00 1.50  ? 3641 TYR A CE1   1 
ATOM   15812 C  CE2   . TYR A 1 3641 ? 206.392 234.101 185.575 1.00 1.37  ? 3641 TYR A CE2   1 
ATOM   15813 C  CZ    . TYR A 1 3641 ? 206.559 233.424 184.389 1.00 1.55  ? 3641 TYR A CZ    1 
ATOM   15814 O  OH    . TYR A 1 3641 ? 207.753 232.802 184.120 1.00 1.69  ? 3641 TYR A OH    1 
ATOM   15815 N  N     . ASP A 1 3642 ? 202.462 232.218 186.362 1.00 4.89  ? 3642 ASP A N     1 
ATOM   15816 C  CA    . ASP A 1 3642 ? 202.995 231.199 187.253 1.00 3.24  ? 3642 ASP A CA    1 
ATOM   15817 C  C     . ASP A 1 3642 ? 204.508 231.147 187.104 1.00 2.84  ? 3642 ASP A C     1 
ATOM   15818 O  O     . ASP A 1 3642 ? 204.999 230.888 185.997 1.00 1.48  ? 3642 ASP A O     1 
ATOM   15819 C  CB    . ASP A 1 3642 ? 202.384 229.844 186.929 1.00 6.12  ? 3642 ASP A CB    1 
ATOM   15820 C  CG    . ASP A 1 3642 ? 202.529 228.846 188.060 1.00 8.14  ? 3642 ASP A CG    1 
ATOM   15821 O  OD1   . ASP A 1 3642 ? 203.157 229.176 189.084 1.00 9.76  ? 3642 ASP A OD1   1 
ATOM   15822 O  OD2   . ASP A 1 3642 ? 202.001 227.723 187.926 1.00 12.16 ? 3642 ASP A OD2   1 
ATOM   15823 N  N     . PRO A 1 3643 ? 205.282 231.381 188.170 1.00 4.52  ? 3643 PRO A N     1 
ATOM   15824 C  CA    . PRO A 1 3643 ? 206.746 231.420 188.033 1.00 2.38  ? 3643 PRO A CA    1 
ATOM   15825 C  C     . PRO A 1 3643 ? 207.364 230.078 187.670 1.00 3.32  ? 3643 PRO A C     1 
ATOM   15826 O  O     . PRO A 1 3643 ? 208.588 229.965 187.569 1.00 6.83  ? 3643 PRO A O     1 
ATOM   15827 C  CB    . PRO A 1 3643 ? 207.213 231.888 189.418 1.00 3.56  ? 3643 PRO A CB    1 
ATOM   15828 C  CG    . PRO A 1 3643 ? 206.023 232.546 190.021 1.00 4.21  ? 3643 PRO A CG    1 
ATOM   15829 C  CD    . PRO A 1 3643 ? 204.849 231.782 189.517 1.00 2.73  ? 3643 PRO A CD    1 
ATOM   15830 N  N     . VAL A 1 3644 ? 206.530 229.055 187.476 1.00 4.27  ? 3644 VAL A N     1 
ATOM   15831 C  CA    . VAL A 1 3644 ? 207.021 227.756 187.037 1.00 3.02  ? 3644 VAL A CA    1 
ATOM   15832 C  C     . VAL A 1 3644 ? 207.586 227.825 185.623 1.00 4.40  ? 3644 VAL A C     1 
ATOM   15833 O  O     . VAL A 1 3644 ? 208.382 226.965 185.233 1.00 11.75 ? 3644 VAL A O     1 
ATOM   15834 C  CB    . VAL A 1 3644 ? 205.894 226.704 187.151 1.00 5.20  ? 3644 VAL A CB    1 
ATOM   15835 C  CG1   . VAL A 1 3644 ? 204.848 226.904 186.059 1.00 6.44  ? 3644 VAL A CG1   1 
ATOM   15836 C  CG2   . VAL A 1 3644 ? 206.460 225.295 187.124 1.00 6.46  ? 3644 VAL A CG2   1 
ATOM   15837 N  N     . LEU A 1 3645 ? 207.205 228.841 184.844 1.00 2.45  ? 3645 LEU A N     1 
ATOM   15838 C  CA    . LEU A 1 3645 ? 207.742 229.035 183.502 1.00 3.23  ? 3645 LEU A CA    1 
ATOM   15839 C  C     . LEU A 1 3645 ? 209.085 229.746 183.468 1.00 1.90  ? 3645 LEU A C     1 
ATOM   15840 O  O     . LEU A 1 3645 ? 209.631 229.923 182.375 1.00 3.07  ? 3645 LEU A O     1 
ATOM   15841 C  CB    . LEU A 1 3645 ? 206.770 229.829 182.625 1.00 4.10  ? 3645 LEU A CB    1 
ATOM   15842 C  CG    . LEU A 1 3645 ? 205.455 229.202 182.192 1.00 1.69  ? 3645 LEU A CG    1 
ATOM   15843 C  CD1   . LEU A 1 3645 ? 204.619 230.230 181.464 1.00 1.95  ? 3645 LEU A CD1   1 
ATOM   15844 C  CD2   . LEU A 1 3645 ? 205.791 228.068 181.262 1.00 0.79  ? 3645 LEU A CD2   1 
ATOM   15845 N  N     . ASN A 1 3646 ? 209.616 230.171 184.613 1.00 2.79  ? 3646 ASN A N     1 
ATOM   15846 C  CA    . ASN A 1 3646 ? 210.870 230.920 184.605 1.00 2.01  ? 3646 ASN A CA    1 
ATOM   15847 C  C     . ASN A 1 3646 ? 211.998 230.180 183.897 1.00 1.97  ? 3646 ASN A C     1 
ATOM   15848 O  O     . ASN A 1 3646 ? 212.667 230.796 183.048 1.00 2.50  ? 3646 ASN A O     1 
ATOM   15849 C  CB    . ASN A 1 3646 ? 211.255 231.298 186.041 1.00 1.30  ? 3646 ASN A CB    1 
ATOM   15850 C  CG    . ASN A 1 3646 ? 210.477 232.486 186.558 1.00 1.12  ? 3646 ASN A CG    1 
ATOM   15851 O  OD1   . ASN A 1 3646 ? 209.676 233.076 185.839 1.00 2.33  ? 3646 ASN A OD1   1 
ATOM   15852 N  ND2   . ASN A 1 3646 ? 210.712 232.847 187.812 1.00 2.58  ? 3646 ASN A ND2   1 
ATOM   15853 N  N     . PRO A 1 3647 ? 212.269 228.898 184.169 1.00 2.48  ? 3647 PRO A N     1 
ATOM   15854 C  CA    . PRO A 1 3647 ? 213.285 228.196 183.367 1.00 2.50  ? 3647 PRO A CA    1 
ATOM   15855 C  C     . PRO A 1 3647 ? 212.917 228.053 181.899 1.00 2.35  ? 3647 PRO A C     1 
ATOM   15856 O  O     . PRO A 1 3647 ? 213.811 228.047 181.046 1.00 2.30  ? 3647 PRO A O     1 
ATOM   15857 C  CB    . PRO A 1 3647 ? 213.395 226.832 184.062 1.00 2.42  ? 3647 PRO A CB    1 
ATOM   15858 C  CG    . PRO A 1 3647 ? 212.085 226.659 184.735 1.00 3.75  ? 3647 PRO A CG    1 
ATOM   15859 C  CD    . PRO A 1 3647 ? 211.723 228.020 185.219 1.00 2.52  ? 3647 PRO A CD    1 
ATOM   15860 N  N     . VAL A 1 3648 ? 211.628 227.925 181.577 1.00 2.90  ? 3648 VAL A N     1 
ATOM   15861 C  CA    . VAL A 1 3648 ? 211.222 227.771 180.183 1.00 1.98  ? 3648 VAL A CA    1 
ATOM   15862 C  C     . VAL A 1 3648 ? 211.466 229.062 179.409 1.00 1.54  ? 3648 VAL A C     1 
ATOM   15863 O  O     . VAL A 1 3648 ? 212.004 229.046 178.298 1.00 2.46  ? 3648 VAL A O     1 
ATOM   15864 C  CB    . VAL A 1 3648 ? 209.750 227.331 180.094 1.00 2.75  ? 3648 VAL A CB    1 
ATOM   15865 C  CG1   . VAL A 1 3648 ? 209.293 227.295 178.644 1.00 0.56  ? 3648 VAL A CG1   1 
ATOM   15866 C  CG2   . VAL A 1 3648 ? 209.561 225.970 180.745 1.00 1.35  ? 3648 VAL A CG2   1 
ATOM   15867 N  N     . LEU A 1 3649 ? 211.075 230.200 179.990 1.00 1.32  ? 3649 LEU A N     1 
ATOM   15868 C  CA    . LEU A 1 3649 ? 211.244 231.474 179.305 1.00 1.11  ? 3649 LEU A CA    1 
ATOM   15869 C  C     . LEU A 1 3649 ? 212.712 231.861 179.182 1.00 1.95  ? 3649 LEU A C     1 
ATOM   15870 O  O     . LEU A 1 3649 ? 213.108 232.460 178.178 1.00 4.82  ? 3649 LEU A O     1 
ATOM   15871 C  CB    . LEU A 1 3649 ? 210.461 232.571 180.028 1.00 1.24  ? 3649 LEU A CB    1 
ATOM   15872 C  CG    . LEU A 1 3649 ? 208.950 232.358 180.137 1.00 1.66  ? 3649 LEU A CG    1 
ATOM   15873 C  CD1   . LEU A 1 3649 ? 208.270 233.591 180.707 1.00 0.67  ? 3649 LEU A CD1   1 
ATOM   15874 C  CD2   . LEU A 1 3649 ? 208.352 231.985 178.789 1.00 1.28  ? 3649 LEU A CD2   1 
ATOM   15875 N  N     . ASN A 1 3650 ? 213.528 231.527 180.179 1.00 1.61  ? 3650 ASN A N     1 
ATOM   15876 C  CA    . ASN A 1 3650 ? 214.961 231.785 180.115 1.00 1.24  ? 3650 ASN A CA    1 
ATOM   15877 C  C     . ASN A 1 3650 ? 215.720 230.739 179.314 1.00 2.22  ? 3650 ASN A C     1 
ATOM   15878 O  O     . ASN A 1 3650 ? 216.928 230.903 179.114 1.00 8.54  ? 3650 ASN A O     1 
ATOM   15879 C  CB    . ASN A 1 3650 ? 215.554 231.870 181.523 1.00 1.86  ? 3650 ASN A CB    1 
ATOM   15880 C  CG    . ASN A 1 3650 ? 215.106 233.101 182.272 1.00 2.65  ? 3650 ASN A CG    1 
ATOM   15881 O  OD1   . ASN A 1 3650 ? 214.489 233.997 181.701 1.00 8.20  ? 3650 ASN A OD1   1 
ATOM   15882 N  ND2   . ASN A 1 3650 ? 215.425 233.159 183.556 1.00 3.65  ? 3650 ASN A ND2   1 
ATOM   15883 N  N     . ARG A 1 3651 ? 215.049 229.678 178.861 1.00 1.82  ? 3651 ARG A N     1 
ATOM   15884 C  CA    . ARG A 1 3651 ? 215.675 228.634 178.048 1.00 2.22  ? 3651 ARG A CA    1 
ATOM   15885 C  C     . ARG A 1 3651 ? 216.847 227.988 178.785 1.00 4.26  ? 3651 ARG A C     1 
ATOM   15886 O  O     . ARG A 1 3651 ? 217.914 227.750 178.216 1.00 5.05  ? 3651 ARG A O     1 
ATOM   15887 C  CB    . ARG A 1 3651 ? 216.111 229.193 176.692 1.00 4.20  ? 3651 ARG A CB    1 
ATOM   15888 C  CG    . ARG A 1 3651 ? 214.948 229.580 175.793 1.00 3.96  ? 3651 ARG A CG    1 
ATOM   15889 C  CD    . ARG A 1 3651 ? 215.415 230.213 174.498 1.00 5.55  ? 3651 ARG A CD    1 
ATOM   15890 N  NE    . ARG A 1 3651 ? 214.354 230.991 173.873 1.00 10.65 ? 3651 ARG A NE    1 
ATOM   15891 C  CZ    . ARG A 1 3651 ? 213.474 230.504 173.008 1.00 3.47  ? 3651 ARG A CZ    1 
ATOM   15892 N  NH1   . ARG A 1 3651 ? 213.512 229.241 172.620 1.00 3.59  ? 3651 ARG A NH1   1 
ATOM   15893 N  NH2   . ARG A 1 3651 ? 212.528 231.305 172.524 1.00 0.49  ? 3651 ARG A NH2   1 
ATOM   15894 N  N     . GLU A 1 3652 ? 216.641 227.707 180.072 1.00 3.95  ? 3652 GLU A N     1 
ATOM   15895 C  CA    . GLU A 1 3652 ? 217.658 227.081 180.920 1.00 3.01  ? 3652 GLU A CA    1 
ATOM   15896 C  C     . GLU A 1 3652 ? 217.620 225.571 180.705 1.00 5.16  ? 3652 GLU A C     1 
ATOM   15897 O  O     . GLU A 1 3652 ? 217.041 224.810 181.482 1.00 12.10 ? 3652 GLU A O     1 
ATOM   15898 C  CB    . GLU A 1 3652 ? 217.428 227.431 182.385 1.00 5.12  ? 3652 GLU A CB    1 
ATOM   15899 C  CG    . GLU A 1 3652 ? 217.160 228.895 182.666 1.00 2.96  ? 3652 GLU A CG    1 
ATOM   15900 C  CD    . GLU A 1 3652 ? 216.620 229.121 184.066 1.00 6.94  ? 3652 GLU A CD    1 
ATOM   15901 O  OE1   . GLU A 1 3652 ? 216.801 228.231 184.924 1.00 7.32  ? 3652 GLU A OE1   1 
ATOM   15902 O  OE2   . GLU A 1 3652 ? 216.009 230.182 184.310 1.00 6.34  ? 3652 GLU A OE2   1 
ATOM   15903 N  N     . VAL A 1 3653 ? 218.259 225.133 179.632 1.00 6.69  ? 3653 VAL A N     1 
ATOM   15904 C  CA    . VAL A 1 3653 ? 218.258 223.725 179.257 1.00 8.89  ? 3653 VAL A CA    1 
ATOM   15905 C  C     . VAL A 1 3653 ? 219.604 223.106 179.605 1.00 9.20  ? 3653 VAL A C     1 
ATOM   15906 O  O     . VAL A 1 3653 ? 220.653 223.756 179.544 1.00 10.84 ? 3653 VAL A O     1 
ATOM   15907 C  CB    . VAL A 1 3653 ? 217.925 223.537 177.763 1.00 8.85  ? 3653 VAL A CB    1 
ATOM   15908 C  CG1   . VAL A 1 3653 ? 216.535 224.063 177.474 1.00 10.30 ? 3653 VAL A CG1   1 
ATOM   15909 C  CG2   . VAL A 1 3653 ? 218.948 224.245 176.894 1.00 7.37  ? 3653 VAL A CG2   1 
ATOM   15910 N  N     . ARG A 1 3654 ? 219.566 221.833 179.990 1.00 10.15 ? 3654 ARG A N     1 
ATOM   15911 C  CA    . ARG A 1 3654 ? 220.757 221.074 180.354 1.00 10.13 ? 3654 ARG A CA    1 
ATOM   15912 C  C     . ARG A 1 3654 ? 220.895 219.929 179.359 1.00 13.24 ? 3654 ARG A C     1 
ATOM   15913 O  O     . ARG A 1 3654 ? 220.057 219.023 179.327 1.00 17.21 ? 3654 ARG A O     1 
ATOM   15914 C  CB    . ARG A 1 3654 ? 220.662 220.585 181.802 1.00 13.68 ? 3654 ARG A CB    1 
ATOM   15915 C  CG    . ARG A 1 3654 ? 221.904 219.892 182.360 1.00 18.06 ? 3654 ARG A CG    1 
ATOM   15916 C  CD    . ARG A 1 3654 ? 221.930 218.401 182.061 1.00 24.65 ? 3654 ARG A CD    1 
ATOM   15917 N  NE    . ARG A 1 3654 ? 220.741 217.722 182.563 1.00 29.87 ? 3654 ARG A NE    1 
ATOM   15918 C  CZ    . ARG A 1 3654 ? 220.584 217.323 183.819 1.00 30.49 ? 3654 ARG A CZ    1 
ATOM   15919 N  NH1   . ARG A 1 3654 ? 221.528 217.507 184.727 1.00 30.25 ? 3654 ARG A NH1   1 
ATOM   15920 N  NH2   . ARG A 1 3654 ? 219.452 216.720 184.170 1.00 24.19 ? 3654 ARG A NH2   1 
ATOM   15921 N  N     . ARG A 1 3655 ? 221.948 219.977 178.544 1.00 13.46 ? 3655 ARG A N     1 
ATOM   15922 C  CA    . ARG A 1 3655 ? 222.187 218.972 177.509 1.00 14.56 ? 3655 ARG A CA    1 
ATOM   15923 C  C     . ARG A 1 3655 ? 223.295 218.036 177.970 1.00 21.35 ? 3655 ARG A C     1 
ATOM   15924 O  O     . ARG A 1 3655 ? 224.483 218.337 177.828 1.00 27.20 ? 3655 ARG A O     1 
ATOM   15925 C  CB    . ARG A 1 3655 ? 222.519 219.637 176.175 1.00 10.95 ? 3655 ARG A CB    1 
ATOM   15926 C  CG    . ARG A 1 3655 ? 221.315 220.291 175.517 1.00 14.37 ? 3655 ARG A CG    1 
ATOM   15927 C  CD    . ARG A 1 3655 ? 221.684 221.188 174.346 1.00 14.99 ? 3655 ARG A CD    1 
ATOM   15928 N  NE    . ARG A 1 3655 ? 220.488 221.701 173.688 1.00 16.53 ? 3655 ARG A NE    1 
ATOM   15929 C  CZ    . ARG A 1 3655 ? 220.148 222.980 173.623 1.00 18.91 ? 3655 ARG A CZ    1 
ATOM   15930 N  NH1   . ARG A 1 3655 ? 220.893 223.924 174.174 1.00 24.71 ? 3655 ARG A NH1   1 
ATOM   15931 N  NH2   . ARG A 1 3655 ? 219.029 223.324 172.990 1.00 17.86 ? 3655 ARG A NH2   1 
ATOM   15932 N  N     . THR A 1 3656 ? 222.901 216.893 178.527 1.00 24.61 ? 3656 THR A N     1 
ATOM   15933 C  CA    . THR A 1 3656 ? 223.830 215.865 178.967 1.00 25.71 ? 3656 THR A CA    1 
ATOM   15934 C  C     . THR A 1 3656 ? 223.275 214.499 178.592 1.00 24.61 ? 3656 THR A C     1 
ATOM   15935 O  O     . THR A 1 3656 ? 222.071 214.249 178.704 1.00 22.38 ? 3656 THR A O     1 
ATOM   15936 C  CB    . THR A 1 3656 ? 224.084 215.941 180.481 1.00 28.57 ? 3656 THR A CB    1 
ATOM   15937 O  OG1   . THR A 1 3656 ? 224.583 217.240 180.818 1.00 31.20 ? 3656 THR A OG1   1 
ATOM   15938 C  CG2   . THR A 1 3656 ? 225.097 214.890 180.918 1.00 25.00 ? 3656 THR A CG2   1 
ATOM   15939 N  N     . GLY A 1 3657 ? 224.164 213.619 178.144 1.00 28.27 ? 3657 GLY A N     1 
ATOM   15940 C  CA    . GLY A 1 3657 ? 223.771 212.264 177.793 1.00 20.72 ? 3657 GLY A CA    1 
ATOM   15941 C  C     . GLY A 1 3657 ? 222.872 212.177 176.581 1.00 16.08 ? 3657 GLY A C     1 
ATOM   15942 O  O     . GLY A 1 3657 ? 221.952 211.349 176.553 1.00 23.89 ? 3657 GLY A O     1 
ATOM   15943 N  N     . GLY A 1 3658 ? 223.116 213.013 175.575 1.00 18.62 ? 3658 GLY A N     1 
ATOM   15944 C  CA    . GLY A 1 3658 ? 222.299 213.000 174.374 1.00 15.15 ? 3658 GLY A CA    1 
ATOM   15945 C  C     . GLY A 1 3658 ? 220.864 213.414 174.604 1.00 16.99 ? 3658 GLY A C     1 
ATOM   15946 O  O     . GLY A 1 3658 ? 220.005 213.155 173.755 1.00 21.69 ? 3658 GLY A O     1 
ATOM   15947 N  N     . ARG A 1 3659 ? 220.582 214.060 175.730 1.00 12.91 ? 3659 ARG A N     1 
ATOM   15948 C  CA    . ARG A 1 3659 ? 219.228 214.445 176.100 1.00 12.13 ? 3659 ARG A CA    1 
ATOM   15949 C  C     . ARG A 1 3659 ? 219.192 215.933 176.407 1.00 14.46 ? 3659 ARG A C     1 
ATOM   15950 O  O     . ARG A 1 3659 ? 220.092 216.456 177.071 1.00 16.99 ? 3659 ARG A O     1 
ATOM   15951 C  CB    . ARG A 1 3659 ? 218.741 213.648 177.312 1.00 14.65 ? 3659 ARG A CB    1 
ATOM   15952 C  CG    . ARG A 1 3659 ? 218.335 212.224 177.025 1.00 14.37 ? 3659 ARG A CG    1 
ATOM   15953 C  CD    . ARG A 1 3659 ? 218.130 211.463 178.322 1.00 14.98 ? 3659 ARG A CD    1 
ATOM   15954 N  NE    . ARG A 1 3659 ? 216.900 211.855 178.997 1.00 11.58 ? 3659 ARG A NE    1 
ATOM   15955 C  CZ    . ARG A 1 3659 ? 216.783 212.023 180.307 1.00 13.61 ? 3659 ARG A CZ    1 
ATOM   15956 N  NH1   . ARG A 1 3659 ? 217.811 211.840 181.121 1.00 13.94 ? 3659 ARG A NH1   1 
ATOM   15957 N  NH2   . ARG A 1 3659 ? 215.607 212.378 180.813 1.00 11.60 ? 3659 ARG A NH2   1 
ATOM   15958 N  N     . VAL A 1 3660 ? 218.152 216.608 175.932 1.00 14.95 ? 3660 VAL A N     1 
ATOM   15959 C  CA    . VAL A 1 3660 ? 217.935 218.021 176.223 1.00 11.27 ? 3660 VAL A CA    1 
ATOM   15960 C  C     . VAL A 1 3660 ? 216.869 218.117 177.305 1.00 8.34  ? 3660 VAL A C     1 
ATOM   15961 O  O     . VAL A 1 3660 ? 215.700 217.792 177.065 1.00 13.78 ? 3660 VAL A O     1 
ATOM   15962 C  CB    . VAL A 1 3660 ? 217.518 218.790 174.962 1.00 8.24  ? 3660 VAL A CB    1 
ATOM   15963 C  CG1   . VAL A 1 3660 ? 217.384 220.272 175.260 1.00 7.05  ? 3660 VAL A CG1   1 
ATOM   15964 C  CG2   . VAL A 1 3660 ? 218.517 218.548 173.842 1.00 9.42  ? 3660 VAL A CG2   1 
ATOM   15965 N  N     . LEU A 1 3661 ? 217.262 218.569 178.491 1.00 5.59  ? 3661 LEU A N     1 
ATOM   15966 C  CA    . LEU A 1 3661 ? 216.399 218.552 179.663 1.00 8.21  ? 3661 LEU A CA    1 
ATOM   15967 C  C     . LEU A 1 3661 ? 216.055 219.967 180.103 1.00 9.17  ? 3661 LEU A C     1 
ATOM   15968 O  O     . LEU A 1 3661 ? 216.911 220.856 180.101 1.00 12.89 ? 3661 LEU A O     1 
ATOM   15969 C  CB    . LEU A 1 3661 ? 217.050 217.804 180.830 1.00 13.12 ? 3661 LEU A CB    1 
ATOM   15970 C  CG    . LEU A 1 3661 ? 216.844 216.290 180.938 1.00 10.81 ? 3661 LEU A CG    1 
ATOM   15971 C  CD1   . LEU A 1 3661 ? 215.413 215.959 181.311 1.00 14.15 ? 3661 LEU A CD1   1 
ATOM   15972 C  CD2   . LEU A 1 3661 ? 217.224 215.592 179.663 1.00 9.36  ? 3661 LEU A CD2   1 
ATOM   15973 N  N     . ILE A 1 3662 ? 214.796 220.164 180.482 1.00 11.97 ? 3662 ILE A N     1 
ATOM   15974 C  CA    . ILE A 1 3662 ? 214.322 221.409 181.073 1.00 6.86  ? 3662 ILE A CA    1 
ATOM   15975 C  C     . ILE A 1 3662 ? 213.748 221.074 182.443 1.00 6.58  ? 3662 ILE A C     1 
ATOM   15976 O  O     . ILE A 1 3662 ? 212.958 220.135 182.579 1.00 11.44 ? 3662 ILE A O     1 
ATOM   15977 C  CB    . ILE A 1 3662 ? 213.282 222.108 180.173 1.00 7.47  ? 3662 ILE A CB    1 
ATOM   15978 C  CG1   . ILE A 1 3662 ? 212.774 223.397 180.821 1.00 7.09  ? 3662 ILE A CG1   1 
ATOM   15979 C  CG2   . ILE A 1 3662 ? 212.132 221.171 179.815 1.00 6.66  ? 3662 ILE A CG2   1 
ATOM   15980 C  CD1   . ILE A 1 3662 ? 213.783 224.519 180.805 1.00 7.55  ? 3662 ILE A CD1   1 
ATOM   15981 N  N     . THR A 1 3663 ? 214.171 221.818 183.461 1.00 9.07  ? 3663 THR A N     1 
ATOM   15982 C  CA    . THR A 1 3663 ? 213.780 221.529 184.839 1.00 12.13 ? 3663 THR A CA    1 
ATOM   15983 C  C     . THR A 1 3663 ? 212.509 222.309 185.149 1.00 12.04 ? 3663 THR A C     1 
ATOM   15984 O  O     . THR A 1 3663 ? 212.549 223.518 185.387 1.00 14.16 ? 3663 THR A O     1 
ATOM   15985 C  CB    . THR A 1 3663 ? 214.903 221.877 185.807 1.00 14.88 ? 3663 THR A CB    1 
ATOM   15986 O  OG1   . THR A 1 3663 ? 216.079 221.138 185.458 1.00 17.82 ? 3663 THR A OG1   1 
ATOM   15987 C  CG2   . THR A 1 3663 ? 214.501 221.525 187.231 1.00 15.35 ? 3663 THR A CG2   1 
ATOM   15988 N  N     . LEU A 1 3664 ? 211.375 221.613 185.147 1.00 9.34  ? 3664 LEU A N     1 
ATOM   15989 C  CA    . LEU A 1 3664 ? 210.075 222.212 185.439 1.00 9.08  ? 3664 LEU A CA    1 
ATOM   15990 C  C     . LEU A 1 3664 ? 209.698 221.823 186.862 1.00 12.01 ? 3664 LEU A C     1 
ATOM   15991 O  O     . LEU A 1 3664 ? 209.283 220.691 187.120 1.00 13.09 ? 3664 LEU A O     1 
ATOM   15992 C  CB    . LEU A 1 3664 ? 209.025 221.751 184.435 1.00 6.33  ? 3664 LEU A CB    1 
ATOM   15993 C  CG    . LEU A 1 3664 ? 207.674 222.448 184.568 1.00 5.33  ? 3664 LEU A CG    1 
ATOM   15994 C  CD1   . LEU A 1 3664 ? 207.802 223.882 184.101 1.00 4.86  ? 3664 LEU A CD1   1 
ATOM   15995 C  CD2   . LEU A 1 3664 ? 206.592 221.715 183.793 1.00 6.50  ? 3664 LEU A CD2   1 
ATOM   15996 N  N     . GLY A 1 3665 ? 209.827 222.770 187.785 1.00 12.69 ? 3665 GLY A N     1 
ATOM   15997 C  CA    . GLY A 1 3665 ? 209.683 222.459 189.191 1.00 11.19 ? 3665 GLY A CA    1 
ATOM   15998 C  C     . GLY A 1 3665 ? 210.787 221.537 189.665 1.00 14.91 ? 3665 GLY A C     1 
ATOM   15999 O  O     . GLY A 1 3665 ? 211.971 221.837 189.491 1.00 25.52 ? 3665 GLY A O     1 
ATOM   16000 N  N     . ASP A 1 3666 ? 210.414 220.410 190.266 1.00 18.53 ? 3666 ASP A N     1 
ATOM   16001 C  CA    . ASP A 1 3666 ? 211.371 219.412 190.720 1.00 18.71 ? 3666 ASP A CA    1 
ATOM   16002 C  C     . ASP A 1 3666 ? 211.485 218.225 189.771 1.00 20.95 ? 3666 ASP A C     1 
ATOM   16003 O  O     . ASP A 1 3666 ? 212.193 217.264 190.088 1.00 25.04 ? 3666 ASP A O     1 
ATOM   16004 C  CB    . ASP A 1 3666 ? 210.991 218.920 192.118 1.00 25.81 ? 3666 ASP A CB    1 
ATOM   16005 C  CG    . ASP A 1 3666 ? 209.649 218.221 192.139 1.00 32.05 ? 3666 ASP A CG    1 
ATOM   16006 O  OD1   . ASP A 1 3666 ? 208.654 218.836 191.700 1.00 28.14 ? 3666 ASP A OD1   1 
ATOM   16007 O  OD2   . ASP A 1 3666 ? 209.588 217.059 192.594 1.00 31.84 ? 3666 ASP A OD2   1 
ATOM   16008 N  N     . GLN A 1 3667 ? 210.814 218.267 188.626 1.00 16.28 ? 3667 GLN A N     1 
ATOM   16009 C  CA    . GLN A 1 3667 ? 210.819 217.179 187.660 1.00 15.92 ? 3667 GLN A CA    1 
ATOM   16010 C  C     . GLN A 1 3667 ? 211.526 217.630 186.390 1.00 17.54 ? 3667 GLN A C     1 
ATOM   16011 O  O     . GLN A 1 3667 ? 211.225 218.702 185.858 1.00 24.38 ? 3667 GLN A O     1 
ATOM   16012 C  CB    . GLN A 1 3667 ? 209.391 216.729 187.340 1.00 21.25 ? 3667 GLN A CB    1 
ATOM   16013 C  CG    . GLN A 1 3667 ? 209.305 215.535 186.403 1.00 24.39 ? 3667 GLN A CG    1 
ATOM   16014 C  CD    . GLN A 1 3667 ? 207.876 215.090 186.160 1.00 32.28 ? 3667 GLN A CD    1 
ATOM   16015 O  OE1   . GLN A 1 3667 ? 206.931 215.696 186.663 1.00 35.44 ? 3667 GLN A OE1   1 
ATOM   16016 N  NE2   . GLN A 1 3667 ? 207.711 214.025 185.384 1.00 36.59 ? 3667 GLN A NE2   1 
ATOM   16017 N  N     . ASP A 1 3668 ? 212.464 216.816 185.914 1.00 11.33 ? 3668 ASP A N     1 
ATOM   16018 C  CA    . ASP A 1 3668 ? 213.153 217.098 184.665 1.00 11.70 ? 3668 ASP A CA    1 
ATOM   16019 C  C     . ASP A 1 3668 ? 212.376 216.527 183.481 1.00 10.67 ? 3668 ASP A C     1 
ATOM   16020 O  O     . ASP A 1 3668 ? 211.851 215.412 183.540 1.00 16.48 ? 3668 ASP A O     1 
ATOM   16021 C  CB    . ASP A 1 3668 ? 214.592 216.566 184.700 1.00 18.96 ? 3668 ASP A CB    1 
ATOM   16022 C  CG    . ASP A 1 3668 ? 214.677 215.057 184.912 1.00 30.90 ? 3668 ASP A CG    1 
ATOM   16023 O  OD1   . ASP A 1 3668 ? 213.640 214.391 185.105 1.00 40.72 ? 3668 ASP A OD1   1 
ATOM   16024 O  OD2   . ASP A 1 3668 ? 215.808 214.528 184.884 1.00 28.09 ? 3668 ASP A OD2   1 
ATOM   16025 N  N     . ILE A 1 3669 ? 212.280 217.316 182.416 1.00 8.40  ? 3669 ILE A N     1 
ATOM   16026 C  CA    . ILE A 1 3669 ? 211.484 216.971 181.245 1.00 4.83  ? 3669 ILE A CA    1 
ATOM   16027 C  C     . ILE A 1 3669 ? 212.354 217.104 180.006 1.00 7.11  ? 3669 ILE A C     1 
ATOM   16028 O  O     . ILE A 1 3669 ? 213.112 218.069 179.871 1.00 9.90  ? 3669 ILE A O     1 
ATOM   16029 C  CB    . ILE A 1 3669 ? 210.229 217.865 181.123 1.00 7.07  ? 3669 ILE A CB    1 
ATOM   16030 C  CG1   . ILE A 1 3669 ? 209.443 217.869 182.432 1.00 8.59  ? 3669 ILE A CG1   1 
ATOM   16031 C  CG2   . ILE A 1 3669 ? 209.346 217.406 179.973 1.00 6.03  ? 3669 ILE A CG2   1 
ATOM   16032 C  CD1   . ILE A 1 3669 ? 208.267 218.797 182.424 1.00 7.93  ? 3669 ILE A CD1   1 
ATOM   16033 N  N     . ASP A 1 3670 ? 212.248 216.130 179.107 1.00 6.80  ? 3670 ASP A N     1 
ATOM   16034 C  CA    . ASP A 1 3670 ? 212.917 216.228 177.817 1.00 8.67  ? 3670 ASP A CA    1 
ATOM   16035 C  C     . ASP A 1 3670 ? 212.229 217.293 176.971 1.00 8.79  ? 3670 ASP A C     1 
ATOM   16036 O  O     . ASP A 1 3670 ? 211.015 217.234 176.752 1.00 10.06 ? 3670 ASP A O     1 
ATOM   16037 C  CB    . ASP A 1 3670 ? 212.896 214.876 177.110 1.00 10.60 ? 3670 ASP A CB    1 
ATOM   16038 C  CG    . ASP A 1 3670 ? 213.578 213.790 177.914 1.00 19.61 ? 3670 ASP A CG    1 
ATOM   16039 O  OD1   . ASP A 1 3670 ? 214.779 213.941 178.219 1.00 18.01 ? 3670 ASP A OD1   1 
ATOM   16040 O  OD2   . ASP A 1 3670 ? 212.914 212.785 178.244 1.00 29.54 ? 3670 ASP A OD2   1 
ATOM   16041 N  N     . LEU A 1 3671 ? 213.002 218.265 176.497 1.00 11.46 ? 3671 LEU A N     1 
ATOM   16042 C  CA    . LEU A 1 3671 ? 212.463 219.392 175.746 1.00 5.58  ? 3671 LEU A CA    1 
ATOM   16043 C  C     . LEU A 1 3671 ? 212.532 219.099 174.253 1.00 6.21  ? 3671 LEU A C     1 
ATOM   16044 O  O     . LEU A 1 3671 ? 213.621 218.921 173.699 1.00 7.62  ? 3671 LEU A O     1 
ATOM   16045 C  CB    . LEU A 1 3671 ? 213.229 220.673 176.072 1.00 6.97  ? 3671 LEU A CB    1 
ATOM   16046 C  CG    . LEU A 1 3671 ? 212.792 221.899 175.269 1.00 5.69  ? 3671 LEU A CG    1 
ATOM   16047 C  CD1   . LEU A 1 3671 ? 211.349 222.249 175.571 1.00 4.34  ? 3671 LEU A CD1   1 
ATOM   16048 C  CD2   . LEU A 1 3671 ? 213.701 223.079 175.534 1.00 6.90  ? 3671 LEU A CD2   1 
ATOM   16049 N  N     . SER A 1 3672 ? 211.374 219.046 173.609 1.00 6.61  ? 3672 SER A N     1 
ATOM   16050 C  CA    . SER A 1 3672 ? 211.344 218.896 172.162 1.00 5.21  ? 3672 SER A CA    1 
ATOM   16051 C  C     . SER A 1 3672 ? 211.633 220.239 171.491 1.00 6.95  ? 3672 SER A C     1 
ATOM   16052 O  O     . SER A 1 3672 ? 211.180 221.281 171.969 1.00 9.07  ? 3672 SER A O     1 
ATOM   16053 C  CB    . SER A 1 3672 ? 209.994 218.360 171.708 1.00 6.67  ? 3672 SER A CB    1 
ATOM   16054 O  OG    . SER A 1 3672 ? 209.821 218.518 170.311 1.00 12.48 ? 3672 SER A OG    1 
ATOM   16055 N  N     . PRO A 1 3673 ? 212.390 220.243 170.391 1.00 7.26  ? 3673 PRO A N     1 
ATOM   16056 C  CA    . PRO A 1 3673 ? 212.755 221.516 169.749 1.00 4.50  ? 3673 PRO A CA    1 
ATOM   16057 C  C     . PRO A 1 3673 ? 211.596 222.233 169.078 1.00 6.46  ? 3673 PRO A C     1 
ATOM   16058 O  O     . PRO A 1 3673 ? 211.735 223.420 168.757 1.00 12.29 ? 3673 PRO A O     1 
ATOM   16059 C  CB    . PRO A 1 3673 ? 213.814 221.094 168.725 1.00 7.37  ? 3673 PRO A CB    1 
ATOM   16060 C  CG    . PRO A 1 3673 ? 213.477 219.683 168.413 1.00 8.59  ? 3673 PRO A CG    1 
ATOM   16061 C  CD    . PRO A 1 3673 ? 212.991 219.089 169.702 1.00 6.20  ? 3673 PRO A CD    1 
ATOM   16062 N  N     . SER A 1 3674 ? 210.468 221.569 168.851 1.00 8.98  ? 3674 SER A N     1 
ATOM   16063 C  CA    . SER A 1 3674 ? 209.324 222.199 168.210 1.00 5.28  ? 3674 SER A CA    1 
ATOM   16064 C  C     . SER A 1 3674 ? 208.412 222.917 169.196 1.00 7.85  ? 3674 SER A C     1 
ATOM   16065 O  O     . SER A 1 3674 ? 207.400 223.485 168.776 1.00 9.02  ? 3674 SER A O     1 
ATOM   16066 C  CB    . SER A 1 3674 ? 208.519 221.159 167.426 1.00 6.26  ? 3674 SER A CB    1 
ATOM   16067 O  OG    . SER A 1 3674 ? 208.296 219.995 168.198 1.00 15.66 ? 3674 SER A OG    1 
ATOM   16068 N  N     . PHE A 1 3675 ? 208.743 222.909 170.483 1.00 6.64  ? 3675 PHE A N     1 
ATOM   16069 C  CA    . PHE A 1 3675 ? 207.907 223.567 171.474 1.00 1.56  ? 3675 PHE A CA    1 
ATOM   16070 C  C     . PHE A 1 3675 ? 207.950 225.081 171.302 1.00 0.74  ? 3675 PHE A C     1 
ATOM   16071 O  O     . PHE A 1 3675 ? 208.998 225.665 171.019 1.00 2.17  ? 3675 PHE A O     1 
ATOM   16072 C  CB    . PHE A 1 3675 ? 208.347 223.192 172.890 1.00 1.92  ? 3675 PHE A CB    1 
ATOM   16073 C  CG    . PHE A 1 3675 ? 207.832 224.125 173.952 1.00 0.56  ? 3675 PHE A CG    1 
ATOM   16074 C  CD1   . PHE A 1 3675 ? 206.574 223.943 174.496 1.00 0.44  ? 3675 PHE A CD1   1 
ATOM   16075 C  CD2   . PHE A 1 3675 ? 208.601 225.186 174.401 1.00 0.21  ? 3675 PHE A CD2   1 
ATOM   16076 C  CE1   . PHE A 1 3675 ? 206.094 224.795 175.462 1.00 0.30  ? 3675 PHE A CE1   1 
ATOM   16077 C  CE2   . PHE A 1 3675 ? 208.123 226.045 175.367 1.00 0.23  ? 3675 PHE A CE2   1 
ATOM   16078 C  CZ    . PHE A 1 3675 ? 206.870 225.847 175.899 1.00 0.15  ? 3675 PHE A CZ    1 
ATOM   16079 N  N     . VAL A 1 3676 ? 206.797 225.712 171.487 1.00 0.46  ? 3676 VAL A N     1 
ATOM   16080 C  CA    . VAL A 1 3676 ? 206.687 227.166 171.516 1.00 0.31  ? 3676 VAL A CA    1 
ATOM   16081 C  C     . VAL A 1 3676 ? 205.525 227.524 172.429 1.00 0.34  ? 3676 VAL A C     1 
ATOM   16082 O  O     . VAL A 1 3676 ? 204.542 226.785 172.521 1.00 0.57  ? 3676 VAL A O     1 
ATOM   16083 C  CB    . VAL A 1 3676 ? 206.523 227.752 170.094 1.00 0.40  ? 3676 VAL A CB    1 
ATOM   16084 C  CG1   . VAL A 1 3676 ? 205.229 227.293 169.462 1.00 0.66  ? 3676 VAL A CG1   1 
ATOM   16085 C  CG2   . VAL A 1 3676 ? 206.577 229.263 170.131 1.00 0.25  ? 3676 VAL A CG2   1 
ATOM   16086 N  N     . ILE A 1 3677 ? 205.655 228.644 173.134 1.00 0.28  ? 3677 ILE A N     1 
ATOM   16087 C  CA    . ILE A 1 3677 ? 204.653 229.090 174.091 1.00 0.18  ? 3677 ILE A CA    1 
ATOM   16088 C  C     . ILE A 1 3677 ? 204.314 230.546 173.807 1.00 0.20  ? 3677 ILE A C     1 
ATOM   16089 O  O     . ILE A 1 3677 ? 205.208 231.365 173.570 1.00 0.25  ? 3677 ILE A O     1 
ATOM   16090 C  CB    . ILE A 1 3677 ? 205.134 228.903 175.545 1.00 0.23  ? 3677 ILE A CB    1 
ATOM   16091 C  CG1   . ILE A 1 3677 ? 204.086 229.413 176.536 1.00 0.11  ? 3677 ILE A CG1   1 
ATOM   16092 C  CG2   . ILE A 1 3677 ? 206.491 229.561 175.767 1.00 0.10  ? 3677 ILE A CG2   1 
ATOM   16093 C  CD1   . ILE A 1 3677 ? 204.255 228.858 177.929 1.00 0.13  ? 3677 ILE A CD1   1 
ATOM   16094 N  N     . PHE A 1 3678 ? 203.022 230.862 173.809 1.00 0.26  ? 3678 PHE A N     1 
ATOM   16095 C  CA    . PHE A 1 3678 ? 202.535 232.228 173.682 1.00 0.13  ? 3678 PHE A CA    1 
ATOM   16096 C  C     . PHE A 1 3678 ? 201.756 232.586 174.939 1.00 0.25  ? 3678 PHE A C     1 
ATOM   16097 O  O     . PHE A 1 3678 ? 200.873 231.835 175.359 1.00 1.39  ? 3678 PHE A O     1 
ATOM   16098 C  CB    . PHE A 1 3678 ? 201.642 232.397 172.448 1.00 0.22  ? 3678 PHE A CB    1 
ATOM   16099 C  CG    . PHE A 1 3678 ? 202.334 232.099 171.150 1.00 0.16  ? 3678 PHE A CG    1 
ATOM   16100 C  CD1   . PHE A 1 3678 ? 202.336 230.816 170.629 1.00 0.12  ? 3678 PHE A CD1   1 
ATOM   16101 C  CD2   . PHE A 1 3678 ? 202.974 233.103 170.446 1.00 0.11  ? 3678 PHE A CD2   1 
ATOM   16102 C  CE1   . PHE A 1 3678 ? 202.969 230.540 169.436 1.00 0.27  ? 3678 PHE A CE1   1 
ATOM   16103 C  CE2   . PHE A 1 3678 ? 203.608 232.833 169.250 1.00 0.19  ? 3678 PHE A CE2   1 
ATOM   16104 C  CZ    . PHE A 1 3678 ? 203.605 231.550 168.744 1.00 0.21  ? 3678 PHE A CZ    1 
ATOM   16105 N  N     . LEU A 1 3679 ? 202.086 233.726 175.532 1.00 0.26  ? 3679 LEU A N     1 
ATOM   16106 C  CA    . LEU A 1 3679 ? 201.366 234.253 176.679 1.00 0.31  ? 3679 LEU A CA    1 
ATOM   16107 C  C     . LEU A 1 3679 ? 200.460 235.389 176.224 1.00 0.62  ? 3679 LEU A C     1 
ATOM   16108 O  O     . LEU A 1 3679 ? 200.853 236.206 175.387 1.00 2.23  ? 3679 LEU A O     1 
ATOM   16109 C  CB    . LEU A 1 3679 ? 202.331 234.747 177.760 1.00 0.20  ? 3679 LEU A CB    1 
ATOM   16110 C  CG    . LEU A 1 3679 ? 203.490 233.815 178.126 1.00 0.35  ? 3679 LEU A CG    1 
ATOM   16111 C  CD1   . LEU A 1 3679 ? 204.303 234.396 179.271 1.00 0.39  ? 3679 LEU A CD1   1 
ATOM   16112 C  CD2   . LEU A 1 3679 ? 202.990 232.419 178.473 1.00 0.21  ? 3679 LEU A CD2   1 
ATOM   16113 N  N     . SER A 1 3680 ? 199.248 235.434 176.767 1.00 0.90  ? 3680 SER A N     1 
ATOM   16114 C  CA    . SER A 1 3680 ? 198.270 236.422 176.339 1.00 0.85  ? 3680 SER A CA    1 
ATOM   16115 C  C     . SER A 1 3680 ? 197.539 237.004 177.537 1.00 1.40  ? 3680 SER A C     1 
ATOM   16116 O  O     . SER A 1 3680 ? 197.346 236.338 178.557 1.00 1.72  ? 3680 SER A O     1 
ATOM   16117 C  CB    . SER A 1 3680 ? 197.261 235.821 175.353 1.00 1.32  ? 3680 SER A CB    1 
ATOM   16118 O  OG    . SER A 1 3680 ? 196.704 234.623 175.857 1.00 3.68  ? 3680 SER A OG    1 
ATOM   16119 N  N     . THR A 1 3681 ? 197.140 238.263 177.396 1.00 1.70  ? 3681 THR A N     1 
ATOM   16120 C  CA    . THR A 1 3681 ? 196.266 238.934 178.345 1.00 1.65  ? 3681 THR A CA    1 
ATOM   16121 C  C     . THR A 1 3681 ? 195.286 239.801 177.573 1.00 1.21  ? 3681 THR A C     1 
ATOM   16122 O  O     . THR A 1 3681 ? 195.580 240.265 176.469 1.00 1.96  ? 3681 THR A O     1 
ATOM   16123 C  CB    . THR A 1 3681 ? 197.045 239.796 179.352 1.00 3.44  ? 3681 THR A CB    1 
ATOM   16124 O  OG1   . THR A 1 3681 ? 196.126 240.461 180.226 1.00 4.00  ? 3681 THR A OG1   1 
ATOM   16125 C  CG2   . THR A 1 3681 ? 197.893 240.835 178.635 1.00 1.58  ? 3681 THR A CG2   1 
ATOM   16126 N  N     . ARG A 1 3682 ? 194.110 240.008 178.158 1.00 3.78  ? 3682 ARG A N     1 
ATOM   16127 C  CA    . ARG A 1 3682 ? 193.111 240.897 177.588 1.00 3.90  ? 3682 ARG A CA    1 
ATOM   16128 C  C     . ARG A 1 3682 ? 193.081 242.260 178.266 1.00 3.89  ? 3682 ARG A C     1 
ATOM   16129 O  O     . ARG A 1 3682 ? 192.259 243.102 177.898 1.00 9.16  ? 3682 ARG A O     1 
ATOM   16130 C  CB    . ARG A 1 3682 ? 191.726 240.248 177.662 1.00 1.97  ? 3682 ARG A CB    1 
ATOM   16131 C  CG    . ARG A 1 3682 ? 191.547 239.066 176.728 1.00 2.19  ? 3682 ARG A CG    1 
ATOM   16132 C  CD    . ARG A 1 3682 ? 190.129 238.532 176.783 1.00 2.16  ? 3682 ARG A CD    1 
ATOM   16133 N  NE    . ARG A 1 3682 ? 189.830 237.924 178.074 1.00 4.32  ? 3682 ARG A NE    1 
ATOM   16134 C  CZ    . ARG A 1 3682 ? 189.037 238.465 178.989 1.00 6.17  ? 3682 ARG A CZ    1 
ATOM   16135 N  NH1   . ARG A 1 3682 ? 188.450 239.633 178.792 1.00 5.54  ? 3682 ARG A NH1   1 
ATOM   16136 N  NH2   . ARG A 1 3682 ? 188.836 237.820 180.133 1.00 8.52  ? 3682 ARG A NH2   1 
ATOM   16137 N  N     . ASP A 1 3683 ? 193.959 242.497 179.239 1.00 3.43  ? 3683 ASP A N     1 
ATOM   16138 C  CA    . ASP A 1 3683 ? 193.963 243.749 179.976 1.00 4.42  ? 3683 ASP A CA    1 
ATOM   16139 C  C     . ASP A 1 3683 ? 195.106 244.616 179.473 1.00 6.56  ? 3683 ASP A C     1 
ATOM   16140 O  O     . ASP A 1 3683 ? 196.273 244.298 179.742 1.00 8.49  ? 3683 ASP A O     1 
ATOM   16141 C  CB    . ASP A 1 3683 ? 194.114 243.480 181.473 1.00 4.56  ? 3683 ASP A CB    1 
ATOM   16142 C  CG    . ASP A 1 3683 ? 193.836 244.705 182.325 1.00 9.98  ? 3683 ASP A CG    1 
ATOM   16143 O  OD1   . ASP A 1 3683 ? 194.037 245.843 181.853 1.00 17.15 ? 3683 ASP A OD1   1 
ATOM   16144 O  OD2   . ASP A 1 3683 ? 193.410 244.527 183.485 1.00 12.26 ? 3683 ASP A OD2   1 
ATOM   16145 N  N     . PRO A 1 3684 ? 194.836 245.700 178.741 1.00 6.94  ? 3684 PRO A N     1 
ATOM   16146 C  CA    . PRO A 1 3684 ? 195.927 246.589 178.314 1.00 7.80  ? 3684 PRO A CA    1 
ATOM   16147 C  C     . PRO A 1 3684 ? 196.556 247.373 179.451 1.00 10.73 ? 3684 PRO A C     1 
ATOM   16148 O  O     . PRO A 1 3684 ? 197.661 247.900 179.275 1.00 15.82 ? 3684 PRO A O     1 
ATOM   16149 C  CB    . PRO A 1 3684 ? 195.241 247.521 177.310 1.00 11.13 ? 3684 PRO A CB    1 
ATOM   16150 C  CG    . PRO A 1 3684 ? 193.821 247.546 177.751 1.00 11.12 ? 3684 PRO A CG    1 
ATOM   16151 C  CD    . PRO A 1 3684 ? 193.525 246.165 178.259 1.00 6.59  ? 3684 PRO A CD    1 
ATOM   16152 N  N     . THR A 1 3685 ? 195.896 247.463 180.603 1.00 9.43  ? 3685 THR A N     1 
ATOM   16153 C  CA    . THR A 1 3685 ? 196.365 248.259 181.726 1.00 7.17  ? 3685 THR A CA    1 
ATOM   16154 C  C     . THR A 1 3685 ? 197.139 247.449 182.753 1.00 9.11  ? 3685 THR A C     1 
ATOM   16155 O  O     . THR A 1 3685 ? 197.529 247.999 183.789 1.00 19.79 ? 3685 THR A O     1 
ATOM   16156 C  CB    . THR A 1 3685 ? 195.176 248.948 182.412 1.00 10.39 ? 3685 THR A CB    1 
ATOM   16157 O  OG1   . THR A 1 3685 ? 194.536 248.025 183.300 1.00 14.50 ? 3685 THR A OG1   1 
ATOM   16158 C  CG2   . THR A 1 3685 ? 194.176 249.427 181.379 1.00 13.17 ? 3685 THR A CG2   1 
ATOM   16159 N  N     . VAL A 1 3686 ? 197.373 246.162 182.502 1.00 8.36  ? 3686 VAL A N     1 
ATOM   16160 C  CA    . VAL A 1 3686 ? 198.077 245.327 183.467 1.00 6.67  ? 3686 VAL A CA    1 
ATOM   16161 C  C     . VAL A 1 3686 ? 199.547 245.727 183.513 1.00 7.71  ? 3686 VAL A C     1 
ATOM   16162 O  O     . VAL A 1 3686 ? 200.148 246.082 182.491 1.00 8.79  ? 3686 VAL A O     1 
ATOM   16163 C  CB    . VAL A 1 3686 ? 197.897 243.840 183.120 1.00 8.64  ? 3686 VAL A CB    1 
ATOM   16164 C  CG1   . VAL A 1 3686 ? 198.548 243.511 181.792 1.00 6.63  ? 3686 VAL A CG1   1 
ATOM   16165 C  CG2   . VAL A 1 3686 ? 198.462 242.961 184.227 1.00 9.51  ? 3686 VAL A CG2   1 
ATOM   16166 N  N     . GLU A 1 3687 ? 200.123 245.699 184.711 1.00 10.49 ? 3687 GLU A N     1 
ATOM   16167 C  CA    . GLU A 1 3687 ? 201.522 246.050 184.907 1.00 6.93  ? 3687 GLU A CA    1 
ATOM   16168 C  C     . GLU A 1 3687 ? 202.337 244.778 185.101 1.00 4.73  ? 3687 GLU A C     1 
ATOM   16169 O  O     . GLU A 1 3687 ? 201.984 243.929 185.925 1.00 11.46 ? 3687 GLU A O     1 
ATOM   16170 C  CB    . GLU A 1 3687 ? 201.689 246.972 186.115 1.00 9.19  ? 3687 GLU A CB    1 
ATOM   16171 C  CG    . GLU A 1 3687 ? 200.658 248.080 186.200 1.00 16.00 ? 3687 GLU A CG    1 
ATOM   16172 C  CD    . GLU A 1 3687 ? 201.159 249.396 185.643 1.00 21.51 ? 3687 GLU A CD    1 
ATOM   16173 O  OE1   . GLU A 1 3687 ? 202.233 249.405 185.006 1.00 24.15 ? 3687 GLU A OE1   1 
ATOM   16174 O  OE2   . GLU A 1 3687 ? 200.480 250.423 185.842 1.00 27.88 ? 3687 GLU A OE2   1 
ATOM   16175 N  N     . PHE A 1 3688 ? 203.414 244.647 184.340 1.00 4.23  ? 3688 PHE A N     1 
ATOM   16176 C  CA    . PHE A 1 3688 ? 204.133 243.436 184.689 1.00 4.45  ? 3688 PHE A CA    1 
ATOM   16177 C  C     . PHE A 1 3688 ? 205.400 243.764 185.464 1.00 7.81  ? 3688 PHE A C     1 
ATOM   16178 O  O     . PHE A 1 3688 ? 205.996 244.829 185.259 1.00 8.67  ? 3688 PHE A O     1 
ATOM   16179 C  CB    . PHE A 1 3688 ? 204.494 242.629 183.439 1.00 4.01  ? 3688 PHE A CB    1 
ATOM   16180 C  CG    . PHE A 1 3688 ? 203.306 242.178 182.647 1.00 4.84  ? 3688 PHE A CG    1 
ATOM   16181 C  CD1   . PHE A 1 3688 ? 202.601 241.048 183.020 1.00 3.79  ? 3688 PHE A CD1   1 
ATOM   16182 C  CD2   . PHE A 1 3688 ? 202.901 242.869 181.522 1.00 3.32  ? 3688 PHE A CD2   1 
ATOM   16183 C  CE1   . PHE A 1 3688 ? 201.512 240.627 182.294 1.00 3.43  ? 3688 PHE A CE1   1 
ATOM   16184 C  CE2   . PHE A 1 3688 ? 201.812 242.452 180.790 1.00 2.26  ? 3688 PHE A CE2   1 
ATOM   16185 C  CZ    . PHE A 1 3688 ? 201.119 241.327 181.175 1.00 3.15  ? 3688 PHE A CZ    1 
ATOM   16186 N  N     . PRO A 1 3689 ? 205.817 242.875 186.366 1.00 6.84  ? 3689 PRO A N     1 
ATOM   16187 C  CA    . PRO A 1 3689 ? 207.062 243.107 187.092 1.00 6.14  ? 3689 PRO A CA    1 
ATOM   16188 C  C     . PRO A 1 3689 ? 208.252 243.050 186.155 1.00 4.26  ? 3689 PRO A C     1 
ATOM   16189 O  O     . PRO A 1 3689 ? 208.200 242.398 185.098 1.00 6.26  ? 3689 PRO A O     1 
ATOM   16190 C  CB    . PRO A 1 3689 ? 207.090 241.957 188.116 1.00 5.73  ? 3689 PRO A CB    1 
ATOM   16191 C  CG    . PRO A 1 3689 ? 206.289 240.886 187.471 1.00 5.56  ? 3689 PRO A CG    1 
ATOM   16192 C  CD    . PRO A 1 3689 ? 205.175 241.611 186.770 1.00 5.77  ? 3689 PRO A CD    1 
ATOM   16193 N  N     . PRO A 1 3690 ? 209.348 243.738 186.488 1.00 7.53  ? 3690 PRO A N     1 
ATOM   16194 C  CA    . PRO A 1 3690 ? 210.495 243.791 185.566 1.00 5.38  ? 3690 PRO A CA    1 
ATOM   16195 C  C     . PRO A 1 3690 ? 211.080 242.433 185.222 1.00 3.90  ? 3690 PRO A C     1 
ATOM   16196 O  O     . PRO A 1 3690 ? 211.632 242.270 184.126 1.00 3.32  ? 3690 PRO A O     1 
ATOM   16197 C  CB    . PRO A 1 3690 ? 211.505 244.664 186.323 1.00 5.15  ? 3690 PRO A CB    1 
ATOM   16198 C  CG    . PRO A 1 3690 ? 210.662 245.504 187.221 1.00 6.85  ? 3690 PRO A CG    1 
ATOM   16199 C  CD    . PRO A 1 3690 ? 209.548 244.602 187.664 1.00 6.71  ? 3690 PRO A CD    1 
ATOM   16200 N  N     . ASP A 1 3691 ? 210.992 241.456 186.127 1.00 4.14  ? 3691 ASP A N     1 
ATOM   16201 C  CA    . ASP A 1 3691 ? 211.536 240.131 185.840 1.00 5.85  ? 3691 ASP A CA    1 
ATOM   16202 C  C     . ASP A 1 3691 ? 210.784 239.457 184.696 1.00 5.19  ? 3691 ASP A C     1 
ATOM   16203 O  O     . ASP A 1 3691 ? 211.394 238.813 183.834 1.00 5.77  ? 3691 ASP A O     1 
ATOM   16204 C  CB    . ASP A 1 3691 ? 211.521 239.271 187.109 1.00 7.52  ? 3691 ASP A CB    1 
ATOM   16205 C  CG    . ASP A 1 3691 ? 210.122 239.022 187.643 1.00 16.88 ? 3691 ASP A CG    1 
ATOM   16206 O  OD1   . ASP A 1 3691 ? 209.145 239.543 187.065 1.00 17.34 ? 3691 ASP A OD1   1 
ATOM   16207 O  OD2   . ASP A 1 3691 ? 209.999 238.299 188.653 1.00 24.80 ? 3691 ASP A OD2   1 
ATOM   16208 N  N     . LEU A 1 3692 ? 209.456 239.593 184.669 1.00 5.18  ? 3692 LEU A N     1 
ATOM   16209 C  CA    . LEU A 1 3692 ? 208.681 239.036 183.564 1.00 2.20  ? 3692 LEU A CA    1 
ATOM   16210 C  C     . LEU A 1 3692 ? 208.933 239.800 182.270 1.00 1.86  ? 3692 LEU A C     1 
ATOM   16211 O  O     . LEU A 1 3692 ? 208.978 239.201 181.189 1.00 2.11  ? 3692 LEU A O     1 
ATOM   16212 C  CB    . LEU A 1 3692 ? 207.192 239.037 183.906 1.00 4.36  ? 3692 LEU A CB    1 
ATOM   16213 C  CG    . LEU A 1 3692 ? 206.274 238.266 182.949 1.00 3.42  ? 3692 LEU A CG    1 
ATOM   16214 C  CD1   . LEU A 1 3692 ? 206.718 236.819 182.795 1.00 0.68  ? 3692 LEU A CD1   1 
ATOM   16215 C  CD2   . LEU A 1 3692 ? 204.830 238.335 183.408 1.00 2.24  ? 3692 LEU A CD2   1 
ATOM   16216 N  N     . CYS A 1 3693 ? 209.096 241.124 182.360 1.00 3.29  ? 3693 CYS A N     1 
ATOM   16217 C  CA    . CYS A 1 3693 ? 209.325 241.928 181.166 1.00 2.12  ? 3693 CYS A CA    1 
ATOM   16218 C  C     . CYS A 1 3693 ? 210.620 241.545 180.466 1.00 2.02  ? 3693 CYS A C     1 
ATOM   16219 O  O     . CYS A 1 3693 ? 210.727 241.680 179.244 1.00 3.12  ? 3693 CYS A O     1 
ATOM   16220 C  CB    . CYS A 1 3693 ? 209.336 243.414 181.529 1.00 1.69  ? 3693 CYS A CB    1 
ATOM   16221 S  SG    . CYS A 1 3693 ? 207.788 244.030 182.216 1.00 6.74  ? 3693 CYS A SG    1 
ATOM   16222 N  N     . SER A 1 3694 ? 211.614 241.074 181.222 1.00 1.73  ? 3694 SER A N     1 
ATOM   16223 C  CA    . SER A 1 3694 ? 212.879 240.667 180.628 1.00 1.04  ? 3694 SER A CA    1 
ATOM   16224 C  C     . SER A 1 3694 ? 212.801 239.305 179.950 1.00 0.97  ? 3694 SER A C     1 
ATOM   16225 O  O     . SER A 1 3694 ? 213.670 238.985 179.135 1.00 1.14  ? 3694 SER A O     1 
ATOM   16226 C  CB    . SER A 1 3694 ? 213.975 240.652 181.697 1.00 1.33  ? 3694 SER A CB    1 
ATOM   16227 O  OG    . SER A 1 3694 ? 213.666 239.740 182.735 1.00 4.22  ? 3694 SER A OG    1 
ATOM   16228 N  N     . ARG A 1 3695 ? 211.789 238.500 180.260 1.00 1.30  ? 3695 ARG A N     1 
ATOM   16229 C  CA    . ARG A 1 3695 ? 211.698 237.138 179.753 1.00 0.99  ? 3695 ARG A CA    1 
ATOM   16230 C  C     . ARG A 1 3695 ? 210.785 236.997 178.545 1.00 0.80  ? 3695 ARG A C     1 
ATOM   16231 O  O     . ARG A 1 3695 ? 210.730 235.914 177.954 1.00 0.54  ? 3695 ARG A O     1 
ATOM   16232 C  CB    . ARG A 1 3695 ? 211.219 236.200 180.862 1.00 1.22  ? 3695 ARG A CB    1 
ATOM   16233 C  CG    . ARG A 1 3695 ? 212.146 236.128 182.051 1.00 1.41  ? 3695 ARG A CG    1 
ATOM   16234 C  CD    . ARG A 1 3695 ? 211.580 235.237 183.138 1.00 1.22  ? 3695 ARG A CD    1 
ATOM   16235 N  NE    . ARG A 1 3695 ? 211.858 235.764 184.468 1.00 2.53  ? 3695 ARG A NE    1 
ATOM   16236 C  CZ    . ARG A 1 3695 ? 212.564 235.129 185.391 1.00 2.65  ? 3695 ARG A CZ    1 
ATOM   16237 N  NH1   . ARG A 1 3695 ? 213.096 233.940 185.157 1.00 2.34  ? 3695 ARG A NH1   1 
ATOM   16238 N  NH2   . ARG A 1 3695 ? 212.748 235.702 186.575 1.00 2.69  ? 3695 ARG A NH2   1 
ATOM   16239 N  N     . VAL A 1 3696 ? 210.072 238.054 178.151 1.00 1.00  ? 3696 VAL A N     1 
ATOM   16240 C  CA    . VAL A 1 3696 ? 209.055 237.952 177.117 1.00 0.81  ? 3696 VAL A CA    1 
ATOM   16241 C  C     . VAL A 1 3696 ? 209.294 239.007 176.049 1.00 0.32  ? 3696 VAL A C     1 
ATOM   16242 O  O     . VAL A 1 3696 ? 210.047 239.965 176.238 1.00 5.18  ? 3696 VAL A O     1 
ATOM   16243 C  CB    . VAL A 1 3696 ? 207.623 238.093 177.683 1.00 0.63  ? 3696 VAL A CB    1 
ATOM   16244 C  CG1   . VAL A 1 3696 ? 207.334 236.996 178.695 1.00 0.27  ? 3696 VAL A CG1   1 
ATOM   16245 C  CG2   . VAL A 1 3696 ? 207.426 239.471 178.293 1.00 0.41  ? 3696 VAL A CG2   1 
ATOM   16246 N  N     . THR A 1 3697 ? 208.643 238.809 174.909 1.00 0.25  ? 3697 THR A N     1 
ATOM   16247 C  CA    . THR A 1 3697 ? 208.584 239.788 173.830 1.00 0.24  ? 3697 THR A CA    1 
ATOM   16248 C  C     . THR A 1 3697 ? 207.178 240.375 173.831 1.00 0.11  ? 3697 THR A C     1 
ATOM   16249 O  O     . THR A 1 3697 ? 206.206 239.668 173.556 1.00 0.14  ? 3697 THR A O     1 
ATOM   16250 C  CB    . THR A 1 3697 ? 208.909 239.146 172.481 1.00 0.42  ? 3697 THR A CB    1 
ATOM   16251 O  OG1   . THR A 1 3697 ? 210.257 238.666 172.487 1.00 1.23  ? 3697 THR A OG1   1 
ATOM   16252 C  CG2   . THR A 1 3697 ? 208.733 240.150 171.352 1.00 1.11  ? 3697 THR A CG2   1 
ATOM   16253 N  N     . PHE A 1 3698 ? 207.066 241.659 174.151 1.00 0.13  ? 3698 PHE A N     1 
ATOM   16254 C  CA    . PHE A 1 3698 ? 205.753 242.288 174.201 1.00 0.16  ? 3698 PHE A CA    1 
ATOM   16255 C  C     . PHE A 1 3698 ? 205.238 242.540 172.791 1.00 0.13  ? 3698 PHE A C     1 
ATOM   16256 O  O     . PHE A 1 3698 ? 205.936 243.119 171.955 1.00 0.55  ? 3698 PHE A O     1 
ATOM   16257 C  CB    . PHE A 1 3698 ? 205.812 243.591 174.993 1.00 0.12  ? 3698 PHE A CB    1 
ATOM   16258 C  CG    . PHE A 1 3698 ? 205.796 243.391 176.478 1.00 0.22  ? 3698 PHE A CG    1 
ATOM   16259 C  CD1   . PHE A 1 3698 ? 204.646 242.969 177.119 1.00 0.16  ? 3698 PHE A CD1   1 
ATOM   16260 C  CD2   . PHE A 1 3698 ? 206.933 243.617 177.232 1.00 0.54  ? 3698 PHE A CD2   1 
ATOM   16261 C  CE1   . PHE A 1 3698 ? 204.629 242.779 178.485 1.00 0.21  ? 3698 PHE A CE1   1 
ATOM   16262 C  CE2   . PHE A 1 3698 ? 206.922 243.428 178.598 1.00 0.82  ? 3698 PHE A CE2   1 
ATOM   16263 C  CZ    . PHE A 1 3698 ? 205.769 243.008 179.223 1.00 0.53  ? 3698 PHE A CZ    1 
ATOM   16264 N  N     . VAL A 1 3699 ? 204.017 242.087 172.526 1.00 0.10  ? 3699 VAL A N     1 
ATOM   16265 C  CA    . VAL A 1 3699 ? 203.350 242.275 171.241 1.00 0.17  ? 3699 VAL A CA    1 
ATOM   16266 C  C     . VAL A 1 3699 ? 201.977 242.853 171.562 1.00 0.14  ? 3699 VAL A C     1 
ATOM   16267 O  O     . VAL A 1 3699 ? 201.054 242.115 171.919 1.00 0.19  ? 3699 VAL A O     1 
ATOM   16268 C  CB    . VAL A 1 3699 ? 203.234 240.971 170.443 1.00 0.18  ? 3699 VAL A CB    1 
ATOM   16269 C  CG1   . VAL A 1 3699 ? 202.533 241.222 169.129 1.00 0.13  ? 3699 VAL A CG1   1 
ATOM   16270 C  CG2   . VAL A 1 3699 ? 204.605 240.361 170.208 1.00 0.14  ? 3699 VAL A CG2   1 
ATOM   16271 N  N     . ASN A 1 3700 ? 201.838 244.169 171.439 1.00 0.20  ? 3700 ASN A N     1 
ATOM   16272 C  CA    . ASN A 1 3700 ? 200.648 244.880 171.889 1.00 0.65  ? 3700 ASN A CA    1 
ATOM   16273 C  C     . ASN A 1 3700 ? 199.732 245.147 170.702 1.00 0.44  ? 3700 ASN A C     1 
ATOM   16274 O  O     . ASN A 1 3700 ? 200.144 245.767 169.719 1.00 0.31  ? 3700 ASN A O     1 
ATOM   16275 C  CB    . ASN A 1 3700 ? 201.035 246.185 172.584 1.00 0.75  ? 3700 ASN A CB    1 
ATOM   16276 C  CG    . ASN A 1 3700 ? 199.925 246.738 173.449 1.00 0.62  ? 3700 ASN A CG    1 
ATOM   16277 O  OD1   . ASN A 1 3700 ? 198.795 246.256 173.416 1.00 1.01  ? 3700 ASN A OD1   1 
ATOM   16278 N  ND2   . ASN A 1 3700 ? 200.244 247.753 174.238 1.00 0.94  ? 3700 ASN A ND2   1 
ATOM   16279 N  N     . PHE A 1 3701 ? 198.490 244.679 170.802 1.00 1.02  ? 3701 PHE A N     1 
ATOM   16280 C  CA    . PHE A 1 3701 ? 197.484 244.872 169.760 1.00 0.91  ? 3701 PHE A CA    1 
ATOM   16281 C  C     . PHE A 1 3701 ? 196.603 246.039 170.186 1.00 1.76  ? 3701 PHE A C     1 
ATOM   16282 O  O     . PHE A 1 3701 ? 195.592 245.867 170.869 1.00 5.53  ? 3701 PHE A O     1 
ATOM   16283 C  CB    . PHE A 1 3701 ? 196.675 243.601 169.540 1.00 0.87  ? 3701 PHE A CB    1 
ATOM   16284 C  CG    . PHE A 1 3701 ? 197.391 242.557 168.734 1.00 0.78  ? 3701 PHE A CG    1 
ATOM   16285 C  CD1   . PHE A 1 3701 ? 198.385 241.779 169.307 1.00 0.33  ? 3701 PHE A CD1   1 
ATOM   16286 C  CD2   . PHE A 1 3701 ? 197.070 242.352 167.404 1.00 0.46  ? 3701 PHE A CD2   1 
ATOM   16287 C  CE1   . PHE A 1 3701 ? 199.044 240.820 168.568 1.00 0.23  ? 3701 PHE A CE1   1 
ATOM   16288 C  CE2   . PHE A 1 3701 ? 197.726 241.391 166.660 1.00 0.26  ? 3701 PHE A CE2   1 
ATOM   16289 C  CZ    . PHE A 1 3701 ? 198.711 240.623 167.242 1.00 0.25  ? 3701 PHE A CZ    1 
ATOM   16290 N  N     . THR A 1 3702 ? 196.996 247.242 169.782 1.00 2.64  ? 3702 THR A N     1 
ATOM   16291 C  CA    . THR A 1 3702 ? 196.240 248.449 170.074 1.00 1.87  ? 3702 THR A CA    1 
ATOM   16292 C  C     . THR A 1 3702 ? 195.473 248.890 168.838 1.00 3.06  ? 3702 THR A C     1 
ATOM   16293 O  O     . THR A 1 3702 ? 195.958 248.751 167.711 1.00 4.80  ? 3702 THR A O     1 
ATOM   16294 C  CB    . THR A 1 3702 ? 197.156 249.579 170.550 1.00 3.67  ? 3702 THR A CB    1 
ATOM   16295 O  OG1   . THR A 1 3702 ? 197.915 250.082 169.444 1.00 2.60  ? 3702 THR A OG1   1 
ATOM   16296 C  CG2   . THR A 1 3702 ? 198.099 249.083 171.632 1.00 2.15  ? 3702 THR A CG2   1 
ATOM   16297 N  N     . VAL A 1 3703 ? 194.270 249.416 169.054 1.00 3.45  ? 3703 VAL A N     1 
ATOM   16298 C  CA    . VAL A 1 3703 ? 193.453 249.895 167.950 1.00 2.05  ? 3703 VAL A CA    1 
ATOM   16299 C  C     . VAL A 1 3703 ? 194.044 251.192 167.413 1.00 1.10  ? 3703 VAL A C     1 
ATOM   16300 O  O     . VAL A 1 3703 ? 194.285 252.144 168.166 1.00 1.58  ? 3703 VAL A O     1 
ATOM   16301 C  CB    . VAL A 1 3703 ? 191.997 250.089 168.401 1.00 1.64  ? 3703 VAL A CB    1 
ATOM   16302 C  CG1   . VAL A 1 3703 ? 191.180 250.755 167.306 1.00 1.68  ? 3703 VAL A CG1   1 
ATOM   16303 C  CG2   . VAL A 1 3703 ? 191.389 248.759 168.795 1.00 1.33  ? 3703 VAL A CG2   1 
ATOM   16304 N  N     . THR A 1 3704 ? 194.286 251.231 166.110 1.00 2.23  ? 3704 THR A N     1 
ATOM   16305 C  CA    . THR A 1 3704 ? 194.755 252.431 165.437 1.00 2.53  ? 3704 THR A CA    1 
ATOM   16306 C  C     . THR A 1 3704 ? 193.586 253.139 164.766 1.00 2.34  ? 3704 THR A C     1 
ATOM   16307 O  O     . THR A 1 3704 ? 192.556 252.536 164.459 1.00 3.22  ? 3704 THR A O     1 
ATOM   16308 C  CB    . THR A 1 3704 ? 195.835 252.097 164.403 1.00 4.95  ? 3704 THR A CB    1 
ATOM   16309 O  OG1   . THR A 1 3704 ? 195.231 251.509 163.245 1.00 5.10  ? 3704 THR A OG1   1 
ATOM   16310 C  CG2   . THR A 1 3704 ? 196.848 251.129 164.987 1.00 2.40  ? 3704 THR A CG2   1 
ATOM   16311 N  N     . ARG A 1 3705 ? 193.759 254.445 164.547 1.00 2.59  ? 3705 ARG A N     1 
ATOM   16312 C  CA    . ARG A 1 3705 ? 192.694 255.238 163.944 1.00 2.90  ? 3705 ARG A CA    1 
ATOM   16313 C  C     . ARG A 1 3705 ? 192.380 254.764 162.532 1.00 3.73  ? 3705 ARG A C     1 
ATOM   16314 O  O     . ARG A 1 3705 ? 191.208 254.698 162.140 1.00 5.71  ? 3705 ARG A O     1 
ATOM   16315 C  CB    . ARG A 1 3705 ? 193.078 256.718 163.942 1.00 3.62  ? 3705 ARG A CB    1 
ATOM   16316 C  CG    . ARG A 1 3705 ? 192.998 257.366 165.307 1.00 4.74  ? 3705 ARG A CG    1 
ATOM   16317 C  CD    . ARG A 1 3705 ? 193.559 258.775 165.294 1.00 6.93  ? 3705 ARG A CD    1 
ATOM   16318 N  NE    . ARG A 1 3705 ? 193.310 259.471 166.551 1.00 6.26  ? 3705 ARG A NE    1 
ATOM   16319 C  CZ    . ARG A 1 3705 ? 192.127 259.938 166.931 1.00 7.96  ? 3705 ARG A CZ    1 
ATOM   16320 N  NH1   . ARG A 1 3705 ? 191.057 259.818 166.163 1.00 4.14  ? 3705 ARG A NH1   1 
ATOM   16321 N  NH2   . ARG A 1 3705 ? 192.018 260.546 168.108 1.00 5.76  ? 3705 ARG A NH2   1 
ATOM   16322 N  N     . SER A 1 3706 ? 193.410 254.434 161.751 1.00 3.20  ? 3706 SER A N     1 
ATOM   16323 C  CA    . SER A 1 3706 ? 193.187 253.962 160.390 1.00 2.25  ? 3706 SER A CA    1 
ATOM   16324 C  C     . SER A 1 3706 ? 192.460 252.622 160.372 1.00 3.44  ? 3706 SER A C     1 
ATOM   16325 O  O     . SER A 1 3706 ? 191.553 252.415 159.556 1.00 4.50  ? 3706 SER A O     1 
ATOM   16326 C  CB    . SER A 1 3706 ? 194.518 253.860 159.646 1.00 4.37  ? 3706 SER A CB    1 
ATOM   16327 O  OG    . SER A 1 3706 ? 195.361 252.894 160.243 1.00 9.37  ? 3706 SER A OG    1 
ATOM   16328 N  N     . SER A 1 3707 ? 192.850 251.697 161.251 1.00 2.96  ? 3707 SER A N     1 
ATOM   16329 C  CA    . SER A 1 3707 ? 192.217 250.382 161.264 1.00 2.58  ? 3707 SER A CA    1 
ATOM   16330 C  C     . SER A 1 3707 ? 190.752 250.475 161.665 1.00 3.31  ? 3707 SER A C     1 
ATOM   16331 O  O     . SER A 1 3707 ? 189.898 249.796 161.085 1.00 5.91  ? 3707 SER A O     1 
ATOM   16332 C  CB    . SER A 1 3707 ? 192.974 249.439 162.198 1.00 3.56  ? 3707 SER A CB    1 
ATOM   16333 O  OG    . SER A 1 3707 ? 192.981 249.924 163.528 1.00 9.39  ? 3707 SER A OG    1 
ATOM   16334 N  N     . LEU A 1 3708 ? 190.442 251.308 162.660 1.00 4.16  ? 3708 LEU A N     1 
ATOM   16335 C  CA    . LEU A 1 3708 ? 189.051 251.488 163.063 1.00 1.85  ? 3708 LEU A CA    1 
ATOM   16336 C  C     . LEU A 1 3708 ? 188.243 252.171 161.966 1.00 1.88  ? 3708 LEU A C     1 
ATOM   16337 O  O     . LEU A 1 3708 ? 187.068 251.845 161.761 1.00 2.04  ? 3708 LEU A O     1 
ATOM   16338 C  CB    . LEU A 1 3708 ? 188.983 252.281 164.364 1.00 2.52  ? 3708 LEU A CB    1 
ATOM   16339 C  CG    . LEU A 1 3708 ? 187.597 252.409 164.993 1.00 1.75  ? 3708 LEU A CG    1 
ATOM   16340 C  CD1   . LEU A 1 3708 ? 186.922 251.053 165.101 1.00 2.41  ? 3708 LEU A CD1   1 
ATOM   16341 C  CD2   . LEU A 1 3708 ? 187.708 253.057 166.350 1.00 0.99  ? 3708 LEU A CD2   1 
ATOM   16342 N  N     . GLN A 1 3709 ? 188.851 253.122 161.254 1.00 2.17  ? 3709 GLN A N     1 
ATOM   16343 C  CA    . GLN A 1 3709 ? 188.167 253.752 160.129 1.00 2.21  ? 3709 GLN A CA    1 
ATOM   16344 C  C     . GLN A 1 3709 ? 187.827 252.732 159.051 1.00 2.75  ? 3709 GLN A C     1 
ATOM   16345 O  O     . GLN A 1 3709 ? 186.724 252.749 158.496 1.00 7.47  ? 3709 GLN A O     1 
ATOM   16346 C  CB    . GLN A 1 3709 ? 189.022 254.877 159.548 1.00 2.22  ? 3709 GLN A CB    1 
ATOM   16347 C  CG    . GLN A 1 3709 ? 188.881 256.202 160.265 1.00 2.40  ? 3709 GLN A CG    1 
ATOM   16348 C  CD    . GLN A 1 3709 ? 190.121 257.066 160.149 1.00 11.14 ? 3709 GLN A CD    1 
ATOM   16349 O  OE1   . GLN A 1 3709 ? 190.995 256.813 159.318 1.00 13.87 ? 3709 GLN A OE1   1 
ATOM   16350 N  NE2   . GLN A 1 3709 ? 190.203 258.097 160.983 1.00 9.68  ? 3709 GLN A NE2   1 
ATOM   16351 N  N     . SER A 1 3710 ? 188.768 251.834 158.737 1.00 2.88  ? 3710 SER A N     1 
ATOM   16352 C  CA    . SER A 1 3710 ? 188.489 250.781 157.766 1.00 3.07  ? 3710 SER A CA    1 
ATOM   16353 C  C     . SER A 1 3710 ? 187.387 249.855 158.260 1.00 3.78  ? 3710 SER A C     1 
ATOM   16354 O  O     . SER A 1 3710 ? 186.514 249.447 157.486 1.00 6.15  ? 3710 SER A O     1 
ATOM   16355 C  CB    . SER A 1 3710 ? 189.760 249.985 157.470 1.00 4.86  ? 3710 SER A CB    1 
ATOM   16356 O  OG    . SER A 1 3710 ? 190.745 250.792 156.854 1.00 12.56 ? 3710 SER A OG    1 
ATOM   16357 N  N     . GLN A 1 3711 ? 187.417 249.505 159.549 1.00 2.05  ? 3711 GLN A N     1 
ATOM   16358 C  CA    . GLN A 1 3711 ? 186.393 248.627 160.105 1.00 2.65  ? 3711 GLN A CA    1 
ATOM   16359 C  C     . GLN A 1 3711 ? 185.012 249.258 160.015 1.00 2.56  ? 3711 GLN A C     1 
ATOM   16360 O  O     . GLN A 1 3711 ? 184.039 248.593 159.645 1.00 4.07  ? 3711 GLN A O     1 
ATOM   16361 C  CB    . GLN A 1 3711 ? 186.721 248.289 161.559 1.00 3.51  ? 3711 GLN A CB    1 
ATOM   16362 C  CG    . GLN A 1 3711 ? 187.848 247.299 161.741 1.00 4.84  ? 3711 GLN A CG    1 
ATOM   16363 C  CD    . GLN A 1 3711 ? 188.203 247.096 163.200 1.00 10.11 ? 3711 GLN A CD    1 
ATOM   16364 O  OE1   . GLN A 1 3711 ? 189.365 247.206 163.591 1.00 12.56 ? 3711 GLN A OE1   1 
ATOM   16365 N  NE2   . GLN A 1 3711 ? 187.197 246.806 164.017 1.00 10.04 ? 3711 GLN A NE2   1 
ATOM   16366 N  N     . CYS A 1 3712 ? 184.905 250.543 160.354 1.00 3.19  ? 3712 CYS A N     1 
ATOM   16367 C  CA    . CYS A 1 3712 ? 183.610 251.209 160.343 1.00 2.49  ? 3712 CYS A CA    1 
ATOM   16368 C  C     . CYS A 1 3712 ? 183.149 251.540 158.931 1.00 2.63  ? 3712 CYS A C     1 
ATOM   16369 O  O     . CYS A 1 3712 ? 181.946 251.509 158.659 1.00 5.65  ? 3712 CYS A O     1 
ATOM   16370 C  CB    . CYS A 1 3712 ? 183.667 252.469 161.203 1.00 1.96  ? 3712 CYS A CB    1 
ATOM   16371 S  SG    . CYS A 1 3712 ? 184.087 252.140 162.929 1.00 2.49  ? 3712 CYS A SG    1 
ATOM   16372 N  N     . LEU A 1 3713 ? 184.081 251.858 158.029 1.00 2.18  ? 3713 LEU A N     1 
ATOM   16373 C  CA    . LEU A 1 3713 ? 183.707 252.057 156.633 1.00 3.10  ? 3713 LEU A CA    1 
ATOM   16374 C  C     . LEU A 1 3713 ? 183.168 250.770 156.023 1.00 3.26  ? 3713 LEU A C     1 
ATOM   16375 O  O     . LEU A 1 3713 ? 182.187 250.790 155.272 1.00 4.68  ? 3713 LEU A O     1 
ATOM   16376 C  CB    . LEU A 1 3713 ? 184.904 252.568 155.832 1.00 4.27  ? 3713 LEU A CB    1 
ATOM   16377 C  CG    . LEU A 1 3713 ? 184.693 252.672 154.321 1.00 3.12  ? 3713 LEU A CG    1 
ATOM   16378 C  CD1   . LEU A 1 3713 ? 183.710 253.782 153.999 1.00 3.80  ? 3713 LEU A CD1   1 
ATOM   16379 C  CD2   . LEU A 1 3713 ? 186.009 252.894 153.601 1.00 7.11  ? 3713 LEU A CD2   1 
ATOM   16380 N  N     . ASN A 1 3714 ? 183.799 249.636 156.338 1.00 3.29  ? 3714 ASN A N     1 
ATOM   16381 C  CA    . ASN A 1 3714 ? 183.321 248.360 155.818 1.00 5.69  ? 3714 ASN A CA    1 
ATOM   16382 C  C     . ASN A 1 3714 ? 181.963 247.996 156.403 1.00 5.50  ? 3714 ASN A C     1 
ATOM   16383 O  O     . ASN A 1 3714 ? 181.098 247.471 155.694 1.00 7.35  ? 3714 ASN A O     1 
ATOM   16384 C  CB    . ASN A 1 3714 ? 184.340 247.258 156.108 1.00 6.78  ? 3714 ASN A CB    1 
ATOM   16385 C  CG    . ASN A 1 3714 ? 185.579 247.365 155.242 1.00 10.38 ? 3714 ASN A CG    1 
ATOM   16386 O  OD1   . ASN A 1 3714 ? 185.637 248.174 154.315 1.00 10.34 ? 3714 ASN A OD1   1 
ATOM   16387 N  ND2   . ASN A 1 3714 ? 186.579 246.546 155.540 1.00 15.05 ? 3714 ASN A ND2   1 
ATOM   16388 N  N     . GLU A 1 3715 ? 181.760 248.258 157.696 1.00 5.45  ? 3715 GLU A N     1 
ATOM   16389 C  CA    . GLU A 1 3715 ? 180.513 247.858 158.339 1.00 6.76  ? 3715 GLU A CA    1 
ATOM   16390 C  C     . GLU A 1 3715 ? 179.322 248.641 157.796 1.00 6.55  ? 3715 GLU A C     1 
ATOM   16391 O  O     . GLU A 1 3715 ? 178.253 248.065 157.564 1.00 9.06  ? 3715 GLU A O     1 
ATOM   16392 C  CB    . GLU A 1 3715 ? 180.625 248.019 159.856 1.00 6.71  ? 3715 GLU A CB    1 
ATOM   16393 C  CG    . GLU A 1 3715 ? 179.382 247.581 160.608 1.00 12.65 ? 3715 GLU A CG    1 
ATOM   16394 C  CD    . GLU A 1 3715 ? 179.106 246.090 160.479 1.00 26.30 ? 3715 GLU A CD    1 
ATOM   16395 O  OE1   . GLU A 1 3715 ? 180.063 245.319 160.251 1.00 31.23 ? 3715 GLU A OE1   1 
ATOM   16396 O  OE2   . GLU A 1 3715 ? 177.929 245.689 160.597 1.00 29.16 ? 3715 GLU A OE2   1 
ATOM   16397 N  N     . VAL A 1 3716 ? 179.478 249.950 157.592 1.00 4.29  ? 3716 VAL A N     1 
ATOM   16398 C  CA    . VAL A 1 3716 ? 178.381 250.735 157.031 1.00 6.05  ? 3716 VAL A CA    1 
ATOM   16399 C  C     . VAL A 1 3716 ? 178.131 250.342 155.580 1.00 9.32  ? 3716 VAL A C     1 
ATOM   16400 O  O     . VAL A 1 3716 ? 176.985 250.327 155.116 1.00 10.30 ? 3716 VAL A O     1 
ATOM   16401 C  CB    . VAL A 1 3716 ? 178.651 252.247 157.181 1.00 3.53  ? 3716 VAL A CB    1 
ATOM   16402 C  CG1   . VAL A 1 3716 ? 179.887 252.675 156.412 1.00 3.88  ? 3716 VAL A CG1   1 
ATOM   16403 C  CG2   . VAL A 1 3716 ? 177.435 253.049 156.742 1.00 4.49  ? 3716 VAL A CG2   1 
ATOM   16404 N  N     . LEU A 1 3717 ? 179.195 250.008 154.843 1.00 6.09  ? 3717 LEU A N     1 
ATOM   16405 C  CA    . LEU A 1 3717 ? 179.027 249.519 153.480 1.00 5.21  ? 3717 LEU A CA    1 
ATOM   16406 C  C     . LEU A 1 3717 ? 178.229 248.221 153.459 1.00 7.74  ? 3717 LEU A C     1 
ATOM   16407 O  O     . LEU A 1 3717 ? 177.373 248.024 152.591 1.00 9.49  ? 3717 LEU A O     1 
ATOM   16408 C  CB    . LEU A 1 3717 ? 180.392 249.324 152.825 1.00 7.44  ? 3717 LEU A CB    1 
ATOM   16409 C  CG    . LEU A 1 3717 ? 180.480 249.526 151.313 1.00 13.63 ? 3717 LEU A CG    1 
ATOM   16410 C  CD1   . LEU A 1 3717 ? 180.334 250.994 150.951 1.00 7.91  ? 3717 LEU A CD1   1 
ATOM   16411 C  CD2   . LEU A 1 3717 ? 181.784 248.959 150.774 1.00 13.29 ? 3717 LEU A CD2   1 
ATOM   16412 N  N     . LYS A 1 3718 ? 178.500 247.326 154.410 1.00 8.34  ? 3718 LYS A N     1 
ATOM   16413 C  CA    . LYS A 1 3718 ? 177.743 246.084 154.500 1.00 9.12  ? 3718 LYS A CA    1 
ATOM   16414 C  C     . LYS A 1 3718 ? 176.274 246.350 154.810 1.00 12.42 ? 3718 LYS A C     1 
ATOM   16415 O  O     . LYS A 1 3718 ? 175.386 245.699 154.253 1.00 12.04 ? 3718 LYS A O     1 
ATOM   16416 C  CB    . LYS A 1 3718 ? 178.362 245.177 155.562 1.00 8.50  ? 3718 LYS A CB    1 
ATOM   16417 C  CG    . LYS A 1 3718 ? 177.684 243.831 155.708 1.00 12.40 ? 3718 LYS A CG    1 
ATOM   16418 C  CD    . LYS A 1 3718 ? 177.888 242.977 154.469 1.00 19.45 ? 3718 LYS A CD    1 
ATOM   16419 C  CE    . LYS A 1 3718 ? 177.197 241.631 154.610 1.00 24.73 ? 3718 LYS A CE    1 
ATOM   16420 N  NZ    . LYS A 1 3718 ? 177.821 240.804 155.679 1.00 25.35 ? 3718 LYS A NZ    1 
ATOM   16421 N  N     . ALA A 1 3719 ? 176.000 247.301 155.703 1.00 10.46 ? 3719 ALA A N     1 
ATOM   16422 C  CA    . ALA A 1 3719 ? 174.626 247.594 156.088 1.00 7.88  ? 3719 ALA A CA    1 
ATOM   16423 C  C     . ALA A 1 3719 ? 173.880 248.369 155.006 1.00 11.19 ? 3719 ALA A C     1 
ATOM   16424 O  O     . ALA A 1 3719 ? 172.709 248.085 154.736 1.00 14.60 ? 3719 ALA A O     1 
ATOM   16425 C  CB    . ALA A 1 3719 ? 174.605 248.373 157.403 1.00 8.42  ? 3719 ALA A CB    1 
ATOM   16426 N  N     . GLU A 1 3720 ? 174.534 249.343 154.380 1.00 15.44 ? 3720 GLU A N     1 
ATOM   16427 C  CA    . GLU A 1 3720 ? 173.863 250.283 153.490 1.00 10.05 ? 3720 GLU A CA    1 
ATOM   16428 C  C     . GLU A 1 3720 ? 173.923 249.889 152.022 1.00 11.07 ? 3720 GLU A C     1 
ATOM   16429 O  O     . GLU A 1 3720 ? 172.947 250.091 151.296 1.00 18.09 ? 3720 GLU A O     1 
ATOM   16430 C  CB    . GLU A 1 3720 ? 174.455 251.683 153.664 1.00 9.63  ? 3720 GLU A CB    1 
ATOM   16431 C  CG    . GLU A 1 3720 ? 174.036 252.347 154.954 1.00 10.37 ? 3720 GLU A CG    1 
ATOM   16432 C  CD    . GLU A 1 3720 ? 172.549 252.623 154.994 1.00 20.42 ? 3720 GLU A CD    1 
ATOM   16433 O  OE1   . GLU A 1 3720 ? 172.097 253.540 154.277 1.00 22.31 ? 3720 GLU A OE1   1 
ATOM   16434 O  OE2   . GLU A 1 3720 ? 171.830 251.913 155.730 1.00 18.54 ? 3720 GLU A OE2   1 
ATOM   16435 N  N     . ARG A 1 3721 ? 175.042 249.335 151.564 1.00 12.92 ? 3721 ARG A N     1 
ATOM   16436 C  CA    . ARG A 1 3721 ? 175.223 248.954 150.163 1.00 11.33 ? 3721 ARG A CA    1 
ATOM   16437 C  C     . ARG A 1 3721 ? 175.701 247.509 150.102 1.00 15.22 ? 3721 ARG A C     1 
ATOM   16438 O  O     . ARG A 1 3721 ? 176.856 247.238 149.760 1.00 17.07 ? 3721 ARG A O     1 
ATOM   16439 C  CB    . ARG A 1 3721 ? 176.209 249.891 149.464 1.00 12.76 ? 3721 ARG A CB    1 
ATOM   16440 C  CG    . ARG A 1 3721 ? 175.891 251.374 149.615 1.00 8.84  ? 3721 ARG A CG    1 
ATOM   16441 C  CD    . ARG A 1 3721 ? 174.541 251.718 149.011 1.00 11.96 ? 3721 ARG A CD    1 
ATOM   16442 N  NE    . ARG A 1 3721 ? 174.527 251.562 147.561 1.00 20.94 ? 3721 ARG A NE    1 
ATOM   16443 C  CZ    . ARG A 1 3721 ? 175.063 252.423 146.707 1.00 25.79 ? 3721 ARG A CZ    1 
ATOM   16444 N  NH1   . ARG A 1 3721 ? 175.644 253.537 147.121 1.00 18.84 ? 3721 ARG A NH1   1 
ATOM   16445 N  NH2   . ARG A 1 3721 ? 175.006 252.164 145.404 1.00 21.06 ? 3721 ARG A NH2   1 
ATOM   16446 N  N     . PRO A 1 3722 ? 174.829 246.552 150.437 1.00 17.52 ? 3722 PRO A N     1 
ATOM   16447 C  CA    . PRO A 1 3722 ? 175.263 245.146 150.459 1.00 13.88 ? 3722 PRO A CA    1 
ATOM   16448 C  C     . PRO A 1 3722 ? 175.755 244.640 149.114 1.00 15.65 ? 3722 PRO A C     1 
ATOM   16449 O  O     . PRO A 1 3722 ? 176.655 243.792 149.073 1.00 21.93 ? 3722 PRO A O     1 
ATOM   16450 C  CB    . PRO A 1 3722 ? 174.004 244.400 150.924 1.00 12.08 ? 3722 PRO A CB    1 
ATOM   16451 C  CG    . PRO A 1 3722 ? 172.877 245.307 150.566 1.00 13.66 ? 3722 PRO A CG    1 
ATOM   16452 C  CD    . PRO A 1 3722 ? 173.400 246.692 150.764 1.00 13.30 ? 3722 PRO A CD    1 
ATOM   16453 N  N     . ASP A 1 3723 ? 175.186 245.128 148.011 1.00 16.27 ? 3723 ASP A N     1 
ATOM   16454 C  CA    . ASP A 1 3723 ? 175.696 244.766 146.693 1.00 12.76 ? 3723 ASP A CA    1 
ATOM   16455 C  C     . ASP A 1 3723 ? 177.104 245.308 146.477 1.00 17.78 ? 3723 ASP A C     1 
ATOM   16456 O  O     . ASP A 1 3723 ? 177.963 244.616 145.916 1.00 20.71 ? 3723 ASP A O     1 
ATOM   16457 C  CB    . ASP A 1 3723 ? 174.744 245.268 145.608 1.00 17.72 ? 3723 ASP A CB    1 
ATOM   16458 C  CG    . ASP A 1 3723 ? 174.696 246.782 145.527 1.00 24.47 ? 3723 ASP A CG    1 
ATOM   16459 O  OD1   . ASP A 1 3723 ? 174.458 247.426 146.569 1.00 18.26 ? 3723 ASP A OD1   1 
ATOM   16460 O  OD2   . ASP A 1 3723 ? 174.895 247.328 144.420 1.00 28.87 ? 3723 ASP A OD2   1 
ATOM   16461 N  N     . VAL A 1 3724 ? 177.360 246.543 146.911 1.00 17.32 ? 3724 VAL A N     1 
ATOM   16462 C  CA    . VAL A 1 3724 ? 178.687 247.131 146.753 1.00 14.28 ? 3724 VAL A CA    1 
ATOM   16463 C  C     . VAL A 1 3724 ? 179.685 246.462 147.689 1.00 17.96 ? 3724 VAL A C     1 
ATOM   16464 O  O     . VAL A 1 3724 ? 180.834 246.203 147.310 1.00 19.22 ? 3724 VAL A O     1 
ATOM   16465 C  CB    . VAL A 1 3724 ? 178.624 248.652 146.980 1.00 12.96 ? 3724 VAL A CB    1 
ATOM   16466 C  CG1   . VAL A 1 3724 ? 180.010 249.273 146.861 1.00 15.38 ? 3724 VAL A CG1   1 
ATOM   16467 C  CG2   . VAL A 1 3724 ? 177.662 249.298 145.996 1.00 16.27 ? 3724 VAL A CG2   1 
ATOM   16468 N  N     . ASP A 1 3725 ? 179.271 246.182 148.928 1.00 18.20 ? 3725 ASP A N     1 
ATOM   16469 C  CA    . ASP A 1 3725 ? 180.181 245.565 149.888 1.00 15.04 ? 3725 ASP A CA    1 
ATOM   16470 C  C     . ASP A 1 3725 ? 180.584 244.165 149.444 1.00 20.02 ? 3725 ASP A C     1 
ATOM   16471 O  O     . ASP A 1 3725 ? 181.750 243.778 149.574 1.00 27.76 ? 3725 ASP A O     1 
ATOM   16472 C  CB    . ASP A 1 3725 ? 179.536 245.523 151.273 1.00 13.06 ? 3725 ASP A CB    1 
ATOM   16473 C  CG    . ASP A 1 3725 ? 180.551 245.315 152.378 1.00 16.88 ? 3725 ASP A CG    1 
ATOM   16474 O  OD1   . ASP A 1 3725 ? 181.403 246.203 152.579 1.00 16.18 ? 3725 ASP A OD1   1 
ATOM   16475 O  OD2   . ASP A 1 3725 ? 180.506 244.260 153.045 1.00 21.68 ? 3725 ASP A OD2   1 
ATOM   16476 N  N     . GLU A 1 3726 ? 179.630 243.391 148.922 1.00 18.89 ? 3726 GLU A N     1 
ATOM   16477 C  CA    . GLU A 1 3726 ? 179.952 242.060 148.420 1.00 18.40 ? 3726 GLU A CA    1 
ATOM   16478 C  C     . GLU A 1 3726 ? 180.913 242.135 147.241 1.00 21.50 ? 3726 GLU A C     1 
ATOM   16479 O  O     . GLU A 1 3726 ? 181.878 241.366 147.168 1.00 24.14 ? 3726 GLU A O     1 
ATOM   16480 C  CB    . GLU A 1 3726 ? 178.671 241.324 148.030 1.00 17.85 ? 3726 GLU A CB    1 
ATOM   16481 C  CG    . GLU A 1 3726 ? 178.886 239.896 147.568 1.00 23.61 ? 3726 GLU A CG    1 
ATOM   16482 C  CD    . GLU A 1 3726 ? 177.586 239.188 147.241 1.00 31.47 ? 3726 GLU A CD    1 
ATOM   16483 O  OE1   . GLU A 1 3726 ? 176.516 239.822 147.357 1.00 32.63 ? 3726 GLU A OE1   1 
ATOM   16484 O  OE2   . GLU A 1 3726 ? 177.632 237.997 146.870 1.00 35.40 ? 3726 GLU A OE2   1 
ATOM   16485 N  N     . LYS A 1 3727 ? 180.673 243.069 146.318 1.00 18.47 ? 3727 LYS A N     1 
ATOM   16486 C  CA    . LYS A 1 3727 ? 181.560 243.232 145.171 1.00 15.56 ? 3727 LYS A CA    1 
ATOM   16487 C  C     . LYS A 1 3727 ? 182.973 243.577 145.617 1.00 20.42 ? 3727 LYS A C     1 
ATOM   16488 O  O     . LYS A 1 3727 ? 183.953 243.083 145.045 1.00 27.89 ? 3727 LYS A O     1 
ATOM   16489 C  CB    . LYS A 1 3727 ? 181.006 244.307 144.234 1.00 16.94 ? 3727 LYS A CB    1 
ATOM   16490 C  CG    . LYS A 1 3727 ? 182.019 244.880 143.259 1.00 21.54 ? 3727 LYS A CG    1 
ATOM   16491 C  CD    . LYS A 1 3727 ? 181.444 246.054 142.481 1.00 21.17 ? 3727 LYS A CD    1 
ATOM   16492 C  CE    . LYS A 1 3727 ? 180.354 245.612 141.523 1.00 18.44 ? 3727 LYS A CE    1 
ATOM   16493 N  NZ    . LYS A 1 3727 ? 180.877 244.673 140.494 1.00 29.49 ? 3727 LYS A NZ    1 
ATOM   16494 N  N     . ARG A 1 3728 ? 183.100 244.424 146.640 1.00 15.40 ? 3728 ARG A N     1 
ATOM   16495 C  CA    . ARG A 1 3728 ? 184.414 244.753 147.179 1.00 17.19 ? 3728 ARG A CA    1 
ATOM   16496 C  C     . ARG A 1 3728 ? 185.099 243.521 147.761 1.00 19.44 ? 3728 ARG A C     1 
ATOM   16497 O  O     . ARG A 1 3728 ? 186.300 243.314 147.555 1.00 20.71 ? 3728 ARG A O     1 
ATOM   16498 C  CB    . ARG A 1 3728 ? 184.280 245.850 148.237 1.00 14.55 ? 3728 ARG A CB    1 
ATOM   16499 C  CG    . ARG A 1 3728 ? 185.544 246.134 149.023 1.00 12.95 ? 3728 ARG A CG    1 
ATOM   16500 C  CD    . ARG A 1 3728 ? 185.225 246.803 150.351 1.00 13.73 ? 3728 ARG A CD    1 
ATOM   16501 N  NE    . ARG A 1 3728 ? 184.628 245.874 151.301 1.00 19.43 ? 3728 ARG A NE    1 
ATOM   16502 C  CZ    . ARG A 1 3728 ? 185.311 245.157 152.183 1.00 21.08 ? 3728 ARG A CZ    1 
ATOM   16503 N  NH1   . ARG A 1 3728 ? 186.628 245.247 152.274 1.00 16.40 ? 3728 ARG A NH1   1 
ATOM   16504 N  NH2   . ARG A 1 3728 ? 184.658 244.329 152.992 1.00 18.20 ? 3728 ARG A NH2   1 
ATOM   16505 N  N     . SER A 1 3729 ? 184.350 242.692 148.494 1.00 21.30 ? 3729 SER A N     1 
ATOM   16506 C  CA    . SER A 1 3729 ? 184.938 241.499 149.096 1.00 17.65 ? 3729 SER A CA    1 
ATOM   16507 C  C     . SER A 1 3729 ? 185.397 240.503 148.036 1.00 20.90 ? 3729 SER A C     1 
ATOM   16508 O  O     . SER A 1 3729 ? 186.478 239.914 148.160 1.00 17.47 ? 3729 SER A O     1 
ATOM   16509 C  CB    . SER A 1 3729 ? 183.936 240.846 150.047 1.00 21.02 ? 3729 SER A CB    1 
ATOM   16510 O  OG    . SER A 1 3729 ? 184.278 239.494 150.295 1.00 29.66 ? 3729 SER A OG    1 
ATOM   16511 N  N     . ASP A 1 3730 ? 184.588 240.292 146.994 1.00 20.23 ? 3730 ASP A N     1 
ATOM   16512 C  CA    . ASP A 1 3730 ? 184.973 239.357 145.942 1.00 17.50 ? 3730 ASP A CA    1 
ATOM   16513 C  C     . ASP A 1 3730 ? 186.224 239.826 145.212 1.00 16.69 ? 3730 ASP A C     1 
ATOM   16514 O  O     . ASP A 1 3730 ? 187.107 239.020 144.901 1.00 17.97 ? 3730 ASP A O     1 
ATOM   16515 C  CB    . ASP A 1 3730 ? 183.822 239.160 144.954 1.00 19.37 ? 3730 ASP A CB    1 
ATOM   16516 C  CG    . ASP A 1 3730 ? 182.509 238.860 145.641 1.00 29.69 ? 3730 ASP A CG    1 
ATOM   16517 O  OD1   . ASP A 1 3730 ? 181.478 239.430 145.229 1.00 32.01 ? 3730 ASP A OD1   1 
ATOM   16518 O  OD2   . ASP A 1 3730 ? 182.508 238.055 146.597 1.00 30.89 ? 3730 ASP A OD2   1 
ATOM   16519 N  N     . LEU A 1 3731 ? 186.314 241.126 144.926 1.00 16.22 ? 3731 LEU A N     1 
ATOM   16520 C  CA    . LEU A 1 3731 ? 187.477 241.646 144.216 1.00 14.72 ? 3731 LEU A CA    1 
ATOM   16521 C  C     . LEU A 1 3731 ? 188.752 241.475 145.031 1.00 14.82 ? 3731 LEU A C     1 
ATOM   16522 O  O     . LEU A 1 3731 ? 189.796 241.097 144.487 1.00 20.55 ? 3731 LEU A O     1 
ATOM   16523 C  CB    . LEU A 1 3731 ? 187.263 243.116 143.866 1.00 14.30 ? 3731 LEU A CB    1 
ATOM   16524 C  CG    . LEU A 1 3731 ? 186.311 243.390 142.703 1.00 17.94 ? 3731 LEU A CG    1 
ATOM   16525 C  CD1   . LEU A 1 3731 ? 186.228 244.875 142.450 1.00 18.88 ? 3731 LEU A CD1   1 
ATOM   16526 C  CD2   . LEU A 1 3731 ? 186.746 242.651 141.448 1.00 18.02 ? 3731 LEU A CD2   1 
ATOM   16527 N  N     . LEU A 1 3732 ? 188.688 241.749 146.335 1.00 10.88 ? 3732 LEU A N     1 
ATOM   16528 C  CA    . LEU A 1 3732 ? 189.868 241.584 147.178 1.00 12.76 ? 3732 LEU A CA    1 
ATOM   16529 C  C     . LEU A 1 3732 ? 190.323 240.133 147.207 1.00 14.89 ? 3732 LEU A C     1 
ATOM   16530 O  O     . LEU A 1 3732 ? 191.527 239.850 147.212 1.00 14.48 ? 3732 LEU A O     1 
ATOM   16531 C  CB    . LEU A 1 3732 ? 189.578 242.092 148.590 1.00 10.24 ? 3732 LEU A CB    1 
ATOM   16532 C  CG    . LEU A 1 3732 ? 189.324 243.595 148.710 1.00 12.57 ? 3732 LEU A CG    1 
ATOM   16533 C  CD1   . LEU A 1 3732 ? 188.910 243.966 150.123 1.00 14.24 ? 3732 LEU A CD1   1 
ATOM   16534 C  CD2   . LEU A 1 3732 ? 190.554 244.380 148.283 1.00 13.58 ? 3732 LEU A CD2   1 
ATOM   16535 N  N     . LYS A 1 3733 ? 189.373 239.197 147.226 1.00 15.03 ? 3733 LYS A N     1 
ATOM   16536 C  CA    . LYS A 1 3733 ? 189.730 237.788 147.110 1.00 15.54 ? 3733 LYS A CA    1 
ATOM   16537 C  C     . LYS A 1 3733 ? 190.301 237.478 145.732 1.00 14.20 ? 3733 LYS A C     1 
ATOM   16538 O  O     . LYS A 1 3733 ? 191.301 236.762 145.618 1.00 14.50 ? 3733 LYS A O     1 
ATOM   16539 C  CB    . LYS A 1 3733 ? 188.511 236.913 147.402 1.00 14.28 ? 3733 LYS A CB    1 
ATOM   16540 C  CG    . LYS A 1 3733 ? 188.791 235.424 147.346 1.00 15.17 ? 3733 LYS A CG    1 
ATOM   16541 C  CD    . LYS A 1 3733 ? 187.581 234.617 147.783 1.00 23.30 ? 3733 LYS A CD    1 
ATOM   16542 C  CE    . LYS A 1 3733 ? 186.479 234.668 146.738 1.00 22.53 ? 3733 LYS A CE    1 
ATOM   16543 N  NZ    . LYS A 1 3733 ? 186.859 233.945 145.494 1.00 21.57 ? 3733 LYS A NZ    1 
ATOM   16544 N  N     . LEU A 1 3734 ? 189.683 238.015 144.678 1.00 11.67 ? 3734 LEU A N     1 
ATOM   16545 C  CA    . LEU A 1 3734 ? 190.187 237.798 143.325 1.00 13.97 ? 3734 LEU A CA    1 
ATOM   16546 C  C     . LEU A 1 3734 ? 191.569 238.414 143.142 1.00 14.10 ? 3734 LEU A C     1 
ATOM   16547 O  O     . LEU A 1 3734 ? 192.473 237.782 142.582 1.00 17.62 ? 3734 LEU A O     1 
ATOM   16548 C  CB    . LEU A 1 3734 ? 189.204 238.368 142.300 1.00 15.89 ? 3734 LEU A CB    1 
ATOM   16549 C  CG    . LEU A 1 3734 ? 188.195 237.419 141.643 1.00 17.52 ? 3734 LEU A CG    1 
ATOM   16550 C  CD1   . LEU A 1 3734 ? 187.316 236.723 142.668 1.00 17.57 ? 3734 LEU A CD1   1 
ATOM   16551 C  CD2   . LEU A 1 3734 ? 187.344 238.179 140.641 1.00 16.76 ? 3734 LEU A CD2   1 
ATOM   16552 N  N     . GLN A 1 3735 ? 191.754 239.651 143.608 1.00 10.73 ? 3735 GLN A N     1 
ATOM   16553 C  CA    . GLN A 1 3735 ? 193.047 240.311 143.449 1.00 14.18 ? 3735 GLN A CA    1 
ATOM   16554 C  C     . GLN A 1 3735 ? 194.124 239.634 144.288 1.00 12.41 ? 3735 GLN A C     1 
ATOM   16555 O  O     . GLN A 1 3735 ? 195.292 239.592 143.888 1.00 14.04 ? 3735 GLN A O     1 
ATOM   16556 C  CB    . GLN A 1 3735 ? 192.935 241.794 143.803 1.00 15.72 ? 3735 GLN A CB    1 
ATOM   16557 C  CG    . GLN A 1 3735 ? 192.067 242.581 142.838 1.00 19.06 ? 3735 GLN A CG    1 
ATOM   16558 C  CD    . GLN A 1 3735 ? 191.948 244.044 143.206 1.00 20.82 ? 3735 GLN A CD    1 
ATOM   16559 O  OE1   . GLN A 1 3735 ? 191.333 244.832 142.488 1.00 25.25 ? 3735 GLN A OE1   1 
ATOM   16560 N  NE2   . GLN A 1 3735 ? 192.542 244.418 144.331 1.00 23.60 ? 3735 GLN A NE2   1 
ATOM   16561 N  N     . GLY A 1 3736 ? 193.754 239.108 145.455 1.00 11.61 ? 3736 GLY A N     1 
ATOM   16562 C  CA    . GLY A 1 3736 ? 194.711 238.354 146.245 1.00 10.65 ? 3736 GLY A CA    1 
ATOM   16563 C  C     . GLY A 1 3736 ? 195.191 237.105 145.534 1.00 17.88 ? 3736 GLY A C     1 
ATOM   16564 O  O     . GLY A 1 3736 ? 196.386 236.799 145.531 1.00 17.66 ? 3736 GLY A O     1 
ATOM   16565 N  N     . GLU A 1 3737 ? 194.267 236.366 144.918 1.00 16.38 ? 3737 GLU A N     1 
ATOM   16566 C  CA    . GLU A 1 3737 ? 194.651 235.193 144.141 1.00 17.00 ? 3737 GLU A CA    1 
ATOM   16567 C  C     . GLU A 1 3737 ? 195.435 235.583 142.896 1.00 15.96 ? 3737 GLU A C     1 
ATOM   16568 O  O     . GLU A 1 3737 ? 196.382 234.890 142.508 1.00 18.21 ? 3737 GLU A O     1 
ATOM   16569 C  CB    . GLU A 1 3737 ? 193.413 234.384 143.759 1.00 17.40 ? 3737 GLU A CB    1 
ATOM   16570 C  CG    . GLU A 1 3737 ? 192.630 233.840 144.935 1.00 16.81 ? 3737 GLU A CG    1 
ATOM   16571 C  CD    . GLU A 1 3737 ? 191.137 233.879 144.694 1.00 24.90 ? 3737 GLU A CD    1 
ATOM   16572 O  OE1   . GLU A 1 3737 ? 190.718 234.457 143.671 1.00 24.07 ? 3737 GLU A OE1   1 
ATOM   16573 O  OE2   . GLU A 1 3737 ? 190.384 233.329 145.525 1.00 26.41 ? 3737 GLU A OE2   1 
ATOM   16574 N  N     . PHE A 1 3738 ? 195.045 236.682 142.247 1.00 15.91 ? 3738 PHE A N     1 
ATOM   16575 C  CA    . PHE A 1 3738 ? 195.711 237.096 141.016 1.00 13.30 ? 3738 PHE A CA    1 
ATOM   16576 C  C     . PHE A 1 3738 ? 197.159 237.491 141.278 1.00 16.56 ? 3738 PHE A C     1 
ATOM   16577 O  O     . PHE A 1 3738 ? 198.060 237.097 140.528 1.00 19.85 ? 3738 PHE A O     1 
ATOM   16578 C  CB    . PHE A 1 3738 ? 194.946 238.253 140.378 1.00 12.98 ? 3738 PHE A CB    1 
ATOM   16579 C  CG    . PHE A 1 3738 ? 193.712 237.828 139.638 1.00 18.03 ? 3738 PHE A CG    1 
ATOM   16580 C  CD1   . PHE A 1 3738 ? 192.758 238.760 139.269 1.00 17.86 ? 3738 PHE A CD1   1 
ATOM   16581 C  CD2   . PHE A 1 3738 ? 193.496 236.497 139.326 1.00 16.68 ? 3738 PHE A CD2   1 
ATOM   16582 C  CE1   . PHE A 1 3738 ? 191.617 238.374 138.598 1.00 18.54 ? 3738 PHE A CE1   1 
ATOM   16583 C  CE2   . PHE A 1 3738 ? 192.357 236.103 138.654 1.00 19.09 ? 3738 PHE A CE2   1 
ATOM   16584 C  CZ    . PHE A 1 3738 ? 191.417 237.044 138.289 1.00 17.27 ? 3738 PHE A CZ    1 
ATOM   16585 N  N     . GLN A 1 3739 ? 197.402 238.265 142.338 1.00 14.54 ? 3739 GLN A N     1 
ATOM   16586 C  CA    . GLN A 1 3739 ? 198.770 238.632 142.688 1.00 16.26 ? 3739 GLN A CA    1 
ATOM   16587 C  C     . GLN A 1 3739 ? 199.567 237.416 143.140 1.00 15.92 ? 3739 GLN A C     1 
ATOM   16588 O  O     . GLN A 1 3739 ? 200.779 237.340 142.912 1.00 14.87 ? 3739 GLN A O     1 
ATOM   16589 C  CB    . GLN A 1 3739 ? 198.769 239.710 143.773 1.00 13.40 ? 3739 GLN A CB    1 
ATOM   16590 C  CG    . GLN A 1 3739 ? 198.163 241.028 143.334 1.00 12.84 ? 3739 GLN A CG    1 
ATOM   16591 C  CD    . GLN A 1 3739 ? 199.005 241.731 142.289 1.00 19.44 ? 3739 GLN A CD    1 
ATOM   16592 O  OE1   . GLN A 1 3739 ? 200.205 241.483 142.171 1.00 21.57 ? 3739 GLN A OE1   1 
ATOM   16593 N  NE2   . GLN A 1 3739 ? 198.377 242.608 141.516 1.00 22.34 ? 3739 GLN A NE2   1 
ATOM   16594 N  N     . LEU A 1 3740 ? 198.903 236.461 143.795 1.00 15.47 ? 3740 LEU A N     1 
ATOM   16595 C  CA    . LEU A 1 3740 ? 199.564 235.212 144.157 1.00 12.36 ? 3740 LEU A CA    1 
ATOM   16596 C  C     . LEU A 1 3740 ? 200.026 234.459 142.917 1.00 17.01 ? 3740 LEU A C     1 
ATOM   16597 O  O     . LEU A 1 3740 ? 201.166 233.989 142.851 1.00 22.04 ? 3740 LEU A O     1 
ATOM   16598 C  CB    . LEU A 1 3740 ? 198.617 234.343 144.984 1.00 12.82 ? 3740 LEU A CB    1 
ATOM   16599 C  CG    . LEU A 1 3740 ? 199.078 232.917 145.297 1.00 14.88 ? 3740 LEU A CG    1 
ATOM   16600 C  CD1   . LEU A 1 3740 ? 200.205 232.894 146.318 1.00 16.79 ? 3740 LEU A CD1   1 
ATOM   16601 C  CD2   . LEU A 1 3740 ? 197.908 232.060 145.750 1.00 11.31 ? 3740 LEU A CD2   1 
ATOM   16602 N  N     . ARG A 1 3741 ? 199.154 234.357 141.913 1.00 14.92 ? 3741 ARG A N     1 
ATOM   16603 C  CA    . ARG A 1 3741 ? 199.480 233.599 140.710 1.00 14.41 ? 3741 ARG A CA    1 
ATOM   16604 C  C     . ARG A 1 3741 ? 200.642 234.225 139.951 1.00 15.85 ? 3741 ARG A C     1 
ATOM   16605 O  O     . ARG A 1 3741 ? 201.510 233.513 139.433 1.00 23.16 ? 3741 ARG A O     1 
ATOM   16606 C  CB    . ARG A 1 3741 ? 198.245 233.490 139.817 1.00 15.89 ? 3741 ARG A CB    1 
ATOM   16607 C  CG    . ARG A 1 3741 ? 198.355 232.451 138.720 1.00 18.49 ? 3741 ARG A CG    1 
ATOM   16608 C  CD    . ARG A 1 3741 ? 198.646 231.070 139.279 1.00 19.24 ? 3741 ARG A CD    1 
ATOM   16609 N  NE    . ARG A 1 3741 ? 198.978 230.129 138.216 1.00 24.46 ? 3741 ARG A NE    1 
ATOM   16610 C  CZ    . ARG A 1 3741 ? 200.160 229.545 138.072 1.00 26.23 ? 3741 ARG A CZ    1 
ATOM   16611 N  NH1   . ARG A 1 3741 ? 201.154 229.780 138.912 1.00 27.26 ? 3741 ARG A NH1   1 
ATOM   16612 N  NH2   . ARG A 1 3741 ? 200.350 228.709 137.057 1.00 23.03 ? 3741 ARG A NH2   1 
ATOM   16613 N  N     . LEU A 1 3742 ? 200.673 235.556 139.869 1.00 14.02 ? 3742 LEU A N     1 
ATOM   16614 C  CA    . LEU A 1 3742 ? 201.762 236.231 139.169 1.00 13.85 ? 3742 LEU A CA    1 
ATOM   16615 C  C     . LEU A 1 3742 ? 203.101 235.961 139.844 1.00 16.70 ? 3742 LEU A C     1 
ATOM   16616 O  O     . LEU A 1 3742 ? 204.127 235.816 139.168 1.00 19.57 ? 3742 LEU A O     1 
ATOM   16617 C  CB    . LEU A 1 3742 ? 201.485 237.730 139.095 1.00 11.59 ? 3742 LEU A CB    1 
ATOM   16618 C  CG    . LEU A 1 3742 ? 200.454 238.184 138.057 1.00 17.75 ? 3742 LEU A CG    1 
ATOM   16619 C  CD1   . LEU A 1 3742 ? 200.580 239.675 137.800 1.00 18.94 ? 3742 LEU A CD1   1 
ATOM   16620 C  CD2   . LEU A 1 3742 ? 200.610 237.401 136.760 1.00 15.40 ? 3742 LEU A CD2   1 
ATOM   16621 N  N     . ARG A 1 3743 ? 203.115 235.906 141.178 1.00 18.35 ? 3743 ARG A N     1 
ATOM   16622 C  CA    . ARG A 1 3743 ? 204.354 235.605 141.888 1.00 16.12 ? 3743 ARG A CA    1 
ATOM   16623 C  C     . ARG A 1 3743 ? 204.841 234.194 141.582 1.00 18.02 ? 3743 ARG A C     1 
ATOM   16624 O  O     . ARG A 1 3743 ? 206.044 233.978 141.390 1.00 20.35 ? 3743 ARG A O     1 
ATOM   16625 C  CB    . ARG A 1 3743 ? 204.160 235.806 143.388 1.00 14.80 ? 3743 ARG A CB    1 
ATOM   16626 C  CG    . ARG A 1 3743 ? 204.360 237.241 143.833 1.00 11.90 ? 3743 ARG A CG    1 
ATOM   16627 C  CD    . ARG A 1 3743 ? 204.149 237.400 145.328 1.00 15.23 ? 3743 ARG A CD    1 
ATOM   16628 N  NE    . ARG A 1 3743 ? 202.793 237.831 145.644 1.00 15.09 ? 3743 ARG A NE    1 
ATOM   16629 C  CZ    . ARG A 1 3743 ? 201.889 237.074 146.249 1.00 16.81 ? 3743 ARG A CZ    1 
ATOM   16630 N  NH1   . ARG A 1 3743 ? 202.165 235.839 146.628 1.00 12.67 ? 3743 ARG A NH1   1 
ATOM   16631 N  NH2   . ARG A 1 3743 ? 200.677 237.570 146.478 1.00 17.20 ? 3743 ARG A NH2   1 
ATOM   16632 N  N     . GLN A 1 3744 ? 203.930 233.219 141.531 1.00 15.05 ? 3744 GLN A N     1 
ATOM   16633 C  CA    . GLN A 1 3744 ? 204.325 231.878 141.113 1.00 17.31 ? 3744 GLN A CA    1 
ATOM   16634 C  C     . GLN A 1 3744 ? 204.783 231.868 139.661 1.00 17.78 ? 3744 GLN A C     1 
ATOM   16635 O  O     . GLN A 1 3744 ? 205.725 231.147 139.307 1.00 23.47 ? 3744 GLN A O     1 
ATOM   16636 C  CB    . GLN A 1 3744 ? 203.174 230.891 141.314 1.00 17.99 ? 3744 GLN A CB    1 
ATOM   16637 C  CG    . GLN A 1 3744 ? 202.288 231.187 142.500 1.00 15.25 ? 3744 GLN A CG    1 
ATOM   16638 C  CD    . GLN A 1 3744 ? 201.450 229.996 142.917 1.00 21.55 ? 3744 GLN A CD    1 
ATOM   16639 O  OE1   . GLN A 1 3744 ? 200.727 229.418 142.107 1.00 21.55 ? 3744 GLN A OE1   1 
ATOM   16640 N  NE2   . GLN A 1 3744 ? 201.540 229.622 144.188 1.00 24.53 ? 3744 GLN A NE2   1 
ATOM   16641 N  N     . LEU A 1 3745 ? 204.125 232.651 138.805 1.00 16.39 ? 3745 LEU A N     1 
ATOM   16642 C  CA    . LEU A 1 3745 ? 204.483 232.670 137.390 1.00 20.25 ? 3745 LEU A CA    1 
ATOM   16643 C  C     . LEU A 1 3745 ? 205.890 233.208 137.172 1.00 18.75 ? 3745 LEU A C     1 
ATOM   16644 O  O     . LEU A 1 3745 ? 206.650 232.661 136.366 1.00 25.03 ? 3745 LEU A O     1 
ATOM   16645 C  CB    . LEU A 1 3745 ? 203.460 233.489 136.603 1.00 22.08 ? 3745 LEU A CB    1 
ATOM   16646 C  CG    . LEU A 1 3745 ? 202.153 232.744 136.332 1.00 19.61 ? 3745 LEU A CG    1 
ATOM   16647 C  CD1   . LEU A 1 3745 ? 201.049 233.700 135.929 1.00 19.86 ? 3745 LEU A CD1   1 
ATOM   16648 C  CD2   . LEU A 1 3745 ? 202.365 231.686 135.266 1.00 20.62 ? 3745 LEU A CD2   1 
ATOM   16649 N  N     . GLU A 1 3746 ? 206.258 234.280 137.878 1.00 19.99 ? 3746 GLU A N     1 
ATOM   16650 C  CA    . GLU A 1 3746 ? 207.611 234.808 137.731 1.00 21.27 ? 3746 GLU A CA    1 
ATOM   16651 C  C     . GLU A 1 3746 ? 208.636 233.903 138.401 1.00 24.63 ? 3746 GLU A C     1 
ATOM   16652 O  O     . GLU A 1 3746 ? 209.780 233.816 137.940 1.00 28.98 ? 3746 GLU A O     1 
ATOM   16653 C  CB    . GLU A 1 3746 ? 207.698 236.227 138.292 1.00 17.59 ? 3746 GLU A CB    1 
ATOM   16654 C  CG    . GLU A 1 3746 ? 207.497 236.331 139.791 1.00 24.21 ? 3746 GLU A CG    1 
ATOM   16655 C  CD    . GLU A 1 3746 ? 207.604 237.754 140.297 1.00 33.23 ? 3746 GLU A CD    1 
ATOM   16656 O  OE1   . GLU A 1 3746 ? 207.822 238.668 139.473 1.00 30.71 ? 3746 GLU A OE1   1 
ATOM   16657 O  OE2   . GLU A 1 3746 ? 207.469 237.959 141.523 1.00 33.03 ? 3746 GLU A OE2   1 
ATOM   16658 N  N     . LYS A 1 3747 ? 208.250 233.226 139.485 1.00 20.21 ? 3747 LYS A N     1 
ATOM   16659 C  CA    . LYS A 1 3747 ? 209.151 232.274 140.124 1.00 20.81 ? 3747 LYS A CA    1 
ATOM   16660 C  C     . LYS A 1 3747 ? 209.364 231.047 139.244 1.00 25.63 ? 3747 LYS A C     1 
ATOM   16661 O  O     . LYS A 1 3747 ? 210.503 230.620 139.024 1.00 32.25 ? 3747 LYS A O     1 
ATOM   16662 C  CB    . LYS A 1 3747 ? 208.601 231.869 141.492 1.00 18.67 ? 3747 LYS A CB    1 
ATOM   16663 C  CG    . LYS A 1 3747 ? 209.270 230.649 142.093 1.00 21.44 ? 3747 LYS A CG    1 
ATOM   16664 C  CD    . LYS A 1 3747 ? 208.761 230.370 143.498 1.00 22.02 ? 3747 LYS A CD    1 
ATOM   16665 C  CE    . LYS A 1 3747 ? 209.071 231.521 144.438 1.00 24.64 ? 3747 LYS A CE    1 
ATOM   16666 N  NZ    . LYS A 1 3747 ? 208.651 231.222 145.835 1.00 24.55 ? 3747 LYS A NZ    1 
ATOM   16667 N  N     . SER A 1 3748 ? 208.275 230.469 138.728 1.00 24.46 ? 3748 SER A N     1 
ATOM   16668 C  CA    . SER A 1 3748 ? 208.392 229.280 137.889 1.00 23.73 ? 3748 SER A CA    1 
ATOM   16669 C  C     . SER A 1 3748 ? 209.165 229.576 136.612 1.00 21.25 ? 3748 SER A C     1 
ATOM   16670 O  O     . SER A 1 3748 ? 209.998 228.772 136.180 1.00 24.11 ? 3748 SER A O     1 
ATOM   16671 C  CB    . SER A 1 3748 ? 207.004 228.732 137.556 1.00 26.74 ? 3748 SER A CB    1 
ATOM   16672 O  OG    . SER A 1 3748 ? 206.277 228.421 138.731 1.00 30.40 ? 3748 SER A OG    1 
ATOM   16673 N  N     . LEU A 1 3749 ? 208.902 230.728 135.991 1.00 18.31 ? 3749 LEU A N     1 
ATOM   16674 C  CA    . LEU A 1 3749 ? 209.598 231.078 134.757 1.00 19.89 ? 3749 LEU A CA    1 
ATOM   16675 C  C     . LEU A 1 3749 ? 211.087 231.269 135.015 1.00 18.43 ? 3749 LEU A C     1 
ATOM   16676 O  O     . LEU A 1 3749 ? 211.924 230.888 134.188 1.00 23.20 ? 3749 LEU A O     1 
ATOM   16677 C  CB    . LEU A 1 3749 ? 208.968 232.329 134.144 1.00 22.59 ? 3749 LEU A CB    1 
ATOM   16678 C  CG    . LEU A 1 3749 ? 209.385 232.818 132.751 1.00 22.99 ? 3749 LEU A CG    1 
ATOM   16679 C  CD1   . LEU A 1 3749 ? 208.235 233.589 132.133 1.00 24.36 ? 3749 LEU A CD1   1 
ATOM   16680 C  CD2   . LEU A 1 3749 ? 210.625 233.687 132.792 1.00 23.72 ? 3749 LEU A CD2   1 
ATOM   16681 N  N     . LEU A 1 3750 ? 211.437 231.861 136.159 1.00 23.04 ? 3750 LEU A N     1 
ATOM   16682 C  CA    . LEU A 1 3750 ? 212.839 231.960 136.544 1.00 22.83 ? 3750 LEU A CA    1 
ATOM   16683 C  C     . LEU A 1 3750 ? 213.445 230.583 136.787 1.00 23.60 ? 3750 LEU A C     1 
ATOM   16684 O  O     . LEU A 1 3750 ? 214.584 230.319 136.383 1.00 25.27 ? 3750 LEU A O     1 
ATOM   16685 C  CB    . LEU A 1 3750 ? 212.980 232.837 137.788 1.00 19.64 ? 3750 LEU A CB    1 
ATOM   16686 C  CG    . LEU A 1 3750 ? 214.307 233.578 137.961 1.00 20.99 ? 3750 LEU A CG    1 
ATOM   16687 C  CD1   . LEU A 1 3750 ? 214.676 234.319 136.692 1.00 23.21 ? 3750 LEU A CD1   1 
ATOM   16688 C  CD2   . LEU A 1 3750 ? 214.239 234.531 139.143 1.00 17.16 ? 3750 LEU A CD2   1 
ATOM   16689 N  N     . GLN A 1 3751 ? 212.698 229.689 137.441 1.00 19.88 ? 3751 GLN A N     1 
ATOM   16690 C  CA    . GLN A 1 3751 ? 213.209 228.347 137.705 1.00 22.08 ? 3751 GLN A CA    1 
ATOM   16691 C  C     . GLN A 1 3751 ? 213.476 227.590 136.409 1.00 27.12 ? 3751 GLN A C     1 
ATOM   16692 O  O     . GLN A 1 3751 ? 214.445 226.828 136.317 1.00 30.51 ? 3751 GLN A O     1 
ATOM   16693 C  CB    . GLN A 1 3751 ? 212.226 227.563 138.577 1.00 18.01 ? 3751 GLN A CB    1 
ATOM   16694 C  CG    . GLN A 1 3751 ? 212.094 228.059 140.006 1.00 26.78 ? 3751 GLN A CG    1 
ATOM   16695 C  CD    . GLN A 1 3751 ? 213.401 228.565 140.581 1.00 33.41 ? 3751 GLN A CD    1 
ATOM   16696 O  OE1   . GLN A 1 3751 ? 214.367 227.813 140.715 1.00 33.36 ? 3751 GLN A OE1   1 
ATOM   16697 N  NE2   . GLN A 1 3751 ? 213.437 229.847 140.929 1.00 30.84 ? 3751 GLN A NE2   1 
ATOM   16698 N  N     . ALA A 1 3752 ? 212.619 227.779 135.403 1.00 22.15 ? 3752 ALA A N     1 
ATOM   16699 C  CA    . ALA A 1 3752 ? 212.785 227.061 134.143 1.00 22.56 ? 3752 ALA A CA    1 
ATOM   16700 C  C     . ALA A 1 3752 ? 214.099 227.424 133.466 1.00 22.13 ? 3752 ALA A C     1 
ATOM   16701 O  O     . ALA A 1 3752 ? 214.782 226.553 132.916 1.00 28.62 ? 3752 ALA A O     1 
ATOM   16702 C  CB    . ALA A 1 3752 ? 211.604 227.351 133.216 1.00 23.42 ? 3752 ALA A CB    1 
ATOM   16703 N  N     . LEU A 1 3753 ? 214.468 228.705 133.491 1.00 20.34 ? 3753 LEU A N     1 
ATOM   16704 C  CA    . LEU A 1 3753 ? 215.744 229.121 132.927 1.00 20.98 ? 3753 LEU A CA    1 
ATOM   16705 C  C     . LEU A 1 3753 ? 216.918 228.760 133.823 1.00 25.48 ? 3753 LEU A C     1 
ATOM   16706 O  O     . LEU A 1 3753 ? 218.054 228.701 133.340 1.00 30.08 ? 3753 LEU A O     1 
ATOM   16707 C  CB    . LEU A 1 3753 ? 215.742 230.627 132.666 1.00 21.66 ? 3753 LEU A CB    1 
ATOM   16708 C  CG    . LEU A 1 3753 ? 215.160 231.109 131.337 1.00 19.11 ? 3753 LEU A CG    1 
ATOM   16709 C  CD1   . LEU A 1 3753 ? 213.646 231.010 131.337 1.00 18.44 ? 3753 LEU A CD1   1 
ATOM   16710 C  CD2   . LEU A 1 3753 ? 215.607 232.534 131.058 1.00 24.37 ? 3753 LEU A CD2   1 
ATOM   16711 N  N     . ASN A 1 3754 ? 216.677 228.528 135.112 1.00 28.93 ? 3754 ASN A N     1 
ATOM   16712 C  CA    . ASN A 1 3754 ? 217.742 228.211 136.053 1.00 21.85 ? 3754 ASN A CA    1 
ATOM   16713 C  C     . ASN A 1 3754 ? 217.968 226.715 136.216 1.00 26.13 ? 3754 ASN A C     1 
ATOM   16714 O  O     . ASN A 1 3754 ? 218.931 226.322 136.885 1.00 34.48 ? 3754 ASN A O     1 
ATOM   16715 C  CB    . ASN A 1 3754 ? 217.434 228.830 137.418 1.00 24.70 ? 3754 ASN A CB    1 
ATOM   16716 C  CG    . ASN A 1 3754 ? 217.461 230.345 137.390 1.00 25.67 ? 3754 ASN A CG    1 
ATOM   16717 O  OD1   . ASN A 1 3754 ? 218.428 230.953 136.938 1.00 24.10 ? 3754 ASN A OD1   1 
ATOM   16718 N  ND2   . ASN A 1 3754 ? 216.385 230.961 137.863 1.00 32.06 ? 3754 ASN A ND2   1 
ATOM   16719 N  N     . GLU A 1 3755 ? 217.118 225.877 135.628 1.00 28.47 ? 3755 GLU A N     1 
ATOM   16720 C  CA    . GLU A 1 3755 ? 217.241 224.432 135.746 1.00 27.24 ? 3755 GLU A CA    1 
ATOM   16721 C  C     . GLU A 1 3755 ? 217.462 223.735 134.412 1.00 27.26 ? 3755 GLU A C     1 
ATOM   16722 O  O     . GLU A 1 3755 ? 217.594 222.507 134.385 1.00 30.13 ? 3755 GLU A O     1 
ATOM   16723 C  CB    . GLU A 1 3755 ? 215.996 223.851 136.428 1.00 24.43 ? 3755 GLU A CB    1 
ATOM   16724 C  CG    . GLU A 1 3755 ? 215.840 224.260 137.883 1.00 26.79 ? 3755 GLU A CG    1 
ATOM   16725 C  CD    . GLU A 1 3755 ? 216.923 223.680 138.772 1.00 33.76 ? 3755 GLU A CD    1 
ATOM   16726 O  OE1   . GLU A 1 3755 ? 217.386 222.555 138.489 1.00 35.42 ? 3755 GLU A OE1   1 
ATOM   16727 O  OE2   . GLU A 1 3755 ? 217.310 224.349 139.752 1.00 37.40 ? 3755 GLU A OE2   1 
ATOM   16728 N  N     . VAL A 1 3756 ? 217.508 224.474 133.313 1.00 25.45 ? 3756 VAL A N     1 
ATOM   16729 C  CA    . VAL A 1 3756 ? 217.663 223.886 131.988 1.00 26.91 ? 3756 VAL A CA    1 
ATOM   16730 C  C     . VAL A 1 3756 ? 219.145 223.811 131.641 1.00 29.49 ? 3756 VAL A C     1 
ATOM   16731 O  O     . VAL A 1 3756 ? 219.908 224.753 131.882 1.00 33.96 ? 3756 VAL A O     1 
ATOM   16732 C  CB    . VAL A 1 3756 ? 216.873 224.689 130.936 1.00 29.60 ? 3756 VAL A CB    1 
ATOM   16733 C  CG1   . VAL A 1 3756 ? 217.307 226.151 130.929 1.00 26.37 ? 3756 VAL A CG1   1 
ATOM   16734 C  CG2   . VAL A 1 3756 ? 217.030 224.066 129.557 1.00 24.41 ? 3756 VAL A CG2   1 
ATOM   16735 N  N     . LYS A 1 3757 ? 219.557 222.675 131.087 1.00 29.85 ? 3757 LYS A N     1 
ATOM   16736 C  CA    . LYS A 1 3757 ? 220.940 222.449 130.700 1.00 31.11 ? 3757 LYS A CA    1 
ATOM   16737 C  C     . LYS A 1 3757 ? 221.122 222.690 129.207 1.00 31.80 ? 3757 LYS A C     1 
ATOM   16738 O  O     . LYS A 1 3757 ? 220.175 222.620 128.420 1.00 30.61 ? 3757 LYS A O     1 
ATOM   16739 C  CB    . LYS A 1 3757 ? 221.378 221.027 131.061 1.00 24.55 ? 3757 LYS A CB    1 
ATOM   16740 C  CG    . LYS A 1 3757 ? 220.975 220.590 132.462 1.00 29.79 ? 3757 LYS A CG    1 
ATOM   16741 C  CD    . LYS A 1 3757 ? 221.548 221.515 133.525 1.00 29.90 ? 3757 LYS A CD    1 
ATOM   16742 C  CE    . LYS A 1 3757 ? 223.065 221.452 133.558 1.00 32.63 ? 3757 LYS A CE    1 
ATOM   16743 N  NZ    . LYS A 1 3757 ? 223.637 222.418 134.537 1.00 31.61 ? 3757 LYS A NZ    1 
ATOM   16744 N  N     . GLY A 1 3758 ? 222.360 222.975 128.826 1.00 33.34 ? 3758 GLY A N     1 
ATOM   16745 C  CA    . GLY A 1 3758 ? 222.653 223.252 127.429 1.00 28.49 ? 3758 GLY A CA    1 
ATOM   16746 C  C     . GLY A 1 3758 ? 221.956 224.518 126.973 1.00 34.08 ? 3758 GLY A C     1 
ATOM   16747 O  O     . GLY A 1 3758 ? 222.102 225.589 127.576 1.00 35.54 ? 3758 GLY A O     1 
ATOM   16748 N  N     . ARG A 1 3759 ? 221.180 224.408 125.898 1.00 32.20 ? 3759 ARG A N     1 
ATOM   16749 C  CA    . ARG A 1 3759 ? 220.469 225.536 125.321 1.00 30.24 ? 3759 ARG A CA    1 
ATOM   16750 C  C     . ARG A 1 3759 ? 218.964 225.325 125.439 1.00 30.90 ? 3759 ARG A C     1 
ATOM   16751 O  O     . ARG A 1 3759 ? 218.479 224.191 125.485 1.00 31.84 ? 3759 ARG A O     1 
ATOM   16752 C  CB    . ARG A 1 3759 ? 220.854 225.743 123.850 1.00 32.34 ? 3759 ARG A CB    1 
ATOM   16753 C  CG    . ARG A 1 3759 ? 222.354 225.727 123.598 1.00 31.12 ? 3759 ARG A CG    1 
ATOM   16754 C  CD    . ARG A 1 3759 ? 222.669 225.566 122.120 1.00 30.13 ? 3759 ARG A CD    1 
ATOM   16755 N  NE    . ARG A 1 3759 ? 222.527 224.180 121.684 1.00 32.77 ? 3759 ARG A NE    1 
ATOM   16756 C  CZ    . ARG A 1 3759 ? 222.706 223.765 120.438 1.00 34.47 ? 3759 ARG A CZ    1 
ATOM   16757 N  NH1   . ARG A 1 3759 ? 223.039 224.604 119.471 1.00 32.33 ? 3759 ARG A NH1   1 
ATOM   16758 N  NH2   . ARG A 1 3759 ? 222.548 222.476 120.155 1.00 29.68 ? 3759 ARG A NH2   1 
ATOM   16759 N  N     . ILE A 1 3760 ? 218.233 226.440 125.502 1.00 29.52 ? 3760 ILE A N     1 
ATOM   16760 C  CA    . ILE A 1 3760 ? 216.778 226.380 125.597 1.00 30.56 ? 3760 ILE A CA    1 
ATOM   16761 C  C     . ILE A 1 3760 ? 216.180 225.769 124.334 1.00 33.58 ? 3760 ILE A C     1 
ATOM   16762 O  O     . ILE A 1 3760 ? 215.264 224.940 124.403 1.00 35.88 ? 3760 ILE A O     1 
ATOM   16763 C  CB    . ILE A 1 3760 ? 216.209 227.782 125.876 1.00 28.28 ? 3760 ILE A CB    1 
ATOM   16764 C  CG1   . ILE A 1 3760 ? 216.681 228.288 127.240 1.00 26.03 ? 3760 ILE A CG1   1 
ATOM   16765 C  CG2   . ILE A 1 3760 ? 214.690 227.776 125.800 1.00 30.06 ? 3760 ILE A CG2   1 
ATOM   16766 C  CD1   . ILE A 1 3760 ? 216.194 229.677 127.576 1.00 25.11 ? 3760 ILE A CD1   1 
ATOM   16767 N  N     . LEU A 1 3761 ? 216.693 226.160 123.163 1.00 28.24 ? 3761 LEU A N     1 
ATOM   16768 C  CA    . LEU A 1 3761 ? 216.120 225.702 121.902 1.00 29.91 ? 3761 LEU A CA    1 
ATOM   16769 C  C     . LEU A 1 3761 ? 216.262 224.196 121.721 1.00 34.98 ? 3761 LEU A C     1 
ATOM   16770 O  O     . LEU A 1 3761 ? 215.479 223.586 120.983 1.00 37.33 ? 3761 LEU A O     1 
ATOM   16771 C  CB    . LEU A 1 3761 ? 216.778 226.429 120.729 1.00 26.37 ? 3761 LEU A CB    1 
ATOM   16772 C  CG    . LEU A 1 3761 ? 216.366 227.876 120.469 1.00 25.49 ? 3761 LEU A CG    1 
ATOM   16773 C  CD1   . LEU A 1 3761 ? 217.226 228.824 121.282 1.00 30.96 ? 3761 LEU A CD1   1 
ATOM   16774 C  CD2   . LEU A 1 3761 ? 216.460 228.199 118.987 1.00 27.54 ? 3761 LEU A CD2   1 
ATOM   16775 N  N     . ASP A 1 3762 ? 217.253 223.581 122.372 1.00 34.56 ? 3762 ASP A N     1 
ATOM   16776 C  CA    . ASP A 1 3762 ? 217.472 222.148 122.197 1.00 33.42 ? 3762 ASP A CA    1 
ATOM   16777 C  C     . ASP A 1 3762 ? 216.280 221.336 122.691 1.00 36.28 ? 3762 ASP A C     1 
ATOM   16778 O  O     . ASP A 1 3762 ? 215.881 220.356 122.053 1.00 39.33 ? 3762 ASP A O     1 
ATOM   16779 C  CB    . ASP A 1 3762 ? 218.749 221.720 122.919 1.00 33.23 ? 3762 ASP A CB    1 
ATOM   16780 C  CG    . ASP A 1 3762 ? 220.001 222.225 122.233 1.00 36.01 ? 3762 ASP A CG    1 
ATOM   16781 O  OD1   . ASP A 1 3762 ? 220.057 222.177 120.987 1.00 33.54 ? 3762 ASP A OD1   1 
ATOM   16782 O  OD2   . ASP A 1 3762 ? 220.933 222.666 122.940 1.00 35.30 ? 3762 ASP A OD2   1 
ATOM   16783 N  N     . ASP A 1 3763 ? 215.702 221.725 123.823 1.00 34.67 ? 3763 ASP A N     1 
ATOM   16784 C  CA    . ASP A 1 3763 ? 214.565 221.024 124.408 1.00 35.48 ? 3763 ASP A CA    1 
ATOM   16785 C  C     . ASP A 1 3763 ? 213.300 221.829 124.132 1.00 35.34 ? 3763 ASP A C     1 
ATOM   16786 O  O     . ASP A 1 3763 ? 213.103 222.905 124.706 1.00 34.87 ? 3763 ASP A O     1 
ATOM   16787 C  CB    . ASP A 1 3763 ? 214.768 220.814 125.907 1.00 33.33 ? 3763 ASP A CB    1 
ATOM   16788 C  CG    . ASP A 1 3763 ? 213.625 220.050 126.547 1.00 39.54 ? 3763 ASP A CG    1 
ATOM   16789 O  OD1   . ASP A 1 3763 ? 213.327 218.926 126.089 1.00 38.21 ? 3763 ASP A OD1   1 
ATOM   16790 O  OD2   . ASP A 1 3763 ? 213.025 220.572 127.511 1.00 38.17 ? 3763 ASP A OD2   1 
ATOM   16791 N  N     . ASP A 1 3764 ? 212.443 221.303 123.253 1.00 37.64 ? 3764 ASP A N     1 
ATOM   16792 C  CA    . ASP A 1 3764 ? 211.197 221.984 122.924 1.00 33.53 ? 3764 ASP A CA    1 
ATOM   16793 C  C     . ASP A 1 3764 ? 210.237 222.041 124.104 1.00 33.26 ? 3764 ASP A C     1 
ATOM   16794 O  O     . ASP A 1 3764 ? 209.349 222.900 124.122 1.00 35.71 ? 3764 ASP A O     1 
ATOM   16795 C  CB    . ASP A 1 3764 ? 210.519 221.298 121.737 1.00 34.27 ? 3764 ASP A CB    1 
ATOM   16796 C  CG    . ASP A 1 3764 ? 211.279 221.492 120.440 1.00 39.45 ? 3764 ASP A CG    1 
ATOM   16797 O  OD1   . ASP A 1 3764 ? 212.364 222.110 120.471 1.00 39.24 ? 3764 ASP A OD1   1 
ATOM   16798 O  OD2   . ASP A 1 3764 ? 210.792 221.026 119.388 1.00 38.74 ? 3764 ASP A OD2   1 
ATOM   16799 N  N     . THR A 1 3765 ? 210.393 221.147 125.084 1.00 28.75 ? 3765 THR A N     1 
ATOM   16800 C  CA    . THR A 1 3765 ? 209.539 221.186 126.266 1.00 30.21 ? 3765 THR A CA    1 
ATOM   16801 C  C     . THR A 1 3765 ? 209.734 222.482 127.043 1.00 30.07 ? 3765 THR A C     1 
ATOM   16802 O  O     . THR A 1 3765 ? 208.759 223.105 127.478 1.00 32.63 ? 3765 THR A O     1 
ATOM   16803 C  CB    . THR A 1 3765 ? 209.820 219.977 127.158 1.00 29.54 ? 3765 THR A CB    1 
ATOM   16804 O  OG1   . THR A 1 3765 ? 209.612 218.772 126.412 1.00 32.13 ? 3765 THR A OG1   1 
ATOM   16805 C  CG2   . THR A 1 3765 ? 208.902 219.981 128.369 1.00 24.81 ? 3765 THR A CG2   1 
ATOM   16806 N  N     . ILE A 1 3766 ? 210.986 222.911 127.214 1.00 27.96 ? 3766 ILE A N     1 
ATOM   16807 C  CA    . ILE A 1 3766 ? 211.262 224.163 127.915 1.00 28.52 ? 3766 ILE A CA    1 
ATOM   16808 C  C     . ILE A 1 3766 ? 210.626 225.336 127.182 1.00 30.34 ? 3766 ILE A C     1 
ATOM   16809 O  O     . ILE A 1 3766 ? 210.068 226.248 127.805 1.00 30.20 ? 3766 ILE A O     1 
ATOM   16810 C  CB    . ILE A 1 3766 ? 212.781 224.355 128.089 1.00 29.48 ? 3766 ILE A CB    1 
ATOM   16811 C  CG1   . ILE A 1 3766 ? 213.322 223.384 129.138 1.00 25.21 ? 3766 ILE A CG1   1 
ATOM   16812 C  CG2   . ILE A 1 3766 ? 213.106 225.788 128.483 1.00 26.89 ? 3766 ILE A CG2   1 
ATOM   16813 C  CD1   . ILE A 1 3766 ? 212.744 223.601 130.518 1.00 28.47 ? 3766 ILE A CD1   1 
ATOM   16814 N  N     . ILE A 1 3767 ? 210.693 225.330 125.847 1.00 28.63 ? 3767 ILE A N     1 
ATOM   16815 C  CA    . ILE A 1 3767 ? 210.092 226.406 125.065 1.00 27.92 ? 3767 ILE A CA    1 
ATOM   16816 C  C     . ILE A 1 3767 ? 208.585 226.445 125.279 1.00 29.17 ? 3767 ILE A C     1 
ATOM   16817 O  O     . ILE A 1 3767 ? 207.997 227.517 125.466 1.00 32.39 ? 3767 ILE A O     1 
ATOM   16818 C  CB    . ILE A 1 3767 ? 210.450 226.251 123.577 1.00 29.39 ? 3767 ILE A CB    1 
ATOM   16819 C  CG1   . ILE A 1 3767 ? 211.968 226.260 123.390 1.00 30.82 ? 3767 ILE A CG1   1 
ATOM   16820 C  CG2   . ILE A 1 3767 ? 209.794 227.347 122.751 1.00 24.98 ? 3767 ILE A CG2   1 
ATOM   16821 C  CD1   . ILE A 1 3767 ? 212.407 226.187 121.943 1.00 31.42 ? 3767 ILE A CD1   1 
ATOM   16822 N  N     . THR A 1 3768 ? 207.935 225.279 125.258 1.00 28.79 ? 3768 THR A N     1 
ATOM   16823 C  CA    . THR A 1 3768 ? 206.493 225.232 125.477 1.00 26.73 ? 3768 THR A CA    1 
ATOM   16824 C  C     . THR A 1 3768 ? 206.127 225.718 126.873 1.00 27.58 ? 3768 THR A C     1 
ATOM   16825 O  O     . THR A 1 3768 ? 205.143 226.448 127.046 1.00 31.65 ? 3768 THR A O     1 
ATOM   16826 C  CB    . THR A 1 3768 ? 205.974 223.814 125.253 1.00 26.93 ? 3768 THR A CB    1 
ATOM   16827 O  OG1   . THR A 1 3768 ? 206.708 222.902 126.078 1.00 32.06 ? 3768 THR A OG1   1 
ATOM   16828 C  CG2   . THR A 1 3768 ? 206.130 223.415 123.794 1.00 25.45 ? 3768 THR A CG2   1 
ATOM   16829 N  N     . THR A 1 3769 ? 206.905 225.325 127.884 1.00 28.08 ? 3769 THR A N     1 
ATOM   16830 C  CA    . THR A 1 3769 ? 206.608 225.744 129.251 1.00 29.74 ? 3769 THR A CA    1 
ATOM   16831 C  C     . THR A 1 3769 ? 206.724 227.253 129.409 1.00 24.98 ? 3769 THR A C     1 
ATOM   16832 O  O     . THR A 1 3769 ? 205.889 227.879 130.072 1.00 30.48 ? 3769 THR A O     1 
ATOM   16833 C  CB    . THR A 1 3769 ? 207.536 225.035 130.235 1.00 27.69 ? 3769 THR A CB    1 
ATOM   16834 O  OG1   . THR A 1 3769 ? 208.901 225.293 129.880 1.00 31.91 ? 3769 THR A OG1   1 
ATOM   16835 C  CG2   . THR A 1 3769 ? 207.279 223.534 130.223 1.00 26.10 ? 3769 THR A CG2   1 
ATOM   16836 N  N     . LEU A 1 3770 ? 207.750 227.858 128.808 1.00 24.18 ? 3770 LEU A N     1 
ATOM   16837 C  CA    . LEU A 1 3770 ? 207.900 229.308 128.888 1.00 25.29 ? 3770 LEU A CA    1 
ATOM   16838 C  C     . LEU A 1 3770 ? 206.725 230.018 128.234 1.00 28.13 ? 3770 LEU A C     1 
ATOM   16839 O  O     . LEU A 1 3770 ? 206.213 231.008 128.768 1.00 30.63 ? 3770 LEU A O     1 
ATOM   16840 C  CB    . LEU A 1 3770 ? 209.214 229.740 128.238 1.00 22.43 ? 3770 LEU A CB    1 
ATOM   16841 C  CG    . LEU A 1 3770 ? 210.504 229.265 128.902 1.00 19.55 ? 3770 LEU A CG    1 
ATOM   16842 C  CD1   . LEU A 1 3770 ? 211.701 229.997 128.320 1.00 20.82 ? 3770 LEU A CD1   1 
ATOM   16843 C  CD2   . LEU A 1 3770 ? 210.430 229.460 130.406 1.00 21.91 ? 3770 LEU A CD2   1 
ATOM   16844 N  N     . GLU A 1 3771 ? 206.283 229.526 127.074 1.00 27.48 ? 3771 GLU A N     1 
ATOM   16845 C  CA    . GLU A 1 3771 ? 205.138 230.132 126.405 1.00 24.20 ? 3771 GLU A CA    1 
ATOM   16846 C  C     . GLU A 1 3771 ? 203.881 230.021 127.257 1.00 28.12 ? 3771 GLU A C     1 
ATOM   16847 O  O     . GLU A 1 3771 ? 203.116 230.984 127.377 1.00 30.17 ? 3771 GLU A O     1 
ATOM   16848 C  CB    . GLU A 1 3771 ? 204.925 229.476 125.043 1.00 29.20 ? 3771 GLU A CB    1 
ATOM   16849 C  CG    . GLU A 1 3771 ? 206.079 229.662 124.076 1.00 27.39 ? 3771 GLU A CG    1 
ATOM   16850 C  CD    . GLU A 1 3771 ? 205.995 228.727 122.887 1.00 30.10 ? 3771 GLU A CD    1 
ATOM   16851 O  OE1   . GLU A 1 3771 ? 205.849 227.505 123.102 1.00 33.11 ? 3771 GLU A OE1   1 
ATOM   16852 O  OE2   . GLU A 1 3771 ? 206.079 229.211 121.738 1.00 33.72 ? 3771 GLU A OE2   1 
ATOM   16853 N  N     . ASN A 1 3772 ? 203.652 228.851 127.860 1.00 24.90 ? 3772 ASN A N     1 
ATOM   16854 C  CA    . ASN A 1 3772 ? 202.470 228.667 128.695 1.00 23.16 ? 3772 ASN A CA    1 
ATOM   16855 C  C     . ASN A 1 3772 ? 202.522 229.552 129.935 1.00 24.10 ? 3772 ASN A C     1 
ATOM   16856 O  O     . ASN A 1 3772 ? 201.506 230.138 130.325 1.00 22.26 ? 3772 ASN A O     1 
ATOM   16857 C  CB    . ASN A 1 3772 ? 202.327 227.196 129.085 1.00 22.74 ? 3772 ASN A CB    1 
ATOM   16858 C  CG    . ASN A 1 3772 ? 202.172 226.287 127.882 1.00 27.39 ? 3772 ASN A CG    1 
ATOM   16859 O  OD1   . ASN A 1 3772 ? 202.222 226.738 126.738 1.00 26.63 ? 3772 ASN A OD1   1 
ATOM   16860 N  ND2   . ASN A 1 3772 ? 201.977 224.999 128.136 1.00 30.93 ? 3772 ASN A ND2   1 
ATOM   16861 N  N     . LEU A 1 3773 ? 203.691 229.653 130.570 1.00 24.89 ? 3773 LEU A N     1 
ATOM   16862 C  CA    . LEU A 1 3773 ? 203.834 230.560 131.705 1.00 23.53 ? 3773 LEU A CA    1 
ATOM   16863 C  C     . LEU A 1 3773 ? 203.657 232.010 131.277 1.00 23.10 ? 3773 LEU A C     1 
ATOM   16864 O  O     . LEU A 1 3773 ? 203.005 232.796 131.973 1.00 28.95 ? 3773 LEU A O     1 
ATOM   16865 C  CB    . LEU A 1 3773 ? 205.193 230.358 132.372 1.00 24.10 ? 3773 LEU A CB    1 
ATOM   16866 C  CG    . LEU A 1 3773 ? 205.419 228.998 133.033 1.00 24.03 ? 3773 LEU A CG    1 
ATOM   16867 C  CD1   . LEU A 1 3773 ? 206.803 228.929 133.652 1.00 19.36 ? 3773 LEU A CD1   1 
ATOM   16868 C  CD2   . LEU A 1 3773 ? 204.346 228.722 134.075 1.00 23.80 ? 3773 LEU A CD2   1 
ATOM   16869 N  N     . LYS A 1 3774 ? 204.231 232.384 130.132 1.00 22.90 ? 3774 LYS A N     1 
ATOM   16870 C  CA    . LYS A 1 3774 ? 204.030 233.733 129.614 1.00 23.26 ? 3774 LYS A CA    1 
ATOM   16871 C  C     . LYS A 1 3774 ? 202.577 233.969 129.223 1.00 23.53 ? 3774 LYS A C     1 
ATOM   16872 O  O     . LYS A 1 3774 ? 202.031 235.050 129.468 1.00 28.20 ? 3774 LYS A O     1 
ATOM   16873 C  CB    . LYS A 1 3774 ? 204.955 233.986 128.424 1.00 20.82 ? 3774 LYS A CB    1 
ATOM   16874 C  CG    . LYS A 1 3774 ? 206.385 234.306 128.815 1.00 22.74 ? 3774 LYS A CG    1 
ATOM   16875 C  CD    . LYS A 1 3774 ? 206.464 235.618 129.578 1.00 26.31 ? 3774 LYS A CD    1 
ATOM   16876 C  CE    . LYS A 1 3774 ? 205.780 236.748 128.820 1.00 27.61 ? 3774 LYS A CE    1 
ATOM   16877 N  NZ    . LYS A 1 3774 ? 205.991 238.072 129.462 1.00 28.37 ? 3774 LYS A NZ    1 
ATOM   16878 N  N     . ARG A 1 3775 ? 201.938 232.973 128.603 1.00 25.31 ? 3775 ARG A N     1 
ATOM   16879 C  CA    . ARG A 1 3775 ? 200.541 233.124 128.210 1.00 24.28 ? 3775 ARG A CA    1 
ATOM   16880 C  C     . ARG A 1 3775 ? 199.640 233.295 129.426 1.00 22.12 ? 3775 ARG A C     1 
ATOM   16881 O  O     . ARG A 1 3775 ? 198.745 234.148 129.428 1.00 24.60 ? 3775 ARG A O     1 
ATOM   16882 C  CB    . ARG A 1 3775 ? 200.097 231.920 127.381 1.00 22.22 ? 3775 ARG A CB    1 
ATOM   16883 C  CG    . ARG A 1 3775 ? 198.655 231.975 126.915 1.00 27.54 ? 3775 ARG A CG    1 
ATOM   16884 C  CD    . ARG A 1 3775 ? 198.268 230.694 126.200 1.00 28.60 ? 3775 ARG A CD    1 
ATOM   16885 N  NE    . ARG A 1 3775 ? 199.270 230.305 125.216 1.00 31.52 ? 3775 ARG A NE    1 
ATOM   16886 C  CZ    . ARG A 1 3775 ? 200.032 229.223 125.306 1.00 33.02 ? 3775 ARG A CZ    1 
ATOM   16887 N  NH1   . ARG A 1 3775 ? 199.934 228.393 126.332 1.00 28.11 ? 3775 ARG A NH1   1 
ATOM   16888 N  NH2   . ARG A 1 3775 ? 200.913 228.969 124.344 1.00 32.14 ? 3775 ARG A NH2   1 
ATOM   16889 N  N     . GLU A 1 3776 ? 199.862 232.500 130.472 1.00 22.36 ? 3776 GLU A N     1 
ATOM   16890 C  CA    . GLU A 1 3776 ? 199.081 232.669 131.691 1.00 21.47 ? 3776 GLU A CA    1 
ATOM   16891 C  C     . GLU A 1 3776 ? 199.439 233.965 132.402 1.00 24.78 ? 3776 GLU A C     1 
ATOM   16892 O  O     . GLU A 1 3776 ? 198.575 234.579 133.037 1.00 24.66 ? 3776 GLU A O     1 
ATOM   16893 C  CB    . GLU A 1 3776 ? 199.279 231.469 132.617 1.00 16.26 ? 3776 GLU A CB    1 
ATOM   16894 C  CG    . GLU A 1 3776 ? 198.154 231.271 133.619 1.00 19.79 ? 3776 GLU A CG    1 
ATOM   16895 C  CD    . GLU A 1 3776 ? 198.457 230.189 134.638 1.00 31.46 ? 3776 GLU A CD    1 
ATOM   16896 O  OE1   . GLU A 1 3776 ? 199.634 230.041 135.026 1.00 26.44 ? 3776 GLU A OE1   1 
ATOM   16897 O  OE2   . GLU A 1 3776 ? 197.513 229.481 135.049 1.00 34.08 ? 3776 GLU A OE2   1 
ATOM   16898 N  N     . ALA A 1 3777 ? 200.698 234.400 132.305 1.00 20.72 ? 3777 ALA A N     1 
ATOM   16899 C  CA    . ALA A 1 3777 ? 201.092 235.668 132.909 1.00 18.97 ? 3777 ALA A CA    1 
ATOM   16900 C  C     . ALA A 1 3777 ? 200.370 236.840 132.258 1.00 20.97 ? 3777 ALA A C     1 
ATOM   16901 O  O     . ALA A 1 3777 ? 199.959 237.783 132.942 1.00 24.41 ? 3777 ALA A O     1 
ATOM   16902 C  CB    . ALA A 1 3777 ? 202.607 235.851 132.814 1.00 23.36 ? 3777 ALA A CB    1 
ATOM   16903 N  N     . ALA A 1 3778 ? 200.213 236.804 130.933 1.00 21.75 ? 3778 ALA A N     1 
ATOM   16904 C  CA    . ALA A 1 3778 ? 199.534 237.896 130.242 1.00 19.73 ? 3778 ALA A CA    1 
ATOM   16905 C  C     . ALA A 1 3778 ? 198.044 237.916 130.562 1.00 23.24 ? 3778 ALA A C     1 
ATOM   16906 O  O     . ALA A 1 3778 ? 197.460 238.989 130.758 1.00 22.09 ? 3778 ALA A O     1 
ATOM   16907 C  CB    . ALA A 1 3778 ? 199.761 237.789 128.736 1.00 19.23 ? 3778 ALA A CB    1 
ATOM   16908 N  N     . GLU A 1 3779 ? 197.408 236.743 130.618 1.00 22.82 ? 3779 GLU A N     1 
ATOM   16909 C  CA    . GLU A 1 3779 ? 195.973 236.693 130.886 1.00 19.84 ? 3779 GLU A CA    1 
ATOM   16910 C  C     . GLU A 1 3779 ? 195.653 237.136 132.308 1.00 23.24 ? 3779 GLU A C     1 
ATOM   16911 O  O     . GLU A 1 3779 ? 194.684 237.870 132.528 1.00 26.95 ? 3779 GLU A O     1 
ATOM   16912 C  CB    . GLU A 1 3779 ? 195.436 235.286 130.632 1.00 19.82 ? 3779 GLU A CB    1 
ATOM   16913 C  CG    . GLU A 1 3779 ? 195.503 234.863 129.179 1.00 23.85 ? 3779 GLU A CG    1 
ATOM   16914 C  CD    . GLU A 1 3779 ? 194.580 235.677 128.294 1.00 31.28 ? 3779 GLU A CD    1 
ATOM   16915 O  OE1   . GLU A 1 3779 ? 193.511 236.109 128.778 1.00 32.77 ? 3779 GLU A OE1   1 
ATOM   16916 O  OE2   . GLU A 1 3779 ? 194.923 235.885 127.112 1.00 30.97 ? 3779 GLU A OE2   1 
ATOM   16917 N  N     . VAL A 1 3780 ? 196.447 236.698 133.286 1.00 22.90 ? 3780 VAL A N     1 
ATOM   16918 C  CA    . VAL A 1 3780 ? 196.230 237.147 134.657 1.00 20.75 ? 3780 VAL A CA    1 
ATOM   16919 C  C     . VAL A 1 3780 ? 196.471 238.647 134.762 1.00 19.95 ? 3780 VAL A C     1 
ATOM   16920 O  O     . VAL A 1 3780 ? 195.714 239.365 135.425 1.00 24.05 ? 3780 VAL A O     1 
ATOM   16921 C  CB    . VAL A 1 3780 ? 197.115 236.349 135.632 1.00 19.17 ? 3780 VAL A CB    1 
ATOM   16922 C  CG1   . VAL A 1 3780 ? 196.960 236.881 137.044 1.00 16.79 ? 3780 VAL A CG1   1 
ATOM   16923 C  CG2   . VAL A 1 3780 ? 196.749 234.880 135.589 1.00 18.55 ? 3780 VAL A CG2   1 
ATOM   16924 N  N     . THR A 1 3781 ? 197.516 239.145 134.100 1.00 20.85 ? 3781 THR A N     1 
ATOM   16925 C  CA    . THR A 1 3781 ? 197.738 240.585 134.040 1.00 19.32 ? 3781 THR A CA    1 
ATOM   16926 C  C     . THR A 1 3781 ? 196.571 241.297 133.373 1.00 20.88 ? 3781 THR A C     1 
ATOM   16927 O  O     . THR A 1 3781 ? 196.247 242.434 133.735 1.00 22.33 ? 3781 THR A O     1 
ATOM   16928 C  CB    . THR A 1 3781 ? 199.045 240.879 133.302 1.00 21.51 ? 3781 THR A CB    1 
ATOM   16929 O  OG1   . THR A 1 3781 ? 200.096 240.085 133.866 1.00 22.05 ? 3781 THR A OG1   1 
ATOM   16930 C  CG2   . THR A 1 3781 ? 199.413 242.346 133.421 1.00 19.86 ? 3781 THR A CG2   1 
ATOM   16931 N  N     . ARG A 1 3782 ? 195.925 240.648 132.401 1.00 28.73 ? 3782 ARG A N     1 
ATOM   16932 C  CA    . ARG A 1 3782 ? 194.697 241.193 131.829 1.00 22.09 ? 3782 ARG A CA    1 
ATOM   16933 C  C     . ARG A 1 3782 ? 193.557 241.165 132.841 1.00 21.27 ? 3782 ARG A C     1 
ATOM   16934 O  O     . ARG A 1 3782 ? 192.727 242.079 132.873 1.00 26.26 ? 3782 ARG A O     1 
ATOM   16935 C  CB    . ARG A 1 3782 ? 194.325 240.422 130.564 1.00 20.54 ? 3782 ARG A CB    1 
ATOM   16936 C  CG    . ARG A 1 3782 ? 193.124 240.973 129.815 1.00 26.83 ? 3782 ARG A CG    1 
ATOM   16937 C  CD    . ARG A 1 3782 ? 192.250 239.848 129.286 1.00 23.39 ? 3782 ARG A CD    1 
ATOM   16938 N  NE    . ARG A 1 3782 ? 191.691 239.036 130.361 1.00 28.16 ? 3782 ARG A NE    1 
ATOM   16939 C  CZ    . ARG A 1 3782 ? 190.871 238.012 130.176 1.00 32.36 ? 3782 ARG A CZ    1 
ATOM   16940 N  NH1   . ARG A 1 3782 ? 190.491 237.641 128.964 1.00 28.66 ? 3782 ARG A NH1   1 
ATOM   16941 N  NH2   . ARG A 1 3782 ? 190.420 237.340 131.232 1.00 32.74 ? 3782 ARG A NH2   1 
ATOM   16942 N  N     . LYS A 1 3783 ? 193.499 240.122 133.674 1.00 22.61 ? 3783 LYS A N     1 
ATOM   16943 C  CA    . LYS A 1 3783 ? 192.450 240.038 134.687 1.00 20.21 ? 3783 LYS A CA    1 
ATOM   16944 C  C     . LYS A 1 3783 ? 192.687 241.014 135.832 1.00 23.62 ? 3783 LYS A C     1 
ATOM   16945 O  O     . LYS A 1 3783 ? 191.729 241.436 136.490 1.00 29.90 ? 3783 LYS A O     1 
ATOM   16946 C  CB    . LYS A 1 3783 ? 192.344 238.613 135.227 1.00 18.10 ? 3783 LYS A CB    1 
ATOM   16947 C  CG    . LYS A 1 3783 ? 191.933 237.578 134.198 1.00 21.82 ? 3783 LYS A CG    1 
ATOM   16948 C  CD    . LYS A 1 3783 ? 192.314 236.176 134.647 1.00 20.57 ? 3783 LYS A CD    1 
ATOM   16949 C  CE    . LYS A 1 3783 ? 192.621 235.284 133.457 1.00 25.96 ? 3783 LYS A CE    1 
ATOM   16950 N  NZ    . LYS A 1 3783 ? 193.262 234.002 133.866 1.00 25.44 ? 3783 LYS A NZ    1 
ATOM   16951 N  N     . VAL A 1 3784 ? 193.944 241.365 136.106 1.00 20.73 ? 3784 VAL A N     1 
ATOM   16952 C  CA    . VAL A 1 3784 ? 194.224 242.345 137.153 1.00 25.08 ? 3784 VAL A CA    1 
ATOM   16953 C  C     . VAL A 1 3784 ? 193.766 243.732 136.722 1.00 23.65 ? 3784 VAL A C     1 
ATOM   16954 O  O     . VAL A 1 3784 ? 193.229 244.501 137.527 1.00 25.36 ? 3784 VAL A O     1 
ATOM   16955 C  CB    . VAL A 1 3784 ? 195.717 242.328 137.523 1.00 22.66 ? 3784 VAL A CB    1 
ATOM   16956 C  CG1   . VAL A 1 3784 ? 196.026 243.431 138.524 1.00 24.33 ? 3784 VAL A CG1   1 
ATOM   16957 C  CG2   . VAL A 1 3784 ? 196.097 240.983 138.103 1.00 19.87 ? 3784 VAL A CG2   1 
ATOM   16958 N  N     . GLU A 1 3785 ? 193.973 244.076 135.449 1.00 23.21 ? 3785 GLU A N     1 
ATOM   16959 C  CA    . GLU A 1 3785 ? 193.557 245.387 134.959 1.00 25.60 ? 3785 GLU A CA    1 
ATOM   16960 C  C     . GLU A 1 3785 ? 192.046 245.558 135.048 1.00 27.49 ? 3785 GLU A C     1 
ATOM   16961 O  O     . GLU A 1 3785 ? 191.556 246.633 135.416 1.00 26.10 ? 3785 GLU A O     1 
ATOM   16962 C  CB    . GLU A 1 3785 ? 194.037 245.588 133.521 1.00 25.59 ? 3785 GLU A CB    1 
ATOM   16963 C  CG    . GLU A 1 3785 ? 195.551 245.625 133.355 1.00 27.97 ? 3785 GLU A CG    1 
ATOM   16964 C  CD    . GLU A 1 3785 ? 196.176 246.906 133.884 1.00 34.63 ? 3785 GLU A CD    1 
ATOM   16965 O  OE1   . GLU A 1 3785 ? 195.428 247.822 134.289 1.00 34.08 ? 3785 GLU A OE1   1 
ATOM   16966 O  OE2   . GLU A 1 3785 ? 197.421 246.996 133.891 1.00 36.15 ? 3785 GLU A OE2   1 
ATOM   16967 N  N     . GLU A 1 3786 ? 191.288 244.511 134.710 1.00 23.93 ? 3786 GLU A N     1 
ATOM   16968 C  CA    . GLU A 1 3786 ? 189.835 244.617 134.756 1.00 24.60 ? 3786 GLU A CA    1 
ATOM   16969 C  C     . GLU A 1 3786 ? 189.316 244.655 136.188 1.00 26.88 ? 3786 GLU A C     1 
ATOM   16970 O  O     . GLU A 1 3786 ? 188.243 245.213 136.439 1.00 30.33 ? 3786 GLU A O     1 
ATOM   16971 C  CB    . GLU A 1 3786 ? 189.195 243.467 133.975 1.00 21.44 ? 3786 GLU A CB    1 
ATOM   16972 C  CG    . GLU A 1 3786 ? 189.352 242.099 134.613 1.00 30.70 ? 3786 GLU A CG    1 
ATOM   16973 C  CD    . GLU A 1 3786 ? 188.854 240.978 133.720 1.00 37.05 ? 3786 GLU A CD    1 
ATOM   16974 O  OE1   . GLU A 1 3786 ? 188.364 241.273 132.610 1.00 34.83 ? 3786 GLU A OE1   1 
ATOM   16975 O  OE2   . GLU A 1 3786 ? 188.955 239.801 134.129 1.00 34.98 ? 3786 GLU A OE2   1 
ATOM   16976 N  N     . THR A 1 3787 ? 190.050 244.069 137.138 1.00 24.35 ? 3787 THR A N     1 
ATOM   16977 C  CA    . THR A 1 3787 ? 189.665 244.199 138.538 1.00 22.60 ? 3787 THR A CA    1 
ATOM   16978 C  C     . THR A 1 3787 ? 190.050 245.553 139.114 1.00 26.98 ? 3787 THR A C     1 
ATOM   16979 O  O     . THR A 1 3787 ? 189.513 245.948 140.153 1.00 31.95 ? 3787 THR A O     1 
ATOM   16980 C  CB    . THR A 1 3787 ? 190.291 243.087 139.380 1.00 21.55 ? 3787 THR A CB    1 
ATOM   16981 O  OG1   . THR A 1 3787 ? 191.682 242.963 139.058 1.00 30.91 ? 3787 THR A OG1   1 
ATOM   16982 C  CG2   . THR A 1 3787 ? 189.590 241.763 139.127 1.00 22.53 ? 3787 THR A CG2   1 
ATOM   16983 N  N     . ASP A 1 3788 ? 190.974 246.270 138.469 1.00 22.22 ? 3788 ASP A N     1 
ATOM   16984 C  CA    . ASP A 1 3788 ? 191.338 247.599 138.947 1.00 24.09 ? 3788 ASP A CA    1 
ATOM   16985 C  C     . ASP A 1 3788 ? 190.218 248.602 138.705 1.00 23.00 ? 3788 ASP A C     1 
ATOM   16986 O  O     . ASP A 1 3788 ? 189.933 249.441 139.568 1.00 29.36 ? 3788 ASP A O     1 
ATOM   16987 C  CB    . ASP A 1 3788 ? 192.631 248.065 138.276 1.00 24.87 ? 3788 ASP A CB    1 
ATOM   16988 C  CG    . ASP A 1 3788 ? 193.858 247.389 138.848 1.00 32.05 ? 3788 ASP A CG    1 
ATOM   16989 O  OD1   . ASP A 1 3788 ? 193.711 246.585 139.792 1.00 27.44 ? 3788 ASP A OD1   1 
ATOM   16990 O  OD2   . ASP A 1 3788 ? 194.973 247.665 138.358 1.00 37.90 ? 3788 ASP A OD2   1 
ATOM   16991 N  N     . ILE A 1 3789 ? 189.573 248.536 137.538 1.00 26.13 ? 3789 ILE A N     1 
ATOM   16992 C  CA    . ILE A 1 3789 ? 188.528 249.505 137.221 1.00 24.08 ? 3789 ILE A CA    1 
ATOM   16993 C  C     . ILE A 1 3789 ? 187.292 249.277 138.083 1.00 25.75 ? 3789 ILE A C     1 
ATOM   16994 O  O     . ILE A 1 3789 ? 186.614 250.237 138.467 1.00 29.69 ? 3789 ILE A O     1 
ATOM   16995 C  CB    . ILE A 1 3789 ? 188.190 249.469 135.717 1.00 23.51 ? 3789 ILE A CB    1 
ATOM   16996 C  CG1   . ILE A 1 3789 ? 187.645 248.103 135.304 1.00 27.06 ? 3789 ILE A CG1   1 
ATOM   16997 C  CG2   . ILE A 1 3789 ? 189.420 249.810 134.891 1.00 23.20 ? 3789 ILE A CG2   1 
ATOM   16998 C  CD1   . ILE A 1 3789 ? 187.081 248.070 133.903 1.00 28.73 ? 3789 ILE A CD1   1 
ATOM   16999 N  N     . VAL A 1 3790 ? 186.975 248.020 138.401 1.00 24.51 ? 3790 VAL A N     1 
ATOM   17000 C  CA    . VAL A 1 3790 ? 185.778 247.742 139.187 1.00 22.50 ? 3790 VAL A CA    1 
ATOM   17001 C  C     . VAL A 1 3790 ? 185.963 248.196 140.633 1.00 22.73 ? 3790 VAL A C     1 
ATOM   17002 O  O     . VAL A 1 3790 ? 185.002 248.623 141.284 1.00 21.50 ? 3790 VAL A O     1 
ATOM   17003 C  CB    . VAL A 1 3790 ? 185.415 246.247 139.087 1.00 23.90 ? 3790 VAL A CB    1 
ATOM   17004 C  CG1   . VAL A 1 3790 ? 184.149 245.941 139.875 1.00 18.96 ? 3790 VAL A CG1   1 
ATOM   17005 C  CG2   . VAL A 1 3790 ? 185.253 245.840 137.633 1.00 18.89 ? 3790 VAL A CG2   1 
ATOM   17006 N  N     . MET A 1 3791 ? 187.191 248.118 141.161 1.00 23.14 ? 3791 MET A N     1 
ATOM   17007 C  CA    . MET A 1 3791 ? 187.482 248.730 142.457 1.00 21.17 ? 3791 MET A CA    1 
ATOM   17008 C  C     . MET A 1 3791 ? 187.228 250.231 142.439 1.00 24.68 ? 3791 MET A C     1 
ATOM   17009 O  O     . MET A 1 3791 ? 186.772 250.801 143.438 1.00 21.79 ? 3791 MET A O     1 
ATOM   17010 C  CB    . MET A 1 3791 ? 188.925 248.439 142.873 1.00 23.05 ? 3791 MET A CB    1 
ATOM   17011 C  CG    . MET A 1 3791 ? 189.217 248.624 144.367 1.00 24.74 ? 3791 MET A CG    1 
ATOM   17012 S  SD    . MET A 1 3791 ? 187.966 248.099 145.559 1.00 50.92 ? 3791 MET A SD    1 
ATOM   17013 C  CE    . MET A 1 3791 ? 187.829 246.358 145.201 1.00 15.97 ? 3791 MET A CE    1 
ATOM   17014 N  N     . GLN A 1 3792 ? 187.525 250.893 141.319 1.00 21.87 ? 3792 GLN A N     1 
ATOM   17015 C  CA    . GLN A 1 3792 ? 187.230 252.318 141.215 1.00 20.96 ? 3792 GLN A CA    1 
ATOM   17016 C  C     . GLN A 1 3792 ? 185.739 252.588 141.362 1.00 22.56 ? 3792 GLN A C     1 
ATOM   17017 O  O     . GLN A 1 3792 ? 185.348 253.632 141.896 1.00 26.59 ? 3792 GLN A O     1 
ATOM   17018 C  CB    . GLN A 1 3792 ? 187.756 252.870 139.891 1.00 23.16 ? 3792 GLN A CB    1 
ATOM   17019 C  CG    . GLN A 1 3792 ? 189.272 252.837 139.778 1.00 26.33 ? 3792 GLN A CG    1 
ATOM   17020 C  CD    . GLN A 1 3792 ? 189.756 252.912 138.343 1.00 34.19 ? 3792 GLN A CD    1 
ATOM   17021 O  OE1   . GLN A 1 3792 ? 190.491 252.040 137.879 1.00 35.96 ? 3792 GLN A OE1   1 
ATOM   17022 N  NE2   . GLN A 1 3792 ? 189.350 253.959 137.634 1.00 30.76 ? 3792 GLN A NE2   1 
ATOM   17023 N  N     . GLU A 1 3793 ? 184.895 251.664 140.899 1.00 21.55 ? 3793 GLU A N     1 
ATOM   17024 C  CA    . GLU A 1 3793 ? 183.466 251.764 141.175 1.00 22.43 ? 3793 GLU A CA    1 
ATOM   17025 C  C     . GLU A 1 3793 ? 183.181 251.591 142.663 1.00 24.04 ? 3793 GLU A C     1 
ATOM   17026 O  O     . GLU A 1 3793 ? 182.337 252.299 143.226 1.00 24.20 ? 3793 GLU A O     1 
ATOM   17027 C  CB    . GLU A 1 3793 ? 182.702 250.727 140.354 1.00 21.76 ? 3793 GLU A CB    1 
ATOM   17028 C  CG    . GLU A 1 3793 ? 181.191 250.768 140.535 1.00 29.15 ? 3793 GLU A CG    1 
ATOM   17029 C  CD    . GLU A 1 3793 ? 180.569 252.057 140.026 1.00 34.64 ? 3793 GLU A CD    1 
ATOM   17030 O  OE1   . GLU A 1 3793 ? 181.158 252.694 139.128 1.00 34.86 ? 3793 GLU A OE1   1 
ATOM   17031 O  OE2   . GLU A 1 3793 ? 179.487 252.431 140.527 1.00 35.03 ? 3793 GLU A OE2   1 
ATOM   17032 N  N     . VAL A 1 3794 ? 183.866 250.650 143.315 1.00 24.44 ? 3794 VAL A N     1 
ATOM   17033 C  CA    . VAL A 1 3794 ? 183.692 250.457 144.751 1.00 19.30 ? 3794 VAL A CA    1 
ATOM   17034 C  C     . VAL A 1 3794 ? 184.226 251.659 145.522 1.00 20.68 ? 3794 VAL A C     1 
ATOM   17035 O  O     . VAL A 1 3794 ? 183.600 252.131 146.478 1.00 24.22 ? 3794 VAL A O     1 
ATOM   17036 C  CB    . VAL A 1 3794 ? 184.366 249.148 145.199 1.00 16.41 ? 3794 VAL A CB    1 
ATOM   17037 C  CG1   . VAL A 1 3794 ? 184.557 249.127 146.706 1.00 14.23 ? 3794 VAL A CG1   1 
ATOM   17038 C  CG2   . VAL A 1 3794 ? 183.540 247.953 144.754 1.00 14.46 ? 3794 VAL A CG2   1 
ATOM   17039 N  N     . GLU A 1 3795 ? 185.389 252.174 145.117 1.00 25.47 ? 3795 GLU A N     1 
ATOM   17040 C  CA    . GLU A 1 3795 ? 186.012 253.276 145.844 1.00 22.53 ? 3795 GLU A CA    1 
ATOM   17041 C  C     . GLU A 1 3795 ? 185.158 254.536 145.786 1.00 20.03 ? 3795 GLU A C     1 
ATOM   17042 O  O     . GLU A 1 3795 ? 185.016 255.245 146.791 1.00 22.27 ? 3795 GLU A O     1 
ATOM   17043 C  CB    . GLU A 1 3795 ? 187.406 253.547 145.281 1.00 17.44 ? 3795 GLU A CB    1 
ATOM   17044 C  CG    . GLU A 1 3795 ? 188.180 254.645 145.990 1.00 22.61 ? 3795 GLU A CG    1 
ATOM   17045 C  CD    . GLU A 1 3795 ? 188.527 254.294 147.426 1.00 35.47 ? 3795 GLU A CD    1 
ATOM   17046 O  OE1   . GLU A 1 3795 ? 188.629 253.089 147.740 1.00 34.94 ? 3795 GLU A OE1   1 
ATOM   17047 O  OE2   . GLU A 1 3795 ? 188.704 255.225 148.239 1.00 41.72 ? 3795 GLU A OE2   1 
ATOM   17048 N  N     . THR A 1 3796 ? 184.579 254.835 144.620 1.00 18.41 ? 3796 THR A N     1 
ATOM   17049 C  CA    . THR A 1 3796 ? 183.798 256.062 144.485 1.00 21.14 ? 3796 THR A CA    1 
ATOM   17050 C  C     . THR A 1 3796 ? 182.482 255.981 145.254 1.00 20.22 ? 3796 THR A C     1 
ATOM   17051 O  O     . THR A 1 3796 ? 181.972 257.010 145.710 1.00 18.38 ? 3796 THR A O     1 
ATOM   17052 C  CB    . THR A 1 3796 ? 183.545 256.376 143.006 1.00 19.42 ? 3796 THR A CB    1 
ATOM   17053 O  OG1   . THR A 1 3796 ? 182.931 257.663 142.884 1.00 31.99 ? 3796 THR A OG1   1 
ATOM   17054 C  CG2   . THR A 1 3796 ? 182.640 255.336 142.372 1.00 18.79 ? 3796 THR A CG2   1 
ATOM   17055 N  N     . VAL A 1 3797 ? 181.921 254.779 145.407 1.00 19.04 ? 3797 VAL A N     1 
ATOM   17056 C  CA    . VAL A 1 3797 ? 180.754 254.612 146.265 1.00 15.85 ? 3797 VAL A CA    1 
ATOM   17057 C  C     . VAL A 1 3797 ? 181.144 254.775 147.730 1.00 17.03 ? 3797 VAL A C     1 
ATOM   17058 O  O     . VAL A 1 3797 ? 180.433 255.420 148.508 1.00 24.07 ? 3797 VAL A O     1 
ATOM   17059 C  CB    . VAL A 1 3797 ? 180.085 253.249 146.006 1.00 20.56 ? 3797 VAL A CB    1 
ATOM   17060 C  CG1   . VAL A 1 3797 ? 178.961 253.005 147.001 1.00 11.19 ? 3797 VAL A CG1   1 
ATOM   17061 C  CG2   . VAL A 1 3797 ? 179.557 253.181 144.585 1.00 21.50 ? 3797 VAL A CG2   1 
ATOM   17062 N  N     . SER A 1 3798 ? 182.282 254.199 148.123 1.00 15.60 ? 3798 SER A N     1 
ATOM   17063 C  CA    . SER A 1 3798 ? 182.743 254.258 149.505 1.00 17.60 ? 3798 SER A CA    1 
ATOM   17064 C  C     . SER A 1 3798 ? 183.151 255.657 149.938 1.00 14.49 ? 3798 SER A C     1 
ATOM   17065 O  O     . SER A 1 3798 ? 183.248 255.906 151.144 1.00 21.02 ? 3798 SER A O     1 
ATOM   17066 C  CB    . SER A 1 3798 ? 183.919 253.300 149.703 1.00 19.14 ? 3798 SER A CB    1 
ATOM   17067 O  OG    . SER A 1 3798 ? 183.580 251.984 149.309 1.00 18.05 ? 3798 SER A OG    1 
ATOM   17068 N  N     . GLN A 1 3799 ? 183.395 256.570 148.993 1.00 14.53 ? 3799 GLN A N     1 
ATOM   17069 C  CA    . GLN A 1 3799 ? 183.795 257.926 149.355 1.00 12.39 ? 3799 GLN A CA    1 
ATOM   17070 C  C     . GLN A 1 3799 ? 182.684 258.668 150.088 1.00 17.14 ? 3799 GLN A C     1 
ATOM   17071 O  O     . GLN A 1 3799 ? 182.967 259.564 150.891 1.00 21.77 ? 3799 GLN A O     1 
ATOM   17072 C  CB    . GLN A 1 3799 ? 184.206 258.701 148.102 1.00 13.67 ? 3799 GLN A CB    1 
ATOM   17073 C  CG    . GLN A 1 3799 ? 185.630 258.445 147.653 1.00 17.16 ? 3799 GLN A CG    1 
ATOM   17074 C  CD    . GLN A 1 3799 ? 186.655 258.968 148.641 1.00 29.20 ? 3799 GLN A CD    1 
ATOM   17075 O  OE1   . GLN A 1 3799 ? 187.445 258.204 149.194 1.00 33.17 ? 3799 GLN A OE1   1 
ATOM   17076 N  NE2   . GLN A 1 3799 ? 186.646 260.278 148.866 1.00 26.01 ? 3799 GLN A NE2   1 
ATOM   17077 N  N     . GLN A 1 3800 ? 181.423 258.321 149.822 1.00 15.03 ? 3800 GLN A N     1 
ATOM   17078 C  CA    . GLN A 1 3800 ? 180.314 258.988 150.497 1.00 10.35 ? 3800 GLN A CA    1 
ATOM   17079 C  C     . GLN A 1 3800 ? 180.280 258.663 151.983 1.00 12.03 ? 3800 GLN A C     1 
ATOM   17080 O  O     . GLN A 1 3800 ? 179.892 259.512 152.793 1.00 13.64 ? 3800 GLN A O     1 
ATOM   17081 C  CB    . GLN A 1 3800 ? 178.991 258.599 149.838 1.00 13.62 ? 3800 GLN A CB    1 
ATOM   17082 C  CG    . GLN A 1 3800 ? 177.838 259.526 150.168 1.00 14.89 ? 3800 GLN A CG    1 
ATOM   17083 C  CD    . GLN A 1 3800 ? 176.502 258.970 149.733 1.00 18.24 ? 3800 GLN A CD    1 
ATOM   17084 O  OE1   . GLN A 1 3800 ? 176.402 257.814 149.322 1.00 25.34 ? 3800 GLN A OE1   1 
ATOM   17085 N  NE2   . GLN A 1 3800 ? 175.462 259.788 149.818 1.00 20.26 ? 3800 GLN A NE2   1 
ATOM   17086 N  N     . TYR A 1 3801 ? 180.682 257.454 152.360 1.00 11.76 ? 3801 TYR A N     1 
ATOM   17087 C  CA    . TYR A 1 3801 ? 180.646 257.013 153.747 1.00 5.46  ? 3801 TYR A CA    1 
ATOM   17088 C  C     . TYR A 1 3801 ? 181.949 257.268 154.488 1.00 7.45  ? 3801 TYR A C     1 
ATOM   17089 O  O     . TYR A 1 3801 ? 182.063 256.891 155.659 1.00 12.44 ? 3801 TYR A O     1 
ATOM   17090 C  CB    . TYR A 1 3801 ? 180.303 255.522 153.808 1.00 5.21  ? 3801 TYR A CB    1 
ATOM   17091 C  CG    . TYR A 1 3801 ? 178.982 255.181 153.168 1.00 8.35  ? 3801 TYR A CG    1 
ATOM   17092 C  CD1   . TYR A 1 3801 ? 177.803 255.234 153.894 1.00 8.18  ? 3801 TYR A CD1   1 
ATOM   17093 C  CD2   . TYR A 1 3801 ? 178.910 254.816 151.830 1.00 11.72 ? 3801 TYR A CD2   1 
ATOM   17094 C  CE1   . TYR A 1 3801 ? 176.592 254.930 153.313 1.00 6.45  ? 3801 TYR A CE1   1 
ATOM   17095 C  CE2   . TYR A 1 3801 ? 177.703 254.508 151.239 1.00 10.70 ? 3801 TYR A CE2   1 
ATOM   17096 C  CZ    . TYR A 1 3801 ? 176.546 254.567 151.986 1.00 8.74  ? 3801 TYR A CZ    1 
ATOM   17097 O  OH    . TYR A 1 3801 ? 175.340 254.261 151.403 1.00 19.06 ? 3801 TYR A OH    1 
ATOM   17098 N  N     . LEU A 1 3802 ? 182.932 257.889 153.838 1.00 8.67  ? 3802 LEU A N     1 
ATOM   17099 C  CA    . LEU A 1 3802 ? 184.201 258.178 154.505 1.00 7.77  ? 3802 LEU A CA    1 
ATOM   17100 C  C     . LEU A 1 3802 ? 184.050 259.118 155.696 1.00 4.39  ? 3802 LEU A C     1 
ATOM   17101 O  O     . LEU A 1 3802 ? 184.661 258.846 156.743 1.00 4.26  ? 3802 LEU A O     1 
ATOM   17102 C  CB    . LEU A 1 3802 ? 185.205 258.711 153.480 1.00 10.93 ? 3802 LEU A CB    1 
ATOM   17103 C  CG    . LEU A 1 3802 ? 186.616 259.008 153.986 1.00 13.47 ? 3802 LEU A CG    1 
ATOM   17104 C  CD1   . LEU A 1 3802 ? 187.274 257.736 154.487 1.00 8.44  ? 3802 LEU A CD1   1 
ATOM   17105 C  CD2   . LEU A 1 3802 ? 187.453 259.643 152.888 1.00 17.30 ? 3802 LEU A CD2   1 
ATOM   17106 N  N     . PRO A 1 3803 ? 183.294 260.223 155.622 1.00 9.24  ? 3803 PRO A N     1 
ATOM   17107 C  CA    . PRO A 1 3803 ? 183.157 261.081 156.814 1.00 3.73  ? 3803 PRO A CA    1 
ATOM   17108 C  C     . PRO A 1 3803 ? 182.540 260.382 158.013 1.00 3.88  ? 3803 PRO A C     1 
ATOM   17109 O  O     . PRO A 1 3803 ? 182.894 260.709 159.152 1.00 2.83  ? 3803 PRO A O     1 
ATOM   17110 C  CB    . PRO A 1 3803 ? 182.273 262.230 156.312 1.00 2.19  ? 3803 PRO A CB    1 
ATOM   17111 C  CG    . PRO A 1 3803 ? 182.530 262.274 154.857 1.00 4.11  ? 3803 PRO A CG    1 
ATOM   17112 C  CD    . PRO A 1 3803 ? 182.635 260.840 154.455 1.00 7.48  ? 3803 PRO A CD    1 
ATOM   17113 N  N     . LEU A 1 3804 ? 181.619 259.440 157.798 1.00 3.53  ? 3804 LEU A N     1 
ATOM   17114 C  CA    . LEU A 1 3804 ? 181.049 258.700 158.919 1.00 2.74  ? 3804 LEU A CA    1 
ATOM   17115 C  C     . LEU A 1 3804 ? 182.103 257.847 159.616 1.00 3.48  ? 3804 LEU A C     1 
ATOM   17116 O  O     . LEU A 1 3804 ? 182.135 257.774 160.849 1.00 2.83  ? 3804 LEU A O     1 
ATOM   17117 C  CB    . LEU A 1 3804 ? 179.887 257.832 158.439 1.00 2.89  ? 3804 LEU A CB    1 
ATOM   17118 C  CG    . LEU A 1 3804 ? 179.227 256.952 159.501 1.00 2.75  ? 3804 LEU A CG    1 
ATOM   17119 C  CD1   . LEU A 1 3804 ? 178.467 257.798 160.509 1.00 3.19  ? 3804 LEU A CD1   1 
ATOM   17120 C  CD2   . LEU A 1 3804 ? 178.317 255.920 158.861 1.00 1.77  ? 3804 LEU A CD2   1 
ATOM   17121 N  N     . SER A 1 3805 ? 182.972 257.193 158.840 1.00 3.73  ? 3805 SER A N     1 
ATOM   17122 C  CA    . SER A 1 3805 ? 184.025 256.374 159.432 1.00 2.06  ? 3805 SER A CA    1 
ATOM   17123 C  C     . SER A 1 3805 ? 185.017 257.226 160.213 1.00 2.42  ? 3805 SER A C     1 
ATOM   17124 O  O     . SER A 1 3805 ? 185.512 256.807 161.266 1.00 1.55  ? 3805 SER A O     1 
ATOM   17125 C  CB    . SER A 1 3805 ? 184.737 255.570 158.344 1.00 3.16  ? 3805 SER A CB    1 
ATOM   17126 O  OG    . SER A 1 3805 ? 185.407 256.419 157.431 1.00 7.78  ? 3805 SER A OG    1 
ATOM   17127 N  N     . THR A 1 3806 ? 185.331 258.422 159.707 1.00 2.71  ? 3806 THR A N     1 
ATOM   17128 C  CA    . THR A 1 3806 ? 186.170 259.346 160.463 1.00 2.10  ? 3806 THR A CA    1 
ATOM   17129 C  C     . THR A 1 3806 ? 185.495 259.757 161.764 1.00 2.52  ? 3806 THR A C     1 
ATOM   17130 O  O     . THR A 1 3806 ? 186.147 259.849 162.810 1.00 3.88  ? 3806 THR A O     1 
ATOM   17131 C  CB    . THR A 1 3806 ? 186.496 260.576 159.615 1.00 1.96  ? 3806 THR A CB    1 
ATOM   17132 O  OG1   . THR A 1 3806 ? 187.055 260.161 158.363 1.00 6.68  ? 3806 THR A OG1   1 
ATOM   17133 C  CG2   . THR A 1 3806 ? 187.488 261.472 160.335 1.00 1.55  ? 3806 THR A CG2   1 
ATOM   17134 N  N     . ALA A 1 3807 ? 184.185 260.013 161.716 1.00 2.05  ? 3807 ALA A N     1 
ATOM   17135 C  CA    . ALA A 1 3807 ? 183.451 260.328 162.936 1.00 1.58  ? 3807 ALA A CA    1 
ATOM   17136 C  C     . ALA A 1 3807 ? 183.475 259.157 163.908 1.00 1.14  ? 3807 ALA A C     1 
ATOM   17137 O  O     . ALA A 1 3807 ? 183.605 259.350 165.122 1.00 1.05  ? 3807 ALA A O     1 
ATOM   17138 C  CB    . ALA A 1 3807 ? 182.011 260.716 162.598 1.00 1.30  ? 3807 ALA A CB    1 
ATOM   17139 N  N     . CYS A 1 3808 ? 183.361 257.931 163.392 1.00 1.09  ? 3808 CYS A N     1 
ATOM   17140 C  CA    . CYS A 1 3808 ? 183.385 256.755 164.253 1.00 1.13  ? 3808 CYS A CA    1 
ATOM   17141 C  C     . CYS A 1 3808 ? 184.705 256.639 165.005 1.00 1.18  ? 3808 CYS A C     1 
ATOM   17142 O  O     . CYS A 1 3808 ? 184.720 256.360 166.210 1.00 1.08  ? 3808 CYS A O     1 
ATOM   17143 C  CB    . CYS A 1 3808 ? 183.136 255.497 163.426 1.00 1.05  ? 3808 CYS A CB    1 
ATOM   17144 S  SG    . CYS A 1 3808 ? 181.416 255.189 163.012 1.00 7.26  ? 3808 CYS A SG    1 
ATOM   17145 N  N     . SER A 1 3809 ? 185.828 256.847 164.313 1.00 1.60  ? 3809 SER A N     1 
ATOM   17146 C  CA    . SER A 1 3809 ? 187.125 256.729 164.969 1.00 1.71  ? 3809 SER A CA    1 
ATOM   17147 C  C     . SER A 1 3809 ? 187.339 257.849 165.979 1.00 1.09  ? 3809 SER A C     1 
ATOM   17148 O  O     . SER A 1 3809 ? 187.888 257.618 167.062 1.00 0.97  ? 3809 SER A O     1 
ATOM   17149 C  CB    . SER A 1 3809 ? 188.246 256.707 163.929 1.00 2.58  ? 3809 SER A CB    1 
ATOM   17150 O  OG    . SER A 1 3809 ? 188.335 257.936 163.233 1.00 7.34  ? 3809 SER A OG    1 
ATOM   17151 N  N     . SER A 1 3810 ? 186.914 259.071 165.646 1.00 1.40  ? 3810 SER A N     1 
ATOM   17152 C  CA    . SER A 1 3810 ? 187.047 260.175 166.590 1.00 1.15  ? 3810 SER A CA    1 
ATOM   17153 C  C     . SER A 1 3810 ? 186.198 259.943 167.834 1.00 1.02  ? 3810 SER A C     1 
ATOM   17154 O  O     . SER A 1 3810 ? 186.626 260.254 168.950 1.00 1.31  ? 3810 SER A O     1 
ATOM   17155 C  CB    . SER A 1 3810 ? 186.667 261.498 165.922 1.00 1.48  ? 3810 SER A CB    1 
ATOM   17156 O  OG    . SER A 1 3810 ? 187.296 261.641 164.663 1.00 5.44  ? 3810 SER A OG    1 
ATOM   17157 N  N     . ILE A 1 3811 ? 184.991 259.402 167.658 1.00 0.73  ? 3811 ILE A N     1 
ATOM   17158 C  CA    . ILE A 1 3811 ? 184.111 259.156 168.798 1.00 0.75  ? 3811 ILE A CA    1 
ATOM   17159 C  C     . ILE A 1 3811 ? 184.716 258.112 169.726 1.00 0.78  ? 3811 ILE A C     1 
ATOM   17160 O  O     . ILE A 1 3811 ? 184.748 258.287 170.950 1.00 2.46  ? 3811 ILE A O     1 
ATOM   17161 C  CB    . ILE A 1 3811 ? 182.708 258.739 168.318 1.00 0.73  ? 3811 ILE A CB    1 
ATOM   17162 C  CG1   . ILE A 1 3811 ? 181.967 259.939 167.727 1.00 0.52  ? 3811 ILE A CG1   1 
ATOM   17163 C  CG2   . ILE A 1 3811 ? 181.906 258.127 169.459 1.00 0.49  ? 3811 ILE A CG2   1 
ATOM   17164 C  CD1   . ILE A 1 3811 ? 180.637 259.590 167.114 1.00 0.59  ? 3811 ILE A CD1   1 
ATOM   17165 N  N     . TYR A 1 3812 ? 185.213 257.008 169.158 1.00 0.88  ? 3812 TYR A N     1 
ATOM   17166 C  CA    . TYR A 1 3812 ? 185.778 255.953 169.994 1.00 0.61  ? 3812 TYR A CA    1 
ATOM   17167 C  C     . TYR A 1 3812 ? 187.023 256.432 170.725 1.00 0.52  ? 3812 TYR A C     1 
ATOM   17168 O  O     . TYR A 1 3812 ? 187.192 256.157 171.919 1.00 0.79  ? 3812 TYR A O     1 
ATOM   17169 C  CB    . TYR A 1 3812 ? 186.105 254.717 169.158 1.00 0.88  ? 3812 TYR A CB    1 
ATOM   17170 C  CG    . TYR A 1 3812 ? 186.917 253.701 169.929 1.00 1.08  ? 3812 TYR A CG    1 
ATOM   17171 C  CD1   . TYR A 1 3812 ? 186.318 252.903 170.893 1.00 0.68  ? 3812 TYR A CD1   1 
ATOM   17172 C  CD2   . TYR A 1 3812 ? 188.284 253.558 169.718 1.00 0.57  ? 3812 TYR A CD2   1 
ATOM   17173 C  CE1   . TYR A 1 3812 ? 187.049 251.986 171.613 1.00 1.04  ? 3812 TYR A CE1   1 
ATOM   17174 C  CE2   . TYR A 1 3812 ? 189.023 252.640 170.434 1.00 0.55  ? 3812 TYR A CE2   1 
ATOM   17175 C  CZ    . TYR A 1 3812 ? 188.400 251.854 171.379 1.00 1.26  ? 3812 TYR A CZ    1 
ATOM   17176 O  OH    . TYR A 1 3812 ? 189.122 250.932 172.100 1.00 2.03  ? 3812 TYR A OH    1 
ATOM   17177 N  N     . PHE A 1 3813 ? 187.908 257.142 170.027 1.00 0.93  ? 3813 PHE A N     1 
ATOM   17178 C  CA    . PHE A 1 3813 ? 189.122 257.632 170.667 1.00 0.88  ? 3813 PHE A CA    1 
ATOM   17179 C  C     . PHE A 1 3813 ? 188.829 258.729 171.681 1.00 1.14  ? 3813 PHE A C     1 
ATOM   17180 O  O     . PHE A 1 3813 ? 189.630 258.935 172.597 1.00 1.31  ? 3813 PHE A O     1 
ATOM   17181 C  CB    . PHE A 1 3813 ? 190.114 258.106 169.605 1.00 1.36  ? 3813 PHE A CB    1 
ATOM   17182 C  CG    . PHE A 1 3813 ? 190.976 257.001 169.063 1.00 1.98  ? 3813 PHE A CG    1 
ATOM   17183 C  CD1   . PHE A 1 3813 ? 190.552 256.237 167.990 1.00 2.70  ? 3813 PHE A CD1   1 
ATOM   17184 C  CD2   . PHE A 1 3813 ? 192.196 256.708 169.644 1.00 3.78  ? 3813 PHE A CD2   1 
ATOM   17185 C  CE1   . PHE A 1 3813 ? 191.333 255.208 167.499 1.00 1.67  ? 3813 PHE A CE1   1 
ATOM   17186 C  CE2   . PHE A 1 3813 ? 192.985 255.682 169.156 1.00 4.50  ? 3813 PHE A CE2   1 
ATOM   17187 C  CZ    . PHE A 1 3813 ? 192.551 254.931 168.081 1.00 2.53  ? 3813 PHE A CZ    1 
ATOM   17188 N  N     . THR A 1 3814 ? 187.705 259.435 171.536 1.00 1.38  ? 3814 THR A N     1 
ATOM   17189 C  CA    . THR A 1 3814 ? 187.236 260.299 172.613 1.00 1.03  ? 3814 THR A CA    1 
ATOM   17190 C  C     . THR A 1 3814 ? 186.760 259.474 173.804 1.00 0.89  ? 3814 THR A C     1 
ATOM   17191 O  O     . THR A 1 3814 ? 187.077 259.796 174.955 1.00 0.94  ? 3814 THR A O     1 
ATOM   17192 C  CB    . THR A 1 3814 ? 186.119 261.212 172.104 1.00 1.25  ? 3814 THR A CB    1 
ATOM   17193 O  OG1   . THR A 1 3814 ? 186.647 262.108 171.118 1.00 3.89  ? 3814 THR A OG1   1 
ATOM   17194 C  CG2   . THR A 1 3814 ? 185.524 262.022 173.243 1.00 1.25  ? 3814 THR A CG2   1 
ATOM   17195 N  N     . MET A 1 3815 ? 186.015 258.397 173.542 1.00 0.79  ? 3815 MET A N     1 
ATOM   17196 C  CA    . MET A 1 3815 ? 185.595 257.495 174.611 1.00 0.74  ? 3815 MET A CA    1 
ATOM   17197 C  C     . MET A 1 3815 ? 186.794 256.864 175.304 1.00 0.97  ? 3815 MET A C     1 
ATOM   17198 O  O     . MET A 1 3815 ? 186.814 256.733 176.532 1.00 2.09  ? 3815 MET A O     1 
ATOM   17199 C  CB    . MET A 1 3815 ? 184.683 256.407 174.047 1.00 0.62  ? 3815 MET A CB    1 
ATOM   17200 C  CG    . MET A 1 3815 ? 183.369 256.895 173.474 1.00 0.47  ? 3815 MET A CG    1 
ATOM   17201 S  SD    . MET A 1 3815 ? 182.465 255.568 172.652 1.00 12.79 ? 3815 MET A SD    1 
ATOM   17202 C  CE    . MET A 1 3815 ? 182.281 254.393 173.987 1.00 0.52  ? 3815 MET A CE    1 
ATOM   17203 N  N     . GLU A 1 3816 ? 187.801 256.462 174.527 1.00 1.75  ? 3816 GLU A N     1 
ATOM   17204 C  CA    . GLU A 1 3816 ? 188.982 255.825 175.095 1.00 1.81  ? 3816 GLU A CA    1 
ATOM   17205 C  C     . GLU A 1 3816 ? 189.739 256.768 176.021 1.00 1.76  ? 3816 GLU A C     1 
ATOM   17206 O  O     . GLU A 1 3816 ? 190.383 256.319 176.975 1.00 4.28  ? 3816 GLU A O     1 
ATOM   17207 C  CB    . GLU A 1 3816 ? 189.889 255.329 173.966 1.00 2.07  ? 3816 GLU A CB    1 
ATOM   17208 C  CG    . GLU A 1 3816 ? 191.143 254.599 174.419 1.00 6.35  ? 3816 GLU A CG    1 
ATOM   17209 C  CD    . GLU A 1 3816 ? 190.837 253.295 175.134 1.00 22.30 ? 3816 GLU A CD    1 
ATOM   17210 O  OE1   . GLU A 1 3816 ? 189.764 252.709 174.873 1.00 22.74 ? 3816 GLU A OE1   1 
ATOM   17211 O  OE2   . GLU A 1 3816 ? 191.674 252.854 175.950 1.00 18.20 ? 3816 GLU A OE2   1 
ATOM   17212 N  N     . SER A 1 3817 ? 189.667 258.073 175.766 1.00 1.77  ? 3817 SER A N     1 
ATOM   17213 C  CA    . SER A 1 3817 ? 190.356 259.062 176.582 1.00 2.05  ? 3817 SER A CA    1 
ATOM   17214 C  C     . SER A 1 3817 ? 189.561 259.483 177.811 1.00 2.18  ? 3817 SER A C     1 
ATOM   17215 O  O     . SER A 1 3817 ? 190.094 260.210 178.653 1.00 3.50  ? 3817 SER A O     1 
ATOM   17216 C  CB    . SER A 1 3817 ? 190.685 260.298 175.740 1.00 2.03  ? 3817 SER A CB    1 
ATOM   17217 O  OG    . SER A 1 3817 ? 189.560 260.710 174.984 1.00 12.12 ? 3817 SER A OG    1 
ATOM   17218 N  N     . LEU A 1 3818 ? 188.307 259.040 177.940 1.00 2.15  ? 3818 LEU A N     1 
ATOM   17219 C  CA    . LEU A 1 3818 ? 187.502 259.411 179.098 1.00 1.16  ? 3818 LEU A CA    1 
ATOM   17220 C  C     . LEU A 1 3818 ? 188.035 258.808 180.392 1.00 1.61  ? 3818 LEU A C     1 
ATOM   17221 O  O     . LEU A 1 3818 ? 187.677 259.285 181.473 1.00 1.99  ? 3818 LEU A O     1 
ATOM   17222 C  CB    . LEU A 1 3818 ? 186.048 258.995 178.883 1.00 1.11  ? 3818 LEU A CB    1 
ATOM   17223 C  CG    . LEU A 1 3818 ? 185.213 259.956 178.033 1.00 0.60  ? 3818 LEU A CG    1 
ATOM   17224 C  CD1   . LEU A 1 3818 ? 183.923 259.299 177.578 1.00 0.33  ? 3818 LEU A CD1   1 
ATOM   17225 C  CD2   . LEU A 1 3818 ? 184.926 261.240 178.793 1.00 0.71  ? 3818 LEU A CD2   1 
ATOM   17226 N  N     . LYS A 1 3819 ? 188.881 257.780 180.308 1.00 2.20  ? 3819 LYS A N     1 
ATOM   17227 C  CA    . LYS A 1 3819 ? 189.517 257.233 181.500 1.00 1.51  ? 3819 LYS A CA    1 
ATOM   17228 C  C     . LYS A 1 3819 ? 190.476 258.224 182.148 1.00 2.46  ? 3819 LYS A C     1 
ATOM   17229 O  O     . LYS A 1 3819 ? 190.832 258.044 183.317 1.00 3.03  ? 3819 LYS A O     1 
ATOM   17230 C  CB    . LYS A 1 3819 ? 190.265 255.945 181.154 1.00 1.35  ? 3819 LYS A CB    1 
ATOM   17231 C  CG    . LYS A 1 3819 ? 191.530 256.168 180.343 1.00 1.30  ? 3819 LYS A CG    1 
ATOM   17232 C  CD    . LYS A 1 3819 ? 192.424 254.944 180.338 1.00 1.31  ? 3819 LYS A CD    1 
ATOM   17233 C  CE    . LYS A 1 3819 ? 191.846 253.832 179.484 1.00 3.02  ? 3819 LYS A CE    1 
ATOM   17234 N  NZ    . LYS A 1 3819 ? 191.849 254.185 178.044 1.00 3.49  ? 3819 LYS A NZ    1 
ATOM   17235 N  N     . GLN A 1 3820 ? 190.898 259.261 181.421 1.00 3.34  ? 3820 GLN A N     1 
ATOM   17236 C  CA    . GLN A 1 3820 ? 191.808 260.249 181.986 1.00 3.30  ? 3820 GLN A CA    1 
ATOM   17237 C  C     . GLN A 1 3820 ? 191.130 261.156 183.003 1.00 3.32  ? 3820 GLN A C     1 
ATOM   17238 O  O     . GLN A 1 3820 ? 191.810 261.695 183.880 1.00 11.08 ? 3820 GLN A O     1 
ATOM   17239 C  CB    . GLN A 1 3820 ? 192.429 261.099 180.875 1.00 4.11  ? 3820 GLN A CB    1 
ATOM   17240 C  CG    . GLN A 1 3820 ? 193.179 260.313 179.813 1.00 2.66  ? 3820 GLN A CG    1 
ATOM   17241 C  CD    . GLN A 1 3820 ? 194.242 259.403 180.394 1.00 9.73  ? 3820 GLN A CD    1 
ATOM   17242 O  OE1   . GLN A 1 3820 ? 194.273 258.206 180.110 1.00 12.82 ? 3820 GLN A OE1   1 
ATOM   17243 N  NE2   . GLN A 1 3820 ? 195.119 259.967 181.215 1.00 13.57 ? 3820 GLN A NE2   1 
ATOM   17244 N  N     . ILE A 1 3821 ? 189.813 261.340 182.908 1.00 2.47  ? 3821 ILE A N     1 
ATOM   17245 C  CA    . ILE A 1 3821 ? 189.111 262.242 183.814 1.00 2.55  ? 3821 ILE A CA    1 
ATOM   17246 C  C     . ILE A 1 3821 ? 188.411 261.514 184.960 1.00 2.83  ? 3821 ILE A C     1 
ATOM   17247 O  O     . ILE A 1 3821 ? 188.088 262.153 185.971 1.00 3.71  ? 3821 ILE A O     1 
ATOM   17248 C  CB    . ILE A 1 3821 ? 188.099 263.118 183.046 1.00 2.03  ? 3821 ILE A CB    1 
ATOM   17249 C  CG1   . ILE A 1 3821 ? 186.931 262.276 182.535 1.00 2.84  ? 3821 ILE A CG1   1 
ATOM   17250 C  CG2   . ILE A 1 3821 ? 188.787 263.832 181.896 1.00 2.04  ? 3821 ILE A CG2   1 
ATOM   17251 C  CD1   . ILE A 1 3821 ? 185.795 263.093 181.973 1.00 1.69  ? 3821 ILE A CD1   1 
ATOM   17252 N  N     . HIS A 1 3822 ? 188.170 260.211 184.835 1.00 2.74  ? 3822 HIS A N     1 
ATOM   17253 C  CA    . HIS A 1 3822 ? 187.596 259.433 185.923 1.00 1.17  ? 3822 HIS A CA    1 
ATOM   17254 C  C     . HIS A 1 3822 ? 187.964 257.971 185.724 1.00 1.25  ? 3822 HIS A C     1 
ATOM   17255 O  O     . HIS A 1 3822 ? 187.888 257.456 184.606 1.00 3.99  ? 3822 HIS A O     1 
ATOM   17256 C  CB    . HIS A 1 3822 ? 186.074 259.595 185.992 1.00 1.26  ? 3822 HIS A CB    1 
ATOM   17257 C  CG    . HIS A 1 3822 ? 185.504 259.344 187.352 1.00 1.11  ? 3822 HIS A CG    1 
ATOM   17258 N  ND1   . HIS A 1 3822 ? 185.393 258.080 187.889 1.00 1.79  ? 3822 HIS A ND1   1 
ATOM   17259 C  CD2   . HIS A 1 3822 ? 185.016 260.194 188.285 1.00 1.17  ? 3822 HIS A CD2   1 
ATOM   17260 C  CE1   . HIS A 1 3822 ? 184.861 258.163 189.095 1.00 1.75  ? 3822 HIS A CE1   1 
ATOM   17261 N  NE2   . HIS A 1 3822 ? 184.622 259.434 189.358 1.00 4.69  ? 3822 HIS A NE2   1 
ATOM   17262 N  N     . PHE A 1 3823 ? 188.355 257.310 186.815 1.00 1.60  ? 3823 PHE A N     1 
ATOM   17263 C  CA    . PHE A 1 3823 ? 188.745 255.906 186.740 1.00 1.62  ? 3823 PHE A CA    1 
ATOM   17264 C  C     . PHE A 1 3823 ? 187.591 255.002 186.331 1.00 1.23  ? 3823 PHE A C     1 
ATOM   17265 O  O     . PHE A 1 3823 ? 187.831 253.902 185.825 1.00 3.13  ? 3823 PHE A O     1 
ATOM   17266 C  CB    . PHE A 1 3823 ? 189.324 255.444 188.080 1.00 1.43  ? 3823 PHE A CB    1 
ATOM   17267 C  CG    . PHE A 1 3823 ? 188.355 255.531 189.231 1.00 2.05  ? 3823 PHE A CG    1 
ATOM   17268 C  CD1   . PHE A 1 3823 ? 187.464 254.503 189.488 1.00 1.77  ? 3823 PHE A CD1   1 
ATOM   17269 C  CD2   . PHE A 1 3823 ? 188.342 256.639 190.058 1.00 2.23  ? 3823 PHE A CD2   1 
ATOM   17270 C  CE1   . PHE A 1 3823 ? 186.575 254.585 190.536 1.00 0.92  ? 3823 PHE A CE1   1 
ATOM   17271 C  CE2   . PHE A 1 3823 ? 187.458 256.722 191.113 1.00 1.25  ? 3823 PHE A CE2   1 
ATOM   17272 C  CZ    . PHE A 1 3823 ? 186.574 255.695 191.353 1.00 0.99  ? 3823 PHE A CZ    1 
ATOM   17273 N  N     . LEU A 1 3824 ? 186.349 255.436 186.538 1.00 0.83  ? 3824 LEU A N     1 
ATOM   17274 C  CA    . LEU A 1 3824 ? 185.193 254.615 186.210 1.00 0.89  ? 3824 LEU A CA    1 
ATOM   17275 C  C     . LEU A 1 3824 ? 184.903 254.565 184.716 1.00 0.54  ? 3824 LEU A C     1 
ATOM   17276 O  O     . LEU A 1 3824 ? 184.228 253.637 184.261 1.00 0.39  ? 3824 LEU A O     1 
ATOM   17277 C  CB    . LEU A 1 3824 ? 183.963 255.131 186.959 1.00 0.91  ? 3824 LEU A CB    1 
ATOM   17278 C  CG    . LEU A 1 3824 ? 182.720 254.240 186.993 1.00 0.42  ? 3824 LEU A CG    1 
ATOM   17279 C  CD1   . LEU A 1 3824 ? 182.981 252.986 187.809 1.00 0.98  ? 3824 LEU A CD1   1 
ATOM   17280 C  CD2   . LEU A 1 3824 ? 181.529 255.000 187.539 1.00 0.27  ? 3824 LEU A CD2   1 
ATOM   17281 N  N     . TYR A 1 3825 ? 185.407 255.523 183.939 1.00 1.38  ? 3825 TYR A N     1 
ATOM   17282 C  CA    . TYR A 1 3825 ? 185.043 255.638 182.525 1.00 0.83  ? 3825 TYR A CA    1 
ATOM   17283 C  C     . TYR A 1 3825 ? 185.940 254.717 181.703 1.00 0.57  ? 3825 TYR A C     1 
ATOM   17284 O  O     . TYR A 1 3825 ? 186.869 255.143 181.013 1.00 1.52  ? 3825 TYR A O     1 
ATOM   17285 C  CB    . TYR A 1 3825 ? 185.142 257.084 182.054 1.00 0.63  ? 3825 TYR A CB    1 
ATOM   17286 C  CG    . TYR A 1 3825 ? 184.321 258.074 182.856 1.00 0.94  ? 3825 TYR A CG    1 
ATOM   17287 C  CD1   . TYR A 1 3825 ? 183.307 257.650 183.706 1.00 0.91  ? 3825 TYR A CD1   1 
ATOM   17288 C  CD2   . TYR A 1 3825 ? 184.556 259.438 182.750 1.00 1.01  ? 3825 TYR A CD2   1 
ATOM   17289 C  CE1   . TYR A 1 3825 ? 182.566 258.552 184.436 1.00 0.66  ? 3825 TYR A CE1   1 
ATOM   17290 C  CE2   . TYR A 1 3825 ? 183.815 260.346 183.472 1.00 0.71  ? 3825 TYR A CE2   1 
ATOM   17291 C  CZ    . TYR A 1 3825 ? 182.821 259.899 184.314 1.00 0.54  ? 3825 TYR A CZ    1 
ATOM   17292 O  OH    . TYR A 1 3825 ? 182.082 260.805 185.034 1.00 0.86  ? 3825 TYR A OH    1 
ATOM   17293 N  N     . GLN A 1 3826 ? 185.644 253.424 181.779 1.00 0.72  ? 3826 GLN A N     1 
ATOM   17294 C  CA    . GLN A 1 3826 ? 186.347 252.398 181.021 1.00 0.39  ? 3826 GLN A CA    1 
ATOM   17295 C  C     . GLN A 1 3826 ? 185.415 251.881 179.937 1.00 0.58  ? 3826 GLN A C     1 
ATOM   17296 O  O     . GLN A 1 3826 ? 184.304 251.430 180.235 1.00 0.95  ? 3826 GLN A O     1 
ATOM   17297 C  CB    . GLN A 1 3826 ? 186.800 251.253 181.926 1.00 0.64  ? 3826 GLN A CB    1 
ATOM   17298 C  CG    . GLN A 1 3826 ? 187.593 251.676 183.151 1.00 0.61  ? 3826 GLN A CG    1 
ATOM   17299 C  CD    . GLN A 1 3826 ? 188.777 252.557 182.822 1.00 0.90  ? 3826 GLN A CD    1 
ATOM   17300 O  OE1   . GLN A 1 3826 ? 189.664 252.170 182.064 1.00 1.77  ? 3826 GLN A OE1   1 
ATOM   17301 N  NE2   . GLN A 1 3826 ? 188.807 253.744 183.410 1.00 0.99  ? 3826 GLN A NE2   1 
ATOM   17302 N  N     . TYR A 1 3827 ? 185.860 251.943 178.686 1.00 0.92  ? 3827 TYR A N     1 
ATOM   17303 C  CA    . TYR A 1 3827 ? 185.037 251.550 177.551 1.00 1.31  ? 3827 TYR A CA    1 
ATOM   17304 C  C     . TYR A 1 3827 ? 185.863 250.731 176.575 1.00 1.88  ? 3827 TYR A C     1 
ATOM   17305 O  O     . TYR A 1 3827 ? 186.910 251.186 176.105 1.00 5.72  ? 3827 TYR A O     1 
ATOM   17306 C  CB    . TYR A 1 3827 ? 184.444 252.777 176.857 1.00 0.89  ? 3827 TYR A CB    1 
ATOM   17307 C  CG    . TYR A 1 3827 ? 183.651 253.640 177.802 1.00 0.88  ? 3827 TYR A CG    1 
ATOM   17308 C  CD1   . TYR A 1 3827 ? 182.455 253.187 178.341 1.00 0.70  ? 3827 TYR A CD1   1 
ATOM   17309 C  CD2   . TYR A 1 3827 ? 184.111 254.889 178.185 1.00 0.78  ? 3827 TYR A CD2   1 
ATOM   17310 C  CE1   . TYR A 1 3827 ? 181.734 253.963 179.216 1.00 1.61  ? 3827 TYR A CE1   1 
ATOM   17311 C  CE2   . TYR A 1 3827 ? 183.394 255.672 179.060 1.00 0.66  ? 3827 TYR A CE2   1 
ATOM   17312 C  CZ    . TYR A 1 3827 ? 182.208 255.206 179.574 1.00 0.74  ? 3827 TYR A CZ    1 
ATOM   17313 O  OH    . TYR A 1 3827 ? 181.487 255.985 180.448 1.00 1.42  ? 3827 TYR A OH    1 
ATOM   17314 N  N     . SER A 1 3828 ? 185.386 249.530 176.272 1.00 2.13  ? 3828 SER A N     1 
ATOM   17315 C  CA    . SER A 1 3828 ? 186.049 248.669 175.312 1.00 1.16  ? 3828 SER A CA    1 
ATOM   17316 C  C     . SER A 1 3828 ? 185.665 249.068 173.890 1.00 1.57  ? 3828 SER A C     1 
ATOM   17317 O  O     . SER A 1 3828 ? 184.763 249.879 173.661 1.00 2.72  ? 3828 SER A O     1 
ATOM   17318 C  CB    . SER A 1 3828 ? 185.694 247.208 175.572 1.00 1.18  ? 3828 SER A CB    1 
ATOM   17319 O  OG    . SER A 1 3828 ? 184.328 246.960 175.294 1.00 1.22  ? 3828 SER A OG    1 
ATOM   17320 N  N     . LEU A 1 3829 ? 186.374 248.491 172.921 1.00 1.78  ? 3829 LEU A N     1 
ATOM   17321 C  CA    . LEU A 1 3829 ? 186.008 248.700 171.527 1.00 0.96  ? 3829 LEU A CA    1 
ATOM   17322 C  C     . LEU A 1 3829 ? 184.672 248.050 171.201 1.00 0.86  ? 3829 LEU A C     1 
ATOM   17323 O  O     . LEU A 1 3829 ? 183.908 248.581 170.387 1.00 1.43  ? 3829 LEU A O     1 
ATOM   17324 C  CB    . LEU A 1 3829 ? 187.105 248.169 170.605 1.00 1.54  ? 3829 LEU A CB    1 
ATOM   17325 C  CG    . LEU A 1 3829 ? 186.819 248.241 169.105 1.00 2.21  ? 3829 LEU A CG    1 
ATOM   17326 C  CD1   . LEU A 1 3829 ? 186.589 249.678 168.670 1.00 0.70  ? 3829 LEU A CD1   1 
ATOM   17327 C  CD2   . LEU A 1 3829 ? 187.943 247.608 168.313 1.00 3.18  ? 3829 LEU A CD2   1 
ATOM   17328 N  N     . GLN A 1 3830 ? 184.367 246.916 171.832 1.00 1.12  ? 3830 GLN A N     1 
ATOM   17329 C  CA    . GLN A 1 3830 ? 183.099 246.245 171.573 1.00 2.07  ? 3830 GLN A CA    1 
ATOM   17330 C  C     . GLN A 1 3830 ? 181.920 247.110 171.999 1.00 2.13  ? 3830 GLN A C     1 
ATOM   17331 O  O     . GLN A 1 3830 ? 180.854 247.066 171.375 1.00 2.81  ? 3830 GLN A O     1 
ATOM   17332 C  CB    . GLN A 1 3830 ? 183.060 244.895 172.289 1.00 1.81  ? 3830 GLN A CB    1 
ATOM   17333 C  CG    . GLN A 1 3830 ? 181.945 243.983 171.812 1.00 4.18  ? 3830 GLN A CG    1 
ATOM   17334 C  CD    . GLN A 1 3830 ? 181.865 243.913 170.300 1.00 9.31  ? 3830 GLN A CD    1 
ATOM   17335 O  OE1   . GLN A 1 3830 ? 182.821 243.516 169.634 1.00 10.17 ? 3830 GLN A OE1   1 
ATOM   17336 N  NE2   . GLN A 1 3830 ? 180.722 244.305 169.747 1.00 8.45  ? 3830 GLN A NE2   1 
ATOM   17337 N  N     . PHE A 1 3831 ? 182.092 247.901 173.060 1.00 1.60  ? 3831 PHE A N     1 
ATOM   17338 C  CA    . PHE A 1 3831 ? 181.021 248.782 173.514 1.00 1.29  ? 3831 PHE A CA    1 
ATOM   17339 C  C     . PHE A 1 3831 ? 180.681 249.820 172.450 1.00 1.43  ? 3831 PHE A C     1 
ATOM   17340 O  O     . PHE A 1 3831 ? 179.503 250.099 172.193 1.00 1.82  ? 3831 PHE A O     1 
ATOM   17341 C  CB    . PHE A 1 3831 ? 181.418 249.454 174.829 1.00 1.67  ? 3831 PHE A CB    1 
ATOM   17342 C  CG    . PHE A 1 3831 ? 180.377 250.390 175.373 1.00 1.63  ? 3831 PHE A CG    1 
ATOM   17343 C  CD1   . PHE A 1 3831 ? 180.654 251.732 175.543 1.00 1.77  ? 3831 PHE A CD1   1 
ATOM   17344 C  CD2   . PHE A 1 3831 ? 179.119 249.924 175.714 1.00 4.28  ? 3831 PHE A CD2   1 
ATOM   17345 C  CE1   . PHE A 1 3831 ? 179.698 252.595 176.046 1.00 3.14  ? 3831 PHE A CE1   1 
ATOM   17346 C  CE2   . PHE A 1 3831 ? 178.159 250.785 176.215 1.00 6.27  ? 3831 PHE A CE2   1 
ATOM   17347 C  CZ    . PHE A 1 3831 ? 178.451 252.121 176.381 1.00 1.47  ? 3831 PHE A CZ    1 
ATOM   17348 N  N     . PHE A 1 3832 ? 181.702 250.400 171.815 1.00 0.99  ? 3832 PHE A N     1 
ATOM   17349 C  CA    . PHE A 1 3832 ? 181.446 251.328 170.720 1.00 0.99  ? 3832 PHE A CA    1 
ATOM   17350 C  C     . PHE A 1 3832 ? 180.887 250.607 169.498 1.00 1.50  ? 3832 PHE A C     1 
ATOM   17351 O  O     . PHE A 1 3832 ? 180.019 251.140 168.802 1.00 1.89  ? 3832 PHE A O     1 
ATOM   17352 C  CB    . PHE A 1 3832 ? 182.717 252.095 170.352 1.00 0.77  ? 3832 PHE A CB    1 
ATOM   17353 C  CG    . PHE A 1 3832 ? 182.601 252.862 169.066 1.00 1.20  ? 3832 PHE A CG    1 
ATOM   17354 C  CD1   . PHE A 1 3832 ? 182.036 254.127 169.052 1.00 1.11  ? 3832 PHE A CD1   1 
ATOM   17355 C  CD2   . PHE A 1 3832 ? 183.052 252.321 167.873 1.00 0.65  ? 3832 PHE A CD2   1 
ATOM   17356 C  CE1   . PHE A 1 3832 ? 181.916 254.829 167.873 1.00 1.23  ? 3832 PHE A CE1   1 
ATOM   17357 C  CE2   . PHE A 1 3832 ? 182.934 253.019 166.692 1.00 0.47  ? 3832 PHE A CE2   1 
ATOM   17358 C  CZ    . PHE A 1 3832 ? 182.366 254.276 166.692 1.00 1.36  ? 3832 PHE A CZ    1 
ATOM   17359 N  N     . LEU A 1 3833 ? 181.385 249.402 169.213 1.00 1.93  ? 3833 LEU A N     1 
ATOM   17360 C  CA    . LEU A 1 3833 ? 180.868 248.646 168.077 1.00 1.75  ? 3833 LEU A CA    1 
ATOM   17361 C  C     . LEU A 1 3833 ? 179.415 248.248 168.287 1.00 2.35  ? 3833 LEU A C     1 
ATOM   17362 O  O     . LEU A 1 3833 ? 178.653 248.160 167.316 1.00 4.68  ? 3833 LEU A O     1 
ATOM   17363 C  CB    . LEU A 1 3833 ? 181.735 247.414 167.829 1.00 2.71  ? 3833 LEU A CB    1 
ATOM   17364 C  CG    . LEU A 1 3833 ? 183.157 247.693 167.343 1.00 1.53  ? 3833 LEU A CG    1 
ATOM   17365 C  CD1   . LEU A 1 3833 ? 183.945 246.402 167.216 1.00 2.77  ? 3833 LEU A CD1   1 
ATOM   17366 C  CD2   . LEU A 1 3833 ? 183.139 248.446 166.024 1.00 2.61  ? 3833 LEU A CD2   1 
ATOM   17367 N  N     . ASP A 1 3834 ? 179.015 247.999 169.533 1.00 2.07  ? 3834 ASP A N     1 
ATOM   17368 C  CA    . ASP A 1 3834 ? 177.604 247.776 169.826 1.00 2.60  ? 3834 ASP A CA    1 
ATOM   17369 C  C     . ASP A 1 3834 ? 176.786 249.033 169.555 1.00 4.70  ? 3834 ASP A C     1 
ATOM   17370 O  O     . ASP A 1 3834 ? 175.655 248.953 169.061 1.00 4.13  ? 3834 ASP A O     1 
ATOM   17371 C  CB    . ASP A 1 3834 ? 177.437 247.326 171.278 1.00 3.74  ? 3834 ASP A CB    1 
ATOM   17372 C  CG    . ASP A 1 3834 ? 178.072 245.978 171.547 1.00 6.92  ? 3834 ASP A CG    1 
ATOM   17373 O  OD1   . ASP A 1 3834 ? 178.499 245.309 170.583 1.00 11.38 ? 3834 ASP A OD1   1 
ATOM   17374 O  OD2   . ASP A 1 3834 ? 178.157 245.592 172.731 1.00 8.68  ? 3834 ASP A OD2   1 
ATOM   17375 N  N     . ILE A 1 3835 ? 177.337 250.202 169.887 1.00 2.64  ? 3835 ILE A N     1 
ATOM   17376 C  CA    . ILE A 1 3835 ? 176.671 251.466 169.579 1.00 1.44  ? 3835 ILE A CA    1 
ATOM   17377 C  C     . ILE A 1 3835 ? 176.549 251.642 168.071 1.00 3.29  ? 3835 ILE A C     1 
ATOM   17378 O  O     . ILE A 1 3835 ? 175.489 252.009 167.551 1.00 2.87  ? 3835 ILE A O     1 
ATOM   17379 C  CB    . ILE A 1 3835 ? 177.435 252.637 170.221 1.00 2.32  ? 3835 ILE A CB    1 
ATOM   17380 C  CG1   . ILE A 1 3835 ? 177.229 252.653 171.736 1.00 2.08  ? 3835 ILE A CG1   1 
ATOM   17381 C  CG2   . ILE A 1 3835 ? 177.028 253.966 169.594 1.00 1.15  ? 3835 ILE A CG2   1 
ATOM   17382 C  CD1   . ILE A 1 3835 ? 178.178 253.577 172.465 1.00 0.90  ? 3835 ILE A CD1   1 
ATOM   17383 N  N     . TYR A 1 3836 ? 177.640 251.374 167.350 1.00 5.54  ? 3836 TYR A N     1 
ATOM   17384 C  CA    . TYR A 1 3836 ? 177.639 251.521 165.899 1.00 2.06  ? 3836 TYR A CA    1 
ATOM   17385 C  C     . TYR A 1 3836 ? 176.667 250.550 165.245 1.00 2.72  ? 3836 TYR A C     1 
ATOM   17386 O  O     . TYR A 1 3836 ? 175.958 250.912 164.299 1.00 3.21  ? 3836 TYR A O     1 
ATOM   17387 C  CB    . TYR A 1 3836 ? 179.057 251.313 165.371 1.00 2.81  ? 3836 TYR A CB    1 
ATOM   17388 C  CG    . TYR A 1 3836 ? 179.263 251.739 163.941 1.00 3.26  ? 3836 TYR A CG    1 
ATOM   17389 C  CD1   . TYR A 1 3836 ? 178.608 252.847 163.422 1.00 3.39  ? 3836 TYR A CD1   1 
ATOM   17390 C  CD2   . TYR A 1 3836 ? 180.119 251.033 163.110 1.00 1.75  ? 3836 TYR A CD2   1 
ATOM   17391 C  CE1   . TYR A 1 3836 ? 178.798 253.233 162.112 1.00 3.19  ? 3836 TYR A CE1   1 
ATOM   17392 C  CE2   . TYR A 1 3836 ? 180.315 251.412 161.806 1.00 2.14  ? 3836 TYR A CE2   1 
ATOM   17393 C  CZ    . TYR A 1 3836 ? 179.656 252.511 161.310 1.00 3.15  ? 3836 TYR A CZ    1 
ATOM   17394 O  OH    . TYR A 1 3836 ? 179.858 252.887 160.008 1.00 2.98  ? 3836 TYR A OH    1 
ATOM   17395 N  N     . HIS A 1 3837 ? 176.619 249.312 165.738 1.00 2.90  ? 3837 HIS A N     1 
ATOM   17396 C  CA    . HIS A 1 3837 ? 175.664 248.339 165.222 1.00 3.68  ? 3837 HIS A CA    1 
ATOM   17397 C  C     . HIS A 1 3837 ? 174.231 248.785 165.478 1.00 5.91  ? 3837 HIS A C     1 
ATOM   17398 O  O     . HIS A 1 3837 ? 173.351 248.591 164.632 1.00 7.29  ? 3837 HIS A O     1 
ATOM   17399 C  CB    . HIS A 1 3837 ? 175.926 246.972 165.856 1.00 5.26  ? 3837 HIS A CB    1 
ATOM   17400 C  CG    . HIS A 1 3837 ? 174.969 245.907 165.425 1.00 10.20 ? 3837 HIS A CG    1 
ATOM   17401 N  ND1   . HIS A 1 3837 ? 175.244 245.033 164.397 1.00 14.46 ? 3837 HIS A ND1   1 
ATOM   17402 C  CD2   . HIS A 1 3837 ? 173.741 245.572 165.886 1.00 8.37  ? 3837 HIS A CD2   1 
ATOM   17403 C  CE1   . HIS A 1 3837 ? 174.226 244.205 164.242 1.00 11.69 ? 3837 HIS A CE1   1 
ATOM   17404 N  NE2   . HIS A 1 3837 ? 173.301 244.512 165.133 1.00 13.25 ? 3837 HIS A NE2   1 
ATOM   17405 N  N     . ASN A 1 3838 ? 173.979 249.381 166.646 1.00 4.53  ? 3838 ASN A N     1 
ATOM   17406 C  CA    . ASN A 1 3838 ? 172.636 249.845 166.978 1.00 4.50  ? 3838 ASN A CA    1 
ATOM   17407 C  C     . ASN A 1 3838 ? 172.169 250.932 166.016 1.00 5.36  ? 3838 ASN A C     1 
ATOM   17408 O  O     . ASN A 1 3838 ? 171.015 250.926 165.574 1.00 6.99  ? 3838 ASN A O     1 
ATOM   17409 C  CB    . ASN A 1 3838 ? 172.611 250.353 168.419 1.00 5.64  ? 3838 ASN A CB    1 
ATOM   17410 C  CG    . ASN A 1 3838 ? 171.236 250.799 168.856 1.00 6.03  ? 3838 ASN A CG    1 
ATOM   17411 O  OD1   . ASN A 1 3838 ? 171.010 251.975 169.133 1.00 4.98  ? 3838 ASN A OD1   1 
ATOM   17412 N  ND2   . ASN A 1 3838 ? 170.305 249.858 168.926 1.00 7.90  ? 3838 ASN A ND2   1 
ATOM   17413 N  N     . VAL A 1 3839 ? 173.052 251.876 165.686 1.00 3.78  ? 3839 VAL A N     1 
ATOM   17414 C  CA    . VAL A 1 3839 ? 172.694 252.958 164.776 1.00 4.05  ? 3839 VAL A CA    1 
ATOM   17415 C  C     . VAL A 1 3839 ? 172.452 252.432 163.366 1.00 5.15  ? 3839 VAL A C     1 
ATOM   17416 O  O     . VAL A 1 3839 ? 171.601 252.956 162.637 1.00 10.33 ? 3839 VAL A O     1 
ATOM   17417 C  CB    . VAL A 1 3839 ? 173.785 254.046 164.804 1.00 3.52  ? 3839 VAL A CB    1 
ATOM   17418 C  CG1   . VAL A 1 3839 ? 173.497 255.132 163.786 1.00 6.41  ? 3839 VAL A CG1   1 
ATOM   17419 C  CG2   . VAL A 1 3839 ? 173.888 254.643 166.193 1.00 5.19  ? 3839 VAL A CG2   1 
ATOM   17420 N  N     . LEU A 1 3840 ? 173.185 251.402 162.953 1.00 4.62  ? 3840 LEU A N     1 
ATOM   17421 C  CA    . LEU A 1 3840 ? 173.082 250.898 161.590 1.00 3.76  ? 3840 LEU A CA    1 
ATOM   17422 C  C     . LEU A 1 3840 ? 171.928 249.923 161.389 1.00 5.90  ? 3840 LEU A C     1 
ATOM   17423 O  O     . LEU A 1 3840 ? 171.352 249.882 160.295 1.00 16.60 ? 3840 LEU A O     1 
ATOM   17424 C  CB    . LEU A 1 3840 ? 174.390 250.220 161.183 1.00 3.86  ? 3840 LEU A CB    1 
ATOM   17425 C  CG    . LEU A 1 3840 ? 175.597 251.137 160.990 1.00 4.45  ? 3840 LEU A CG    1 
ATOM   17426 C  CD1   . LEU A 1 3840 ? 176.842 250.318 160.704 1.00 3.26  ? 3840 LEU A CD1   1 
ATOM   17427 C  CD2   . LEU A 1 3840 ? 175.341 252.145 159.881 1.00 3.52  ? 3840 LEU A CD2   1 
ATOM   17428 N  N     . TYR A 1 3841 ? 171.571 249.141 162.402 1.00 5.24  ? 3841 TYR A N     1 
ATOM   17429 C  CA    . TYR A 1 3841 ? 170.612 248.058 162.227 1.00 7.19  ? 3841 TYR A CA    1 
ATOM   17430 C  C     . TYR A 1 3841 ? 169.372 248.161 163.098 1.00 8.62  ? 3841 TYR A C     1 
ATOM   17431 O  O     . TYR A 1 3841 ? 168.336 247.605 162.730 1.00 12.16 ? 3841 TYR A O     1 
ATOM   17432 C  CB    . TYR A 1 3841 ? 171.285 246.704 162.493 1.00 6.55  ? 3841 TYR A CB    1 
ATOM   17433 C  CG    . TYR A 1 3841 ? 172.360 246.356 161.494 1.00 13.01 ? 3841 TYR A CG    1 
ATOM   17434 C  CD1   . TYR A 1 3841 ? 172.030 245.942 160.211 1.00 11.97 ? 3841 TYR A CD1   1 
ATOM   17435 C  CD2   . TYR A 1 3841 ? 173.703 246.445 161.829 1.00 10.99 ? 3841 TYR A CD2   1 
ATOM   17436 C  CE1   . TYR A 1 3841 ? 173.006 245.621 159.294 1.00 9.92  ? 3841 TYR A CE1   1 
ATOM   17437 C  CE2   . TYR A 1 3841 ? 174.688 246.125 160.916 1.00 10.61 ? 3841 TYR A CE2   1 
ATOM   17438 C  CZ    . TYR A 1 3841 ? 174.332 245.715 159.650 1.00 16.94 ? 3841 TYR A CZ    1 
ATOM   17439 O  OH    . TYR A 1 3841 ? 175.308 245.396 158.731 1.00 19.23 ? 3841 TYR A OH    1 
ATOM   17440 N  N     . GLU A 1 3842 ? 169.439 248.849 164.233 1.00 7.58  ? 3842 GLU A N     1 
ATOM   17441 C  CA    . GLU A 1 3842 ? 168.312 248.968 165.149 1.00 8.98  ? 3842 GLU A CA    1 
ATOM   17442 C  C     . GLU A 1 3842 ? 167.892 250.424 165.304 1.00 10.68 ? 3842 GLU A C     1 
ATOM   17443 O  O     . GLU A 1 3842 ? 167.633 250.905 166.409 1.00 16.10 ? 3842 GLU A O     1 
ATOM   17444 C  CB    . GLU A 1 3842 ? 168.648 248.351 166.503 1.00 8.38  ? 3842 GLU A CB    1 
ATOM   17445 C  CG    . GLU A 1 3842 ? 169.165 246.926 166.418 1.00 11.85 ? 3842 GLU A CG    1 
ATOM   17446 C  CD    . GLU A 1 3842 ? 170.259 246.637 167.426 1.00 14.15 ? 3842 GLU A CD    1 
ATOM   17447 O  OE1   . GLU A 1 3842 ? 170.633 247.558 168.182 1.00 18.36 ? 3842 GLU A OE1   1 
ATOM   17448 O  OE2   . GLU A 1 3842 ? 170.746 245.489 167.461 1.00 16.59 ? 3842 GLU A OE2   1 
ATOM   17449 N  N     . ASN A 1 3843 ? 167.818 251.144 164.187 1.00 9.06  ? 3843 ASN A N     1 
ATOM   17450 C  CA    . ASN A 1 3843 ? 167.510 252.564 164.205 1.00 12.91 ? 3843 ASN A CA    1 
ATOM   17451 C  C     . ASN A 1 3843 ? 166.074 252.778 163.757 1.00 16.19 ? 3843 ASN A C     1 
ATOM   17452 O  O     . ASN A 1 3843 ? 165.752 252.504 162.590 1.00 19.30 ? 3843 ASN A O     1 
ATOM   17453 C  CB    . ASN A 1 3843 ? 168.472 253.324 163.298 1.00 11.18 ? 3843 ASN A CB    1 
ATOM   17454 C  CG    . ASN A 1 3843 ? 168.288 254.827 163.375 1.00 12.82 ? 3843 ASN A CG    1 
ATOM   17455 O  OD1   . ASN A 1 3843 ? 167.394 255.327 164.054 1.00 17.59 ? 3843 ASN A OD1   1 
ATOM   17456 N  ND2   . ASN A 1 3843 ? 169.156 255.558 162.686 1.00 13.62 ? 3843 ASN A ND2   1 
ATOM   17457 N  N     . PRO A 1 3844 ? 165.187 253.262 164.632 1.00 17.68 ? 3844 PRO A N     1 
ATOM   17458 C  CA    . PRO A 1 3844 ? 163.794 253.494 164.213 1.00 13.01 ? 3844 PRO A CA    1 
ATOM   17459 C  C     . PRO A 1 3844 ? 163.643 254.592 163.179 1.00 15.55 ? 3844 PRO A C     1 
ATOM   17460 O  O     . PRO A 1 3844 ? 162.589 254.672 162.536 1.00 29.14 ? 3844 PRO A O     1 
ATOM   17461 C  CB    . PRO A 1 3844 ? 163.087 253.866 165.526 1.00 17.98 ? 3844 PRO A CB    1 
ATOM   17462 C  CG    . PRO A 1 3844 ? 164.044 253.471 166.623 1.00 15.73 ? 3844 PRO A CG    1 
ATOM   17463 C  CD    . PRO A 1 3844 ? 165.406 253.627 166.039 1.00 12.23 ? 3844 PRO A CD    1 
ATOM   17464 N  N     . ASN A 1 3845 ? 164.650 255.438 162.996 1.00 15.10 ? 3845 ASN A N     1 
ATOM   17465 C  CA    . ASN A 1 3845 ? 164.576 256.545 162.054 1.00 13.34 ? 3845 ASN A CA    1 
ATOM   17466 C  C     . ASN A 1 3845 ? 164.885 256.132 160.620 1.00 15.82 ? 3845 ASN A C     1 
ATOM   17467 O  O     . ASN A 1 3845 ? 164.811 256.973 159.721 1.00 14.29 ? 3845 ASN A O     1 
ATOM   17468 C  CB    . ASN A 1 3845 ? 165.529 257.661 162.489 1.00 12.48 ? 3845 ASN A CB    1 
ATOM   17469 C  CG    . ASN A 1 3845 ? 165.148 258.262 163.828 1.00 18.94 ? 3845 ASN A CG    1 
ATOM   17470 O  OD1   . ASN A 1 3845 ? 165.884 258.142 164.806 1.00 15.01 ? 3845 ASN A OD1   1 
ATOM   17471 N  ND2   . ASN A 1 3845 ? 163.994 258.913 163.877 1.00 23.97 ? 3845 ASN A ND2   1 
ATOM   17472 N  N     . LEU A 1 3846 ? 165.228 254.864 160.388 1.00 12.88 ? 3846 LEU A N     1 
ATOM   17473 C  CA    . LEU A 1 3846 ? 165.520 254.354 159.052 1.00 14.65 ? 3846 LEU A CA    1 
ATOM   17474 C  C     . LEU A 1 3846 ? 164.458 253.376 158.560 1.00 19.51 ? 3846 LEU A C     1 
ATOM   17475 O  O     . LEU A 1 3846 ? 164.702 252.640 157.599 1.00 19.95 ? 3846 LEU A O     1 
ATOM   17476 C  CB    . LEU A 1 3846 ? 166.894 253.683 159.031 1.00 15.56 ? 3846 LEU A CB    1 
ATOM   17477 C  CG    . LEU A 1 3846 ? 168.126 254.517 159.376 1.00 10.80 ? 3846 LEU A CG    1 
ATOM   17478 C  CD1   . LEU A 1 3846 ? 169.302 253.604 159.650 1.00 7.29  ? 3846 LEU A CD1   1 
ATOM   17479 C  CD2   . LEU A 1 3846 ? 168.448 255.482 158.252 1.00 11.71 ? 3846 LEU A CD2   1 
ATOM   17480 N  N     . LYS A 1 3847 ? 163.285 253.354 159.200 1.00 20.82 ? 3847 LYS A N     1 
ATOM   17481 C  CA    . LYS A 1 3847 ? 162.285 252.335 158.892 1.00 20.41 ? 3847 LYS A CA    1 
ATOM   17482 C  C     . LYS A 1 3847 ? 161.798 252.441 157.451 1.00 23.96 ? 3847 LYS A C     1 
ATOM   17483 O  O     . LYS A 1 3847 ? 161.715 251.435 156.737 1.00 32.38 ? 3847 LYS A O     1 
ATOM   17484 C  CB    . LYS A 1 3847 ? 161.110 252.446 159.865 1.00 23.94 ? 3847 LYS A CB    1 
ATOM   17485 C  CG    . LYS A 1 3847 ? 160.096 251.323 159.743 1.00 23.56 ? 3847 LYS A CG    1 
ATOM   17486 C  CD    . LYS A 1 3847 ? 160.678 249.994 160.193 1.00 24.67 ? 3847 LYS A CD    1 
ATOM   17487 C  CE    . LYS A 1 3847 ? 161.083 250.036 161.657 1.00 23.32 ? 3847 LYS A CE    1 
ATOM   17488 N  NZ    . LYS A 1 3847 ? 161.664 248.742 162.106 1.00 24.96 ? 3847 LYS A NZ    1 
ATOM   17489 N  N     . GLY A 1 3848 ? 161.477 253.650 157.002 1.00 17.02 ? 3848 GLY A N     1 
ATOM   17490 C  CA    . GLY A 1 3848 ? 160.931 253.819 155.669 1.00 14.80 ? 3848 GLY A CA    1 
ATOM   17491 C  C     . GLY A 1 3848 ? 161.839 254.568 154.719 1.00 19.95 ? 3848 GLY A C     1 
ATOM   17492 O  O     . GLY A 1 3848 ? 161.513 254.740 153.541 1.00 27.00 ? 3848 GLY A O     1 
ATOM   17493 N  N     . VAL A 1 3849 ? 162.988 255.018 155.220 1.00 17.34 ? 3849 VAL A N     1 
ATOM   17494 C  CA    . VAL A 1 3849 ? 163.884 255.835 154.415 1.00 15.40 ? 3849 VAL A CA    1 
ATOM   17495 C  C     . VAL A 1 3849 ? 164.587 254.961 153.384 1.00 21.18 ? 3849 VAL A C     1 
ATOM   17496 O  O     . VAL A 1 3849 ? 165.123 253.894 153.710 1.00 18.76 ? 3849 VAL A O     1 
ATOM   17497 C  CB    . VAL A 1 3849 ? 164.893 256.565 155.311 1.00 16.79 ? 3849 VAL A CB    1 
ATOM   17498 C  CG1   . VAL A 1 3849 ? 165.716 257.527 154.488 1.00 11.65 ? 3849 VAL A CG1   1 
ATOM   17499 C  CG2   . VAL A 1 3849 ? 164.174 257.287 156.442 1.00 21.12 ? 3849 VAL A CG2   1 
ATOM   17500 N  N     . THR A 1 3850 ? 164.586 255.413 152.128 1.00 21.75 ? 3850 THR A N     1 
ATOM   17501 C  CA    . THR A 1 3850 ? 165.210 254.677 151.039 1.00 14.94 ? 3850 THR A CA    1 
ATOM   17502 C  C     . THR A 1 3850 ? 166.368 255.409 150.378 1.00 20.58 ? 3850 THR A C     1 
ATOM   17503 O  O     . THR A 1 3850 ? 167.222 254.750 149.776 1.00 24.99 ? 3850 THR A O     1 
ATOM   17504 C  CB    . THR A 1 3850 ? 164.176 254.332 149.957 1.00 18.77 ? 3850 THR A CB    1 
ATOM   17505 O  OG1   . THR A 1 3850 ? 163.387 255.491 149.660 1.00 20.64 ? 3850 THR A OG1   1 
ATOM   17506 C  CG2   . THR A 1 3850 ? 163.264 253.211 150.427 1.00 20.04 ? 3850 THR A CG2   1 
ATOM   17507 N  N     . ASP A 1 3851 ? 166.425 256.734 150.469 1.00 20.12 ? 3851 ASP A N     1 
ATOM   17508 C  CA    . ASP A 1 3851 ? 167.507 257.474 149.838 1.00 17.18 ? 3851 ASP A CA    1 
ATOM   17509 C  C     . ASP A 1 3851 ? 168.794 257.301 150.635 1.00 19.98 ? 3851 ASP A C     1 
ATOM   17510 O  O     . ASP A 1 3851 ? 168.824 257.539 151.845 1.00 20.94 ? 3851 ASP A O     1 
ATOM   17511 C  CB    . ASP A 1 3851 ? 167.140 258.951 149.724 1.00 14.46 ? 3851 ASP A CB    1 
ATOM   17512 C  CG    . ASP A 1 3851 ? 168.322 259.818 149.354 1.00 21.05 ? 3851 ASP A CG    1 
ATOM   17513 O  OD1   . ASP A 1 3851 ? 168.989 259.508 148.347 1.00 23.66 ? 3851 ASP A OD1   1 
ATOM   17514 O  OD2   . ASP A 1 3851 ? 168.578 260.814 150.064 1.00 21.93 ? 3851 ASP A OD2   1 
ATOM   17515 N  N     . HIS A 1 3852 ? 169.862 256.891 149.944 1.00 19.12 ? 3852 HIS A N     1 
ATOM   17516 C  CA    . HIS A 1 3852 ? 171.118 256.588 150.624 1.00 13.14 ? 3852 HIS A CA    1 
ATOM   17517 C  C     . HIS A 1 3852 ? 171.683 257.817 151.324 1.00 13.16 ? 3852 HIS A C     1 
ATOM   17518 O  O     . HIS A 1 3852 ? 172.193 257.721 152.446 1.00 15.64 ? 3852 HIS A O     1 
ATOM   17519 C  CB    . HIS A 1 3852 ? 172.132 256.029 149.627 1.00 15.22 ? 3852 HIS A CB    1 
ATOM   17520 C  CG    . HIS A 1 3852 ? 171.714 254.736 149.000 1.00 18.50 ? 3852 HIS A CG    1 
ATOM   17521 N  ND1   . HIS A 1 3852 ? 170.826 253.870 149.600 1.00 17.50 ? 3852 HIS A ND1   1 
ATOM   17522 C  CD2   . HIS A 1 3852 ? 172.067 254.160 147.827 1.00 17.37 ? 3852 HIS A CD2   1 
ATOM   17523 C  CE1   . HIS A 1 3852 ? 170.646 252.818 148.822 1.00 13.83 ? 3852 HIS A CE1   1 
ATOM   17524 N  NE2   . HIS A 1 3852 ? 171.388 252.969 147.740 1.00 20.41 ? 3852 HIS A NE2   1 
ATOM   17525 N  N     . THR A 1 3853 ? 171.606 258.980 150.675 1.00 11.61 ? 3853 THR A N     1 
ATOM   17526 C  CA    . THR A 1 3853 ? 172.127 260.199 151.285 1.00 13.27 ? 3853 THR A CA    1 
ATOM   17527 C  C     . THR A 1 3853 ? 171.374 260.543 152.565 1.00 13.17 ? 3853 THR A C     1 
ATOM   17528 O  O     . THR A 1 3853 ? 171.987 260.911 153.574 1.00 16.01 ? 3853 THR A O     1 
ATOM   17529 C  CB    . THR A 1 3853 ? 172.050 261.356 150.290 1.00 12.40 ? 3853 THR A CB    1 
ATOM   17530 O  OG1   . THR A 1 3853 ? 172.883 261.071 149.158 1.00 19.61 ? 3853 THR A OG1   1 
ATOM   17531 C  CG2   . THR A 1 3853 ? 172.514 262.650 150.937 1.00 11.63 ? 3853 THR A CG2   1 
ATOM   17532 N  N     . GLN A 1 3854 ? 170.046 260.423 152.545 1.00 11.10 ? 3854 GLN A N     1 
ATOM   17533 C  CA    . GLN A 1 3854 ? 169.261 260.782 153.720 1.00 13.83 ? 3854 GLN A CA    1 
ATOM   17534 C  C     . GLN A 1 3854 ? 169.453 259.763 154.838 1.00 13.43 ? 3854 GLN A C     1 
ATOM   17535 O  O     . GLN A 1 3854 ? 169.473 260.127 156.020 1.00 15.67 ? 3854 GLN A O     1 
ATOM   17536 C  CB    . GLN A 1 3854 ? 167.786 260.919 153.338 1.00 14.86 ? 3854 GLN A CB    1 
ATOM   17537 C  CG    . GLN A 1 3854 ? 166.822 260.869 154.506 1.00 16.29 ? 3854 GLN A CG    1 
ATOM   17538 C  CD    . GLN A 1 3854 ? 165.378 261.016 154.072 1.00 24.00 ? 3854 GLN A CD    1 
ATOM   17539 O  OE1   . GLN A 1 3854 ? 165.056 260.889 152.891 1.00 16.52 ? 3854 GLN A OE1   1 
ATOM   17540 N  NE2   . GLN A 1 3854 ? 164.498 261.284 155.030 1.00 23.79 ? 3854 GLN A NE2   1 
ATOM   17541 N  N     . ARG A 1 3855 ? 169.611 258.485 154.485 1.00 11.73 ? 3855 ARG A N     1 
ATOM   17542 C  CA    . ARG A 1 3855 ? 169.938 257.476 155.488 1.00 7.78  ? 3855 ARG A CA    1 
ATOM   17543 C  C     . ARG A 1 3855 ? 171.280 257.765 156.140 1.00 9.63  ? 3855 ARG A C     1 
ATOM   17544 O  O     . ARG A 1 3855 ? 171.447 257.576 157.351 1.00 12.99 ? 3855 ARG A O     1 
ATOM   17545 C  CB    . ARG A 1 3855 ? 169.948 256.084 154.858 1.00 8.25  ? 3855 ARG A CB    1 
ATOM   17546 C  CG    . ARG A 1 3855 ? 168.615 255.623 154.325 1.00 9.36  ? 3855 ARG A CG    1 
ATOM   17547 C  CD    . ARG A 1 3855 ? 168.626 254.145 154.000 1.00 13.57 ? 3855 ARG A CD    1 
ATOM   17548 N  NE    . ARG A 1 3855 ? 169.126 253.343 155.108 1.00 12.05 ? 3855 ARG A NE    1 
ATOM   17549 C  CZ    . ARG A 1 3855 ? 168.415 252.430 155.750 1.00 13.71 ? 3855 ARG A CZ    1 
ATOM   17550 N  NH1   . ARG A 1 3855 ? 167.161 252.174 155.423 1.00 14.34 ? 3855 ARG A NH1   1 
ATOM   17551 N  NH2   . ARG A 1 3855 ? 168.980 251.754 156.749 1.00 19.32 ? 3855 ARG A NH2   1 
ATOM   17552 N  N     . LEU A 1 3856 ? 172.255 258.216 155.349 1.00 8.30  ? 3856 LEU A N     1 
ATOM   17553 C  CA    . LEU A 1 3856 ? 173.569 258.534 155.896 1.00 6.66  ? 3856 LEU A CA    1 
ATOM   17554 C  C     . LEU A 1 3856 ? 173.491 259.679 156.896 1.00 10.20 ? 3856 LEU A C     1 
ATOM   17555 O  O     . LEU A 1 3856 ? 174.151 259.647 157.941 1.00 10.52 ? 3856 LEU A O     1 
ATOM   17556 C  CB    . LEU A 1 3856 ? 174.536 258.868 154.763 1.00 6.20  ? 3856 LEU A CB    1 
ATOM   17557 C  CG    . LEU A 1 3856 ? 176.021 258.908 155.114 1.00 5.15  ? 3856 LEU A CG    1 
ATOM   17558 C  CD1   . LEU A 1 3856 ? 176.399 257.724 155.988 1.00 6.38  ? 3856 LEU A CD1   1 
ATOM   17559 C  CD2   . LEU A 1 3856 ? 176.856 258.927 153.845 1.00 7.00  ? 3856 LEU A CD2   1 
ATOM   17560 N  N     . SER A 1 3857 ? 172.696 260.708 156.591 1.00 9.50  ? 3857 SER A N     1 
ATOM   17561 C  CA    . SER A 1 3857 ? 172.521 261.808 157.533 1.00 10.27 ? 3857 SER A CA    1 
ATOM   17562 C  C     . SER A 1 3857 ? 171.864 261.327 158.821 1.00 7.98  ? 3857 SER A C     1 
ATOM   17563 O  O     . SER A 1 3857 ? 172.254 261.740 159.918 1.00 10.23 ? 3857 SER A O     1 
ATOM   17564 C  CB    . SER A 1 3857 ? 171.696 262.926 156.896 1.00 11.35 ? 3857 SER A CB    1 
ATOM   17565 O  OG    . SER A 1 3857 ? 170.360 262.512 156.678 1.00 13.15 ? 3857 SER A OG    1 
ATOM   17566 N  N     . ILE A 1 3858 ? 170.861 260.454 158.703 1.00 7.48  ? 3858 ILE A N     1 
ATOM   17567 C  CA    . ILE A 1 3858 ? 170.219 259.890 159.885 1.00 7.76  ? 3858 ILE A CA    1 
ATOM   17568 C  C     . ILE A 1 3858 ? 171.213 259.063 160.690 1.00 9.49  ? 3858 ILE A C     1 
ATOM   17569 O  O     . ILE A 1 3858 ? 171.278 259.170 161.920 1.00 11.50 ? 3858 ILE A O     1 
ATOM   17570 C  CB    . ILE A 1 3858 ? 168.990 259.058 159.478 1.00 9.12  ? 3858 ILE A CB    1 
ATOM   17571 C  CG1   . ILE A 1 3858 ? 167.890 259.963 158.923 1.00 8.97  ? 3858 ILE A CG1   1 
ATOM   17572 C  CG2   . ILE A 1 3858 ? 168.490 258.238 160.652 1.00 10.23 ? 3858 ILE A CG2   1 
ATOM   17573 C  CD1   . ILE A 1 3858 ? 166.823 259.221 158.158 1.00 12.89 ? 3858 ILE A CD1   1 
ATOM   17574 N  N     . ILE A 1 3859 ? 172.001 258.230 160.008 1.00 7.70  ? 3859 ILE A N     1 
ATOM   17575 C  CA    . ILE A 1 3859 ? 172.994 257.409 160.694 1.00 6.49  ? 3859 ILE A CA    1 
ATOM   17576 C  C     . ILE A 1 3859 ? 174.033 258.287 161.376 1.00 5.26  ? 3859 ILE A C     1 
ATOM   17577 O  O     . ILE A 1 3859 ? 174.408 258.049 162.530 1.00 7.24  ? 3859 ILE A O     1 
ATOM   17578 C  CB    . ILE A 1 3859 ? 173.640 256.420 159.705 1.00 5.49  ? 3859 ILE A CB    1 
ATOM   17579 C  CG1   . ILE A 1 3859 ? 172.677 255.275 159.391 1.00 5.49  ? 3859 ILE A CG1   1 
ATOM   17580 C  CG2   . ILE A 1 3859 ? 174.951 255.884 160.254 1.00 4.53  ? 3859 ILE A CG2   1 
ATOM   17581 C  CD1   . ILE A 1 3859 ? 173.041 254.494 158.152 1.00 5.80  ? 3859 ILE A CD1   1 
ATOM   17582 N  N     . THR A 1 3860 ? 174.508 259.321 160.676 1.00 4.96  ? 3860 THR A N     1 
ATOM   17583 C  CA    . THR A 1 3860 ? 175.508 260.213 161.254 1.00 5.64  ? 3860 THR A CA    1 
ATOM   17584 C  C     . THR A 1 3860 ? 174.961 260.942 162.473 1.00 9.01  ? 3860 THR A C     1 
ATOM   17585 O  O     . THR A 1 3860 ? 175.634 261.032 163.507 1.00 7.19  ? 3860 THR A O     1 
ATOM   17586 C  CB    . THR A 1 3860 ? 175.980 261.220 160.204 1.00 5.67  ? 3860 THR A CB    1 
ATOM   17587 O  OG1   . THR A 1 3860 ? 176.432 260.521 159.037 1.00 9.38  ? 3860 THR A OG1   1 
ATOM   17588 C  CG2   . THR A 1 3860 ? 177.113 262.072 160.752 1.00 3.81  ? 3860 THR A CG2   1 
ATOM   17589 N  N     . LYS A 1 3861 ? 173.741 261.469 162.370 1.00 8.90  ? 3861 LYS A N     1 
ATOM   17590 C  CA    . LYS A 1 3861 ? 173.125 262.150 163.503 1.00 6.27  ? 3861 LYS A CA    1 
ATOM   17591 C  C     . LYS A 1 3861 ? 172.898 261.191 164.664 1.00 4.72  ? 3861 LYS A C     1 
ATOM   17592 O  O     . LYS A 1 3861 ? 173.197 261.515 165.819 1.00 4.21  ? 3861 LYS A O     1 
ATOM   17593 C  CB    . LYS A 1 3861 ? 171.804 262.786 163.067 1.00 6.75  ? 3861 LYS A CB    1 
ATOM   17594 C  CG    . LYS A 1 3861 ? 171.096 263.567 164.157 1.00 6.33  ? 3861 LYS A CG    1 
ATOM   17595 C  CD    . LYS A 1 3861 ? 169.855 264.260 163.620 1.00 8.70  ? 3861 LYS A CD    1 
ATOM   17596 C  CE    . LYS A 1 3861 ? 169.064 264.914 164.738 1.00 18.23 ? 3861 LYS A CE    1 
ATOM   17597 N  NZ    . LYS A 1 3861 ? 169.816 266.035 165.368 1.00 13.24 ? 3861 LYS A NZ    1 
ATOM   17598 N  N     . ASP A 1 3862 ? 172.380 259.997 164.371 1.00 7.05  ? 3862 ASP A N     1 
ATOM   17599 C  CA    . ASP A 1 3862 ? 171.986 259.089 165.439 1.00 3.24  ? 3862 ASP A CA    1 
ATOM   17600 C  C     . ASP A 1 3862 ? 173.214 258.470 166.099 1.00 3.67  ? 3862 ASP A C     1 
ATOM   17601 O  O     . ASP A 1 3862 ? 173.165 258.089 167.274 1.00 4.76  ? 3862 ASP A O     1 
ATOM   17602 C  CB    . ASP A 1 3862 ? 171.053 258.016 164.871 1.00 6.33  ? 3862 ASP A CB    1 
ATOM   17603 C  CG    . ASP A 1 3862 ? 170.404 257.161 165.944 1.00 23.33 ? 3862 ASP A CG    1 
ATOM   17604 O  OD1   . ASP A 1 3862 ? 170.679 257.363 167.137 1.00 21.22 ? 3862 ASP A OD1   1 
ATOM   17605 O  OD2   . ASP A 1 3862 ? 169.599 256.279 165.588 1.00 21.89 ? 3862 ASP A OD2   1 
ATOM   17606 N  N     . LEU A 1 3863 ? 174.331 258.383 165.368 1.00 5.19  ? 3863 LEU A N     1 
ATOM   17607 C  CA    . LEU A 1 3863 ? 175.568 257.872 165.949 1.00 1.88  ? 3863 LEU A CA    1 
ATOM   17608 C  C     . LEU A 1 3863 ? 176.031 258.740 167.111 1.00 1.59  ? 3863 LEU A C     1 
ATOM   17609 O  O     . LEU A 1 3863 ? 176.446 258.223 168.155 1.00 2.50  ? 3863 LEU A O     1 
ATOM   17610 C  CB    . LEU A 1 3863 ? 176.656 257.792 164.879 1.00 1.99  ? 3863 LEU A CB    1 
ATOM   17611 C  CG    . LEU A 1 3863 ? 178.061 257.419 165.357 1.00 3.79  ? 3863 LEU A CG    1 
ATOM   17612 C  CD1   . LEU A 1 3863 ? 178.114 255.975 165.826 1.00 1.35  ? 3863 LEU A CD1   1 
ATOM   17613 C  CD2   . LEU A 1 3863 ? 179.093 257.676 164.272 1.00 1.82  ? 3863 LEU A CD2   1 
ATOM   17614 N  N     . PHE A 1 3864 ? 175.974 260.061 166.947 1.00 1.71  ? 3864 PHE A N     1 
ATOM   17615 C  CA    . PHE A 1 3864 ? 176.356 260.957 168.032 1.00 1.98  ? 3864 PHE A CA    1 
ATOM   17616 C  C     . PHE A 1 3864 ? 175.384 260.858 169.199 1.00 0.97  ? 3864 PHE A C     1 
ATOM   17617 O  O     . PHE A 1 3864 ? 175.790 260.954 170.363 1.00 0.35  ? 3864 PHE A O     1 
ATOM   17618 C  CB    . PHE A 1 3864 ? 176.440 262.394 167.520 1.00 1.18  ? 3864 PHE A CB    1 
ATOM   17619 C  CG    . PHE A 1 3864 ? 177.710 262.704 166.787 1.00 0.94  ? 3864 PHE A CG    1 
ATOM   17620 C  CD1   . PHE A 1 3864 ? 178.834 263.123 167.475 1.00 1.59  ? 3864 PHE A CD1   1 
ATOM   17621 C  CD2   . PHE A 1 3864 ? 177.782 262.579 165.411 1.00 1.00  ? 3864 PHE A CD2   1 
ATOM   17622 C  CE1   . PHE A 1 3864 ? 180.008 263.409 166.803 1.00 2.89  ? 3864 PHE A CE1   1 
ATOM   17623 C  CE2   . PHE A 1 3864 ? 178.952 262.861 164.735 1.00 1.14  ? 3864 PHE A CE2   1 
ATOM   17624 C  CZ    . PHE A 1 3864 ? 180.065 263.278 165.432 1.00 1.70  ? 3864 PHE A CZ    1 
ATOM   17625 N  N     . GLN A 1 3865 ? 174.094 260.667 168.908 1.00 0.97  ? 3865 GLN A N     1 
ATOM   17626 C  CA    . GLN A 1 3865 ? 173.087 260.649 169.962 1.00 0.65  ? 3865 GLN A CA    1 
ATOM   17627 C  C     . GLN A 1 3865 ? 173.199 259.392 170.820 1.00 0.55  ? 3865 GLN A C     1 
ATOM   17628 O  O     . GLN A 1 3865 ? 173.180 259.471 172.052 1.00 0.58  ? 3865 GLN A O     1 
ATOM   17629 C  CB    . GLN A 1 3865 ? 171.690 260.762 169.350 1.00 0.77  ? 3865 GLN A CB    1 
ATOM   17630 C  CG    . GLN A 1 3865 ? 170.584 260.923 170.375 1.00 1.37  ? 3865 GLN A CG    1 
ATOM   17631 C  CD    . GLN A 1 3865 ? 170.656 262.250 171.103 1.00 0.98  ? 3865 GLN A CD    1 
ATOM   17632 O  OE1   . GLN A 1 3865 ? 170.310 263.290 170.551 1.00 2.53  ? 3865 GLN A OE1   1 
ATOM   17633 N  NE2   . GLN A 1 3865 ? 171.123 262.221 172.343 1.00 0.60  ? 3865 GLN A NE2   1 
ATOM   17634 N  N     . VAL A 1 3866 ? 173.313 258.224 170.187 1.00 0.45  ? 3866 VAL A N     1 
ATOM   17635 C  CA    . VAL A 1 3866 ? 173.418 256.982 170.947 1.00 0.59  ? 3866 VAL A CA    1 
ATOM   17636 C  C     . VAL A 1 3866 ? 174.739 256.927 171.702 1.00 0.43  ? 3866 VAL A C     1 
ATOM   17637 O  O     . VAL A 1 3866 ? 174.807 256.413 172.825 1.00 0.55  ? 3866 VAL A O     1 
ATOM   17638 C  CB    . VAL A 1 3866 ? 173.231 255.763 170.028 1.00 1.67  ? 3866 VAL A CB    1 
ATOM   17639 C  CG1   . VAL A 1 3866 ? 173.433 254.474 170.801 1.00 1.39  ? 3866 VAL A CG1   1 
ATOM   17640 C  CG2   . VAL A 1 3866 ? 171.847 255.775 169.432 1.00 1.19  ? 3866 VAL A CG2   1 
ATOM   17641 N  N     . ALA A 1 3867 ? 175.808 257.457 171.103 1.00 0.36  ? 3867 ALA A N     1 
ATOM   17642 C  CA    . ALA A 1 3867 ? 177.092 257.483 171.791 1.00 0.37  ? 3867 ALA A CA    1 
ATOM   17643 C  C     . ALA A 1 3867 ? 177.004 258.280 173.085 1.00 0.47  ? 3867 ALA A C     1 
ATOM   17644 O  O     . ALA A 1 3867 ? 177.526 257.853 174.120 1.00 1.02  ? 3867 ALA A O     1 
ATOM   17645 C  CB    . ALA A 1 3867 ? 178.172 258.059 170.876 1.00 0.38  ? 3867 ALA A CB    1 
ATOM   17646 N  N     . PHE A 1 3868 ? 176.339 259.435 173.049 1.00 0.26  ? 3868 PHE A N     1 
ATOM   17647 C  CA    . PHE A 1 3868 ? 176.173 260.209 174.272 1.00 0.22  ? 3868 PHE A CA    1 
ATOM   17648 C  C     . PHE A 1 3868 ? 175.251 259.500 175.256 1.00 0.29  ? 3868 PHE A C     1 
ATOM   17649 O  O     . PHE A 1 3868 ? 175.522 259.485 176.460 1.00 0.49  ? 3868 PHE A O     1 
ATOM   17650 C  CB    . PHE A 1 3868 ? 175.637 261.604 173.956 1.00 0.24  ? 3868 PHE A CB    1 
ATOM   17651 C  CG    . PHE A 1 3868 ? 175.453 262.464 175.173 1.00 0.21  ? 3868 PHE A CG    1 
ATOM   17652 C  CD1   . PHE A 1 3868 ? 176.540 263.071 175.779 1.00 0.26  ? 3868 PHE A CD1   1 
ATOM   17653 C  CD2   . PHE A 1 3868 ? 174.198 262.654 175.723 1.00 0.17  ? 3868 PHE A CD2   1 
ATOM   17654 C  CE1   . PHE A 1 3868 ? 176.380 263.854 176.900 1.00 0.50  ? 3868 PHE A CE1   1 
ATOM   17655 C  CE2   . PHE A 1 3868 ? 174.030 263.439 176.846 1.00 0.39  ? 3868 PHE A CE2   1 
ATOM   17656 C  CZ    . PHE A 1 3868 ? 175.120 264.040 177.434 1.00 0.67  ? 3868 PHE A CZ    1 
ATOM   17657 N  N     . ASN A 1 3869 ? 174.164 258.906 174.764 1.00 0.26  ? 3869 ASN A N     1 
ATOM   17658 C  CA    . ASN A 1 3869 ? 173.174 258.312 175.654 1.00 0.36  ? 3869 ASN A CA    1 
ATOM   17659 C  C     . ASN A 1 3869 ? 173.760 257.149 176.443 1.00 1.23  ? 3869 ASN A C     1 
ATOM   17660 O  O     . ASN A 1 3869 ? 173.597 257.070 177.666 1.00 3.71  ? 3869 ASN A O     1 
ATOM   17661 C  CB    . ASN A 1 3869 ? 171.951 257.864 174.854 1.00 0.46  ? 3869 ASN A CB    1 
ATOM   17662 C  CG    . ASN A 1 3869 ? 171.077 259.027 174.429 1.00 1.17  ? 3869 ASN A CG    1 
ATOM   17663 O  OD1   . ASN A 1 3869 ? 171.302 260.166 174.830 1.00 2.15  ? 3869 ASN A OD1   1 
ATOM   17664 N  ND2   . ASN A 1 3869 ? 170.072 258.743 173.611 1.00 2.27  ? 3869 ASN A ND2   1 
ATOM   17665 N  N     . ARG A 1 3870 ? 174.461 256.241 175.766 1.00 0.73  ? 3870 ARG A N     1 
ATOM   17666 C  CA    . ARG A 1 3870 ? 174.971 255.062 176.455 1.00 0.67  ? 3870 ARG A CA    1 
ATOM   17667 C  C     . ARG A 1 3870 ? 176.179 255.386 177.329 1.00 0.59  ? 3870 ARG A C     1 
ATOM   17668 O  O     . ARG A 1 3870 ? 176.315 254.835 178.426 1.00 2.66  ? 3870 ARG A O     1 
ATOM   17669 C  CB    . ARG A 1 3870 ? 175.312 253.973 175.441 1.00 1.05  ? 3870 ARG A CB    1 
ATOM   17670 C  CG    . ARG A 1 3870 ? 174.129 253.558 174.583 1.00 1.16  ? 3870 ARG A CG    1 
ATOM   17671 C  CD    . ARG A 1 3870 ? 174.363 252.216 173.928 1.00 1.95  ? 3870 ARG A CD    1 
ATOM   17672 N  NE    . ARG A 1 3870 ? 173.205 251.762 173.169 1.00 6.94  ? 3870 ARG A NE    1 
ATOM   17673 C  CZ    . ARG A 1 3870 ? 173.129 250.592 172.552 1.00 5.89  ? 3870 ARG A CZ    1 
ATOM   17674 N  NH1   . ARG A 1 3870 ? 174.131 249.733 172.579 1.00 3.93  ? 3870 ARG A NH1   1 
ATOM   17675 N  NH2   . ARG A 1 3870 ? 172.015 250.276 171.899 1.00 7.59  ? 3870 ARG A NH2   1 
ATOM   17676 N  N     . VAL A 1 3871 ? 177.064 256.271 176.867 1.00 0.38  ? 3871 VAL A N     1 
ATOM   17677 C  CA    . VAL A 1 3871 ? 178.247 256.601 177.657 1.00 0.48  ? 3871 VAL A CA    1 
ATOM   17678 C  C     . VAL A 1 3871 ? 177.869 257.418 178.888 1.00 0.38  ? 3871 VAL A C     1 
ATOM   17679 O  O     . VAL A 1 3871 ? 178.357 257.157 179.994 1.00 0.45  ? 3871 VAL A O     1 
ATOM   17680 C  CB    . VAL A 1 3871 ? 179.288 257.325 176.785 1.00 0.32  ? 3871 VAL A CB    1 
ATOM   17681 C  CG1   . VAL A 1 3871 ? 180.389 257.916 177.645 1.00 0.49  ? 3871 VAL A CG1   1 
ATOM   17682 C  CG2   . VAL A 1 3871 ? 179.877 256.373 175.760 1.00 0.20  ? 3871 VAL A CG2   1 
ATOM   17683 N  N     . ALA A 1 3872 ? 176.989 258.411 178.723 1.00 0.32  ? 3872 ALA A N     1 
ATOM   17684 C  CA    . ALA A 1 3872 ? 176.661 259.312 179.826 1.00 0.28  ? 3872 ALA A CA    1 
ATOM   17685 C  C     . ALA A 1 3872 ? 175.856 258.633 180.925 1.00 0.36  ? 3872 ALA A C     1 
ATOM   17686 O  O     . ALA A 1 3872 ? 175.887 259.096 182.069 1.00 0.25  ? 3872 ALA A O     1 
ATOM   17687 C  CB    . ALA A 1 3872 ? 175.900 260.535 179.312 1.00 0.35  ? 3872 ALA A CB    1 
ATOM   17688 N  N     . ARG A 1 3873 ? 175.137 257.551 180.615 1.00 0.90  ? 3873 ARG A N     1 
ATOM   17689 C  CA    . ARG A 1 3873 ? 174.456 256.810 181.668 1.00 0.72  ? 3873 ARG A CA    1 
ATOM   17690 C  C     . ARG A 1 3873 ? 175.455 256.203 182.644 1.00 0.47  ? 3873 ARG A C     1 
ATOM   17691 O  O     . ARG A 1 3873 ? 175.109 255.922 183.796 1.00 0.59  ? 3873 ARG A O     1 
ATOM   17692 C  CB    . ARG A 1 3873 ? 173.571 255.719 181.067 1.00 1.49  ? 3873 ARG A CB    1 
ATOM   17693 C  CG    . ARG A 1 3873 ? 172.314 256.234 180.395 1.00 2.93  ? 3873 ARG A CG    1 
ATOM   17694 C  CD    . ARG A 1 3873 ? 171.499 257.137 181.298 1.00 4.18  ? 3873 ARG A CD    1 
ATOM   17695 N  NE    . ARG A 1 3873 ? 170.142 257.308 180.792 1.00 7.41  ? 3873 ARG A NE    1 
ATOM   17696 C  CZ    . ARG A 1 3873 ? 169.224 258.088 181.343 1.00 6.50  ? 3873 ARG A CZ    1 
ATOM   17697 N  NH1   . ARG A 1 3873 ? 169.484 258.807 182.421 1.00 5.32  ? 3873 ARG A NH1   1 
ATOM   17698 N  NH2   . ARG A 1 3873 ? 168.013 258.150 180.797 1.00 8.38  ? 3873 ARG A NH2   1 
ATOM   17699 N  N     . GLY A 1 3874 ? 176.692 256.000 182.200 1.00 0.21  ? 3874 GLY A N     1 
ATOM   17700 C  CA    . GLY A 1 3874 ? 177.751 255.526 183.064 1.00 0.22  ? 3874 GLY A CA    1 
ATOM   17701 C  C     . GLY A 1 3874 ? 178.744 256.599 183.449 1.00 0.24  ? 3874 GLY A C     1 
ATOM   17702 O  O     . GLY A 1 3874 ? 179.873 256.293 183.837 1.00 0.42  ? 3874 GLY A O     1 
ATOM   17703 N  N     . MET A 1 3875 ? 178.342 257.861 183.348 1.00 0.41  ? 3875 MET A N     1 
ATOM   17704 C  CA    . MET A 1 3875 ? 179.181 258.979 183.753 1.00 0.39  ? 3875 MET A CA    1 
ATOM   17705 C  C     . MET A 1 3875 ? 178.494 259.756 184.862 1.00 0.36  ? 3875 MET A C     1 
ATOM   17706 O  O     . MET A 1 3875 ? 177.267 259.740 184.986 1.00 0.87  ? 3875 MET A O     1 
ATOM   17707 C  CB    . MET A 1 3875 ? 179.490 259.937 182.589 1.00 0.45  ? 3875 MET A CB    1 
ATOM   17708 C  CG    . MET A 1 3875 ? 180.351 259.353 181.490 1.00 0.55  ? 3875 MET A CG    1 
ATOM   17709 S  SD    . MET A 1 3875 ? 180.607 260.501 180.119 1.00 7.22  ? 3875 MET A SD    1 
ATOM   17710 C  CE    . MET A 1 3875 ? 181.684 261.712 180.865 1.00 1.00  ? 3875 MET A CE    1 
ATOM   17711 N  N     . LEU A 1 3876 ? 179.303 260.419 185.680 1.00 0.47  ? 3876 LEU A N     1 
ATOM   17712 C  CA    . LEU A 1 3876 ? 178.775 261.406 186.607 1.00 0.68  ? 3876 LEU A CA    1 
ATOM   17713 C  C     . LEU A 1 3876 ? 178.172 262.565 185.828 1.00 0.99  ? 3876 LEU A C     1 
ATOM   17714 O  O     . LEU A 1 3876 ? 178.698 262.974 184.790 1.00 2.95  ? 3876 LEU A O     1 
ATOM   17715 C  CB    . LEU A 1 3876 ? 179.877 261.907 187.538 1.00 1.32  ? 3876 LEU A CB    1 
ATOM   17716 C  CG    . LEU A 1 3876 ? 180.467 260.870 188.498 1.00 1.21  ? 3876 LEU A CG    1 
ATOM   17717 C  CD1   . LEU A 1 3876 ? 181.636 261.456 189.268 1.00 2.11  ? 3876 LEU A CD1   1 
ATOM   17718 C  CD2   . LEU A 1 3876 ? 179.401 260.348 189.446 1.00 0.69  ? 3876 LEU A CD2   1 
ATOM   17719 N  N     . HIS A 1 3877 ? 177.054 263.093 186.332 1.00 1.17  ? 3877 HIS A N     1 
ATOM   17720 C  CA    . HIS A 1 3877 ? 176.334 264.134 185.604 1.00 1.20  ? 3877 HIS A CA    1 
ATOM   17721 C  C     . HIS A 1 3877 ? 177.195 265.368 185.373 1.00 1.36  ? 3877 HIS A C     1 
ATOM   17722 O  O     . HIS A 1 3877 ? 177.014 266.069 184.372 1.00 1.80  ? 3877 HIS A O     1 
ATOM   17723 C  CB    . HIS A 1 3877 ? 175.061 264.507 186.362 1.00 0.92  ? 3877 HIS A CB    1 
ATOM   17724 C  CG    . HIS A 1 3877 ? 174.152 265.421 185.602 1.00 1.45  ? 3877 HIS A CG    1 
ATOM   17725 N  ND1   . HIS A 1 3877 ? 174.219 266.792 185.707 1.00 1.38  ? 3877 HIS A ND1   1 
ATOM   17726 C  CD2   . HIS A 1 3877 ? 173.155 265.158 184.725 1.00 4.45  ? 3877 HIS A CD2   1 
ATOM   17727 C  CE1   . HIS A 1 3877 ? 173.303 267.337 184.927 1.00 2.25  ? 3877 HIS A CE1   1 
ATOM   17728 N  NE2   . HIS A 1 3877 ? 172.642 266.367 184.322 1.00 7.03  ? 3877 HIS A NE2   1 
ATOM   17729 N  N     . GLN A 1 3878 ? 178.139 265.642 186.276 1.00 1.31  ? 3878 GLN A N     1 
ATOM   17730 C  CA    . GLN A 1 3878 ? 179.019 266.792 186.109 1.00 1.78  ? 3878 GLN A CA    1 
ATOM   17731 C  C     . GLN A 1 3878 ? 179.904 266.655 184.876 1.00 3.65  ? 3878 GLN A C     1 
ATOM   17732 O  O     . GLN A 1 3878 ? 180.340 267.665 184.312 1.00 6.22  ? 3878 GLN A O     1 
ATOM   17733 C  CB    . GLN A 1 3878 ? 179.876 266.978 187.361 1.00 3.86  ? 3878 GLN A CB    1 
ATOM   17734 C  CG    . GLN A 1 3878 ? 181.003 265.972 187.495 1.00 7.62  ? 3878 GLN A CG    1 
ATOM   17735 C  CD    . GLN A 1 3878 ? 181.646 265.997 188.861 1.00 13.16 ? 3878 GLN A CD    1 
ATOM   17736 O  OE1   . GLN A 1 3878 ? 182.863 266.141 188.986 1.00 18.64 ? 3878 GLN A OE1   1 
ATOM   17737 N  NE2   . GLN A 1 3878 ? 180.833 265.857 189.901 1.00 13.55 ? 3878 GLN A NE2   1 
ATOM   17738 N  N     . ASP A 1 3879 ? 180.180 265.429 184.444 1.00 3.28  ? 3879 ASP A N     1 
ATOM   17739 C  CA    . ASP A 1 3879 ? 181.015 265.192 183.277 1.00 2.17  ? 3879 ASP A CA    1 
ATOM   17740 C  C     . ASP A 1 3879 ? 180.218 265.063 181.985 1.00 1.22  ? 3879 ASP A C     1 
ATOM   17741 O  O     . ASP A 1 3879 ? 180.820 264.891 180.921 1.00 1.84  ? 3879 ASP A O     1 
ATOM   17742 C  CB    . ASP A 1 3879 ? 181.866 263.937 183.486 1.00 1.76  ? 3879 ASP A CB    1 
ATOM   17743 C  CG    . ASP A 1 3879 ? 182.842 264.073 184.634 1.00 6.16  ? 3879 ASP A CG    1 
ATOM   17744 O  OD1   . ASP A 1 3879 ? 183.635 265.033 184.631 1.00 10.65 ? 3879 ASP A OD1   1 
ATOM   17745 O  OD2   . ASP A 1 3879 ? 182.826 263.208 185.534 1.00 8.37  ? 3879 ASP A OD2   1 
ATOM   17746 N  N     . HIS A 1 3880 ? 178.887 265.142 182.050 1.00 1.14  ? 3880 HIS A N     1 
ATOM   17747 C  CA    . HIS A 1 3880 ? 178.075 264.998 180.845 1.00 0.90  ? 3880 HIS A CA    1 
ATOM   17748 C  C     . HIS A 1 3880 ? 178.352 266.116 179.850 1.00 1.19  ? 3880 HIS A C     1 
ATOM   17749 O  O     . HIS A 1 3880 ? 178.420 265.876 178.639 1.00 1.60  ? 3880 HIS A O     1 
ATOM   17750 C  CB    . HIS A 1 3880 ? 176.591 264.967 181.210 1.00 0.63  ? 3880 HIS A CB    1 
ATOM   17751 C  CG    . HIS A 1 3880 ? 176.163 263.706 181.893 1.00 1.03  ? 3880 HIS A CG    1 
ATOM   17752 N  ND1   . HIS A 1 3880 ? 174.843 263.421 182.165 1.00 0.58  ? 3880 HIS A ND1   1 
ATOM   17753 C  CD2   . HIS A 1 3880 ? 176.878 262.657 182.357 1.00 0.46  ? 3880 HIS A CD2   1 
ATOM   17754 C  CE1   . HIS A 1 3880 ? 174.763 262.250 182.770 1.00 0.33  ? 3880 HIS A CE1   1 
ATOM   17755 N  NE2   . HIS A 1 3880 ? 175.985 261.766 182.899 1.00 0.51  ? 3880 HIS A NE2   1 
ATOM   17756 N  N     . ILE A 1 3881 ? 178.512 267.346 180.340 1.00 2.27  ? 3881 ILE A N     1 
ATOM   17757 C  CA    . ILE A 1 3881 ? 178.780 268.467 179.447 1.00 1.31  ? 3881 ILE A CA    1 
ATOM   17758 C  C     . ILE A 1 3881 ? 180.137 268.312 178.779 1.00 1.28  ? 3881 ILE A C     1 
ATOM   17759 O  O     . ILE A 1 3881 ? 180.312 268.700 177.619 1.00 1.44  ? 3881 ILE A O     1 
ATOM   17760 C  CB    . ILE A 1 3881 ? 178.656 269.803 180.211 1.00 1.17  ? 3881 ILE A CB    1 
ATOM   17761 C  CG1   . ILE A 1 3881 ? 178.718 270.988 179.241 1.00 3.08  ? 3881 ILE A CG1   1 
ATOM   17762 C  CG2   . ILE A 1 3881 ? 179.718 269.920 181.298 1.00 1.17  ? 3881 ILE A CG2   1 
ATOM   17763 C  CD1   . ILE A 1 3881 ? 177.680 270.940 178.149 1.00 0.92  ? 3881 ILE A CD1   1 
ATOM   17764 N  N     . THR A 1 3882 ? 181.117 267.739 179.483 1.00 1.26  ? 3882 THR A N     1 
ATOM   17765 C  CA    . THR A 1 3882 ? 182.447 267.571 178.911 1.00 2.08  ? 3882 THR A CA    1 
ATOM   17766 C  C     . THR A 1 3882 ? 182.420 266.630 177.713 1.00 1.25  ? 3882 THR A C     1 
ATOM   17767 O  O     . THR A 1 3882 ? 183.012 266.920 176.669 1.00 2.68  ? 3882 THR A O     1 
ATOM   17768 C  CB    . THR A 1 3882 ? 183.413 267.058 179.978 1.00 3.01  ? 3882 THR A CB    1 
ATOM   17769 O  OG1   . THR A 1 3882 ? 183.346 267.907 181.130 1.00 6.09  ? 3882 THR A OG1   1 
ATOM   17770 C  CG2   . THR A 1 3882 ? 184.834 267.049 179.450 1.00 2.14  ? 3882 THR A CG2   1 
ATOM   17771 N  N     . PHE A 1 3883 ? 181.738 265.490 177.849 1.00 1.10  ? 3883 PHE A N     1 
ATOM   17772 C  CA    . PHE A 1 3883 ? 181.631 264.555 176.734 1.00 0.78  ? 3883 PHE A CA    1 
ATOM   17773 C  C     . PHE A 1 3883 ? 180.818 265.143 175.586 1.00 0.68  ? 3883 PHE A C     1 
ATOM   17774 O  O     . PHE A 1 3883 ? 181.181 264.979 174.416 1.00 0.75  ? 3883 PHE A O     1 
ATOM   17775 C  CB    . PHE A 1 3883 ? 181.020 263.236 177.206 1.00 0.45  ? 3883 PHE A CB    1 
ATOM   17776 C  CG    . PHE A 1 3883 ? 181.035 262.156 176.165 1.00 0.29  ? 3883 PHE A CG    1 
ATOM   17777 C  CD1   . PHE A 1 3883 ? 182.136 261.978 175.348 1.00 0.35  ? 3883 PHE A CD1   1 
ATOM   17778 C  CD2   . PHE A 1 3883 ? 179.942 261.327 175.993 1.00 0.35  ? 3883 PHE A CD2   1 
ATOM   17779 C  CE1   . PHE A 1 3883 ? 182.149 260.991 174.385 1.00 0.40  ? 3883 PHE A CE1   1 
ATOM   17780 C  CE2   . PHE A 1 3883 ? 179.951 260.338 175.031 1.00 0.25  ? 3883 PHE A CE2   1 
ATOM   17781 C  CZ    . PHE A 1 3883 ? 181.055 260.170 174.227 1.00 0.22  ? 3883 PHE A CZ    1 
ATOM   17782 N  N     . ALA A 1 3884 ? 179.715 265.823 175.900 1.00 0.96  ? 3884 ALA A N     1 
ATOM   17783 C  CA    . ALA A 1 3884 ? 178.913 266.454 174.857 1.00 0.62  ? 3884 ALA A CA    1 
ATOM   17784 C  C     . ALA A 1 3884 ? 179.674 267.578 174.167 1.00 0.91  ? 3884 ALA A C     1 
ATOM   17785 O  O     . ALA A 1 3884 ? 179.475 267.815 172.971 1.00 0.84  ? 3884 ALA A O     1 
ATOM   17786 C  CB    . ALA A 1 3884 ? 177.602 266.975 175.441 1.00 0.59  ? 3884 ALA A CB    1 
ATOM   17787 N  N     . MET A 1 3885 ? 180.542 268.279 174.901 1.00 0.71  ? 3885 MET A N     1 
ATOM   17788 C  CA    . MET A 1 3885 ? 181.368 269.317 174.296 1.00 0.83  ? 3885 MET A CA    1 
ATOM   17789 C  C     . MET A 1 3885 ? 182.299 268.728 173.245 1.00 1.76  ? 3885 MET A C     1 
ATOM   17790 O  O     . MET A 1 3885 ? 182.510 269.321 172.181 1.00 2.05  ? 3885 MET A O     1 
ATOM   17791 C  CB    . MET A 1 3885 ? 182.179 270.035 175.374 1.00 3.43  ? 3885 MET A CB    1 
ATOM   17792 C  CG    . MET A 1 3885 ? 181.479 271.210 176.038 1.00 1.92  ? 3885 MET A CG    1 
ATOM   17793 S  SD    . MET A 1 3885 ? 180.934 272.487 174.898 1.00 16.65 ? 3885 MET A SD    1 
ATOM   17794 C  CE    . MET A 1 3885 ? 182.374 273.550 174.872 1.00 11.80 ? 3885 MET A CE    1 
ATOM   17795 N  N     . LEU A 1 3886 ? 182.871 267.556 173.530 1.00 1.30  ? 3886 LEU A N     1 
ATOM   17796 C  CA    . LEU A 1 3886 ? 183.790 266.925 172.591 1.00 1.05  ? 3886 LEU A CA    1 
ATOM   17797 C  C     . LEU A 1 3886 ? 183.054 266.358 171.386 1.00 1.42  ? 3886 LEU A C     1 
ATOM   17798 O  O     . LEU A 1 3886 ? 183.540 266.458 170.253 1.00 5.14  ? 3886 LEU A O     1 
ATOM   17799 C  CB    . LEU A 1 3886 ? 184.586 265.831 173.298 1.00 1.12  ? 3886 LEU A CB    1 
ATOM   17800 C  CG    . LEU A 1 3886 ? 185.456 266.302 174.464 1.00 1.45  ? 3886 LEU A CG    1 
ATOM   17801 C  CD1   . LEU A 1 3886 ? 185.889 265.118 175.302 1.00 1.59  ? 3886 LEU A CD1   1 
ATOM   17802 C  CD2   . LEU A 1 3886 ? 186.658 267.082 173.962 1.00 1.36  ? 3886 LEU A CD2   1 
ATOM   17803 N  N     . LEU A 1 3887 ? 181.882 265.756 171.605 1.00 0.86  ? 3887 LEU A N     1 
ATOM   17804 C  CA    . LEU A 1 3887 ? 181.102 265.243 170.482 1.00 1.39  ? 3887 LEU A CA    1 
ATOM   17805 C  C     . LEU A 1 3887 ? 180.681 266.373 169.553 1.00 1.84  ? 3887 LEU A C     1 
ATOM   17806 O  O     . LEU A 1 3887 ? 180.636 266.198 168.332 1.00 3.42  ? 3887 LEU A O     1 
ATOM   17807 C  CB    . LEU A 1 3887 ? 179.877 264.480 170.990 1.00 1.35  ? 3887 LEU A CB    1 
ATOM   17808 C  CG    . LEU A 1 3887 ? 180.125 263.203 171.793 1.00 1.07  ? 3887 LEU A CG    1 
ATOM   17809 C  CD1   . LEU A 1 3887 ? 178.804 262.582 172.221 1.00 0.35  ? 3887 LEU A CD1   1 
ATOM   17810 C  CD2   . LEU A 1 3887 ? 180.962 262.207 171.005 1.00 0.51  ? 3887 LEU A CD2   1 
ATOM   17811 N  N     . ALA A 1 3888 ? 180.368 267.540 170.120 1.00 2.17  ? 3888 ALA A N     1 
ATOM   17812 C  CA    . ALA A 1 3888 ? 180.064 268.706 169.298 1.00 2.50  ? 3888 ALA A CA    1 
ATOM   17813 C  C     . ALA A 1 3888 ? 181.272 269.132 168.477 1.00 3.16  ? 3888 ALA A C     1 
ATOM   17814 O  O     . ALA A 1 3888 ? 181.138 269.491 167.302 1.00 5.87  ? 3888 ALA A O     1 
ATOM   17815 C  CB    . ALA A 1 3888 ? 179.579 269.854 170.182 1.00 2.93  ? 3888 ALA A CB    1 
ATOM   17816 N  N     . ARG A 1 3889 ? 182.463 269.101 169.077 1.00 3.44  ? 3889 ARG A N     1 
ATOM   17817 C  CA    . ARG A 1 3889 ? 183.670 269.480 168.350 1.00 3.07  ? 3889 ARG A CA    1 
ATOM   17818 C  C     . ARG A 1 3889 ? 183.987 268.482 167.243 1.00 5.54  ? 3889 ARG A C     1 
ATOM   17819 O  O     . ARG A 1 3889 ? 184.478 268.867 166.178 1.00 12.10 ? 3889 ARG A O     1 
ATOM   17820 C  CB    . ARG A 1 3889 ? 184.845 269.609 169.318 1.00 4.44  ? 3889 ARG A CB    1 
ATOM   17821 C  CG    . ARG A 1 3889 ? 184.713 270.772 170.284 1.00 3.83  ? 3889 ARG A CG    1 
ATOM   17822 C  CD    . ARG A 1 3889 ? 186.047 271.433 170.555 1.00 3.81  ? 3889 ARG A CD    1 
ATOM   17823 N  NE    . ARG A 1 3889 ? 186.777 271.718 169.327 1.00 8.69  ? 3889 ARG A NE    1 
ATOM   17824 C  CZ    . ARG A 1 3889 ? 188.086 271.919 169.265 1.00 9.13  ? 3889 ARG A CZ    1 
ATOM   17825 N  NH1   . ARG A 1 3889 ? 188.847 271.860 170.346 1.00 5.19  ? 3889 ARG A NH1   1 
ATOM   17826 N  NH2   . ARG A 1 3889 ? 188.644 272.190 168.088 1.00 11.56 ? 3889 ARG A NH2   1 
ATOM   17827 N  N     . ILE A 1 3890 ? 183.727 267.194 167.482 1.00 3.33  ? 3890 ILE A N     1 
ATOM   17828 C  CA    . ILE A 1 3890 ? 183.882 266.198 166.427 1.00 2.97  ? 3890 ILE A CA    1 
ATOM   17829 C  C     . ILE A 1 3890 ? 182.885 266.449 165.304 1.00 4.24  ? 3890 ILE A C     1 
ATOM   17830 O  O     . ILE A 1 3890 ? 183.236 266.393 164.120 1.00 9.23  ? 3890 ILE A O     1 
ATOM   17831 C  CB    . ILE A 1 3890 ? 183.741 264.778 167.006 1.00 2.54  ? 3890 ILE A CB    1 
ATOM   17832 C  CG1   . ILE A 1 3890 ? 184.861 264.491 168.003 1.00 1.32  ? 3890 ILE A CG1   1 
ATOM   17833 C  CG2   . ILE A 1 3890 ? 183.742 263.740 165.896 1.00 2.00  ? 3890 ILE A CG2   1 
ATOM   17834 C  CD1   . ILE A 1 3890 ? 184.727 263.156 168.692 1.00 1.44  ? 3890 ILE A CD1   1 
ATOM   17835 N  N     . LYS A 1 3891 ? 181.626 266.729 165.652 1.00 3.66  ? 3891 LYS A N     1 
ATOM   17836 C  CA    . LYS A 1 3891 ? 180.620 267.012 164.633 1.00 3.54  ? 3891 LYS A CA    1 
ATOM   17837 C  C     . LYS A 1 3891 ? 180.938 268.290 163.871 1.00 8.81  ? 3891 LYS A C     1 
ATOM   17838 O  O     . LYS A 1 3891 ? 180.654 268.382 162.671 1.00 6.04  ? 3891 LYS A O     1 
ATOM   17839 C  CB    . LYS A 1 3891 ? 179.235 267.109 165.268 1.00 3.80  ? 3891 LYS A CB    1 
ATOM   17840 C  CG    . LYS A 1 3891 ? 178.094 267.001 164.269 1.00 3.36  ? 3891 LYS A CG    1 
ATOM   17841 C  CD    . LYS A 1 3891 ? 176.849 267.703 164.776 1.00 6.76  ? 3891 LYS A CD    1 
ATOM   17842 C  CE    . LYS A 1 3891 ? 175.701 267.577 163.788 1.00 9.23  ? 3891 LYS A CE    1 
ATOM   17843 N  NZ    . LYS A 1 3891 ? 174.389 267.885 164.423 1.00 9.56  ? 3891 LYS A NZ    1 
ATOM   17844 N  N     . LEU A 1 3892 ? 181.515 269.282 164.550 1.00 7.83  ? 3892 LEU A N     1 
ATOM   17845 C  CA    . LEU A 1 3892 ? 181.883 270.527 163.885 1.00 9.03  ? 3892 LEU A CA    1 
ATOM   17846 C  C     . LEU A 1 3892 ? 182.937 270.288 162.811 1.00 12.64 ? 3892 LEU A C     1 
ATOM   17847 O  O     . LEU A 1 3892 ? 182.877 270.884 161.730 1.00 18.84 ? 3892 LEU A O     1 
ATOM   17848 C  CB    . LEU A 1 3892 ? 182.378 271.535 164.921 1.00 10.91 ? 3892 LEU A CB    1 
ATOM   17849 C  CG    . LEU A 1 3892 ? 182.671 272.957 164.451 1.00 11.09 ? 3892 LEU A CG    1 
ATOM   17850 C  CD1   . LEU A 1 3892 ? 181.522 273.486 163.615 1.00 10.28 ? 3892 LEU A CD1   1 
ATOM   17851 C  CD2   . LEU A 1 3892 ? 182.919 273.849 165.652 1.00 11.23 ? 3892 LEU A CD2   1 
ATOM   17852 N  N     . LYS A 1 3893 ? 183.908 269.413 163.092 1.00 10.53 ? 3893 LYS A N     1 
ATOM   17853 C  CA    . LYS A 1 3893 ? 184.921 269.076 162.096 1.00 8.91  ? 3893 LYS A CA    1 
ATOM   17854 C  C     . LYS A 1 3893 ? 184.313 268.406 160.871 1.00 13.92 ? 3893 LYS A C     1 
ATOM   17855 O  O     . LYS A 1 3893 ? 184.861 268.518 159.769 1.00 25.43 ? 3893 LYS A O     1 
ATOM   17856 C  CB    . LYS A 1 3893 ? 185.983 268.172 162.720 1.00 11.48 ? 3893 LYS A CB    1 
ATOM   17857 C  CG    . LYS A 1 3893 ? 186.968 268.899 163.620 1.00 11.61 ? 3893 LYS A CG    1 
ATOM   17858 C  CD    . LYS A 1 3893 ? 188.080 267.973 164.067 1.00 10.27 ? 3893 LYS A CD    1 
ATOM   17859 C  CE    . LYS A 1 3893 ? 188.778 267.329 162.883 1.00 10.25 ? 3893 LYS A CE    1 
ATOM   17860 N  NZ    . LYS A 1 3893 ? 189.923 266.481 163.314 1.00 19.11 ? 3893 LYS A NZ    1 
ATOM   17861 N  N     . GLY A 1 3894 ? 183.194 267.701 161.037 1.00 14.16 ? 3894 GLY A N     1 
ATOM   17862 C  CA    . GLY A 1 3894 ? 182.559 267.040 159.912 1.00 12.21 ? 3894 GLY A CA    1 
ATOM   17863 C  C     . GLY A 1 3894 ? 181.853 267.980 158.959 1.00 17.24 ? 3894 GLY A C     1 
ATOM   17864 O  O     . GLY A 1 3894 ? 181.578 267.598 157.819 1.00 25.37 ? 3894 GLY A O     1 
ATOM   17865 N  N     . THR A 1 3895 ? 181.557 269.201 159.398 1.00 20.73 ? 3895 THR A N     1 
ATOM   17866 C  CA    . THR A 1 3895 ? 180.859 270.174 158.565 1.00 21.16 ? 3895 THR A CA    1 
ATOM   17867 C  C     . THR A 1 3895 ? 181.865 270.841 157.634 1.00 25.29 ? 3895 THR A C     1 
ATOM   17868 O  O     . THR A 1 3895 ? 182.769 271.551 158.090 1.00 25.69 ? 3895 THR A O     1 
ATOM   17869 C  CB    . THR A 1 3895 ? 180.149 271.209 159.431 1.00 21.10 ? 3895 THR A CB    1 
ATOM   17870 O  OG1   . THR A 1 3895 ? 179.206 270.554 160.288 1.00 18.37 ? 3895 THR A OG1   1 
ATOM   17871 C  CG2   . THR A 1 3895 ? 179.408 272.204 158.553 1.00 19.24 ? 3895 THR A CG2   1 
ATOM   17872 N  N     . VAL A 1 3896 ? 181.711 270.612 156.328 1.00 24.38 ? 3896 VAL A N     1 
ATOM   17873 C  CA    . VAL A 1 3896 ? 182.634 271.185 155.353 1.00 25.72 ? 3896 VAL A CA    1 
ATOM   17874 C  C     . VAL A 1 3896 ? 182.494 272.703 155.307 1.00 24.22 ? 3896 VAL A C     1 
ATOM   17875 O  O     . VAL A 1 3896 ? 183.482 273.427 155.146 1.00 28.09 ? 3896 VAL A O     1 
ATOM   17876 C  CB    . VAL A 1 3896 ? 182.407 270.550 153.970 1.00 27.19 ? 3896 VAL A CB    1 
ATOM   17877 C  CG1   . VAL A 1 3896 ? 183.376 271.126 152.949 1.00 27.09 ? 3896 VAL A CG1   1 
ATOM   17878 C  CG2   . VAL A 1 3896 ? 182.549 269.037 154.052 1.00 20.76 ? 3896 VAL A CG2   1 
ATOM   17879 N  N     . GLY A 1 3897 ? 181.273 273.207 155.461 1.00 23.13 ? 3897 GLY A N     1 
ATOM   17880 C  CA    . GLY A 1 3897 ? 181.014 274.630 155.412 1.00 21.82 ? 3897 GLY A CA    1 
ATOM   17881 C  C     . GLY A 1 3897 ? 181.389 275.413 156.648 1.00 25.95 ? 3897 GLY A C     1 
ATOM   17882 O  O     . GLY A 1 3897 ? 181.248 276.640 156.655 1.00 24.45 ? 3897 GLY A O     1 
ATOM   17883 N  N     . GLU A 1 3898 ? 181.869 274.745 157.708 1.00 21.54 ? 3898 GLU A N     1 
ATOM   17884 C  CA    . GLU A 1 3898 ? 182.241 275.505 158.887 1.00 19.21 ? 3898 GLU A CA    1 
ATOM   17885 C  C     . GLU A 1 3898 ? 183.753 275.680 158.967 1.00 19.90 ? 3898 GLU A C     1 
ATOM   17886 O  O     . GLU A 1 3898 ? 184.511 274.808 158.531 1.00 23.28 ? 3898 GLU A O     1 
ATOM   17887 C  CB    . GLU A 1 3898 ? 181.751 274.812 160.162 1.00 18.00 ? 3898 GLU A CB    1 
ATOM   17888 C  CG    . GLU A 1 3898 ? 180.286 275.057 160.485 1.00 17.86 ? 3898 GLU A CG    1 
ATOM   17889 C  CD    . GLU A 1 3898 ? 179.955 276.523 160.633 1.00 18.55 ? 3898 GLU A CD    1 
ATOM   17890 O  OE1   . GLU A 1 3898 ? 180.536 277.182 161.520 1.00 17.01 ? 3898 GLU A OE1   1 
ATOM   17891 O  OE2   . GLU A 1 3898 ? 179.110 277.017 159.859 1.00 24.41 ? 3898 GLU A OE2   1 
ATOM   17892 N  N     . PRO A 1 3899 ? 184.217 276.799 159.514 1.00 19.15 ? 3899 PRO A N     1 
ATOM   17893 C  CA    . PRO A 1 3899 ? 185.653 276.966 159.766 1.00 17.01 ? 3899 PRO A CA    1 
ATOM   17894 C  C     . PRO A 1 3899 ? 186.120 276.071 160.905 1.00 19.92 ? 3899 PRO A C     1 
ATOM   17895 O  O     . PRO A 1 3899 ? 185.336 275.413 161.591 1.00 21.33 ? 3899 PRO A O     1 
ATOM   17896 C  CB    . PRO A 1 3899 ? 185.795 278.448 160.129 1.00 11.58 ? 3899 PRO A CB    1 
ATOM   17897 C  CG    . PRO A 1 3899 ? 184.514 279.089 159.693 1.00 14.03 ? 3899 PRO A CG    1 
ATOM   17898 C  CD    . PRO A 1 3899 ? 183.463 278.033 159.783 1.00 16.05 ? 3899 PRO A CD    1 
ATOM   17899 N  N     . THR A 1 3900 ? 187.438 276.058 161.101 1.00 20.23 ? 3900 THR A N     1 
ATOM   17900 C  CA    . THR A 1 3900 ? 188.035 275.202 162.121 1.00 19.11 ? 3900 THR A CA    1 
ATOM   17901 C  C     . THR A 1 3900 ? 187.820 275.748 163.527 1.00 16.18 ? 3900 THR A C     1 
ATOM   17902 O  O     . THR A 1 3900 ? 187.631 274.971 164.471 1.00 16.65 ? 3900 THR A O     1 
ATOM   17903 C  CB    . THR A 1 3900 ? 189.531 275.028 161.851 1.00 17.93 ? 3900 THR A CB    1 
ATOM   17904 O  OG1   . THR A 1 3900 ? 190.235 276.195 162.292 1.00 19.77 ? 3900 THR A OG1   1 
ATOM   17905 C  CG2   . THR A 1 3900 ? 189.785 274.822 160.367 1.00 19.32 ? 3900 THR A CG2   1 
ATOM   17906 N  N     . TYR A 1 3901 ? 187.857 277.071 163.686 1.00 15.44 ? 3901 TYR A N     1 
ATOM   17907 C  CA    . TYR A 1 3901 ? 187.806 277.724 164.996 1.00 13.36 ? 3901 TYR A CA    1 
ATOM   17908 C  C     . TYR A 1 3901 ? 188.906 277.220 165.925 1.00 16.94 ? 3901 TYR A C     1 
ATOM   17909 O  O     . TYR A 1 3901 ? 188.733 277.183 167.146 1.00 19.10 ? 3901 TYR A O     1 
ATOM   17910 C  CB    . TYR A 1 3901 ? 186.438 277.557 165.663 1.00 11.24 ? 3901 TYR A CB    1 
ATOM   17911 C  CG    . TYR A 1 3901 ? 185.260 277.923 164.793 1.00 12.64 ? 3901 TYR A CG    1 
ATOM   17912 C  CD1   . TYR A 1 3901 ? 184.970 279.250 164.507 1.00 9.25  ? 3901 TYR A CD1   1 
ATOM   17913 C  CD2   . TYR A 1 3901 ? 184.428 276.942 164.271 1.00 11.07 ? 3901 TYR A CD2   1 
ATOM   17914 C  CE1   . TYR A 1 3901 ? 183.892 279.589 163.717 1.00 8.60  ? 3901 TYR A CE1   1 
ATOM   17915 C  CE2   . TYR A 1 3901 ? 183.347 277.271 163.485 1.00 12.37 ? 3901 TYR A CE2   1 
ATOM   17916 C  CZ    . TYR A 1 3901 ? 183.083 278.597 163.210 1.00 13.22 ? 3901 TYR A CZ    1 
ATOM   17917 O  OH    . TYR A 1 3901 ? 182.004 278.927 162.424 1.00 17.14 ? 3901 TYR A OH    1 
ATOM   17918 N  N     . ASP A 1 3902 ? 190.050 276.830 165.357 1.00 16.11 ? 3902 ASP A N     1 
ATOM   17919 C  CA    . ASP A 1 3902 ? 191.129 276.283 166.172 1.00 16.25 ? 3902 ASP A CA    1 
ATOM   17920 C  C     . ASP A 1 3902 ? 191.690 277.329 167.127 1.00 18.72 ? 3902 ASP A C     1 
ATOM   17921 O  O     . ASP A 1 3902 ? 191.997 277.021 168.283 1.00 21.46 ? 3902 ASP A O     1 
ATOM   17922 C  CB    . ASP A 1 3902 ? 192.233 275.723 165.275 1.00 21.74 ? 3902 ASP A CB    1 
ATOM   17923 C  CG    . ASP A 1 3902 ? 191.804 274.467 164.543 1.00 29.64 ? 3902 ASP A CG    1 
ATOM   17924 O  OD1   . ASP A 1 3902 ? 190.676 273.991 164.793 1.00 26.85 ? 3902 ASP A OD1   1 
ATOM   17925 O  OD2   . ASP A 1 3902 ? 192.592 273.957 163.721 1.00 31.50 ? 3902 ASP A OD2   1 
ATOM   17926 N  N     . ALA A 1 3903 ? 191.835 278.572 166.660 1.00 16.87 ? 3903 ALA A N     1 
ATOM   17927 C  CA    . ALA A 1 3903 ? 192.344 279.629 167.527 1.00 19.13 ? 3903 ALA A CA    1 
ATOM   17928 C  C     . ALA A 1 3903 ? 191.386 279.915 168.678 1.00 17.52 ? 3903 ALA A C     1 
ATOM   17929 O  O     . ALA A 1 3903 ? 191.817 280.081 169.825 1.00 19.93 ? 3903 ALA A O     1 
ATOM   17930 C  CB    . ALA A 1 3903 ? 192.596 280.897 166.711 1.00 15.49 ? 3903 ALA A CB    1 
ATOM   17931 N  N     . GLU A 1 3904 ? 190.085 279.979 168.390 1.00 15.16 ? 3904 GLU A N     1 
ATOM   17932 C  CA    . GLU A 1 3904 ? 189.106 280.236 169.444 1.00 14.43 ? 3904 GLU A CA    1 
ATOM   17933 C  C     . GLU A 1 3904 ? 189.060 279.101 170.459 1.00 16.42 ? 3904 GLU A C     1 
ATOM   17934 O  O     . GLU A 1 3904 ? 188.963 279.347 171.667 1.00 23.24 ? 3904 GLU A O     1 
ATOM   17935 C  CB    . GLU A 1 3904 ? 187.729 280.482 168.829 1.00 17.08 ? 3904 GLU A CB    1 
ATOM   17936 C  CG    . GLU A 1 3904 ? 187.630 281.772 168.019 1.00 20.28 ? 3904 GLU A CG    1 
ATOM   17937 C  CD    . GLU A 1 3904 ? 188.154 281.636 166.604 1.00 24.44 ? 3904 GLU A CD    1 
ATOM   17938 O  OE1   . GLU A 1 3904 ? 188.546 280.518 166.215 1.00 22.42 ? 3904 GLU A OE1   1 
ATOM   17939 O  OE2   . GLU A 1 3904 ? 188.176 282.654 165.880 1.00 26.53 ? 3904 GLU A OE2   1 
ATOM   17940 N  N     . PHE A 1 3905 ? 189.125 277.851 169.996 1.00 12.56 ? 3905 PHE A N     1 
ATOM   17941 C  CA    . PHE A 1 3905 ? 189.203 276.741 170.940 1.00 10.17 ? 3905 PHE A CA    1 
ATOM   17942 C  C     . PHE A 1 3905 ? 190.565 276.686 171.620 1.00 13.78 ? 3905 PHE A C     1 
ATOM   17943 O  O     . PHE A 1 3905 ? 190.669 276.206 172.754 1.00 18.47 ? 3905 PHE A O     1 
ATOM   17944 C  CB    . PHE A 1 3905 ? 188.897 275.416 170.242 1.00 13.24 ? 3905 PHE A CB    1 
ATOM   17945 C  CG    . PHE A 1 3905 ? 187.433 275.183 170.008 1.00 7.06  ? 3905 PHE A CG    1 
ATOM   17946 C  CD1   . PHE A 1 3905 ? 186.570 275.016 171.075 1.00 5.03  ? 3905 PHE A CD1   1 
ATOM   17947 C  CD2   . PHE A 1 3905 ? 186.925 275.123 168.723 1.00 7.15  ? 3905 PHE A CD2   1 
ATOM   17948 C  CE1   . PHE A 1 3905 ? 185.224 274.805 170.866 1.00 6.98  ? 3905 PHE A CE1   1 
ATOM   17949 C  CE2   . PHE A 1 3905 ? 185.579 274.908 168.508 1.00 8.41  ? 3905 PHE A CE2   1 
ATOM   17950 C  CZ    . PHE A 1 3905 ? 184.727 274.749 169.581 1.00 10.25 ? 3905 PHE A CZ    1 
ATOM   17951 N  N     . GLN A 1 3906 ? 191.612 277.167 170.947 1.00 16.31 ? 3906 GLN A N     1 
ATOM   17952 C  CA    . GLN A 1 3906 ? 192.908 277.297 171.602 1.00 14.87 ? 3906 GLN A CA    1 
ATOM   17953 C  C     . GLN A 1 3906 ? 192.834 278.285 172.756 1.00 17.32 ? 3906 GLN A C     1 
ATOM   17954 O  O     . GLN A 1 3906 ? 193.441 278.070 173.810 1.00 18.78 ? 3906 GLN A O     1 
ATOM   17955 C  CB    . GLN A 1 3906 ? 193.967 277.735 170.591 1.00 16.96 ? 3906 GLN A CB    1 
ATOM   17956 C  CG    . GLN A 1 3906 ? 195.376 277.833 171.149 1.00 18.38 ? 3906 GLN A CG    1 
ATOM   17957 C  CD    . GLN A 1 3906 ? 195.899 276.503 171.648 1.00 28.40 ? 3906 GLN A CD    1 
ATOM   17958 O  OE1   . GLN A 1 3906 ? 195.969 276.261 172.850 1.00 27.89 ? 3906 GLN A OE1   1 
ATOM   17959 N  NE2   . GLN A 1 3906 ? 196.273 275.629 170.720 1.00 24.72 ? 3906 GLN A NE2   1 
ATOM   17960 N  N     . HIS A 1 3907 ? 192.091 279.379 172.573 1.00 15.08 ? 3907 HIS A N     1 
ATOM   17961 C  CA    . HIS A 1 3907 ? 191.925 280.349 173.648 1.00 13.51 ? 3907 HIS A CA    1 
ATOM   17962 C  C     . HIS A 1 3907 ? 190.945 279.861 174.707 1.00 17.04 ? 3907 HIS A C     1 
ATOM   17963 O  O     . HIS A 1 3907 ? 191.116 280.158 175.893 1.00 20.96 ? 3907 HIS A O     1 
ATOM   17964 C  CB    . HIS A 1 3907 ? 191.462 281.691 173.085 1.00 20.07 ? 3907 HIS A CB    1 
ATOM   17965 C  CG    . HIS A 1 3907 ? 191.569 282.814 174.065 1.00 19.22 ? 3907 HIS A CG    1 
ATOM   17966 N  ND1   . HIS A 1 3907 ? 192.766 283.426 174.367 1.00 19.23 ? 3907 HIS A ND1   1 
ATOM   17967 C  CD2   . HIS A 1 3907 ? 190.632 283.420 174.831 1.00 17.67 ? 3907 HIS A CD2   1 
ATOM   17968 C  CE1   . HIS A 1 3907 ? 192.559 284.368 175.270 1.00 22.86 ? 3907 HIS A CE1   1 
ATOM   17969 N  NE2   . HIS A 1 3907 ? 191.273 284.385 175.569 1.00 24.61 ? 3907 HIS A NE2   1 
ATOM   17970 N  N     . PHE A 1 3908 ? 189.910 279.124 174.298 1.00 15.09 ? 3908 PHE A N     1 
ATOM   17971 C  CA    . PHE A 1 3908 ? 188.935 278.621 175.260 1.00 14.69 ? 3908 PHE A CA    1 
ATOM   17972 C  C     . PHE A 1 3908 ? 189.590 277.666 176.249 1.00 12.70 ? 3908 PHE A C     1 
ATOM   17973 O  O     . PHE A 1 3908 ? 189.357 277.751 177.460 1.00 13.63 ? 3908 PHE A O     1 
ATOM   17974 C  CB    . PHE A 1 3908 ? 187.780 277.944 174.524 1.00 11.81 ? 3908 PHE A CB    1 
ATOM   17975 C  CG    . PHE A 1 3908 ? 186.688 277.456 175.430 1.00 10.99 ? 3908 PHE A CG    1 
ATOM   17976 C  CD1   . PHE A 1 3908 ? 185.928 278.350 176.163 1.00 9.43  ? 3908 PHE A CD1   1 
ATOM   17977 C  CD2   . PHE A 1 3908 ? 186.402 276.105 175.526 1.00 11.32 ? 3908 PHE A CD2   1 
ATOM   17978 C  CE1   . PHE A 1 3908 ? 184.923 277.906 176.991 1.00 11.19 ? 3908 PHE A CE1   1 
ATOM   17979 C  CE2   . PHE A 1 3908 ? 185.388 275.656 176.347 1.00 13.55 ? 3908 PHE A CE2   1 
ATOM   17980 C  CZ    . PHE A 1 3908 ? 184.645 276.557 177.078 1.00 9.38  ? 3908 PHE A CZ    1 
ATOM   17981 N  N     . LEU A 1 3909 ? 190.417 276.754 175.751 1.00 10.26 ? 3909 LEU A N     1 
ATOM   17982 C  CA    . LEU A 1 3909 ? 191.248 275.942 176.620 1.00 10.25 ? 3909 LEU A CA    1 
ATOM   17983 C  C     . LEU A 1 3909 ? 192.490 276.730 177.025 1.00 17.73 ? 3909 LEU A C     1 
ATOM   17984 O  O     . LEU A 1 3909 ? 192.805 277.776 176.450 1.00 22.32 ? 3909 LEU A O     1 
ATOM   17985 C  CB    . LEU A 1 3909 ? 191.636 274.638 175.929 1.00 13.05 ? 3909 LEU A CB    1 
ATOM   17986 C  CG    . LEU A 1 3909 ? 190.496 273.817 175.323 1.00 13.56 ? 3909 LEU A CG    1 
ATOM   17987 C  CD1   . LEU A 1 3909 ? 191.022 272.507 174.765 1.00 16.38 ? 3909 LEU A CD1   1 
ATOM   17988 C  CD2   . LEU A 1 3909 ? 189.405 273.566 176.348 1.00 10.10 ? 3909 LEU A CD2   1 
ATOM   17989 N  N     . ARG A 1 3910 ? 193.198 276.220 178.033 1.00 19.10 ? 3910 ARG A N     1 
ATOM   17990 C  CA    . ARG A 1 3910 ? 194.402 276.875 178.535 1.00 26.49 ? 3910 ARG A CA    1 
ATOM   17991 C  C     . ARG A 1 3910 ? 194.104 278.331 178.874 1.00 32.31 ? 3910 ARG A C     1 
ATOM   17992 O  O     . ARG A 1 3910 ? 193.574 278.625 179.952 1.00 29.90 ? 3910 ARG A O     1 
ATOM   17993 C  CB    . ARG A 1 3910 ? 195.537 276.763 177.509 1.00 21.06 ? 3910 ARG A CB    1 
ATOM   17994 C  CG    . ARG A 1 3910 ? 195.823 275.327 177.099 1.00 26.55 ? 3910 ARG A CG    1 
ATOM   17995 C  CD    . ARG A 1 3910 ? 196.598 275.212 175.800 1.00 23.50 ? 3910 ARG A CD    1 
ATOM   17996 N  NE    . ARG A 1 3910 ? 197.994 275.607 175.943 1.00 36.38 ? 3910 ARG A NE    1 
ATOM   17997 C  CZ    . ARG A 1 3910 ? 198.923 275.423 175.016 1.00 37.67 ? 3910 ARG A CZ    1 
ATOM   17998 N  NH1   . ARG A 1 3910 ? 198.641 274.840 173.862 1.00 28.79 ? 3910 ARG A NH1   1 
ATOM   17999 N  NH2   . ARG A 1 3910 ? 200.167 275.831 175.251 1.00 38.44 ? 3910 ARG A NH2   1 
ATOM   18000 N  N     . GLY A 1 3911 ? 194.435 279.246 177.965 1.00 23.19 ? 3911 GLY A N     1 
ATOM   18001 C  CA    . GLY A 1 3911 ? 194.027 280.633 178.107 1.00 22.47 ? 3911 GLY A CA    1 
ATOM   18002 C  C     . GLY A 1 3911 ? 194.784 281.403 179.167 1.00 23.75 ? 3911 GLY A C     1 
ATOM   18003 O  O     . GLY A 1 3911 ? 195.267 282.511 178.913 1.00 28.10 ? 3911 GLY A O     1 
ATOM   18004 N  N     . ASN A 1 3912 ? 194.884 280.830 180.366 1.00 26.39 ? 3912 ASN A N     1 
ATOM   18005 C  CA    . ASN A 1 3912 ? 195.643 281.448 181.445 1.00 26.32 ? 3912 ASN A CA    1 
ATOM   18006 C  C     . ASN A 1 3912 ? 197.139 281.493 181.162 1.00 30.39 ? 3912 ASN A C     1 
ATOM   18007 O  O     . ASN A 1 3912 ? 197.859 282.212 181.863 1.00 39.00 ? 3912 ASN A O     1 
ATOM   18008 C  CB    . ASN A 1 3912 ? 195.387 280.700 182.755 1.00 22.44 ? 3912 ASN A CB    1 
ATOM   18009 C  CG    . ASN A 1 3912 ? 195.585 279.201 182.619 1.00 35.31 ? 3912 ASN A CG    1 
ATOM   18010 O  OD1   . ASN A 1 3912 ? 195.928 278.701 181.547 1.00 37.44 ? 3912 ASN A OD1   1 
ATOM   18011 N  ND2   . ASN A 1 3912 ? 195.368 278.475 183.709 1.00 37.61 ? 3912 ASN A ND2   1 
ATOM   18012 N  N     . GLU A 1 3913 ? 197.617 280.751 180.161 1.00 23.90 ? 3913 GLU A N     1 
ATOM   18013 C  CA    . GLU A 1 3913 ? 199.040 280.735 179.849 1.00 28.83 ? 3913 GLU A CA    1 
ATOM   18014 C  C     . GLU A 1 3913 ? 199.529 282.062 179.283 1.00 34.17 ? 3913 GLU A C     1 
ATOM   18015 O  O     . GLU A 1 3913 ? 200.742 282.296 179.250 1.00 35.21 ? 3913 GLU A O     1 
ATOM   18016 C  CB    . GLU A 1 3913 ? 199.346 279.606 178.865 1.00 32.48 ? 3913 GLU A CB    1 
ATOM   18017 C  CG    . GLU A 1 3913 ? 198.984 278.226 179.382 1.00 29.44 ? 3913 GLU A CG    1 
ATOM   18018 C  CD    . GLU A 1 3913 ? 199.226 277.140 178.358 1.00 35.38 ? 3913 GLU A CD    1 
ATOM   18019 O  OE1   . GLU A 1 3913 ? 199.576 277.473 177.207 1.00 37.72 ? 3913 GLU A OE1   1 
ATOM   18020 O  OE2   . GLU A 1 3913 ? 199.066 275.950 178.702 1.00 36.99 ? 3913 GLU A OE2   1 
ATOM   18021 N  N     . ILE A 1 3914 ? 198.621 282.930 178.842 1.00 28.08 ? 3914 ILE A N     1 
ATOM   18022 C  CA    . ILE A 1 3914 ? 199.004 284.238 178.327 1.00 24.43 ? 3914 ILE A CA    1 
ATOM   18023 C  C     . ILE A 1 3914 ? 199.322 285.146 179.505 1.00 28.77 ? 3914 ILE A C     1 
ATOM   18024 O  O     . ILE A 1 3914 ? 198.424 285.748 180.103 1.00 27.68 ? 3914 ILE A O     1 
ATOM   18025 C  CB    . ILE A 1 3914 ? 197.897 284.838 177.439 1.00 26.21 ? 3914 ILE A CB    1 
ATOM   18026 C  CG1   . ILE A 1 3914 ? 197.479 283.838 176.360 1.00 20.17 ? 3914 ILE A CG1   1 
ATOM   18027 C  CG2   . ILE A 1 3914 ? 198.361 286.146 176.819 1.00 24.66 ? 3914 ILE A CG2   1 
ATOM   18028 C  CD1   . ILE A 1 3914 ? 196.413 284.357 175.422 1.00 17.14 ? 3914 ILE A CD1   1 
ATOM   18029 N  N     . VAL A 1 3915 ? 200.607 285.248 179.844 1.00 30.17 ? 3915 VAL A N     1 
ATOM   18030 C  CA    . VAL A 1 3915 ? 201.025 285.994 181.024 1.00 25.66 ? 3915 VAL A CA    1 
ATOM   18031 C  C     . VAL A 1 3915 ? 200.874 287.487 180.769 1.00 30.83 ? 3915 VAL A C     1 
ATOM   18032 O  O     . VAL A 1 3915 ? 201.315 288.005 179.734 1.00 27.74 ? 3915 VAL A O     1 
ATOM   18033 C  CB    . VAL A 1 3915 ? 202.469 285.634 181.402 1.00 32.28 ? 3915 VAL A CB    1 
ATOM   18034 C  CG1   . VAL A 1 3915 ? 202.921 286.439 182.610 1.00 28.07 ? 3915 VAL A CG1   1 
ATOM   18035 C  CG2   . VAL A 1 3915 ? 202.585 284.142 181.676 1.00 30.55 ? 3915 VAL A CG2   1 
ATOM   18036 N  N     . LEU A 1 3916 ? 200.250 288.184 181.712 1.00 27.50 ? 3916 LEU A N     1 
ATOM   18037 C  CA    . LEU A 1 3916 ? 200.019 289.618 181.619 1.00 28.77 ? 3916 LEU A CA    1 
ATOM   18038 C  C     . LEU A 1 3916 ? 200.832 290.336 182.686 1.00 34.60 ? 3916 LEU A C     1 
ATOM   18039 O  O     . LEU A 1 3916 ? 200.768 289.977 183.867 1.00 36.99 ? 3916 LEU A O     1 
ATOM   18040 C  CB    . LEU A 1 3916 ? 198.534 289.946 181.784 1.00 28.93 ? 3916 LEU A CB    1 
ATOM   18041 C  CG    . LEU A 1 3916 ? 197.564 289.211 180.861 1.00 29.68 ? 3916 LEU A CG    1 
ATOM   18042 C  CD1   . LEU A 1 3916 ? 196.143 289.696 181.103 1.00 27.15 ? 3916 LEU A CD1   1 
ATOM   18043 C  CD2   . LEU A 1 3916 ? 197.962 289.398 179.408 1.00 27.69 ? 3916 LEU A CD2   1 
ATOM   18044 N  N     . SER A 1 3917 ? 201.591 291.346 182.268 1.00 32.55 ? 3917 SER A N     1 
ATOM   18045 C  CA    . SER A 1 3917 ? 202.344 292.164 183.203 1.00 33.84 ? 3917 SER A CA    1 
ATOM   18046 C  C     . SER A 1 3917 ? 201.422 293.173 183.888 1.00 38.29 ? 3917 SER A C     1 
ATOM   18047 O  O     . SER A 1 3917 ? 200.244 293.309 183.549 1.00 37.87 ? 3917 SER A O     1 
ATOM   18048 C  CB    . SER A 1 3917 ? 203.486 292.882 182.487 1.00 34.97 ? 3917 SER A CB    1 
ATOM   18049 O  OG    . SER A 1 3917 ? 204.350 291.958 181.850 1.00 33.72 ? 3917 SER A OG    1 
ATOM   18050 N  N     . ALA A 1 3918 ? 201.978 293.880 184.874 1.00 35.18 ? 3918 ALA A N     1 
ATOM   18051 C  CA    . ALA A 1 3918 ? 201.194 294.875 185.600 1.00 31.72 ? 3918 ALA A CA    1 
ATOM   18052 C  C     . ALA A 1 3918 ? 200.740 296.001 184.679 1.00 31.16 ? 3918 ALA A C     1 
ATOM   18053 O  O     . ALA A 1 3918 ? 199.583 296.437 184.740 1.00 35.85 ? 3918 ALA A O     1 
ATOM   18054 C  CB    . ALA A 1 3918 ? 202.005 295.432 186.770 1.00 27.24 ? 3918 ALA A CB    1 
ATOM   18055 N  N     . GLY A 1 3919 ? 201.636 296.486 183.816 1.00 29.92 ? 3919 GLY A N     1 
ATOM   18056 C  CA    . GLY A 1 3919 ? 201.251 297.520 182.871 1.00 29.32 ? 3919 GLY A CA    1 
ATOM   18057 C  C     . GLY A 1 3919 ? 200.423 296.994 181.718 1.00 33.40 ? 3919 GLY A C     1 
ATOM   18058 O  O     . GLY A 1 3919 ? 199.717 297.762 181.056 1.00 33.87 ? 3919 GLY A O     1 
ATOM   18059 N  N     . SER A 1 3920 ? 200.497 295.687 181.455 1.00 33.65 ? 3920 SER A N     1 
ATOM   18060 C  CA    . SER A 1 3920 ? 199.720 295.105 180.365 1.00 33.65 ? 3920 SER A CA    1 
ATOM   18061 C  C     . SER A 1 3920 ? 198.227 295.159 180.660 1.00 33.41 ? 3920 SER A C     1 
ATOM   18062 O  O     . SER A 1 3920 ? 197.415 295.384 179.754 1.00 31.21 ? 3920 SER A O     1 
ATOM   18063 C  CB    . SER A 1 3920 ? 200.167 293.666 180.112 1.00 32.45 ? 3920 SER A CB    1 
ATOM   18064 O  OG    . SER A 1 3920 ? 201.563 293.597 179.878 1.00 36.94 ? 3920 SER A OG    1 
ATOM   18065 N  N     . THR A 1 3921 ? 197.841 294.952 181.920 1.00 30.86 ? 3921 THR A N     1 
ATOM   18066 C  CA    . THR A 1 3921 ? 196.436 294.946 182.290 1.00 29.52 ? 3921 THR A CA    1 
ATOM   18067 C  C     . THR A 1 3921 ? 196.062 296.293 182.882 1.00 28.40 ? 3921 THR A C     1 
ATOM   18068 O  O     . THR A 1 3921 ? 196.514 296.619 183.990 1.00 29.08 ? 3921 THR A O     1 
ATOM   18069 C  CB    . THR A 1 3921 ? 196.143 293.829 183.289 1.00 28.10 ? 3921 THR A CB    1 
ATOM   18070 O  OG1   . THR A 1 3921 ? 196.470 292.562 182.703 1.00 30.51 ? 3921 THR A OG1   1 
ATOM   18071 C  CG2   . THR A 1 3921 ? 194.674 293.836 183.680 1.00 26.28 ? 3921 THR A CG2   1 
ATOM   18072 N  N     . PRO A 1 3922 ? 195.253 297.101 182.206 1.00 25.91 ? 3922 PRO A N     1 
ATOM   18073 C  CA    . PRO A 1 3922 ? 194.812 298.376 182.769 1.00 27.24 ? 3922 PRO A CA    1 
ATOM   18074 C  C     . PRO A 1 3922 ? 193.622 298.160 183.697 1.00 33.11 ? 3922 PRO A C     1 
ATOM   18075 O  O     . PRO A 1 3922 ? 193.221 297.034 183.987 1.00 37.21 ? 3922 PRO A O     1 
ATOM   18076 C  CB    . PRO A 1 3922 ? 194.425 299.181 181.527 1.00 31.92 ? 3922 PRO A CB    1 
ATOM   18077 C  CG    . PRO A 1 3922 ? 193.929 298.146 180.576 1.00 29.65 ? 3922 PRO A CG    1 
ATOM   18078 C  CD    . PRO A 1 3922 ? 194.754 296.901 180.833 1.00 29.63 ? 3922 PRO A CD    1 
ATOM   18079 N  N     . ARG A 1 3923 ? 193.058 299.269 184.169 1.00 32.60 ? 3923 ARG A N     1 
ATOM   18080 C  CA    . ARG A 1 3923 ? 191.875 299.243 185.025 1.00 30.09 ? 3923 ARG A CA    1 
ATOM   18081 C  C     . ARG A 1 3923 ? 190.690 299.738 184.206 1.00 34.03 ? 3923 ARG A C     1 
ATOM   18082 O  O     . ARG A 1 3923 ? 190.516 300.944 184.010 1.00 35.02 ? 3923 ARG A O     1 
ATOM   18083 C  CB    . ARG A 1 3923 ? 192.082 300.090 186.277 1.00 32.40 ? 3923 ARG A CB    1 
ATOM   18084 C  CG    . ARG A 1 3923 ? 190.860 300.164 187.178 1.00 33.62 ? 3923 ARG A CG    1 
ATOM   18085 C  CD    . ARG A 1 3923 ? 191.057 301.160 188.307 1.00 31.12 ? 3923 ARG A CD    1 
ATOM   18086 N  NE    . ARG A 1 3923 ? 191.281 302.511 187.807 1.00 42.52 ? 3923 ARG A NE    1 
ATOM   18087 C  CZ    . ARG A 1 3923 ? 191.444 303.577 188.578 1.00 42.29 ? 3923 ARG A CZ    1 
ATOM   18088 N  NH1   . ARG A 1 3923 ? 191.411 303.488 189.897 1.00 36.12 ? 3923 ARG A NH1   1 
ATOM   18089 N  NH2   . ARG A 1 3923 ? 191.642 304.763 188.010 1.00 39.72 ? 3923 ARG A NH2   1 
ATOM   18090 N  N     . ILE A 1 3924 ? 189.875 298.807 183.724 1.00 33.73 ? 3924 ILE A N     1 
ATOM   18091 C  CA    . ILE A 1 3924 ? 188.655 299.142 182.998 1.00 30.12 ? 3924 ILE A CA    1 
ATOM   18092 C  C     . ILE A 1 3924 ? 187.549 299.381 184.016 1.00 29.87 ? 3924 ILE A C     1 
ATOM   18093 O  O     . ILE A 1 3924 ? 187.244 298.504 184.832 1.00 33.07 ? 3924 ILE A O     1 
ATOM   18094 C  CB    . ILE A 1 3924 ? 188.260 298.034 182.009 1.00 31.62 ? 3924 ILE A CB    1 
ATOM   18095 C  CG1   . ILE A 1 3924 ? 189.358 297.812 180.966 1.00 30.56 ? 3924 ILE A CG1   1 
ATOM   18096 C  CG2   . ILE A 1 3924 ? 186.943 298.380 181.331 1.00 29.66 ? 3924 ILE A CG2   1 
ATOM   18097 C  CD1   . ILE A 1 3924 ? 190.311 296.684 181.301 1.00 25.26 ? 3924 ILE A CD1   1 
ATOM   18098 N  N     . GLN A 1 3925 ? 186.951 300.570 183.976 1.00 32.11 ? 3925 GLN A N     1 
ATOM   18099 C  CA    . GLN A 1 3925 ? 185.854 300.879 184.878 1.00 28.79 ? 3925 GLN A CA    1 
ATOM   18100 C  C     . GLN A 1 3925 ? 184.643 300.016 184.545 1.00 28.99 ? 3925 GLN A C     1 
ATOM   18101 O  O     . GLN A 1 3925 ? 184.244 299.902 183.382 1.00 23.96 ? 3925 GLN A O     1 
ATOM   18102 C  CB    . GLN A 1 3925 ? 185.494 302.362 184.786 1.00 29.70 ? 3925 GLN A CB    1 
ATOM   18103 C  CG    . GLN A 1 3925 ? 184.351 302.783 185.693 1.00 27.88 ? 3925 GLN A CG    1 
ATOM   18104 C  CD    . GLN A 1 3925 ? 183.856 304.184 185.395 1.00 34.24 ? 3925 GLN A CD    1 
ATOM   18105 O  OE1   . GLN A 1 3925 ? 184.342 304.846 184.478 1.00 34.20 ? 3925 GLN A OE1   1 
ATOM   18106 N  NE2   . GLN A 1 3925 ? 182.885 304.648 186.174 1.00 36.88 ? 3925 GLN A NE2   1 
ATOM   18107 N  N     . GLY A 1 3926 ? 184.053 299.413 185.573 1.00 26.47 ? 3926 GLY A N     1 
ATOM   18108 C  CA    . GLY A 1 3926 ? 182.941 298.503 185.410 1.00 25.07 ? 3926 GLY A CA    1 
ATOM   18109 C  C     . GLY A 1 3926 ? 183.307 297.034 185.456 1.00 25.65 ? 3926 GLY A C     1 
ATOM   18110 O  O     . GLY A 1 3926 ? 182.406 296.189 185.407 1.00 25.80 ? 3926 GLY A O     1 
ATOM   18111 N  N     . LEU A 1 3927 ? 184.594 296.705 185.546 1.00 24.08 ? 3927 LEU A N     1 
ATOM   18112 C  CA    . LEU A 1 3927 ? 185.048 295.326 185.636 1.00 25.33 ? 3927 LEU A CA    1 
ATOM   18113 C  C     . LEU A 1 3927 ? 186.015 295.185 186.802 1.00 26.64 ? 3927 LEU A C     1 
ATOM   18114 O  O     . LEU A 1 3927 ? 186.637 296.153 187.243 1.00 29.26 ? 3927 LEU A O     1 
ATOM   18115 C  CB    . LEU A 1 3927 ? 185.729 294.861 184.343 1.00 22.02 ? 3927 LEU A CB    1 
ATOM   18116 C  CG    . LEU A 1 3927 ? 185.096 295.270 183.014 1.00 23.15 ? 3927 LEU A CG    1 
ATOM   18117 C  CD1   . LEU A 1 3927 ? 186.031 294.934 181.865 1.00 23.64 ? 3927 LEU A CD1   1 
ATOM   18118 C  CD2   . LEU A 1 3927 ? 183.756 294.588 182.829 1.00 21.30 ? 3927 LEU A CD2   1 
ATOM   18119 N  N     . THR A 1 3928 ? 186.133 293.959 187.300 1.00 20.48 ? 3928 THR A N     1 
ATOM   18120 C  CA    . THR A 1 3928 ? 187.048 293.658 188.387 1.00 22.01 ? 3928 THR A CA    1 
ATOM   18121 C  C     . THR A 1 3928 ? 188.436 293.373 187.816 1.00 22.44 ? 3928 THR A C     1 
ATOM   18122 O  O     . THR A 1 3928 ? 188.662 293.449 186.606 1.00 23.76 ? 3928 THR A O     1 
ATOM   18123 C  CB    . THR A 1 3928 ? 186.528 292.488 189.220 1.00 21.61 ? 3928 THR A CB    1 
ATOM   18124 O  OG1   . THR A 1 3928 ? 186.434 291.320 188.398 1.00 31.34 ? 3928 THR A OG1   1 
ATOM   18125 C  CG2   . THR A 1 3928 ? 185.158 292.812 189.786 1.00 21.81 ? 3928 THR A CG2   1 
ATOM   18126 N  N     . VAL A 1 3929 ? 189.385 293.045 188.695 1.00 25.65 ? 3929 VAL A N     1 
ATOM   18127 C  CA    . VAL A 1 3929 ? 190.747 292.768 188.251 1.00 21.59 ? 3929 VAL A CA    1 
ATOM   18128 C  C     . VAL A 1 3929 ? 190.784 291.511 187.390 1.00 26.74 ? 3929 VAL A C     1 
ATOM   18129 O  O     . VAL A 1 3929 ? 191.380 291.500 186.306 1.00 28.24 ? 3929 VAL A O     1 
ATOM   18130 C  CB    . VAL A 1 3929 ? 191.691 292.648 189.462 1.00 28.64 ? 3929 VAL A CB    1 
ATOM   18131 C  CG1   . VAL A 1 3929 ? 193.080 292.221 189.014 1.00 26.11 ? 3929 VAL A CG1   1 
ATOM   18132 C  CG2   . VAL A 1 3929 ? 191.751 293.965 190.219 1.00 22.75 ? 3929 VAL A CG2   1 
ATOM   18133 N  N     . GLU A 1 3930 ? 190.146 290.435 187.856 1.00 27.53 ? 3930 GLU A N     1 
ATOM   18134 C  CA    . GLU A 1 3930 ? 190.149 289.187 187.098 1.00 24.19 ? 3930 GLU A CA    1 
ATOM   18135 C  C     . GLU A 1 3930 ? 189.413 289.336 185.772 1.00 24.18 ? 3930 GLU A C     1 
ATOM   18136 O  O     . GLU A 1 3930 ? 189.844 288.785 184.754 1.00 24.09 ? 3930 GLU A O     1 
ATOM   18137 C  CB    . GLU A 1 3930 ? 189.547 288.055 187.933 1.00 20.20 ? 3930 GLU A CB    1 
ATOM   18138 C  CG    . GLU A 1 3930 ? 188.127 288.300 188.424 1.00 25.47 ? 3930 GLU A CG    1 
ATOM   18139 C  CD    . GLU A 1 3930 ? 188.087 289.026 189.756 1.00 30.86 ? 3930 GLU A CD    1 
ATOM   18140 O  OE1   . GLU A 1 3930 ? 189.156 289.469 190.223 1.00 31.41 ? 3930 GLU A OE1   1 
ATOM   18141 O  OE2   . GLU A 1 3930 ? 186.987 289.147 190.335 1.00 33.14 ? 3930 GLU A OE2   1 
ATOM   18142 N  N     . GLN A 1 3931 ? 188.300 290.075 185.764 1.00 19.42 ? 3931 GLN A N     1 
ATOM   18143 C  CA    . GLN A 1 3931 ? 187.583 290.309 184.514 1.00 22.30 ? 3931 GLN A CA    1 
ATOM   18144 C  C     . GLN A 1 3931 ? 188.435 291.103 183.534 1.00 25.98 ? 3931 GLN A C     1 
ATOM   18145 O  O     . GLN A 1 3931 ? 188.453 290.807 182.335 1.00 27.35 ? 3931 GLN A O     1 
ATOM   18146 C  CB    . GLN A 1 3931 ? 186.265 291.031 184.785 1.00 20.01 ? 3931 GLN A CB    1 
ATOM   18147 C  CG    . GLN A 1 3931 ? 185.151 290.131 185.289 1.00 19.53 ? 3931 GLN A CG    1 
ATOM   18148 C  CD    . GLN A 1 3931 ? 183.844 290.875 185.472 1.00 22.97 ? 3931 GLN A CD    1 
ATOM   18149 O  OE1   . GLN A 1 3931 ? 183.801 292.101 185.385 1.00 27.96 ? 3931 GLN A OE1   1 
ATOM   18150 N  NE2   . GLN A 1 3931 ? 182.770 290.135 185.714 1.00 19.60 ? 3931 GLN A NE2   1 
ATOM   18151 N  N     . ALA A 1 3932 ? 189.149 292.117 184.026 1.00 26.55 ? 3932 ALA A N     1 
ATOM   18152 C  CA    . ALA A 1 3932 ? 189.998 292.920 183.153 1.00 25.75 ? 3932 ALA A CA    1 
ATOM   18153 C  C     . ALA A 1 3932 ? 191.099 292.076 182.525 1.00 25.97 ? 3932 ALA A C     1 
ATOM   18154 O  O     . ALA A 1 3932 ? 191.405 292.226 181.337 1.00 27.58 ? 3932 ALA A O     1 
ATOM   18155 C  CB    . ALA A 1 3932 ? 190.595 294.091 183.933 1.00 30.37 ? 3932 ALA A CB    1 
ATOM   18156 N  N     . GLU A 1 3933 ? 191.709 291.184 183.309 1.00 23.14 ? 3933 GLU A N     1 
ATOM   18157 C  CA    . GLU A 1 3933 ? 192.735 290.302 182.760 1.00 23.47 ? 3933 GLU A CA    1 
ATOM   18158 C  C     . GLU A 1 3933 ? 192.158 289.389 181.686 1.00 23.64 ? 3933 GLU A C     1 
ATOM   18159 O  O     . GLU A 1 3933 ? 192.786 289.167 180.645 1.00 28.88 ? 3933 GLU A O     1 
ATOM   18160 C  CB    . GLU A 1 3933 ? 193.370 289.475 183.880 1.00 24.84 ? 3933 GLU A CB    1 
ATOM   18161 C  CG    . GLU A 1 3933 ? 194.085 290.302 184.932 1.00 23.95 ? 3933 GLU A CG    1 
ATOM   18162 C  CD    . GLU A 1 3933 ? 195.347 289.634 185.440 1.00 34.01 ? 3933 GLU A CD    1 
ATOM   18163 O  OE1   . GLU A 1 3933 ? 196.112 289.097 184.612 1.00 39.33 ? 3933 GLU A OE1   1 
ATOM   18164 O  OE2   . GLU A 1 3933 ? 195.574 289.644 186.668 1.00 33.35 ? 3933 GLU A OE2   1 
ATOM   18165 N  N     . ALA A 1 3934 ? 190.958 288.854 181.919 1.00 24.58 ? 3934 ALA A N     1 
ATOM   18166 C  CA    . ALA A 1 3934 ? 190.311 288.024 180.911 1.00 24.44 ? 3934 ALA A CA    1 
ATOM   18167 C  C     . ALA A 1 3934 ? 190.016 288.818 179.647 1.00 25.61 ? 3934 ALA A C     1 
ATOM   18168 O  O     . ALA A 1 3934 ? 190.009 288.254 178.547 1.00 24.27 ? 3934 ALA A O     1 
ATOM   18169 C  CB    . ALA A 1 3934 ? 189.029 287.416 181.476 1.00 19.43 ? 3934 ALA A CB    1 
ATOM   18170 N  N     . VAL A 1 3935 ? 189.760 290.120 179.780 1.00 22.20 ? 3935 VAL A N     1 
ATOM   18171 C  CA    . VAL A 1 3935 ? 189.592 290.972 178.608 1.00 20.49 ? 3935 VAL A CA    1 
ATOM   18172 C  C     . VAL A 1 3935 ? 190.908 291.098 177.852 1.00 27.65 ? 3935 VAL A C     1 
ATOM   18173 O  O     . VAL A 1 3935 ? 190.950 290.983 176.620 1.00 26.41 ? 3935 VAL A O     1 
ATOM   18174 C  CB    . VAL A 1 3935 ? 189.044 292.348 179.021 1.00 21.11 ? 3935 VAL A CB    1 
ATOM   18175 C  CG1   . VAL A 1 3935 ? 189.052 293.299 177.845 1.00 21.38 ? 3935 VAL A CG1   1 
ATOM   18176 C  CG2   . VAL A 1 3935 ? 187.646 292.212 179.580 1.00 23.33 ? 3935 VAL A CG2   1 
ATOM   18177 N  N     . VAL A 1 3936 ? 192.002 291.340 178.576 1.00 25.71 ? 3936 VAL A N     1 
ATOM   18178 C  CA    . VAL A 1 3936 ? 193.295 291.536 177.929 1.00 24.70 ? 3936 VAL A CA    1 
ATOM   18179 C  C     . VAL A 1 3936 ? 193.740 290.263 177.220 1.00 28.51 ? 3936 VAL A C     1 
ATOM   18180 O  O     . VAL A 1 3936 ? 194.238 290.309 176.090 1.00 30.20 ? 3936 VAL A O     1 
ATOM   18181 C  CB    . VAL A 1 3936 ? 194.340 292.011 178.955 1.00 27.45 ? 3936 VAL A CB    1 
ATOM   18182 C  CG1   . VAL A 1 3936 ? 195.701 292.172 178.294 1.00 25.24 ? 3936 VAL A CG1   1 
ATOM   18183 C  CG2   . VAL A 1 3936 ? 193.898 293.316 179.593 1.00 23.37 ? 3936 VAL A CG2   1 
ATOM   18184 N  N     . ARG A 1 3937 ? 193.574 289.109 177.872 1.00 28.41 ? 3937 ARG A N     1 
ATOM   18185 C  CA    . ARG A 1 3937 ? 193.945 287.849 177.233 1.00 21.58 ? 3937 ARG A CA    1 
ATOM   18186 C  C     . ARG A 1 3937 ? 193.074 287.577 176.013 1.00 22.87 ? 3937 ARG A C     1 
ATOM   18187 O  O     . ARG A 1 3937 ? 193.578 287.153 174.965 1.00 31.71 ? 3937 ARG A O     1 
ATOM   18188 C  CB    . ARG A 1 3937 ? 193.852 286.702 178.236 1.00 21.47 ? 3937 ARG A CB    1 
ATOM   18189 C  CG    . ARG A 1 3937 ? 194.817 286.834 179.397 1.00 22.27 ? 3937 ARG A CG    1 
ATOM   18190 C  CD    . ARG A 1 3937 ? 194.709 285.674 180.366 1.00 22.29 ? 3937 ARG A CD    1 
ATOM   18191 N  NE    . ARG A 1 3937 ? 195.193 286.042 181.693 1.00 25.08 ? 3937 ARG A NE    1 
ATOM   18192 C  CZ    . ARG A 1 3937 ? 196.260 285.514 182.276 1.00 27.06 ? 3937 ARG A CZ    1 
ATOM   18193 N  NH1   . ARG A 1 3937 ? 196.995 284.595 181.673 1.00 28.71 ? 3937 ARG A NH1   1 
ATOM   18194 N  NH2   . ARG A 1 3937 ? 196.599 285.921 183.495 1.00 28.62 ? 3937 ARG A NH2   1 
ATOM   18195 N  N     . LEU A 1 3938 ? 191.768 287.820 176.124 1.00 23.01 ? 3938 LEU A N     1 
ATOM   18196 C  CA    . LEU A 1 3938 ? 190.882 287.639 174.981 1.00 19.52 ? 3938 LEU A CA    1 
ATOM   18197 C  C     . LEU A 1 3938 ? 191.170 288.642 173.871 1.00 22.12 ? 3938 LEU A C     1 
ATOM   18198 O  O     . LEU A 1 3938 ? 190.816 288.389 172.715 1.00 23.65 ? 3938 LEU A O     1 
ATOM   18199 C  CB    . LEU A 1 3938 ? 189.420 287.745 175.426 1.00 15.64 ? 3938 LEU A CB    1 
ATOM   18200 C  CG    . LEU A 1 3938 ? 188.332 287.427 174.395 1.00 18.73 ? 3938 LEU A CG    1 
ATOM   18201 C  CD1   . LEU A 1 3938 ? 188.411 285.977 173.948 1.00 19.45 ? 3938 LEU A CD1   1 
ATOM   18202 C  CD2   . LEU A 1 3938 ? 186.955 287.740 174.950 1.00 17.86 ? 3938 LEU A CD2   1 
ATOM   18203 N  N     . SER A 1 3939 ? 191.817 289.763 174.194 1.00 24.52 ? 3939 SER A N     1 
ATOM   18204 C  CA    . SER A 1 3939 ? 192.155 290.763 173.190 1.00 23.20 ? 3939 SER A CA    1 
ATOM   18205 C  C     . SER A 1 3939 ? 193.173 290.263 172.175 1.00 26.18 ? 3939 SER A C     1 
ATOM   18206 O  O     . SER A 1 3939 ? 193.323 290.886 171.119 1.00 27.70 ? 3939 SER A O     1 
ATOM   18207 C  CB    . SER A 1 3939 ? 192.683 292.027 173.868 1.00 23.41 ? 3939 SER A CB    1 
ATOM   18208 O  OG    . SER A 1 3939 ? 194.007 291.832 174.332 1.00 34.46 ? 3939 SER A OG    1 
ATOM   18209 N  N     . CYS A 1 3940 ? 193.869 289.160 172.463 1.00 23.50 ? 3940 CYS A N     1 
ATOM   18210 C  CA    . CYS A 1 3940 ? 194.855 288.629 171.533 1.00 20.75 ? 3940 CYS A CA    1 
ATOM   18211 C  C     . CYS A 1 3940 ? 194.217 288.069 170.268 1.00 27.75 ? 3940 CYS A C     1 
ATOM   18212 O  O     . CYS A 1 3940 ? 194.904 287.926 169.251 1.00 30.84 ? 3940 CYS A O     1 
ATOM   18213 C  CB    . CYS A 1 3940 ? 195.692 287.548 172.221 1.00 20.70 ? 3940 CYS A CB    1 
ATOM   18214 S  SG    . CYS A 1 3940 ? 197.153 287.018 171.296 1.00 64.87 ? 3940 CYS A SG    1 
ATOM   18215 N  N     . LEU A 1 3941 ? 192.928 287.738 170.308 1.00 23.19 ? 3941 LEU A N     1 
ATOM   18216 C  CA    . LEU A 1 3941 ? 192.350 287.292 169.047 1.00 22.47 ? 3941 LEU A CA    1 
ATOM   18217 C  C     . LEU A 1 3941 ? 192.057 288.490 168.148 1.00 23.60 ? 3941 LEU A C     1 
ATOM   18218 O  O     . LEU A 1 3941 ? 191.728 289.571 168.644 1.00 30.53 ? 3941 LEU A O     1 
ATOM   18219 C  CB    . LEU A 1 3941 ? 191.062 286.509 169.282 1.00 28.56 ? 3941 LEU A CB    1 
ATOM   18220 C  CG    . LEU A 1 3941 ? 191.148 285.198 170.065 1.00 24.28 ? 3941 LEU A CG    1 
ATOM   18221 C  CD1   . LEU A 1 3941 ? 189.933 284.338 169.766 1.00 17.23 ? 3941 LEU A CD1   1 
ATOM   18222 C  CD2   . LEU A 1 3941 ? 192.432 284.448 169.749 1.00 27.19 ? 3941 LEU A CD2   1 
ATOM   18223 N  N     . PRO A 1 3942 ? 192.183 288.315 166.830 1.00 24.61 ? 3942 PRO A N     1 
ATOM   18224 C  CA    . PRO A 1 3942 ? 191.822 289.411 165.917 1.00 21.09 ? 3942 PRO A CA    1 
ATOM   18225 C  C     . PRO A 1 3942 ? 190.378 289.861 166.055 1.00 21.45 ? 3942 PRO A C     1 
ATOM   18226 O  O     . PRO A 1 3942 ? 190.087 291.052 165.890 1.00 25.80 ? 3942 PRO A O     1 
ATOM   18227 C  CB    . PRO A 1 3942 ? 192.106 288.808 164.536 1.00 21.01 ? 3942 PRO A CB    1 
ATOM   18228 C  CG    . PRO A 1 3942 ? 193.188 287.815 164.791 1.00 20.97 ? 3942 PRO A CG    1 
ATOM   18229 C  CD    . PRO A 1 3942 ? 192.863 287.213 166.131 1.00 23.96 ? 3942 PRO A CD    1 
ATOM   18230 N  N     . ALA A 1 3943 ? 189.460 288.939 166.353 1.00 20.64 ? 3943 ALA A N     1 
ATOM   18231 C  CA    . ALA A 1 3943 ? 188.058 289.316 166.498 1.00 25.80 ? 3943 ALA A CA    1 
ATOM   18232 C  C     . ALA A 1 3943 ? 187.828 290.175 167.736 1.00 23.62 ? 3943 ALA A C     1 
ATOM   18233 O  O     . ALA A 1 3943 ? 186.949 291.043 167.732 1.00 26.56 ? 3943 ALA A O     1 
ATOM   18234 C  CB    . ALA A 1 3943 ? 187.177 288.069 166.547 1.00 19.80 ? 3943 ALA A CB    1 
ATOM   18235 N  N     . PHE A 1 3944 ? 188.601 289.950 168.798 1.00 19.48 ? 3944 PHE A N     1 
ATOM   18236 C  CA    . PHE A 1 3944 ? 188.468 290.712 170.032 1.00 24.79 ? 3944 PHE A CA    1 
ATOM   18237 C  C     . PHE A 1 3944 ? 189.611 291.701 170.232 1.00 27.36 ? 3944 PHE A C     1 
ATOM   18238 O  O     . PHE A 1 3944 ? 189.926 292.049 171.373 1.00 27.33 ? 3944 PHE A O     1 
ATOM   18239 C  CB    . PHE A 1 3944 ? 188.374 289.769 171.235 1.00 24.26 ? 3944 PHE A CB    1 
ATOM   18240 C  CG    . PHE A 1 3944 ? 187.187 288.848 171.198 1.00 22.16 ? 3944 PHE A CG    1 
ATOM   18241 C  CD1   . PHE A 1 3944 ? 185.933 289.301 171.563 1.00 21.12 ? 3944 PHE A CD1   1 
ATOM   18242 C  CD2   . PHE A 1 3944 ? 187.330 287.527 170.808 1.00 20.77 ? 3944 PHE A CD2   1 
ATOM   18243 C  CE1   . PHE A 1 3944 ? 184.841 288.457 171.536 1.00 22.73 ? 3944 PHE A CE1   1 
ATOM   18244 C  CE2   . PHE A 1 3944 ? 186.241 286.679 170.779 1.00 21.83 ? 3944 PHE A CE2   1 
ATOM   18245 C  CZ    . PHE A 1 3944 ? 184.996 287.144 171.142 1.00 21.78 ? 3944 PHE A CZ    1 
ATOM   18246 N  N     . LYS A 1 3945 ? 190.247 292.159 169.149 1.00 25.92 ? 3945 LYS A N     1 
ATOM   18247 C  CA    . LYS A 1 3945 ? 191.329 293.127 169.298 1.00 24.84 ? 3945 LYS A CA    1 
ATOM   18248 C  C     . LYS A 1 3945 ? 190.814 294.444 169.870 1.00 26.19 ? 3945 LYS A C     1 
ATOM   18249 O  O     . LYS A 1 3945 ? 191.466 295.052 170.727 1.00 23.33 ? 3945 LYS A O     1 
ATOM   18250 C  CB    . LYS A 1 3945 ? 192.043 293.343 167.958 1.00 26.87 ? 3945 LYS A CB    1 
ATOM   18251 C  CG    . LYS A 1 3945 ? 191.220 294.028 166.872 1.00 27.24 ? 3945 LYS A CG    1 
ATOM   18252 C  CD    . LYS A 1 3945 ? 192.019 294.168 165.587 1.00 25.52 ? 3945 LYS A CD    1 
ATOM   18253 C  CE    . LYS A 1 3945 ? 191.194 294.811 164.483 1.00 29.77 ? 3945 LYS A CE    1 
ATOM   18254 N  NZ    . LYS A 1 3945 ? 190.862 296.230 164.787 1.00 34.26 ? 3945 LYS A NZ    1 
ATOM   18255 N  N     . ASP A 1 3946 ? 189.646 294.895 169.417 1.00 24.22 ? 3946 ASP A N     1 
ATOM   18256 C  CA    . ASP A 1 3946 ? 189.012 296.099 169.954 1.00 22.40 ? 3946 ASP A CA    1 
ATOM   18257 C  C     . ASP A 1 3946 ? 187.988 295.739 171.036 1.00 26.95 ? 3946 ASP A C     1 
ATOM   18258 O  O     . ASP A 1 3946 ? 186.827 296.149 171.012 1.00 25.98 ? 3946 ASP A O     1 
ATOM   18259 C  CB    . ASP A 1 3946 ? 188.390 296.911 168.821 1.00 22.69 ? 3946 ASP A CB    1 
ATOM   18260 C  CG    . ASP A 1 3946 ? 187.286 296.165 168.088 1.00 37.13 ? 3946 ASP A CG    1 
ATOM   18261 O  OD1   . ASP A 1 3946 ? 187.015 294.990 168.420 1.00 37.34 ? 3946 ASP A OD1   1 
ATOM   18262 O  OD2   . ASP A 1 3946 ? 186.683 296.759 167.170 1.00 35.38 ? 3946 ASP A OD2   1 
ATOM   18263 N  N     . LEU A 1 3947 ? 188.455 294.968 172.018 1.00 29.23 ? 3947 LEU A N     1 
ATOM   18264 C  CA    . LEU A 1 3947 ? 187.596 294.480 173.090 1.00 23.40 ? 3947 LEU A CA    1 
ATOM   18265 C  C     . LEU A 1 3947 ? 187.409 295.510 174.199 1.00 26.14 ? 3947 LEU A C     1 
ATOM   18266 O  O     . LEU A 1 3947 ? 186.282 295.740 174.648 1.00 27.59 ? 3947 LEU A O     1 
ATOM   18267 C  CB    . LEU A 1 3947 ? 188.174 293.183 173.666 1.00 21.96 ? 3947 LEU A CB    1 
ATOM   18268 C  CG    . LEU A 1 3947 ? 187.350 292.424 174.708 1.00 25.55 ? 3947 LEU A CG    1 
ATOM   18269 C  CD1   . LEU A 1 3947 ? 185.999 292.048 174.153 1.00 18.51 ? 3947 LEU A CD1   1 
ATOM   18270 C  CD2   . LEU A 1 3947 ? 188.097 291.181 175.149 1.00 23.82 ? 3947 LEU A CD2   1 
ATOM   18271 N  N     . ILE A 1 3948 ? 188.502 296.132 174.653 1.00 22.23 ? 3948 ILE A N     1 
ATOM   18272 C  CA    . ILE A 1 3948 ? 188.410 297.116 175.729 1.00 23.33 ? 3948 ILE A CA    1 
ATOM   18273 C  C     . ILE A 1 3948 ? 187.556 298.300 175.296 1.00 25.49 ? 3948 ILE A C     1 
ATOM   18274 O  O     . ILE A 1 3948 ? 186.726 298.802 176.065 1.00 25.75 ? 3948 ILE A O     1 
ATOM   18275 C  CB    . ILE A 1 3948 ? 189.818 297.563 176.167 1.00 25.29 ? 3948 ILE A CB    1 
ATOM   18276 C  CG1   . ILE A 1 3948 ? 190.541 296.427 176.887 1.00 20.06 ? 3948 ILE A CG1   1 
ATOM   18277 C  CG2   . ILE A 1 3948 ? 189.742 298.797 177.056 1.00 26.37 ? 3948 ILE A CG2   1 
ATOM   18278 C  CD1   . ILE A 1 3948 ? 191.924 296.791 177.363 1.00 25.80 ? 3948 ILE A CD1   1 
ATOM   18279 N  N     . ALA A 1 3949 ? 187.747 298.765 174.060 1.00 24.30 ? 3949 ALA A N     1 
ATOM   18280 C  CA    . ALA A 1 3949 ? 186.963 299.888 173.559 1.00 23.27 ? 3949 ALA A CA    1 
ATOM   18281 C  C     . ALA A 1 3949 ? 185.486 299.536 173.455 1.00 27.55 ? 3949 ALA A C     1 
ATOM   18282 O  O     . ALA A 1 3949 ? 184.622 300.343 173.817 1.00 31.13 ? 3949 ALA A O     1 
ATOM   18283 C  CB    . ALA A 1 3949 ? 187.505 300.341 172.204 1.00 19.38 ? 3949 ALA A CB    1 
ATOM   18284 N  N     . LYS A 1 3950 ? 185.173 298.336 172.958 1.00 27.81 ? 3950 LYS A N     1 
ATOM   18285 C  CA    . LYS A 1 3950 ? 183.777 297.959 172.760 1.00 25.34 ? 3950 LYS A CA    1 
ATOM   18286 C  C     . LYS A 1 3950 ? 183.024 297.899 174.085 1.00 27.32 ? 3950 LYS A C     1 
ATOM   18287 O  O     . LYS A 1 3950 ? 181.859 298.306 174.163 1.00 27.35 ? 3950 LYS A O     1 
ATOM   18288 C  CB    . LYS A 1 3950 ? 183.688 296.623 172.026 1.00 26.75 ? 3950 LYS A CB    1 
ATOM   18289 C  CG    . LYS A 1 3950 ? 183.379 296.759 170.544 1.00 23.15 ? 3950 LYS A CG    1 
ATOM   18290 C  CD    . LYS A 1 3950 ? 183.632 295.458 169.800 1.00 23.67 ? 3950 LYS A CD    1 
ATOM   18291 C  CE    . LYS A 1 3950 ? 183.344 295.608 168.319 1.00 27.97 ? 3950 LYS A CE    1 
ATOM   18292 N  NZ    . LYS A 1 3950 ? 184.139 296.709 167.707 1.00 30.79 ? 3950 LYS A NZ    1 
ATOM   18293 N  N     . VAL A 1 3951 ? 183.668 297.380 175.132 1.00 25.92 ? 3951 VAL A N     1 
ATOM   18294 C  CA    . VAL A 1 3951 ? 183.056 297.401 176.457 1.00 23.41 ? 3951 VAL A CA    1 
ATOM   18295 C  C     . VAL A 1 3951 ? 182.896 298.831 176.953 1.00 27.49 ? 3951 VAL A C     1 
ATOM   18296 O  O     . VAL A 1 3951 ? 181.837 299.208 177.470 1.00 36.05 ? 3951 VAL A O     1 
ATOM   18297 C  CB    . VAL A 1 3951 ? 183.881 296.552 177.441 1.00 21.90 ? 3951 VAL A CB    1 
ATOM   18298 C  CG1   . VAL A 1 3951 ? 183.310 296.669 178.840 1.00 21.91 ? 3951 VAL A CG1   1 
ATOM   18299 C  CG2   . VAL A 1 3951 ? 183.899 295.102 176.997 1.00 24.86 ? 3951 VAL A CG2   1 
ATOM   18300 N  N     . GLN A 1 3952 ? 183.938 299.652 176.801 1.00 26.47 ? 3952 GLN A N     1 
ATOM   18301 C  CA    . GLN A 1 3952 ? 183.857 301.037 177.253 1.00 28.00 ? 3952 GLN A CA    1 
ATOM   18302 C  C     . GLN A 1 3952 ? 182.815 301.819 176.462 1.00 26.88 ? 3952 GLN A C     1 
ATOM   18303 O  O     . GLN A 1 3952 ? 182.087 302.641 177.027 1.00 31.03 ? 3952 GLN A O     1 
ATOM   18304 C  CB    . GLN A 1 3952 ? 185.230 301.703 177.151 1.00 25.16 ? 3952 GLN A CB    1 
ATOM   18305 C  CG    . GLN A 1 3952 ? 186.150 301.395 178.319 1.00 27.06 ? 3952 GLN A CG    1 
ATOM   18306 C  CD    . GLN A 1 3952 ? 187.600 301.715 178.023 1.00 31.51 ? 3952 GLN A CD    1 
ATOM   18307 O  OE1   . GLN A 1 3952 ? 187.958 302.037 176.891 1.00 32.18 ? 3952 GLN A OE1   1 
ATOM   18308 N  NE2   . GLN A 1 3952 ? 188.445 301.630 179.044 1.00 27.67 ? 3952 GLN A NE2   1 
ATOM   18309 N  N     . ALA A 1 3953 ? 182.724 301.570 175.153 1.00 25.45 ? 3953 ALA A N     1 
ATOM   18310 C  CA    . ALA A 1 3953 ? 181.720 302.244 174.340 1.00 28.51 ? 3953 ALA A CA    1 
ATOM   18311 C  C     . ALA A 1 3953 ? 180.302 301.795 174.671 1.00 30.18 ? 3953 ALA A C     1 
ATOM   18312 O  O     . ALA A 1 3953 ? 179.347 302.475 174.287 1.00 35.10 ? 3953 ALA A O     1 
ATOM   18313 C  CB    . ALA A 1 3953 ? 182.004 302.016 172.855 1.00 25.32 ? 3953 ALA A CB    1 
ATOM   18314 N  N     . ASP A 1 3954 ? 180.144 300.672 175.368 1.00 30.40 ? 3954 ASP A N     1 
ATOM   18315 C  CA    . ASP A 1 3954 ? 178.830 300.130 175.707 1.00 30.17 ? 3954 ASP A CA    1 
ATOM   18316 C  C     . ASP A 1 3954 ? 178.583 300.338 177.197 1.00 30.79 ? 3954 ASP A C     1 
ATOM   18317 O  O     . ASP A 1 3954 ? 179.091 299.586 178.033 1.00 33.61 ? 3954 ASP A O     1 
ATOM   18318 C  CB    . ASP A 1 3954 ? 178.745 298.653 175.332 1.00 29.16 ? 3954 ASP A CB    1 
ATOM   18319 C  CG    . ASP A 1 3954 ? 177.341 298.097 175.471 1.00 31.54 ? 3954 ASP A CG    1 
ATOM   18320 O  OD1   . ASP A 1 3954 ? 176.404 298.890 175.692 1.00 30.23 ? 3954 ASP A OD1   1 
ATOM   18321 O  OD2   . ASP A 1 3954 ? 177.178 296.863 175.364 1.00 36.44 ? 3954 ASP A OD2   1 
ATOM   18322 N  N     . GLU A 1 3955 ? 177.793 301.360 177.531 1.00 30.17 ? 3955 GLU A N     1 
ATOM   18323 C  CA    . GLU A 1 3955 ? 177.398 301.564 178.919 1.00 32.50 ? 3955 GLU A CA    1 
ATOM   18324 C  C     . GLU A 1 3955 ? 176.349 300.555 179.368 1.00 35.34 ? 3955 GLU A C     1 
ATOM   18325 O  O     . GLU A 1 3955 ? 176.221 300.309 180.572 1.00 33.95 ? 3955 GLU A O     1 
ATOM   18326 C  CB    . GLU A 1 3955 ? 176.877 302.989 179.125 1.00 29.47 ? 3955 GLU A CB    1 
ATOM   18327 C  CG    . GLU A 1 3955 ? 175.791 303.421 178.150 1.00 29.37 ? 3955 GLU A CG    1 
ATOM   18328 C  CD    . GLU A 1 3955 ? 176.345 303.913 176.827 1.00 37.69 ? 3955 GLU A CD    1 
ATOM   18329 O  OE1   . GLU A 1 3955 ? 177.585 303.944 176.673 1.00 35.51 ? 3955 GLU A OE1   1 
ATOM   18330 O  OE2   . GLU A 1 3955 ? 175.542 304.271 175.940 1.00 34.58 ? 3955 GLU A OE2   1 
ATOM   18331 N  N     . GLN A 1 3956 ? 175.600 299.970 178.431 1.00 29.95 ? 3956 GLN A N     1 
ATOM   18332 C  CA    . GLN A 1 3956 ? 174.670 298.898 178.763 1.00 28.43 ? 3956 GLN A CA    1 
ATOM   18333 C  C     . GLN A 1 3956 ? 175.382 297.599 179.115 1.00 27.22 ? 3956 GLN A C     1 
ATOM   18334 O  O     . GLN A 1 3956 ? 174.730 296.664 179.592 1.00 24.81 ? 3956 GLN A O     1 
ATOM   18335 C  CB    . GLN A 1 3956 ? 173.698 298.649 177.606 1.00 25.39 ? 3956 GLN A CB    1 
ATOM   18336 C  CG    . GLN A 1 3956 ? 172.645 299.733 177.391 1.00 29.80 ? 3956 GLN A CG    1 
ATOM   18337 C  CD    . GLN A 1 3956 ? 173.230 301.061 176.950 1.00 34.71 ? 3956 GLN A CD    1 
ATOM   18338 O  OE1   . GLN A 1 3956 ? 174.051 301.118 176.034 1.00 33.90 ? 3956 GLN A OE1   1 
ATOM   18339 N  NE2   . GLN A 1 3956 ? 172.804 302.139 177.597 1.00 36.41 ? 3956 GLN A NE2   1 
ATOM   18340 N  N     . PHE A 1 3957 ? 176.695 297.518 178.885 1.00 25.41 ? 3957 PHE A N     1 
ATOM   18341 C  CA    . PHE A 1 3957 ? 177.445 296.321 179.247 1.00 25.27 ? 3957 PHE A CA    1 
ATOM   18342 C  C     . PHE A 1 3957 ? 177.403 296.065 180.747 1.00 23.49 ? 3957 PHE A C     1 
ATOM   18343 O  O     . PHE A 1 3957 ? 177.478 294.909 181.180 1.00 27.94 ? 3957 PHE A O     1 
ATOM   18344 C  CB    . PHE A 1 3957 ? 178.891 296.450 178.766 1.00 20.15 ? 3957 PHE A CB    1 
ATOM   18345 C  CG    . PHE A 1 3957 ? 179.668 295.172 178.833 1.00 21.30 ? 3957 PHE A CG    1 
ATOM   18346 C  CD1   . PHE A 1 3957 ? 179.616 294.261 177.794 1.00 22.57 ? 3957 PHE A CD1   1 
ATOM   18347 C  CD2   . PHE A 1 3957 ? 180.462 294.884 179.931 1.00 13.88 ? 3957 PHE A CD2   1 
ATOM   18348 C  CE1   . PHE A 1 3957 ? 180.332 293.086 177.849 1.00 21.31 ? 3957 PHE A CE1   1 
ATOM   18349 C  CE2   . PHE A 1 3957 ? 181.182 293.712 179.990 1.00 16.68 ? 3957 PHE A CE2   1 
ATOM   18350 C  CZ    . PHE A 1 3957 ? 181.116 292.811 178.948 1.00 16.35 ? 3957 PHE A CZ    1 
ATOM   18351 N  N     . GLY A 1 3958 ? 177.282 297.121 181.553 1.00 21.11 ? 3958 GLY A N     1 
ATOM   18352 C  CA    . GLY A 1 3958 ? 177.174 296.934 182.990 1.00 15.61 ? 3958 GLY A CA    1 
ATOM   18353 C  C     . GLY A 1 3958 ? 175.908 296.203 183.390 1.00 23.18 ? 3958 GLY A C     1 
ATOM   18354 O  O     . GLY A 1 3958 ? 175.923 295.378 184.309 1.00 24.38 ? 3958 GLY A O     1 
ATOM   18355 N  N     . ILE A 1 3959 ? 174.796 296.495 182.713 1.00 23.05 ? 3959 ILE A N     1 
ATOM   18356 C  CA    . ILE A 1 3959 ? 173.542 295.810 183.013 1.00 17.80 ? 3959 ILE A CA    1 
ATOM   18357 C  C     . ILE A 1 3959 ? 173.629 294.336 182.632 1.00 23.77 ? 3959 ILE A C     1 
ATOM   18358 O  O     . ILE A 1 3959 ? 173.224 293.458 183.403 1.00 32.10 ? 3959 ILE A O     1 
ATOM   18359 C  CB    . ILE A 1 3959 ? 172.371 296.512 182.304 1.00 19.84 ? 3959 ILE A CB    1 
ATOM   18360 C  CG1   . ILE A 1 3959 ? 172.240 297.955 182.792 1.00 25.80 ? 3959 ILE A CG1   1 
ATOM   18361 C  CG2   . ILE A 1 3959 ? 171.076 295.752 182.528 1.00 16.62 ? 3959 ILE A CG2   1 
ATOM   18362 C  CD1   . ILE A 1 3959 ? 172.067 298.078 184.290 1.00 21.22 ? 3959 ILE A CD1   1 
ATOM   18363 N  N     . TRP A 1 3960 ? 174.155 294.041 181.441 1.00 24.48 ? 3960 TRP A N     1 
ATOM   18364 C  CA    . TRP A 1 3960 ? 174.289 292.652 181.014 1.00 15.57 ? 3960 TRP A CA    1 
ATOM   18365 C  C     . TRP A 1 3960 ? 175.265 291.887 181.897 1.00 15.90 ? 3960 TRP A C     1 
ATOM   18366 O  O     . TRP A 1 3960 ? 175.078 290.688 182.133 1.00 22.45 ? 3960 TRP A O     1 
ATOM   18367 C  CB    . TRP A 1 3960 ? 174.736 292.586 179.554 1.00 18.79 ? 3960 TRP A CB    1 
ATOM   18368 C  CG    . TRP A 1 3960 ? 175.116 291.205 179.100 1.00 18.26 ? 3960 TRP A CG    1 
ATOM   18369 C  CD1   . TRP A 1 3960 ? 174.283 290.247 178.608 1.00 15.81 ? 3960 TRP A CD1   1 
ATOM   18370 C  CD2   . TRP A 1 3960 ? 176.430 290.633 179.099 1.00 15.87 ? 3960 TRP A CD2   1 
ATOM   18371 N  NE1   . TRP A 1 3960 ? 174.992 289.113 178.301 1.00 15.92 ? 3960 TRP A NE1   1 
ATOM   18372 C  CE2   . TRP A 1 3960 ? 176.313 289.324 178.596 1.00 14.43 ? 3960 TRP A CE2   1 
ATOM   18373 C  CE3   . TRP A 1 3960 ? 177.691 291.099 179.476 1.00 12.91 ? 3960 TRP A CE3   1 
ATOM   18374 C  CZ2   . TRP A 1 3960 ? 177.409 288.476 178.457 1.00 16.69 ? 3960 TRP A CZ2   1 
ATOM   18375 C  CZ3   . TRP A 1 3960 ? 178.777 290.257 179.339 1.00 13.40 ? 3960 TRP A CZ3   1 
ATOM   18376 C  CH2   . TRP A 1 3960 ? 178.630 288.960 178.835 1.00 18.59 ? 3960 TRP A CH2   1 
ATOM   18377 N  N     . LEU A 1 3961 ? 176.304 292.560 182.393 1.00 20.19 ? 3961 LEU A N     1 
ATOM   18378 C  CA    . LEU A 1 3961 ? 177.304 291.895 183.219 1.00 18.58 ? 3961 LEU A CA    1 
ATOM   18379 C  C     . LEU A 1 3961 ? 176.730 291.390 184.536 1.00 20.65 ? 3961 LEU A C     1 
ATOM   18380 O  O     . LEU A 1 3961 ? 177.267 290.435 185.108 1.00 23.34 ? 3961 LEU A O     1 
ATOM   18381 C  CB    . LEU A 1 3961 ? 178.471 292.848 183.486 1.00 16.25 ? 3961 LEU A CB    1 
ATOM   18382 C  CG    . LEU A 1 3961 ? 179.726 292.242 184.114 1.00 20.94 ? 3961 LEU A CG    1 
ATOM   18383 C  CD1   . LEU A 1 3961 ? 180.346 291.232 183.172 1.00 17.61 ? 3961 LEU A CD1   1 
ATOM   18384 C  CD2   . LEU A 1 3961 ? 180.728 293.326 184.475 1.00 20.01 ? 3961 LEU A CD2   1 
ATOM   18385 N  N     . ASP A 1 3962 ? 175.654 292.000 185.030 1.00 20.09 ? 3962 ASP A N     1 
ATOM   18386 C  CA    . ASP A 1 3962 ? 175.061 291.622 186.307 1.00 20.77 ? 3962 ASP A CA    1 
ATOM   18387 C  C     . ASP A 1 3962 ? 173.649 291.070 186.135 1.00 23.78 ? 3962 ASP A C     1 
ATOM   18388 O  O     . ASP A 1 3962 ? 172.802 291.231 187.014 1.00 28.83 ? 3962 ASP A O     1 
ATOM   18389 C  CB    . ASP A 1 3962 ? 175.062 292.809 187.269 1.00 21.19 ? 3962 ASP A CB    1 
ATOM   18390 C  CG    . ASP A 1 3962 ? 176.447 293.382 187.480 1.00 25.03 ? 3962 ASP A CG    1 
ATOM   18391 O  OD1   . ASP A 1 3962 ? 177.333 292.638 187.948 1.00 26.71 ? 3962 ASP A OD1   1 
ATOM   18392 O  OD2   . ASP A 1 3962 ? 176.652 294.575 187.175 1.00 28.21 ? 3962 ASP A OD2   1 
ATOM   18393 N  N     . SER A 1 3963 ? 173.385 290.418 185.009 1.00 25.58 ? 3963 SER A N     1 
ATOM   18394 C  CA    . SER A 1 3963 ? 172.103 289.782 184.756 1.00 19.43 ? 3963 SER A CA    1 
ATOM   18395 C  C     . SER A 1 3963 ? 172.147 288.318 185.176 1.00 19.51 ? 3963 SER A C     1 
ATOM   18396 O  O     . SER A 1 3963 ? 173.213 287.703 185.274 1.00 23.34 ? 3963 SER A O     1 
ATOM   18397 C  CB    . SER A 1 3963 ? 171.722 289.898 183.278 1.00 18.90 ? 3963 SER A CB    1 
ATOM   18398 O  OG    . SER A 1 3963 ? 172.673 289.256 182.450 1.00 23.22 ? 3963 SER A OG    1 
ATOM   18399 N  N     . SER A 1 3964 ? 170.961 287.765 185.436 1.00 20.36 ? 3964 SER A N     1 
ATOM   18400 C  CA    . SER A 1 3964 ? 170.866 286.387 185.905 1.00 14.40 ? 3964 SER A CA    1 
ATOM   18401 C  C     . SER A 1 3964 ? 171.320 285.399 184.838 1.00 18.76 ? 3964 SER A C     1 
ATOM   18402 O  O     . SER A 1 3964 ? 171.973 284.397 185.149 1.00 18.24 ? 3964 SER A O     1 
ATOM   18403 C  CB    . SER A 1 3964 ? 169.435 286.079 186.343 1.00 12.31 ? 3964 SER A CB    1 
ATOM   18404 O  OG    . SER A 1 3964 ? 168.538 286.191 185.255 1.00 15.68 ? 3964 SER A OG    1 
ATOM   18405 N  N     . SER A 1 3965 ? 170.982 285.660 183.578 1.00 18.93 ? 3965 SER A N     1 
ATOM   18406 C  CA    . SER A 1 3965 ? 171.287 284.756 182.470 1.00 14.70 ? 3965 SER A CA    1 
ATOM   18407 C  C     . SER A 1 3965 ? 171.971 285.539 181.358 1.00 16.16 ? 3965 SER A C     1 
ATOM   18408 O  O     . SER A 1 3965 ? 171.398 285.750 180.284 1.00 22.34 ? 3965 SER A O     1 
ATOM   18409 C  CB    . SER A 1 3965 ? 170.016 284.076 181.960 1.00 17.89 ? 3965 SER A CB    1 
ATOM   18410 O  OG    . SER A 1 3965 ? 169.361 283.375 183.002 1.00 18.18 ? 3965 SER A OG    1 
ATOM   18411 N  N     . PRO A 1 3966 ? 173.215 285.977 181.579 1.00 11.93 ? 3966 PRO A N     1 
ATOM   18412 C  CA    . PRO A 1 3966 ? 173.917 286.740 180.539 1.00 13.66 ? 3966 PRO A CA    1 
ATOM   18413 C  C     . PRO A 1 3966 ? 174.234 285.927 179.297 1.00 16.84 ? 3966 PRO A C     1 
ATOM   18414 O  O     . PRO A 1 3966 ? 174.541 286.518 178.255 1.00 22.87 ? 3966 PRO A O     1 
ATOM   18415 C  CB    . PRO A 1 3966 ? 175.196 287.199 181.250 1.00 13.80 ? 3966 PRO A CB    1 
ATOM   18416 C  CG    . PRO A 1 3966 ? 175.437 286.143 182.262 1.00 11.09 ? 3966 PRO A CG    1 
ATOM   18417 C  CD    . PRO A 1 3966 ? 174.076 285.731 182.750 1.00 13.27 ? 3966 PRO A CD    1 
ATOM   18418 N  N     . GLU A 1 3967 ? 174.177 284.596 179.373 1.00 13.38 ? 3967 GLU A N     1 
ATOM   18419 C  CA    . GLU A 1 3967 ? 174.531 283.753 178.237 1.00 12.48 ? 3967 GLU A CA    1 
ATOM   18420 C  C     . GLU A 1 3967 ? 173.473 283.766 177.143 1.00 15.49 ? 3967 GLU A C     1 
ATOM   18421 O  O     . GLU A 1 3967 ? 173.773 283.386 176.007 1.00 23.01 ? 3967 GLU A O     1 
ATOM   18422 C  CB    . GLU A 1 3967 ? 174.769 282.316 178.701 1.00 9.43  ? 3967 GLU A CB    1 
ATOM   18423 C  CG    . GLU A 1 3967 ? 173.510 281.603 179.164 1.00 13.05 ? 3967 GLU A CG    1 
ATOM   18424 C  CD    . GLU A 1 3967 ? 173.146 281.928 180.599 1.00 13.76 ? 3967 GLU A CD    1 
ATOM   18425 O  OE1   . GLU A 1 3967 ? 173.970 282.556 181.295 1.00 14.28 ? 3967 GLU A OE1   1 
ATOM   18426 O  OE2   . GLU A 1 3967 ? 172.032 281.569 181.028 1.00 18.57 ? 3967 GLU A OE2   1 
ATOM   18427 N  N     . GLN A 1 3968 ? 172.247 284.181 177.454 1.00 14.57 ? 3968 GLN A N     1 
ATOM   18428 C  CA    . GLN A 1 3968 ? 171.178 284.205 176.467 1.00 14.76 ? 3968 GLN A CA    1 
ATOM   18429 C  C     . GLN A 1 3968 ? 171.076 285.529 175.723 1.00 18.28 ? 3968 GLN A C     1 
ATOM   18430 O  O     . GLN A 1 3968 ? 170.342 285.607 174.731 1.00 21.39 ? 3968 GLN A O     1 
ATOM   18431 C  CB    . GLN A 1 3968 ? 169.836 283.894 177.135 1.00 16.61 ? 3968 GLN A CB    1 
ATOM   18432 C  CG    . GLN A 1 3968 ? 169.789 282.550 177.840 1.00 16.95 ? 3968 GLN A CG    1 
ATOM   18433 C  CD    . GLN A 1 3968 ? 168.473 282.316 178.549 1.00 25.67 ? 3968 GLN A CD    1 
ATOM   18434 O  OE1   . GLN A 1 3968 ? 167.578 283.159 178.513 1.00 30.82 ? 3968 GLN A OE1   1 
ATOM   18435 N  NE2   . GLN A 1 3968 ? 168.347 281.166 179.199 1.00 23.51 ? 3968 GLN A NE2   1 
ATOM   18436 N  N     . THR A 1 3969 ? 171.781 286.562 176.172 1.00 18.53 ? 3969 THR A N     1 
ATOM   18437 C  CA    . THR A 1 3969 ? 171.745 287.885 175.557 1.00 15.74 ? 3969 THR A CA    1 
ATOM   18438 C  C     . THR A 1 3969 ? 173.149 288.460 175.446 1.00 18.12 ? 3969 THR A C     1 
ATOM   18439 O  O     . THR A 1 3969 ? 173.372 289.646 175.696 1.00 22.62 ? 3969 THR A O     1 
ATOM   18440 C  CB    . THR A 1 3969 ? 170.847 288.838 176.341 1.00 22.23 ? 3969 THR A CB    1 
ATOM   18441 O  OG1   . THR A 1 3969 ? 171.314 288.936 177.691 1.00 22.64 ? 3969 THR A OG1   1 
ATOM   18442 C  CG2   . THR A 1 3969 ? 169.398 288.359 176.333 1.00 18.44 ? 3969 THR A CG2   1 
ATOM   18443 N  N     . VAL A 1 3970 ? 174.113 287.588 175.133 1.00 22.70 ? 3970 VAL A N     1 
ATOM   18444 C  CA    . VAL A 1 3970 ? 175.539 288.024 175.038 1.00 17.78 ? 3970 VAL A CA    1 
ATOM   18445 C  C     . VAL A 1 3970 ? 175.642 289.102 173.951 1.00 20.23 ? 3970 VAL A C     1 
ATOM   18446 O  O     . VAL A 1 3970 ? 175.287 288.810 172.789 1.00 24.70 ? 3970 VAL A O     1 
ATOM   18447 C  CB    . VAL A 1 3970 ? 176.485 286.844 174.745 1.00 15.47 ? 3970 VAL A CB    1 
ATOM   18448 C  CG1   . VAL A 1 3970 ? 177.941 287.291 174.680 1.00 18.46 ? 3970 VAL A CG1   1 
ATOM   18449 C  CG2   . VAL A 1 3970 ? 176.316 285.714 175.751 1.00 12.54 ? 3970 VAL A CG2   1 
ATOM   18450 N  N     . PRO A 1 3971 ? 176.108 290.326 174.278 1.00 25.62 ? 3971 PRO A N     1 
ATOM   18451 C  CA    . PRO A 1 3971 ? 176.165 291.397 173.296 1.00 23.62 ? 3971 PRO A CA    1 
ATOM   18452 C  C     . PRO A 1 3971 ? 177.115 291.063 172.159 1.00 25.30 ? 3971 PRO A C     1 
ATOM   18453 O  O     . PRO A 1 3971 ? 178.135 290.385 172.402 1.00 30.73 ? 3971 PRO A O     1 
ATOM   18454 C  CB    . PRO A 1 3971 ? 176.652 292.597 174.124 1.00 19.09 ? 3971 PRO A CB    1 
ATOM   18455 C  CG    . PRO A 1 3971 ? 177.388 291.968 175.285 1.00 19.43 ? 3971 PRO A CG    1 
ATOM   18456 C  CD    . PRO A 1 3971 ? 176.601 290.707 175.591 1.00 17.37 ? 3971 PRO A CD    1 
ATOM   18457 N  N     . TYR A 1 3972 ? 176.801 291.527 170.948 1.00 23.44 ? 3972 TYR A N     1 
ATOM   18458 C  CA    . TYR A 1 3972 ? 177.715 291.317 169.793 1.00 23.21 ? 3972 TYR A CA    1 
ATOM   18459 C  C     . TYR A 1 3972 ? 178.928 292.210 170.009 1.00 26.33 ? 3972 TYR A C     1 
ATOM   18460 O  O     . TYR A 1 3972 ? 179.012 293.285 169.376 1.00 34.57 ? 3972 TYR A O     1 
ATOM   18461 C  CB    . TYR A 1 3972 ? 176.954 291.632 168.502 1.00 24.46 ? 3972 TYR A CB    1 
ATOM   18462 C  CG    . TYR A 1 3972 ? 177.760 291.462 167.223 1.00 26.69 ? 3972 TYR A CG    1 
ATOM   18463 C  CD1   . TYR A 1 3972 ? 178.757 290.499 167.123 1.00 25.45 ? 3972 TYR A CD1   1 
ATOM   18464 C  CD2   . TYR A 1 3972 ? 177.526 292.271 166.118 1.00 26.33 ? 3972 TYR A CD2   1 
ATOM   18465 C  CE1   . TYR A 1 3972 ? 179.491 290.343 165.959 1.00 25.52 ? 3972 TYR A CE1   1 
ATOM   18466 C  CE2   . TYR A 1 3972 ? 178.253 292.125 164.951 1.00 27.34 ? 3972 TYR A CE2   1 
ATOM   18467 C  CZ    . TYR A 1 3972 ? 179.239 291.159 164.871 1.00 26.76 ? 3972 TYR A CZ    1 
ATOM   18468 O  OH    . TYR A 1 3972 ? 179.957 291.018 163.721 1.00 32.46 ? 3972 TYR A OH    1 
ATOM   18469 N  N     . LEU A 1 3973 ? 179.845 291.785 170.880 1.00 25.13 ? 3973 LEU A N     1 
ATOM   18470 C  CA    . LEU A 1 3973 ? 181.014 292.631 171.232 1.00 21.68 ? 3973 LEU A CA    1 
ATOM   18471 C  C     . LEU A 1 3973 ? 182.279 292.123 170.519 1.00 24.62 ? 3973 LEU A C     1 
ATOM   18472 O  O     . LEU A 1 3973 ? 183.389 292.414 171.016 1.00 26.30 ? 3973 LEU A O     1 
ATOM   18473 C  CB    . LEU A 1 3973 ? 181.154 292.574 172.750 1.00 20.01 ? 3973 LEU A CB    1 
ATOM   18474 C  CG    . LEU A 1 3973 ? 181.910 293.729 173.411 1.00 24.80 ? 3973 LEU A CG    1 
ATOM   18475 C  CD1   . LEU A 1 3973 ? 181.059 294.985 173.419 1.00 22.14 ? 3973 LEU A CD1   1 
ATOM   18476 C  CD2   . LEU A 1 3973 ? 182.290 293.328 174.823 1.00 24.20 ? 3973 LEU A CD2   1 
ATOM   18477 N  N     . TRP A 1 3974 ? 182.123 291.395 169.409 1.00 22.83 ? 3974 TRP A N     1 
ATOM   18478 C  CA    . TRP A 1 3974 ? 183.305 290.930 168.635 1.00 21.87 ? 3974 TRP A CA    1 
ATOM   18479 C  C     . TRP A 1 3974 ? 183.244 291.465 167.202 1.00 25.59 ? 3974 TRP A C     1 
ATOM   18480 O  O     . TRP A 1 3974 ? 182.140 291.491 166.616 1.00 27.53 ? 3974 TRP A O     1 
ATOM   18481 C  CB    . TRP A 1 3974 ? 183.411 289.397 168.657 1.00 21.98 ? 3974 TRP A CB    1 
ATOM   18482 C  CG    . TRP A 1 3974 ? 182.279 288.683 167.969 1.00 21.19 ? 3974 TRP A CG    1 
ATOM   18483 C  CD1   . TRP A 1 3974 ? 182.219 288.310 166.657 1.00 20.98 ? 3974 TRP A CD1   1 
ATOM   18484 C  CD2   . TRP A 1 3974 ? 181.043 288.240 168.570 1.00 21.39 ? 3974 TRP A CD2   1 
ATOM   18485 N  NE1   . TRP A 1 3974 ? 181.035 287.672 166.398 1.00 23.47 ? 3974 TRP A NE1   1 
ATOM   18486 C  CE2   . TRP A 1 3974 ? 180.293 287.613 167.550 1.00 23.78 ? 3974 TRP A CE2   1 
ATOM   18487 C  CE3   . TRP A 1 3974 ? 180.502 288.312 169.857 1.00 20.21 ? 3974 TRP A CE3   1 
ATOM   18488 C  CZ2   . TRP A 1 3974 ? 179.035 287.067 167.786 1.00 21.47 ? 3974 TRP A CZ2   1 
ATOM   18489 C  CZ3   . TRP A 1 3974 ? 179.257 287.771 170.087 1.00 21.55 ? 3974 TRP A CZ3   1 
ATOM   18490 C  CH2   . TRP A 1 3974 ? 178.536 287.156 169.064 1.00 19.88 ? 3974 TRP A CH2   1 
ATOM   18491 N  N     . SER A 1 3975 ? 184.392 291.876 166.659 1.00 23.87 ? 3975 SER A N     1 
ATOM   18492 C  CA    . SER A 1 3975 ? 184.444 292.411 165.272 1.00 28.16 ? 3975 SER A CA    1 
ATOM   18493 C  C     . SER A 1 3975 ? 184.662 291.263 164.277 1.00 28.01 ? 3975 SER A C     1 
ATOM   18494 O  O     . SER A 1 3975 ? 185.215 290.221 164.693 1.00 27.13 ? 3975 SER A O     1 
ATOM   18495 C  CB    . SER A 1 3975 ? 185.517 293.459 165.139 1.00 29.88 ? 3975 SER A CB    1 
ATOM   18496 O  OG    . SER A 1 3975 ? 186.783 292.934 165.513 1.00 30.03 ? 3975 SER A OG    1 
ATOM   18497 N  N     . GLU A 1 3976 ? 184.247 291.451 163.020 1.00 29.52 ? 3976 GLU A N     1 
ATOM   18498 C  CA    . GLU A 1 3976 ? 184.438 290.410 161.974 1.00 28.56 ? 3976 GLU A CA    1 
ATOM   18499 C  C     . GLU A 1 3976 ? 184.216 291.032 160.587 1.00 34.16 ? 3976 GLU A C     1 
ATOM   18500 O  O     . GLU A 1 3976 ? 183.649 292.145 160.523 1.00 26.83 ? 3976 GLU A O     1 
ATOM   18501 C  CB    . GLU A 1 3976 ? 183.488 289.237 162.206 1.00 27.29 ? 3976 GLU A CB    1 
ATOM   18502 C  CG    . GLU A 1 3976 ? 182.017 289.620 162.074 1.00 24.24 ? 3976 GLU A CG    1 
ATOM   18503 C  CD    . GLU A 1 3976 ? 181.055 288.505 162.441 1.00 30.90 ? 3976 GLU A CD    1 
ATOM   18504 O  OE1   . GLU A 1 3976 ? 181.121 288.029 163.594 1.00 33.13 ? 3976 GLU A OE1   1 
ATOM   18505 O  OE2   . GLU A 1 3976 ? 180.239 288.120 161.580 1.00 30.05 ? 3976 GLU A OE2   1 
ATOM   18506 N  N     . GLU A 1 3977 ? 184.643 290.343 159.523 1.00 33.07 ? 3977 GLU A N     1 
ATOM   18507 C  CA    . GLU A 1 3977 ? 184.486 290.858 158.166 1.00 32.49 ? 3977 GLU A CA    1 
ATOM   18508 C  C     . GLU A 1 3977 ? 183.221 290.318 157.505 1.00 31.38 ? 3977 GLU A C     1 
ATOM   18509 O  O     . GLU A 1 3977 ? 182.329 291.087 157.132 1.00 35.92 ? 3977 GLU A O     1 
ATOM   18510 C  CB    . GLU A 1 3977 ? 185.720 290.513 157.325 1.00 32.39 ? 3977 GLU A CB    1 
ATOM   18511 C  CG    . GLU A 1 3977 ? 187.004 291.193 157.780 1.00 33.83 ? 3977 GLU A CG    1 
ATOM   18512 C  CD    . GLU A 1 3977 ? 187.670 290.477 158.941 1.00 41.07 ? 3977 GLU A CD    1 
ATOM   18513 O  OE1   . GLU A 1 3977 ? 187.158 289.417 159.362 1.00 35.48 ? 3977 GLU A OE1   1 
ATOM   18514 O  OE2   . GLU A 1 3977 ? 188.706 290.972 159.431 1.00 41.16 ? 3977 GLU A OE2   1 
ATOM   18515 N  N     . THR A 1 3978 ? 183.131 289.012 157.359 1.00 33.42 ? 3978 THR A N     1 
ATOM   18516 C  CA    . THR A 1 3978 ? 181.948 288.370 156.808 1.00 32.32 ? 3978 THR A CA    1 
ATOM   18517 C  C     . THR A 1 3978 ? 180.986 287.992 157.932 1.00 31.08 ? 3978 THR A C     1 
ATOM   18518 O  O     . THR A 1 3978 ? 181.414 287.757 159.066 1.00 29.07 ? 3978 THR A O     1 
ATOM   18519 C  CB    . THR A 1 3978 ? 182.340 287.121 156.019 1.00 35.03 ? 3978 THR A CB    1 
ATOM   18520 O  OG1   . THR A 1 3978 ? 181.163 286.435 155.575 1.00 36.32 ? 3978 THR A OG1   1 
ATOM   18521 C  CG2   . THR A 1 3978 ? 183.175 286.182 156.879 1.00 28.02 ? 3978 THR A CG2   1 
ATOM   18522 N  N     . PRO A 1 3979 ? 179.683 287.958 157.656 1.00 32.34 ? 3979 PRO A N     1 
ATOM   18523 C  CA    . PRO A 1 3979 ? 178.729 287.521 158.687 1.00 29.52 ? 3979 PRO A CA    1 
ATOM   18524 C  C     . PRO A 1 3979 ? 179.073 286.128 159.194 1.00 28.90 ? 3979 PRO A C     1 
ATOM   18525 O  O     . PRO A 1 3979 ? 179.354 285.216 158.416 1.00 31.39 ? 3979 PRO A O     1 
ATOM   18526 C  CB    . PRO A 1 3979 ? 177.386 287.543 157.953 1.00 29.04 ? 3979 PRO A CB    1 
ATOM   18527 C  CG    . PRO A 1 3979 ? 177.559 288.595 156.916 1.00 29.58 ? 3979 PRO A CG    1 
ATOM   18528 C  CD    . PRO A 1 3979 ? 179.000 288.514 156.477 1.00 31.77 ? 3979 PRO A CD    1 
ATOM   18529 N  N     . ALA A 1 3980 ? 179.042 285.973 160.515 1.00 29.17 ? 3980 ALA A N     1 
ATOM   18530 C  CA    . ALA A 1 3980 ? 179.445 284.726 161.139 1.00 25.53 ? 3980 ALA A CA    1 
ATOM   18531 C  C     . ALA A 1 3980 ? 178.331 283.689 161.049 1.00 23.00 ? 3980 ALA A C     1 
ATOM   18532 O  O     . ALA A 1 3980 ? 177.174 283.994 160.737 1.00 25.29 ? 3980 ALA A O     1 
ATOM   18533 C  CB    . ALA A 1 3980 ? 179.839 284.957 162.597 1.00 22.32 ? 3980 ALA A CB    1 
ATOM   18534 N  N     . THR A 1 3981 ? 178.691 282.453 161.322 1.00 18.58 ? 3981 THR A N     1 
ATOM   18535 C  CA    . THR A 1 3981 ? 177.772 281.329 161.332 1.00 17.58 ? 3981 THR A CA    1 
ATOM   18536 C  C     . THR A 1 3981 ? 177.162 281.155 162.720 1.00 16.29 ? 3981 THR A C     1 
ATOM   18537 O  O     . THR A 1 3981 ? 177.748 281.585 163.718 1.00 18.03 ? 3981 THR A O     1 
ATOM   18538 C  CB    . THR A 1 3981 ? 178.496 280.050 160.920 1.00 17.89 ? 3981 THR A CB    1 
ATOM   18539 O  OG1   . THR A 1 3981 ? 179.536 279.759 161.861 1.00 20.51 ? 3981 THR A OG1   1 
ATOM   18540 C  CG2   . THR A 1 3981 ? 179.107 280.219 159.541 1.00 14.65 ? 3981 THR A CG2   1 
ATOM   18541 N  N     . PRO A 1 3982 ? 175.978 280.534 162.814 1.00 17.23 ? 3982 PRO A N     1 
ATOM   18542 C  CA    . PRO A 1 3982 ? 175.384 280.309 164.144 1.00 13.78 ? 3982 PRO A CA    1 
ATOM   18543 C  C     . PRO A 1 3982 ? 176.290 279.536 165.085 1.00 13.67 ? 3982 PRO A C     1 
ATOM   18544 O  O     . PRO A 1 3982 ? 176.322 279.827 166.286 1.00 15.16 ? 3982 PRO A O     1 
ATOM   18545 C  CB    . PRO A 1 3982 ? 174.100 279.535 163.822 1.00 13.27 ? 3982 PRO A CB    1 
ATOM   18546 C  CG    . PRO A 1 3982 ? 173.775 279.918 162.422 1.00 8.38  ? 3982 PRO A CG    1 
ATOM   18547 C  CD    . PRO A 1 3982 ? 175.096 280.066 161.732 1.00 17.34 ? 3982 PRO A CD    1 
ATOM   18548 N  N     . ILE A 1 3983 ? 177.035 278.557 164.571 1.00 13.79 ? 3983 ILE A N     1 
ATOM   18549 C  CA    . ILE A 1 3983 ? 178.025 277.871 165.394 1.00 14.08 ? 3983 ILE A CA    1 
ATOM   18550 C  C     . ILE A 1 3983 ? 179.179 278.811 165.726 1.00 13.02 ? 3983 ILE A C     1 
ATOM   18551 O  O     . ILE A 1 3983 ? 179.689 278.824 166.852 1.00 13.39 ? 3983 ILE A O     1 
ATOM   18552 C  CB    . ILE A 1 3983 ? 178.515 276.593 164.690 1.00 12.88 ? 3983 ILE A CB    1 
ATOM   18553 C  CG1   . ILE A 1 3983 ? 177.352 275.616 164.506 1.00 8.68  ? 3983 ILE A CG1   1 
ATOM   18554 C  CG2   . ILE A 1 3983 ? 179.629 275.940 165.483 1.00 9.29  ? 3983 ILE A CG2   1 
ATOM   18555 C  CD1   . ILE A 1 3983 ? 177.666 274.453 163.599 1.00 17.19 ? 3983 ILE A CD1   1 
ATOM   18556 N  N     . GLY A 1 3984 ? 179.603 279.617 164.750 1.00 14.70 ? 3984 GLY A N     1 
ATOM   18557 C  CA    . GLY A 1 3984 ? 180.661 280.578 165.002 1.00 11.61 ? 3984 GLY A CA    1 
ATOM   18558 C  C     . GLY A 1 3984 ? 180.267 281.655 165.992 1.00 16.57 ? 3984 GLY A C     1 
ATOM   18559 O  O     . GLY A 1 3984 ? 181.100 282.117 166.777 1.00 11.66 ? 3984 GLY A O     1 
ATOM   18560 N  N     . GLN A 1 3985 ? 179.002 282.082 165.963 1.00 15.33 ? 3985 GLN A N     1 
ATOM   18561 C  CA    . GLN A 1 3985 ? 178.528 283.061 166.937 1.00 15.24 ? 3985 GLN A CA    1 
ATOM   18562 C  C     . GLN A 1 3985 ? 178.516 282.480 168.344 1.00 14.05 ? 3985 GLN A C     1 
ATOM   18563 O  O     . GLN A 1 3985 ? 178.829 283.179 169.315 1.00 16.95 ? 3985 GLN A O     1 
ATOM   18564 C  CB    . GLN A 1 3985 ? 177.135 283.557 166.555 1.00 14.52 ? 3985 GLN A CB    1 
ATOM   18565 C  CG    . GLN A 1 3985 ? 177.077 284.367 165.278 1.00 20.34 ? 3985 GLN A CG    1 
ATOM   18566 C  CD    . GLN A 1 3985 ? 175.666 284.811 164.946 1.00 27.54 ? 3985 GLN A CD    1 
ATOM   18567 O  OE1   . GLN A 1 3985 ? 174.713 284.457 165.639 1.00 22.89 ? 3985 GLN A OE1   1 
ATOM   18568 N  NE2   . GLN A 1 3985 ? 175.527 285.589 163.879 1.00 30.69 ? 3985 GLN A NE2   1 
ATOM   18569 N  N     . ALA A 1 3986 ? 178.144 281.205 168.475 1.00 15.82 ? 3986 ALA A N     1 
ATOM   18570 C  CA    . ALA A 1 3986 ? 178.130 280.564 169.787 1.00 9.91  ? 3986 ALA A CA    1 
ATOM   18571 C  C     . ALA A 1 3986 ? 179.530 280.494 170.384 1.00 9.45  ? 3986 ALA A C     1 
ATOM   18572 O  O     . ALA A 1 3986 ? 179.704 280.688 171.592 1.00 12.94 ? 3986 ALA A O     1 
ATOM   18573 C  CB    . ALA A 1 3986 ? 177.520 279.167 169.679 1.00 6.12  ? 3986 ALA A CB    1 
ATOM   18574 N  N     . ILE A 1 3987 ? 180.537 280.216 169.555 1.00 8.42  ? 3987 ILE A N     1 
ATOM   18575 C  CA    . ILE A 1 3987 ? 181.907 280.127 170.051 1.00 11.44 ? 3987 ILE A CA    1 
ATOM   18576 C  C     . ILE A 1 3987 ? 182.383 281.488 170.544 1.00 13.20 ? 3987 ILE A C     1 
ATOM   18577 O  O     . ILE A 1 3987 ? 183.082 281.584 171.561 1.00 11.73 ? 3987 ILE A O     1 
ATOM   18578 C  CB    . ILE A 1 3987 ? 182.830 279.562 168.959 1.00 13.05 ? 3987 ILE A CB    1 
ATOM   18579 C  CG1   . ILE A 1 3987 ? 182.402 278.142 168.605 1.00 11.93 ? 3987 ILE A CG1   1 
ATOM   18580 C  CG2   . ILE A 1 3987 ? 184.270 279.542 169.434 1.00 12.05 ? 3987 ILE A CG2   1 
ATOM   18581 C  CD1   . ILE A 1 3987 ? 183.067 277.599 167.385 1.00 14.14 ? 3987 ILE A CD1   1 
ATOM   18582 N  N     . HIS A 1 3988 ? 182.024 282.557 169.832 1.00 15.24 ? 3988 HIS A N     1 
ATOM   18583 C  CA    . HIS A 1 3988 ? 182.363 283.900 170.291 1.00 12.92 ? 3988 HIS A CA    1 
ATOM   18584 C  C     . HIS A 1 3988 ? 181.659 284.232 171.599 1.00 14.08 ? 3988 HIS A C     1 
ATOM   18585 O  O     . HIS A 1 3988 ? 182.262 284.818 172.504 1.00 18.60 ? 3988 HIS A O     1 
ATOM   18586 C  CB    . HIS A 1 3988 ? 182.019 284.925 169.210 1.00 13.43 ? 3988 HIS A CB    1 
ATOM   18587 C  CG    . HIS A 1 3988 ? 182.937 284.886 168.030 1.00 16.70 ? 3988 HIS A CG    1 
ATOM   18588 N  ND1   . HIS A 1 3988 ? 182.501 285.102 166.740 1.00 22.16 ? 3988 HIS A ND1   1 
ATOM   18589 C  CD2   . HIS A 1 3988 ? 184.267 284.660 167.943 1.00 16.92 ? 3988 HIS A CD2   1 
ATOM   18590 C  CE1   . HIS A 1 3988 ? 183.524 285.007 165.910 1.00 17.27 ? 3988 HIS A CE1   1 
ATOM   18591 N  NE2   . HIS A 1 3988 ? 184.608 284.739 166.615 1.00 18.78 ? 3988 HIS A NE2   1 
ATOM   18592 N  N     . ARG A 1 3989 ? 180.378 283.870 171.716 1.00 14.36 ? 3989 ARG A N     1 
ATOM   18593 C  CA    . ARG A 1 3989 ? 179.688 284.046 172.989 1.00 11.82 ? 3989 ARG A CA    1 
ATOM   18594 C  C     . ARG A 1 3989 ? 180.314 283.194 174.084 1.00 8.11  ? 3989 ARG A C     1 
ATOM   18595 O  O     . ARG A 1 3989 ? 180.342 283.606 175.248 1.00 13.91 ? 3989 ARG A O     1 
ATOM   18596 C  CB    . ARG A 1 3989 ? 178.203 283.708 172.856 1.00 8.04  ? 3989 ARG A CB    1 
ATOM   18597 C  CG    . ARG A 1 3989 ? 177.401 284.666 171.995 1.00 8.83  ? 3989 ARG A CG    1 
ATOM   18598 C  CD    . ARG A 1 3989 ? 175.947 284.238 171.941 1.00 10.89 ? 3989 ARG A CD    1 
ATOM   18599 N  NE    . ARG A 1 3989 ? 175.124 285.143 171.149 1.00 18.15 ? 3989 ARG A NE    1 
ATOM   18600 C  CZ    . ARG A 1 3989 ? 174.893 285.011 169.851 1.00 18.96 ? 3989 ARG A CZ    1 
ATOM   18601 N  NH1   . ARG A 1 3989 ? 175.369 283.986 169.166 1.00 25.03 ? 3989 ARG A NH1   1 
ATOM   18602 N  NH2   . ARG A 1 3989 ? 174.148 285.921 169.229 1.00 24.21 ? 3989 ARG A NH2   1 
ATOM   18603 N  N     . LEU A 1 3990 ? 180.806 282.007 173.732 1.00 7.53  ? 3990 LEU A N     1 
ATOM   18604 C  CA    . LEU A 1 3990 ? 181.432 281.139 174.721 1.00 8.46  ? 3990 LEU A CA    1 
ATOM   18605 C  C     . LEU A 1 3990 ? 182.706 281.768 175.274 1.00 11.21 ? 3990 LEU A C     1 
ATOM   18606 O  O     . LEU A 1 3990 ? 182.974 281.692 176.480 1.00 14.81 ? 3990 LEU A O     1 
ATOM   18607 C  CB    . LEU A 1 3990 ? 181.716 279.776 174.096 1.00 8.83  ? 3990 LEU A CB    1 
ATOM   18608 C  CG    . LEU A 1 3990 ? 182.301 278.685 174.982 1.00 6.45  ? 3990 LEU A CG    1 
ATOM   18609 C  CD1   . LEU A 1 3990 ? 181.338 278.336 176.104 1.00 6.90  ? 3990 LEU A CD1   1 
ATOM   18610 C  CD2   . LEU A 1 3990 ? 182.622 277.462 174.147 1.00 9.50  ? 3990 LEU A CD2   1 
ATOM   18611 N  N     . LEU A 1 3991 ? 183.504 282.393 174.406 1.00 15.90 ? 3991 LEU A N     1 
ATOM   18612 C  CA    . LEU A 1 3991 ? 184.697 283.096 174.867 1.00 9.85  ? 3991 LEU A CA    1 
ATOM   18613 C  C     . LEU A 1 3991 ? 184.333 284.328 175.687 1.00 11.14 ? 3991 LEU A C     1 
ATOM   18614 O  O     . LEU A 1 3991 ? 185.003 284.637 176.680 1.00 11.69 ? 3991 LEU A O     1 
ATOM   18615 C  CB    . LEU A 1 3991 ? 185.568 283.483 173.674 1.00 10.01 ? 3991 LEU A CB    1 
ATOM   18616 C  CG    . LEU A 1 3991 ? 186.271 282.350 172.928 1.00 10.95 ? 3991 LEU A CG    1 
ATOM   18617 C  CD1   . LEU A 1 3991 ? 186.838 282.856 171.617 1.00 16.84 ? 3991 LEU A CD1   1 
ATOM   18618 C  CD2   . LEU A 1 3991 ? 187.367 281.744 173.786 1.00 13.66 ? 3991 LEU A CD2   1 
ATOM   18619 N  N     . LEU A 1 3992 ? 183.286 285.049 175.280 1.00 11.12 ? 3992 LEU A N     1 
ATOM   18620 C  CA    . LEU A 1 3992 ? 182.862 286.229 176.030 1.00 9.61  ? 3992 LEU A CA    1 
ATOM   18621 C  C     . LEU A 1 3992 ? 182.359 285.855 177.417 1.00 11.83 ? 3992 LEU A C     1 
ATOM   18622 O  O     . LEU A 1 3992 ? 182.688 286.524 178.402 1.00 14.64 ? 3992 LEU A O     1 
ATOM   18623 C  CB    . LEU A 1 3992 ? 181.783 286.984 175.256 1.00 10.94 ? 3992 LEU A CB    1 
ATOM   18624 C  CG    . LEU A 1 3992 ? 182.275 287.849 174.097 1.00 14.23 ? 3992 LEU A CG    1 
ATOM   18625 C  CD1   . LEU A 1 3992 ? 181.109 288.344 173.262 1.00 12.71 ? 3992 LEU A CD1   1 
ATOM   18626 C  CD2   . LEU A 1 3992 ? 183.103 289.016 174.616 1.00 10.13 ? 3992 LEU A CD2   1 
ATOM   18627 N  N     . ILE A 1 3993 ? 181.563 284.789 177.517 1.00 11.52 ? 3993 ILE A N     1 
ATOM   18628 C  CA    . ILE A 1 3993 ? 181.042 284.372 178.815 1.00 10.28 ? 3993 ILE A CA    1 
ATOM   18629 C  C     . ILE A 1 3993 ? 182.179 283.945 179.732 1.00 10.18 ? 3993 ILE A C     1 
ATOM   18630 O  O     . ILE A 1 3993 ? 182.218 284.314 180.910 1.00 11.92 ? 3993 ILE A O     1 
ATOM   18631 C  CB    . ILE A 1 3993 ? 179.998 283.254 178.638 1.00 11.22 ? 3993 ILE A CB    1 
ATOM   18632 C  CG1   . ILE A 1 3993 ? 178.688 283.835 178.105 1.00 9.17  ? 3993 ILE A CG1   1 
ATOM   18633 C  CG2   . ILE A 1 3993 ? 179.767 282.519 179.948 1.00 4.37  ? 3993 ILE A CG2   1 
ATOM   18634 C  CD1   . ILE A 1 3993 ? 178.046 284.841 179.031 1.00 9.46  ? 3993 ILE A CD1   1 
ATOM   18635 N  N     . GLN A 1 3994 ? 183.134 283.177 179.200 1.00 11.19 ? 3994 GLN A N     1 
ATOM   18636 C  CA    . GLN A 1 3994 ? 184.274 282.752 180.005 1.00 8.02  ? 3994 GLN A CA    1 
ATOM   18637 C  C     . GLN A 1 3994 ? 185.079 283.942 180.511 1.00 10.53 ? 3994 GLN A C     1 
ATOM   18638 O  O     . GLN A 1 3994 ? 185.634 283.893 181.616 1.00 12.86 ? 3994 GLN A O     1 
ATOM   18639 C  CB    . GLN A 1 3994 ? 185.162 281.816 179.186 1.00 9.20  ? 3994 GLN A CB    1 
ATOM   18640 C  CG    . GLN A 1 3994 ? 186.488 281.463 179.835 1.00 10.60 ? 3994 GLN A CG    1 
ATOM   18641 C  CD    . GLN A 1 3994 ? 187.303 280.506 178.994 1.00 11.80 ? 3994 GLN A CD    1 
ATOM   18642 O  OE1   . GLN A 1 3994 ? 187.656 280.811 177.857 1.00 19.16 ? 3994 GLN A OE1   1 
ATOM   18643 N  NE2   . GLN A 1 3994 ? 187.602 279.338 179.548 1.00 10.78 ? 3994 GLN A NE2   1 
ATOM   18644 N  N     . ALA A 1 3995 ? 185.147 285.018 179.726 1.00 14.45 ? 3995 ALA A N     1 
ATOM   18645 C  CA    . ALA A 1 3995 ? 185.908 286.188 180.148 1.00 15.50 ? 3995 ALA A CA    1 
ATOM   18646 C  C     . ALA A 1 3995 ? 185.175 286.974 181.230 1.00 15.96 ? 3995 ALA A C     1 
ATOM   18647 O  O     . ALA A 1 3995 ? 185.789 287.411 182.209 1.00 19.39 ? 3995 ALA A O     1 
ATOM   18648 C  CB    . ALA A 1 3995 ? 186.207 287.080 178.943 1.00 13.41 ? 3995 ALA A CB    1 
ATOM   18649 N  N     . PHE A 1 3996 ? 183.865 287.157 181.080 1.00 13.25 ? 3996 PHE A N     1 
ATOM   18650 C  CA    . PHE A 1 3996 ? 183.107 288.048 181.950 1.00 13.04 ? 3996 PHE A CA    1 
ATOM   18651 C  C     . PHE A 1 3996 ? 182.278 287.328 183.004 1.00 18.76 ? 3996 PHE A C     1 
ATOM   18652 O  O     . PHE A 1 3996 ? 182.233 287.775 184.153 1.00 23.54 ? 3996 PHE A O     1 
ATOM   18653 C  CB    . PHE A 1 3996 ? 182.194 288.944 181.110 1.00 13.99 ? 3996 PHE A CB    1 
ATOM   18654 C  CG    . PHE A 1 3996 ? 182.937 289.878 180.205 1.00 18.42 ? 3996 PHE A CG    1 
ATOM   18655 C  CD1   . PHE A 1 3996 ? 183.545 291.011 180.713 1.00 17.79 ? 3996 PHE A CD1   1 
ATOM   18656 C  CD2   . PHE A 1 3996 ? 183.035 289.621 178.849 1.00 16.68 ? 3996 PHE A CD2   1 
ATOM   18657 C  CE1   . PHE A 1 3996 ? 184.231 291.873 179.886 1.00 19.94 ? 3996 PHE A CE1   1 
ATOM   18658 C  CE2   . PHE A 1 3996 ? 183.720 290.478 178.017 1.00 17.25 ? 3996 PHE A CE2   1 
ATOM   18659 C  CZ    . PHE A 1 3996 ? 184.318 291.606 178.534 1.00 21.11 ? 3996 PHE A CZ    1 
ATOM   18660 N  N     . ARG A 1 3997 ? 181.619 286.225 182.655 1.00 11.02 ? 3997 ARG A N     1 
ATOM   18661 C  CA    . ARG A 1 3997 ? 180.738 285.509 183.577 1.00 10.00 ? 3997 ARG A CA    1 
ATOM   18662 C  C     . ARG A 1 3997 ? 181.107 284.031 183.601 1.00 8.13  ? 3997 ARG A C     1 
ATOM   18663 O  O     . ARG A 1 3997 ? 180.378 283.185 183.073 1.00 11.96 ? 3997 ARG A O     1 
ATOM   18664 C  CB    . ARG A 1 3997 ? 179.272 285.699 183.186 1.00 10.25 ? 3997 ARG A CB    1 
ATOM   18665 C  CG    . ARG A 1 3997 ? 178.768 287.122 183.357 1.00 14.08 ? 3997 ARG A CG    1 
ATOM   18666 C  CD    . ARG A 1 3997 ? 178.970 287.608 184.783 1.00 12.25 ? 3997 ARG A CD    1 
ATOM   18667 N  NE    . ARG A 1 3997 ? 178.189 286.831 185.740 1.00 15.04 ? 3997 ARG A NE    1 
ATOM   18668 C  CZ    . ARG A 1 3997 ? 176.873 286.909 185.876 1.00 15.19 ? 3997 ARG A CZ    1 
ATOM   18669 N  NH1   . ARG A 1 3997 ? 176.149 287.750 185.156 1.00 15.51 ? 3997 ARG A NH1   1 
ATOM   18670 N  NH2   . ARG A 1 3997 ? 176.267 286.124 186.761 1.00 18.41 ? 3997 ARG A NH2   1 
ATOM   18671 N  N     . PRO A 1 3998 ? 182.241 283.685 184.214 1.00 7.79  ? 3998 PRO A N     1 
ATOM   18672 C  CA    . PRO A 1 3998 ? 182.638 282.270 184.265 1.00 8.18  ? 3998 PRO A CA    1 
ATOM   18673 C  C     . PRO A 1 3998 ? 181.663 281.390 185.030 1.00 8.28  ? 3998 PRO A C     1 
ATOM   18674 O  O     . PRO A 1 3998 ? 181.664 280.172 184.824 1.00 11.15 ? 3998 PRO A O     1 
ATOM   18675 C  CB    . PRO A 1 3998 ? 184.016 282.314 184.942 1.00 5.81  ? 3998 PRO A CB    1 
ATOM   18676 C  CG    . PRO A 1 3998 ? 184.014 283.585 185.713 1.00 7.81  ? 3998 PRO A CG    1 
ATOM   18677 C  CD    . PRO A 1 3998 ? 183.207 284.554 184.907 1.00 8.60  ? 3998 PRO A CD    1 
ATOM   18678 N  N     . ASP A 1 3999 ? 180.833 281.963 185.904 1.00 6.86  ? 3999 ASP A N     1 
ATOM   18679 C  CA    . ASP A 1 3999 ? 179.802 281.179 186.572 1.00 5.44  ? 3999 ASP A CA    1 
ATOM   18680 C  C     . ASP A 1 3999 ? 178.724 280.707 185.608 1.00 5.68  ? 3999 ASP A C     1 
ATOM   18681 O  O     . ASP A 1 3999 ? 178.027 279.731 185.904 1.00 7.23  ? 3999 ASP A O     1 
ATOM   18682 C  CB    . ASP A 1 3999 ? 179.173 281.992 187.703 1.00 7.46  ? 3999 ASP A CB    1 
ATOM   18683 C  CG    . ASP A 1 3999 ? 178.814 283.401 187.281 1.00 13.45 ? 3999 ASP A CG    1 
ATOM   18684 O  OD1   . ASP A 1 3999 ? 179.716 284.135 186.829 1.00 12.82 ? 3999 ASP A OD1   1 
ATOM   18685 O  OD2   . ASP A 1 3999 ? 177.629 283.776 187.401 1.00 13.60 ? 3999 ASP A OD2   1 
ATOM   18686 N  N     . ARG A 1 4000 ? 178.575 281.369 184.462 1.00 6.23  ? 4000 ARG A N     1 
ATOM   18687 C  CA    . ARG A 1 4000 ? 177.634 280.963 183.431 1.00 4.40  ? 4000 ARG A CA    1 
ATOM   18688 C  C     . ARG A 1 4000 ? 178.301 280.182 182.307 1.00 3.51  ? 4000 ARG A C     1 
ATOM   18689 O  O     . ARG A 1 4000 ? 177.680 279.963 181.264 1.00 4.68  ? 4000 ARG A O     1 
ATOM   18690 C  CB    . ARG A 1 4000 ? 176.914 282.188 182.868 1.00 6.26  ? 4000 ARG A CB    1 
ATOM   18691 C  CG    . ARG A 1 4000 ? 176.254 283.045 183.928 1.00 7.38  ? 4000 ARG A CG    1 
ATOM   18692 C  CD    . ARG A 1 4000 ? 175.240 282.250 184.723 1.00 8.73  ? 4000 ARG A CD    1 
ATOM   18693 N  NE    . ARG A 1 4000 ? 174.153 281.760 183.887 1.00 11.29 ? 4000 ARG A NE    1 
ATOM   18694 C  CZ    . ARG A 1 4000 ? 173.176 280.973 184.318 1.00 9.06  ? 4000 ARG A CZ    1 
ATOM   18695 N  NH1   . ARG A 1 4000 ? 173.130 280.551 185.571 1.00 10.14 ? 4000 ARG A NH1   1 
ATOM   18696 N  NH2   . ARG A 1 4000 ? 172.224 280.599 183.469 1.00 7.53  ? 4000 ARG A NH2   1 
ATOM   18697 N  N     . LEU A 1 4001 ? 179.552 279.761 182.500 1.00 3.79  ? 4001 LEU A N     1 
ATOM   18698 C  CA    . LEU A 1 4001 ? 180.269 279.047 181.449 1.00 4.53  ? 4001 LEU A CA    1 
ATOM   18699 C  C     . LEU A 1 4001 ? 179.608 277.711 181.131 1.00 3.09  ? 4001 LEU A C     1 
ATOM   18700 O  O     . LEU A 1 4001 ? 179.548 277.304 179.965 1.00 4.70  ? 4001 LEU A O     1 
ATOM   18701 C  CB    . LEU A 1 4001 ? 181.728 278.847 181.856 1.00 5.04  ? 4001 LEU A CB    1 
ATOM   18702 C  CG    . LEU A 1 4001 ? 182.649 278.254 180.792 1.00 3.66  ? 4001 LEU A CG    1 
ATOM   18703 C  CD1   . LEU A 1 4001 ? 182.609 279.102 179.532 1.00 6.19  ? 4001 LEU A CD1   1 
ATOM   18704 C  CD2   . LEU A 1 4001 ? 184.061 278.141 181.325 1.00 4.96  ? 4001 LEU A CD2   1 
ATOM   18705 N  N     . LEU A 1 4002 ? 179.116 277.010 182.155 1.00 2.36  ? 4002 LEU A N     1 
ATOM   18706 C  CA    . LEU A 1 4002 ? 178.386 275.769 181.915 1.00 2.19  ? 4002 LEU A CA    1 
ATOM   18707 C  C     . LEU A 1 4002 ? 177.106 276.023 181.130 1.00 2.41  ? 4002 LEU A C     1 
ATOM   18708 O  O     . LEU A 1 4002 ? 176.770 275.264 180.214 1.00 4.39  ? 4002 LEU A O     1 
ATOM   18709 C  CB    . LEU A 1 4002 ? 178.066 275.079 183.240 1.00 2.48  ? 4002 LEU A CB    1 
ATOM   18710 C  CG    . LEU A 1 4002 ? 179.244 274.508 184.023 1.00 2.78  ? 4002 LEU A CG    1 
ATOM   18711 C  CD1   . LEU A 1 4002 ? 178.742 273.823 185.279 1.00 1.87  ? 4002 LEU A CD1   1 
ATOM   18712 C  CD2   . LEU A 1 4002 ? 180.052 273.547 183.162 1.00 1.77  ? 4002 LEU A CD2   1 
ATOM   18713 N  N     . ALA A 1 4003 ? 176.375 277.084 181.479 1.00 2.89  ? 4003 ALA A N     1 
ATOM   18714 C  CA    . ALA A 1 4003 ? 175.153 277.411 180.754 1.00 3.07  ? 4003 ALA A CA    1 
ATOM   18715 C  C     . ALA A 1 4003 ? 175.453 277.750 179.298 1.00 3.21  ? 4003 ALA A C     1 
ATOM   18716 O  O     . ALA A 1 4003 ? 174.716 277.342 178.394 1.00 3.14  ? 4003 ALA A O     1 
ATOM   18717 C  CB    . ALA A 1 4003 ? 174.430 278.568 181.441 1.00 2.66  ? 4003 ALA A CB    1 
ATOM   18718 N  N     . MET A 1 4004 ? 176.531 278.497 179.055 1.00 4.05  ? 4004 MET A N     1 
ATOM   18719 C  CA    . MET A 1 4004 ? 176.928 278.799 177.685 1.00 4.54  ? 4004 MET A CA    1 
ATOM   18720 C  C     . MET A 1 4004 ? 177.414 277.553 176.955 1.00 3.87  ? 4004 MET A C     1 
ATOM   18721 O  O     . MET A 1 4004 ? 177.175 277.407 175.752 1.00 3.99  ? 4004 MET A O     1 
ATOM   18722 C  CB    . MET A 1 4004 ? 178.010 279.879 177.680 1.00 5.00  ? 4004 MET A CB    1 
ATOM   18723 C  CG    . MET A 1 4004 ? 178.280 280.489 176.320 1.00 4.87  ? 4004 MET A CG    1 
ATOM   18724 S  SD    . MET A 1 4004 ? 176.827 281.243 175.575 1.00 14.52 ? 4004 MET A SD    1 
ATOM   18725 C  CE    . MET A 1 4004 ? 176.684 280.296 174.066 1.00 6.42  ? 4004 MET A CE    1 
ATOM   18726 N  N     . ALA A 1 4005 ? 178.097 276.648 177.662 1.00 2.64  ? 4005 ALA A N     1 
ATOM   18727 C  CA    . ALA A 1 4005 ? 178.546 275.405 177.044 1.00 1.71  ? 4005 ALA A CA    1 
ATOM   18728 C  C     . ALA A 1 4005 ? 177.365 274.552 176.604 1.00 3.69  ? 4005 ALA A C     1 
ATOM   18729 O  O     . ALA A 1 4005 ? 177.404 273.923 175.539 1.00 3.44  ? 4005 ALA A O     1 
ATOM   18730 C  CB    . ALA A 1 4005 ? 179.441 274.629 178.008 1.00 1.59  ? 4005 ALA A CB    1 
ATOM   18731 N  N     . HIS A 1 4006 ? 176.307 274.511 177.416 1.00 2.64  ? 4006 HIS A N     1 
ATOM   18732 C  CA    . HIS A 1 4006 ? 175.105 273.777 177.032 1.00 2.21  ? 4006 HIS A CA    1 
ATOM   18733 C  C     . HIS A 1 4006 ? 174.466 274.383 175.790 1.00 2.75  ? 4006 HIS A C     1 
ATOM   18734 O  O     . HIS A 1 4006 ? 173.929 273.660 174.942 1.00 4.17  ? 4006 HIS A O     1 
ATOM   18735 C  CB    . HIS A 1 4006 ? 174.112 273.749 178.194 1.00 1.74  ? 4006 HIS A CB    1 
ATOM   18736 C  CG    . HIS A 1 4006 ? 174.372 272.652 179.180 1.00 3.06  ? 4006 HIS A CG    1 
ATOM   18737 N  ND1   . HIS A 1 4006 ? 175.270 272.781 180.218 1.00 4.66  ? 4006 HIS A ND1   1 
ATOM   18738 C  CD2   . HIS A 1 4006 ? 173.853 271.406 179.284 1.00 1.38  ? 4006 HIS A CD2   1 
ATOM   18739 C  CE1   . HIS A 1 4006 ? 175.294 271.662 180.918 1.00 2.47  ? 4006 HIS A CE1   1 
ATOM   18740 N  NE2   . HIS A 1 4006 ? 174.444 270.812 180.372 1.00 1.56  ? 4006 HIS A NE2   1 
ATOM   18741 N  N     . MET A 1 4007 ? 174.507 275.712 175.668 1.00 2.68  ? 4007 MET A N     1 
ATOM   18742 C  CA    . MET A 1 4007 ? 173.985 276.358 174.468 1.00 3.69  ? 4007 MET A CA    1 
ATOM   18743 C  C     . MET A 1 4007 ? 174.859 276.056 173.256 1.00 3.85  ? 4007 MET A C     1 
ATOM   18744 O  O     . MET A 1 4007 ? 174.351 275.904 172.140 1.00 3.50  ? 4007 MET A O     1 
ATOM   18745 C  CB    . MET A 1 4007 ? 173.870 277.865 174.693 1.00 4.91  ? 4007 MET A CB    1 
ATOM   18746 C  CG    . MET A 1 4007 ? 172.613 278.277 175.435 1.00 4.92  ? 4007 MET A CG    1 
ATOM   18747 S  SD    . MET A 1 4007 ? 172.644 279.994 175.974 1.00 26.38 ? 4007 MET A SD    1 
ATOM   18748 C  CE    . MET A 1 4007 ? 172.362 280.841 174.423 1.00 11.79 ? 4007 MET A CE    1 
ATOM   18749 N  N     . PHE A 1 4008 ? 176.177 275.970 173.456 1.00 4.91  ? 4008 PHE A N     1 
ATOM   18750 C  CA    . PHE A 1 4008 ? 177.065 275.575 172.366 1.00 4.59  ? 4008 PHE A CA    1 
ATOM   18751 C  C     . PHE A 1 4008 ? 176.759 274.160 171.895 1.00 3.73  ? 4008 PHE A C     1 
ATOM   18752 O  O     . PHE A 1 4008 ? 176.754 273.888 170.688 1.00 8.33  ? 4008 PHE A O     1 
ATOM   18753 C  CB    . PHE A 1 4008 ? 178.524 275.694 172.812 1.00 5.19  ? 4008 PHE A CB    1 
ATOM   18754 C  CG    . PHE A 1 4008 ? 179.509 275.121 171.834 1.00 6.54  ? 4008 PHE A CG    1 
ATOM   18755 C  CD1   . PHE A 1 4008 ? 179.955 275.867 170.759 1.00 8.87  ? 4008 PHE A CD1   1 
ATOM   18756 C  CD2   . PHE A 1 4008 ? 179.999 273.837 171.996 1.00 9.75  ? 4008 PHE A CD2   1 
ATOM   18757 C  CE1   . PHE A 1 4008 ? 180.862 275.337 169.861 1.00 8.97  ? 4008 PHE A CE1   1 
ATOM   18758 C  CE2   . PHE A 1 4008 ? 180.907 273.305 171.104 1.00 7.91  ? 4008 PHE A CE2   1 
ATOM   18759 C  CZ    . PHE A 1 4008 ? 181.338 274.057 170.036 1.00 6.32  ? 4008 PHE A CZ    1 
ATOM   18760 N  N     . VAL A 1 4009 ? 176.505 273.245 172.831 1.00 3.07  ? 4009 VAL A N     1 
ATOM   18761 C  CA    . VAL A 1 4009 ? 176.132 271.882 172.461 1.00 2.96  ? 4009 VAL A CA    1 
ATOM   18762 C  C     . VAL A 1 4009 ? 174.788 271.881 171.744 1.00 3.37  ? 4009 VAL A C     1 
ATOM   18763 O  O     . VAL A 1 4009 ? 174.587 271.151 170.766 1.00 4.06  ? 4009 VAL A O     1 
ATOM   18764 C  CB    . VAL A 1 4009 ? 176.120 270.976 173.706 1.00 2.67  ? 4009 VAL A CB    1 
ATOM   18765 C  CG1   . VAL A 1 4009 ? 175.539 269.610 173.377 1.00 1.22  ? 4009 VAL A CG1   1 
ATOM   18766 C  CG2   . VAL A 1 4009 ? 177.523 270.839 174.271 1.00 1.27  ? 4009 VAL A CG2   1 
ATOM   18767 N  N     . SER A 1 4010 ? 173.852 272.707 172.215 1.00 6.95  ? 4010 SER A N     1 
ATOM   18768 C  CA    . SER A 1 4010 ? 172.550 272.812 171.563 1.00 3.81  ? 4010 SER A CA    1 
ATOM   18769 C  C     . SER A 1 4010 ? 172.682 273.348 170.142 1.00 4.43  ? 4010 SER A C     1 
ATOM   18770 O  O     . SER A 1 4010 ? 171.954 272.922 169.239 1.00 6.28  ? 4010 SER A O     1 
ATOM   18771 C  CB    . SER A 1 4010 ? 171.627 273.705 172.390 1.00 4.05  ? 4010 SER A CB    1 
ATOM   18772 O  OG    . SER A 1 4010 ? 170.298 273.655 171.908 1.00 14.46 ? 4010 SER A OG    1 
ATOM   18773 N  N     . THR A 1 4011 ? 173.594 274.298 169.926 1.00 6.70  ? 4011 THR A N     1 
ATOM   18774 C  CA    . THR A 1 4011 ? 173.796 274.836 168.585 1.00 6.74  ? 4011 THR A CA    1 
ATOM   18775 C  C     . THR A 1 4011 ? 174.342 273.774 167.638 1.00 7.35  ? 4011 THR A C     1 
ATOM   18776 O  O     . THR A 1 4011 ? 173.910 273.681 166.484 1.00 4.89  ? 4011 THR A O     1 
ATOM   18777 C  CB    . THR A 1 4011 ? 174.734 276.041 168.642 1.00 6.15  ? 4011 THR A CB    1 
ATOM   18778 O  OG1   . THR A 1 4011 ? 174.165 277.052 169.481 1.00 9.84  ? 4011 THR A OG1   1 
ATOM   18779 C  CG2   . THR A 1 4011 ? 174.952 276.615 167.255 1.00 6.87  ? 4011 THR A CG2   1 
ATOM   18780 N  N     . ASN A 1 4012 ? 175.286 272.960 168.111 1.00 6.86  ? 4012 ASN A N     1 
ATOM   18781 C  CA    . ASN A 1 4012 ? 175.918 271.967 167.250 1.00 5.35  ? 4012 ASN A CA    1 
ATOM   18782 C  C     . ASN A 1 4012 ? 175.086 270.695 167.129 1.00 2.17  ? 4012 ASN A C     1 
ATOM   18783 O  O     . ASN A 1 4012 ? 174.905 270.175 166.025 1.00 3.73  ? 4012 ASN A O     1 
ATOM   18784 C  CB    . ASN A 1 4012 ? 177.315 271.635 167.777 1.00 4.90  ? 4012 ASN A CB    1 
ATOM   18785 C  CG    . ASN A 1 4012 ? 178.386 272.524 167.190 1.00 7.26  ? 4012 ASN A CG    1 
ATOM   18786 O  OD1   . ASN A 1 4012 ? 178.663 272.475 165.992 1.00 14.12 ? 4012 ASN A OD1   1 
ATOM   18787 N  ND2   . ASN A 1 4012 ? 178.996 273.348 168.030 1.00 11.43 ? 4012 ASN A ND2   1 
ATOM   18788 N  N     . LEU A 1 4013 ? 174.563 270.188 168.245 1.00 3.40  ? 4013 LEU A N     1 
ATOM   18789 C  CA    . LEU A 1 4013 ? 173.932 268.876 168.270 1.00 3.02  ? 4013 LEU A CA    1 
ATOM   18790 C  C     . LEU A 1 4013 ? 172.418 268.911 168.423 1.00 2.52  ? 4013 LEU A C     1 
ATOM   18791 O  O     . LEU A 1 4013 ? 171.777 267.870 168.248 1.00 4.76  ? 4013 LEU A O     1 
ATOM   18792 C  CB    . LEU A 1 4013 ? 174.536 268.028 169.399 1.00 1.06  ? 4013 LEU A CB    1 
ATOM   18793 C  CG    . LEU A 1 4013 ? 176.031 267.727 169.256 1.00 0.98  ? 4013 LEU A CG    1 
ATOM   18794 C  CD1   . LEU A 1 4013 ? 176.631 267.300 170.580 1.00 0.92  ? 4013 LEU A CD1   1 
ATOM   18795 C  CD2   . LEU A 1 4013 ? 176.264 266.663 168.200 1.00 1.23  ? 4013 LEU A CD2   1 
ATOM   18796 N  N     . GLY A 1 4014 ? 171.831 270.055 168.740 1.00 2.67  ? 4014 GLY A N     1 
ATOM   18797 C  CA    . GLY A 1 4014 ? 170.393 270.158 168.867 1.00 3.45  ? 4014 GLY A CA    1 
ATOM   18798 C  C     . GLY A 1 4014 ? 169.959 270.390 170.309 1.00 5.89  ? 4014 GLY A C     1 
ATOM   18799 O  O     . GLY A 1 4014 ? 170.691 270.126 171.268 1.00 5.97  ? 4014 GLY A O     1 
ATOM   18800 N  N     . GLU A 1 4015 ? 168.727 270.888 170.449 1.00 9.64  ? 4015 GLU A N     1 
ATOM   18801 C  CA    . GLU A 1 4015 ? 168.216 271.268 171.764 1.00 6.16  ? 4015 GLU A CA    1 
ATOM   18802 C  C     . GLU A 1 4015 ? 167.943 270.054 172.642 1.00 7.11  ? 4015 GLU A C     1 
ATOM   18803 O  O     . GLU A 1 4015 ? 168.123 270.122 173.862 1.00 11.35 ? 4015 GLU A O     1 
ATOM   18804 C  CB    . GLU A 1 4015 ? 166.946 272.110 171.605 1.00 8.66  ? 4015 GLU A CB    1 
ATOM   18805 C  CG    . GLU A 1 4015 ? 166.443 272.768 172.888 1.00 19.16 ? 4015 GLU A CG    1 
ATOM   18806 C  CD    . GLU A 1 4015 ? 165.588 271.845 173.742 1.00 26.83 ? 4015 GLU A CD    1 
ATOM   18807 O  OE1   . GLU A 1 4015 ? 164.931 270.945 173.177 1.00 24.03 ? 4015 GLU A OE1   1 
ATOM   18808 O  OE2   . GLU A 1 4015 ? 165.581 272.016 174.979 1.00 24.55 ? 4015 GLU A OE2   1 
ATOM   18809 N  N     . SER A 1 4016 ? 167.523 268.940 172.048 1.00 7.48  ? 4016 SER A N     1 
ATOM   18810 C  CA    . SER A 1 4016 ? 167.153 267.747 172.793 1.00 5.88  ? 4016 SER A CA    1 
ATOM   18811 C  C     . SER A 1 4016 ? 168.279 266.727 172.876 1.00 6.71  ? 4016 SER A C     1 
ATOM   18812 O  O     . SER A 1 4016 ? 168.034 265.582 173.264 1.00 7.92  ? 4016 SER A O     1 
ATOM   18813 C  CB    . SER A 1 4016 ? 165.912 267.106 172.168 1.00 10.70 ? 4016 SER A CB    1 
ATOM   18814 O  OG    . SER A 1 4016 ? 166.005 267.099 170.756 1.00 19.27 ? 4016 SER A OG    1 
ATOM   18815 N  N     . PHE A 1 4017 ? 169.505 267.114 172.516 1.00 8.41  ? 4017 PHE A N     1 
ATOM   18816 C  CA    . PHE A 1 4017 ? 170.611 266.164 172.511 1.00 2.35  ? 4017 PHE A CA    1 
ATOM   18817 C  C     . PHE A 1 4017 ? 170.902 265.633 173.911 1.00 2.39  ? 4017 PHE A C     1 
ATOM   18818 O  O     . PHE A 1 4017 ? 171.131 264.433 174.090 1.00 1.95  ? 4017 PHE A O     1 
ATOM   18819 C  CB    . PHE A 1 4017 ? 171.857 266.816 171.912 1.00 1.14  ? 4017 PHE A CB    1 
ATOM   18820 C  CG    . PHE A 1 4017 ? 173.028 265.886 171.797 1.00 1.23  ? 4017 PHE A CG    1 
ATOM   18821 C  CD1   . PHE A 1 4017 ? 173.154 265.043 170.710 1.00 0.51  ? 4017 PHE A CD1   1 
ATOM   18822 C  CD2   . PHE A 1 4017 ? 174.002 265.854 172.781 1.00 0.92  ? 4017 PHE A CD2   1 
ATOM   18823 C  CE1   . PHE A 1 4017 ? 174.228 264.185 170.603 1.00 0.50  ? 4017 PHE A CE1   1 
ATOM   18824 C  CE2   . PHE A 1 4017 ? 175.076 264.996 172.680 1.00 0.50  ? 4017 PHE A CE2   1 
ATOM   18825 C  CZ    . PHE A 1 4017 ? 175.189 264.162 171.587 1.00 0.57  ? 4017 PHE A CZ    1 
ATOM   18826 N  N     . MET A 1 4018 ? 170.892 266.509 174.912 1.00 2.28  ? 4018 MET A N     1 
ATOM   18827 C  CA    . MET A 1 4018 ? 171.218 266.132 176.280 1.00 1.38  ? 4018 MET A CA    1 
ATOM   18828 C  C     . MET A 1 4018 ? 169.982 265.867 177.131 1.00 4.22  ? 4018 MET A C     1 
ATOM   18829 O  O     . MET A 1 4018 ? 170.106 265.689 178.346 1.00 7.92  ? 4018 MET A O     1 
ATOM   18830 C  CB    . MET A 1 4018 ? 172.078 267.217 176.926 1.00 1.46  ? 4018 MET A CB    1 
ATOM   18831 C  CG    . MET A 1 4018 ? 173.503 267.264 176.409 1.00 1.69  ? 4018 MET A CG    1 
ATOM   18832 S  SD    . MET A 1 4018 ? 174.489 268.549 177.196 1.00 13.64 ? 4018 MET A SD    1 
ATOM   18833 C  CE    . MET A 1 4018 ? 175.365 267.590 178.427 1.00 1.18  ? 4018 MET A CE    1 
ATOM   18834 N  N     . SER A 1 4019 ? 168.798 265.821 176.517 1.00 5.71  ? 4019 SER A N     1 
ATOM   18835 C  CA    . SER A 1 4019 ? 167.557 265.747 177.275 1.00 5.50  ? 4019 SER A CA    1 
ATOM   18836 C  C     . SER A 1 4019 ? 167.317 264.379 177.902 1.00 7.52  ? 4019 SER A C     1 
ATOM   18837 O  O     . SER A 1 4019 ? 166.543 264.283 178.859 1.00 14.85 ? 4019 SER A O     1 
ATOM   18838 C  CB    . SER A 1 4019 ? 166.380 266.119 176.373 1.00 8.68  ? 4019 SER A CB    1 
ATOM   18839 O  OG    . SER A 1 4019 ? 166.382 267.508 176.087 1.00 14.84 ? 4019 SER A OG    1 
ATOM   18840 N  N     . ILE A 1 4020 ? 167.956 263.324 177.395 1.00 6.74  ? 4020 ILE A N     1 
ATOM   18841 C  CA    . ILE A 1 4020 ? 167.729 261.988 177.941 1.00 4.67  ? 4020 ILE A CA    1 
ATOM   18842 C  C     . ILE A 1 4020 ? 168.255 261.893 179.367 1.00 7.51  ? 4020 ILE A C     1 
ATOM   18843 O  O     . ILE A 1 4020 ? 167.655 261.234 180.224 1.00 11.73 ? 4020 ILE A O     1 
ATOM   18844 C  CB    . ILE A 1 4020 ? 168.364 260.922 177.027 1.00 5.71  ? 4020 ILE A CB    1 
ATOM   18845 C  CG1   . ILE A 1 4020 ? 167.767 261.007 175.624 1.00 8.18  ? 4020 ILE A CG1   1 
ATOM   18846 C  CG2   . ILE A 1 4020 ? 168.163 259.527 177.595 1.00 3.27  ? 4020 ILE A CG2   1 
ATOM   18847 C  CD1   . ILE A 1 4020 ? 166.276 260.761 175.582 1.00 3.84  ? 4020 ILE A CD1   1 
ATOM   18848 N  N     . MET A 1 4021 ? 169.377 262.555 179.651 1.00 7.11  ? 4021 MET A N     1 
ATOM   18849 C  CA    . MET A 1 4021 ? 169.967 262.479 180.980 1.00 6.02  ? 4021 MET A CA    1 
ATOM   18850 C  C     . MET A 1 4021 ? 169.078 263.106 182.046 1.00 9.87  ? 4021 MET A C     1 
ATOM   18851 O  O     . MET A 1 4021 ? 169.211 262.768 183.227 1.00 15.57 ? 4021 MET A O     1 
ATOM   18852 C  CB    . MET A 1 4021 ? 171.340 263.151 180.978 1.00 5.72  ? 4021 MET A CB    1 
ATOM   18853 C  CG    . MET A 1 4021 ? 172.435 262.370 180.257 1.00 6.34  ? 4021 MET A CG    1 
ATOM   18854 S  SD    . MET A 1 4021 ? 172.348 260.573 180.409 1.00 12.12 ? 4021 MET A SD    1 
ATOM   18855 C  CE    . MET A 1 4021 ? 171.566 260.127 178.859 1.00 2.74  ? 4021 MET A CE    1 
ATOM   18856 N  N     . GLU A 1 4022 ? 168.177 264.009 181.660 1.00 11.79 ? 4022 GLU A N     1 
ATOM   18857 C  CA    . GLU A 1 4022 ? 167.239 264.597 182.609 1.00 8.03  ? 4022 GLU A CA    1 
ATOM   18858 C  C     . GLU A 1 4022 ? 166.115 263.642 182.985 1.00 8.05  ? 4022 GLU A C     1 
ATOM   18859 O  O     . GLU A 1 4022 ? 165.518 263.801 184.055 1.00 6.82  ? 4022 GLU A O     1 
ATOM   18860 C  CB    . GLU A 1 4022 ? 166.640 265.881 182.029 1.00 11.50 ? 4022 GLU A CB    1 
ATOM   18861 C  CG    . GLU A 1 4022 ? 167.539 267.103 182.134 1.00 11.79 ? 4022 GLU A CG    1 
ATOM   18862 C  CD    . GLU A 1 4022 ? 168.431 267.072 183.355 1.00 17.93 ? 4022 GLU A CD    1 
ATOM   18863 O  OE1   . GLU A 1 4022 ? 169.657 266.896 183.192 1.00 20.91 ? 4022 GLU A OE1   1 
ATOM   18864 O  OE2   . GLU A 1 4022 ? 167.905 267.226 184.478 1.00 18.17 ? 4022 GLU A OE2   1 
ATOM   18865 N  N     . GLN A 1 4023 ? 165.812 262.663 182.133 1.00 11.18 ? 4023 GLN A N     1 
ATOM   18866 C  CA    . GLN A 1 4023 ? 164.754 261.702 182.388 1.00 7.79  ? 4023 GLN A CA    1 
ATOM   18867 C  C     . GLN A 1 4023 ? 165.239 260.596 183.324 1.00 6.91  ? 4023 GLN A C     1 
ATOM   18868 O  O     . GLN A 1 4023 ? 166.437 260.311 183.394 1.00 7.87  ? 4023 GLN A O     1 
ATOM   18869 C  CB    . GLN A 1 4023 ? 164.272 261.084 181.080 1.00 8.93  ? 4023 GLN A CB    1 
ATOM   18870 C  CG    . GLN A 1 4023 ? 163.423 262.006 180.227 1.00 12.21 ? 4023 GLN A CG    1 
ATOM   18871 C  CD    . GLN A 1 4023 ? 162.202 262.514 180.962 1.00 20.30 ? 4023 GLN A CD    1 
ATOM   18872 O  OE1   . GLN A 1 4023 ? 161.416 261.733 181.496 1.00 19.90 ? 4023 GLN A OE1   1 
ATOM   18873 N  NE2   . GLN A 1 4023 ? 162.034 263.830 180.994 1.00 16.60 ? 4023 GLN A NE2   1 
ATOM   18874 N  N     . PRO A 1 4024 ? 164.327 259.967 184.068 1.00 7.40  ? 4024 PRO A N     1 
ATOM   18875 C  CA    . PRO A 1 4024 ? 164.715 258.806 184.874 1.00 6.28  ? 4024 PRO A CA    1 
ATOM   18876 C  C     . PRO A 1 4024 ? 165.159 257.646 183.995 1.00 9.02  ? 4024 PRO A C     1 
ATOM   18877 O  O     . PRO A 1 4024 ? 164.692 257.473 182.867 1.00 11.29 ? 4024 PRO A O     1 
ATOM   18878 C  CB    . PRO A 1 4024 ? 163.435 258.467 185.649 1.00 7.37  ? 4024 PRO A CB    1 
ATOM   18879 C  CG    . PRO A 1 4024 ? 162.336 259.095 184.863 1.00 8.93  ? 4024 PRO A CG    1 
ATOM   18880 C  CD    . PRO A 1 4024 ? 162.919 260.340 184.283 1.00 8.51  ? 4024 PRO A CD    1 
ATOM   18881 N  N     . LEU A 1 4025 ? 166.079 256.849 184.532 1.00 6.44  ? 4025 LEU A N     1 
ATOM   18882 C  CA    . LEU A 1 4025 ? 166.679 255.761 183.770 1.00 6.68  ? 4025 LEU A CA    1 
ATOM   18883 C  C     . LEU A 1 4025 ? 165.640 254.700 183.425 1.00 10.76 ? 4025 LEU A C     1 
ATOM   18884 O  O     . LEU A 1 4025 ? 164.912 254.220 184.298 1.00 12.16 ? 4025 LEU A O     1 
ATOM   18885 C  CB    . LEU A 1 4025 ? 167.828 255.142 184.565 1.00 5.51  ? 4025 LEU A CB    1 
ATOM   18886 C  CG    . LEU A 1 4025 ? 168.654 254.057 183.874 1.00 7.24  ? 4025 LEU A CG    1 
ATOM   18887 C  CD1   . LEU A 1 4025 ? 169.311 254.608 182.626 1.00 10.52 ? 4025 LEU A CD1   1 
ATOM   18888 C  CD2   . LEU A 1 4025 ? 169.695 253.503 184.828 1.00 5.28  ? 4025 LEU A CD2   1 
ATOM   18889 N  N     . ASP A 1 4026 ? 165.586 254.328 182.149 1.00 13.22 ? 4026 ASP A N     1 
ATOM   18890 C  CA    . ASP A 1 4026 ? 164.659 253.310 181.656 1.00 11.30 ? 4026 ASP A CA    1 
ATOM   18891 C  C     . ASP A 1 4026 ? 165.395 251.974 181.696 1.00 14.54 ? 4026 ASP A C     1 
ATOM   18892 O  O     . ASP A 1 4026 ? 165.867 251.471 180.676 1.00 15.52 ? 4026 ASP A O     1 
ATOM   18893 C  CB    . ASP A 1 4026 ? 164.173 253.651 180.252 1.00 13.93 ? 4026 ASP A CB    1 
ATOM   18894 C  CG    . ASP A 1 4026 ? 163.049 252.748 179.782 1.00 20.14 ? 4026 ASP A CG    1 
ATOM   18895 O  OD1   . ASP A 1 4026 ? 162.676 251.811 180.520 1.00 20.11 ? 4026 ASP A OD1   1 
ATOM   18896 O  OD2   . ASP A 1 4026 ? 162.535 252.977 178.668 1.00 28.61 ? 4026 ASP A OD2   1 
ATOM   18897 N  N     . LEU A 1 4027 ? 165.490 251.399 182.896 1.00 12.88 ? 4027 LEU A N     1 
ATOM   18898 C  CA    . LEU A 1 4027 ? 166.233 250.156 183.067 1.00 9.86  ? 4027 LEU A CA    1 
ATOM   18899 C  C     . LEU A 1 4027 ? 165.566 248.991 182.345 1.00 14.65 ? 4027 LEU A C     1 
ATOM   18900 O  O     . LEU A 1 4027 ? 166.246 248.032 181.965 1.00 17.97 ? 4027 LEU A O     1 
ATOM   18901 C  CB    . LEU A 1 4027 ? 166.384 249.847 184.556 1.00 9.11  ? 4027 LEU A CB    1 
ATOM   18902 C  CG    . LEU A 1 4027 ? 167.659 249.125 184.991 1.00 15.37 ? 4027 LEU A CG    1 
ATOM   18903 C  CD1   . LEU A 1 4027 ? 168.876 249.979 184.702 1.00 12.18 ? 4027 LEU A CD1   1 
ATOM   18904 C  CD2   . LEU A 1 4027 ? 167.589 248.776 186.468 1.00 11.92 ? 4027 LEU A CD2   1 
ATOM   18905 N  N     . THR A 1 4028 ? 164.249 249.061 182.143 1.00 11.88 ? 4028 THR A N     1 
ATOM   18906 C  CA    . THR A 1 4028 ? 163.541 247.974 181.475 1.00 13.95 ? 4028 THR A CA    1 
ATOM   18907 C  C     . THR A 1 4028 ? 163.999 247.820 180.029 1.00 14.83 ? 4028 THR A C     1 
ATOM   18908 O  O     . THR A 1 4028 ? 164.335 246.716 179.585 1.00 19.04 ? 4028 THR A O     1 
ATOM   18909 C  CB    . THR A 1 4028 ? 162.033 248.222 181.529 1.00 14.30 ? 4028 THR A CB    1 
ATOM   18910 O  OG1   . THR A 1 4028 ? 161.606 248.288 182.896 1.00 16.75 ? 4028 THR A OG1   1 
ATOM   18911 C  CG2   . THR A 1 4028 ? 161.283 247.111 180.817 1.00 10.28 ? 4028 THR A CG2   1 
ATOM   18912 N  N     . HIS A 1 4029 ? 164.018 248.922 179.279 1.00 14.90 ? 4029 HIS A N     1 
ATOM   18913 C  CA    . HIS A 1 4029 ? 164.364 248.847 177.864 1.00 14.10 ? 4029 HIS A CA    1 
ATOM   18914 C  C     . HIS A 1 4029 ? 165.824 248.458 177.664 1.00 12.56 ? 4029 HIS A C     1 
ATOM   18915 O  O     . HIS A 1 4029 ? 166.143 247.668 176.769 1.00 13.73 ? 4029 HIS A O     1 
ATOM   18916 C  CB    . HIS A 1 4029 ? 164.066 250.183 177.184 1.00 18.48 ? 4029 HIS A CB    1 
ATOM   18917 C  CG    . HIS A 1 4029 ? 164.426 250.214 175.732 1.00 17.10 ? 4029 HIS A CG    1 
ATOM   18918 N  ND1   . HIS A 1 4029 ? 164.179 249.157 174.883 1.00 14.45 ? 4029 HIS A ND1   1 
ATOM   18919 C  CD2   . HIS A 1 4029 ? 165.023 251.170 174.982 1.00 17.43 ? 4029 HIS A CD2   1 
ATOM   18920 C  CE1   . HIS A 1 4029 ? 164.603 249.463 173.670 1.00 18.35 ? 4029 HIS A CE1   1 
ATOM   18921 N  NE2   . HIS A 1 4029 ? 165.120 250.678 173.703 1.00 23.78 ? 4029 HIS A NE2   1 
ATOM   18922 N  N     . ILE A 1 4030 ? 166.722 249.004 178.484 1.00 14.22 ? 4030 ILE A N     1 
ATOM   18923 C  CA    . ILE A 1 4030 ? 168.147 248.755 178.296 1.00 14.39 ? 4030 ILE A CA    1 
ATOM   18924 C  C     . ILE A 1 4030 ? 168.491 247.300 178.587 1.00 9.95  ? 4030 ILE A C     1 
ATOM   18925 O  O     . ILE A 1 4030 ? 169.223 246.659 177.823 1.00 11.74 ? 4030 ILE A O     1 
ATOM   18926 C  CB    . ILE A 1 4030 ? 168.975 249.717 179.166 1.00 9.20  ? 4030 ILE A CB    1 
ATOM   18927 C  CG1   . ILE A 1 4030 ? 168.582 251.166 178.875 1.00 4.08  ? 4030 ILE A CG1   1 
ATOM   18928 C  CG2   . ILE A 1 4030 ? 170.454 249.497 178.927 1.00 8.59  ? 4030 ILE A CG2   1 
ATOM   18929 C  CD1   . ILE A 1 4030 ? 169.264 252.173 179.759 1.00 5.98  ? 4030 ILE A CD1   1 
ATOM   18930 N  N     . VAL A 1 4031 ? 167.979 246.754 179.690 1.00 12.04 ? 4031 VAL A N     1 
ATOM   18931 C  CA    . VAL A 1 4031 ? 168.308 245.380 180.056 1.00 8.82  ? 4031 VAL A CA    1 
ATOM   18932 C  C     . VAL A 1 4031 ? 167.716 244.400 179.051 1.00 8.34  ? 4031 VAL A C     1 
ATOM   18933 O  O     . VAL A 1 4031 ? 168.348 243.399 178.694 1.00 15.27 ? 4031 VAL A O     1 
ATOM   18934 C  CB    . VAL A 1 4031 ? 167.837 245.085 181.494 1.00 10.45 ? 4031 VAL A CB    1 
ATOM   18935 C  CG1   . VAL A 1 4031 ? 167.897 243.593 181.790 1.00 10.44 ? 4031 VAL A CG1   1 
ATOM   18936 C  CG2   . VAL A 1 4031 ? 168.683 245.856 182.491 1.00 4.90  ? 4031 VAL A CG2   1 
ATOM   18937 N  N     . GLY A 1 4032 ? 166.501 244.673 178.569 1.00 10.46 ? 4032 GLY A N     1 
ATOM   18938 C  CA    . GLY A 1 4032 ? 165.843 243.745 177.668 1.00 10.53 ? 4032 GLY A CA    1 
ATOM   18939 C  C     . GLY A 1 4032 ? 166.365 243.748 176.247 1.00 15.31 ? 4032 GLY A C     1 
ATOM   18940 O  O     . GLY A 1 4032 ? 166.232 242.744 175.542 1.00 20.02 ? 4032 GLY A O     1 
ATOM   18941 N  N     . THR A 1 4033 ? 166.954 244.854 175.799 1.00 16.96 ? 4033 THR A N     1 
ATOM   18942 C  CA    . THR A 1 4033 ? 167.343 244.983 174.399 1.00 12.12 ? 4033 THR A CA    1 
ATOM   18943 C  C     . THR A 1 4033 ? 168.809 245.318 174.188 1.00 11.82 ? 4033 THR A C     1 
ATOM   18944 O  O     . THR A 1 4033 ? 169.414 244.823 173.234 1.00 18.74 ? 4033 THR A O     1 
ATOM   18945 C  CB    . THR A 1 4033 ? 166.484 246.056 173.704 1.00 15.35 ? 4033 THR A CB    1 
ATOM   18946 O  OG1   . THR A 1 4033 ? 166.690 247.324 174.339 1.00 19.76 ? 4033 THR A OG1   1 
ATOM   18947 C  CG2   . THR A 1 4033 ? 165.011 245.692 173.766 1.00 17.42 ? 4033 THR A CG2   1 
ATOM   18948 N  N     . GLU A 1 4034 ? 169.405 246.147 175.042 1.00 11.21 ? 4034 GLU A N     1 
ATOM   18949 C  CA    . GLU A 1 4034 ? 170.755 246.635 174.793 1.00 8.28  ? 4034 GLU A CA    1 
ATOM   18950 C  C     . GLU A 1 4034 ? 171.840 245.814 175.476 1.00 9.51  ? 4034 GLU A C     1 
ATOM   18951 O  O     . GLU A 1 4034 ? 173.000 245.880 175.056 1.00 13.38 ? 4034 GLU A O     1 
ATOM   18952 C  CB    . GLU A 1 4034 ? 170.881 248.095 175.239 1.00 8.27  ? 4034 GLU A CB    1 
ATOM   18953 C  CG    . GLU A 1 4034 ? 170.063 249.075 174.420 1.00 10.94 ? 4034 GLU A CG    1 
ATOM   18954 C  CD    . GLU A 1 4034 ? 170.203 250.504 174.909 1.00 14.83 ? 4034 GLU A CD    1 
ATOM   18955 O  OE1   . GLU A 1 4034 ? 170.839 250.714 175.959 1.00 13.73 ? 4034 GLU A OE1   1 
ATOM   18956 O  OE2   . GLU A 1 4034 ? 169.675 251.418 174.243 1.00 25.10 ? 4034 GLU A OE2   1 
ATOM   18957 N  N     . VAL A 1 4035 ? 171.505 245.048 176.508 1.00 11.60 ? 4035 VAL A N     1 
ATOM   18958 C  CA    . VAL A 1 4035 ? 172.496 244.336 177.306 1.00 8.56  ? 4035 VAL A CA    1 
ATOM   18959 C  C     . VAL A 1 4035 ? 172.547 242.884 176.851 1.00 7.42  ? 4035 VAL A C     1 
ATOM   18960 O  O     . VAL A 1 4035 ? 171.518 242.199 176.812 1.00 10.23 ? 4035 VAL A O     1 
ATOM   18961 C  CB    . VAL A 1 4035 ? 172.185 244.435 178.807 1.00 4.86  ? 4035 VAL A CB    1 
ATOM   18962 C  CG1   . VAL A 1 4035 ? 173.042 243.457 179.591 1.00 5.06  ? 4035 VAL A CG1   1 
ATOM   18963 C  CG2   . VAL A 1 4035 ? 172.411 245.854 179.298 1.00 5.57  ? 4035 VAL A CG2   1 
ATOM   18964 N  N     . LYS A 1 4036 ? 173.739 242.422 176.499 1.00 6.64  ? 4036 LYS A N     1 
ATOM   18965 C  CA    . LYS A 1 4036 ? 173.947 241.020 176.183 1.00 7.62  ? 4036 LYS A CA    1 
ATOM   18966 C  C     . LYS A 1 4036 ? 174.007 240.197 177.468 1.00 5.63  ? 4036 LYS A C     1 
ATOM   18967 O  O     . LYS A 1 4036 ? 174.447 240.692 178.509 1.00 8.00  ? 4036 LYS A O     1 
ATOM   18968 C  CB    . LYS A 1 4036 ? 175.238 240.839 175.395 1.00 8.18  ? 4036 LYS A CB    1 
ATOM   18969 C  CG    . LYS A 1 4036 ? 175.253 241.563 174.065 1.00 9.02  ? 4036 LYS A CG    1 
ATOM   18970 C  CD    . LYS A 1 4036 ? 174.283 240.951 173.078 1.00 9.13  ? 4036 LYS A CD    1 
ATOM   18971 C  CE    . LYS A 1 4036 ? 174.312 241.701 171.757 1.00 21.95 ? 4036 LYS A CE    1 
ATOM   18972 N  NZ    . LYS A 1 4036 ? 175.605 241.516 171.044 1.00 19.75 ? 4036 LYS A NZ    1 
ATOM   18973 N  N     . PRO A 1 4037 ? 173.562 238.939 177.423 1.00 5.86  ? 4037 PRO A N     1 
ATOM   18974 C  CA    . PRO A 1 4037 ? 173.610 238.106 178.638 1.00 4.69  ? 4037 PRO A CA    1 
ATOM   18975 C  C     . PRO A 1 4037 ? 175.010 237.920 179.192 1.00 5.32  ? 4037 PRO A C     1 
ATOM   18976 O  O     . PRO A 1 4037 ? 175.175 237.836 180.416 1.00 9.28  ? 4037 PRO A O     1 
ATOM   18977 C  CB    . PRO A 1 4037 ? 172.997 236.775 178.177 1.00 5.13  ? 4037 PRO A CB    1 
ATOM   18978 C  CG    . PRO A 1 4037 ? 173.055 236.806 176.684 1.00 7.92  ? 4037 PRO A CG    1 
ATOM   18979 C  CD    . PRO A 1 4037 ? 172.940 238.238 176.291 1.00 5.21  ? 4037 PRO A CD    1 
ATOM   18980 N  N     . ASN A 1 4038 ? 176.028 237.857 178.333 1.00 7.13  ? 4038 ASN A N     1 
ATOM   18981 C  CA    . ASN A 1 4038 ? 177.404 237.737 178.800 1.00 6.94  ? 4038 ASN A CA    1 
ATOM   18982 C  C     . ASN A 1 4038 ? 177.937 239.030 179.401 1.00 4.50  ? 4038 ASN A C     1 
ATOM   18983 O  O     . ASN A 1 4038 ? 178.986 239.001 180.055 1.00 4.56  ? 4038 ASN A O     1 
ATOM   18984 C  CB    . ASN A 1 4038 ? 178.311 237.297 177.648 1.00 7.71  ? 4038 ASN A CB    1 
ATOM   18985 C  CG    . ASN A 1 4038 ? 178.188 238.198 176.436 1.00 19.60 ? 4038 ASN A CG    1 
ATOM   18986 O  OD1   . ASN A 1 4038 ? 178.919 239.180 176.300 1.00 18.25 ? 4038 ASN A OD1   1 
ATOM   18987 N  ND2   . ASN A 1 4038 ? 177.256 237.873 175.547 1.00 15.21 ? 4038 ASN A ND2   1 
ATOM   18988 N  N     . THR A 1 4039 ? 177.252 240.152 179.199 1.00 3.75  ? 4039 THR A N     1 
ATOM   18989 C  CA    . THR A 1 4039 ? 177.718 241.436 179.701 1.00 3.09  ? 4039 THR A CA    1 
ATOM   18990 C  C     . THR A 1 4039 ? 177.098 241.715 181.062 1.00 3.02  ? 4039 THR A C     1 
ATOM   18991 O  O     . THR A 1 4039 ? 175.868 241.833 181.154 1.00 8.32  ? 4039 THR A O     1 
ATOM   18992 C  CB    . THR A 1 4039 ? 177.363 242.550 178.732 1.00 3.29  ? 4039 THR A CB    1 
ATOM   18993 O  OG1   . THR A 1 4039 ? 178.052 242.346 177.491 1.00 10.34 ? 4039 THR A OG1   1 
ATOM   18994 C  CG2   . THR A 1 4039 ? 177.754 243.899 179.303 1.00 1.62  ? 4039 THR A CG2   1 
ATOM   18995 N  N     . PRO A 1 4040 ? 177.885 241.817 182.127 1.00 1.06  ? 4040 PRO A N     1 
ATOM   18996 C  CA    . PRO A 1 4040 ? 177.315 242.188 183.426 1.00 0.37  ? 4040 PRO A CA    1 
ATOM   18997 C  C     . PRO A 1 4040 ? 176.803 243.619 183.419 1.00 0.39  ? 4040 PRO A C     1 
ATOM   18998 O  O     . PRO A 1 4040 ? 177.312 244.486 182.706 1.00 0.34  ? 4040 PRO A O     1 
ATOM   18999 C  CB    . PRO A 1 4040 ? 178.495 242.023 184.390 1.00 0.25  ? 4040 PRO A CB    1 
ATOM   19000 C  CG    . PRO A 1 4040 ? 179.701 242.174 183.536 1.00 0.36  ? 4040 PRO A CG    1 
ATOM   19001 C  CD    . PRO A 1 4040 ? 179.338 241.597 182.200 1.00 0.71  ? 4040 PRO A CD    1 
ATOM   19002 N  N     . VAL A 1 4041 ? 175.776 243.860 184.225 1.00 0.53  ? 4041 VAL A N     1 
ATOM   19003 C  CA    . VAL A 1 4041 ? 175.205 245.189 184.386 1.00 0.24  ? 4041 VAL A CA    1 
ATOM   19004 C  C     . VAL A 1 4041 ? 175.750 245.761 185.687 1.00 0.24  ? 4041 VAL A C     1 
ATOM   19005 O  O     . VAL A 1 4041 ? 175.397 245.298 186.777 1.00 0.31  ? 4041 VAL A O     1 
ATOM   19006 C  CB    . VAL A 1 4041 ? 173.672 245.157 184.386 1.00 0.33  ? 4041 VAL A CB    1 
ATOM   19007 C  CG1   . VAL A 1 4041 ? 173.125 246.555 184.558 1.00 0.28  ? 4041 VAL A CG1   1 
ATOM   19008 C  CG2   . VAL A 1 4041 ? 173.154 244.528 183.106 1.00 0.96  ? 4041 VAL A CG2   1 
ATOM   19009 N  N     . LEU A 1 4042 ? 176.606 246.771 185.580 1.00 0.36  ? 4042 LEU A N     1 
ATOM   19010 C  CA    . LEU A 1 4042 ? 177.272 247.352 186.736 1.00 0.46  ? 4042 LEU A CA    1 
ATOM   19011 C  C     . LEU A 1 4042 ? 176.429 248.495 187.287 1.00 0.61  ? 4042 LEU A C     1 
ATOM   19012 O  O     . LEU A 1 4042 ? 176.217 249.503 186.606 1.00 0.57  ? 4042 LEU A O     1 
ATOM   19013 C  CB    . LEU A 1 4042 ? 178.672 247.837 186.364 1.00 0.44  ? 4042 LEU A CB    1 
ATOM   19014 C  CG    . LEU A 1 4042 ? 179.527 246.863 185.546 1.00 0.68  ? 4042 LEU A CG    1 
ATOM   19015 C  CD1   . LEU A 1 4042 ? 180.915 247.430 185.311 1.00 0.83  ? 4042 LEU A CD1   1 
ATOM   19016 C  CD2   . LEU A 1 4042 ? 179.610 245.501 186.219 1.00 0.24  ? 4042 LEU A CD2   1 
ATOM   19017 N  N     . MET A 1 4043 ? 175.949 248.333 188.516 1.00 1.42  ? 4043 MET A N     1 
ATOM   19018 C  CA    . MET A 1 4043 ? 175.138 249.343 189.193 1.00 0.78  ? 4043 MET A CA    1 
ATOM   19019 C  C     . MET A 1 4043 ? 176.070 250.122 190.115 1.00 0.91  ? 4043 MET A C     1 
ATOM   19020 O  O     . MET A 1 4043 ? 176.238 249.786 191.286 1.00 1.91  ? 4043 MET A O     1 
ATOM   19021 C  CB    . MET A 1 4043 ? 173.997 248.696 189.968 1.00 1.36  ? 4043 MET A CB    1 
ATOM   19022 C  CG    . MET A 1 4043 ? 172.950 247.974 189.131 1.00 0.78  ? 4043 MET A CG    1 
ATOM   19023 S  SD    . MET A 1 4043 ? 172.035 249.054 188.024 1.00 33.78 ? 4043 MET A SD    1 
ATOM   19024 C  CE    . MET A 1 4043 ? 171.096 247.875 187.070 1.00 18.30 ? 4043 MET A CE    1 
ATOM   19025 N  N     . CYS A 1 4044 ? 176.691 251.169 189.576 1.00 1.05  ? 4044 CYS A N     1 
ATOM   19026 C  CA    . CYS A 1 4044 ? 177.635 251.991 190.320 1.00 0.59  ? 4044 CYS A CA    1 
ATOM   19027 C  C     . CYS A 1 4044 ? 176.908 253.190 190.912 1.00 0.71  ? 4044 CYS A C     1 
ATOM   19028 O  O     . CYS A 1 4044 ? 176.201 253.907 190.197 1.00 1.04  ? 4044 CYS A O     1 
ATOM   19029 C  CB    . CYS A 1 4044 ? 178.780 252.460 189.422 1.00 0.81  ? 4044 CYS A CB    1 
ATOM   19030 S  SG    . CYS A 1 4044 ? 179.547 251.165 188.431 1.00 6.85  ? 4044 CYS A SG    1 
ATOM   19031 N  N     . SER A 1 4045 ? 177.084 253.409 192.210 1.00 1.00  ? 4045 SER A N     1 
ATOM   19032 C  CA    . SER A 1 4045 ? 176.370 254.466 192.907 1.00 1.65  ? 4045 SER A CA    1 
ATOM   19033 C  C     . SER A 1 4045 ? 177.319 255.250 193.799 1.00 1.51  ? 4045 SER A C     1 
ATOM   19034 O  O     . SER A 1 4045 ? 178.309 254.718 194.307 1.00 1.80  ? 4045 SER A O     1 
ATOM   19035 C  CB    . SER A 1 4045 ? 175.213 253.900 193.741 1.00 1.27  ? 4045 SER A CB    1 
ATOM   19036 O  OG    . SER A 1 4045 ? 175.679 252.962 194.688 1.00 5.16  ? 4045 SER A OG    1 
ATOM   19037 N  N     . VAL A 1 4046 ? 177.005 256.529 193.970 1.00 2.22  ? 4046 VAL A N     1 
ATOM   19038 C  CA    . VAL A 1 4046 ? 177.707 257.397 194.912 1.00 4.55  ? 4046 VAL A CA    1 
ATOM   19039 C  C     . VAL A 1 4046 ? 177.231 257.046 196.317 1.00 5.11  ? 4046 VAL A C     1 
ATOM   19040 O  O     . VAL A 1 4046 ? 176.164 256.432 196.465 1.00 6.92  ? 4046 VAL A O     1 
ATOM   19041 C  CB    . VAL A 1 4046 ? 177.472 258.880 194.579 1.00 4.23  ? 4046 VAL A CB    1 
ATOM   19042 C  CG1   . VAL A 1 4046 ? 177.923 259.179 193.156 1.00 1.34  ? 4046 VAL A CG1   1 
ATOM   19043 C  CG2   . VAL A 1 4046 ? 176.010 259.239 194.770 1.00 4.84  ? 4046 VAL A CG2   1 
ATOM   19044 N  N     . PRO A 1 4047 ? 177.980 257.392 197.366 1.00 6.02  ? 4047 PRO A N     1 
ATOM   19045 C  CA    . PRO A 1 4047 ? 177.551 257.036 198.724 1.00 5.31  ? 4047 PRO A CA    1 
ATOM   19046 C  C     . PRO A 1 4047 ? 176.174 257.593 199.054 1.00 8.70  ? 4047 PRO A C     1 
ATOM   19047 O  O     . PRO A 1 4047 ? 175.838 258.726 198.704 1.00 14.05 ? 4047 PRO A O     1 
ATOM   19048 C  CB    . PRO A 1 4047 ? 178.635 257.662 199.603 1.00 7.29  ? 4047 PRO A CB    1 
ATOM   19049 C  CG    . PRO A 1 4047 ? 179.846 257.643 198.740 1.00 9.24  ? 4047 PRO A CG    1 
ATOM   19050 C  CD    . PRO A 1 4047 ? 179.348 257.936 197.352 1.00 6.69  ? 4047 PRO A CD    1 
ATOM   19051 N  N     . GLY A 1 4048 ? 175.379 256.779 199.743 1.00 12.00 ? 4048 GLY A N     1 
ATOM   19052 C  CA    . GLY A 1 4048 ? 174.006 257.109 200.045 1.00 10.70 ? 4048 GLY A CA    1 
ATOM   19053 C  C     . GLY A 1 4048 ? 173.003 256.642 199.017 1.00 11.02 ? 4048 GLY A C     1 
ATOM   19054 O  O     . GLY A 1 4048 ? 171.795 256.717 199.273 1.00 13.22 ? 4048 GLY A O     1 
ATOM   19055 N  N     . TYR A 1 4049 ? 173.459 256.157 197.868 1.00 8.49  ? 4049 TYR A N     1 
ATOM   19056 C  CA    . TYR A 1 4049 ? 172.590 255.659 196.815 1.00 5.81  ? 4049 TYR A CA    1 
ATOM   19057 C  C     . TYR A 1 4049 ? 172.914 254.198 196.550 1.00 10.92 ? 4049 TYR A C     1 
ATOM   19058 O  O     . TYR A 1 4049 ? 174.065 253.768 196.664 1.00 11.51 ? 4049 TYR A O     1 
ATOM   19059 C  CB    . TYR A 1 4049 ? 172.729 256.497 195.535 1.00 5.97  ? 4049 TYR A CB    1 
ATOM   19060 C  CG    . TYR A 1 4049 ? 172.079 257.858 195.654 1.00 7.55  ? 4049 TYR A CG    1 
ATOM   19061 C  CD1   . TYR A 1 4049 ? 172.596 258.822 196.510 1.00 5.81  ? 4049 TYR A CD1   1 
ATOM   19062 C  CD2   . TYR A 1 4049 ? 170.939 258.172 194.928 1.00 3.06  ? 4049 TYR A CD2   1 
ATOM   19063 C  CE1   . TYR A 1 4049 ? 171.998 260.056 196.640 1.00 6.49  ? 4049 TYR A CE1   1 
ATOM   19064 C  CE2   . TYR A 1 4049 ? 170.336 259.407 195.049 1.00 4.41  ? 4049 TYR A CE2   1 
ATOM   19065 C  CZ    . TYR A 1 4049 ? 170.871 260.345 195.904 1.00 8.36  ? 4049 TYR A CZ    1 
ATOM   19066 O  OH    . TYR A 1 4049 ? 170.277 261.579 196.030 1.00 8.00  ? 4049 TYR A OH    1 
ATOM   19067 N  N     . ASP A 1 4050 ? 171.879 253.430 196.224 1.00 11.61 ? 4050 ASP A N     1 
ATOM   19068 C  CA    . ASP A 1 4050 ? 172.021 251.991 196.044 1.00 11.03 ? 4050 ASP A CA    1 
ATOM   19069 C  C     . ASP A 1 4050 ? 170.967 251.537 195.050 1.00 8.03  ? 4050 ASP A C     1 
ATOM   19070 O  O     . ASP A 1 4050 ? 169.771 251.745 195.275 1.00 7.78  ? 4050 ASP A O     1 
ATOM   19071 C  CB    . ASP A 1 4050 ? 171.873 251.256 197.381 1.00 8.29  ? 4050 ASP A CB    1 
ATOM   19072 C  CG    . ASP A 1 4050 ? 171.670 249.766 197.212 1.00 15.20 ? 4050 ASP A CG    1 
ATOM   19073 O  OD1   . ASP A 1 4050 ? 172.551 249.109 196.620 1.00 14.92 ? 4050 ASP A OD1   1 
ATOM   19074 O  OD2   . ASP A 1 4050 ? 170.631 249.251 197.676 1.00 15.59 ? 4050 ASP A OD2   1 
ATOM   19075 N  N     . ALA A 1 4051 ? 171.411 250.924 193.957 1.00 7.02  ? 4051 ALA A N     1 
ATOM   19076 C  CA    . ALA A 1 4051 ? 170.535 250.536 192.862 1.00 6.66  ? 4051 ALA A CA    1 
ATOM   19077 C  C     . ALA A 1 4051 ? 169.949 249.142 193.038 1.00 5.65  ? 4051 ALA A C     1 
ATOM   19078 O  O     . ALA A 1 4051 ? 169.262 248.656 192.134 1.00 7.95  ? 4051 ALA A O     1 
ATOM   19079 C  CB    . ALA A 1 4051 ? 171.289 250.618 191.533 1.00 4.36  ? 4051 ALA A CB    1 
ATOM   19080 N  N     . SER A 1 4052 ? 170.207 248.492 194.175 1.00 5.69  ? 4052 SER A N     1 
ATOM   19081 C  CA    . SER A 1 4052 ? 169.701 247.141 194.389 1.00 7.08  ? 4052 SER A CA    1 
ATOM   19082 C  C     . SER A 1 4052 ? 168.180 247.108 194.347 1.00 8.99  ? 4052 SER A C     1 
ATOM   19083 O  O     . SER A 1 4052 ? 167.588 246.194 193.761 1.00 5.02  ? 4052 SER A O     1 
ATOM   19084 C  CB    . SER A 1 4052 ? 170.210 246.599 195.725 1.00 9.21  ? 4052 SER A CB    1 
ATOM   19085 O  OG    . SER A 1 4052 ? 171.597 246.844 195.878 1.00 9.31  ? 4052 SER A OG    1 
ATOM   19086 N  N     . GLY A 1 4053 ? 167.531 248.102 194.957 1.00 7.18  ? 4053 GLY A N     1 
ATOM   19087 C  CA    . GLY A 1 4053 ? 166.079 248.150 194.933 1.00 5.11  ? 4053 GLY A CA    1 
ATOM   19088 C  C     . GLY A 1 4053 ? 165.517 248.296 193.533 1.00 10.18 ? 4053 GLY A C     1 
ATOM   19089 O  O     . GLY A 1 4053 ? 164.495 247.693 193.201 1.00 13.63 ? 4053 GLY A O     1 
ATOM   19090 N  N     . HIS A 1 4054 ? 166.178 249.095 192.691 1.00 7.53  ? 4054 HIS A N     1 
ATOM   19091 C  CA    . HIS A 1 4054 ? 165.714 249.260 191.316 1.00 8.65  ? 4054 HIS A CA    1 
ATOM   19092 C  C     . HIS A 1 4054 ? 165.723 247.933 190.568 1.00 9.33  ? 4054 HIS A C     1 
ATOM   19093 O  O     . HIS A 1 4054 ? 164.782 247.624 189.828 1.00 15.14 ? 4054 HIS A O     1 
ATOM   19094 C  CB    . HIS A 1 4054 ? 166.575 250.290 190.584 1.00 6.72  ? 4054 HIS A CB    1 
ATOM   19095 C  CG    . HIS A 1 4054 ? 166.718 251.588 191.315 1.00 15.32 ? 4054 HIS A CG    1 
ATOM   19096 N  ND1   . HIS A 1 4054 ? 165.668 252.193 191.966 1.00 22.85 ? 4054 HIS A ND1   1 
ATOM   19097 C  CD2   . HIS A 1 4054 ? 167.791 252.392 191.499 1.00 14.10 ? 4054 HIS A CD2   1 
ATOM   19098 C  CE1   . HIS A 1 4054 ? 166.085 253.319 192.518 1.00 21.62 ? 4054 HIS A CE1   1 
ATOM   19099 N  NE2   . HIS A 1 4054 ? 167.370 253.464 192.251 1.00 15.59 ? 4054 HIS A NE2   1 
ATOM   19100 N  N     . VAL A 1 4055 ? 166.780 247.138 190.745 1.00 5.23  ? 4055 VAL A N     1 
ATOM   19101 C  CA    . VAL A 1 4055 ? 166.832 245.824 190.114 1.00 8.16  ? 4055 VAL A CA    1 
ATOM   19102 C  C     . VAL A 1 4055 ? 165.737 244.923 190.668 1.00 6.88  ? 4055 VAL A C     1 
ATOM   19103 O  O     . VAL A 1 4055 ? 165.066 244.203 189.919 1.00 7.08  ? 4055 VAL A O     1 
ATOM   19104 C  CB    . VAL A 1 4055 ? 168.226 245.196 190.298 1.00 6.16  ? 4055 VAL A CB    1 
ATOM   19105 C  CG1   . VAL A 1 4055 ? 168.314 243.878 189.549 1.00 1.50  ? 4055 VAL A CG1   1 
ATOM   19106 C  CG2   . VAL A 1 4055 ? 169.307 246.156 189.832 1.00 4.86  ? 4055 VAL A CG2   1 
ATOM   19107 N  N     . GLU A 1 4056 ? 165.540 244.947 191.988 1.00 10.41 ? 4056 GLU A N     1 
ATOM   19108 C  CA    . GLU A 1 4056 ? 164.500 244.132 192.605 1.00 9.99  ? 4056 GLU A CA    1 
ATOM   19109 C  C     . GLU A 1 4056 ? 163.120 244.512 192.088 1.00 12.17 ? 4056 GLU A C     1 
ATOM   19110 O  O     . GLU A 1 4056 ? 162.292 243.638 191.802 1.00 14.21 ? 4056 GLU A O     1 
ATOM   19111 C  CB    . GLU A 1 4056 ? 164.567 244.276 194.125 1.00 8.14  ? 4056 GLU A CB    1 
ATOM   19112 C  CG    . GLU A 1 4056 ? 165.826 243.687 194.734 1.00 11.70 ? 4056 GLU A CG    1 
ATOM   19113 C  CD    . GLU A 1 4056 ? 165.887 243.859 196.236 1.00 16.63 ? 4056 GLU A CD    1 
ATOM   19114 O  OE1   . GLU A 1 4056 ? 165.008 244.549 196.796 1.00 14.57 ? 4056 GLU A OE1   1 
ATOM   19115 O  OE2   . GLU A 1 4056 ? 166.824 243.313 196.856 1.00 19.81 ? 4056 GLU A OE2   1 
ATOM   19116 N  N     . ASP A 1 4057 ? 162.851 245.813 191.965 1.00 11.26 ? 4057 ASP A N     1 
ATOM   19117 C  CA    . ASP A 1 4057 ? 161.587 246.252 191.382 1.00 13.64 ? 4057 ASP A CA    1 
ATOM   19118 C  C     . ASP A 1 4057 ? 161.498 245.868 189.910 1.00 14.11 ? 4057 ASP A C     1 
ATOM   19119 O  O     . ASP A 1 4057 ? 160.434 245.459 189.435 1.00 18.23 ? 4057 ASP A O     1 
ATOM   19120 C  CB    . ASP A 1 4057 ? 161.424 247.762 191.554 1.00 12.67 ? 4057 ASP A CB    1 
ATOM   19121 C  CG    . ASP A 1 4057 ? 161.510 248.194 193.002 1.00 18.89 ? 4057 ASP A CG    1 
ATOM   19122 O  OD1   . ASP A 1 4057 ? 160.971 247.480 193.871 1.00 21.54 ? 4057 ASP A OD1   1 
ATOM   19123 O  OD2   . ASP A 1 4057 ? 162.114 249.253 193.271 1.00 22.48 ? 4057 ASP A OD2   1 
ATOM   19124 N  N     . LEU A 1 4058 ? 162.608 245.985 189.179 1.00 13.04 ? 4058 LEU A N     1 
ATOM   19125 C  CA    . LEU A 1 4058 ? 162.608 245.653 187.758 1.00 12.48 ? 4058 LEU A CA    1 
ATOM   19126 C  C     . LEU A 1 4058 ? 162.258 244.189 187.532 1.00 15.72 ? 4058 LEU A C     1 
ATOM   19127 O  O     . LEU A 1 4058 ? 161.522 243.856 186.595 1.00 16.85 ? 4058 LEU A O     1 
ATOM   19128 C  CB    . LEU A 1 4058 ? 163.971 245.978 187.148 1.00 13.05 ? 4058 LEU A CB    1 
ATOM   19129 C  CG    . LEU A 1 4058 ? 164.245 245.426 185.748 1.00 17.12 ? 4058 LEU A CG    1 
ATOM   19130 C  CD1   . LEU A 1 4058 ? 163.346 246.094 184.719 1.00 7.09  ? 4058 LEU A CD1   1 
ATOM   19131 C  CD2   . LEU A 1 4058 ? 165.711 245.594 185.385 1.00 10.96 ? 4058 LEU A CD2   1 
ATOM   19132 N  N     . ALA A 1 4059 ? 162.785 243.296 188.373 1.00 14.15 ? 4059 ALA A N     1 
ATOM   19133 C  CA    . ALA A 1 4059 ? 162.439 241.885 188.259 1.00 12.02 ? 4059 ALA A CA    1 
ATOM   19134 C  C     . ALA A 1 4059 ? 160.958 241.656 188.534 1.00 17.47 ? 4059 ALA A C     1 
ATOM   19135 O  O     . ALA A 1 4059 ? 160.325 240.804 187.901 1.00 15.78 ? 4059 ALA A O     1 
ATOM   19136 C  CB    . ALA A 1 4059 ? 163.303 241.056 189.209 1.00 7.00  ? 4059 ALA A CB    1 
ATOM   19137 N  N     . ALA A 1 4060 ? 160.391 242.402 189.486 1.00 16.19 ? 4060 ALA A N     1 
ATOM   19138 C  CA    . ALA A 1 4060 ? 158.967 242.277 189.773 1.00 16.53 ? 4060 ALA A CA    1 
ATOM   19139 C  C     . ALA A 1 4060 ? 158.115 242.712 188.585 1.00 19.58 ? 4060 ALA A C     1 
ATOM   19140 O  O     . ALA A 1 4060 ? 157.126 242.051 188.249 1.00 24.13 ? 4060 ALA A O     1 
ATOM   19141 C  CB    . ALA A 1 4060 ? 158.611 243.093 191.015 1.00 13.79 ? 4060 ALA A CB    1 
ATOM   19142 N  N     . GLU A 1 4061 ? 158.485 243.821 187.936 1.00 17.94 ? 4061 GLU A N     1 
ATOM   19143 C  CA    . GLU A 1 4061 ? 157.728 244.290 186.778 1.00 19.93 ? 4061 GLU A CA    1 
ATOM   19144 C  C     . GLU A 1 4061 ? 157.745 243.260 185.658 1.00 20.35 ? 4061 GLU A C     1 
ATOM   19145 O  O     . GLU A 1 4061 ? 156.708 242.964 185.049 1.00 29.14 ? 4061 GLU A O     1 
ATOM   19146 C  CB    . GLU A 1 4061 ? 158.294 245.622 186.281 1.00 23.86 ? 4061 GLU A CB    1 
ATOM   19147 C  CG    . GLU A 1 4061 ? 158.442 246.689 187.352 1.00 21.35 ? 4061 GLU A CG    1 
ATOM   19148 C  CD    . GLU A 1 4061 ? 159.602 247.625 187.079 1.00 29.84 ? 4061 GLU A CD    1 
ATOM   19149 O  OE1   . GLU A 1 4061 ? 160.272 247.456 186.038 1.00 31.13 ? 4061 GLU A OE1   1 
ATOM   19150 O  OE2   . GLU A 1 4061 ? 159.849 248.527 187.905 1.00 30.83 ? 4061 GLU A OE2   1 
ATOM   19151 N  N     . GLN A 1 4062 ? 158.916 242.693 185.376 1.00 18.42 ? 4062 GLN A N     1 
ATOM   19152 C  CA    . GLN A 1 4062 ? 159.040 241.679 184.340 1.00 22.17 ? 4062 GLN A CA    1 
ATOM   19153 C  C     . GLN A 1 4062 ? 158.505 240.323 184.777 1.00 22.95 ? 4062 GLN A C     1 
ATOM   19154 O  O     . GLN A 1 4062 ? 158.446 239.406 183.951 1.00 23.94 ? 4062 GLN A O     1 
ATOM   19155 C  CB    . GLN A 1 4062 ? 160.504 241.543 183.914 1.00 20.24 ? 4062 GLN A CB    1 
ATOM   19156 C  CG    . GLN A 1 4062 ? 161.068 242.787 183.244 1.00 14.92 ? 4062 GLN A CG    1 
ATOM   19157 C  CD    . GLN A 1 4062 ? 160.355 243.130 181.955 1.00 24.49 ? 4062 GLN A CD    1 
ATOM   19158 O  OE1   . GLN A 1 4062 ? 159.620 244.115 181.883 1.00 28.62 ? 4062 GLN A OE1   1 
ATOM   19159 N  NE2   . GLN A 1 4062 ? 160.563 242.315 180.926 1.00 30.51 ? 4062 GLN A NE2   1 
ATOM   19160 N  N     . ASN A 1 4063 ? 158.120 240.181 186.049 1.00 22.74 ? 4063 ASN A N     1 
ATOM   19161 C  CA    . ASN A 1 4063 ? 157.669 238.906 186.609 1.00 19.76 ? 4063 ASN A CA    1 
ATOM   19162 C  C     . ASN A 1 4063 ? 158.717 237.817 186.393 1.00 22.60 ? 4063 ASN A C     1 
ATOM   19163 O  O     . ASN A 1 4063 ? 158.394 236.662 186.113 1.00 32.15 ? 4063 ASN A O     1 
ATOM   19164 C  CB    . ASN A 1 4063 ? 156.313 238.488 186.035 1.00 20.16 ? 4063 ASN A CB    1 
ATOM   19165 C  CG    . ASN A 1 4063 ? 155.149 239.063 186.815 1.00 28.95 ? 4063 ASN A CG    1 
ATOM   19166 O  OD1   . ASN A 1 4063 ? 154.470 239.981 186.354 1.00 29.66 ? 4063 ASN A OD1   1 
ATOM   19167 N  ND2   . ASN A 1 4063 ? 154.916 238.528 188.008 1.00 32.38 ? 4063 ASN A ND2   1 
ATOM   19168 N  N     . THR A 1 4064 ? 159.983 238.200 186.515 1.00 17.22 ? 4064 THR A N     1 
ATOM   19169 C  CA    . THR A 1 4064 ? 161.107 237.284 186.405 1.00 13.76 ? 4064 THR A CA    1 
ATOM   19170 C  C     . THR A 1 4064 ? 161.700 237.020 187.783 1.00 18.63 ? 4064 THR A C     1 
ATOM   19171 O  O     . THR A 1 4064 ? 161.599 237.845 188.695 1.00 17.75 ? 4064 THR A O     1 
ATOM   19172 C  CB    . THR A 1 4064 ? 162.178 237.842 185.461 1.00 16.68 ? 4064 THR A CB    1 
ATOM   19173 O  OG1   . THR A 1 4064 ? 163.194 236.855 185.240 1.00 18.02 ? 4064 THR A OG1   1 
ATOM   19174 C  CG2   . THR A 1 4064 ? 162.811 239.095 186.031 1.00 14.23 ? 4064 THR A CG2   1 
ATOM   19175 N  N     . GLN A 1 4065 ? 162.308 235.850 187.930 1.00 14.40 ? 4065 GLN A N     1 
ATOM   19176 C  CA    . GLN A 1 4065 ? 162.900 235.439 189.192 1.00 15.05 ? 4065 GLN A CA    1 
ATOM   19177 C  C     . GLN A 1 4065 ? 164.338 235.927 189.275 1.00 11.67 ? 4065 GLN A C     1 
ATOM   19178 O  O     . GLN A 1 4065 ? 165.064 235.930 188.278 1.00 16.26 ? 4065 GLN A O     1 
ATOM   19179 C  CB    . GLN A 1 4065 ? 162.843 233.919 189.340 1.00 15.17 ? 4065 GLN A CB    1 
ATOM   19180 C  CG    . GLN A 1 4065 ? 161.435 233.359 189.368 1.00 16.69 ? 4065 GLN A CG    1 
ATOM   19181 C  CD    . GLN A 1 4065 ? 160.557 234.055 190.389 1.00 24.90 ? 4065 GLN A CD    1 
ATOM   19182 O  OE1   . GLN A 1 4065 ? 160.791 233.960 191.593 1.00 27.46 ? 4065 GLN A OE1   1 
ATOM   19183 N  NE2   . GLN A 1 4065 ? 159.540 234.764 189.911 1.00 22.75 ? 4065 GLN A NE2   1 
ATOM   19184 N  N     . ILE A 1 4066 ? 164.743 236.355 190.468 1.00 8.69  ? 4066 ILE A N     1 
ATOM   19185 C  CA    . ILE A 1 4066 ? 166.077 236.899 190.683 1.00 6.58  ? 4066 ILE A CA    1 
ATOM   19186 C  C     . ILE A 1 4066 ? 166.624 236.384 192.007 1.00 8.22  ? 4066 ILE A C     1 
ATOM   19187 O  O     . ILE A 1 4066 ? 165.894 236.282 192.999 1.00 14.71 ? 4066 ILE A O     1 
ATOM   19188 C  CB    . ILE A 1 4066 ? 166.072 238.444 190.643 1.00 6.44  ? 4066 ILE A CB    1 
ATOM   19189 C  CG1   . ILE A 1 4066 ? 167.486 238.992 190.855 1.00 3.98  ? 4066 ILE A CG1   1 
ATOM   19190 C  CG2   . ILE A 1 4066 ? 165.098 239.012 191.663 1.00 5.02  ? 4066 ILE A CG2   1 
ATOM   19191 C  CD1   . ILE A 1 4066 ? 167.714 240.342 190.236 1.00 2.96  ? 4066 ILE A CD1   1 
ATOM   19192 N  N     . THR A 1 4067 ? 167.910 236.045 192.014 1.00 7.13  ? 4067 THR A N     1 
ATOM   19193 C  CA    . THR A 1 4067 ? 168.626 235.648 193.218 1.00 4.94  ? 4067 THR A CA    1 
ATOM   19194 C  C     . THR A 1 4067 ? 169.581 236.774 193.594 1.00 4.32  ? 4067 THR A C     1 
ATOM   19195 O  O     . THR A 1 4067 ? 170.447 237.147 192.796 1.00 3.08  ? 4067 THR A O     1 
ATOM   19196 C  CB    . THR A 1 4067 ? 169.391 234.341 193.000 1.00 7.80  ? 4067 THR A CB    1 
ATOM   19197 O  OG1   . THR A 1 4067 ? 168.464 233.263 192.844 1.00 17.27 ? 4067 THR A OG1   1 
ATOM   19198 C  CG2   . THR A 1 4067 ? 170.306 234.048 194.182 1.00 2.02  ? 4067 THR A CG2   1 
ATOM   19199 N  N     . SER A 1 4068 ? 169.419 237.309 194.800 1.00 3.15  ? 4068 SER A N     1 
ATOM   19200 C  CA    . SER A 1 4068 ? 170.231 238.414 195.290 1.00 1.61  ? 4068 SER A CA    1 
ATOM   19201 C  C     . SER A 1 4068 ? 171.173 237.901 196.367 1.00 1.35  ? 4068 SER A C     1 
ATOM   19202 O  O     . SER A 1 4068 ? 170.747 237.192 197.285 1.00 2.21  ? 4068 SER A O     1 
ATOM   19203 C  CB    . SER A 1 4068 ? 169.353 239.537 195.846 1.00 2.83  ? 4068 SER A CB    1 
ATOM   19204 O  OG    . SER A 1 4068 ? 168.378 239.929 194.900 1.00 8.40  ? 4068 SER A OG    1 
ATOM   19205 N  N     . ILE A 1 4069 ? 172.451 238.250 196.249 1.00 1.75  ? 4069 ILE A N     1 
ATOM   19206 C  CA    . ILE A 1 4069 ? 173.489 237.761 197.147 1.00 1.04  ? 4069 ILE A CA    1 
ATOM   19207 C  C     . ILE A 1 4069 ? 174.382 238.923 197.557 1.00 0.78  ? 4069 ILE A C     1 
ATOM   19208 O  O     . ILE A 1 4069 ? 174.831 239.697 196.706 1.00 1.46  ? 4069 ILE A O     1 
ATOM   19209 C  CB    . ILE A 1 4069 ? 174.326 236.645 196.493 1.00 2.23  ? 4069 ILE A CB    1 
ATOM   19210 C  CG1   . ILE A 1 4069 ? 173.417 235.517 196.001 1.00 1.73  ? 4069 ILE A CG1   1 
ATOM   19211 C  CG2   . ILE A 1 4069 ? 175.361 236.113 197.462 1.00 1.37  ? 4069 ILE A CG2   1 
ATOM   19212 C  CD1   . ILE A 1 4069 ? 174.125 234.469 195.215 1.00 3.42  ? 4069 ILE A CD1   1 
ATOM   19213 N  N     . ALA A 1 4070 ? 174.630 239.046 198.858 1.00 1.98  ? 4070 ALA A N     1 
ATOM   19214 C  CA    . ALA A 1 4070 ? 175.703 239.896 199.354 1.00 0.93  ? 4070 ALA A CA    1 
ATOM   19215 C  C     . ALA A 1 4070 ? 177.032 239.156 199.254 1.00 3.04  ? 4070 ALA A C     1 
ATOM   19216 O  O     . ALA A 1 4070 ? 177.091 237.928 199.352 1.00 9.36  ? 4070 ALA A O     1 
ATOM   19217 C  CB    . ALA A 1 4070 ? 175.435 240.316 200.795 1.00 1.50  ? 4070 ALA A CB    1 
ATOM   19218 N  N     . ILE A 1 4071 ? 178.109 239.917 199.076 1.00 1.50  ? 4071 ILE A N     1 
ATOM   19219 C  CA    . ILE A 1 4071 ? 179.358 239.353 198.571 1.00 4.91  ? 4071 ILE A CA    1 
ATOM   19220 C  C     . ILE A 1 4071 ? 180.371 239.060 199.673 1.00 9.66  ? 4071 ILE A C     1 
ATOM   19221 O  O     . ILE A 1 4071 ? 181.180 238.132 199.550 1.00 10.07 ? 4071 ILE A O     1 
ATOM   19222 C  CB    . ILE A 1 4071 ? 179.945 240.292 197.497 1.00 2.77  ? 4071 ILE A CB    1 
ATOM   19223 C  CG1   . ILE A 1 4071 ? 179.095 240.203 196.231 1.00 3.87  ? 4071 ILE A CG1   1 
ATOM   19224 C  CG2   . ILE A 1 4071 ? 181.389 239.967 197.184 1.00 1.16  ? 4071 ILE A CG2   1 
ATOM   19225 C  CD1   . ILE A 1 4071 ? 178.833 238.781 195.785 1.00 5.29  ? 4071 ILE A CD1   1 
ATOM   19226 N  N     . GLY A 1 4072 ? 180.306 239.809 200.775 1.00 2.84  ? 4072 GLY A N     1 
ATOM   19227 C  CA    . GLY A 1 4072 ? 181.402 239.812 201.734 1.00 1.57  ? 4072 GLY A CA    1 
ATOM   19228 C  C     . GLY A 1 4072 ? 181.735 238.457 202.334 1.00 2.91  ? 4072 GLY A C     1 
ATOM   19229 O  O     . GLY A 1 4072 ? 182.906 238.156 202.574 1.00 5.69  ? 4072 GLY A O     1 
ATOM   19230 N  N     . SER A 1 4073 ? 180.726 237.633 202.596 1.00 4.21  ? 4073 SER A N     1 
ATOM   19231 C  CA    . SER A 1 4073 ? 180.958 236.359 203.267 1.00 3.05  ? 4073 SER A CA    1 
ATOM   19232 C  C     . SER A 1 4073 ? 181.667 235.365 202.354 1.00 7.65  ? 4073 SER A C     1 
ATOM   19233 O  O     . SER A 1 4073 ? 181.569 235.431 201.125 1.00 9.06  ? 4073 SER A O     1 
ATOM   19234 C  CB    . SER A 1 4073 ? 179.633 235.760 203.744 1.00 3.47  ? 4073 SER A CB    1 
ATOM   19235 O  OG    . SER A 1 4073 ? 179.811 234.447 204.238 1.00 7.93  ? 4073 SER A OG    1 
ATOM   19236 N  N     . ALA A 1 4074 ? 182.392 234.432 202.975 1.00 9.55  ? 4074 ALA A N     1 
ATOM   19237 C  CA    . ALA A 1 4074 ? 182.961 233.317 202.227 1.00 4.39  ? 4074 ALA A CA    1 
ATOM   19238 C  C     . ALA A 1 4074 ? 181.863 232.437 201.644 1.00 7.25  ? 4074 ALA A C     1 
ATOM   19239 O  O     . ALA A 1 4074 ? 181.988 231.939 200.519 1.00 15.22 ? 4074 ALA A O     1 
ATOM   19240 C  CB    . ALA A 1 4074 ? 183.890 232.499 203.122 1.00 2.82  ? 4074 ALA A CB    1 
ATOM   19241 N  N     . GLU A 1 4075 ? 180.784 232.227 202.402 1.00 5.57  ? 4075 GLU A N     1 
ATOM   19242 C  CA    . GLU A 1 4075 ? 179.636 231.499 201.872 1.00 8.43  ? 4075 GLU A CA    1 
ATOM   19243 C  C     . GLU A 1 4075 ? 178.975 232.253 200.727 1.00 7.82  ? 4075 GLU A C     1 
ATOM   19244 O  O     . GLU A 1 4075 ? 178.397 231.633 199.827 1.00 9.25  ? 4075 GLU A O     1 
ATOM   19245 C  CB    . GLU A 1 4075 ? 178.629 231.232 202.992 1.00 8.11  ? 4075 GLU A CB    1 
ATOM   19246 C  CG    . GLU A 1 4075 ? 177.404 230.440 202.562 1.00 8.66  ? 4075 GLU A CG    1 
ATOM   19247 C  CD    . GLU A 1 4075 ? 177.742 229.027 202.125 1.00 20.96 ? 4075 GLU A CD    1 
ATOM   19248 O  OE1   . GLU A 1 4075 ? 178.771 228.486 202.583 1.00 21.29 ? 4075 GLU A OE1   1 
ATOM   19249 O  OE2   . GLU A 1 4075 ? 176.978 228.458 201.317 1.00 21.58 ? 4075 GLU A OE2   1 
ATOM   19250 N  N     . GLY A 1 4076 ? 179.049 233.586 200.742 1.00 6.37  ? 4076 GLY A N     1 
ATOM   19251 C  CA    . GLY A 1 4076 ? 178.475 234.358 199.652 1.00 3.40  ? 4076 GLY A CA    1 
ATOM   19252 C  C     . GLY A 1 4076 ? 179.153 234.084 198.324 1.00 5.29  ? 4076 GLY A C     1 
ATOM   19253 O  O     . GLY A 1 4076 ? 178.501 234.053 197.279 1.00 4.23  ? 4076 GLY A O     1 
ATOM   19254 N  N     . PHE A 1 4077 ? 180.474 233.891 198.347 1.00 8.34  ? 4077 PHE A N     1 
ATOM   19255 C  CA    . PHE A 1 4077 ? 181.198 233.557 197.123 1.00 4.46  ? 4077 PHE A CA    1 
ATOM   19256 C  C     . PHE A 1 4077 ? 180.745 232.215 196.564 1.00 6.01  ? 4077 PHE A C     1 
ATOM   19257 O  O     . PHE A 1 4077 ? 180.519 232.082 195.356 1.00 9.13  ? 4077 PHE A O     1 
ATOM   19258 C  CB    . PHE A 1 4077 ? 182.700 233.545 197.394 1.00 2.40  ? 4077 PHE A CB    1 
ATOM   19259 C  CG    . PHE A 1 4077 ? 183.270 234.897 197.691 1.00 3.45  ? 4077 PHE A CG    1 
ATOM   19260 C  CD1   . PHE A 1 4077 ? 183.006 235.972 196.861 1.00 2.52  ? 4077 PHE A CD1   1 
ATOM   19261 C  CD2   . PHE A 1 4077 ? 184.050 235.100 198.816 1.00 5.73  ? 4077 PHE A CD2   1 
ATOM   19262 C  CE1   . PHE A 1 4077 ? 183.528 237.216 197.137 1.00 4.20  ? 4077 PHE A CE1   1 
ATOM   19263 C  CE2   . PHE A 1 4077 ? 184.568 236.344 199.099 1.00 4.20  ? 4077 PHE A CE2   1 
ATOM   19264 C  CZ    . PHE A 1 4077 ? 184.307 237.403 198.260 1.00 4.80  ? 4077 PHE A CZ    1 
ATOM   19265 N  N     . ASN A 1 4078 ? 180.609 231.208 197.429 1.00 6.37  ? 4078 ASN A N     1 
ATOM   19266 C  CA    . ASN A 1 4078 ? 180.130 229.908 196.975 1.00 5.36  ? 4078 ASN A CA    1 
ATOM   19267 C  C     . ASN A 1 4078 ? 178.708 230.005 196.443 1.00 5.16  ? 4078 ASN A C     1 
ATOM   19268 O  O     . ASN A 1 4078 ? 178.383 229.422 195.402 1.00 5.86  ? 4078 ASN A O     1 
ATOM   19269 C  CB    . ASN A 1 4078 ? 180.202 228.886 198.112 1.00 5.92  ? 4078 ASN A CB    1 
ATOM   19270 C  CG    . ASN A 1 4078 ? 181.593 228.760 198.696 1.00 13.40 ? 4078 ASN A CG    1 
ATOM   19271 O  OD1   . ASN A 1 4078 ? 182.592 228.859 197.984 1.00 17.61 ? 4078 ASN A OD1   1 
ATOM   19272 N  ND2   . ASN A 1 4078 ? 181.665 228.531 200.002 1.00 19.38 ? 4078 ASN A ND2   1 
ATOM   19273 N  N     . GLN A 1 4079 ? 177.845 230.742 197.146 1.00 6.59  ? 4079 GLN A N     1 
ATOM   19274 C  CA    . GLN A 1 4079 ? 176.466 230.889 196.700 1.00 6.63  ? 4079 GLN A CA    1 
ATOM   19275 C  C     . GLN A 1 4079 ? 176.391 231.642 195.378 1.00 5.34  ? 4079 GLN A C     1 
ATOM   19276 O  O     . GLN A 1 4079 ? 175.558 231.320 194.522 1.00 6.08  ? 4079 GLN A O     1 
ATOM   19277 C  CB    . GLN A 1 4079 ? 175.642 231.600 197.772 1.00 6.01  ? 4079 GLN A CB    1 
ATOM   19278 C  CG    . GLN A 1 4079 ? 174.174 231.716 197.429 1.00 11.21 ? 4079 GLN A CG    1 
ATOM   19279 C  CD    . GLN A 1 4079 ? 173.362 232.372 198.525 1.00 19.56 ? 4079 GLN A CD    1 
ATOM   19280 O  OE1   . GLN A 1 4079 ? 173.900 232.787 199.550 1.00 14.26 ? 4079 GLN A OE1   1 
ATOM   19281 N  NE2   . GLN A 1 4079 ? 172.055 232.470 198.312 1.00 27.68 ? 4079 GLN A NE2   1 
ATOM   19282 N  N     . ALA A 1 4080 ? 177.252 232.645 195.192 1.00 5.01  ? 4080 ALA A N     1 
ATOM   19283 C  CA    . ALA A 1 4080 ? 177.244 233.413 193.950 1.00 3.51  ? 4080 ALA A CA    1 
ATOM   19284 C  C     . ALA A 1 4080 ? 177.582 232.532 192.757 1.00 4.51  ? 4080 ALA A C     1 
ATOM   19285 O  O     . ALA A 1 4080 ? 176.933 232.609 191.709 1.00 6.82  ? 4080 ALA A O     1 
ATOM   19286 C  CB    . ALA A 1 4080 ? 178.217 234.587 194.050 1.00 2.35  ? 4080 ALA A CB    1 
ATOM   19287 N  N     . ASP A 1 4081 ? 178.597 231.677 192.903 1.00 5.53  ? 4081 ASP A N     1 
ATOM   19288 C  CA    . ASP A 1 4081 ? 178.987 230.803 191.803 1.00 4.50  ? 4081 ASP A CA    1 
ATOM   19289 C  C     . ASP A 1 4081 ? 177.875 229.823 191.449 1.00 9.39  ? 4081 ASP A C     1 
ATOM   19290 O  O     . ASP A 1 4081 ? 177.578 229.615 190.267 1.00 9.18  ? 4081 ASP A O     1 
ATOM   19291 C  CB    . ASP A 1 4081 ? 180.271 230.055 192.160 1.00 6.98  ? 4081 ASP A CB    1 
ATOM   19292 C  CG    . ASP A 1 4081 ? 180.690 229.074 191.086 1.00 15.79 ? 4081 ASP A CG    1 
ATOM   19293 O  OD1   . ASP A 1 4081 ? 180.357 227.876 191.213 1.00 20.66 ? 4081 ASP A OD1   1 
ATOM   19294 O  OD2   . ASP A 1 4081 ? 181.351 229.498 190.116 1.00 14.26 ? 4081 ASP A OD2   1 
ATOM   19295 N  N     . LYS A 1 4082 ? 177.240 229.217 192.456 1.00 7.06  ? 4082 LYS A N     1 
ATOM   19296 C  CA    . LYS A 1 4082 ? 176.146 228.292 192.177 1.00 6.36  ? 4082 LYS A CA    1 
ATOM   19297 C  C     . LYS A 1 4082 ? 174.956 229.010 191.552 1.00 7.10  ? 4082 LYS A C     1 
ATOM   19298 O  O     . LYS A 1 4082 ? 174.334 228.491 190.619 1.00 8.37  ? 4082 LYS A O     1 
ATOM   19299 C  CB    . LYS A 1 4082 ? 175.718 227.554 193.447 1.00 9.13  ? 4082 LYS A CB    1 
ATOM   19300 C  CG    . LYS A 1 4082 ? 176.782 226.650 194.048 1.00 13.78 ? 4082 LYS A CG    1 
ATOM   19301 C  CD    . LYS A 1 4082 ? 176.246 225.897 195.263 1.00 15.58 ? 4082 LYS A CD    1 
ATOM   19302 C  CE    . LYS A 1 4082 ? 176.020 226.802 196.463 1.00 13.57 ? 4082 LYS A CE    1 
ATOM   19303 N  NZ    . LYS A 1 4082 ? 177.290 227.358 196.993 1.00 10.96 ? 4082 LYS A NZ    1 
ATOM   19304 N  N     . ALA A 1 4083 ? 174.619 230.201 192.056 1.00 7.79  ? 4083 ALA A N     1 
ATOM   19305 C  CA    . ALA A 1 4083 ? 173.502 230.950 191.489 1.00 5.51  ? 4083 ALA A CA    1 
ATOM   19306 C  C     . ALA A 1 4083 ? 173.775 231.334 190.041 1.00 6.03  ? 4083 ALA A C     1 
ATOM   19307 O  O     . ALA A 1 4083 ? 172.891 231.223 189.185 1.00 5.83  ? 4083 ALA A O     1 
ATOM   19308 C  CB    . ALA A 1 4083 ? 173.219 232.193 192.331 1.00 3.91  ? 4083 ALA A CB    1 
ATOM   19309 N  N     . ILE A 1 4084 ? 174.997 231.781 189.750 1.00 4.32  ? 4084 ILE A N     1 
ATOM   19310 C  CA    . ILE A 1 4084 ? 175.355 232.156 188.384 1.00 3.95  ? 4084 ILE A CA    1 
ATOM   19311 C  C     . ILE A 1 4084 ? 175.319 230.937 187.470 1.00 7.21  ? 4084 ILE A C     1 
ATOM   19312 O  O     . ILE A 1 4084 ? 174.777 230.987 186.360 1.00 9.31  ? 4084 ILE A O     1 
ATOM   19313 C  CB    . ILE A 1 4084 ? 176.733 232.842 188.366 1.00 4.63  ? 4084 ILE A CB    1 
ATOM   19314 C  CG1   . ILE A 1 4084 ? 176.618 234.269 188.908 1.00 2.26  ? 4084 ILE A CG1   1 
ATOM   19315 C  CG2   . ILE A 1 4084 ? 177.326 232.834 186.967 1.00 3.60  ? 4084 ILE A CG2   1 
ATOM   19316 C  CD1   . ILE A 1 4084 ? 177.948 234.933 189.159 1.00 2.46  ? 4084 ILE A CD1   1 
ATOM   19317 N  N     . ASN A 1 4085 ? 175.886 229.819 187.928 1.00 6.49  ? 4085 ASN A N     1 
ATOM   19318 C  CA    . ASN A 1 4085 ? 175.924 228.612 187.108 1.00 5.00  ? 4085 ASN A CA    1 
ATOM   19319 C  C     . ASN A 1 4085 ? 174.523 228.096 186.813 1.00 7.12  ? 4085 ASN A C     1 
ATOM   19320 O  O     . ASN A 1 4085 ? 174.243 227.634 185.700 1.00 12.86 ? 4085 ASN A O     1 
ATOM   19321 C  CB    . ASN A 1 4085 ? 176.759 227.533 187.799 1.00 6.85  ? 4085 ASN A CB    1 
ATOM   19322 C  CG    . ASN A 1 4085 ? 178.234 227.872 187.832 1.00 6.28  ? 4085 ASN A CG    1 
ATOM   19323 O  OD1   . ASN A 1 4085 ? 178.693 228.768 187.125 1.00 6.85  ? 4085 ASN A OD1   1 
ATOM   19324 N  ND2   . ASN A 1 4085 ? 178.986 227.161 188.663 1.00 6.89  ? 4085 ASN A ND2   1 
ATOM   19325 N  N     . THR A 1 4086 ? 173.631 228.146 187.803 1.00 7.76  ? 4086 THR A N     1 
ATOM   19326 C  CA    . THR A 1 4086 ? 172.248 227.748 187.568 1.00 7.38  ? 4086 THR A CA    1 
ATOM   19327 C  C     . THR A 1 4086 ? 171.541 228.725 186.636 1.00 5.94  ? 4086 THR A C     1 
ATOM   19328 O  O     . THR A 1 4086 ? 170.768 228.313 185.764 1.00 6.89  ? 4086 THR A O     1 
ATOM   19329 C  CB    . THR A 1 4086 ? 171.500 227.640 188.896 1.00 5.54  ? 4086 THR A CB    1 
ATOM   19330 O  OG1   . THR A 1 4086 ? 172.263 226.849 189.813 1.00 8.59  ? 4086 THR A OG1   1 
ATOM   19331 C  CG2   . THR A 1 4086 ? 170.145 226.989 188.690 1.00 6.84  ? 4086 THR A CG2   1 
ATOM   19332 N  N     . ALA A 1 4087 ? 171.800 230.024 186.804 1.00 8.07  ? 4087 ALA A N     1 
ATOM   19333 C  CA    . ALA A 1 4087 ? 171.076 231.036 186.045 1.00 6.92  ? 4087 ALA A CA    1 
ATOM   19334 C  C     . ALA A 1 4087 ? 171.464 231.043 184.572 1.00 9.30  ? 4087 ALA A C     1 
ATOM   19335 O  O     . ALA A 1 4087 ? 170.612 231.289 183.713 1.00 9.92  ? 4087 ALA A O     1 
ATOM   19336 C  CB    . ALA A 1 4087 ? 171.307 232.415 186.657 1.00 7.01  ? 4087 ALA A CB    1 
ATOM   19337 N  N     . VAL A 1 4088 ? 172.735 230.783 184.259 1.00 6.84  ? 4088 VAL A N     1 
ATOM   19338 C  CA    . VAL A 1 4088 ? 173.182 230.825 182.871 1.00 5.88  ? 4088 VAL A CA    1 
ATOM   19339 C  C     . VAL A 1 4088 ? 172.618 229.686 182.039 1.00 11.89 ? 4088 VAL A C     1 
ATOM   19340 O  O     . VAL A 1 4088 ? 172.755 229.701 180.812 1.00 18.26 ? 4088 VAL A O     1 
ATOM   19341 C  CB    . VAL A 1 4088 ? 174.721 230.815 182.789 1.00 8.19  ? 4088 VAL A CB    1 
ATOM   19342 C  CG1   . VAL A 1 4088 ? 175.291 232.069 183.431 1.00 3.33  ? 4088 VAL A CG1   1 
ATOM   19343 C  CG2   . VAL A 1 4088 ? 175.287 229.563 183.427 1.00 7.92  ? 4088 VAL A CG2   1 
ATOM   19344 N  N     . LYS A 1 4089 ? 171.987 228.700 182.675 1.00 10.18 ? 4089 LYS A N     1 
ATOM   19345 C  CA    . LYS A 1 4089 ? 171.336 227.613 181.964 1.00 8.83  ? 4089 LYS A CA    1 
ATOM   19346 C  C     . LYS A 1 4089 ? 169.818 227.700 181.978 1.00 9.67  ? 4089 LYS A C     1 
ATOM   19347 O  O     . LYS A 1 4089 ? 169.165 226.870 181.339 1.00 23.73 ? 4089 LYS A O     1 
ATOM   19348 C  CB    . LYS A 1 4089 ? 171.763 226.258 182.552 1.00 10.31 ? 4089 LYS A CB    1 
ATOM   19349 C  CG    . LYS A 1 4089 ? 173.222 225.915 182.338 1.00 13.51 ? 4089 LYS A CG    1 
ATOM   19350 C  CD    . LYS A 1 4089 ? 173.512 224.499 182.803 1.00 11.92 ? 4089 LYS A CD    1 
ATOM   19351 C  CE    . LYS A 1 4089 ? 173.526 224.404 184.318 1.00 18.93 ? 4089 LYS A CE    1 
ATOM   19352 N  NZ    . LYS A 1 4089 ? 173.916 223.047 184.786 1.00 26.90 ? 4089 LYS A NZ    1 
ATOM   19353 N  N     . SER A 1 4090 ? 169.239 228.673 182.686 1.00 8.63  ? 4090 SER A N     1 
ATOM   19354 C  CA    . SER A 1 4090 ? 167.792 228.789 182.798 1.00 9.50  ? 4090 SER A CA    1 
ATOM   19355 C  C     . SER A 1 4090 ? 167.243 230.174 182.491 1.00 13.39 ? 4090 SER A C     1 
ATOM   19356 O  O     . SER A 1 4090 ? 166.019 230.344 182.512 1.00 19.35 ? 4090 SER A O     1 
ATOM   19357 C  CB    . SER A 1 4090 ? 167.328 228.386 184.208 1.00 7.86  ? 4090 SER A CB    1 
ATOM   19358 O  OG    . SER A 1 4090 ? 167.863 229.253 185.191 1.00 12.93 ? 4090 SER A OG    1 
ATOM   19359 N  N     . GLY A 1 4091 ? 168.093 231.160 182.218 1.00 9.74  ? 4091 GLY A N     1 
ATOM   19360 C  CA    . GLY A 1 4091 ? 167.634 232.520 182.015 1.00 6.42  ? 4091 GLY A CA    1 
ATOM   19361 C  C     . GLY A 1 4091 ? 167.338 233.285 183.283 1.00 8.55  ? 4091 GLY A C     1 
ATOM   19362 O  O     . GLY A 1 4091 ? 166.782 234.385 183.209 1.00 10.13 ? 4091 GLY A O     1 
ATOM   19363 N  N     . ARG A 1 4092 ? 167.687 232.730 184.440 1.00 13.21 ? 4092 ARG A N     1 
ATOM   19364 C  CA    . ARG A 1 4092 ? 167.472 233.352 185.735 1.00 7.23  ? 4092 ARG A CA    1 
ATOM   19365 C  C     . ARG A 1 4092 ? 168.344 234.604 185.870 1.00 6.50  ? 4092 ARG A C     1 
ATOM   19366 O  O     . ARG A 1 4092 ? 169.391 234.737 185.232 1.00 9.16  ? 4092 ARG A O     1 
ATOM   19367 C  CB    . ARG A 1 4092 ? 167.780 232.331 186.833 1.00 12.44 ? 4092 ARG A CB    1 
ATOM   19368 C  CG    . ARG A 1 4092 ? 167.619 232.771 188.278 1.00 15.70 ? 4092 ARG A CG    1 
ATOM   19369 C  CD    . ARG A 1 4092 ? 166.171 233.009 188.619 1.00 17.17 ? 4092 ARG A CD    1 
ATOM   19370 N  NE    . ARG A 1 4092 ? 166.001 233.408 190.011 1.00 22.77 ? 4092 ARG A NE    1 
ATOM   19371 C  CZ    . ARG A 1 4092 ? 165.814 232.558 191.009 1.00 12.39 ? 4092 ARG A CZ    1 
ATOM   19372 N  NH1   . ARG A 1 4092 ? 165.747 231.254 190.801 1.00 15.54 ? 4092 ARG A NH1   1 
ATOM   19373 N  NH2   . ARG A 1 4092 ? 165.689 233.027 192.246 1.00 10.11 ? 4092 ARG A NH2   1 
ATOM   19374 N  N     . TRP A 1 4093 ? 167.892 235.539 186.699 1.00 8.64  ? 4093 TRP A N     1 
ATOM   19375 C  CA    . TRP A 1 4093 ? 168.622 236.764 186.991 1.00 3.02  ? 4093 TRP A CA    1 
ATOM   19376 C  C     . TRP A 1 4093 ? 169.377 236.625 188.308 1.00 2.71  ? 4093 TRP A C     1 
ATOM   19377 O  O     . TRP A 1 4093 ? 168.860 236.056 189.274 1.00 4.19  ? 4093 TRP A O     1 
ATOM   19378 C  CB    . TRP A 1 4093 ? 167.678 237.966 187.059 1.00 2.67  ? 4093 TRP A CB    1 
ATOM   19379 C  CG    . TRP A 1 4093 ? 167.260 238.500 185.724 1.00 3.25  ? 4093 TRP A CG    1 
ATOM   19380 C  CD1   . TRP A 1 4093 ? 167.415 237.894 184.513 1.00 2.47  ? 4093 TRP A CD1   1 
ATOM   19381 C  CD2   . TRP A 1 4093 ? 166.574 239.731 185.469 1.00 2.92  ? 4093 TRP A CD2   1 
ATOM   19382 N  NE1   . TRP A 1 4093 ? 166.892 238.679 183.520 1.00 1.67  ? 4093 TRP A NE1   1 
ATOM   19383 C  CE2   . TRP A 1 4093 ? 166.365 239.812 184.081 1.00 1.36  ? 4093 TRP A CE2   1 
ATOM   19384 C  CE3   . TRP A 1 4093 ? 166.121 240.775 186.281 1.00 2.29  ? 4093 TRP A CE3   1 
ATOM   19385 C  CZ2   . TRP A 1 4093 ? 165.728 240.895 183.485 1.00 2.85  ? 4093 TRP A CZ2   1 
ATOM   19386 C  CZ3   . TRP A 1 4093 ? 165.490 241.849 185.688 1.00 3.38  ? 4093 TRP A CZ3   1 
ATOM   19387 C  CH2   . TRP A 1 4093 ? 165.298 241.902 184.303 1.00 5.56  ? 4093 TRP A CH2   1 
ATOM   19388 N  N     . VAL A 1 4094 ? 170.603 237.139 188.336 1.00 1.15  ? 4094 VAL A N     1 
ATOM   19389 C  CA    . VAL A 1 4094 ? 171.445 237.130 189.528 1.00 1.48  ? 4094 VAL A CA    1 
ATOM   19390 C  C     . VAL A 1 4094 ? 171.928 238.550 189.784 1.00 0.81  ? 4094 VAL A C     1 
ATOM   19391 O  O     . VAL A 1 4094 ? 172.446 239.206 188.874 1.00 0.74  ? 4094 VAL A O     1 
ATOM   19392 C  CB    . VAL A 1 4094 ? 172.639 236.168 189.376 1.00 0.95  ? 4094 VAL A CB    1 
ATOM   19393 C  CG1   . VAL A 1 4094 ? 173.570 236.280 190.571 1.00 0.57  ? 4094 VAL A CG1   1 
ATOM   19394 C  CG2   . VAL A 1 4094 ? 172.160 234.743 189.211 1.00 1.35  ? 4094 VAL A CG2   1 
ATOM   19395 N  N     . MET A 1 4095 ? 171.762 239.022 191.018 1.00 0.67  ? 4095 MET A N     1 
ATOM   19396 C  CA    . MET A 1 4095 ? 172.293 240.313 191.435 1.00 0.41  ? 4095 MET A CA    1 
ATOM   19397 C  C     . MET A 1 4095 ? 173.246 240.104 192.602 1.00 0.32  ? 4095 MET A C     1 
ATOM   19398 O  O     . MET A 1 4095 ? 172.884 239.474 193.600 1.00 0.51  ? 4095 MET A O     1 
ATOM   19399 C  CB    . MET A 1 4095 ? 171.179 241.289 191.818 1.00 0.71  ? 4095 MET A CB    1 
ATOM   19400 C  CG    . MET A 1 4095 ? 171.698 242.562 192.473 1.00 0.51  ? 4095 MET A CG    1 
ATOM   19401 S  SD    . MET A 1 4095 ? 170.424 243.775 192.854 1.00 8.70  ? 4095 MET A SD    1 
ATOM   19402 C  CE    . MET A 1 4095 ? 169.212 242.755 193.678 1.00 2.96  ? 4095 MET A CE    1 
ATOM   19403 N  N     . LEU A 1 4096 ? 174.458 240.634 192.474 1.00 0.31  ? 4096 LEU A N     1 
ATOM   19404 C  CA    . LEU A 1 4096 ? 175.469 240.577 193.519 1.00 0.24  ? 4096 LEU A CA    1 
ATOM   19405 C  C     . LEU A 1 4096 ? 175.718 241.992 194.025 1.00 0.43  ? 4096 LEU A C     1 
ATOM   19406 O  O     . LEU A 1 4096 ? 176.062 242.883 193.242 1.00 0.42  ? 4096 LEU A O     1 
ATOM   19407 C  CB    . LEU A 1 4096 ? 176.754 239.940 192.993 1.00 0.27  ? 4096 LEU A CB    1 
ATOM   19408 C  CG    . LEU A 1 4096 ? 176.552 238.588 192.297 1.00 0.29  ? 4096 LEU A CG    1 
ATOM   19409 C  CD1   . LEU A 1 4096 ? 177.863 238.008 191.815 1.00 0.30  ? 4096 LEU A CD1   1 
ATOM   19410 C  CD2   . LEU A 1 4096 ? 175.837 237.603 193.209 1.00 0.33  ? 4096 LEU A CD2   1 
ATOM   19411 N  N     . LYS A 1 4097 ? 175.542 242.194 195.326 1.00 0.70  ? 4097 LYS A N     1 
ATOM   19412 C  CA    . LYS A 1 4097 ? 175.609 243.518 195.926 1.00 0.48  ? 4097 LYS A CA    1 
ATOM   19413 C  C     . LYS A 1 4097 ? 176.939 243.732 196.630 1.00 0.43  ? 4097 LYS A C     1 
ATOM   19414 O  O     . LYS A 1 4097 ? 177.526 242.801 197.188 1.00 1.25  ? 4097 LYS A O     1 
ATOM   19415 C  CB    . LYS A 1 4097 ? 174.465 243.727 196.921 1.00 0.84  ? 4097 LYS A CB    1 
ATOM   19416 C  CG    . LYS A 1 4097 ? 173.127 243.187 196.469 1.00 1.56  ? 4097 LYS A CG    1 
ATOM   19417 C  CD    . LYS A 1 4097 ? 172.077 243.399 197.547 1.00 5.14  ? 4097 LYS A CD    1 
ATOM   19418 C  CE    . LYS A 1 4097 ? 171.080 242.260 197.581 1.00 4.20  ? 4097 LYS A CE    1 
ATOM   19419 N  NZ    . LYS A 1 4097 ? 170.139 242.393 198.724 1.00 5.79  ? 4097 LYS A NZ    1 
ATOM   19420 N  N     . ASN A 1 4098 ? 177.403 244.983 196.607 1.00 0.45  ? 4098 ASN A N     1 
ATOM   19421 C  CA    . ASN A 1 4098 ? 178.627 245.401 197.295 1.00 0.69  ? 4098 ASN A CA    1 
ATOM   19422 C  C     . ASN A 1 4098 ? 179.841 244.612 196.811 1.00 0.65  ? 4098 ASN A C     1 
ATOM   19423 O  O     . ASN A 1 4098 ? 180.684 244.190 197.602 1.00 1.26  ? 4098 ASN A O     1 
ATOM   19424 C  CB    . ASN A 1 4098 ? 178.472 245.286 198.813 1.00 0.74  ? 4098 ASN A CB    1 
ATOM   19425 C  CG    . ASN A 1 4098 ? 177.191 245.915 199.320 1.00 0.39  ? 4098 ASN A CG    1 
ATOM   19426 O  OD1   . ASN A 1 4098 ? 176.996 247.122 199.208 1.00 0.87  ? 4098 ASN A OD1   1 
ATOM   19427 N  ND2   . ASN A 1 4098 ? 176.312 245.098 199.884 1.00 0.28  ? 4098 ASN A ND2   1 
ATOM   19428 N  N     . VAL A 1 4099 ? 179.937 244.418 195.494 1.00 0.61  ? 4099 VAL A N     1 
ATOM   19429 C  CA    . VAL A 1 4099 ? 181.047 243.652 194.937 1.00 0.56  ? 4099 VAL A CA    1 
ATOM   19430 C  C     . VAL A 1 4099 ? 182.362 244.411 195.034 1.00 0.77  ? 4099 VAL A C     1 
ATOM   19431 O  O     . VAL A 1 4099 ? 183.431 243.806 194.897 1.00 0.88  ? 4099 VAL A O     1 
ATOM   19432 C  CB    . VAL A 1 4099 ? 180.753 243.252 193.480 1.00 0.31  ? 4099 VAL A CB    1 
ATOM   19433 C  CG1   . VAL A 1 4099 ? 179.440 242.494 193.399 1.00 0.36  ? 4099 VAL A CG1   1 
ATOM   19434 C  CG2   . VAL A 1 4099 ? 180.735 244.472 192.579 1.00 0.52  ? 4099 VAL A CG2   1 
ATOM   19435 N  N     . HIS A 1 4100 ? 182.316 245.724 195.273 1.00 0.53  ? 4100 HIS A N     1 
ATOM   19436 C  CA    . HIS A 1 4100 ? 183.531 246.496 195.496 1.00 0.63  ? 4100 HIS A CA    1 
ATOM   19437 C  C     . HIS A 1 4100 ? 184.262 246.079 196.764 1.00 0.98  ? 4100 HIS A C     1 
ATOM   19438 O  O     . HIS A 1 4100 ? 185.428 246.445 196.936 1.00 2.95  ? 4100 HIS A O     1 
ATOM   19439 C  CB    . HIS A 1 4100 ? 183.203 247.988 195.554 1.00 1.08  ? 4100 HIS A CB    1 
ATOM   19440 C  CG    . HIS A 1 4100 ? 182.361 248.377 196.729 1.00 1.44  ? 4100 HIS A CG    1 
ATOM   19441 N  ND1   . HIS A 1 4100 ? 180.999 248.174 196.768 1.00 0.85  ? 4100 HIS A ND1   1 
ATOM   19442 C  CD2   . HIS A 1 4100 ? 182.689 248.956 197.908 1.00 1.63  ? 4100 HIS A CD2   1 
ATOM   19443 C  CE1   . HIS A 1 4100 ? 180.524 248.610 197.920 1.00 0.70  ? 4100 HIS A CE1   1 
ATOM   19444 N  NE2   . HIS A 1 4100 ? 181.529 249.088 198.630 1.00 3.07  ? 4100 HIS A NE2   1 
ATOM   19445 N  N     . LEU A 1 4101 ? 183.607 245.332 197.651 1.00 0.85  ? 4101 LEU A N     1 
ATOM   19446 C  CA    . LEU A 1 4101 ? 184.249 244.816 198.851 1.00 0.97  ? 4101 LEU A CA    1 
ATOM   19447 C  C     . LEU A 1 4101 ? 185.139 243.613 198.578 1.00 1.96  ? 4101 LEU A C     1 
ATOM   19448 O  O     . LEU A 1 4101 ? 185.894 243.209 199.468 1.00 4.23  ? 4101 LEU A O     1 
ATOM   19449 C  CB    . LEU A 1 4101 ? 183.187 244.448 199.890 1.00 1.49  ? 4101 LEU A CB    1 
ATOM   19450 C  CG    . LEU A 1 4101 ? 182.286 245.587 200.367 1.00 2.03  ? 4101 LEU A CG    1 
ATOM   19451 C  CD1   . LEU A 1 4101 ? 181.248 245.077 201.352 1.00 1.16  ? 4101 LEU A CD1   1 
ATOM   19452 C  CD2   . LEU A 1 4101 ? 183.104 246.710 200.981 1.00 0.53  ? 4101 LEU A CD2   1 
ATOM   19453 N  N     . ALA A 1 4102 ? 185.074 243.031 197.382 1.00 2.76  ? 4102 ALA A N     1 
ATOM   19454 C  CA    . ALA A 1 4102 ? 185.899 241.883 197.005 1.00 1.62  ? 4102 ALA A CA    1 
ATOM   19455 C  C     . ALA A 1 4102 ? 186.547 242.143 195.650 1.00 2.60  ? 4102 ALA A C     1 
ATOM   19456 O  O     . ALA A 1 4102 ? 186.201 241.506 194.649 1.00 2.42  ? 4102 ALA A O     1 
ATOM   19457 C  CB    . ALA A 1 4102 ? 185.066 240.602 196.975 1.00 0.76  ? 4102 ALA A CB    1 
ATOM   19458 N  N     . PRO A 1 4103 ? 187.495 243.084 195.583 1.00 4.00  ? 4103 PRO A N     1 
ATOM   19459 C  CA    . PRO A 1 4103 ? 188.138 243.372 194.288 1.00 4.15  ? 4103 PRO A CA    1 
ATOM   19460 C  C     . PRO A 1 4103 ? 188.863 242.178 193.691 1.00 3.65  ? 4103 PRO A C     1 
ATOM   19461 O  O     . PRO A 1 4103 ? 188.844 241.998 192.468 1.00 4.94  ? 4103 PRO A O     1 
ATOM   19462 C  CB    . PRO A 1 4103 ? 189.104 244.516 194.625 1.00 4.04  ? 4103 PRO A CB    1 
ATOM   19463 C  CG    . PRO A 1 4103 ? 189.327 244.409 196.090 1.00 4.43  ? 4103 PRO A CG    1 
ATOM   19464 C  CD    . PRO A 1 4103 ? 188.044 243.915 196.666 1.00 2.94  ? 4103 PRO A CD    1 
ATOM   19465 N  N     . GLY A 1 4104 ? 189.498 241.351 194.524 1.00 3.80  ? 4104 GLY A N     1 
ATOM   19466 C  CA    . GLY A 1 4104 ? 190.203 240.192 194.004 1.00 1.45  ? 4104 GLY A CA    1 
ATOM   19467 C  C     . GLY A 1 4104 ? 189.274 239.166 193.384 1.00 2.46  ? 4104 GLY A C     1 
ATOM   19468 O  O     . GLY A 1 4104 ? 189.563 238.618 192.317 1.00 8.42  ? 4104 GLY A O     1 
ATOM   19469 N  N     . TRP A 1 4105 ? 188.147 238.893 194.044 1.00 1.87  ? 4105 TRP A N     1 
ATOM   19470 C  CA    . TRP A 1 4105 ? 187.183 237.946 193.498 1.00 1.45  ? 4105 TRP A CA    1 
ATOM   19471 C  C     . TRP A 1 4105 ? 186.513 238.496 192.244 1.00 2.21  ? 4105 TRP A C     1 
ATOM   19472 O  O     . TRP A 1 4105 ? 186.089 237.723 191.378 1.00 2.04  ? 4105 TRP A O     1 
ATOM   19473 C  CB    . TRP A 1 4105 ? 186.146 237.597 194.568 1.00 1.45  ? 4105 TRP A CB    1 
ATOM   19474 C  CG    . TRP A 1 4105 ? 184.898 236.973 194.041 1.00 1.03  ? 4105 TRP A CG    1 
ATOM   19475 C  CD1   . TRP A 1 4105 ? 184.691 235.650 193.778 1.00 0.92  ? 4105 TRP A CD1   1 
ATOM   19476 C  CD2   . TRP A 1 4105 ? 183.678 237.642 193.712 1.00 1.23  ? 4105 TRP A CD2   1 
ATOM   19477 N  NE1   . TRP A 1 4105 ? 183.416 235.455 193.308 1.00 1.64  ? 4105 TRP A NE1   1 
ATOM   19478 C  CE2   . TRP A 1 4105 ? 182.775 236.665 193.256 1.00 1.23  ? 4105 TRP A CE2   1 
ATOM   19479 C  CE3   . TRP A 1 4105 ? 183.261 238.976 193.760 1.00 2.17  ? 4105 TRP A CE3   1 
ATOM   19480 C  CZ2   . TRP A 1 4105 ? 181.482 236.977 192.850 1.00 1.90  ? 4105 TRP A CZ2   1 
ATOM   19481 C  CZ3   . TRP A 1 4105 ? 181.980 239.283 193.358 1.00 2.42  ? 4105 TRP A CZ3   1 
ATOM   19482 C  CH2   . TRP A 1 4105 ? 181.104 238.289 192.909 1.00 2.01  ? 4105 TRP A CH2   1 
ATOM   19483 N  N     . LEU A 1 4106 ? 186.423 239.824 192.127 1.00 3.19  ? 4106 LEU A N     1 
ATOM   19484 C  CA    . LEU A 1 4106 ? 185.814 240.438 190.949 1.00 2.41  ? 4106 LEU A CA    1 
ATOM   19485 C  C     . LEU A 1 4106 ? 186.620 240.153 189.689 1.00 5.53  ? 4106 LEU A C     1 
ATOM   19486 O  O     . LEU A 1 4106 ? 186.046 239.948 188.614 1.00 10.30 ? 4106 LEU A O     1 
ATOM   19487 C  CB    . LEU A 1 4106 ? 185.668 241.944 191.161 1.00 2.93  ? 4106 LEU A CB    1 
ATOM   19488 C  CG    . LEU A 1 4106 ? 184.320 242.434 191.692 1.00 1.01  ? 4106 LEU A CG    1 
ATOM   19489 C  CD1   . LEU A 1 4106 ? 184.274 243.950 191.693 1.00 0.61  ? 4106 LEU A CD1   1 
ATOM   19490 C  CD2   . LEU A 1 4106 ? 183.177 241.857 190.879 1.00 0.49  ? 4106 LEU A CD2   1 
ATOM   19491 N  N     . MET A 1 4107 ? 187.953 240.152 189.795 1.00 5.24  ? 4107 MET A N     1 
ATOM   19492 C  CA    . MET A 1 4107 ? 188.784 239.820 188.642 1.00 4.82  ? 4107 MET A CA    1 
ATOM   19493 C  C     . MET A 1 4107 ? 188.512 238.403 188.162 1.00 5.01  ? 4107 MET A C     1 
ATOM   19494 O  O     . MET A 1 4107 ? 188.455 238.146 186.954 1.00 8.65  ? 4107 MET A O     1 
ATOM   19495 C  CB    . MET A 1 4107 ? 190.263 239.989 188.983 1.00 8.13  ? 4107 MET A CB    1 
ATOM   19496 C  CG    . MET A 1 4107 ? 190.634 241.351 189.536 1.00 12.60 ? 4107 MET A CG    1 
ATOM   19497 S  SD    . MET A 1 4107 ? 192.285 241.369 190.256 1.00 42.64 ? 4107 MET A SD    1 
ATOM   19498 C  CE    . MET A 1 4107 ? 192.014 242.373 191.711 1.00 13.27 ? 4107 MET A CE    1 
ATOM   19499 N  N     . GLN A 1 4108 ? 188.346 237.467 189.095 1.00 4.71  ? 4108 GLN A N     1 
ATOM   19500 C  CA    . GLN A 1 4108 ? 188.065 236.088 188.716 1.00 3.60  ? 4108 GLN A CA    1 
ATOM   19501 C  C     . GLN A 1 4108 ? 186.671 235.942 188.121 1.00 4.33  ? 4108 GLN A C     1 
ATOM   19502 O  O     . GLN A 1 4108 ? 186.449 235.064 187.280 1.00 4.77  ? 4108 GLN A O     1 
ATOM   19503 C  CB    . GLN A 1 4108 ? 188.238 235.174 189.927 1.00 5.29  ? 4108 GLN A CB    1 
ATOM   19504 C  CG    . GLN A 1 4108 ? 189.672 235.095 190.424 1.00 9.04  ? 4108 GLN A CG    1 
ATOM   19505 C  CD    . GLN A 1 4108 ? 190.686 235.133 189.294 1.00 18.20 ? 4108 GLN A CD    1 
ATOM   19506 O  OE1   . GLN A 1 4108 ? 190.761 234.215 188.476 1.00 14.25 ? 4108 GLN A OE1   1 
ATOM   19507 N  NE2   . GLN A 1 4108 ? 191.471 236.202 189.244 1.00 12.64 ? 4108 GLN A NE2   1 
ATOM   19508 N  N     . LEU A 1 4109 ? 185.724 236.781 188.546 1.00 9.18  ? 4109 LEU A N     1 
ATOM   19509 C  CA    . LEU A 1 4109 ? 184.388 236.747 187.960 1.00 3.87  ? 4109 LEU A CA    1 
ATOM   19510 C  C     . LEU A 1 4109 ? 184.407 237.245 186.521 1.00 2.94  ? 4109 LEU A C     1 
ATOM   19511 O  O     . LEU A 1 4109 ? 183.675 236.727 185.669 1.00 4.61  ? 4109 LEU A O     1 
ATOM   19512 C  CB    . LEU A 1 4109 ? 183.422 237.575 188.806 1.00 4.47  ? 4109 LEU A CB    1 
ATOM   19513 C  CG    . LEU A 1 4109 ? 181.992 237.657 188.265 1.00 2.68  ? 4109 LEU A CG    1 
ATOM   19514 C  CD1   . LEU A 1 4109 ? 181.286 236.330 188.459 1.00 1.60  ? 4109 LEU A CD1   1 
ATOM   19515 C  CD2   . LEU A 1 4109 ? 181.219 238.791 188.912 1.00 1.88  ? 4109 LEU A CD2   1 
ATOM   19516 N  N     . GLU A 1 4110 ? 185.233 238.253 186.233 1.00 4.53  ? 4110 GLU A N     1 
ATOM   19517 C  CA    . GLU A 1 4110 ? 185.338 238.761 184.868 1.00 4.06  ? 4110 GLU A CA    1 
ATOM   19518 C  C     . GLU A 1 4110 ? 185.864 237.688 183.924 1.00 4.77  ? 4110 GLU A C     1 
ATOM   19519 O  O     . GLU A 1 4110 ? 185.382 237.553 182.794 1.00 7.39  ? 4110 GLU A O     1 
ATOM   19520 C  CB    . GLU A 1 4110 ? 186.233 240.000 184.843 1.00 3.04  ? 4110 GLU A CB    1 
ATOM   19521 C  CG    . GLU A 1 4110 ? 186.213 240.783 183.537 1.00 5.48  ? 4110 GLU A CG    1 
ATOM   19522 C  CD    . GLU A 1 4110 ? 187.151 240.215 182.487 1.00 7.74  ? 4110 GLU A CD    1 
ATOM   19523 O  OE1   . GLU A 1 4110 ? 188.334 239.979 182.812 1.00 9.47  ? 4110 GLU A OE1   1 
ATOM   19524 O  OE2   . GLU A 1 4110 ? 186.708 240.009 181.337 1.00 4.50  ? 4110 GLU A OE2   1 
ATOM   19525 N  N     . LYS A 1 4111 ? 186.858 236.915 184.370 1.00 4.56  ? 4111 LYS A N     1 
ATOM   19526 C  CA    . LYS A 1 4111 ? 187.366 235.816 183.558 1.00 4.74  ? 4111 LYS A CA    1 
ATOM   19527 C  C     . LYS A 1 4111 ? 186.320 234.721 183.392 1.00 3.19  ? 4111 LYS A C     1 
ATOM   19528 O  O     . LYS A 1 4111 ? 186.229 234.100 182.327 1.00 5.69  ? 4111 LYS A O     1 
ATOM   19529 C  CB    . LYS A 1 4111 ? 188.649 235.262 184.176 1.00 5.72  ? 4111 LYS A CB    1 
ATOM   19530 C  CG    . LYS A 1 4111 ? 189.871 236.132 183.931 1.00 8.42  ? 4111 LYS A CG    1 
ATOM   19531 C  CD    . LYS A 1 4111 ? 190.829 236.091 185.105 1.00 11.55 ? 4111 LYS A CD    1 
ATOM   19532 C  CE    . LYS A 1 4111 ? 192.182 236.684 184.745 1.00 7.89  ? 4111 LYS A CE    1 
ATOM   19533 N  NZ    . LYS A 1 4111 ? 192.087 238.077 184.240 1.00 8.21  ? 4111 LYS A NZ    1 
ATOM   19534 N  N     . LYS A 1 4112 ? 185.526 234.464 184.434 1.00 4.07  ? 4112 LYS A N     1 
ATOM   19535 C  CA    . LYS A 1 4112 ? 184.472 233.458 184.338 1.00 3.22  ? 4112 LYS A CA    1 
ATOM   19536 C  C     . LYS A 1 4112 ? 183.399 233.866 183.337 1.00 4.66  ? 4112 LYS A C     1 
ATOM   19537 O  O     . LYS A 1 4112 ? 182.924 233.037 182.552 1.00 6.00  ? 4112 LYS A O     1 
ATOM   19538 C  CB    . LYS A 1 4112 ? 183.852 233.215 185.714 1.00 3.93  ? 4112 LYS A CB    1 
ATOM   19539 C  CG    . LYS A 1 4112 ? 182.596 232.367 185.677 1.00 5.03  ? 4112 LYS A CG    1 
ATOM   19540 C  CD    . LYS A 1 4112 ? 181.990 232.199 187.055 1.00 4.33  ? 4112 LYS A CD    1 
ATOM   19541 C  CE    . LYS A 1 4112 ? 180.767 231.303 186.997 1.00 7.29  ? 4112 LYS A CE    1 
ATOM   19542 N  NZ    . LYS A 1 4112 ? 180.202 231.026 188.345 1.00 6.97  ? 4112 LYS A NZ    1 
ATOM   19543 N  N     . LEU A 1 4113 ? 182.997 235.139 183.352 1.00 7.00  ? 4113 LEU A N     1 
ATOM   19544 C  CA    . LEU A 1 4113 ? 181.953 235.600 182.445 1.00 5.99  ? 4113 LEU A CA    1 
ATOM   19545 C  C     . LEU A 1 4113 ? 182.411 235.581 180.995 1.00 7.16  ? 4113 LEU A C     1 
ATOM   19546 O  O     . LEU A 1 4113 ? 181.594 235.365 180.092 1.00 9.03  ? 4113 LEU A O     1 
ATOM   19547 C  CB    . LEU A 1 4113 ? 181.507 237.008 182.832 1.00 4.96  ? 4113 LEU A CB    1 
ATOM   19548 C  CG    . LEU A 1 4113 ? 180.789 237.152 184.170 1.00 6.96  ? 4113 LEU A CG    1 
ATOM   19549 C  CD1   . LEU A 1 4113 ? 180.651 238.619 184.536 1.00 4.35  ? 4113 LEU A CD1   1 
ATOM   19550 C  CD2   . LEU A 1 4113 ? 179.432 236.472 184.108 1.00 7.07  ? 4113 LEU A CD2   1 
ATOM   19551 N  N     . HIS A 1 4114 ? 183.702 235.809 180.752 1.00 8.93  ? 4114 HIS A N     1 
ATOM   19552 C  CA    . HIS A 1 4114 ? 184.204 235.877 179.385 1.00 7.34  ? 4114 HIS A CA    1 
ATOM   19553 C  C     . HIS A 1 4114 ? 184.009 234.556 178.652 1.00 8.54  ? 4114 HIS A C     1 
ATOM   19554 O  O     . HIS A 1 4114 ? 183.584 234.539 177.491 1.00 8.61  ? 4114 HIS A O     1 
ATOM   19555 C  CB    . HIS A 1 4114 ? 185.680 236.273 179.394 1.00 7.09  ? 4114 HIS A CB    1 
ATOM   19556 C  CG    . HIS A 1 4114 ? 186.266 236.454 178.030 1.00 6.15  ? 4114 HIS A CG    1 
ATOM   19557 N  ND1   . HIS A 1 4114 ? 186.163 237.635 177.328 1.00 5.76  ? 4114 HIS A ND1   1 
ATOM   19558 C  CD2   . HIS A 1 4114 ? 186.956 235.602 177.237 1.00 4.85  ? 4114 HIS A CD2   1 
ATOM   19559 C  CE1   . HIS A 1 4114 ? 186.766 237.504 176.160 1.00 8.25  ? 4114 HIS A CE1   1 
ATOM   19560 N  NE2   . HIS A 1 4114 ? 187.256 236.280 176.080 1.00 7.67  ? 4114 HIS A NE2   1 
ATOM   19561 N  N     . SER A 1 4115 ? 184.306 233.441 179.314 1.00 9.60  ? 4115 SER A N     1 
ATOM   19562 C  CA    . SER A 1 4115 ? 184.187 232.120 178.706 1.00 10.14 ? 4115 SER A CA    1 
ATOM   19563 C  C     . SER A 1 4115 ? 182.855 231.488 179.102 1.00 14.74 ? 4115 SER A C     1 
ATOM   19564 O  O     . SER A 1 4115 ? 182.786 230.490 179.818 1.00 17.48 ? 4115 SER A O     1 
ATOM   19565 C  CB    . SER A 1 4115 ? 185.366 231.244 179.115 1.00 9.24  ? 4115 SER A CB    1 
ATOM   19566 O  OG    . SER A 1 4115 ? 185.446 231.135 180.524 1.00 17.12 ? 4115 SER A OG    1 
ATOM   19567 N  N     . LEU A 1 4116 ? 181.777 232.093 178.608 1.00 13.45 ? 4116 LEU A N     1 
ATOM   19568 C  CA    . LEU A 1 4116 ? 180.443 231.641 178.972 1.00 12.58 ? 4116 LEU A CA    1 
ATOM   19569 C  C     . LEU A 1 4116 ? 179.441 232.157 177.949 1.00 15.91 ? 4116 LEU A C     1 
ATOM   19570 O  O     . LEU A 1 4116 ? 179.506 233.316 177.537 1.00 21.12 ? 4116 LEU A O     1 
ATOM   19571 C  CB    . LEU A 1 4116 ? 180.082 232.120 180.381 1.00 12.87 ? 4116 LEU A CB    1 
ATOM   19572 C  CG    . LEU A 1 4116 ? 178.706 231.802 180.953 1.00 15.75 ? 4116 LEU A CG    1 
ATOM   19573 C  CD1   . LEU A 1 4116 ? 178.393 230.322 180.809 1.00 14.08 ? 4116 LEU A CD1   1 
ATOM   19574 C  CD2   . LEU A 1 4116 ? 178.694 232.207 182.409 1.00 9.78  ? 4116 LEU A CD2   1 
ATOM   19575 N  N     . GLN A 1 4117 ? 178.519 231.283 177.545 1.00 12.52 ? 4117 GLN A N     1 
ATOM   19576 C  CA    . GLN A 1 4117 ? 177.460 231.614 176.589 1.00 15.35 ? 4117 GLN A CA    1 
ATOM   19577 C  C     . GLN A 1 4117 ? 176.133 231.280 177.250 1.00 15.19 ? 4117 GLN A C     1 
ATOM   19578 O  O     . GLN A 1 4117 ? 175.561 230.206 177.024 1.00 18.21 ? 4117 GLN A O     1 
ATOM   19579 C  CB    . GLN A 1 4117 ? 177.628 230.859 175.268 1.00 17.71 ? 4117 GLN A CB    1 
ATOM   19580 C  CG    . GLN A 1 4117 ? 178.772 231.338 174.384 1.00 19.72 ? 4117 GLN A CG    1 
ATOM   19581 C  CD    . GLN A 1 4117 ? 180.140 231.022 174.958 1.00 27.43 ? 4117 GLN A CD    1 
ATOM   19582 O  OE1   . GLN A 1 4117 ? 180.938 231.919 175.224 1.00 32.12 ? 4117 GLN A OE1   1 
ATOM   19583 N  NE2   . GLN A 1 4117 ? 180.416 229.737 175.150 1.00 22.70 ? 4117 GLN A NE2   1 
ATOM   19584 N  N     . PRO A 1 4118 ? 175.611 232.178 178.072 1.00 14.65 ? 4118 PRO A N     1 
ATOM   19585 C  CA    . PRO A 1 4118 ? 174.440 231.865 178.893 1.00 10.92 ? 4118 PRO A CA    1 
ATOM   19586 C  C     . PRO A 1 4118 ? 173.149 231.897 178.082 1.00 10.22 ? 4118 PRO A C     1 
ATOM   19587 O  O     . PRO A 1 4118 ? 173.139 232.127 176.874 1.00 13.85 ? 4118 PRO A O     1 
ATOM   19588 C  CB    . PRO A 1 4118 ? 174.460 232.965 179.954 1.00 6.82  ? 4118 PRO A CB    1 
ATOM   19589 C  CG    . PRO A 1 4118 ? 175.141 234.108 179.301 1.00 11.07 ? 4118 PRO A CG    1 
ATOM   19590 C  CD    . PRO A 1 4118 ? 176.116 233.542 178.311 1.00 8.99  ? 4118 PRO A CD    1 
ATOM   19591 N  N     . HIS A 1 4119 ? 172.049 231.642 178.783 1.00 9.85  ? 4119 HIS A N     1 
ATOM   19592 C  CA    . HIS A 1 4119 ? 170.727 231.742 178.185 1.00 9.96  ? 4119 HIS A CA    1 
ATOM   19593 C  C     . HIS A 1 4119 ? 170.450 233.179 177.765 1.00 11.53 ? 4119 HIS A C     1 
ATOM   19594 O  O     . HIS A 1 4119 ? 170.946 234.129 178.377 1.00 14.56 ? 4119 HIS A O     1 
ATOM   19595 C  CB    . HIS A 1 4119 ? 169.675 231.257 179.182 1.00 9.04  ? 4119 HIS A CB    1 
ATOM   19596 C  CG    . HIS A 1 4119 ? 168.292 231.172 178.621 1.00 11.90 ? 4119 HIS A CG    1 
ATOM   19597 N  ND1   . HIS A 1 4119 ? 167.424 232.242 178.613 1.00 16.86 ? 4119 HIS A ND1   1 
ATOM   19598 C  CD2   . HIS A 1 4119 ? 167.621 230.141 178.056 1.00 14.70 ? 4119 HIS A CD2   1 
ATOM   19599 C  CE1   . HIS A 1 4119 ? 166.280 231.876 178.065 1.00 17.39 ? 4119 HIS A CE1   1 
ATOM   19600 N  NE2   . HIS A 1 4119 ? 166.373 230.605 177.719 1.00 21.91 ? 4119 HIS A NE2   1 
ATOM   19601 N  N     . ALA A 1 4120 ? 169.655 233.337 176.702 1.00 8.63  ? 4120 ALA A N     1 
ATOM   19602 C  CA    . ALA A 1 4120 ? 169.415 234.664 176.145 1.00 7.55  ? 4120 ALA A CA    1 
ATOM   19603 C  C     . ALA A 1 4120 ? 168.759 235.598 177.155 1.00 10.28 ? 4120 ALA A C     1 
ATOM   19604 O  O     . ALA A 1 4120 ? 168.938 236.819 177.075 1.00 14.81 ? 4120 ALA A O     1 
ATOM   19605 C  CB    . ALA A 1 4120 ? 168.557 234.556 174.887 1.00 10.84 ? 4120 ALA A CB    1 
ATOM   19606 N  N     . CYS A 1 4121 ? 168.003 235.053 178.104 1.00 9.22  ? 4121 CYS A N     1 
ATOM   19607 C  CA    . CYS A 1 4121 ? 167.332 235.860 179.114 1.00 6.62  ? 4121 CYS A CA    1 
ATOM   19608 C  C     . CYS A 1 4121 ? 168.163 236.073 180.371 1.00 4.55  ? 4121 CYS A C     1 
ATOM   19609 O  O     . CYS A 1 4121 ? 167.749 236.846 181.240 1.00 3.72  ? 4121 CYS A O     1 
ATOM   19610 C  CB    . CYS A 1 4121 ? 165.993 235.218 179.497 1.00 9.21  ? 4121 CYS A CB    1 
ATOM   19611 S  SG    . CYS A 1 4121 ? 164.614 235.663 178.427 1.00 38.83 ? 4121 CYS A SG    1 
ATOM   19612 N  N     . PHE A 1 4122 ? 169.317 235.419 180.495 1.00 4.81  ? 4122 PHE A N     1 
ATOM   19613 C  CA    . PHE A 1 4122 ? 170.132 235.576 181.691 1.00 3.08  ? 4122 PHE A CA    1 
ATOM   19614 C  C     . PHE A 1 4122 ? 170.681 236.992 181.791 1.00 2.55  ? 4122 PHE A C     1 
ATOM   19615 O  O     . PHE A 1 4122 ? 171.157 237.567 180.809 1.00 3.64  ? 4122 PHE A O     1 
ATOM   19616 C  CB    . PHE A 1 4122 ? 171.290 234.577 181.697 1.00 1.83  ? 4122 PHE A CB    1 
ATOM   19617 C  CG    . PHE A 1 4122 ? 172.396 234.942 182.651 1.00 1.98  ? 4122 PHE A CG    1 
ATOM   19618 C  CD1   . PHE A 1 4122 ? 172.265 234.698 184.007 1.00 1.58  ? 4122 PHE A CD1   1 
ATOM   19619 C  CD2   . PHE A 1 4122 ? 173.558 235.541 182.197 1.00 1.44  ? 4122 PHE A CD2   1 
ATOM   19620 C  CE1   . PHE A 1 4122 ? 173.270 235.036 184.887 1.00 0.84  ? 4122 PHE A CE1   1 
ATOM   19621 C  CE2   . PHE A 1 4122 ? 174.565 235.882 183.075 1.00 0.59  ? 4122 PHE A CE2   1 
ATOM   19622 C  CZ    . PHE A 1 4122 ? 174.422 235.629 184.421 1.00 0.57  ? 4122 PHE A CZ    1 
ATOM   19623 N  N     . ARG A 1 4123 ? 170.622 237.550 182.995 1.00 1.55  ? 4123 ARG A N     1 
ATOM   19624 C  CA    . ARG A 1 4123 ? 171.211 238.847 183.282 1.00 1.23  ? 4123 ARG A CA    1 
ATOM   19625 C  C     . ARG A 1 4123 ? 171.933 238.773 184.618 1.00 0.50  ? 4123 ARG A C     1 
ATOM   19626 O  O     . ARG A 1 4123 ? 171.427 238.174 185.570 1.00 0.45  ? 4123 ARG A O     1 
ATOM   19627 C  CB    . ARG A 1 4123 ? 170.152 239.956 183.312 1.00 0.97  ? 4123 ARG A CB    1 
ATOM   19628 C  CG    . ARG A 1 4123 ? 169.522 240.248 181.964 1.00 1.44  ? 4123 ARG A CG    1 
ATOM   19629 C  CD    . ARG A 1 4123 ? 170.543 240.794 180.978 1.00 2.74  ? 4123 ARG A CD    1 
ATOM   19630 N  NE    . ARG A 1 4123 ? 169.968 241.015 179.658 1.00 6.51  ? 4123 ARG A NE    1 
ATOM   19631 C  CZ    . ARG A 1 4123 ? 169.660 240.053 178.797 1.00 4.73  ? 4123 ARG A CZ    1 
ATOM   19632 N  NH1   . ARG A 1 4123 ? 169.900 238.781 179.066 1.00 3.24  ? 4123 ARG A NH1   1 
ATOM   19633 N  NH2   . ARG A 1 4123 ? 169.102 240.379 177.636 1.00 7.65  ? 4123 ARG A NH2   1 
ATOM   19634 N  N     . LEU A 1 4124 ? 173.117 239.371 184.679 1.00 0.67  ? 4124 LEU A N     1 
ATOM   19635 C  CA    . LEU A 1 4124 ? 173.886 239.473 185.913 1.00 0.38  ? 4124 LEU A CA    1 
ATOM   19636 C  C     . LEU A 1 4124 ? 174.005 240.941 186.293 1.00 0.22  ? 4124 LEU A C     1 
ATOM   19637 O  O     . LEU A 1 4124 ? 174.507 241.750 185.506 1.00 0.41  ? 4124 LEU A O     1 
ATOM   19638 C  CB    . LEU A 1 4124 ? 175.270 238.842 185.758 1.00 0.25  ? 4124 LEU A CB    1 
ATOM   19639 C  CG    . LEU A 1 4124 ? 176.195 239.030 186.962 1.00 0.37  ? 4124 LEU A CG    1 
ATOM   19640 C  CD1   . LEU A 1 4124 ? 175.674 238.258 188.165 1.00 0.24  ? 4124 LEU A CD1   1 
ATOM   19641 C  CD2   . LEU A 1 4124 ? 177.618 238.625 186.629 1.00 0.55  ? 4124 LEU A CD2   1 
ATOM   19642 N  N     . PHE A 1 4125 ? 173.546 241.281 187.493 1.00 0.18  ? 4125 PHE A N     1 
ATOM   19643 C  CA    . PHE A 1 4125 ? 173.621 242.638 188.014 1.00 0.41  ? 4125 PHE A CA    1 
ATOM   19644 C  C     . PHE A 1 4125 ? 174.664 242.692 189.118 1.00 0.15  ? 4125 PHE A C     1 
ATOM   19645 O  O     . PHE A 1 4125 ? 174.636 241.878 190.045 1.00 0.15  ? 4125 PHE A O     1 
ATOM   19646 C  CB    . PHE A 1 4125 ? 172.265 243.109 188.549 1.00 0.43  ? 4125 PHE A CB    1 
ATOM   19647 C  CG    . PHE A 1 4125 ? 171.185 243.174 187.509 1.00 0.48  ? 4125 PHE A CG    1 
ATOM   19648 C  CD1   . PHE A 1 4125 ? 170.428 242.056 187.202 1.00 0.42  ? 4125 PHE A CD1   1 
ATOM   19649 C  CD2   . PHE A 1 4125 ? 170.922 244.357 186.842 1.00 0.23  ? 4125 PHE A CD2   1 
ATOM   19650 C  CE1   . PHE A 1 4125 ? 169.434 242.118 186.247 1.00 0.47  ? 4125 PHE A CE1   1 
ATOM   19651 C  CE2   . PHE A 1 4125 ? 169.929 244.426 185.887 1.00 0.24  ? 4125 PHE A CE2   1 
ATOM   19652 C  CZ    . PHE A 1 4125 ? 169.184 243.306 185.590 1.00 0.93  ? 4125 PHE A CZ    1 
ATOM   19653 N  N     . LEU A 1 4126 ? 175.586 243.641 189.012 1.00 0.27  ? 4126 LEU A N     1 
ATOM   19654 C  CA    . LEU A 1 4126 ? 176.606 243.856 190.029 1.00 0.43  ? 4126 LEU A CA    1 
ATOM   19655 C  C     . LEU A 1 4126 ? 176.390 245.230 190.641 1.00 0.56  ? 4126 LEU A C     1 
ATOM   19656 O  O     . LEU A 1 4126 ? 176.390 246.239 189.931 1.00 0.97  ? 4126 LEU A O     1 
ATOM   19657 C  CB    . LEU A 1 4126 ? 178.012 243.735 189.440 1.00 0.43  ? 4126 LEU A CB    1 
ATOM   19658 C  CG    . LEU A 1 4126 ? 178.348 242.416 188.741 1.00 0.25  ? 4126 LEU A CG    1 
ATOM   19659 C  CD1   . LEU A 1 4126 ? 179.804 242.395 188.306 1.00 0.13  ? 4126 LEU A CD1   1 
ATOM   19660 C  CD2   . LEU A 1 4126 ? 178.035 241.237 189.642 1.00 0.12  ? 4126 LEU A CD2   1 
ATOM   19661 N  N     . THR A 1 4127 ? 176.205 245.260 191.954 1.00 1.38  ? 4127 THR A N     1 
ATOM   19662 C  CA    . THR A 1 4127 ? 176.032 246.497 192.698 1.00 0.62  ? 4127 THR A CA    1 
ATOM   19663 C  C     . THR A 1 4127 ? 177.331 246.821 193.417 1.00 0.61  ? 4127 THR A C     1 
ATOM   19664 O  O     . THR A 1 4127 ? 177.885 245.972 194.124 1.00 2.04  ? 4127 THR A O     1 
ATOM   19665 C  CB    . THR A 1 4127 ? 174.880 246.376 193.698 1.00 0.98  ? 4127 THR A CB    1 
ATOM   19666 O  OG1   . THR A 1 4127 ? 173.635 246.309 192.992 1.00 1.71  ? 4127 THR A OG1   1 
ATOM   19667 C  CG2   . THR A 1 4127 ? 174.862 247.555 194.649 1.00 5.74  ? 4127 THR A CG2   1 
ATOM   19668 N  N     . MET A 1 4128 ? 177.826 248.037 193.217 1.00 1.01  ? 4128 MET A N     1 
ATOM   19669 C  CA    . MET A 1 4128 ? 179.042 248.473 193.879 1.00 1.10  ? 4128 MET A CA    1 
ATOM   19670 C  C     . MET A 1 4128 ? 178.989 249.979 194.066 1.00 1.04  ? 4128 MET A C     1 
ATOM   19671 O  O     . MET A 1 4128 ? 178.261 250.689 193.367 1.00 1.70  ? 4128 MET A O     1 
ATOM   19672 C  CB    . MET A 1 4128 ? 180.295 248.081 193.086 1.00 1.12  ? 4128 MET A CB    1 
ATOM   19673 C  CG    . MET A 1 4128 ? 180.504 248.894 191.822 1.00 1.90  ? 4128 MET A CG    1 
ATOM   19674 S  SD    . MET A 1 4128 ? 179.261 248.538 190.569 1.00 31.07 ? 4128 MET A SD    1 
ATOM   19675 C  CE    . MET A 1 4128 ? 179.708 246.870 190.114 1.00 4.24  ? 4128 MET A CE    1 
ATOM   19676 N  N     . GLU A 1 4129 ? 179.759 250.455 195.034 1.00 1.37  ? 4129 GLU A N     1 
ATOM   19677 C  CA    . GLU A 1 4129 ? 180.006 251.877 195.156 1.00 1.70  ? 4129 GLU A CA    1 
ATOM   19678 C  C     . GLU A 1 4129 ? 181.043 252.303 194.123 1.00 2.99  ? 4129 GLU A C     1 
ATOM   19679 O  O     . GLU A 1 4129 ? 181.801 251.486 193.592 1.00 8.77  ? 4129 GLU A O     1 
ATOM   19680 C  CB    . GLU A 1 4129 ? 180.488 252.226 196.563 1.00 4.16  ? 4129 GLU A CB    1 
ATOM   19681 C  CG    . GLU A 1 4129 ? 179.474 251.953 197.653 1.00 7.20  ? 4129 GLU A CG    1 
ATOM   19682 C  CD    . GLU A 1 4129 ? 179.879 252.550 198.986 1.00 18.36 ? 4129 GLU A CD    1 
ATOM   19683 O  OE1   . GLU A 1 4129 ? 181.092 252.720 199.218 1.00 20.86 ? 4129 GLU A OE1   1 
ATOM   19684 O  OE2   . GLU A 1 4129 ? 178.983 252.848 199.804 1.00 16.50 ? 4129 GLU A OE2   1 
ATOM   19685 N  N     . ILE A 1 4130 ? 181.076 253.600 193.837 1.00 2.27  ? 4130 ILE A N     1 
ATOM   19686 C  CA    . ILE A 1 4130 ? 182.076 254.123 192.916 1.00 2.47  ? 4130 ILE A CA    1 
ATOM   19687 C  C     . ILE A 1 4130 ? 183.410 254.110 193.647 1.00 2.95  ? 4130 ILE A C     1 
ATOM   19688 O  O     . ILE A 1 4130 ? 183.707 255.001 194.449 1.00 10.47 ? 4130 ILE A O     1 
ATOM   19689 C  CB    . ILE A 1 4130 ? 181.706 255.527 192.409 1.00 3.42  ? 4130 ILE A CB    1 
ATOM   19690 C  CG1   . ILE A 1 4130 ? 180.366 255.475 191.668 1.00 1.25  ? 4130 ILE A CG1   1 
ATOM   19691 C  CG2   . ILE A 1 4130 ? 182.804 256.079 191.517 1.00 1.17  ? 4130 ILE A CG2   1 
ATOM   19692 C  CD1   . ILE A 1 4130 ? 179.968 256.775 191.015 1.00 0.56  ? 4130 ILE A CD1   1 
ATOM   19693 N  N     . ASN A 1 4131 ? 184.212 253.084 193.380 1.00 2.80  ? 4131 ASN A N     1 
ATOM   19694 C  CA    . ASN A 1 4131 ? 185.416 252.804 194.139 1.00 3.53  ? 4131 ASN A CA    1 
ATOM   19695 C  C     . ASN A 1 4131 ? 186.564 252.533 193.176 1.00 2.64  ? 4131 ASN A C     1 
ATOM   19696 O  O     . ASN A 1 4131 ? 186.403 251.748 192.226 1.00 3.15  ? 4131 ASN A O     1 
ATOM   19697 C  CB    . ASN A 1 4131 ? 185.195 251.599 195.066 1.00 3.56  ? 4131 ASN A CB    1 
ATOM   19698 C  CG    . ASN A 1 4131 ? 186.172 251.560 196.220 1.00 6.70  ? 4131 ASN A CG    1 
ATOM   19699 O  OD1   . ASN A 1 4131 ? 187.386 251.577 196.022 1.00 10.94 ? 4131 ASN A OD1   1 
ATOM   19700 N  ND2   . ASN A 1 4131 ? 185.648 251.503 197.435 1.00 10.11 ? 4131 ASN A ND2   1 
ATOM   19701 N  N     . PRO A 1 4132 ? 187.730 253.148 193.379 1.00 2.69  ? 4132 PRO A N     1 
ATOM   19702 C  CA    . PRO A 1 4132 ? 188.888 252.834 192.526 1.00 2.21  ? 4132 PRO A CA    1 
ATOM   19703 C  C     . PRO A 1 4132 ? 189.372 251.399 192.658 1.00 4.75  ? 4132 PRO A C     1 
ATOM   19704 O  O     . PRO A 1 4132 ? 190.144 250.949 191.802 1.00 7.22  ? 4132 PRO A O     1 
ATOM   19705 C  CB    . PRO A 1 4132 ? 189.955 253.833 192.998 1.00 2.41  ? 4132 PRO A CB    1 
ATOM   19706 C  CG    . PRO A 1 4132 ? 189.518 254.251 194.361 1.00 2.36  ? 4132 PRO A CG    1 
ATOM   19707 C  CD    . PRO A 1 4132 ? 188.025 254.227 194.337 1.00 2.18  ? 4132 PRO A CD    1 
ATOM   19708 N  N     . LYS A 1 4133 ? 188.958 250.677 193.699 1.00 5.64  ? 4133 LYS A N     1 
ATOM   19709 C  CA    . LYS A 1 4133 ? 189.358 249.284 193.858 1.00 4.69  ? 4133 LYS A CA    1 
ATOM   19710 C  C     . LYS A 1 4133 ? 188.717 248.367 192.823 1.00 5.70  ? 4133 LYS A C     1 
ATOM   19711 O  O     . LYS A 1 4133 ? 189.231 247.266 192.594 1.00 11.84 ? 4133 LYS A O     1 
ATOM   19712 C  CB    . LYS A 1 4133 ? 189.009 248.794 195.264 1.00 8.60  ? 4133 LYS A CB    1 
ATOM   19713 C  CG    . LYS A 1 4133 ? 189.897 249.362 196.358 1.00 8.35  ? 4133 LYS A CG    1 
ATOM   19714 C  CD    . LYS A 1 4133 ? 191.341 248.934 196.175 1.00 11.04 ? 4133 LYS A CD    1 
ATOM   19715 C  CE    . LYS A 1 4133 ? 191.486 247.424 196.251 1.00 16.94 ? 4133 LYS A CE    1 
ATOM   19716 N  NZ    . LYS A 1 4133 ? 191.005 246.891 197.555 1.00 16.56 ? 4133 LYS A NZ    1 
ATOM   19717 N  N     . VAL A 1 4134 ? 187.615 248.784 192.207 1.00 2.43  ? 4134 VAL A N     1 
ATOM   19718 C  CA    . VAL A 1 4134 ? 186.951 247.930 191.213 1.00 1.68  ? 4134 VAL A CA    1 
ATOM   19719 C  C     . VAL A 1 4134 ? 187.883 247.728 190.023 1.00 2.10  ? 4134 VAL A C     1 
ATOM   19720 O  O     . VAL A 1 4134 ? 188.426 248.715 189.487 1.00 5.20  ? 4134 VAL A O     1 
ATOM   19721 C  CB    . VAL A 1 4134 ? 185.615 248.550 190.771 1.00 2.53  ? 4134 VAL A CB    1 
ATOM   19722 C  CG1   . VAL A 1 4134 ? 185.086 247.857 189.525 1.00 0.97  ? 4134 VAL A CG1   1 
ATOM   19723 C  CG2   . VAL A 1 4134 ? 184.593 248.469 191.897 1.00 1.38  ? 4134 VAL A CG2   1 
ATOM   19724 N  N     . PRO A 1 4135 ? 188.115 246.493 189.579 1.00 2.82  ? 4135 PRO A N     1 
ATOM   19725 C  CA    . PRO A 1 4135 ? 189.076 246.262 188.495 1.00 2.82  ? 4135 PRO A CA    1 
ATOM   19726 C  C     . PRO A 1 4135 ? 188.636 246.914 187.192 1.00 2.20  ? 4135 PRO A C     1 
ATOM   19727 O  O     . PRO A 1 4135 ? 187.449 246.978 186.870 1.00 1.68  ? 4135 PRO A O     1 
ATOM   19728 C  CB    . PRO A 1 4135 ? 189.111 244.735 188.368 1.00 2.16  ? 4135 PRO A CB    1 
ATOM   19729 C  CG    . PRO A 1 4135 ? 188.484 244.218 189.621 1.00 3.20  ? 4135 PRO A CG    1 
ATOM   19730 C  CD    . PRO A 1 4135 ? 187.490 245.243 190.035 1.00 1.37  ? 4135 PRO A CD    1 
ATOM   19731 N  N     . VAL A 1 4136 ? 189.626 247.390 186.435 1.00 2.84  ? 4136 VAL A N     1 
ATOM   19732 C  CA    . VAL A 1 4136 ? 189.358 247.972 185.123 1.00 2.46  ? 4136 VAL A CA    1 
ATOM   19733 C  C     . VAL A 1 4136 ? 188.790 246.926 184.176 1.00 1.59  ? 4136 VAL A C     1 
ATOM   19734 O  O     . VAL A 1 4136 ? 187.874 247.207 183.394 1.00 1.92  ? 4136 VAL A O     1 
ATOM   19735 C  CB    . VAL A 1 4136 ? 190.639 248.613 184.556 1.00 3.88  ? 4136 VAL A CB    1 
ATOM   19736 C  CG1   . VAL A 1 4136 ? 190.402 249.124 183.146 1.00 6.22  ? 4136 VAL A CG1   1 
ATOM   19737 C  CG2   . VAL A 1 4136 ? 191.103 249.745 185.454 1.00 2.35  ? 4136 VAL A CG2   1 
ATOM   19738 N  N     . ASN A 1 4137 ? 189.317 245.702 184.232 1.00 1.99  ? 4137 ASN A N     1 
ATOM   19739 C  CA    . ASN A 1 4137 ? 188.894 244.665 183.297 1.00 2.08  ? 4137 ASN A CA    1 
ATOM   19740 C  C     . ASN A 1 4137 ? 187.415 244.338 183.461 1.00 1.76  ? 4137 ASN A C     1 
ATOM   19741 O  O     . ASN A 1 4137 ? 186.717 244.084 182.474 1.00 3.49  ? 4137 ASN A O     1 
ATOM   19742 C  CB    . ASN A 1 4137 ? 189.750 243.411 183.481 1.00 3.53  ? 4137 ASN A CB    1 
ATOM   19743 C  CG    . ASN A 1 4137 ? 190.187 242.809 182.162 1.00 11.36 ? 4137 ASN A CG    1 
ATOM   19744 O  OD1   . ASN A 1 4137 ? 190.319 243.513 181.160 1.00 10.95 ? 4137 ASN A OD1   1 
ATOM   19745 N  ND2   . ASN A 1 4137 ? 190.414 241.501 182.153 1.00 10.80 ? 4137 ASN A ND2   1 
ATOM   19746 N  N     . LEU A 1 4138 ? 186.923 244.324 184.701 1.00 2.25  ? 4138 LEU A N     1 
ATOM   19747 C  CA    . LEU A 1 4138 ? 185.495 244.131 184.922 1.00 0.85  ? 4138 LEU A CA    1 
ATOM   19748 C  C     . LEU A 1 4138 ? 184.687 245.296 184.364 1.00 0.82  ? 4138 LEU A C     1 
ATOM   19749 O  O     . LEU A 1 4138 ? 183.626 245.095 183.764 1.00 1.15  ? 4138 LEU A O     1 
ATOM   19750 C  CB    . LEU A 1 4138 ? 185.207 243.951 186.410 1.00 1.97  ? 4138 LEU A CB    1 
ATOM   19751 C  CG    . LEU A 1 4138 ? 183.715 243.833 186.732 1.00 0.60  ? 4138 LEU A CG    1 
ATOM   19752 C  CD1   . LEU A 1 4138 ? 183.231 242.407 186.537 1.00 0.38  ? 4138 LEU A CD1   1 
ATOM   19753 C  CD2   . LEU A 1 4138 ? 183.411 244.335 188.129 1.00 0.42  ? 4138 LEU A CD2   1 
ATOM   19754 N  N     . LEU A 1 4139 ? 185.177 246.524 184.550 1.00 0.74  ? 4139 LEU A N     1 
ATOM   19755 C  CA    . LEU A 1 4139 ? 184.455 247.697 184.069 1.00 0.48  ? 4139 LEU A CA    1 
ATOM   19756 C  C     . LEU A 1 4139 ? 184.311 247.677 182.552 1.00 0.97  ? 4139 LEU A C     1 
ATOM   19757 O  O     . LEU A 1 4139 ? 183.251 248.017 182.017 1.00 2.07  ? 4139 LEU A O     1 
ATOM   19758 C  CB    . LEU A 1 4139 ? 185.163 248.971 184.522 1.00 0.61  ? 4139 LEU A CB    1 
ATOM   19759 C  CG    . LEU A 1 4139 ? 185.129 249.297 186.016 1.00 1.15  ? 4139 LEU A CG    1 
ATOM   19760 C  CD1   . LEU A 1 4139 ? 185.992 250.507 186.316 1.00 0.45  ? 4139 LEU A CD1   1 
ATOM   19761 C  CD2   . LEU A 1 4139 ? 183.704 249.524 186.491 1.00 0.68  ? 4139 LEU A CD2   1 
ATOM   19762 N  N     . ARG A 1 4140 ? 185.372 247.288 181.842 1.00 0.77  ? 4140 ARG A N     1 
ATOM   19763 C  CA    . ARG A 1 4140 ? 185.302 247.221 180.387 1.00 0.99  ? 4140 ARG A CA    1 
ATOM   19764 C  C     . ARG A 1 4140 ? 184.339 246.141 179.914 1.00 0.87  ? 4140 ARG A C     1 
ATOM   19765 O  O     . ARG A 1 4140 ? 183.638 246.332 178.914 1.00 0.89  ? 4140 ARG A O     1 
ATOM   19766 C  CB    . ARG A 1 4140 ? 186.696 246.985 179.808 1.00 1.56  ? 4140 ARG A CB    1 
ATOM   19767 C  CG    . ARG A 1 4140 ? 187.696 248.073 180.151 1.00 1.77  ? 4140 ARG A CG    1 
ATOM   19768 C  CD    . ARG A 1 4140 ? 189.081 247.746 179.631 1.00 1.49  ? 4140 ARG A CD    1 
ATOM   19769 N  NE    . ARG A 1 4140 ? 189.032 247.026 178.366 1.00 5.75  ? 4140 ARG A NE    1 
ATOM   19770 C  CZ    . ARG A 1 4140 ? 189.328 247.559 177.189 1.00 4.95  ? 4140 ARG A CZ    1 
ATOM   19771 N  NH1   . ARG A 1 4140 ? 189.699 248.823 177.079 1.00 4.99  ? 4140 ARG A NH1   1 
ATOM   19772 N  NH2   . ARG A 1 4140 ? 189.241 246.807 176.097 1.00 1.87  ? 4140 ARG A NH2   1 
ATOM   19773 N  N     . ALA A 1 4141 ? 184.288 245.008 180.614 1.00 1.13  ? 4141 ALA A N     1 
ATOM   19774 C  CA    . ALA A 1 4141 ? 183.433 243.899 180.211 1.00 0.95  ? 4141 ALA A CA    1 
ATOM   19775 C  C     . ALA A 1 4141 ? 181.951 244.189 180.399 1.00 1.43  ? 4141 ALA A C     1 
ATOM   19776 O  O     . ALA A 1 4141 ? 181.130 243.660 179.642 1.00 3.03  ? 4141 ALA A O     1 
ATOM   19777 C  CB    . ALA A 1 4141 ? 183.809 242.639 180.989 1.00 1.05  ? 4141 ALA A CB    1 
ATOM   19778 N  N     . GLY A 1 4142 ? 181.588 245.007 181.385 1.00 0.59  ? 4142 GLY A N     1 
ATOM   19779 C  CA    . GLY A 1 4142 ? 180.206 245.307 181.673 1.00 0.77  ? 4142 GLY A CA    1 
ATOM   19780 C  C     . GLY A 1 4142 ? 179.797 246.676 181.150 1.00 0.59  ? 4142 GLY A C     1 
ATOM   19781 O  O     . GLY A 1 4142 ? 180.601 247.448 180.636 1.00 0.74  ? 4142 GLY A O     1 
ATOM   19782 N  N     . ARG A 1 4143 ? 178.508 246.959 181.283 1.00 0.39  ? 4143 ARG A N     1 
ATOM   19783 C  CA    . ARG A 1 4143 ? 177.971 248.273 180.963 1.00 0.40  ? 4143 ARG A CA    1 
ATOM   19784 C  C     . ARG A 1 4143 ? 177.670 249.005 182.264 1.00 0.26  ? 4143 ARG A C     1 
ATOM   19785 O  O     . ARG A 1 4143 ? 176.971 248.477 183.134 1.00 0.91  ? 4143 ARG A O     1 
ATOM   19786 C  CB    . ARG A 1 4143 ? 176.732 248.181 180.078 1.00 0.56  ? 4143 ARG A CB    1 
ATOM   19787 C  CG    . ARG A 1 4143 ? 176.218 249.546 179.662 1.00 2.52  ? 4143 ARG A CG    1 
ATOM   19788 C  CD    . ARG A 1 4143 ? 175.049 249.465 178.712 1.00 7.27  ? 4143 ARG A CD    1 
ATOM   19789 N  NE    . ARG A 1 4143 ? 174.557 250.793 178.367 1.00 8.71  ? 4143 ARG A NE    1 
ATOM   19790 C  CZ    . ARG A 1 4143 ? 173.549 251.027 177.540 1.00 7.39  ? 4143 ARG A CZ    1 
ATOM   19791 N  NH1   . ARG A 1 4143 ? 172.970 250.050 176.864 1.00 5.18  ? 4143 ARG A NH1   1 
ATOM   19792 N  NH2   . ARG A 1 4143 ? 173.109 252.272 177.388 1.00 9.84  ? 4143 ARG A NH2   1 
ATOM   19793 N  N     . ILE A 1 4144 ? 178.201 250.212 182.387 1.00 0.24  ? 4144 ILE A N     1 
ATOM   19794 C  CA    . ILE A 1 4144 ? 178.192 250.956 183.637 1.00 0.44  ? 4144 ILE A CA    1 
ATOM   19795 C  C     . ILE A 1 4144 ? 176.978 251.871 183.672 1.00 0.38  ? 4144 ILE A C     1 
ATOM   19796 O  O     . ILE A 1 4144 ? 176.676 252.560 182.689 1.00 0.30  ? 4144 ILE A O     1 
ATOM   19797 C  CB    . ILE A 1 4144 ? 179.494 251.757 183.795 1.00 0.38  ? 4144 ILE A CB    1 
ATOM   19798 C  CG1   . ILE A 1 4144 ? 180.698 250.822 183.662 1.00 0.56  ? 4144 ILE A CG1   1 
ATOM   19799 C  CG2   . ILE A 1 4144 ? 179.511 252.513 185.110 1.00 0.45  ? 4144 ILE A CG2   1 
ATOM   19800 C  CD1   . ILE A 1 4144 ? 181.994 251.521 183.352 1.00 0.97  ? 4144 ILE A CD1   1 
ATOM   19801 N  N     . PHE A 1 4145 ? 176.267 251.866 184.796 1.00 0.66  ? 4145 PHE A N     1 
ATOM   19802 C  CA    . PHE A 1 4145 ? 175.186 252.806 185.059 1.00 0.24  ? 4145 PHE A CA    1 
ATOM   19803 C  C     . PHE A 1 4145 ? 175.482 253.511 186.372 1.00 0.29  ? 4145 PHE A C     1 
ATOM   19804 O  O     . PHE A 1 4145 ? 175.639 252.857 187.408 1.00 1.56  ? 4145 PHE A O     1 
ATOM   19805 C  CB    . PHE A 1 4145 ? 173.832 252.100 185.110 1.00 0.52  ? 4145 PHE A CB    1 
ATOM   19806 C  CG    . PHE A 1 4145 ? 173.440 251.463 183.815 1.00 1.59  ? 4145 PHE A CG    1 
ATOM   19807 C  CD1   . PHE A 1 4145 ? 172.805 252.198 182.830 1.00 1.86  ? 4145 PHE A CD1   1 
ATOM   19808 C  CD2   . PHE A 1 4145 ? 173.715 250.127 183.578 1.00 1.60  ? 4145 PHE A CD2   1 
ATOM   19809 C  CE1   . PHE A 1 4145 ? 172.452 251.611 181.634 1.00 5.21  ? 4145 PHE A CE1   1 
ATOM   19810 C  CE2   . PHE A 1 4145 ? 173.362 249.537 182.386 1.00 1.13  ? 4145 PHE A CE2   1 
ATOM   19811 C  CZ    . PHE A 1 4145 ? 172.730 250.279 181.414 1.00 4.80  ? 4145 PHE A CZ    1 
ATOM   19812 N  N     . VAL A 1 4146 ? 175.566 254.833 186.328 1.00 0.25  ? 4146 VAL A N     1 
ATOM   19813 C  CA    . VAL A 1 4146 ? 175.870 255.632 187.508 1.00 0.44  ? 4146 VAL A CA    1 
ATOM   19814 C  C     . VAL A 1 4146 ? 174.564 256.066 188.157 1.00 0.31  ? 4146 VAL A C     1 
ATOM   19815 O  O     . VAL A 1 4146 ? 173.672 256.598 187.488 1.00 0.23  ? 4146 VAL A O     1 
ATOM   19816 C  CB    . VAL A 1 4146 ? 176.741 256.846 187.144 1.00 0.30  ? 4146 VAL A CB    1 
ATOM   19817 C  CG1   . VAL A 1 4146 ? 176.729 257.870 188.272 1.00 0.59  ? 4146 VAL A CG1   1 
ATOM   19818 C  CG2   . VAL A 1 4146 ? 178.157 256.407 186.843 1.00 0.14  ? 4146 VAL A CG2   1 
ATOM   19819 N  N     . PHE A 1 4147 ? 174.448 255.829 189.458 1.00 0.46  ? 4147 PHE A N     1 
ATOM   19820 C  CA    . PHE A 1 4147 ? 173.298 256.262 190.240 1.00 0.64  ? 4147 PHE A CA    1 
ATOM   19821 C  C     . PHE A 1 4147 ? 173.757 257.304 191.247 1.00 0.60  ? 4147 PHE A C     1 
ATOM   19822 O  O     . PHE A 1 4147 ? 174.658 257.048 192.050 1.00 0.94  ? 4147 PHE A O     1 
ATOM   19823 C  CB    . PHE A 1 4147 ? 172.628 255.075 190.928 1.00 0.91  ? 4147 PHE A CB    1 
ATOM   19824 C  CG    . PHE A 1 4147 ? 171.951 254.150 189.973 1.00 1.09  ? 4147 PHE A CG    1 
ATOM   19825 C  CD1   . PHE A 1 4147 ? 172.659 253.143 189.348 1.00 0.88  ? 4147 PHE A CD1   1 
ATOM   19826 C  CD2   . PHE A 1 4147 ? 170.607 254.297 189.681 1.00 1.04  ? 4147 PHE A CD2   1 
ATOM   19827 C  CE1   . PHE A 1 4147 ? 172.045 252.302 188.456 1.00 0.59  ? 4147 PHE A CE1   1 
ATOM   19828 C  CE2   . PHE A 1 4147 ? 169.983 253.451 188.791 1.00 1.89  ? 4147 PHE A CE2   1 
ATOM   19829 C  CZ    . PHE A 1 4147 ? 170.702 252.449 188.179 1.00 2.12  ? 4147 PHE A CZ    1 
ATOM   19830 N  N     . GLU A 1 4148 ? 173.135 258.472 191.192 1.00 0.94  ? 4148 GLU A N     1 
ATOM   19831 C  CA    . GLU A 1 4148 ? 173.568 259.628 191.960 1.00 1.56  ? 4148 GLU A CA    1 
ATOM   19832 C  C     . GLU A 1 4148 ? 172.345 260.490 192.212 1.00 2.66  ? 4148 GLU A C     1 
ATOM   19833 O  O     . GLU A 1 4148 ? 171.254 260.190 191.713 1.00 4.18  ? 4148 GLU A O     1 
ATOM   19834 C  CB    . GLU A 1 4148 ? 174.661 260.405 191.212 1.00 2.26  ? 4148 GLU A CB    1 
ATOM   19835 C  CG    . GLU A 1 4148 ? 174.202 261.088 189.940 1.00 2.95  ? 4148 GLU A CG    1 
ATOM   19836 C  CD    . GLU A 1 4148 ? 175.357 261.659 189.140 1.00 6.17  ? 4148 GLU A CD    1 
ATOM   19837 O  OE1   . GLU A 1 4148 ? 176.157 262.429 189.713 1.00 3.92  ? 4148 GLU A OE1   1 
ATOM   19838 O  OE2   . GLU A 1 4148 ? 175.463 261.342 187.938 1.00 9.18  ? 4148 GLU A OE2   1 
ATOM   19839 N  N     . PRO A 1 4149 ? 172.477 261.547 193.012 1.00 3.72  ? 4149 PRO A N     1 
ATOM   19840 C  CA    . PRO A 1 4149 ? 171.362 262.480 193.180 1.00 3.52  ? 4149 PRO A CA    1 
ATOM   19841 C  C     . PRO A 1 4149 ? 170.905 263.026 191.840 1.00 3.49  ? 4149 PRO A C     1 
ATOM   19842 O  O     . PRO A 1 4149 ? 171.731 263.305 190.960 1.00 5.88  ? 4149 PRO A O     1 
ATOM   19843 C  CB    . PRO A 1 4149 ? 171.961 263.588 194.056 1.00 5.03  ? 4149 PRO A CB    1 
ATOM   19844 C  CG    . PRO A 1 4149 ? 172.984 262.899 194.856 1.00 5.56  ? 4149 PRO A CG    1 
ATOM   19845 C  CD    . PRO A 1 4149 ? 173.549 261.808 193.991 1.00 3.91  ? 4149 PRO A CD    1 
ATOM   19846 N  N     . PRO A 1 4150 ? 169.596 263.171 191.641 1.00 3.04  ? 4150 PRO A N     1 
ATOM   19847 C  CA    . PRO A 1 4150 ? 169.112 263.727 190.383 1.00 3.86  ? 4150 PRO A CA    1 
ATOM   19848 C  C     . PRO A 1 4150 ? 169.632 265.132 190.183 1.00 3.95  ? 4150 PRO A C     1 
ATOM   19849 O  O     . PRO A 1 4150 ? 169.850 265.882 191.156 1.00 4.15  ? 4150 PRO A O     1 
ATOM   19850 C  CB    . PRO A 1 4150 ? 167.587 263.703 190.548 1.00 3.35  ? 4150 PRO A CB    1 
ATOM   19851 C  CG    . PRO A 1 4150 ? 167.326 262.682 191.590 1.00 2.14  ? 4150 PRO A CG    1 
ATOM   19852 C  CD    . PRO A 1 4150 ? 168.502 262.719 192.514 1.00 2.44  ? 4150 PRO A CD    1 
ATOM   19853 N  N     . PRO A 1 4151 ? 169.867 265.536 188.933 1.00 6.99  ? 4151 PRO A N     1 
ATOM   19854 C  CA    . PRO A 1 4151 ? 170.517 266.834 188.683 1.00 6.79  ? 4151 PRO A CA    1 
ATOM   19855 C  C     . PRO A 1 4151 ? 169.765 268.037 189.235 1.00 9.58  ? 4151 PRO A C     1 
ATOM   19856 O  O     . PRO A 1 4151 ? 170.406 269.043 189.564 1.00 21.82 ? 4151 PRO A O     1 
ATOM   19857 C  CB    . PRO A 1 4151 ? 170.624 266.887 187.152 1.00 5.63  ? 4151 PRO A CB    1 
ATOM   19858 C  CG    . PRO A 1 4151 ? 169.775 265.763 186.639 1.00 7.11  ? 4151 PRO A CG    1 
ATOM   19859 C  CD    . PRO A 1 4151 ? 169.730 264.735 187.707 1.00 4.78  ? 4151 PRO A CD    1 
ATOM   19860 N  N     . GLY A 1 4152 ? 168.444 267.982 189.345 1.00 4.04  ? 4152 GLY A N     1 
ATOM   19861 C  CA    . GLY A 1 4152 ? 167.718 269.130 189.841 1.00 1.65  ? 4152 GLY A CA    1 
ATOM   19862 C  C     . GLY A 1 4152 ? 166.353 268.765 190.381 1.00 1.30  ? 4152 GLY A C     1 
ATOM   19863 O  O     . GLY A 1 4152 ? 165.994 267.591 190.481 1.00 3.79  ? 4152 GLY A O     1 
ATOM   19864 N  N     . VAL A 1 4153 ? 165.592 269.807 190.728 1.00 1.11  ? 4153 VAL A N     1 
ATOM   19865 C  CA    . VAL A 1 4153 ? 164.274 269.618 191.331 1.00 0.70  ? 4153 VAL A CA    1 
ATOM   19866 C  C     . VAL A 1 4153 ? 163.336 268.907 190.365 1.00 0.53  ? 4153 VAL A C     1 
ATOM   19867 O  O     . VAL A 1 4153 ? 162.610 267.984 190.751 1.00 0.73  ? 4153 VAL A O     1 
ATOM   19868 C  CB    . VAL A 1 4153 ? 163.696 270.975 191.783 1.00 0.77  ? 4153 VAL A CB    1 
ATOM   19869 C  CG1   . VAL A 1 4153 ? 162.225 270.837 192.148 1.00 0.52  ? 4153 VAL A CG1   1 
ATOM   19870 C  CG2   . VAL A 1 4153 ? 164.491 271.522 192.952 1.00 0.37  ? 4153 VAL A CG2   1 
ATOM   19871 N  N     . LYS A 1 4154 ? 163.330 269.328 189.099 1.00 1.29  ? 4154 LYS A N     1 
ATOM   19872 C  CA    . LYS A 1 4154 ? 162.483 268.682 188.102 1.00 1.21  ? 4154 LYS A CA    1 
ATOM   19873 C  C     . LYS A 1 4154 ? 162.848 267.212 187.941 1.00 0.79  ? 4154 LYS A C     1 
ATOM   19874 O  O     . LYS A 1 4154 ? 161.973 266.339 187.941 1.00 1.10  ? 4154 LYS A O     1 
ATOM   19875 C  CB    . LYS A 1 4154 ? 162.603 269.416 186.767 1.00 1.93  ? 4154 LYS A CB    1 
ATOM   19876 C  CG    . LYS A 1 4154 ? 161.789 268.809 185.644 1.00 2.33  ? 4154 LYS A CG    1 
ATOM   19877 C  CD    . LYS A 1 4154 ? 161.935 269.621 184.374 1.00 4.80  ? 4154 LYS A CD    1 
ATOM   19878 C  CE    . LYS A 1 4154 ? 160.987 269.138 183.294 1.00 6.93  ? 4154 LYS A CE    1 
ATOM   19879 N  NZ    . LYS A 1 4154 ? 161.023 270.027 182.107 1.00 12.41 ? 4154 LYS A NZ    1 
ATOM   19880 N  N     . ALA A 1 4155 ? 164.143 266.918 187.819 1.00 1.07  ? 4155 ALA A N     1 
ATOM   19881 C  CA    . ALA A 1 4155 ? 164.573 265.536 187.648 1.00 1.43  ? 4155 ALA A CA    1 
ATOM   19882 C  C     . ALA A 1 4155 ? 164.327 264.717 188.909 1.00 2.70  ? 4155 ALA A C     1 
ATOM   19883 O  O     . ALA A 1 4155 ? 163.998 263.528 188.826 1.00 5.24  ? 4155 ALA A O     1 
ATOM   19884 C  CB    . ALA A 1 4155 ? 166.049 265.494 187.256 1.00 2.80  ? 4155 ALA A CB    1 
ATOM   19885 N  N     . ASN A 1 4156 ? 164.483 265.335 190.082 1.00 1.42  ? 4156 ASN A N     1 
ATOM   19886 C  CA    . ASN A 1 4156 ? 164.228 264.631 191.334 1.00 0.71  ? 4156 ASN A CA    1 
ATOM   19887 C  C     . ASN A 1 4156 ? 162.773 264.201 191.440 1.00 0.79  ? 4156 ASN A C     1 
ATOM   19888 O  O     . ASN A 1 4156 ? 162.478 263.068 191.839 1.00 1.38  ? 4156 ASN A O     1 
ATOM   19889 C  CB    . ASN A 1 4156 ? 164.613 265.521 192.518 1.00 0.94  ? 4156 ASN A CB    1 
ATOM   19890 C  CG    . ASN A 1 4156 ? 164.748 264.751 193.816 1.00 0.63  ? 4156 ASN A CG    1 
ATOM   19891 O  OD1   . ASN A 1 4156 ? 163.808 264.106 194.274 1.00 0.60  ? 4156 ASN A OD1   1 
ATOM   19892 N  ND2   . ASN A 1 4156 ? 165.922 264.830 194.425 1.00 1.26  ? 4156 ASN A ND2   1 
ATOM   19893 N  N     . MET A 1 4157 ? 161.848 265.087 191.080 1.00 0.52  ? 4157 MET A N     1 
ATOM   19894 C  CA    . MET A 1 4157 ? 160.431 264.789 191.238 1.00 0.50  ? 4157 MET A CA    1 
ATOM   19895 C  C     . MET A 1 4157 ? 159.935 263.808 190.186 1.00 1.87  ? 4157 MET A C     1 
ATOM   19896 O  O     . MET A 1 4157 ? 159.043 263.002 190.471 1.00 2.59  ? 4157 MET A O     1 
ATOM   19897 C  CB    . MET A 1 4157 ? 159.626 266.086 191.194 1.00 0.42  ? 4157 MET A CB    1 
ATOM   19898 C  CG    . MET A 1 4157 ? 159.348 266.659 192.572 1.00 0.38  ? 4157 MET A CG    1 
ATOM   19899 S  SD    . MET A 1 4157 ? 158.653 268.314 192.539 1.00 1.69  ? 4157 MET A SD    1 
ATOM   19900 C  CE    . MET A 1 4157 ? 156.919 267.923 192.667 1.00 0.79  ? 4157 MET A CE    1 
ATOM   19901 N  N     . LEU A 1 4158 ? 160.494 263.857 188.976 1.00 3.40  ? 4158 LEU A N     1 
ATOM   19902 C  CA    . LEU A 1 4158 ? 160.128 262.882 187.955 1.00 2.17  ? 4158 LEU A CA    1 
ATOM   19903 C  C     . LEU A 1 4158 ? 160.598 261.484 188.337 1.00 3.82  ? 4158 LEU A C     1 
ATOM   19904 O  O     . LEU A 1 4158 ? 159.910 260.494 188.063 1.00 6.28  ? 4158 LEU A O     1 
ATOM   19905 C  CB    . LEU A 1 4158 ? 160.703 263.298 186.602 1.00 3.44  ? 4158 LEU A CB    1 
ATOM   19906 C  CG    . LEU A 1 4158 ? 159.981 264.458 185.917 1.00 1.88  ? 4158 LEU A CG    1 
ATOM   19907 C  CD1   . LEU A 1 4158 ? 160.743 264.930 184.693 1.00 2.61  ? 4158 LEU A CD1   1 
ATOM   19908 C  CD2   . LEU A 1 4158 ? 158.560 264.064 185.552 1.00 3.52  ? 4158 LEU A CD2   1 
ATOM   19909 N  N     . ARG A 1 4159 ? 161.772 261.384 188.964 1.00 2.25  ? 4159 ARG A N     1 
ATOM   19910 C  CA    . ARG A 1 4159 ? 162.250 260.093 189.442 1.00 2.39  ? 4159 ARG A CA    1 
ATOM   19911 C  C     . ARG A 1 4159 ? 161.347 259.550 190.542 1.00 3.60  ? 4159 ARG A C     1 
ATOM   19912 O  O     . ARG A 1 4159 ? 161.091 258.342 190.609 1.00 9.02  ? 4159 ARG A O     1 
ATOM   19913 C  CB    . ARG A 1 4159 ? 163.690 260.215 189.940 1.00 4.62  ? 4159 ARG A CB    1 
ATOM   19914 C  CG    . ARG A 1 4159 ? 164.296 258.900 190.397 1.00 8.01  ? 4159 ARG A CG    1 
ATOM   19915 C  CD    . ARG A 1 4159 ? 165.748 259.059 190.811 1.00 11.92 ? 4159 ARG A CD    1 
ATOM   19916 N  NE    . ARG A 1 4159 ? 166.608 259.379 189.676 1.00 16.13 ? 4159 ARG A NE    1 
ATOM   19917 C  CZ    . ARG A 1 4159 ? 167.882 259.729 189.776 1.00 11.36 ? 4159 ARG A CZ    1 
ATOM   19918 N  NH1   . ARG A 1 4159 ? 168.509 259.732 190.941 1.00 7.22  ? 4159 ARG A NH1   1 
ATOM   19919 N  NH2   . ARG A 1 4159 ? 168.548 260.073 188.677 1.00 6.22  ? 4159 ARG A NH2   1 
ATOM   19920 N  N     . THR A 1 4160 ? 160.861 260.430 191.419 1.00 4.01  ? 4160 THR A N     1 
ATOM   19921 C  CA    . THR A 1 4160 ? 159.985 259.997 192.504 1.00 3.61  ? 4160 THR A CA    1 
ATOM   19922 C  C     . THR A 1 4160 ? 158.663 259.458 191.972 1.00 5.18  ? 4160 THR A C     1 
ATOM   19923 O  O     . THR A 1 4160 ? 158.183 258.413 192.427 1.00 5.19  ? 4160 THR A O     1 
ATOM   19924 C  CB    . THR A 1 4160 ? 159.742 261.156 193.471 1.00 1.72  ? 4160 THR A CB    1 
ATOM   19925 O  OG1   . THR A 1 4160 ? 160.955 261.459 194.167 1.00 2.25  ? 4160 THR A OG1   1 
ATOM   19926 C  CG2   . THR A 1 4160 ? 158.658 260.805 194.476 1.00 1.04  ? 4160 THR A CG2   1 
ATOM   19927 N  N     . PHE A 1 4161 ? 158.059 260.155 191.008 1.00 7.05  ? 4161 PHE A N     1 
ATOM   19928 C  CA    . PHE A 1 4161 ? 156.751 259.736 190.519 1.00 6.69  ? 4161 PHE A CA    1 
ATOM   19929 C  C     . PHE A 1 4161 ? 156.839 258.467 189.682 1.00 8.30  ? 4161 PHE A C     1 
ATOM   19930 O  O     . PHE A 1 4161 ? 155.854 257.728 189.578 1.00 14.48 ? 4161 PHE A O     1 
ATOM   19931 C  CB    . PHE A 1 4161 ? 156.099 260.865 189.726 1.00 3.55  ? 4161 PHE A CB    1 
ATOM   19932 C  CG    . PHE A 1 4161 ? 155.309 261.815 190.575 1.00 2.28  ? 4161 PHE A CG    1 
ATOM   19933 C  CD1   . PHE A 1 4161 ? 154.042 261.476 191.015 1.00 4.68  ? 4161 PHE A CD1   1 
ATOM   19934 C  CD2   . PHE A 1 4161 ? 155.837 263.038 190.944 1.00 2.37  ? 4161 PHE A CD2   1 
ATOM   19935 C  CE1   . PHE A 1 4161 ? 153.311 262.346 191.803 1.00 6.97  ? 4161 PHE A CE1   1 
ATOM   19936 C  CE2   . PHE A 1 4161 ? 155.114 263.911 191.729 1.00 2.38  ? 4161 PHE A CE2   1 
ATOM   19937 C  CZ    . PHE A 1 4161 ? 153.849 263.565 192.160 1.00 4.96  ? 4161 PHE A CZ    1 
ATOM   19938 N  N     . SER A 1 4162 ? 157.997 258.197 189.080 1.00 6.57  ? 4162 SER A N     1 
ATOM   19939 C  CA    . SER A 1 4162 ? 158.176 256.942 188.361 1.00 6.58  ? 4162 SER A CA    1 
ATOM   19940 C  C     . SER A 1 4162 ? 158.409 255.770 189.306 1.00 11.57 ? 4162 SER A C     1 
ATOM   19941 O  O     . SER A 1 4162 ? 157.993 254.646 189.005 1.00 19.32 ? 4162 SER A O     1 
ATOM   19942 C  CB    . SER A 1 4162 ? 159.337 257.060 187.373 1.00 6.98  ? 4162 SER A CB    1 
ATOM   19943 O  OG    . SER A 1 4162 ? 160.570 257.231 188.048 1.00 13.26 ? 4162 SER A OG    1 
ATOM   19944 N  N     . SER A 1 4163 ? 159.060 256.010 190.445 1.00 9.59  ? 4163 SER A N     1 
ATOM   19945 C  CA    . SER A 1 4163 ? 159.377 254.927 191.369 1.00 7.22  ? 4163 SER A CA    1 
ATOM   19946 C  C     . SER A 1 4163 ? 158.158 254.447 192.148 1.00 9.06  ? 4163 SER A C     1 
ATOM   19947 O  O     . SER A 1 4163 ? 158.111 253.280 192.551 1.00 18.45 ? 4163 SER A O     1 
ATOM   19948 C  CB    . SER A 1 4163 ? 160.480 255.363 192.334 1.00 5.33  ? 4163 SER A CB    1 
ATOM   19949 O  OG    . SER A 1 4163 ? 160.082 256.487 193.097 1.00 13.82 ? 4163 SER A OG    1 
ATOM   19950 N  N     . ILE A 1 4164 ? 157.177 255.312 192.375 1.00 7.46  ? 4164 ILE A N     1 
ATOM   19951 C  CA    . ILE A 1 4164 ? 155.990 254.966 193.150 1.00 8.69  ? 4164 ILE A CA    1 
ATOM   19952 C  C     . ILE A 1 4164 ? 154.919 254.479 192.180 1.00 14.37 ? 4164 ILE A C     1 
ATOM   19953 O  O     . ILE A 1 4164 ? 154.594 255.201 191.223 1.00 18.38 ? 4164 ILE A O     1 
ATOM   19954 C  CB    . ILE A 1 4164 ? 155.483 256.154 193.975 1.00 11.50 ? 4164 ILE A CB    1 
ATOM   19955 C  CG1   . ILE A 1 4164 ? 156.611 256.733 194.826 1.00 6.71  ? 4164 ILE A CG1   1 
ATOM   19956 C  CG2   . ILE A 1 4164 ? 154.362 255.712 194.885 1.00 12.74 ? 4164 ILE A CG2   1 
ATOM   19957 C  CD1   . ILE A 1 4164 ? 156.249 258.027 195.507 1.00 5.15  ? 4164 ILE A CD1   1 
ATOM   19958 N  N     . PRO A 1 4165 ? 154.363 253.282 192.373 1.00 15.61 ? 4165 PRO A N     1 
ATOM   19959 C  CA    . PRO A 1 4165 ? 153.324 252.787 191.461 1.00 9.56  ? 4165 PRO A CA    1 
ATOM   19960 C  C     . PRO A 1 4165 ? 152.109 253.700 191.428 1.00 11.32 ? 4165 PRO A C     1 
ATOM   19961 O  O     . PRO A 1 4165 ? 151.749 254.327 192.423 1.00 14.55 ? 4165 PRO A O     1 
ATOM   19962 C  CB    . PRO A 1 4165 ? 152.969 251.417 192.046 1.00 10.84 ? 4165 PRO A CB    1 
ATOM   19963 C  CG    . PRO A 1 4165 ? 154.202 250.993 192.767 1.00 12.27 ? 4165 PRO A CG    1 
ATOM   19964 C  CD    . PRO A 1 4165 ? 154.791 252.252 193.334 1.00 12.14 ? 4165 PRO A CD    1 
ATOM   19965 N  N     . VAL A 1 4166 ? 151.468 253.759 190.257 1.00 12.49 ? 4166 VAL A N     1 
ATOM   19966 C  CA    . VAL A 1 4166 ? 150.335 254.661 190.062 1.00 14.41 ? 4166 VAL A CA    1 
ATOM   19967 C  C     . VAL A 1 4166 ? 149.181 254.291 190.986 1.00 17.98 ? 4166 VAL A C     1 
ATOM   19968 O  O     . VAL A 1 4166 ? 148.530 255.166 191.570 1.00 18.39 ? 4166 VAL A O     1 
ATOM   19969 C  CB    . VAL A 1 4166 ? 149.904 254.662 188.584 1.00 12.81 ? 4166 VAL A CB    1 
ATOM   19970 C  CG1   . VAL A 1 4166 ? 148.663 255.513 188.391 1.00 12.10 ? 4166 VAL A CG1   1 
ATOM   19971 C  CG2   . VAL A 1 4166 ? 151.034 255.168 187.709 1.00 10.32 ? 4166 VAL A CG2   1 
ATOM   19972 N  N     . SER A 1 4167 ? 148.902 252.992 191.126 1.00 13.41 ? 4167 SER A N     1 
ATOM   19973 C  CA    . SER A 1 4167 ? 147.812 252.558 191.996 1.00 10.84 ? 4167 SER A CA    1 
ATOM   19974 C  C     . SER A 1 4167 ? 148.040 252.980 193.440 1.00 16.76 ? 4167 SER A C     1 
ATOM   19975 O  O     . SER A 1 4167 ? 147.077 253.146 194.200 1.00 18.13 ? 4167 SER A O     1 
ATOM   19976 C  CB    . SER A 1 4167 ? 147.647 251.041 191.908 1.00 13.57 ? 4167 SER A CB    1 
ATOM   19977 O  OG    . SER A 1 4167 ? 148.890 250.388 192.081 1.00 23.95 ? 4167 SER A OG    1 
ATOM   19978 N  N     . ARG A 1 4168 ? 149.302 253.149 193.839 1.00 17.16 ? 4168 ARG A N     1 
ATOM   19979 C  CA    . ARG A 1 4168 ? 149.612 253.641 195.176 1.00 12.84 ? 4168 ARG A CA    1 
ATOM   19980 C  C     . ARG A 1 4168 ? 149.042 255.040 195.393 1.00 12.86 ? 4168 ARG A C     1 
ATOM   19981 O  O     . ARG A 1 4168 ? 148.403 255.303 196.419 1.00 17.41 ? 4168 ARG A O     1 
ATOM   19982 C  CB    . ARG A 1 4168 ? 151.128 253.640 195.374 1.00 11.70 ? 4168 ARG A CB    1 
ATOM   19983 C  CG    . ARG A 1 4168 ? 151.640 254.113 196.721 1.00 10.31 ? 4168 ARG A CG    1 
ATOM   19984 C  CD    . ARG A 1 4168 ? 151.307 253.150 197.834 1.00 10.08 ? 4168 ARG A CD    1 
ATOM   19985 N  NE    . ARG A 1 4168 ? 151.822 253.628 199.112 1.00 17.82 ? 4168 ARG A NE    1 
ATOM   19986 C  CZ    . ARG A 1 4168 ? 153.033 253.360 199.582 1.00 9.18  ? 4168 ARG A CZ    1 
ATOM   19987 N  NH1   . ARG A 1 4168 ? 153.900 252.641 198.887 1.00 6.48  ? 4168 ARG A NH1   1 
ATOM   19988 N  NH2   . ARG A 1 4168 ? 153.382 253.827 200.776 1.00 3.39  ? 4168 ARG A NH2   1 
ATOM   19989 N  N     . ILE A 1 4169 ? 149.254 255.946 194.435 1.00 11.72 ? 4169 ILE A N     1 
ATOM   19990 C  CA    . ILE A 1 4169 ? 148.777 257.320 194.579 1.00 12.11 ? 4169 ILE A CA    1 
ATOM   19991 C  C     . ILE A 1 4169 ? 147.264 257.393 194.410 1.00 12.52 ? 4169 ILE A C     1 
ATOM   19992 O  O     . ILE A 1 4169 ? 146.587 258.172 195.089 1.00 16.47 ? 4169 ILE A O     1 
ATOM   19993 C  CB    . ILE A 1 4169 ? 149.496 258.260 193.590 1.00 12.30 ? 4169 ILE A CB    1 
ATOM   19994 C  CG1   . ILE A 1 4169 ? 151.000 258.332 193.857 1.00 10.09 ? 4169 ILE A CG1   1 
ATOM   19995 C  CG2   . ILE A 1 4169 ? 148.906 259.650 193.630 1.00 13.42 ? 4169 ILE A CG2   1 
ATOM   19996 C  CD1   . ILE A 1 4169 ? 151.805 257.307 193.137 1.00 13.68 ? 4169 ILE A CD1   1 
ATOM   19997 N  N     . CYS A 1 4170 ? 146.706 256.574 193.516 1.00 17.55 ? 4170 CYS A N     1 
ATOM   19998 C  CA    . CYS A 1 4170 ? 145.328 256.730 193.068 1.00 15.20 ? 4170 CYS A CA    1 
ATOM   19999 C  C     . CYS A 1 4170 ? 144.330 255.948 193.916 1.00 19.12 ? 4170 CYS A C     1 
ATOM   20000 O  O     . CYS A 1 4170 ? 143.290 255.519 193.398 1.00 23.74 ? 4170 CYS A O     1 
ATOM   20001 C  CB    . CYS A 1 4170 ? 145.212 256.319 191.600 1.00 14.43 ? 4170 CYS A CB    1 
ATOM   20002 S  SG    . CYS A 1 4170 ? 146.244 257.285 190.475 1.00 43.43 ? 4170 CYS A SG    1 
ATOM   20003 N  N     . LYS A 1 4171 ? 144.610 255.750 195.203 1.00 20.80 ? 4171 LYS A N     1 
ATOM   20004 C  CA    . LYS A 1 4171 ? 143.675 255.048 196.069 1.00 15.75 ? 4171 LYS A CA    1 
ATOM   20005 C  C     . LYS A 1 4171 ? 142.446 255.919 196.341 1.00 21.93 ? 4171 LYS A C     1 
ATOM   20006 O  O     . LYS A 1 4171 ? 142.327 257.049 195.857 1.00 27.51 ? 4171 LYS A O     1 
ATOM   20007 C  CB    . LYS A 1 4171 ? 144.362 254.622 197.362 1.00 14.10 ? 4171 LYS A CB    1 
ATOM   20008 C  CG    . LYS A 1 4171 ? 144.746 253.149 197.383 1.00 7.12  ? 4171 LYS A CG    1 
ATOM   20009 C  CD    . LYS A 1 4171 ? 145.725 252.821 198.498 1.00 13.35 ? 4171 LYS A CD    1 
ATOM   20010 C  CE    . LYS A 1 4171 ? 145.180 253.197 199.865 1.00 15.37 ? 4171 LYS A CE    1 
ATOM   20011 N  NZ    . LYS A 1 4171 ? 143.983 252.399 200.243 1.00 10.97 ? 4171 LYS A NZ    1 
ATOM   20012 N  N     . SER A 1 4172 ? 141.518 255.376 197.133 1.00 21.01 ? 4172 SER A N     1 
ATOM   20013 C  CA    . SER A 1 4172 ? 140.170 255.915 197.307 1.00 17.70 ? 4172 SER A CA    1 
ATOM   20014 C  C     . SER A 1 4172 ? 140.144 257.388 197.715 1.00 23.45 ? 4172 SER A C     1 
ATOM   20015 O  O     . SER A 1 4172 ? 139.372 258.158 197.131 1.00 27.17 ? 4172 SER A O     1 
ATOM   20016 C  CB    . SER A 1 4172 ? 139.392 255.073 198.322 1.00 23.70 ? 4172 SER A CB    1 
ATOM   20017 O  OG    . SER A 1 4172 ? 139.324 253.716 197.918 1.00 31.43 ? 4172 SER A OG    1 
ATOM   20018 N  N     . PRO A 1 4173 ? 140.935 257.835 198.694 1.00 22.33 ? 4173 PRO A N     1 
ATOM   20019 C  CA    . PRO A 1 4173 ? 140.955 259.275 198.998 1.00 14.49 ? 4173 PRO A CA    1 
ATOM   20020 C  C     . PRO A 1 4173 ? 141.612 260.056 197.872 1.00 20.17 ? 4173 PRO A C     1 
ATOM   20021 O  O     . PRO A 1 4173 ? 142.791 259.865 197.567 1.00 21.90 ? 4173 PRO A O     1 
ATOM   20022 C  CB    . PRO A 1 4173 ? 141.763 259.355 200.299 1.00 10.31 ? 4173 PRO A CB    1 
ATOM   20023 C  CG    . PRO A 1 4173 ? 141.747 257.984 200.856 1.00 15.85 ? 4173 PRO A CG    1 
ATOM   20024 C  CD    . PRO A 1 4173 ? 141.732 257.078 199.675 1.00 17.09 ? 4173 PRO A CD    1 
ATOM   20025 N  N     . ASN A 1 4174 ? 140.833 260.945 197.249 1.00 17.75 ? 4174 ASN A N     1 
ATOM   20026 C  CA    . ASN A 1 4174 ? 141.346 261.734 196.136 1.00 17.66 ? 4174 ASN A CA    1 
ATOM   20027 C  C     . ASN A 1 4174 ? 142.439 262.699 196.566 1.00 15.38 ? 4174 ASN A C     1 
ATOM   20028 O  O     . ASN A 1 4174 ? 143.276 263.080 195.743 1.00 17.04 ? 4174 ASN A O     1 
ATOM   20029 C  CB    . ASN A 1 4174 ? 140.207 262.507 195.472 1.00 19.74 ? 4174 ASN A CB    1 
ATOM   20030 C  CG    . ASN A 1 4174 ? 139.266 261.608 194.702 1.00 19.81 ? 4174 ASN A CG    1 
ATOM   20031 O  OD1   . ASN A 1 4174 ? 139.491 260.403 194.597 1.00 22.37 ? 4174 ASN A OD1   1 
ATOM   20032 N  ND2   . ASN A 1 4174 ? 138.202 262.188 194.164 1.00 19.87 ? 4174 ASN A ND2   1 
ATOM   20033 N  N     . GLU A 1 4175 ? 142.450 263.098 197.836 1.00 13.13 ? 4175 GLU A N     1 
ATOM   20034 C  CA    . GLU A 1 4175 ? 143.456 264.011 198.357 1.00 11.67 ? 4175 GLU A CA    1 
ATOM   20035 C  C     . GLU A 1 4175 ? 144.815 263.350 198.534 1.00 10.94 ? 4175 GLU A C     1 
ATOM   20036 O  O     . GLU A 1 4175 ? 145.791 264.047 198.825 1.00 15.29 ? 4175 GLU A O     1 
ATOM   20037 C  CB    . GLU A 1 4175 ? 142.983 264.598 199.691 1.00 10.39 ? 4175 GLU A CB    1 
ATOM   20038 C  CG    . GLU A 1 4175 ? 141.805 265.564 199.574 1.00 12.07 ? 4175 GLU A CG    1 
ATOM   20039 C  CD    . GLU A 1 4175 ? 140.487 264.878 199.243 1.00 17.52 ? 4175 GLU A CD    1 
ATOM   20040 O  OE1   . GLU A 1 4175 ? 140.448 263.630 199.194 1.00 21.37 ? 4175 GLU A OE1   1 
ATOM   20041 O  OE2   . GLU A 1 4175 ? 139.487 265.590 199.025 1.00 18.95 ? 4175 GLU A OE2   1 
ATOM   20042 N  N     . ARG A 1 4176 ? 144.895 262.029 198.362 1.00 8.42  ? 4176 ARG A N     1 
ATOM   20043 C  CA    . ARG A 1 4176 ? 146.170 261.331 198.502 1.00 8.34  ? 4176 ARG A CA    1 
ATOM   20044 C  C     . ARG A 1 4176 ? 147.163 261.779 197.438 1.00 8.16  ? 4176 ARG A C     1 
ATOM   20045 O  O     . ARG A 1 4176 ? 148.372 261.829 197.690 1.00 9.18  ? 4176 ARG A O     1 
ATOM   20046 C  CB    . ARG A 1 4176 ? 145.940 259.821 198.428 1.00 8.75  ? 4176 ARG A CB    1 
ATOM   20047 C  CG    . ARG A 1 4176 ? 147.188 258.978 198.616 1.00 7.95  ? 4176 ARG A CG    1 
ATOM   20048 C  CD    . ARG A 1 4176 ? 146.865 257.496 198.549 1.00 9.34  ? 4176 ARG A CD    1 
ATOM   20049 N  NE    . ARG A 1 4176 ? 145.672 257.161 199.317 1.00 13.24 ? 4176 ARG A NE    1 
ATOM   20050 C  CZ    . ARG A 1 4176 ? 145.679 256.489 200.458 1.00 13.28 ? 4176 ARG A CZ    1 
ATOM   20051 N  NH1   . ARG A 1 4176 ? 146.806 256.065 201.003 1.00 11.78 ? 4176 ARG A NH1   1 
ATOM   20052 N  NH2   . ARG A 1 4176 ? 144.527 256.232 201.070 1.00 11.84 ? 4176 ARG A NH2   1 
ATOM   20053 N  N     . ALA A 1 4177 ? 146.670 262.112 196.242 1.00 12.25 ? 4177 ALA A N     1 
ATOM   20054 C  CA    . ALA A 1 4177 ? 147.560 262.514 195.157 1.00 7.85  ? 4177 ALA A CA    1 
ATOM   20055 C  C     . ALA A 1 4177 ? 148.302 263.801 195.487 1.00 3.47  ? 4177 ALA A C     1 
ATOM   20056 O  O     . ALA A 1 4177 ? 149.500 263.925 195.210 1.00 3.42  ? 4177 ALA A O     1 
ATOM   20057 C  CB    . ALA A 1 4177 ? 146.769 262.667 193.860 1.00 9.64  ? 4177 ALA A CB    1 
ATOM   20058 N  N     . ARG A 1 4178 ? 147.607 264.775 196.075 1.00 2.53  ? 4178 ARG A N     1 
ATOM   20059 C  CA    . ARG A 1 4178 ? 148.251 266.038 196.416 1.00 3.77  ? 4178 ARG A CA    1 
ATOM   20060 C  C     . ARG A 1 4178 ? 149.257 265.867 197.547 1.00 4.46  ? 4178 ARG A C     1 
ATOM   20061 O  O     . ARG A 1 4178 ? 150.282 266.558 197.571 1.00 3.53  ? 4178 ARG A O     1 
ATOM   20062 C  CB    . ARG A 1 4178 ? 147.193 267.076 196.782 1.00 5.75  ? 4178 ARG A CB    1 
ATOM   20063 C  CG    . ARG A 1 4178 ? 147.704 268.499 196.854 1.00 3.53  ? 4178 ARG A CG    1 
ATOM   20064 C  CD    . ARG A 1 4178 ? 146.549 269.480 196.870 1.00 8.92  ? 4178 ARG A CD    1 
ATOM   20065 N  NE    . ARG A 1 4178 ? 146.887 270.738 196.215 1.00 14.24 ? 4178 ARG A NE    1 
ATOM   20066 C  CZ    . ARG A 1 4178 ? 146.374 271.143 195.061 1.00 16.17 ? 4178 ARG A CZ    1 
ATOM   20067 N  NH1   . ARG A 1 4178 ? 145.502 270.404 194.396 1.00 12.41 ? 4178 ARG A NH1   1 
ATOM   20068 N  NH2   . ARG A 1 4178 ? 146.750 272.315 194.562 1.00 20.56 ? 4178 ARG A NH2   1 
ATOM   20069 N  N     . LEU A 1 4179 ? 148.984 264.960 198.489 1.00 3.56  ? 4179 LEU A N     1 
ATOM   20070 C  CA    . LEU A 1 4179 ? 149.948 264.678 199.548 1.00 2.63  ? 4179 LEU A CA    1 
ATOM   20071 C  C     . LEU A 1 4179 ? 151.236 264.103 198.978 1.00 2.08  ? 4179 LEU A C     1 
ATOM   20072 O  O     . LEU A 1 4179 ? 152.335 264.484 199.398 1.00 1.99  ? 4179 LEU A O     1 
ATOM   20073 C  CB    . LEU A 1 4179 ? 149.344 263.716 200.569 1.00 5.62  ? 4179 LEU A CB    1 
ATOM   20074 C  CG    . LEU A 1 4179 ? 148.100 264.184 201.323 1.00 4.07  ? 4179 LEU A CG    1 
ATOM   20075 C  CD1   . LEU A 1 4179 ? 147.651 263.118 202.300 1.00 4.79  ? 4179 LEU A CD1   1 
ATOM   20076 C  CD2   . LEU A 1 4179 ? 148.375 265.483 202.044 1.00 3.56  ? 4179 LEU A CD2   1 
ATOM   20077 N  N     . TYR A 1 4180 ? 151.123 263.181 198.021 1.00 3.73  ? 4180 TYR A N     1 
ATOM   20078 C  CA    . TYR A 1 4180 ? 152.312 262.613 197.394 1.00 2.17  ? 4180 TYR A CA    1 
ATOM   20079 C  C     . TYR A 1 4180 ? 153.087 263.672 196.623 1.00 1.48  ? 4180 TYR A C     1 
ATOM   20080 O  O     . TYR A 1 4180 ? 154.322 263.665 196.616 1.00 1.54  ? 4180 TYR A O     1 
ATOM   20081 C  CB    . TYR A 1 4180 ? 151.921 261.453 196.482 1.00 3.13  ? 4180 TYR A CB    1 
ATOM   20082 C  CG    . TYR A 1 4180 ? 151.874 260.122 197.190 1.00 3.96  ? 4180 TYR A CG    1 
ATOM   20083 C  CD1   . TYR A 1 4180 ? 150.785 259.769 197.975 1.00 5.34  ? 4180 TYR A CD1   1 
ATOM   20084 C  CD2   . TYR A 1 4180 ? 152.922 259.221 197.082 1.00 4.85  ? 4180 TYR A CD2   1 
ATOM   20085 C  CE1   . TYR A 1 4180 ? 150.742 258.553 198.629 1.00 6.85  ? 4180 TYR A CE1   1 
ATOM   20086 C  CE2   . TYR A 1 4180 ? 152.888 258.007 197.729 1.00 6.38  ? 4180 TYR A CE2   1 
ATOM   20087 C  CZ    . TYR A 1 4180 ? 151.795 257.678 198.501 1.00 6.87  ? 4180 TYR A CZ    1 
ATOM   20088 O  OH    . TYR A 1 4180 ? 151.761 256.466 199.146 1.00 8.99  ? 4180 TYR A OH    1 
ATOM   20089 N  N     . PHE A 1 4181 ? 152.376 264.586 195.959 1.00 1.98  ? 4181 PHE A N     1 
ATOM   20090 C  CA    . PHE A 1 4181 ? 153.051 265.686 195.280 1.00 1.16  ? 4181 PHE A CA    1 
ATOM   20091 C  C     . PHE A 1 4181 ? 153.813 266.555 196.272 1.00 0.60  ? 4181 PHE A C     1 
ATOM   20092 O  O     . PHE A 1 4181 ? 154.965 266.927 196.024 1.00 0.50  ? 4181 PHE A O     1 
ATOM   20093 C  CB    . PHE A 1 4181 ? 152.038 266.524 194.499 1.00 1.59  ? 4181 PHE A CB    1 
ATOM   20094 C  CG    . PHE A 1 4181 ? 152.628 267.758 193.887 1.00 2.86  ? 4181 PHE A CG    1 
ATOM   20095 C  CD1   . PHE A 1 4181 ? 153.176 267.720 192.619 1.00 3.10  ? 4181 PHE A CD1   1 
ATOM   20096 C  CD2   . PHE A 1 4181 ? 152.649 268.957 194.583 1.00 2.30  ? 4181 PHE A CD2   1 
ATOM   20097 C  CE1   . PHE A 1 4181 ? 153.722 268.847 192.056 1.00 4.05  ? 4181 PHE A CE1   1 
ATOM   20098 C  CE2   . PHE A 1 4181 ? 153.203 270.086 194.024 1.00 3.29  ? 4181 PHE A CE2   1 
ATOM   20099 C  CZ    . PHE A 1 4181 ? 153.740 270.031 192.761 1.00 3.51  ? 4181 PHE A CZ    1 
ATOM   20100 N  N     . LEU A 1 4182 ? 153.182 266.892 197.399 1.00 0.73  ? 4182 LEU A N     1 
ATOM   20101 C  CA    . LEU A 1 4182 ? 153.858 267.684 198.420 1.00 0.82  ? 4182 LEU A CA    1 
ATOM   20102 C  C     . LEU A 1 4182 ? 155.069 266.947 198.967 1.00 0.42  ? 4182 LEU A C     1 
ATOM   20103 O  O     . LEU A 1 4182 ? 156.123 267.548 199.198 1.00 0.44  ? 4182 LEU A O     1 
ATOM   20104 C  CB    . LEU A 1 4182 ? 152.886 268.022 199.547 1.00 1.07  ? 4182 LEU A CB    1 
ATOM   20105 C  CG    . LEU A 1 4182 ? 151.823 269.072 199.232 1.00 2.48  ? 4182 LEU A CG    1 
ATOM   20106 C  CD1   . LEU A 1 4182 ? 150.723 269.019 200.274 1.00 5.38  ? 4182 LEU A CD1   1 
ATOM   20107 C  CD2   . LEU A 1 4182 ? 152.445 270.457 199.157 1.00 2.17  ? 4182 LEU A CD2   1 
ATOM   20108 N  N     . LEU A 1 4183 ? 154.933 265.639 199.181 1.00 0.40  ? 4183 LEU A N     1 
ATOM   20109 C  CA    . LEU A 1 4183 ? 156.065 264.831 199.607 1.00 0.38  ? 4183 LEU A CA    1 
ATOM   20110 C  C     . LEU A 1 4183 ? 157.161 264.812 198.549 1.00 0.42  ? 4183 LEU A C     1 
ATOM   20111 O  O     . LEU A 1 4183 ? 158.349 264.907 198.876 1.00 0.50  ? 4183 LEU A O     1 
ATOM   20112 C  CB    . LEU A 1 4183 ? 155.592 263.415 199.926 1.00 1.35  ? 4183 LEU A CB    1 
ATOM   20113 C  CG    . LEU A 1 4183 ? 156.621 262.461 200.525 1.00 2.76  ? 4183 LEU A CG    1 
ATOM   20114 C  CD1   . LEU A 1 4183 ? 157.324 263.118 201.700 1.00 1.50  ? 4183 LEU A CD1   1 
ATOM   20115 C  CD2   . LEU A 1 4183 ? 155.938 261.176 200.945 1.00 5.33  ? 4183 LEU A CD2   1 
ATOM   20116 N  N     . ALA A 1 4184 ? 156.782 264.689 197.274 1.00 0.29  ? 4184 ALA A N     1 
ATOM   20117 C  CA    . ALA A 1 4184 ? 157.776 264.700 196.206 1.00 0.30  ? 4184 ALA A CA    1 
ATOM   20118 C  C     . ALA A 1 4184 ? 158.479 266.048 196.120 1.00 0.26  ? 4184 ALA A C     1 
ATOM   20119 O  O     . ALA A 1 4184 ? 159.704 266.109 195.966 1.00 0.29  ? 4184 ALA A O     1 
ATOM   20120 C  CB    . ALA A 1 4184 ? 157.121 264.350 194.869 1.00 0.60  ? 4184 ALA A CB    1 
ATOM   20121 N  N     . TRP A 1 4185 ? 157.720 267.141 196.216 1.00 0.24  ? 4185 TRP A N     1 
ATOM   20122 C  CA    . TRP A 1 4185 ? 158.335 268.462 196.224 1.00 0.30  ? 4185 TRP A CA    1 
ATOM   20123 C  C     . TRP A 1 4185 ? 159.234 268.640 197.440 1.00 0.45  ? 4185 TRP A C     1 
ATOM   20124 O  O     . TRP A 1 4185 ? 160.355 269.144 197.323 1.00 0.53  ? 4185 TRP A O     1 
ATOM   20125 C  CB    . TRP A 1 4185 ? 157.257 269.547 196.192 1.00 0.90  ? 4185 TRP A CB    1 
ATOM   20126 C  CG    . TRP A 1 4185 ? 157.811 270.927 196.360 1.00 0.93  ? 4185 TRP A CG    1 
ATOM   20127 C  CD1   . TRP A 1 4185 ? 157.940 271.623 197.525 1.00 0.66  ? 4185 TRP A CD1   1 
ATOM   20128 C  CD2   . TRP A 1 4185 ? 158.322 271.777 195.328 1.00 1.58  ? 4185 TRP A CD2   1 
ATOM   20129 N  NE1   . TRP A 1 4185 ? 158.498 272.854 197.283 1.00 1.19  ? 4185 TRP A NE1   1 
ATOM   20130 C  CE2   . TRP A 1 4185 ? 158.741 272.972 195.941 1.00 1.83  ? 4185 TRP A CE2   1 
ATOM   20131 C  CE3   . TRP A 1 4185 ? 158.463 271.643 193.943 1.00 0.91  ? 4185 TRP A CE3   1 
ATOM   20132 C  CZ2   . TRP A 1 4185 ? 159.291 274.028 195.219 1.00 1.53  ? 4185 TRP A CZ2   1 
ATOM   20133 C  CZ3   . TRP A 1 4185 ? 159.011 272.688 193.231 1.00 1.25  ? 4185 TRP A CZ3   1 
ATOM   20134 C  CH2   . TRP A 1 4185 ? 159.418 273.866 193.869 1.00 1.59  ? 4185 TRP A CH2   1 
ATOM   20135 N  N     . PHE A 1 4186 ? 158.758 268.225 198.616 1.00 0.27  ? 4186 PHE A N     1 
ATOM   20136 C  CA    . PHE A 1 4186 ? 159.564 268.349 199.822 1.00 0.12  ? 4186 PHE A CA    1 
ATOM   20137 C  C     . PHE A 1 4186 ? 160.833 267.515 199.717 1.00 0.09  ? 4186 PHE A C     1 
ATOM   20138 O  O     . PHE A 1 4186 ? 161.913 267.964 200.111 1.00 0.12  ? 4186 PHE A O     1 
ATOM   20139 C  CB    . PHE A 1 4186 ? 158.739 267.937 201.046 1.00 0.19  ? 4186 PHE A CB    1 
ATOM   20140 C  CG    . PHE A 1 4186 ? 159.548 267.775 202.300 1.00 0.10  ? 4186 PHE A CG    1 
ATOM   20141 C  CD1   . PHE A 1 4186 ? 159.823 268.864 203.107 1.00 0.14  ? 4186 PHE A CD1   1 
ATOM   20142 C  CD2   . PHE A 1 4186 ? 160.031 266.530 202.678 1.00 0.23  ? 4186 PHE A CD2   1 
ATOM   20143 C  CE1   . PHE A 1 4186 ? 160.568 268.717 204.259 1.00 0.19  ? 4186 PHE A CE1   1 
ATOM   20144 C  CE2   . PHE A 1 4186 ? 160.776 266.380 203.828 1.00 0.21  ? 4186 PHE A CE2   1 
ATOM   20145 C  CZ    . PHE A 1 4186 ? 161.042 267.475 204.618 1.00 0.17  ? 4186 PHE A CZ    1 
ATOM   20146 N  N     . HIS A 1 4187 ? 160.719 266.300 199.183 1.00 0.23  ? 4187 HIS A N     1 
ATOM   20147 C  CA    . HIS A 1 4187 ? 161.891 265.444 199.034 1.00 0.13  ? 4187 HIS A CA    1 
ATOM   20148 C  C     . HIS A 1 4187 ? 162.885 266.034 198.039 1.00 0.13  ? 4187 HIS A C     1 
ATOM   20149 O  O     . HIS A 1 4187 ? 164.100 265.909 198.222 1.00 0.16  ? 4187 HIS A O     1 
ATOM   20150 C  CB    . HIS A 1 4187 ? 161.459 264.042 198.616 1.00 0.14  ? 4187 HIS A CB    1 
ATOM   20151 C  CG    . HIS A 1 4187 ? 162.589 263.070 198.501 1.00 0.31  ? 4187 HIS A CG    1 
ATOM   20152 N  ND1   . HIS A 1 4187 ? 163.163 262.465 199.597 1.00 0.23  ? 4187 HIS A ND1   1 
ATOM   20153 C  CD2   . HIS A 1 4187 ? 163.252 262.595 197.420 1.00 0.22  ? 4187 HIS A CD2   1 
ATOM   20154 C  CE1   . HIS A 1 4187 ? 164.133 261.663 199.197 1.00 0.34  ? 4187 HIS A CE1   1 
ATOM   20155 N  NE2   . HIS A 1 4187 ? 164.206 261.722 197.879 1.00 0.28  ? 4187 HIS A NE2   1 
ATOM   20156 N  N     . ALA A 1 4188 ? 162.391 266.669 196.976 1.00 0.12  ? 4188 ALA A N     1 
ATOM   20157 C  CA    . ALA A 1 4188 ? 163.289 267.282 196.002 1.00 0.15  ? 4188 ALA A CA    1 
ATOM   20158 C  C     . ALA A 1 4188 ? 164.016 268.481 196.594 1.00 0.34  ? 4188 ALA A C     1 
ATOM   20159 O  O     . ALA A 1 4188 ? 165.228 268.628 196.407 1.00 0.67  ? 4188 ALA A O     1 
ATOM   20160 C  CB    . ALA A 1 4188 ? 162.514 267.688 194.750 1.00 0.23  ? 4188 ALA A CB    1 
ATOM   20161 N  N     . ILE A 1 4189 ? 163.295 269.344 197.313 1.00 0.27  ? 4189 ILE A N     1 
ATOM   20162 C  CA    . ILE A 1 4189 ? 163.910 270.538 197.886 1.00 0.39  ? 4189 ILE A CA    1 
ATOM   20163 C  C     . ILE A 1 4189 ? 164.971 270.155 198.908 1.00 0.46  ? 4189 ILE A C     1 
ATOM   20164 O  O     . ILE A 1 4189 ? 166.071 270.721 198.924 1.00 1.94  ? 4189 ILE A O     1 
ATOM   20165 C  CB    . ILE A 1 4189 ? 162.837 271.454 198.502 1.00 0.57  ? 4189 ILE A CB    1 
ATOM   20166 C  CG1   . ILE A 1 4189 ? 161.817 271.883 197.445 1.00 1.13  ? 4189 ILE A CG1   1 
ATOM   20167 C  CG2   . ILE A 1 4189 ? 163.476 272.667 199.159 1.00 0.59  ? 4189 ILE A CG2   1 
ATOM   20168 C  CD1   . ILE A 1 4189 ? 162.423 272.387 196.161 1.00 0.48  ? 4189 ILE A CD1   1 
ATOM   20169 N  N     . ILE A 1 4190 ? 164.662 269.185 199.770 1.00 0.26  ? 4190 ILE A N     1 
ATOM   20170 C  CA    . ILE A 1 4190 ? 165.604 268.787 200.812 1.00 0.46  ? 4190 ILE A CA    1 
ATOM   20171 C  C     . ILE A 1 4190 ? 166.858 268.172 200.200 1.00 0.42  ? 4190 ILE A C     1 
ATOM   20172 O  O     . ILE A 1 4190 ? 167.980 268.458 200.632 1.00 0.47  ? 4190 ILE A O     1 
ATOM   20173 C  CB    . ILE A 1 4190 ? 164.919 267.829 201.807 1.00 0.29  ? 4190 ILE A CB    1 
ATOM   20174 C  CG1   . ILE A 1 4190 ? 163.756 268.526 202.514 1.00 0.29  ? 4190 ILE A CG1   1 
ATOM   20175 C  CG2   . ILE A 1 4190 ? 165.908 267.303 202.823 1.00 0.38  ? 4190 ILE A CG2   1 
ATOM   20176 C  CD1   . ILE A 1 4190 ? 164.045 269.942 202.936 1.00 0.96  ? 4190 ILE A CD1   1 
ATOM   20177 N  N     . GLN A 1 4191 ? 166.689 267.320 199.187 1.00 0.73  ? 4191 GLN A N     1 
ATOM   20178 C  CA    . GLN A 1 4191 ? 167.844 266.678 198.565 1.00 1.10  ? 4191 GLN A CA    1 
ATOM   20179 C  C     . GLN A 1 4191 ? 168.686 267.674 197.779 1.00 0.85  ? 4191 GLN A C     1 
ATOM   20180 O  O     . GLN A 1 4191 ? 169.921 267.602 197.803 1.00 2.76  ? 4191 GLN A O     1 
ATOM   20181 C  CB    . GLN A 1 4191 ? 167.389 265.532 197.665 1.00 0.77  ? 4191 GLN A CB    1 
ATOM   20182 C  CG    . GLN A 1 4191 ? 166.968 264.283 198.418 1.00 0.82  ? 4191 GLN A CG    1 
ATOM   20183 C  CD    . GLN A 1 4191 ? 167.044 263.034 197.565 1.00 2.40  ? 4191 GLN A CD    1 
ATOM   20184 O  OE1   . GLN A 1 4191 ? 166.428 262.955 196.504 1.00 7.40  ? 4191 GLN A OE1   1 
ATOM   20185 N  NE2   . GLN A 1 4191 ? 167.797 262.047 198.029 1.00 1.86  ? 4191 GLN A NE2   1 
ATOM   20186 N  N     . GLU A 1 4192 ? 168.030 268.615 197.096 1.00 0.59  ? 4192 GLU A N     1 
ATOM   20187 C  CA    . GLU A 1 4192 ? 168.769 269.585 196.240 1.00 0.88  ? 4192 GLU A CA    1 
ATOM   20188 C  C     . GLU A 1 4192 ? 169.602 270.543 197.112 1.00 1.75  ? 4192 GLU A C     1 
ATOM   20189 O  O     . GLU A 1 4192 ? 170.642 271.032 196.619 1.00 5.62  ? 4192 GLU A O     1 
ATOM   20190 C  CB    . GLU A 1 4192 ? 167.794 270.339 195.335 1.00 0.81  ? 4192 GLU A CB    1 
ATOM   20191 C  CG    . GLU A 1 4192 ? 167.356 269.533 194.116 1.00 0.84  ? 4192 GLU A CG    1 
ATOM   20192 C  CD    . GLU A 1 4192 ? 168.474 269.303 193.115 1.00 10.12 ? 4192 GLU A CD    1 
ATOM   20193 O  OE1   . GLU A 1 4192 ? 169.015 270.302 192.600 1.00 14.74 ? 4192 GLU A OE1   1 
ATOM   20194 O  OE2   . GLU A 1 4192 ? 168.805 268.129 192.851 1.00 11.24 ? 4192 GLU A OE2   1 
ATOM   20195 N  N     . ARG A 1 4193 ? 169.162 270.801 198.346 1.00 1.03  ? 4193 ARG A N     1 
ATOM   20196 C  CA    . ARG A 1 4193 ? 169.894 271.723 199.255 1.00 0.85  ? 4193 ARG A CA    1 
ATOM   20197 C  C     . ARG A 1 4193 ? 171.242 271.096 199.645 1.00 1.39  ? 4193 ARG A C     1 
ATOM   20198 O  O     . ARG A 1 4193 ? 172.167 271.857 200.000 1.00 3.98  ? 4193 ARG A O     1 
ATOM   20199 C  CB    . ARG A 1 4193 ? 169.043 272.066 200.483 1.00 0.75  ? 4193 ARG A CB    1 
ATOM   20200 C  CG    . ARG A 1 4193 ? 167.838 272.941 200.169 1.00 0.97  ? 4193 ARG A CG    1 
ATOM   20201 C  CD    . ARG A 1 4193 ? 167.157 273.451 201.428 1.00 1.47  ? 4193 ARG A CD    1 
ATOM   20202 N  NE    . ARG A 1 4193 ? 168.086 274.209 202.273 1.00 1.11  ? 4193 ARG A NE    1 
ATOM   20203 C  CZ    . ARG A 1 4193 ? 167.949 275.490 202.587 1.00 0.77  ? 4193 ARG A CZ    1 
ATOM   20204 N  NH1   . ARG A 1 4193 ? 166.928 276.183 202.114 1.00 0.70  ? 4193 ARG A NH1   1 
ATOM   20205 N  NH2   . ARG A 1 4193 ? 168.835 276.076 203.371 1.00 1.09  ? 4193 ARG A NH2   1 
ATOM   20206 N  N     . LEU A 1 4194 ? 171.351 269.766 199.569 1.00 2.15  ? 4194 LEU A N     1 
ATOM   20207 C  CA    . LEU A 1 4194 ? 172.626 269.072 199.887 1.00 1.87  ? 4194 LEU A CA    1 
ATOM   20208 C  C     . LEU A 1 4194 ? 173.709 269.514 198.889 1.00 2.94  ? 4194 LEU A C     1 
ATOM   20209 O  O     . LEU A 1 4194 ? 174.896 269.544 199.279 1.00 3.91  ? 4194 LEU A O     1 
ATOM   20210 C  CB    . LEU A 1 4194 ? 172.410 267.559 199.862 1.00 1.93  ? 4194 LEU A CB    1 
ATOM   20211 C  CG    . LEU A 1 4194 ? 171.463 267.004 200.932 1.00 3.56  ? 4194 LEU A CG    1 
ATOM   20212 C  CD1   . LEU A 1 4194 ? 171.151 265.539 200.679 1.00 2.48  ? 4194 LEU A CD1   1 
ATOM   20213 C  CD2   . LEU A 1 4194 ? 172.048 267.194 202.320 1.00 1.47  ? 4194 LEU A CD2   1 
ATOM   20214 N  N     . ARG A 1 4195 ? 173.311 269.850 197.658 1.00 2.88  ? 4195 ARG A N     1 
ATOM   20215 C  CA    . ARG A 1 4195 ? 174.283 270.326 196.638 1.00 2.92  ? 4195 ARG A CA    1 
ATOM   20216 C  C     . ARG A 1 4195 ? 175.008 271.558 197.198 1.00 4.49  ? 4195 ARG A C     1 
ATOM   20217 O  O     . ARG A 1 4195 ? 176.225 271.690 196.952 1.00 6.99  ? 4195 ARG A O     1 
ATOM   20218 C  CB    . ARG A 1 4195 ? 173.562 270.612 195.314 1.00 3.32  ? 4195 ARG A CB    1 
ATOM   20219 C  CG    . ARG A 1 4195 ? 172.958 269.366 194.685 1.00 8.06  ? 4195 ARG A CG    1 
ATOM   20220 C  CD    . ARG A 1 4195 ? 172.124 269.676 193.451 1.00 6.82  ? 4195 ARG A CD    1 
ATOM   20221 N  NE    . ARG A 1 4195 ? 171.711 268.454 192.750 1.00 18.64 ? 4195 ARG A NE    1 
ATOM   20222 C  CZ    . ARG A 1 4195 ? 172.556 267.582 192.212 1.00 10.31 ? 4195 ARG A CZ    1 
ATOM   20223 N  NH1   . ARG A 1 4195 ? 173.765 267.970 191.851 1.00 6.56  ? 4195 ARG A NH1   1 
ATOM   20224 N  NH2   . ARG A 1 4195 ? 172.185 266.327 192.033 1.00 8.84  ? 4195 ARG A NH2   1 
ATOM   20225 N  N     . TYR A 1 4196 ? 174.288 272.424 197.916 1.00 3.63  ? 4196 TYR A N     1 
ATOM   20226 C  CA    . TYR A 1 4196 ? 174.940 273.587 198.577 1.00 4.04  ? 4196 TYR A CA    1 
ATOM   20227 C  C     . TYR A 1 4196 ? 175.491 273.077 199.902 1.00 7.21  ? 4196 TYR A C     1 
ATOM   20228 O  O     . TYR A 1 4196 ? 175.010 273.511 200.970 1.00 4.89  ? 4196 TYR A O     1 
ATOM   20229 C  CB    . TYR A 1 4196 ? 173.899 274.711 198.626 1.00 3.77  ? 4196 TYR A CB    1 
ATOM   20230 C  CG    . TYR A 1 4196 ? 173.349 275.034 197.243 1.00 5.05  ? 4196 TYR A CG    1 
ATOM   20231 C  CD1   . TYR A 1 4196 ? 173.956 275.987 196.436 1.00 5.10  ? 4196 TYR A CD1   1 
ATOM   20232 C  CD2   . TYR A 1 4196 ? 172.243 274.363 196.735 1.00 3.89  ? 4196 TYR A CD2   1 
ATOM   20233 C  CE1   . TYR A 1 4196 ? 173.468 276.277 195.173 1.00 8.03  ? 4196 TYR A CE1   1 
ATOM   20234 C  CE2   . TYR A 1 4196 ? 171.747 274.644 195.473 1.00 4.55  ? 4196 TYR A CE2   1 
ATOM   20235 C  CZ    . TYR A 1 4196 ? 172.362 275.603 194.689 1.00 5.86  ? 4196 TYR A CZ    1 
ATOM   20236 O  OH    . TYR A 1 4196 ? 171.877 275.887 193.445 1.00 7.12  ? 4196 TYR A OH    1 
ATOM   20237 N  N     . ALA A 1 4197 ? 176.483 272.184 199.831 1.00 16.48 ? 4197 ALA A N     1 
ATOM   20238 C  CA    . ALA A 1 4197 ? 177.057 271.540 201.041 1.00 8.60  ? 4197 ALA A CA    1 
ATOM   20239 C  C     . ALA A 1 4197 ? 176.781 272.337 202.319 1.00 7.10  ? 4197 ALA A C     1 
ATOM   20240 O  O     . ALA A 1 4197 ? 176.024 271.811 203.158 1.00 8.44  ? 4197 ALA A O     1 
ATOM   20241 C  CB    . ALA A 1 4197 ? 178.540 271.289 200.839 1.00 8.34  ? 4197 ALA A CB    1 
ATOM   20242 N  N     . PRO A 1 4198 ? 177.347 273.546 202.534 1.00 30.00 ? 4198 PRO A N     1 
ATOM   20243 C  CA    . PRO A 1 4198 ? 177.178 274.240 203.811 1.00 30.00 ? 4198 PRO A CA    1 
ATOM   20244 C  C     . PRO A 1 4198 ? 175.894 275.045 204.030 1.00 30.00 ? 4198 PRO A C     1 
ATOM   20245 O  O     . PRO A 1 4198 ? 175.324 274.951 205.134 1.00 30.00 ? 4198 PRO A O     1 
ATOM   20246 C  CB    . PRO A 1 4198 ? 178.429 275.144 203.796 1.00 30.00 ? 4198 PRO A CB    1 
ATOM   20247 C  CG    . PRO A 1 4198 ? 178.575 275.533 202.345 1.00 30.00 ? 4198 PRO A CG    1 
ATOM   20248 C  CD    . PRO A 1 4198 ? 178.138 274.300 201.570 1.00 30.00 ? 4198 PRO A CD    1 
ATOM   20249 N  N     . LEU A 1 4199 ? 175.457 275.816 203.031 1.00 2.46  ? 4199 LEU A N     1 
ATOM   20250 C  CA    . LEU A 1 4199 ? 174.276 276.704 203.213 1.00 2.37  ? 4199 LEU A CA    1 
ATOM   20251 C  C     . LEU A 1 4199 ? 172.971 275.888 203.262 1.00 3.82  ? 4199 LEU A C     1 
ATOM   20252 O  O     . LEU A 1 4199 ? 172.167 276.126 204.186 1.00 5.74  ? 4199 LEU A O     1 
ATOM   20253 C  CB    . LEU A 1 4199 ? 174.255 277.738 202.087 1.00 3.87  ? 4199 LEU A CB    1 
ATOM   20254 C  CG    . LEU A 1 4199 ? 173.575 279.070 202.416 1.00 3.83  ? 4199 LEU A CG    1 
ATOM   20255 C  CD1   . LEU A 1 4199 ? 174.267 279.735 203.590 1.00 4.08  ? 4199 LEU A CD1   1 
ATOM   20256 C  CD2   . LEU A 1 4199 ? 173.579 279.987 201.206 1.00 2.85  ? 4199 LEU A CD2   1 
ATOM   20257 N  N     . GLY A 1 4200 ? 172.767 274.974 202.307 1.00 2.34  ? 4200 GLY A N     1 
ATOM   20258 C  CA    . GLY A 1 4200 ? 171.515 274.193 202.261 1.00 1.50  ? 4200 GLY A CA    1 
ATOM   20259 C  C     . GLY A 1 4200 ? 171.319 273.436 203.555 1.00 1.34  ? 4200 GLY A C     1 
ATOM   20260 O  O     . GLY A 1 4200 ? 170.189 273.455 204.084 1.00 1.16  ? 4200 GLY A O     1 
ATOM   20261 N  N     . TRP A 1 4201 ? 172.375 272.786 204.049 1.00 1.55  ? 4201 TRP A N     1 
ATOM   20262 C  CA    . TRP A 1 4201 ? 172.322 272.082 205.351 1.00 1.07  ? 4201 TRP A CA    1 
ATOM   20263 C  C     . TRP A 1 4201 ? 173.711 272.169 205.977 1.00 1.71  ? 4201 TRP A C     1 
ATOM   20264 O  O     . TRP A 1 4201 ? 174.699 272.157 205.221 1.00 4.86  ? 4201 TRP A O     1 
ATOM   20265 C  CB    . TRP A 1 4201 ? 171.897 270.618 205.170 1.00 1.40  ? 4201 TRP A CB    1 
ATOM   20266 C  CG    . TRP A 1 4201 ? 170.513 270.431 204.607 1.00 0.59  ? 4201 TRP A CG    1 
ATOM   20267 C  CD1   . TRP A 1 4201 ? 170.173 270.241 203.300 1.00 0.61  ? 4201 TRP A CD1   1 
ATOM   20268 C  CD2   . TRP A 1 4201 ? 169.274 270.427 205.349 1.00 0.76  ? 4201 TRP A CD2   1 
ATOM   20269 N  NE1   . TRP A 1 4201 ? 168.816 270.109 203.177 1.00 0.41  ? 4201 TRP A NE1   1 
ATOM   20270 C  CE2   . TRP A 1 4201 ? 168.237 270.221 204.414 1.00 0.56  ? 4201 TRP A CE2   1 
ATOM   20271 C  CE3   . TRP A 1 4201 ? 168.945 270.575 206.701 1.00 0.61  ? 4201 TRP A CE3   1 
ATOM   20272 C  CZ2   . TRP A 1 4201 ? 166.899 270.162 204.792 1.00 0.44  ? 4201 TRP A CZ2   1 
ATOM   20273 C  CZ3   . TRP A 1 4201 ? 167.621 270.516 207.072 1.00 0.66  ? 4201 TRP A CZ3   1 
ATOM   20274 C  CH2   . TRP A 1 4201 ? 166.613 270.310 206.129 1.00 0.50  ? 4201 TRP A CH2   1 
ATOM   20275 N  N     . SER A 1 4202 ? 173.790 272.265 207.304 1.00 2.65  ? 4202 SER A N     1 
ATOM   20276 C  CA    . SER A 1 4202 ? 175.108 272.398 207.974 1.00 2.54  ? 4202 SER A CA    1 
ATOM   20277 C  C     . SER A 1 4202 ? 175.952 271.158 207.652 1.00 1.48  ? 4202 SER A C     1 
ATOM   20278 O  O     . SER A 1 4202 ? 177.194 271.280 207.619 1.00 7.15  ? 4202 SER A O     1 
ATOM   20279 C  CB    . SER A 1 4202 ? 174.957 272.587 209.460 1.00 2.84  ? 4202 SER A CB    1 
ATOM   20280 O  OG    . SER A 1 4202 ? 174.620 271.364 210.100 1.00 5.05  ? 4202 SER A OG    1 
ATOM   20281 N  N     . LYS A 1 4203 ? 175.299 270.017 207.416 1.00 3.30  ? 4203 LYS A N     1 
ATOM   20282 C  CA    . LYS A 1 4203 ? 176.041 268.754 207.170 1.00 2.67  ? 4203 LYS A CA    1 
ATOM   20283 C  C     . LYS A 1 4203 ? 175.490 268.050 205.923 1.00 2.78  ? 4203 LYS A C     1 
ATOM   20284 O  O     . LYS A 1 4203 ? 174.382 268.416 205.477 1.00 4.17  ? 4203 LYS A O     1 
ATOM   20285 C  CB    . LYS A 1 4203 ? 175.914 267.839 208.394 1.00 3.70  ? 4203 LYS A CB    1 
ATOM   20286 C  CG    . LYS A 1 4203 ? 176.088 268.543 209.732 1.00 8.54  ? 4203 LYS A CG    1 
ATOM   20287 C  CD    . LYS A 1 4203 ? 176.066 267.603 210.929 1.00 7.88  ? 4203 LYS A CD    1 
ATOM   20288 C  CE    . LYS A 1 4203 ? 177.177 266.603 210.871 1.00 12.22 ? 4203 LYS A CE    1 
ATOM   20289 N  NZ    . LYS A 1 4203 ? 177.228 265.777 212.079 1.00 20.16 ? 4203 LYS A NZ    1 
ATOM   20290 N  N     . LYS A 1 4204 ? 176.236 267.079 205.391 1.00 4.11  ? 4204 LYS A N     1 
ATOM   20291 C  CA    . LYS A 1 4204 ? 175.797 266.321 204.221 1.00 2.85  ? 4204 LYS A CA    1 
ATOM   20292 C  C     . LYS A 1 4204 ? 174.993 265.102 204.680 1.00 4.14  ? 4204 LYS A C     1 
ATOM   20293 O  O     . LYS A 1 4204 ? 175.474 263.970 204.723 1.00 14.52 ? 4204 LYS A O     1 
ATOM   20294 C  CB    . LYS A 1 4204 ? 176.996 265.918 203.374 1.00 4.95  ? 4204 LYS A CB    1 
ATOM   20295 C  CG    . LYS A 1 4204 ? 176.643 265.171 202.104 1.00 9.70  ? 4204 LYS A CG    1 
ATOM   20296 C  CD    . LYS A 1 4204 ? 175.813 266.040 201.187 1.00 11.87 ? 4204 LYS A CD    1 
ATOM   20297 C  CE    . LYS A 1 4204 ? 176.632 267.218 200.705 1.00 9.20  ? 4204 LYS A CE    1 
ATOM   20298 N  NZ    . LYS A 1 4204 ? 177.729 266.781 199.798 1.00 18.69 ? 4204 LYS A NZ    1 
ATOM   20299 N  N     . TYR A 1 4205 ? 173.738 265.359 205.044 1.00 3.02  ? 4205 TYR A N     1 
ATOM   20300 C  CA    . TYR A 1 4205 ? 172.866 264.276 205.475 1.00 3.92  ? 4205 TYR A CA    1 
ATOM   20301 C  C     . TYR A 1 4205 ? 172.515 263.368 204.304 1.00 3.36  ? 4205 TYR A C     1 
ATOM   20302 O  O     . TYR A 1 4205 ? 172.476 263.790 203.146 1.00 4.16  ? 4205 TYR A O     1 
ATOM   20303 C  CB    . TYR A 1 4205 ? 171.583 264.816 206.101 1.00 1.51  ? 4205 TYR A CB    1 
ATOM   20304 C  CG    . TYR A 1 4205 ? 171.796 265.754 207.258 1.00 1.60  ? 4205 TYR A CG    1 
ATOM   20305 C  CD1   . TYR A 1 4205 ? 172.155 265.270 208.510 1.00 1.21  ? 4205 TYR A CD1   1 
ATOM   20306 C  CD2   . TYR A 1 4205 ? 171.606 267.118 207.109 1.00 1.37  ? 4205 TYR A CD2   1 
ATOM   20307 C  CE1   . TYR A 1 4205 ? 172.343 266.124 209.572 1.00 1.56  ? 4205 TYR A CE1   1 
ATOM   20308 C  CE2   . TYR A 1 4205 ? 171.787 267.977 208.166 1.00 1.69  ? 4205 TYR A CE2   1 
ATOM   20309 C  CZ    . TYR A 1 4205 ? 172.156 267.476 209.396 1.00 4.41  ? 4205 TYR A CZ    1 
ATOM   20310 O  OH    . TYR A 1 4205 ? 172.339 268.334 210.454 1.00 5.77  ? 4205 TYR A OH    1 
ATOM   20311 N  N     . GLU A 1 4206 ? 172.258 262.103 204.621 1.00 3.34  ? 4206 GLU A N     1 
ATOM   20312 C  CA    . GLU A 1 4206 ? 171.902 261.113 203.608 1.00 3.93  ? 4206 GLU A CA    1 
ATOM   20313 C  C     . GLU A 1 4206 ? 170.382 260.968 203.502 1.00 2.05  ? 4206 GLU A C     1 
ATOM   20314 O  O     . GLU A 1 4206 ? 169.814 259.898 203.706 1.00 5.07  ? 4206 GLU A O     1 
ATOM   20315 C  CB    . GLU A 1 4206 ? 172.569 259.779 203.918 1.00 2.88  ? 4206 GLU A CB    1 
ATOM   20316 C  CG    . GLU A 1 4206 ? 174.083 259.811 203.839 1.00 3.40  ? 4206 GLU A CG    1 
ATOM   20317 C  CD    . GLU A 1 4206 ? 174.687 258.435 203.634 1.00 14.86 ? 4206 GLU A CD    1 
ATOM   20318 O  OE1   . GLU A 1 4206 ? 174.304 257.501 204.369 1.00 23.29 ? 4206 GLU A OE1   1 
ATOM   20319 O  OE2   . GLU A 1 4206 ? 175.546 258.289 202.739 1.00 15.05 ? 4206 GLU A OE2   1 
ATOM   20320 N  N     . PHE A 1 4207 ? 169.719 262.077 203.183 1.00 1.68  ? 4207 PHE A N     1 
ATOM   20321 C  CA    . PHE A 1 4207 ? 168.315 262.005 202.803 1.00 1.60  ? 4207 PHE A CA    1 
ATOM   20322 C  C     . PHE A 1 4207 ? 168.204 261.225 201.499 1.00 3.07  ? 4207 PHE A C     1 
ATOM   20323 O  O     . PHE A 1 4207 ? 168.774 261.626 200.480 1.00 8.97  ? 4207 PHE A O     1 
ATOM   20324 C  CB    . PHE A 1 4207 ? 167.708 263.397 202.639 1.00 1.06  ? 4207 PHE A CB    1 
ATOM   20325 C  CG    . PHE A 1 4207 ? 167.867 264.288 203.835 1.00 0.98  ? 4207 PHE A CG    1 
ATOM   20326 C  CD1   . PHE A 1 4207 ? 167.206 264.008 205.019 1.00 0.76  ? 4207 PHE A CD1   1 
ATOM   20327 C  CD2   . PHE A 1 4207 ? 168.634 265.439 203.761 1.00 1.28  ? 4207 PHE A CD2   1 
ATOM   20328 C  CE1   . PHE A 1 4207 ? 167.334 264.839 206.113 1.00 0.59  ? 4207 PHE A CE1   1 
ATOM   20329 C  CE2   . PHE A 1 4207 ? 168.761 266.278 204.849 1.00 0.67  ? 4207 PHE A CE2   1 
ATOM   20330 C  CZ    . PHE A 1 4207 ? 168.113 265.975 206.029 1.00 0.78  ? 4207 PHE A CZ    1 
ATOM   20331 N  N     . GLY A 1 4208 ? 167.478 260.114 201.527 1.00 1.80  ? 4208 GLY A N     1 
ATOM   20332 C  CA    . GLY A 1 4208 ? 167.442 259.243 200.373 1.00 1.18  ? 4208 GLY A CA    1 
ATOM   20333 C  C     . GLY A 1 4208 ? 166.126 258.536 200.141 1.00 1.23  ? 4208 GLY A C     1 
ATOM   20334 O  O     . GLY A 1 4208 ? 165.077 258.974 200.620 1.00 2.57  ? 4208 GLY A O     1 
ATOM   20335 N  N     . GLU A 1 4209 ? 166.181 257.430 199.397 1.00 2.16  ? 4209 GLU A N     1 
ATOM   20336 C  CA    . GLU A 1 4209 ? 164.969 256.715 199.019 1.00 3.09  ? 4209 GLU A CA    1 
ATOM   20337 C  C     . GLU A 1 4209 ? 164.286 256.100 200.235 1.00 2.58  ? 4209 GLU A C     1 
ATOM   20338 O  O     . GLU A 1 4209 ? 163.051 256.044 200.298 1.00 1.73  ? 4209 GLU A O     1 
ATOM   20339 C  CB    . GLU A 1 4209 ? 165.309 255.644 197.980 1.00 3.10  ? 4209 GLU A CB    1 
ATOM   20340 C  CG    . GLU A 1 4209 ? 164.279 254.529 197.797 1.00 5.99  ? 4209 GLU A CG    1 
ATOM   20341 C  CD    . GLU A 1 4209 ? 162.979 254.996 197.146 1.00 14.81 ? 4209 GLU A CD    1 
ATOM   20342 O  OE1   . GLU A 1 4209 ? 162.767 256.216 196.987 1.00 5.10  ? 4209 GLU A OE1   1 
ATOM   20343 O  OE2   . GLU A 1 4209 ? 162.166 254.125 196.772 1.00 23.81 ? 4209 GLU A OE2   1 
ATOM   20344 N  N     . SER A 1 4210 ? 165.070 255.633 201.210 1.00 2.01  ? 4210 SER A N     1 
ATOM   20345 C  CA    . SER A 1 4210 ? 164.485 255.039 202.407 1.00 1.75  ? 4210 SER A CA    1 
ATOM   20346 C  C     . SER A 1 4210 ? 163.653 256.054 203.176 1.00 1.61  ? 4210 SER A C     1 
ATOM   20347 O  O     . SER A 1 4210 ? 162.571 255.729 203.679 1.00 2.58  ? 4210 SER A O     1 
ATOM   20348 C  CB    . SER A 1 4210 ? 165.585 254.457 203.298 1.00 2.17  ? 4210 SER A CB    1 
ATOM   20349 O  OG    . SER A 1 4210 ? 166.433 255.476 203.791 1.00 4.35  ? 4210 SER A OG    1 
ATOM   20350 N  N     . ASP A 1 4211 ? 164.141 257.291 203.283 1.00 1.48  ? 4211 ASP A N     1 
ATOM   20351 C  CA    . ASP A 1 4211 ? 163.356 258.343 203.918 1.00 1.40  ? 4211 ASP A CA    1 
ATOM   20352 C  C     . ASP A 1 4211 ? 162.078 258.619 203.141 1.00 1.68  ? 4211 ASP A C     1 
ATOM   20353 O  O     . ASP A 1 4211 ? 161.010 258.805 203.735 1.00 4.55  ? 4211 ASP A O     1 
ATOM   20354 C  CB    . ASP A 1 4211 ? 164.191 259.616 204.048 1.00 1.39  ? 4211 ASP A CB    1 
ATOM   20355 C  CG    . ASP A 1 4211 ? 165.285 259.494 205.088 1.00 4.31  ? 4211 ASP A CG    1 
ATOM   20356 O  OD1   . ASP A 1 4211 ? 165.380 258.432 205.736 1.00 7.84  ? 4211 ASP A OD1   1 
ATOM   20357 O  OD2   . ASP A 1 4211 ? 166.051 260.461 205.258 1.00 9.31  ? 4211 ASP A OD2   1 
ATOM   20358 N  N     . LEU A 1 4212 ? 162.164 258.646 201.811 1.00 1.45  ? 4212 LEU A N     1 
ATOM   20359 C  CA    . LEU A 1 4212 ? 160.984 258.900 200.993 1.00 0.71  ? 4212 LEU A CA    1 
ATOM   20360 C  C     . LEU A 1 4212 ? 159.965 257.772 201.115 1.00 0.89  ? 4212 LEU A C     1 
ATOM   20361 O  O     . LEU A 1 4212 ? 158.761 258.027 201.230 1.00 0.96  ? 4212 LEU A O     1 
ATOM   20362 C  CB    . LEU A 1 4212 ? 161.397 259.110 199.538 1.00 0.58  ? 4212 LEU A CB    1 
ATOM   20363 C  CG    . LEU A 1 4212 ? 160.286 259.345 198.514 1.00 0.49  ? 4212 LEU A CG    1 
ATOM   20364 C  CD1   . LEU A 1 4212 ? 159.508 260.611 198.831 1.00 0.34  ? 4212 LEU A CD1   1 
ATOM   20365 C  CD2   . LEU A 1 4212 ? 160.871 259.407 197.116 1.00 0.54  ? 4212 LEU A CD2   1 
ATOM   20366 N  N     . ARG A 1 4213 ? 160.423 256.515 201.087 1.00 1.70  ? 4213 ARG A N     1 
ATOM   20367 C  CA    . ARG A 1 4213 ? 159.491 255.397 201.226 1.00 1.77  ? 4213 ARG A CA    1 
ATOM   20368 C  C     . ARG A 1 4213 ? 158.823 255.388 202.594 1.00 1.77  ? 4213 ARG A C     1 
ATOM   20369 O  O     . ARG A 1 4213 ? 157.619 255.126 202.696 1.00 2.92  ? 4213 ARG A O     1 
ATOM   20370 C  CB    . ARG A 1 4213 ? 160.194 254.061 200.978 1.00 2.89  ? 4213 ARG A CB    1 
ATOM   20371 C  CG    . ARG A 1 4213 ? 160.656 253.827 199.554 1.00 5.93  ? 4213 ARG A CG    1 
ATOM   20372 C  CD    . ARG A 1 4213 ? 161.333 252.469 199.437 1.00 15.22 ? 4213 ARG A CD    1 
ATOM   20373 N  NE    . ARG A 1 4213 ? 161.816 252.194 198.090 1.00 10.51 ? 4213 ARG A NE    1 
ATOM   20374 C  CZ    . ARG A 1 4213 ? 162.487 251.103 197.746 1.00 22.36 ? 4213 ARG A CZ    1 
ATOM   20375 N  NH1   . ARG A 1 4213 ? 162.774 250.160 198.628 1.00 30.10 ? 4213 ARG A NH1   1 
ATOM   20376 N  NH2   . ARG A 1 4213 ? 162.883 250.955 196.484 1.00 24.98 ? 4213 ARG A NH2   1 
ATOM   20377 N  N     . SER A 1 4214 ? 159.583 255.662 203.656 1.00 1.63  ? 4214 SER A N     1 
ATOM   20378 C  CA    . SER A 1 4214 ? 158.990 255.730 204.987 1.00 1.11  ? 4214 SER A CA    1 
ATOM   20379 C  C     . SER A 1 4214 ? 157.958 256.847 205.069 1.00 1.50  ? 4214 SER A C     1 
ATOM   20380 O  O     . SER A 1 4214 ? 156.897 256.679 205.679 1.00 2.21  ? 4214 SER A O     1 
ATOM   20381 C  CB    . SER A 1 4214 ? 160.077 255.924 206.044 1.00 1.67  ? 4214 SER A CB    1 
ATOM   20382 O  OG    . SER A 1 4214 ? 160.943 254.807 206.094 1.00 5.86  ? 4214 SER A OG    1 
ATOM   20383 N  N     . ALA A 1 4215 ? 158.254 257.994 204.459 1.00 1.33  ? 4215 ALA A N     1 
ATOM   20384 C  CA    . ALA A 1 4215 ? 157.295 259.092 204.437 1.00 1.75  ? 4215 ALA A CA    1 
ATOM   20385 C  C     . ALA A 1 4215 ? 156.039 258.716 203.659 1.00 2.96  ? 4215 ALA A C     1 
ATOM   20386 O  O     . ALA A 1 4215 ? 154.929 259.111 204.033 1.00 4.25  ? 4215 ALA A O     1 
ATOM   20387 C  CB    . ALA A 1 4215 ? 157.946 260.341 203.849 1.00 1.00  ? 4215 ALA A CB    1 
ATOM   20388 N  N     . CYS A 1 4216 ? 156.194 257.957 202.571 1.00 2.84  ? 4216 CYS A N     1 
ATOM   20389 C  CA    . CYS A 1 4216 ? 155.030 257.503 201.815 1.00 2.58  ? 4216 CYS A CA    1 
ATOM   20390 C  C     . CYS A 1 4216 ? 154.174 256.542 202.630 1.00 3.36  ? 4216 CYS A C     1 
ATOM   20391 O  O     . CYS A 1 4216 ? 152.940 256.618 202.590 1.00 2.75  ? 4216 CYS A O     1 
ATOM   20392 C  CB    . CYS A 1 4216 ? 155.467 256.854 200.502 1.00 4.69  ? 4216 CYS A CB    1 
ATOM   20393 S  SG    . CYS A 1 4216 ? 156.194 257.994 199.302 1.00 8.86  ? 4216 CYS A SG    1 
ATOM   20394 N  N     . ASP A 1 4217 ? 154.805 255.625 203.369 1.00 4.66  ? 4217 ASP A N     1 
ATOM   20395 C  CA    . ASP A 1 4217 ? 154.043 254.721 204.225 1.00 3.05  ? 4217 ASP A CA    1 
ATOM   20396 C  C     . ASP A 1 4217 ? 153.322 255.485 205.327 1.00 2.72  ? 4217 ASP A C     1 
ATOM   20397 O  O     . ASP A 1 4217 ? 152.169 255.181 205.652 1.00 4.33  ? 4217 ASP A O     1 
ATOM   20398 C  CB    . ASP A 1 4217 ? 154.955 253.651 204.827 1.00 2.86  ? 4217 ASP A CB    1 
ATOM   20399 C  CG    . ASP A 1 4217 ? 155.628 252.792 203.775 1.00 12.53 ? 4217 ASP A CG    1 
ATOM   20400 O  OD1   . ASP A 1 4217 ? 154.914 252.211 202.932 1.00 19.90 ? 4217 ASP A OD1   1 
ATOM   20401 O  OD2   . ASP A 1 4217 ? 156.870 252.671 203.809 1.00 19.72 ? 4217 ASP A OD2   1 
ATOM   20402 N  N     . THR A 1 4218 ? 153.990 256.477 205.917 1.00 1.69  ? 4218 THR A N     1 
ATOM   20403 C  CA    . THR A 1 4218 ? 153.365 257.278 206.964 1.00 1.51  ? 4218 THR A CA    1 
ATOM   20404 C  C     . THR A 1 4218 ? 152.170 258.055 206.426 1.00 1.59  ? 4218 THR A C     1 
ATOM   20405 O  O     . THR A 1 4218 ? 151.125 258.141 207.080 1.00 1.71  ? 4218 THR A O     1 
ATOM   20406 C  CB    . THR A 1 4218 ? 154.396 258.222 207.582 1.00 1.24  ? 4218 THR A CB    1 
ATOM   20407 O  OG1   . THR A 1 4218 ? 155.399 257.453 208.253 1.00 4.16  ? 4218 THR A OG1   1 
ATOM   20408 C  CG2   . THR A 1 4218 ? 153.742 259.166 208.573 1.00 0.99  ? 4218 THR A CG2   1 
ATOM   20409 N  N     . VAL A 1 4219 ? 152.305 258.621 205.226 1.00 2.22  ? 4219 VAL A N     1 
ATOM   20410 C  CA    . VAL A 1 4219 ? 151.190 259.338 204.614 1.00 2.90  ? 4219 VAL A CA    1 
ATOM   20411 C  C     . VAL A 1 4219 ? 150.012 258.398 204.401 1.00 4.20  ? 4219 VAL A C     1 
ATOM   20412 O  O     . VAL A 1 4219 ? 148.863 258.735 204.702 1.00 10.11 ? 4219 VAL A O     1 
ATOM   20413 C  CB    . VAL A 1 4219 ? 151.635 259.998 203.295 1.00 2.98  ? 4219 VAL A CB    1 
ATOM   20414 C  CG1   . VAL A 1 4219 ? 150.430 260.333 202.429 1.00 5.36  ? 4219 VAL A CG1   1 
ATOM   20415 C  CG2   . VAL A 1 4219 ? 152.441 261.248 203.578 1.00 2.71  ? 4219 VAL A CG2   1 
ATOM   20416 N  N     . ASP A 1 4220 ? 150.285 257.194 203.893 1.00 3.14  ? 4220 ASP A N     1 
ATOM   20417 C  CA    . ASP A 1 4220 ? 149.213 256.242 203.626 1.00 3.43  ? 4220 ASP A CA    1 
ATOM   20418 C  C     . ASP A 1 4220 ? 148.601 255.716 204.919 1.00 5.05  ? 4220 ASP A C     1 
ATOM   20419 O  O     . ASP A 1 4220 ? 147.383 255.523 205.008 1.00 9.46  ? 4220 ASP A O     1 
ATOM   20420 C  CB    . ASP A 1 4220 ? 149.740 255.092 202.771 1.00 5.29  ? 4220 ASP A CB    1 
ATOM   20421 C  CG    . ASP A 1 4220 ? 149.891 255.475 201.317 1.00 10.97 ? 4220 ASP A CG    1 
ATOM   20422 O  OD1   . ASP A 1 4220 ? 150.851 255.006 200.680 1.00 12.99 ? 4220 ASP A OD1   1 
ATOM   20423 O  OD2   . ASP A 1 4220 ? 149.056 256.250 200.811 1.00 10.71 ? 4220 ASP A OD2   1 
ATOM   20424 N  N     . THR A 1 4221 ? 149.433 255.468 205.932 1.00 4.57  ? 4221 THR A N     1 
ATOM   20425 C  CA    . THR A 1 4221 ? 148.930 254.936 207.195 1.00 3.33  ? 4221 THR A CA    1 
ATOM   20426 C  C     . THR A 1 4221 ? 147.944 255.898 207.845 1.00 3.24  ? 4221 THR A C     1 
ATOM   20427 O  O     . THR A 1 4221 ? 146.840 255.506 208.240 1.00 5.43  ? 4221 THR A O     1 
ATOM   20428 C  CB    . THR A 1 4221 ? 150.094 254.641 208.142 1.00 2.99  ? 4221 THR A CB    1 
ATOM   20429 O  OG1   . THR A 1 4221 ? 150.884 253.567 207.617 1.00 6.80  ? 4221 THR A OG1   1 
ATOM   20430 C  CG2   . THR A 1 4221 ? 149.585 254.262 209.521 1.00 1.44  ? 4221 THR A CG2   1 
ATOM   20431 N  N     . TRP A 1 4222 ? 148.320 257.172 207.950 1.00 2.89  ? 4222 TRP A N     1 
ATOM   20432 C  CA    . TRP A 1 4222 ? 147.498 258.133 208.673 1.00 3.39  ? 4222 TRP A CA    1 
ATOM   20433 C  C     . TRP A 1 4222 ? 146.352 258.677 207.832 1.00 6.85  ? 4222 TRP A C     1 
ATOM   20434 O  O     . TRP A 1 4222 ? 145.314 259.053 208.384 1.00 7.12  ? 4222 TRP A O     1 
ATOM   20435 C  CB    . TRP A 1 4222 ? 148.377 259.266 209.198 1.00 1.81  ? 4222 TRP A CB    1 
ATOM   20436 C  CG    . TRP A 1 4222 ? 149.310 258.782 210.253 1.00 1.59  ? 4222 TRP A CG    1 
ATOM   20437 C  CD1   . TRP A 1 4222 ? 150.573 258.308 210.077 1.00 1.05  ? 4222 TRP A CD1   1 
ATOM   20438 C  CD2   . TRP A 1 4222 ? 149.042 258.698 211.656 1.00 0.87  ? 4222 TRP A CD2   1 
ATOM   20439 N  NE1   . TRP A 1 4222 ? 151.114 257.940 211.282 1.00 0.91  ? 4222 TRP A NE1   1 
ATOM   20440 C  CE2   . TRP A 1 4222 ? 150.195 258.172 212.270 1.00 0.91  ? 4222 TRP A CE2   1 
ATOM   20441 C  CE3   . TRP A 1 4222 ? 147.941 259.023 212.452 1.00 0.69  ? 4222 TRP A CE3   1 
ATOM   20442 C  CZ2   . TRP A 1 4222 ? 150.278 257.963 213.643 1.00 0.91  ? 4222 TRP A CZ2   1 
ATOM   20443 C  CZ3   . TRP A 1 4222 ? 148.026 258.814 213.814 1.00 0.97  ? 4222 TRP A CZ3   1 
ATOM   20444 C  CH2   . TRP A 1 4222 ? 149.186 258.289 214.396 1.00 1.30  ? 4222 TRP A CH2   1 
ATOM   20445 N  N     . LEU A 1 4223 ? 146.513 258.733 206.509 1.00 7.41  ? 4223 LEU A N     1 
ATOM   20446 C  CA    . LEU A 1 4223 ? 145.393 259.125 205.662 1.00 6.80  ? 4223 LEU A CA    1 
ATOM   20447 C  C     . LEU A 1 4223 ? 144.310 258.053 205.660 1.00 7.97  ? 4223 LEU A C     1 
ATOM   20448 O  O     . LEU A 1 4223 ? 143.116 258.370 205.701 1.00 11.52 ? 4223 LEU A O     1 
ATOM   20449 C  CB    . LEU A 1 4223 ? 145.877 259.405 204.242 1.00 11.22 ? 4223 LEU A CB    1 
ATOM   20450 C  CG    . LEU A 1 4223 ? 144.822 259.933 203.275 1.00 10.07 ? 4223 LEU A CG    1 
ATOM   20451 C  CD1   . LEU A 1 4223 ? 144.153 261.172 203.842 1.00 11.94 ? 4223 LEU A CD1   1 
ATOM   20452 C  CD2   . LEU A 1 4223 ? 145.459 260.225 201.936 1.00 8.03  ? 4223 LEU A CD2   1 
ATOM   20453 N  N     . ASP A 1 4224 ? 144.709 256.783 205.619 1.00 7.87  ? 4224 ASP A N     1 
ATOM   20454 C  CA    . ASP A 1 4224 ? 143.741 255.695 205.707 1.00 9.85  ? 4224 ASP A CA    1 
ATOM   20455 C  C     . ASP A 1 4224 ? 143.067 255.672 207.072 1.00 10.82 ? 4224 ASP A C     1 
ATOM   20456 O  O     . ASP A 1 4224 ? 141.881 255.340 207.179 1.00 20.04 ? 4224 ASP A O     1 
ATOM   20457 C  CB    . ASP A 1 4224 ? 144.425 254.359 205.420 1.00 10.93 ? 4224 ASP A CB    1 
ATOM   20458 C  CG    . ASP A 1 4224 ? 144.553 254.074 203.936 1.00 19.61 ? 4224 ASP A CG    1 
ATOM   20459 O  OD1   . ASP A 1 4224 ? 145.653 253.681 203.497 1.00 17.62 ? 4224 ASP A OD1   1 
ATOM   20460 O  OD2   . ASP A 1 4224 ? 143.551 254.238 203.209 1.00 24.65 ? 4224 ASP A OD2   1 
ATOM   20461 N  N     . ASP A 1 4225 ? 143.812 256.013 208.126 1.00 11.09 ? 4225 ASP A N     1 
ATOM   20462 C  CA    . ASP A 1 4225 ? 143.240 256.040 209.467 1.00 11.89 ? 4225 ASP A CA    1 
ATOM   20463 C  C     . ASP A 1 4225 ? 142.148 257.097 209.584 1.00 11.35 ? 4225 ASP A C     1 
ATOM   20464 O  O     . ASP A 1 4225 ? 141.103 256.855 210.198 1.00 21.31 ? 4225 ASP A O     1 
ATOM   20465 C  CB    . ASP A 1 4225 ? 144.343 256.282 210.498 1.00 14.69 ? 4225 ASP A CB    1 
ATOM   20466 C  CG    . ASP A 1 4225 ? 143.802 256.730 211.839 1.00 21.89 ? 4225 ASP A CG    1 
ATOM   20467 O  OD1   . ASP A 1 4225 ? 143.908 257.934 212.152 1.00 28.85 ? 4225 ASP A OD1   1 
ATOM   20468 O  OD2   . ASP A 1 4225 ? 143.274 255.879 212.584 1.00 27.99 ? 4225 ASP A OD2   1 
ATOM   20469 N  N     . THR A 1 4226 ? 142.366 258.275 208.999 1.00 10.66 ? 4226 THR A N     1 
ATOM   20470 C  CA    . THR A 1 4226 ? 141.381 259.347 209.106 1.00 16.25 ? 4226 THR A CA    1 
ATOM   20471 C  C     . THR A 1 4226 ? 140.264 259.178 208.081 1.00 21.55 ? 4226 THR A C     1 
ATOM   20472 O  O     . THR A 1 4226 ? 139.082 259.142 208.436 1.00 19.63 ? 4226 THR A O     1 
ATOM   20473 C  CB    . THR A 1 4226 ? 142.061 260.707 208.945 1.00 14.84 ? 4226 THR A CB    1 
ATOM   20474 O  OG1   . THR A 1 4226 ? 142.899 260.958 210.078 1.00 22.41 ? 4226 THR A OG1   1 
ATOM   20475 C  CG2   . THR A 1 4226 ? 141.017 261.800 208.860 1.00 16.04 ? 4226 THR A CG2   1 
ATOM   20476 N  N     . ALA A 1 4227 ? 140.622 259.076 206.803 1.00 19.67 ? 4227 ALA A N     1 
ATOM   20477 C  CA    . ALA A 1 4227 ? 139.644 258.831 205.744 1.00 18.53 ? 4227 ALA A CA    1 
ATOM   20478 C  C     . ALA A 1 4227 ? 139.342 257.340 205.732 1.00 23.21 ? 4227 ALA A C     1 
ATOM   20479 O  O     . ALA A 1 4227 ? 139.969 256.560 205.015 1.00 27.83 ? 4227 ALA A O     1 
ATOM   20480 C  CB    . ALA A 1 4227 ? 140.168 259.313 204.396 1.00 19.32 ? 4227 ALA A CB    1 
ATOM   20481 N  N     . LYS A 1 4228 ? 138.368 256.940 206.547 1.00 23.42 ? 4228 LYS A N     1 
ATOM   20482 C  CA    . LYS A 1 4228 ? 138.038 255.527 206.730 1.00 21.42 ? 4228 LYS A CA    1 
ATOM   20483 C  C     . LYS A 1 4228 ? 137.257 255.046 205.511 1.00 22.17 ? 4228 LYS A C     1 
ATOM   20484 O  O     . LYS A 1 4228 ? 136.026 254.983 205.499 1.00 23.11 ? 4228 LYS A O     1 
ATOM   20485 C  CB    . LYS A 1 4228 ? 137.256 255.320 208.020 1.00 14.34 ? 4228 LYS A CB    1 
ATOM   20486 C  CG    . LYS A 1 4228 ? 138.032 255.669 209.274 1.00 16.26 ? 4228 LYS A CG    1 
ATOM   20487 C  CD    . LYS A 1 4228 ? 137.477 254.942 210.487 1.00 26.05 ? 4228 LYS A CD    1 
ATOM   20488 C  CE    . LYS A 1 4228 ? 138.258 255.292 211.742 1.00 21.20 ? 4228 LYS A CE    1 
ATOM   20489 N  NZ    . LYS A 1 4228 ? 138.578 256.745 211.805 1.00 21.66 ? 4228 LYS A NZ    1 
ATOM   20490 N  N     . GLY A 1 4229 ? 138.003 254.698 204.468 1.00 20.06 ? 4229 GLY A N     1 
ATOM   20491 C  CA    . GLY A 1 4229 ? 137.396 254.194 203.245 1.00 21.62 ? 4229 GLY A CA    1 
ATOM   20492 C  C     . GLY A 1 4229 ? 136.455 255.174 202.578 1.00 21.95 ? 4229 GLY A C     1 
ATOM   20493 O  O     . GLY A 1 4229 ? 135.358 254.786 202.157 1.00 27.83 ? 4229 GLY A O     1 
ATOM   20494 N  N     . ARG A 1 4230 ? 136.855 256.436 202.478 1.00 22.25 ? 4230 ARG A N     1 
ATOM   20495 C  CA    . ARG A 1 4230 ? 136.030 257.479 201.890 1.00 20.83 ? 4230 ARG A CA    1 
ATOM   20496 C  C     . ARG A 1 4230 ? 136.653 257.967 200.589 1.00 22.39 ? 4230 ARG A C     1 
ATOM   20497 O  O     . ARG A 1 4230 ? 137.823 257.713 200.292 1.00 24.18 ? 4230 ARG A O     1 
ATOM   20498 C  CB    . ARG A 1 4230 ? 135.835 258.646 202.866 1.00 19.01 ? 4230 ARG A CB    1 
ATOM   20499 C  CG    . ARG A 1 4230 ? 134.635 258.481 203.785 1.00 14.18 ? 4230 ARG A CG    1 
ATOM   20500 C  CD    . ARG A 1 4230 ? 134.238 259.796 204.438 1.00 15.50 ? 4230 ARG A CD    1 
ATOM   20501 N  NE    . ARG A 1 4230 ? 134.868 259.976 205.740 1.00 28.38 ? 4230 ARG A NE    1 
ATOM   20502 C  CZ    . ARG A 1 4230 ? 136.050 260.544 205.935 1.00 28.21 ? 4230 ARG A CZ    1 
ATOM   20503 N  NH1   . ARG A 1 4230 ? 136.767 261.015 204.928 1.00 24.55 ? 4230 ARG A NH1   1 
ATOM   20504 N  NH2   . ARG A 1 4230 ? 136.526 260.646 207.172 1.00 27.65 ? 4230 ARG A NH2   1 
ATOM   20505 N  N     . GLN A 1 4231 ? 135.845 258.679 199.805 1.00 24.92 ? 4231 GLN A N     1 
ATOM   20506 C  CA    . GLN A 1 4231 ? 136.268 259.139 198.489 1.00 24.05 ? 4231 GLN A CA    1 
ATOM   20507 C  C     . GLN A 1 4231 ? 136.971 260.490 198.536 1.00 25.06 ? 4231 GLN A C     1 
ATOM   20508 O  O     . GLN A 1 4231 ? 137.978 260.687 197.849 1.00 26.32 ? 4231 GLN A O     1 
ATOM   20509 C  CB    . GLN A 1 4231 ? 135.061 259.218 197.550 1.00 18.64 ? 4231 GLN A CB    1 
ATOM   20510 C  CG    . GLN A 1 4231 ? 135.404 259.117 196.072 1.00 22.39 ? 4231 GLN A CG    1 
ATOM   20511 C  CD    . GLN A 1 4231 ? 136.555 258.169 195.793 1.00 24.71 ? 4231 GLN A CD    1 
ATOM   20512 O  OE1   . GLN A 1 4231 ? 137.541 258.536 195.154 1.00 26.23 ? 4231 GLN A OE1   1 
ATOM   20513 N  NE2   . GLN A 1 4231 ? 136.431 256.937 196.272 1.00 23.21 ? 4231 GLN A NE2   1 
ATOM   20514 N  N     . ASN A 1 4232 ? 136.462 261.428 199.334 1.00 22.49 ? 4232 ASN A N     1 
ATOM   20515 C  CA    . ASN A 1 4232 ? 137.003 262.786 199.386 1.00 19.28 ? 4232 ASN A CA    1 
ATOM   20516 C  C     . ASN A 1 4232 ? 137.072 263.221 200.845 1.00 24.47 ? 4232 ASN A C     1 
ATOM   20517 O  O     . ASN A 1 4232 ? 136.046 263.517 201.463 1.00 34.28 ? 4232 ASN A O     1 
ATOM   20518 C  CB    . ASN A 1 4232 ? 136.152 263.745 198.562 1.00 16.36 ? 4232 ASN A CB    1 
ATOM   20519 C  CG    . ASN A 1 4232 ? 136.227 263.457 197.077 1.00 24.87 ? 4232 ASN A CG    1 
ATOM   20520 O  OD1   . ASN A 1 4232 ? 137.253 263.691 196.439 1.00 28.18 ? 4232 ASN A OD1   1 
ATOM   20521 N  ND2   . ASN A 1 4232 ? 135.142 262.933 196.521 1.00 25.19 ? 4232 ASN A ND2   1 
ATOM   20522 N  N     . ILE A 1 4233 ? 138.276 263.265 201.384 1.00 21.70 ? 4233 ILE A N     1 
ATOM   20523 C  CA    . ILE A 1 4233 ? 138.512 263.731 202.744 1.00 18.87 ? 4233 ILE A CA    1 
ATOM   20524 C  C     . ILE A 1 4233 ? 138.688 265.242 202.721 1.00 18.33 ? 4233 ILE A C     1 
ATOM   20525 O  O     . ILE A 1 4233 ? 139.334 265.796 201.823 1.00 21.05 ? 4233 ILE A O     1 
ATOM   20526 C  CB    . ILE A 1 4233 ? 139.737 263.026 203.358 1.00 18.30 ? 4233 ILE A CB    1 
ATOM   20527 C  CG1   . ILE A 1 4233 ? 139.964 263.488 204.798 1.00 11.72 ? 4233 ILE A CG1   1 
ATOM   20528 C  CG2   . ILE A 1 4233 ? 140.981 263.243 202.504 1.00 16.18 ? 4233 ILE A CG2   1 
ATOM   20529 C  CD1   . ILE A 1 4233 ? 141.126 262.812 205.467 1.00 15.52 ? 4233 ILE A CD1   1 
ATOM   20530 N  N     . SER A 1 4234 ? 138.096 265.918 203.698 1.00 21.34 ? 4234 SER A N     1 
ATOM   20531 C  CA    . SER A 1 4234 ? 138.250 267.363 203.782 1.00 13.91 ? 4234 SER A CA    1 
ATOM   20532 C  C     . SER A 1 4234 ? 139.712 267.711 204.051 1.00 17.27 ? 4234 SER A C     1 
ATOM   20533 O  O     . SER A 1 4234 ? 140.370 267.045 204.859 1.00 26.78 ? 4234 SER A O     1 
ATOM   20534 C  CB    . SER A 1 4234 ? 137.361 267.936 204.885 1.00 19.14 ? 4234 SER A CB    1 
ATOM   20535 O  OG    . SER A 1 4234 ? 137.669 269.297 205.127 1.00 23.45 ? 4234 SER A OG    1 
ATOM   20536 N  N     . PRO A 1 4235 ? 140.256 268.732 203.383 1.00 18.05 ? 4235 PRO A N     1 
ATOM   20537 C  CA    . PRO A 1 4235 ? 141.672 269.077 203.597 1.00 15.39 ? 4235 PRO A CA    1 
ATOM   20538 C  C     . PRO A 1 4235 ? 142.005 269.421 205.035 1.00 14.41 ? 4235 PRO A C     1 
ATOM   20539 O  O     . PRO A 1 4235 ? 143.103 269.093 205.502 1.00 19.04 ? 4235 PRO A O     1 
ATOM   20540 C  CB    . PRO A 1 4235 ? 141.876 270.279 202.666 1.00 10.26 ? 4235 PRO A CB    1 
ATOM   20541 C  CG    . PRO A 1 4235 ? 140.832 270.112 201.612 1.00 14.33 ? 4235 PRO A CG    1 
ATOM   20542 C  CD    . PRO A 1 4235 ? 139.641 269.561 202.335 1.00 13.97 ? 4235 PRO A CD    1 
ATOM   20543 N  N     . ASP A 1 4236 ? 141.094 270.071 205.756 1.00 18.33 ? 4236 ASP A N     1 
ATOM   20544 C  CA    . ASP A 1 4236 ? 141.344 270.408 207.150 1.00 18.51 ? 4236 ASP A CA    1 
ATOM   20545 C  C     . ASP A 1 4236 ? 141.233 269.207 208.079 1.00 17.04 ? 4236 ASP A C     1 
ATOM   20546 O  O     . ASP A 1 4236 ? 141.658 269.300 209.235 1.00 20.02 ? 4236 ASP A O     1 
ATOM   20547 C  CB    . ASP A 1 4236 ? 140.392 271.523 207.594 1.00 13.64 ? 4236 ASP A CB    1 
ATOM   20548 C  CG    . ASP A 1 4236 ? 138.931 271.111 207.535 1.00 27.84 ? 4236 ASP A CG    1 
ATOM   20549 O  OD1   . ASP A 1 4236 ? 138.635 269.975 207.111 1.00 27.28 ? 4236 ASP A OD1   1 
ATOM   20550 O  OD2   . ASP A 1 4236 ? 138.070 271.938 207.903 1.00 31.45 ? 4236 ASP A OD2   1 
ATOM   20551 N  N     . LYS A 1 4237 ? 140.673 268.095 207.608 1.00 15.00 ? 4237 LYS A N     1 
ATOM   20552 C  CA    . LYS A 1 4237 ? 140.628 266.857 208.370 1.00 10.82 ? 4237 LYS A CA    1 
ATOM   20553 C  C     . LYS A 1 4237 ? 141.831 265.962 208.102 1.00 10.05 ? 4237 LYS A C     1 
ATOM   20554 O  O     . LYS A 1 4237 ? 141.966 264.918 208.749 1.00 13.68 ? 4237 LYS A O     1 
ATOM   20555 C  CB    . LYS A 1 4237 ? 139.337 266.090 208.063 1.00 12.41 ? 4237 LYS A CB    1 
ATOM   20556 C  CG    . LYS A 1 4237 ? 138.037 266.827 208.397 1.00 15.94 ? 4237 LYS A CG    1 
ATOM   20557 C  CD    . LYS A 1 4237 ? 137.784 266.966 209.896 1.00 16.29 ? 4237 LYS A CD    1 
ATOM   20558 C  CE    . LYS A 1 4237 ? 138.299 268.285 210.459 1.00 23.00 ? 4237 LYS A CE    1 
ATOM   20559 N  NZ    . LYS A 1 4237 ? 137.947 268.444 211.897 1.00 24.00 ? 4237 LYS A NZ    1 
ATOM   20560 N  N     . ILE A 1 4238 ? 142.692 266.337 207.166 1.00 12.61 ? 4238 ILE A N     1 
ATOM   20561 C  CA    . ILE A 1 4238 ? 143.937 265.599 206.937 1.00 10.06 ? 4238 ILE A CA    1 
ATOM   20562 C  C     . ILE A 1 4238 ? 144.821 265.722 208.174 1.00 11.49 ? 4238 ILE A C     1 
ATOM   20563 O  O     . ILE A 1 4238 ? 144.983 266.832 208.708 1.00 10.77 ? 4238 ILE A O     1 
ATOM   20564 C  CB    . ILE A 1 4238 ? 144.649 266.135 205.691 1.00 8.66  ? 4238 ILE A CB    1 
ATOM   20565 C  CG1   . ILE A 1 4238 ? 143.762 265.949 204.456 1.00 11.11 ? 4238 ILE A CG1   1 
ATOM   20566 C  CG2   . ILE A 1 4238 ? 145.998 265.461 205.501 1.00 5.79  ? 4238 ILE A CG2   1 
ATOM   20567 C  CD1   . ILE A 1 4238 ? 144.346 266.518 203.187 1.00 12.26 ? 4238 ILE A CD1   1 
ATOM   20568 N  N     . PRO A 1 4239 ? 145.397 264.629 208.675 1.00 11.30 ? 4239 PRO A N     1 
ATOM   20569 C  CA    . PRO A 1 4239 ? 146.220 264.723 209.887 1.00 7.09  ? 4239 PRO A CA    1 
ATOM   20570 C  C     . PRO A 1 4239 ? 147.557 265.404 209.639 1.00 6.69  ? 4239 PRO A C     1 
ATOM   20571 O  O     . PRO A 1 4239 ? 148.601 264.744 209.584 1.00 3.53  ? 4239 PRO A O     1 
ATOM   20572 C  CB    . PRO A 1 4239 ? 146.396 263.256 210.295 1.00 6.89  ? 4239 PRO A CB    1 
ATOM   20573 C  CG    . PRO A 1 4239 ? 146.309 262.513 209.012 1.00 5.51  ? 4239 PRO A CG    1 
ATOM   20574 C  CD    . PRO A 1 4239 ? 145.278 263.243 208.195 1.00 5.97  ? 4239 PRO A CD    1 
ATOM   20575 N  N     . TRP A 1 4240 ? 147.530 266.730 209.495 1.00 5.50  ? 4240 TRP A N     1 
ATOM   20576 C  CA    . TRP A 1 4240 ? 148.757 267.479 209.244 1.00 3.42  ? 4240 TRP A CA    1 
ATOM   20577 C  C     . TRP A 1 4240 ? 149.715 267.384 210.422 1.00 2.89  ? 4240 TRP A C     1 
ATOM   20578 O  O     . TRP A 1 4240 ? 150.934 267.286 210.235 1.00 2.41  ? 4240 TRP A O     1 
ATOM   20579 C  CB    . TRP A 1 4240 ? 148.426 268.939 208.938 1.00 3.85  ? 4240 TRP A CB    1 
ATOM   20580 C  CG    . TRP A 1 4240 ? 147.559 269.109 207.744 1.00 3.31  ? 4240 TRP A CG    1 
ATOM   20581 C  CD1   . TRP A 1 4240 ? 146.268 269.543 207.724 1.00 3.98  ? 4240 TRP A CD1   1 
ATOM   20582 C  CD2   . TRP A 1 4240 ? 147.914 268.842 206.383 1.00 5.26  ? 4240 TRP A CD2   1 
ATOM   20583 N  NE1   . TRP A 1 4240 ? 145.795 269.562 206.438 1.00 8.58  ? 4240 TRP A NE1   1 
ATOM   20584 C  CE2   . TRP A 1 4240 ? 146.788 269.138 205.594 1.00 5.69  ? 4240 TRP A CE2   1 
ATOM   20585 C  CE3   . TRP A 1 4240 ? 149.074 268.383 205.757 1.00 3.78  ? 4240 TRP A CE3   1 
ATOM   20586 C  CZ2   . TRP A 1 4240 ? 146.787 268.986 204.213 1.00 5.99  ? 4240 TRP A CZ2   1 
ATOM   20587 C  CZ3   . TRP A 1 4240 ? 149.072 268.236 204.386 1.00 3.59  ? 4240 TRP A CZ3   1 
ATOM   20588 C  CH2   . TRP A 1 4240 ? 147.938 268.541 203.628 1.00 4.60  ? 4240 TRP A CH2   1 
ATOM   20589 N  N     . SER A 1 4241 ? 149.181 267.422 211.644 1.00 5.85  ? 4241 SER A N     1 
ATOM   20590 C  CA    . SER A 1 4241 ? 150.030 267.323 212.825 1.00 3.20  ? 4241 SER A CA    1 
ATOM   20591 C  C     . SER A 1 4241 ? 150.751 265.983 212.878 1.00 2.01  ? 4241 SER A C     1 
ATOM   20592 O  O     . SER A 1 4241 ? 151.938 265.923 213.213 1.00 1.91  ? 4241 SER A O     1 
ATOM   20593 C  CB    . SER A 1 4241 ? 149.193 267.537 214.087 1.00 3.76  ? 4241 SER A CB    1 
ATOM   20594 O  OG    . SER A 1 4241 ? 149.986 267.413 215.251 1.00 14.94 ? 4241 SER A OG    1 
ATOM   20595 N  N     . ALA A 1 4242 ? 150.050 264.897 212.551 1.00 2.34  ? 4242 ALA A N     1 
ATOM   20596 C  CA    . ALA A 1 4242 ? 150.682 263.582 212.550 1.00 1.30  ? 4242 ALA A CA    1 
ATOM   20597 C  C     . ALA A 1 4242 ? 151.775 263.492 211.491 1.00 3.55  ? 4242 ALA A C     1 
ATOM   20598 O  O     . ALA A 1 4242 ? 152.869 262.984 211.761 1.00 4.22  ? 4242 ALA A O     1 
ATOM   20599 C  CB    . ALA A 1 4242 ? 149.632 262.495 212.323 1.00 1.38  ? 4242 ALA A CB    1 
ATOM   20600 N  N     . LEU A 1 4243 ? 151.496 263.980 210.278 1.00 2.08  ? 4243 LEU A N     1 
ATOM   20601 C  CA    . LEU A 1 4243 ? 152.475 263.882 209.200 1.00 1.06  ? 4243 LEU A CA    1 
ATOM   20602 C  C     . LEU A 1 4243 ? 153.700 264.740 209.481 1.00 1.32  ? 4243 LEU A C     1 
ATOM   20603 O  O     . LEU A 1 4243 ? 154.835 264.288 209.292 1.00 3.83  ? 4243 LEU A O     1 
ATOM   20604 C  CB    . LEU A 1 4243 ? 151.838 264.282 207.870 1.00 2.70  ? 4243 LEU A CB    1 
ATOM   20605 C  CG    . LEU A 1 4243 ? 150.645 263.455 207.392 1.00 3.18  ? 4243 LEU A CG    1 
ATOM   20606 C  CD1   . LEU A 1 4243 ? 150.148 263.966 206.050 1.00 1.69  ? 4243 LEU A CD1   1 
ATOM   20607 C  CD2   . LEU A 1 4243 ? 150.995 261.974 207.317 1.00 1.48  ? 4243 LEU A CD2   1 
ATOM   20608 N  N     . LYS A 1 4244 ? 153.493 265.979 209.931 1.00 1.50  ? 4244 LYS A N     1 
ATOM   20609 C  CA    . LYS A 1 4244 ? 154.615 266.885 210.149 1.00 0.98  ? 4244 LYS A CA    1 
ATOM   20610 C  C     . LYS A 1 4244 ? 155.507 266.400 211.283 1.00 0.66  ? 4244 LYS A C     1 
ATOM   20611 O  O     . LYS A 1 4244 ? 156.735 266.370 211.149 1.00 1.01  ? 4244 LYS A O     1 
ATOM   20612 C  CB    . LYS A 1 4244 ? 154.104 268.297 210.433 1.00 1.77  ? 4244 LYS A CB    1 
ATOM   20613 C  CG    . LYS A 1 4244 ? 153.724 269.080 209.192 1.00 2.47  ? 4244 LYS A CG    1 
ATOM   20614 C  CD    . LYS A 1 4244 ? 153.291 270.493 209.544 1.00 3.57  ? 4244 LYS A CD    1 
ATOM   20615 C  CE    . LYS A 1 4244 ? 152.113 270.482 210.502 1.00 6.04  ? 4244 LYS A CE    1 
ATOM   20616 N  NZ    . LYS A 1 4244 ? 151.579 271.847 210.728 1.00 10.30 ? 4244 LYS A NZ    1 
ATOM   20617 N  N     . THR A 1 4245 ? 154.905 266.014 212.411 1.00 0.88  ? 4245 THR A N     1 
ATOM   20618 C  CA    . THR A 1 4245 ? 155.691 265.590 213.564 1.00 0.65  ? 4245 THR A CA    1 
ATOM   20619 C  C     . THR A 1 4245 ? 156.506 264.341 213.256 1.00 0.46  ? 4245 THR A C     1 
ATOM   20620 O  O     . THR A 1 4245 ? 157.686 264.257 213.614 1.00 0.45  ? 4245 THR A O     1 
ATOM   20621 C  CB    . THR A 1 4245 ? 154.777 265.340 214.761 1.00 0.92  ? 4245 THR A CB    1 
ATOM   20622 O  OG1   . THR A 1 4245 ? 153.893 266.457 214.935 1.00 3.46  ? 4245 THR A OG1   1 
ATOM   20623 C  CG2   . THR A 1 4245 ? 155.592 265.131 216.026 1.00 0.40  ? 4245 THR A CG2   1 
ATOM   20624 N  N     . LEU A 1 4246 ? 155.894 263.358 212.592 1.00 0.57  ? 4246 LEU A N     1 
ATOM   20625 C  CA    . LEU A 1 4246 ? 156.611 262.129 212.278 1.00 0.48  ? 4246 LEU A CA    1 
ATOM   20626 C  C     . LEU A 1 4246 ? 157.768 262.399 211.328 1.00 0.53  ? 4246 LEU A C     1 
ATOM   20627 O  O     . LEU A 1 4246 ? 158.841 261.800 211.459 1.00 0.73  ? 4246 LEU A O     1 
ATOM   20628 C  CB    . LEU A 1 4246 ? 155.647 261.094 211.696 1.00 0.58  ? 4246 LEU A CB    1 
ATOM   20629 C  CG    . LEU A 1 4246 ? 154.865 260.344 212.776 1.00 0.50  ? 4246 LEU A CG    1 
ATOM   20630 C  CD1   . LEU A 1 4246 ? 153.909 259.340 212.176 1.00 0.69  ? 4246 LEU A CD1   1 
ATOM   20631 C  CD2   . LEU A 1 4246 ? 155.818 259.661 213.748 1.00 0.16  ? 4246 LEU A CD2   1 
ATOM   20632 N  N     . MET A 1 4247 ? 157.574 263.302 210.368 1.00 0.99  ? 4247 MET A N     1 
ATOM   20633 C  CA    . MET A 1 4247 ? 158.677 263.717 209.513 1.00 0.80  ? 4247 MET A CA    1 
ATOM   20634 C  C     . MET A 1 4247 ? 159.638 264.658 210.234 1.00 0.82  ? 4247 MET A C     1 
ATOM   20635 O  O     . MET A 1 4247 ? 160.825 264.701 209.902 1.00 2.88  ? 4247 MET A O     1 
ATOM   20636 C  CB    . MET A 1 4247 ? 158.140 264.373 208.243 1.00 1.12  ? 4247 MET A CB    1 
ATOM   20637 C  CG    . MET A 1 4247 ? 157.701 263.379 207.183 1.00 1.46  ? 4247 MET A CG    1 
ATOM   20638 S  SD    . MET A 1 4247 ? 157.278 264.149 205.615 1.00 23.95 ? 4247 MET A SD    1 
ATOM   20639 C  CE    . MET A 1 4247 ? 155.563 264.571 205.909 1.00 3.57  ? 4247 MET A CE    1 
ATOM   20640 N  N     . ALA A 1 4248 ? 159.162 265.421 211.214 1.00 0.47  ? 4248 ALA A N     1 
ATOM   20641 C  CA    . ALA A 1 4248 ? 160.073 266.288 211.949 1.00 0.47  ? 4248 ALA A CA    1 
ATOM   20642 C  C     . ALA A 1 4248 ? 160.997 265.479 212.850 1.00 0.68  ? 4248 ALA A C     1 
ATOM   20643 O  O     . ALA A 1 4248 ? 162.176 265.821 213.004 1.00 1.54  ? 4248 ALA A O     1 
ATOM   20644 C  CB    . ALA A 1 4248 ? 159.288 267.312 212.763 1.00 2.47  ? 4248 ALA A CB    1 
ATOM   20645 N  N     . GLN A 1 4249 ? 160.490 264.403 213.441 1.00 0.50  ? 4249 GLN A N     1 
ATOM   20646 C  CA    . GLN A 1 4249 ? 161.207 263.659 214.469 1.00 0.72  ? 4249 GLN A CA    1 
ATOM   20647 C  C     . GLN A 1 4249 ? 161.809 262.351 213.986 1.00 1.00  ? 4249 GLN A C     1 
ATOM   20648 O  O     . GLN A 1 4249 ? 162.884 261.970 214.451 1.00 1.48  ? 4249 GLN A O     1 
ATOM   20649 C  CB    . GLN A 1 4249 ? 160.273 263.372 215.651 1.00 1.02  ? 4249 GLN A CB    1 
ATOM   20650 C  CG    . GLN A 1 4249 ? 159.685 264.621 216.287 1.00 0.83  ? 4249 GLN A CG    1 
ATOM   20651 C  CD    . GLN A 1 4249 ? 160.752 265.611 216.711 1.00 2.79  ? 4249 GLN A CD    1 
ATOM   20652 O  OE1   . GLN A 1 4249 ? 161.519 265.354 217.637 1.00 6.22  ? 4249 GLN A OE1   1 
ATOM   20653 N  NE2   . GLN A 1 4249 ? 160.812 266.744 216.022 1.00 2.19  ? 4249 GLN A NE2   1 
ATOM   20654 N  N     . SER A 1 4250 ? 161.151 261.647 213.064 1.00 1.57  ? 4250 SER A N     1 
ATOM   20655 C  CA    . SER A 1 4250 ? 161.540 260.289 212.710 1.00 1.32  ? 4250 SER A CA    1 
ATOM   20656 C  C     . SER A 1 4250 ? 161.983 260.159 211.258 1.00 2.16  ? 4250 SER A C     1 
ATOM   20657 O  O     . SER A 1 4250 ? 163.046 259.595 210.988 1.00 7.82  ? 4250 SER A O     1 
ATOM   20658 C  CB    . SER A 1 4250 ? 160.377 259.333 213.004 1.00 1.12  ? 4250 SER A CB    1 
ATOM   20659 O  OG    . SER A 1 4250 ? 159.954 259.460 214.348 1.00 1.03  ? 4250 SER A OG    1 
ATOM   20660 N  N     . ILE A 1 4251 ? 161.199 260.663 210.311 1.00 2.10  ? 4251 ILE A N     1 
ATOM   20661 C  CA    . ILE A 1 4251 ? 161.481 260.523 208.887 1.00 1.49  ? 4251 ILE A CA    1 
ATOM   20662 C  C     . ILE A 1 4251 ? 162.092 261.828 208.400 1.00 7.46  ? 4251 ILE A C     1 
ATOM   20663 O  O     . ILE A 1 4251 ? 161.405 262.849 208.360 1.00 17.96 ? 4251 ILE A O     1 
ATOM   20664 C  CB    . ILE A 1 4251 ? 160.205 260.205 208.098 1.00 2.01  ? 4251 ILE A CB    1 
ATOM   20665 C  CG1   . ILE A 1 4251 ? 159.598 258.889 208.558 1.00 1.74  ? 4251 ILE A CG1   1 
ATOM   20666 C  CG2   . ILE A 1 4251 ? 160.513 260.119 206.620 1.00 3.14  ? 4251 ILE A CG2   1 
ATOM   20667 C  CD1   . ILE A 1 4251 ? 158.226 258.672 208.014 1.00 0.97  ? 4251 ILE A CD1   1 
ATOM   20668 N  N     . TYR A 1 4252 ? 163.362 261.780 207.990 1.00 2.51  ? 4252 TYR A N     1 
ATOM   20669 C  CA    . TYR A 1 4252 ? 164.193 262.941 207.656 1.00 1.93  ? 4252 TYR A CA    1 
ATOM   20670 C  C     . TYR A 1 4252 ? 164.651 263.673 208.912 1.00 2.47  ? 4252 TYR A C     1 
ATOM   20671 O  O     . TYR A 1 4252 ? 165.517 264.549 208.839 1.00 8.60  ? 4252 TYR A O     1 
ATOM   20672 C  CB    . TYR A 1 4252 ? 163.478 263.956 206.751 1.00 0.57  ? 4252 TYR A CB    1 
ATOM   20673 C  CG    . TYR A 1 4252 ? 162.931 263.444 205.440 1.00 0.79  ? 4252 TYR A CG    1 
ATOM   20674 C  CD1   . TYR A 1 4252 ? 163.744 263.330 204.320 1.00 0.45  ? 4252 TYR A CD1   1 
ATOM   20675 C  CD2   . TYR A 1 4252 ? 161.585 263.128 205.307 1.00 0.98  ? 4252 TYR A CD2   1 
ATOM   20676 C  CE1   . TYR A 1 4252 ? 163.239 262.884 203.119 1.00 0.60  ? 4252 TYR A CE1   1 
ATOM   20677 C  CE2   . TYR A 1 4252 ? 161.073 262.679 204.111 1.00 0.87  ? 4252 TYR A CE2   1 
ATOM   20678 C  CZ    . TYR A 1 4252 ? 161.904 262.559 203.020 1.00 0.46  ? 4252 TYR A CZ    1 
ATOM   20679 O  OH    . TYR A 1 4252 ? 161.397 262.112 201.825 1.00 0.46  ? 4252 TYR A OH    1 
ATOM   20680 N  N     . GLY A 1 4253 ? 164.102 263.312 210.065 1.00 5.57  ? 4253 GLY A N     1 
ATOM   20681 C  CA    . GLY A 1 4253 ? 164.435 263.998 211.296 1.00 0.87  ? 4253 GLY A CA    1 
ATOM   20682 C  C     . GLY A 1 4253 ? 165.458 263.240 212.109 1.00 1.01  ? 4253 GLY A C     1 
ATOM   20683 O  O     . GLY A 1 4253 ? 166.259 263.840 212.831 1.00 3.47  ? 4253 GLY A O     1 
ATOM   20684 N  N     . GLY A 1 4254 ? 165.447 261.912 211.982 1.00 1.11  ? 4254 GLY A N     1 
ATOM   20685 C  CA    . GLY A 1 4254 ? 166.385 261.083 212.712 1.00 0.61  ? 4254 GLY A CA    1 
ATOM   20686 C  C     . GLY A 1 4254 ? 167.831 261.296 212.321 1.00 1.08  ? 4254 GLY A C     1 
ATOM   20687 O  O     . GLY A 1 4254 ? 168.726 261.032 213.129 1.00 5.76  ? 4254 GLY A O     1 
ATOM   20688 N  N     . ARG A 1 4255 ? 168.080 261.768 211.100 1.00 1.59  ? 4255 ARG A N     1 
ATOM   20689 C  CA    . ARG A 1 4255 ? 169.442 262.009 210.651 1.00 2.00  ? 4255 ARG A CA    1 
ATOM   20690 C  C     . ARG A 1 4255 ? 170.022 263.308 211.190 1.00 1.54  ? 4255 ARG A C     1 
ATOM   20691 O  O     . ARG A 1 4255 ? 171.246 263.463 211.202 1.00 3.77  ? 4255 ARG A O     1 
ATOM   20692 C  CB    . ARG A 1 4255 ? 169.489 262.029 209.124 1.00 1.47  ? 4255 ARG A CB    1 
ATOM   20693 C  CG    . ARG A 1 4255 ? 168.772 260.863 208.486 1.00 3.06  ? 4255 ARG A CG    1 
ATOM   20694 C  CD    . ARG A 1 4255 ? 168.775 260.967 206.974 1.00 3.56  ? 4255 ARG A CD    1 
ATOM   20695 N  NE    . ARG A 1 4255 ? 168.300 259.741 206.346 1.00 2.44  ? 4255 ARG A NE    1 
ATOM   20696 C  CZ    . ARG A 1 4255 ? 168.955 258.588 206.353 1.00 2.40  ? 4255 ARG A CZ    1 
ATOM   20697 N  NH1   . ARG A 1 4255 ? 170.139 258.468 206.933 1.00 2.20  ? 4255 ARG A NH1   1 
ATOM   20698 N  NH2   . ARG A 1 4255 ? 168.413 257.532 205.755 1.00 2.48  ? 4255 ARG A NH2   1 
ATOM   20699 N  N     . VAL A 1 4256 ? 169.181 264.229 211.643 1.00 1.08  ? 4256 VAL A N     1 
ATOM   20700 C  CA    . VAL A 1 4256 ? 169.630 265.572 211.990 1.00 1.68  ? 4256 VAL A CA    1 
ATOM   20701 C  C     . VAL A 1 4256 ? 170.194 265.575 213.404 1.00 1.54  ? 4256 VAL A C     1 
ATOM   20702 O  O     . VAL A 1 4256 ? 169.523 265.160 214.357 1.00 3.01  ? 4256 VAL A O     1 
ATOM   20703 C  CB    . VAL A 1 4256 ? 168.480 266.581 211.846 1.00 1.93  ? 4256 VAL A CB    1 
ATOM   20704 C  CG1   . VAL A 1 4256 ? 168.967 267.985 212.144 1.00 1.31  ? 4256 VAL A CG1   1 
ATOM   20705 C  CG2   . VAL A 1 4256 ? 167.886 266.503 210.449 1.00 0.90  ? 4256 VAL A CG2   1 
ATOM   20706 N  N     . ASP A 1 4257 ? 171.431 266.048 213.542 1.00 1.84  ? 4257 ASP A N     1 
ATOM   20707 C  CA    . ASP A 1 4257 ? 172.102 266.167 214.831 1.00 4.26  ? 4257 ASP A CA    1 
ATOM   20708 C  C     . ASP A 1 4257 ? 172.445 267.622 215.138 1.00 4.09  ? 4257 ASP A C     1 
ATOM   20709 O  O     . ASP A 1 4257 ? 173.354 267.904 215.920 1.00 4.64  ? 4257 ASP A O     1 
ATOM   20710 C  CB    . ASP A 1 4257 ? 173.358 265.299 214.868 1.00 4.50  ? 4257 ASP A CB    1 
ATOM   20711 C  CG    . ASP A 1 4257 ? 174.248 265.503 213.657 1.00 8.46  ? 4257 ASP A CG    1 
ATOM   20712 O  OD1   . ASP A 1 4257 ? 173.908 266.338 212.795 1.00 9.36  ? 4257 ASP A OD1   1 
ATOM   20713 O  OD2   . ASP A 1 4257 ? 175.292 264.826 213.566 1.00 20.93 ? 4257 ASP A OD2   1 
ATOM   20714 N  N     . ASN A 1 4258 ? 171.719 268.551 214.523 1.00 3.34  ? 4258 ASN A N     1 
ATOM   20715 C  CA    . ASN A 1 4258 ? 171.986 269.978 214.634 1.00 3.59  ? 4258 ASN A CA    1 
ATOM   20716 C  C     . ASN A 1 4258 ? 170.654 270.688 214.810 1.00 2.72  ? 4258 ASN A C     1 
ATOM   20717 O  O     . ASN A 1 4258 ? 169.718 270.442 214.045 1.00 5.09  ? 4258 ASN A O     1 
ATOM   20718 C  CB    . ASN A 1 4258 ? 172.736 270.478 213.387 1.00 2.64  ? 4258 ASN A CB    1 
ATOM   20719 C  CG    . ASN A 1 4258 ? 172.953 271.980 213.379 1.00 5.22  ? 4258 ASN A CG    1 
ATOM   20720 O  OD1   . ASN A 1 4258 ? 172.005 272.760 213.349 1.00 10.75 ? 4258 ASN A OD1   1 
ATOM   20721 N  ND2   . ASN A 1 4258 ? 174.214 272.390 213.382 1.00 4.76  ? 4258 ASN A ND2   1 
ATOM   20722 N  N     . GLU A 1 4259 ? 170.566 271.565 215.813 1.00 3.36  ? 4259 GLU A N     1 
ATOM   20723 C  CA    . GLU A 1 4259 ? 169.288 272.208 216.106 1.00 3.59  ? 4259 GLU A CA    1 
ATOM   20724 C  C     . GLU A 1 4259 ? 168.887 273.185 215.007 1.00 1.79  ? 4259 GLU A C     1 
ATOM   20725 O  O     . GLU A 1 4259 ? 167.695 273.368 214.735 1.00 1.51  ? 4259 GLU A O     1 
ATOM   20726 C  CB    . GLU A 1 4259 ? 169.344 272.915 217.462 1.00 3.35  ? 4259 GLU A CB    1 
ATOM   20727 C  CG    . GLU A 1 4259 ? 170.309 274.086 217.527 1.00 6.60  ? 4259 GLU A CG    1 
ATOM   20728 C  CD    . GLU A 1 4259 ? 170.376 274.714 218.906 1.00 19.69 ? 4259 GLU A CD    1 
ATOM   20729 O  OE1   . GLU A 1 4259 ? 169.683 274.219 219.820 1.00 25.07 ? 4259 GLU A OE1   1 
ATOM   20730 O  OE2   . GLU A 1 4259 ? 171.122 275.701 219.074 1.00 21.82 ? 4259 GLU A OE2   1 
ATOM   20731 N  N     . PHE A 1 4260 ? 169.865 273.827 214.368 1.00 2.56  ? 4260 PHE A N     1 
ATOM   20732 C  CA    . PHE A 1 4260 ? 169.550 274.791 213.320 1.00 3.59  ? 4260 PHE A CA    1 
ATOM   20733 C  C     . PHE A 1 4260 ? 169.145 274.086 212.032 1.00 2.25  ? 4260 PHE A C     1 
ATOM   20734 O  O     . PHE A 1 4260 ? 168.311 274.594 211.274 1.00 1.53  ? 4260 PHE A O     1 
ATOM   20735 C  CB    . PHE A 1 4260 ? 170.746 275.713 213.099 1.00 3.82  ? 4260 PHE A CB    1 
ATOM   20736 C  CG    . PHE A 1 4260 ? 171.138 276.475 214.327 1.00 6.01  ? 4260 PHE A CG    1 
ATOM   20737 C  CD1   . PHE A 1 4260 ? 170.496 277.650 214.660 1.00 6.15  ? 4260 PHE A CD1   1 
ATOM   20738 C  CD2   . PHE A 1 4260 ? 172.122 275.992 215.169 1.00 4.02  ? 4260 PHE A CD2   1 
ATOM   20739 C  CE1   . PHE A 1 4260 ? 170.841 278.341 215.794 1.00 6.71  ? 4260 PHE A CE1   1 
ATOM   20740 C  CE2   . PHE A 1 4260 ? 172.469 276.678 216.305 1.00 4.16  ? 4260 PHE A CE2   1 
ATOM   20741 C  CZ    . PHE A 1 4260 ? 171.829 277.857 216.618 1.00 5.40  ? 4260 PHE A CZ    1 
ATOM   20742 N  N     . ASP A 1 4261 ? 169.724 272.914 211.773 1.00 1.93  ? 4261 ASP A N     1 
ATOM   20743 C  CA    . ASP A 1 4261 ? 169.240 272.078 210.683 1.00 1.47  ? 4261 ASP A CA    1 
ATOM   20744 C  C     . ASP A 1 4261 ? 167.869 271.500 211.009 1.00 1.28  ? 4261 ASP A C     1 
ATOM   20745 O  O     . ASP A 1 4261 ? 167.037 271.318 210.113 1.00 1.57  ? 4261 ASP A O     1 
ATOM   20746 C  CB    . ASP A 1 4261 ? 170.247 270.971 210.390 1.00 1.86  ? 4261 ASP A CB    1 
ATOM   20747 C  CG    . ASP A 1 4261 ? 171.434 271.462 209.588 1.00 2.59  ? 4261 ASP A CG    1 
ATOM   20748 O  OD1   . ASP A 1 4261 ? 171.449 272.651 209.208 1.00 2.64  ? 4261 ASP A OD1   1 
ATOM   20749 O  OD2   . ASP A 1 4261 ? 172.365 270.669 209.352 1.00 3.18  ? 4261 ASP A OD2   1 
ATOM   20750 N  N     . GLN A 1 4262 ? 167.619 271.199 212.285 1.00 1.27  ? 4262 GLN A N     1 
ATOM   20751 C  CA    . GLN A 1 4262 ? 166.294 270.752 212.703 1.00 0.94  ? 4262 GLN A CA    1 
ATOM   20752 C  C     . GLN A 1 4262 ? 165.257 271.852 212.525 1.00 1.14  ? 4262 GLN A C     1 
ATOM   20753 O  O     . GLN A 1 4262 ? 164.129 271.586 212.092 1.00 1.82  ? 4262 GLN A O     1 
ATOM   20754 C  CB    . GLN A 1 4262 ? 166.333 270.278 214.156 1.00 1.21  ? 4262 GLN A CB    1 
ATOM   20755 C  CG    . GLN A 1 4262 ? 165.022 269.703 214.673 1.00 1.05  ? 4262 GLN A CG    1 
ATOM   20756 C  CD    . GLN A 1 4262 ? 164.602 268.442 213.943 1.00 2.28  ? 4262 GLN A CD    1 
ATOM   20757 O  OE1   . GLN A 1 4262 ? 165.345 267.464 213.891 1.00 3.18  ? 4262 GLN A OE1   1 
ATOM   20758 N  NE2   . GLN A 1 4262 ? 163.398 268.455 213.385 1.00 1.09  ? 4262 GLN A NE2   1 
ATOM   20759 N  N     . ARG A 1 4263 ? 165.615 273.093 212.864 1.00 1.32  ? 4263 ARG A N     1 
ATOM   20760 C  CA    . ARG A 1 4263 ? 164.694 274.208 212.674 1.00 1.29  ? 4263 ARG A CA    1 
ATOM   20761 C  C     . ARG A 1 4263 ? 164.384 274.412 211.199 1.00 2.37  ? 4263 ARG A C     1 
ATOM   20762 O  O     . ARG A 1 4263 ? 163.241 274.701 210.828 1.00 3.21  ? 4263 ARG A O     1 
ATOM   20763 C  CB    . ARG A 1 4263 ? 165.281 275.482 213.277 1.00 3.58  ? 4263 ARG A CB    1 
ATOM   20764 C  CG    . ARG A 1 4263 ? 164.544 276.751 212.892 1.00 4.91  ? 4263 ARG A CG    1 
ATOM   20765 C  CD    . ARG A 1 4263 ? 165.190 277.968 213.516 1.00 7.17  ? 4263 ARG A CD    1 
ATOM   20766 N  NE    . ARG A 1 4263 ? 166.554 278.165 213.043 1.00 6.61  ? 4263 ARG A NE    1 
ATOM   20767 C  CZ    . ARG A 1 4263 ? 167.365 279.117 213.479 1.00 10.34 ? 4263 ARG A CZ    1 
ATOM   20768 N  NH1   . ARG A 1 4263 ? 167.021 279.915 214.477 1.00 7.83  ? 4263 ARG A NH1   1 
ATOM   20769 N  NH2   . ARG A 1 4263 ? 168.549 279.278 212.898 1.00 9.08  ? 4263 ARG A NH2   1 
ATOM   20770 N  N     . LEU A 1 4264 ? 165.398 274.275 210.345 1.00 1.23  ? 4264 LEU A N     1 
ATOM   20771 C  CA    . LEU A 1 4264 ? 165.191 274.388 208.906 1.00 0.91  ? 4264 LEU A CA    1 
ATOM   20772 C  C     . LEU A 1 4264 ? 164.249 273.302 208.403 1.00 1.35  ? 4264 LEU A C     1 
ATOM   20773 O  O     . LEU A 1 4264 ? 163.358 273.565 207.588 1.00 1.30  ? 4264 LEU A O     1 
ATOM   20774 C  CB    . LEU A 1 4264 ? 166.536 274.318 208.187 1.00 2.38  ? 4264 LEU A CB    1 
ATOM   20775 C  CG    . LEU A 1 4264 ? 166.497 274.486 206.672 1.00 1.31  ? 4264 LEU A CG    1 
ATOM   20776 C  CD1   . LEU A 1 4264 ? 165.933 275.842 206.329 1.00 0.90  ? 4264 LEU A CD1   1 
ATOM   20777 C  CD2   . LEU A 1 4264 ? 167.885 274.314 206.095 1.00 0.88  ? 4264 LEU A CD2   1 
ATOM   20778 N  N     . LEU A 1 4265 ? 164.431 272.073 208.888 1.00 1.92  ? 4265 LEU A N     1 
ATOM   20779 C  CA    . LEU A 1 4265 ? 163.528 270.986 208.523 1.00 0.73  ? 4265 LEU A CA    1 
ATOM   20780 C  C     . LEU A 1 4265 ? 162.106 271.273 208.994 1.00 1.00  ? 4265 LEU A C     1 
ATOM   20781 O  O     . LEU A 1 4265 ? 161.141 271.004 208.270 1.00 0.96  ? 4265 LEU A O     1 
ATOM   20782 C  CB    . LEU A 1 4265 ? 164.037 269.672 209.110 1.00 0.43  ? 4265 LEU A CB    1 
ATOM   20783 C  CG    . LEU A 1 4265 ? 163.179 268.427 208.891 1.00 0.71  ? 4265 LEU A CG    1 
ATOM   20784 C  CD1   . LEU A 1 4265 ? 163.095 268.094 207.413 1.00 1.08  ? 4265 LEU A CD1   1 
ATOM   20785 C  CD2   . LEU A 1 4265 ? 163.733 267.255 209.679 1.00 0.56  ? 4265 LEU A CD2   1 
ATOM   20786 N  N     . ASN A 1 4266 ? 161.960 271.819 210.203 1.00 0.89  ? 4266 ASN A N     1 
ATOM   20787 C  CA    . ASN A 1 4266 ? 160.636 272.173 210.704 1.00 1.56  ? 4266 ASN A CA    1 
ATOM   20788 C  C     . ASN A 1 4266 ? 160.003 273.278 209.870 1.00 1.54  ? 4266 ASN A C     1 
ATOM   20789 O  O     . ASN A 1 4266 ? 158.789 273.269 209.642 1.00 2.55  ? 4266 ASN A O     1 
ATOM   20790 C  CB    . ASN A 1 4266 ? 160.722 272.601 212.170 1.00 2.06  ? 4266 ASN A CB    1 
ATOM   20791 C  CG    . ASN A 1 4266 ? 160.956 271.437 213.104 1.00 2.71  ? 4266 ASN A CG    1 
ATOM   20792 O  OD1   . ASN A 1 4266 ? 160.340 270.384 212.964 1.00 8.52  ? 4266 ASN A OD1   1 
ATOM   20793 N  ND2   . ASN A 1 4266 ? 161.847 271.621 214.070 1.00 3.13  ? 4266 ASN A ND2   1 
ATOM   20794 N  N     . THR A 1 4267 ? 160.808 274.241 209.421 1.00 1.97  ? 4267 THR A N     1 
ATOM   20795 C  CA    . THR A 1 4267 ? 160.277 275.371 208.664 1.00 1.80  ? 4267 THR A CA    1 
ATOM   20796 C  C     . THR A 1 4267 ? 159.648 274.914 207.352 1.00 1.61  ? 4267 THR A C     1 
ATOM   20797 O  O     . THR A 1 4267 ? 158.548 275.351 206.995 1.00 3.93  ? 4267 THR A O     1 
ATOM   20798 C  CB    . THR A 1 4267 ? 161.388 276.392 208.410 1.00 3.07  ? 4267 THR A CB    1 
ATOM   20799 O  OG1   . THR A 1 4267 ? 161.857 276.908 209.660 1.00 5.34  ? 4267 THR A OG1   1 
ATOM   20800 C  CG2   . THR A 1 4267 ? 160.880 277.544 207.558 1.00 4.91  ? 4267 THR A CG2   1 
ATOM   20801 N  N     . PHE A 1 4268 ? 160.326 274.024 206.624 1.00 1.61  ? 4268 PHE A N     1 
ATOM   20802 C  CA    . PHE A 1 4268 ? 159.777 273.526 205.367 1.00 1.51  ? 4268 PHE A CA    1 
ATOM   20803 C  C     . PHE A 1 4268 ? 158.516 272.705 205.601 1.00 1.83  ? 4268 PHE A C     1 
ATOM   20804 O  O     . PHE A 1 4268 ? 157.522 272.853 204.881 1.00 3.49  ? 4268 PHE A O     1 
ATOM   20805 C  CB    . PHE A 1 4268 ? 160.821 272.696 204.619 1.00 1.06  ? 4268 PHE A CB    1 
ATOM   20806 C  CG    . PHE A 1 4268 ? 161.817 273.519 203.860 1.00 3.02  ? 4268 PHE A CG    1 
ATOM   20807 C  CD1   . PHE A 1 4268 ? 161.493 274.049 202.623 1.00 3.47  ? 4268 PHE A CD1   1 
ATOM   20808 C  CD2   . PHE A 1 4268 ? 163.084 273.740 204.366 1.00 4.21  ? 4268 PHE A CD2   1 
ATOM   20809 C  CE1   . PHE A 1 4268 ? 162.408 274.805 201.919 1.00 4.70  ? 4268 PHE A CE1   1 
ATOM   20810 C  CE2   . PHE A 1 4268 ? 164.004 274.492 203.661 1.00 3.03  ? 4268 PHE A CE2   1 
ATOM   20811 C  CZ    . PHE A 1 4268 ? 163.666 275.024 202.438 1.00 3.05  ? 4268 PHE A CZ    1 
ATOM   20812 N  N     . LEU A 1 4269 ? 158.541 271.827 206.607 1.00 2.01  ? 4269 LEU A N     1 
ATOM   20813 C  CA    . LEU A 1 4269 ? 157.379 270.990 206.886 1.00 1.46  ? 4269 LEU A CA    1 
ATOM   20814 C  C     . LEU A 1 4269 ? 156.180 271.832 207.295 1.00 2.08  ? 4269 LEU A C     1 
ATOM   20815 O  O     . LEU A 1 4269 ? 155.044 271.543 206.901 1.00 3.06  ? 4269 LEU A O     1 
ATOM   20816 C  CB    . LEU A 1 4269 ? 157.714 269.968 207.972 1.00 1.31  ? 4269 LEU A CB    1 
ATOM   20817 C  CG    . LEU A 1 4269 ? 158.647 268.822 207.578 1.00 0.91  ? 4269 LEU A CG    1 
ATOM   20818 C  CD1   . LEU A 1 4269 ? 159.106 268.058 208.812 1.00 0.62  ? 4269 LEU A CD1   1 
ATOM   20819 C  CD2   . LEU A 1 4269 ? 157.968 267.889 206.588 1.00 0.58  ? 4269 LEU A CD2   1 
ATOM   20820 N  N     . GLU A 1 4270 ? 156.410 272.880 208.089 1.00 1.84  ? 4270 GLU A N     1 
ATOM   20821 C  CA    . GLU A 1 4270 ? 155.306 273.733 208.510 1.00 3.87  ? 4270 GLU A CA    1 
ATOM   20822 C  C     . GLU A 1 4270 ? 154.728 274.520 207.342 1.00 5.43  ? 4270 GLU A C     1 
ATOM   20823 O  O     . GLU A 1 4270 ? 153.520 274.766 207.304 1.00 7.28  ? 4270 GLU A O     1 
ATOM   20824 C  CB    . GLU A 1 4270 ? 155.764 274.681 209.618 1.00 4.77  ? 4270 GLU A CB    1 
ATOM   20825 C  CG    . GLU A 1 4270 ? 154.632 275.476 210.251 1.00 9.24  ? 4270 GLU A CG    1 
ATOM   20826 C  CD    . GLU A 1 4270 ? 153.446 274.602 210.617 1.00 17.04 ? 4270 GLU A CD    1 
ATOM   20827 O  OE1   . GLU A 1 4270 ? 153.621 273.669 211.428 1.00 17.50 ? 4270 GLU A OE1   1 
ATOM   20828 O  OE2   . GLU A 1 4270 ? 152.343 274.845 210.088 1.00 15.46 ? 4270 GLU A OE2   1 
ATOM   20829 N  N     . ARG A 1 4271 ? 155.562 274.920 206.382 1.00 6.77  ? 4271 ARG A N     1 
ATOM   20830 C  CA    . ARG A 1 4271 ? 155.084 275.671 205.231 1.00 5.24  ? 4271 ARG A CA    1 
ATOM   20831 C  C     . ARG A 1 4271 ? 154.368 274.812 204.199 1.00 5.04  ? 4271 ARG A C     1 
ATOM   20832 O  O     . ARG A 1 4271 ? 153.422 275.294 203.569 1.00 11.26 ? 4271 ARG A O     1 
ATOM   20833 C  CB    . ARG A 1 4271 ? 156.246 276.402 204.548 1.00 4.81  ? 4271 ARG A CB    1 
ATOM   20834 C  CG    . ARG A 1 4271 ? 155.790 277.444 203.539 1.00 5.58  ? 4271 ARG A CG    1 
ATOM   20835 C  CD    . ARG A 1 4271 ? 156.875 278.458 203.216 1.00 9.38  ? 4271 ARG A CD    1 
ATOM   20836 N  NE    . ARG A 1 4271 ? 158.175 277.862 202.935 1.00 17.30 ? 4271 ARG A NE    1 
ATOM   20837 C  CZ    . ARG A 1 4271 ? 158.433 277.022 201.940 1.00 14.43 ? 4271 ARG A CZ    1 
ATOM   20838 N  NH1   . ARG A 1 4271 ? 157.501 276.675 201.067 1.00 13.48 ? 4271 ARG A NH1   1 
ATOM   20839 N  NH2   . ARG A 1 4271 ? 159.660 276.533 201.806 1.00 13.19 ? 4271 ARG A NH2   1 
ATOM   20840 N  N     . LEU A 1 4272 ? 154.785 273.559 204.015 1.00 2.39  ? 4272 LEU A N     1 
ATOM   20841 C  CA    . LEU A 1 4272 ? 154.282 272.741 202.919 1.00 3.56  ? 4272 LEU A CA    1 
ATOM   20842 C  C     . LEU A 1 4272 ? 153.121 271.831 203.295 1.00 3.76  ? 4272 LEU A C     1 
ATOM   20843 O  O     . LEU A 1 4272 ? 152.346 271.456 202.410 1.00 4.27  ? 4272 LEU A O     1 
ATOM   20844 C  CB    . LEU A 1 4272 ? 155.409 271.880 202.334 1.00 2.44  ? 4272 LEU A CB    1 
ATOM   20845 C  CG    . LEU A 1 4272 ? 156.550 272.627 201.645 1.00 3.09  ? 4272 LEU A CG    1 
ATOM   20846 C  CD1   . LEU A 1 4272 ? 157.663 271.669 201.265 1.00 1.29  ? 4272 LEU A CD1   1 
ATOM   20847 C  CD2   . LEU A 1 4272 ? 156.032 273.363 200.421 1.00 4.44  ? 4272 LEU A CD2   1 
ATOM   20848 N  N     . PHE A 1 4273 ? 152.981 271.453 204.563 1.00 5.38  ? 4273 PHE A N     1 
ATOM   20849 C  CA    . PHE A 1 4273 ? 151.955 270.494 204.970 1.00 3.45  ? 4273 PHE A CA    1 
ATOM   20850 C  C     . PHE A 1 4273 ? 150.957 271.195 205.885 1.00 4.35  ? 4273 PHE A C     1 
ATOM   20851 O  O     . PHE A 1 4273 ? 151.031 271.096 207.111 1.00 8.91  ? 4273 PHE A O     1 
ATOM   20852 C  CB    . PHE A 1 4273 ? 152.601 269.273 205.640 1.00 2.75  ? 4273 PHE A CB    1 
ATOM   20853 C  CG    . PHE A 1 4273 ? 153.419 268.434 204.700 1.00 1.51  ? 4273 PHE A CG    1 
ATOM   20854 C  CD1   . PHE A 1 4273 ? 152.829 267.414 203.968 1.00 2.88  ? 4273 PHE A CD1   1 
ATOM   20855 C  CD2   . PHE A 1 4273 ? 154.770 268.673 204.531 1.00 2.48  ? 4273 PHE A CD2   1 
ATOM   20856 C  CE1   . PHE A 1 4273 ? 153.575 266.646 203.093 1.00 1.17  ? 4273 PHE A CE1   1 
ATOM   20857 C  CE2   . PHE A 1 4273 ? 155.523 267.909 203.658 1.00 3.80  ? 4273 PHE A CE2   1 
ATOM   20858 C  CZ    . PHE A 1 4273 ? 154.924 266.893 202.939 1.00 1.03  ? 4273 PHE A CZ    1 
ATOM   20859 N  N     . THR A 1 4274 ? 150.002 271.892 205.269 1.00 4.53  ? 4274 THR A N     1 
ATOM   20860 C  CA    . THR A 1 4274 ? 148.888 272.535 205.953 1.00 3.13  ? 4274 THR A CA    1 
ATOM   20861 C  C     . THR A 1 4274 ? 147.654 272.411 205.072 1.00 7.42  ? 4274 THR A C     1 
ATOM   20862 O  O     . THR A 1 4274 ? 147.706 271.867 203.966 1.00 17.08 ? 4274 THR A O     1 
ATOM   20863 C  CB    . THR A 1 4274 ? 149.150 274.021 206.252 1.00 7.72  ? 4274 THR A CB    1 
ATOM   20864 O  OG1   . THR A 1 4274 ? 149.155 274.765 205.026 1.00 17.71 ? 4274 THR A OG1   1 
ATOM   20865 C  CG2   . THR A 1 4274 ? 150.461 274.232 206.981 1.00 7.45  ? 4274 THR A CG2   1 
ATOM   20866 N  N     . THR A 1 4275 ? 146.533 272.938 205.565 1.00 11.24 ? 4275 THR A N     1 
ATOM   20867 C  CA    . THR A 1 4275 ? 145.333 273.025 204.741 1.00 11.32 ? 4275 THR A CA    1 
ATOM   20868 C  C     . THR A 1 4275 ? 145.495 274.023 203.599 1.00 14.59 ? 4275 THR A C     1 
ATOM   20869 O  O     . THR A 1 4275 ? 144.820 273.889 202.574 1.00 18.69 ? 4275 THR A O     1 
ATOM   20870 C  CB    . THR A 1 4275 ? 144.129 273.403 205.606 1.00 12.04 ? 4275 THR A CB    1 
ATOM   20871 O  OG1   . THR A 1 4275 ? 144.170 272.663 206.831 1.00 13.10 ? 4275 THR A OG1   1 
ATOM   20872 C  CG2   . THR A 1 4275 ? 142.835 273.077 204.884 1.00 13.90 ? 4275 THR A CG2   1 
ATOM   20873 N  N     . ARG A 1 4276 ? 146.379 275.013 203.750 1.00 11.07 ? 4276 ARG A N     1 
ATOM   20874 C  CA    . ARG A 1 4276 ? 146.596 275.999 202.696 1.00 14.66 ? 4276 ARG A CA    1 
ATOM   20875 C  C     . ARG A 1 4276 ? 147.195 275.389 201.438 1.00 11.72 ? 4276 ARG A C     1 
ATOM   20876 O  O     . ARG A 1 4276 ? 147.094 275.991 200.365 1.00 12.55 ? 4276 ARG A O     1 
ATOM   20877 C  CB    . ARG A 1 4276 ? 147.497 277.125 203.205 1.00 10.88 ? 4276 ARG A CB    1 
ATOM   20878 C  CG    . ARG A 1 4276 ? 146.914 277.924 204.361 1.00 15.80 ? 4276 ARG A CG    1 
ATOM   20879 C  CD    . ARG A 1 4276 ? 145.820 278.887 203.908 1.00 18.05 ? 4276 ARG A CD    1 
ATOM   20880 N  NE    . ARG A 1 4276 ? 144.573 278.202 203.588 1.00 22.18 ? 4276 ARG A NE    1 
ATOM   20881 C  CZ    . ARG A 1 4276 ? 143.707 277.755 204.487 1.00 26.16 ? 4276 ARG A CZ    1 
ATOM   20882 N  NH1   . ARG A 1 4276 ? 143.908 277.925 205.784 1.00 22.43 ? 4276 ARG A NH1   1 
ATOM   20883 N  NH2   . ARG A 1 4276 ? 142.616 277.116 204.075 1.00 24.42 ? 4276 ARG A NH2   1 
ATOM   20884 N  N     . SER A 1 4277 ? 147.815 274.211 201.542 1.00 14.23 ? 4277 SER A N     1 
ATOM   20885 C  CA    . SER A 1 4277 ? 148.371 273.556 200.366 1.00 11.18 ? 4277 SER A CA    1 
ATOM   20886 C  C     . SER A 1 4277 ? 147.296 273.148 199.371 1.00 10.83 ? 4277 SER A C     1 
ATOM   20887 O  O     . SER A 1 4277 ? 147.601 272.953 198.190 1.00 17.47 ? 4277 SER A O     1 
ATOM   20888 C  CB    . SER A 1 4277 ? 149.186 272.333 200.783 1.00 10.92 ? 4277 SER A CB    1 
ATOM   20889 O  OG    . SER A 1 4277 ? 150.412 272.718 201.373 1.00 14.06 ? 4277 SER A OG    1 
ATOM   20890 N  N     . PHE A 1 4278 ? 146.052 273.012 199.818 1.00 10.88 ? 4278 PHE A N     1 
ATOM   20891 C  CA    . PHE A 1 4278 ? 144.939 272.662 198.950 1.00 11.00 ? 4278 PHE A CA    1 
ATOM   20892 C  C     . PHE A 1 4278 ? 144.203 273.883 198.412 1.00 16.41 ? 4278 PHE A C     1 
ATOM   20893 O  O     . PHE A 1 4278 ? 143.221 273.722 197.681 1.00 15.03 ? 4278 PHE A O     1 
ATOM   20894 C  CB    . PHE A 1 4278 ? 143.962 271.747 199.694 1.00 10.09 ? 4278 PHE A CB    1 
ATOM   20895 C  CG    . PHE A 1 4278 ? 144.398 270.313 199.739 1.00 7.94  ? 4278 PHE A CG    1 
ATOM   20896 C  CD1   . PHE A 1 4278 ? 145.478 269.927 200.513 1.00 11.65 ? 4278 PHE A CD1   1 
ATOM   20897 C  CD2   . PHE A 1 4278 ? 143.731 269.350 199.002 1.00 8.42  ? 4278 PHE A CD2   1 
ATOM   20898 C  CE1   . PHE A 1 4278 ? 145.884 268.612 200.551 1.00 7.73  ? 4278 PHE A CE1   1 
ATOM   20899 C  CE2   . PHE A 1 4278 ? 144.136 268.033 199.038 1.00 7.43  ? 4278 PHE A CE2   1 
ATOM   20900 C  CZ    . PHE A 1 4278 ? 145.212 267.664 199.814 1.00 9.65  ? 4278 PHE A CZ    1 
ATOM   20901 N  N     . ASP A 1 4279 ? 144.650 275.086 198.755 1.00 17.15 ? 4279 ASP A N     1 
ATOM   20902 C  CA    . ASP A 1 4279 ? 144.077 276.299 198.196 1.00 17.44 ? 4279 ASP A CA    1 
ATOM   20903 C  C     . ASP A 1 4279 ? 144.551 276.505 196.762 1.00 26.93 ? 4279 ASP A C     1 
ATOM   20904 O  O     . ASP A 1 4279 ? 145.582 275.975 196.334 1.00 27.20 ? 4279 ASP A O     1 
ATOM   20905 C  CB    . ASP A 1 4279 ? 144.443 277.517 199.043 1.00 16.47 ? 4279 ASP A CB    1 
ATOM   20906 C  CG    . ASP A 1 4279 ? 143.967 277.396 200.474 1.00 18.30 ? 4279 ASP A CG    1 
ATOM   20907 O  OD1   . ASP A 1 4279 ? 143.419 276.335 200.834 1.00 23.40 ? 4279 ASP A OD1   1 
ATOM   20908 O  OD2   . ASP A 1 4279 ? 144.133 278.370 201.234 1.00 19.49 ? 4279 ASP A OD2   1 
ATOM   20909 N  N     . SER A 1 4280 ? 143.772 277.291 196.015 1.00 27.58 ? 4280 SER A N     1 
ATOM   20910 C  CA    . SER A 1 4280 ? 144.081 277.527 194.609 1.00 23.00 ? 4280 SER A CA    1 
ATOM   20911 C  C     . SER A 1 4280 ? 145.391 278.288 194.440 1.00 28.81 ? 4280 SER A C     1 
ATOM   20912 O  O     . SER A 1 4280 ? 146.171 277.996 193.527 1.00 32.57 ? 4280 SER A O     1 
ATOM   20913 C  CB    . SER A 1 4280 ? 142.933 278.288 193.945 1.00 27.86 ? 4280 SER A CB    1 
ATOM   20914 O  OG    . SER A 1 4280 ? 141.710 277.589 194.081 1.00 33.83 ? 4280 SER A OG    1 
ATOM   20915 N  N     . GLU A 1 4281 ? 145.653 279.269 195.306 1.00 25.73 ? 4281 GLU A N     1 
ATOM   20916 C  CA    . GLU A 1 4281 ? 146.791 280.167 195.154 1.00 27.49 ? 4281 GLU A CA    1 
ATOM   20917 C  C     . GLU A 1 4281 ? 147.957 279.808 196.074 1.00 23.05 ? 4281 GLU A C     1 
ATOM   20918 O  O     . GLU A 1 4281 ? 148.732 280.691 196.457 1.00 18.08 ? 4281 GLU A O     1 
ATOM   20919 C  CB    . GLU A 1 4281 ? 146.360 281.613 195.394 1.00 26.68 ? 4281 GLU A CB    1 
ATOM   20920 C  CG    . GLU A 1 4281 ? 145.339 282.131 194.394 1.00 31.28 ? 4281 GLU A CG    1 
ATOM   20921 C  CD    . GLU A 1 4281 ? 145.802 281.972 192.961 1.00 38.71 ? 4281 GLU A CD    1 
ATOM   20922 O  OE1   . GLU A 1 4281 ? 146.859 282.536 192.611 1.00 37.79 ? 4281 GLU A OE1   1 
ATOM   20923 O  OE2   . GLU A 1 4281 ? 145.106 281.284 192.184 1.00 44.44 ? 4281 GLU A OE2   1 
ATOM   20924 N  N     . PHE A 1 4282 ? 148.098 278.535 196.436 1.00 18.68 ? 4282 PHE A N     1 
ATOM   20925 C  CA    . PHE A 1 4282 ? 149.224 278.121 197.262 1.00 12.00 ? 4282 PHE A CA    1 
ATOM   20926 C  C     . PHE A 1 4282 ? 150.534 278.301 196.504 1.00 14.61 ? 4282 PHE A C     1 
ATOM   20927 O  O     . PHE A 1 4282 ? 150.600 278.101 195.288 1.00 14.37 ? 4282 PHE A O     1 
ATOM   20928 C  CB    . PHE A 1 4282 ? 149.063 276.668 197.704 1.00 11.30 ? 4282 PHE A CB    1 
ATOM   20929 C  CG    . PHE A 1 4282 ? 150.127 276.206 198.655 1.00 8.40  ? 4282 PHE A CG    1 
ATOM   20930 C  CD1   . PHE A 1 4282 ? 150.333 276.864 199.855 1.00 9.92  ? 4282 PHE A CD1   1 
ATOM   20931 C  CD2   . PHE A 1 4282 ? 150.924 275.119 198.348 1.00 10.27 ? 4282 PHE A CD2   1 
ATOM   20932 C  CE1   . PHE A 1 4282 ? 151.312 276.447 200.731 1.00 10.53 ? 4282 PHE A CE1   1 
ATOM   20933 C  CE2   . PHE A 1 4282 ? 151.906 274.694 199.222 1.00 11.19 ? 4282 PHE A CE2   1 
ATOM   20934 C  CZ    . PHE A 1 4282 ? 152.099 275.361 200.415 1.00 15.93 ? 4282 PHE A CZ    1 
ATOM   20935 N  N     . LYS A 1 4283 ? 151.584 278.673 197.231 1.00 15.15 ? 4283 LYS A N     1 
ATOM   20936 C  CA    . LYS A 1 4283 ? 152.836 279.128 196.635 1.00 12.01 ? 4283 LYS A CA    1 
ATOM   20937 C  C     . LYS A 1 4283 ? 153.967 278.245 197.147 1.00 10.21 ? 4283 LYS A C     1 
ATOM   20938 O  O     . LYS A 1 4283 ? 154.395 278.386 198.297 1.00 19.43 ? 4283 LYS A O     1 
ATOM   20939 C  CB    . LYS A 1 4283 ? 153.076 280.596 196.982 1.00 16.10 ? 4283 LYS A CB    1 
ATOM   20940 C  CG    . LYS A 1 4283 ? 152.563 281.563 195.932 1.00 17.25 ? 4283 LYS A CG    1 
ATOM   20941 C  CD    . LYS A 1 4283 ? 152.824 283.004 196.321 1.00 22.21 ? 4283 LYS A CD    1 
ATOM   20942 C  CE    . LYS A 1 4283 ? 152.467 283.948 195.188 1.00 25.92 ? 4283 LYS A CE    1 
ATOM   20943 N  NZ    . LYS A 1 4283 ? 153.131 285.270 195.332 1.00 26.57 ? 4283 LYS A NZ    1 
ATOM   20944 N  N     . LEU A 1 4284 ? 154.447 277.331 196.298 1.00 9.81  ? 4284 LEU A N     1 
ATOM   20945 C  CA    . LEU A 1 4284 ? 155.531 276.441 196.704 1.00 10.73 ? 4284 LEU A CA    1 
ATOM   20946 C  C     . LEU A 1 4284 ? 156.818 277.214 196.971 1.00 10.74 ? 4284 LEU A C     1 
ATOM   20947 O  O     . LEU A 1 4284 ? 157.522 276.938 197.948 1.00 9.46  ? 4284 LEU A O     1 
ATOM   20948 C  CB    . LEU A 1 4284 ? 155.758 275.366 195.642 1.00 4.27  ? 4284 LEU A CB    1 
ATOM   20949 C  CG    . LEU A 1 4284 ? 154.640 274.332 195.494 1.00 5.98  ? 4284 LEU A CG    1 
ATOM   20950 C  CD1   . LEU A 1 4284 ? 154.545 273.831 194.062 1.00 5.88  ? 4284 LEU A CD1   1 
ATOM   20951 C  CD2   . LEU A 1 4284 ? 154.843 273.177 196.459 1.00 4.71  ? 4284 LEU A CD2   1 
ATOM   20952 N  N     . ALA A 1 4285 ? 157.140 278.177 196.113 1.00 10.43 ? 4285 ALA A N     1 
ATOM   20953 C  CA    . ALA A 1 4285 ? 158.299 279.037 196.298 1.00 7.58  ? 4285 ALA A CA    1 
ATOM   20954 C  C     . ALA A 1 4285 ? 157.917 280.456 195.909 1.00 14.45 ? 4285 ALA A C     1 
ATOM   20955 O  O     . ALA A 1 4285 ? 157.065 280.665 195.041 1.00 17.43 ? 4285 ALA A O     1 
ATOM   20956 C  CB    . ALA A 1 4285 ? 159.500 278.556 195.475 1.00 5.29  ? 4285 ALA A CB    1 
ATOM   20957 N  N     . CYS A 1 4286 ? 158.550 281.430 196.558 1.00 13.94 ? 4286 CYS A N     1 
ATOM   20958 C  CA    . CYS A 1 4286 ? 158.197 282.837 196.398 1.00 20.94 ? 4286 CYS A CA    1 
ATOM   20959 C  C     . CYS A 1 4286 ? 159.387 283.614 195.852 1.00 19.02 ? 4286 CYS A C     1 
ATOM   20960 O  O     . CYS A 1 4286 ? 160.469 283.596 196.445 1.00 16.18 ? 4286 CYS A O     1 
ATOM   20961 C  CB    . CYS A 1 4286 ? 157.730 283.434 197.728 1.00 23.30 ? 4286 CYS A CB    1 
ATOM   20962 S  SG    . CYS A 1 4286 ? 156.214 282.705 198.379 1.00 47.31 ? 4286 CYS A SG    1 
ATOM   20963 N  N     . LYS A 1 4287 ? 159.173 284.300 194.725 1.00 25.76 ? 4287 LYS A N     1 
ATOM   20964 C  CA    . LYS A 1 4287 ? 160.144 285.222 194.133 1.00 26.89 ? 4287 LYS A CA    1 
ATOM   20965 C  C     . LYS A 1 4287 ? 161.478 284.526 193.856 1.00 25.41 ? 4287 LYS A C     1 
ATOM   20966 O  O     . LYS A 1 4287 ? 162.514 284.837 194.446 1.00 25.56 ? 4287 LYS A O     1 
ATOM   20967 C  CB    . LYS A 1 4287 ? 160.332 286.460 195.020 1.00 28.33 ? 4287 LYS A CB    1 
ATOM   20968 C  CG    . LYS A 1 4287 ? 159.389 287.618 194.702 1.00 30.47 ? 4287 LYS A CG    1 
ATOM   20969 C  CD    . LYS A 1 4287 ? 157.924 287.219 194.799 1.00 30.63 ? 4287 LYS A CD    1 
ATOM   20970 C  CE    . LYS A 1 4287 ? 157.530 286.885 196.230 1.00 29.36 ? 4287 LYS A CE    1 
ATOM   20971 N  NZ    . LYS A 1 4287 ? 156.101 286.474 196.328 1.00 33.20 ? 4287 LYS A NZ    1 
ATOM   20972 N  N     . VAL A 1 4288 ? 161.430 283.557 192.941 1.00 22.89 ? 4288 VAL A N     1 
ATOM   20973 C  CA    . VAL A 1 4288 ? 162.638 282.827 192.574 1.00 20.28 ? 4288 VAL A CA    1 
ATOM   20974 C  C     . VAL A 1 4288 ? 163.582 283.718 191.771 1.00 26.71 ? 4288 VAL A C     1 
ATOM   20975 O  O     . VAL A 1 4288 ? 164.788 283.769 192.036 1.00 24.48 ? 4288 VAL A O     1 
ATOM   20976 C  CB    . VAL A 1 4288 ? 162.273 281.539 191.810 1.00 12.31 ? 4288 VAL A CB    1 
ATOM   20977 C  CG1   . VAL A 1 4288 ? 161.718 280.506 192.771 1.00 12.64 ? 4288 VAL A CG1   1 
ATOM   20978 C  CG2   . VAL A 1 4288 ? 161.256 281.831 190.719 1.00 19.22 ? 4288 VAL A CG2   1 
ATOM   20979 N  N     . ASP A 1 4289 ? 163.048 284.443 190.789 1.00 26.22 ? 4289 ASP A N     1 
ATOM   20980 C  CA    . ASP A 1 4289 ? 163.834 285.351 189.966 1.00 26.31 ? 4289 ASP A CA    1 
ATOM   20981 C  C     . ASP A 1 4289 ? 163.545 286.816 190.278 1.00 24.89 ? 4289 ASP A C     1 
ATOM   20982 O  O     . ASP A 1 4289 ? 163.787 287.683 189.432 1.00 31.91 ? 4289 ASP A O     1 
ATOM   20983 C  CB    . ASP A 1 4289 ? 163.602 285.058 188.482 1.00 28.49 ? 4289 ASP A CB    1 
ATOM   20984 C  CG    . ASP A 1 4289 ? 162.157 285.261 188.059 1.00 32.24 ? 4289 ASP A CG    1 
ATOM   20985 O  OD1   . ASP A 1 4289 ? 161.310 285.586 188.915 1.00 34.55 ? 4289 ASP A OD1   1 
ATOM   20986 O  OD2   . ASP A 1 4289 ? 161.867 285.092 186.856 1.00 36.54 ? 4289 ASP A OD2   1 
ATOM   20987 N  N     . GLY A 1 4290 ? 163.028 287.102 191.470 1.00 28.18 ? 4290 GLY A N     1 
ATOM   20988 C  CA    . GLY A 1 4290 ? 162.663 288.439 191.867 1.00 29.17 ? 4290 GLY A CA    1 
ATOM   20989 C  C     . GLY A 1 4290 ? 161.228 288.817 191.563 1.00 35.89 ? 4290 GLY A C     1 
ATOM   20990 O  O     . GLY A 1 4290 ? 160.607 289.541 192.349 1.00 37.64 ? 4290 GLY A O     1 
ATOM   20991 N  N     . HIS A 1 4291 ? 160.684 288.347 190.440 1.00 32.69 ? 4291 HIS A N     1 
ATOM   20992 C  CA    . HIS A 1 4291 ? 159.319 288.664 190.045 1.00 36.28 ? 4291 HIS A CA    1 
ATOM   20993 C  C     . HIS A 1 4291 ? 158.434 287.431 189.963 1.00 35.85 ? 4291 HIS A C     1 
ATOM   20994 O  O     . HIS A 1 4291 ? 157.374 287.390 190.600 1.00 35.80 ? 4291 HIS A O     1 
ATOM   20995 C  CB    . HIS A 1 4291 ? 159.321 289.397 188.694 1.00 29.59 ? 4291 HIS A CB    1 
ATOM   20996 C  CG    . HIS A 1 4291 ? 159.975 290.742 188.740 1.00 36.37 ? 4291 HIS A CG    1 
ATOM   20997 N  ND1   . HIS A 1 4291 ? 161.325 290.920 188.531 1.00 36.74 ? 4291 HIS A ND1   1 
ATOM   20998 C  CD2   . HIS A 1 4291 ? 159.464 291.975 188.968 1.00 40.94 ? 4291 HIS A CD2   1 
ATOM   20999 C  CE1   . HIS A 1 4291 ? 161.619 292.204 188.628 1.00 36.14 ? 4291 HIS A CE1   1 
ATOM   21000 N  NE2   . HIS A 1 4291 ? 160.508 292.866 188.893 1.00 42.03 ? 4291 HIS A NE2   1 
ATOM   21001 N  N     . LYS A 1 4292 ? 158.841 286.420 189.202 1.00 30.98 ? 4292 LYS A N     1 
ATOM   21002 C  CA    . LYS A 1 4292 ? 158.043 285.212 189.051 1.00 28.10 ? 4292 LYS A CA    1 
ATOM   21003 C  C     . LYS A 1 4292 ? 158.251 284.285 190.239 1.00 27.86 ? 4292 LYS A C     1 
ATOM   21004 O  O     . LYS A 1 4292 ? 159.231 284.409 190.979 1.00 28.23 ? 4292 LYS A O     1 
ATOM   21005 C  CB    . LYS A 1 4292 ? 158.405 284.489 187.754 1.00 29.88 ? 4292 LYS A CB    1 
ATOM   21006 C  CG    . LYS A 1 4292 ? 158.377 285.370 186.518 1.00 32.05 ? 4292 LYS A CG    1 
ATOM   21007 C  CD    . LYS A 1 4292 ? 158.805 284.594 185.281 1.00 34.72 ? 4292 LYS A CD    1 
ATOM   21008 C  CE    . LYS A 1 4292 ? 159.090 285.525 184.113 1.00 36.07 ? 4292 LYS A CE    1 
ATOM   21009 N  NZ    . LYS A 1 4292 ? 160.183 286.488 184.422 1.00 34.05 ? 4292 LYS A NZ    1 
ATOM   21010 N  N     . ASP A 1 4293 ? 157.318 283.355 190.422 1.00 26.20 ? 4293 ASP A N     1 
ATOM   21011 C  CA    . ASP A 1 4293 ? 157.402 282.368 191.486 1.00 20.61 ? 4293 ASP A CA    1 
ATOM   21012 C  C     . ASP A 1 4293 ? 156.594 281.128 191.129 1.00 19.63 ? 4293 ASP A C     1 
ATOM   21013 O  O     . ASP A 1 4293 ? 155.798 281.133 190.184 1.00 22.96 ? 4293 ASP A O     1 
ATOM   21014 C  CB    . ASP A 1 4293 ? 156.983 282.982 192.843 1.00 21.83 ? 4293 ASP A CB    1 
ATOM   21015 C  CG    . ASP A 1 4293 ? 155.491 283.260 192.960 1.00 22.30 ? 4293 ASP A CG    1 
ATOM   21016 O  OD1   . ASP A 1 4293 ? 154.659 282.658 192.256 1.00 27.94 ? 4293 ASP A OD1   1 
ATOM   21017 O  OD2   . ASP A 1 4293 ? 155.152 284.128 193.785 1.00 24.31 ? 4293 ASP A OD2   1 
ATOM   21018 N  N     . ILE A 1 4294 ? 156.816 280.062 191.888 1.00 16.45 ? 4294 ILE A N     1 
ATOM   21019 C  CA    . ILE A 1 4294 ? 156.290 278.747 191.542 1.00 12.10 ? 4294 ILE A CA    1 
ATOM   21020 C  C     . ILE A 1 4294 ? 154.957 278.534 192.245 1.00 13.31 ? 4294 ILE A C     1 
ATOM   21021 O  O     . ILE A 1 4294 ? 154.875 278.578 193.477 1.00 15.59 ? 4294 ILE A O     1 
ATOM   21022 C  CB    . ILE A 1 4294 ? 157.303 277.652 191.911 1.00 8.30  ? 4294 ILE A CB    1 
ATOM   21023 C  CG1   . ILE A 1 4294 ? 158.667 277.986 191.305 1.00 12.29 ? 4294 ILE A CG1   1 
ATOM   21024 C  CG2   . ILE A 1 4294 ? 156.819 276.295 191.436 1.00 7.68  ? 4294 ILE A CG2   1 
ATOM   21025 C  CD1   . ILE A 1 4294 ? 159.744 276.975 191.600 1.00 7.55  ? 4294 ILE A CD1   1 
ATOM   21026 N  N     . GLN A 1 4295 ? 153.910 278.294 191.460 1.00 15.18 ? 4295 GLN A N     1 
ATOM   21027 C  CA    . GLN A 1 4295 ? 152.560 278.107 191.973 1.00 13.39 ? 4295 GLN A CA    1 
ATOM   21028 C  C     . GLN A 1 4295 ? 152.260 276.631 192.184 1.00 9.27  ? 4295 GLN A C     1 
ATOM   21029 O  O     . GLN A 1 4295 ? 152.788 275.761 191.488 1.00 15.15 ? 4295 GLN A O     1 
ATOM   21030 C  CB    . GLN A 1 4295 ? 151.522 278.704 191.018 1.00 14.17 ? 4295 GLN A CB    1 
ATOM   21031 C  CG    . GLN A 1 4295 ? 151.592 280.209 190.864 1.00 17.58 ? 4295 GLN A CG    1 
ATOM   21032 C  CD    . GLN A 1 4295 ? 151.320 280.939 192.163 1.00 24.26 ? 4295 GLN A CD    1 
ATOM   21033 O  OE1   . GLN A 1 4295 ? 152.221 281.523 192.758 1.00 28.18 ? 4295 GLN A OE1   1 
ATOM   21034 N  NE2   . GLN A 1 4295 ? 150.069 280.916 192.608 1.00 23.07 ? 4295 GLN A NE2   1 
ATOM   21035 N  N     . MET A 1 4296 ? 151.404 276.361 193.154 1.00 12.50 ? 4296 MET A N     1 
ATOM   21036 C  CA    . MET A 1 4296 ? 150.951 275.000 193.407 1.00 11.51 ? 4296 MET A CA    1 
ATOM   21037 C  C     . MET A 1 4296 ? 149.972 274.573 192.321 1.00 11.43 ? 4296 MET A C     1 
ATOM   21038 O  O     . MET A 1 4296 ? 148.987 275.275 192.074 1.00 20.19 ? 4296 MET A O     1 
ATOM   21039 C  CB    . MET A 1 4296 ? 150.290 274.907 194.776 1.00 11.90 ? 4296 MET A CB    1 
ATOM   21040 C  CG    . MET A 1 4296 ? 149.773 273.530 195.124 1.00 12.79 ? 4296 MET A CG    1 
ATOM   21041 S  SD    . MET A 1 4296 ? 151.099 272.399 195.573 1.00 7.43  ? 4296 MET A SD    1 
ATOM   21042 C  CE    . MET A 1 4296 ? 150.176 271.129 196.424 1.00 9.99  ? 4296 MET A CE    1 
ATOM   21043 N  N     . PRO A 1 4297 ? 150.211 273.450 191.646 1.00 8.99  ? 4297 PRO A N     1 
ATOM   21044 C  CA    . PRO A 1 4297 ? 149.258 272.984 190.634 1.00 10.86 ? 4297 PRO A CA    1 
ATOM   21045 C  C     . PRO A 1 4297 ? 147.897 272.686 191.246 1.00 18.16 ? 4297 PRO A C     1 
ATOM   21046 O  O     . PRO A 1 4297 ? 147.796 272.184 192.367 1.00 22.82 ? 4297 PRO A O     1 
ATOM   21047 C  CB    . PRO A 1 4297 ? 149.915 271.713 190.081 1.00 6.08  ? 4297 PRO A CB    1 
ATOM   21048 C  CG    . PRO A 1 4297 ? 150.883 271.291 191.138 1.00 9.45  ? 4297 PRO A CG    1 
ATOM   21049 C  CD    . PRO A 1 4297 ? 151.366 272.548 191.787 1.00 7.00  ? 4297 PRO A CD    1 
ATOM   21050 N  N     . ASP A 1 4298 ? 146.848 273.003 190.496 1.00 19.04 ? 4298 ASP A N     1 
ATOM   21051 C  CA    . ASP A 1 4298 ? 145.475 272.770 190.937 1.00 20.39 ? 4298 ASP A CA    1 
ATOM   21052 C  C     . ASP A 1 4298 ? 144.952 271.411 190.473 1.00 20.58 ? 4298 ASP A C     1 
ATOM   21053 O  O     . ASP A 1 4298 ? 143.845 271.276 189.959 1.00 21.95 ? 4298 ASP A O     1 
ATOM   21054 C  CB    . ASP A 1 4298 ? 144.585 273.914 190.460 1.00 23.18 ? 4298 ASP A CB    1 
ATOM   21055 C  CG    . ASP A 1 4298 ? 144.426 273.951 188.948 1.00 31.98 ? 4298 ASP A CG    1 
ATOM   21056 O  OD1   . ASP A 1 4298 ? 145.287 274.560 188.280 1.00 31.33 ? 4298 ASP A OD1   1 
ATOM   21057 O  OD2   . ASP A 1 4298 ? 143.431 273.402 188.431 1.00 35.99 ? 4298 ASP A OD2   1 
ATOM   21058 N  N     . GLY A 1 4299 ? 145.749 270.372 190.705 1.00 17.69 ? 4299 GLY A N     1 
ATOM   21059 C  CA    . GLY A 1 4299 ? 145.385 269.039 190.280 1.00 21.52 ? 4299 GLY A CA    1 
ATOM   21060 C  C     . GLY A 1 4299 ? 144.725 268.224 191.379 1.00 23.45 ? 4299 GLY A C     1 
ATOM   21061 O  O     . GLY A 1 4299 ? 144.989 268.409 192.564 1.00 22.96 ? 4299 GLY A O     1 
ATOM   21062 N  N     . ILE A 1 4300 ? 143.844 267.318 190.961 1.00 18.77 ? 4300 ILE A N     1 
ATOM   21063 C  CA    . ILE A 1 4300 ? 143.222 266.347 191.850 1.00 14.02 ? 4300 ILE A CA    1 
ATOM   21064 C  C     . ILE A 1 4300 ? 143.601 264.918 191.501 1.00 19.80 ? 4300 ILE A C     1 
ATOM   21065 O  O     . ILE A 1 4300 ? 143.210 263.993 192.220 1.00 26.09 ? 4300 ILE A O     1 
ATOM   21066 C  CB    . ILE A 1 4300 ? 141.687 266.502 191.868 1.00 16.84 ? 4300 ILE A CB    1 
ATOM   21067 C  CG1   . ILE A 1 4300 ? 141.101 266.193 190.491 1.00 25.10 ? 4300 ILE A CG1   1 
ATOM   21068 C  CG2   . ILE A 1 4300 ? 141.298 267.900 192.321 1.00 20.39 ? 4300 ILE A CG2   1 
ATOM   21069 C  CD1   . ILE A 1 4300 ? 139.595 266.326 190.423 1.00 28.64 ? 4300 ILE A CD1   1 
ATOM   21070 N  N     . ARG A 1 4301 ? 144.351 264.709 190.421 1.00 16.29 ? 4301 ARG A N     1 
ATOM   21071 C  CA    . ARG A 1 4301 ? 144.765 263.385 189.985 1.00 17.02 ? 4301 ARG A CA    1 
ATOM   21072 C  C     . ARG A 1 4301 ? 146.273 263.372 189.781 1.00 15.53 ? 4301 ARG A C     1 
ATOM   21073 O  O     . ARG A 1 4301 ? 146.903 264.415 189.587 1.00 11.48 ? 4301 ARG A O     1 
ATOM   21074 C  CB    . ARG A 1 4301 ? 144.049 262.968 188.690 1.00 20.00 ? 4301 ARG A CB    1 
ATOM   21075 C  CG    . ARG A 1 4301 ? 142.539 262.850 188.827 1.00 22.40 ? 4301 ARG A CG    1 
ATOM   21076 C  CD    . ARG A 1 4301 ? 141.858 262.825 187.467 1.00 24.53 ? 4301 ARG A CD    1 
ATOM   21077 N  NE    . ARG A 1 4301 ? 141.977 264.102 186.772 1.00 29.73 ? 4301 ARG A NE    1 
ATOM   21078 C  CZ    . ARG A 1 4301 ? 142.592 264.266 185.609 1.00 29.78 ? 4301 ARG A CZ    1 
ATOM   21079 N  NH1   . ARG A 1 4301 ? 143.165 263.253 184.981 1.00 20.31 ? 4301 ARG A NH1   1 
ATOM   21080 N  NH2   . ARG A 1 4301 ? 142.635 265.477 185.064 1.00 32.23 ? 4301 ARG A NH2   1 
ATOM   21081 N  N     . ARG A 1 4302 ? 146.848 262.167 189.831 1.00 13.17 ? 4302 ARG A N     1 
ATOM   21082 C  CA    . ARG A 1 4302 ? 148.300 262.035 189.749 1.00 11.40 ? 4302 ARG A CA    1 
ATOM   21083 C  C     . ARG A 1 4302 ? 148.840 262.562 188.424 1.00 12.72 ? 4302 ARG A C     1 
ATOM   21084 O  O     . ARG A 1 4302 ? 149.857 263.264 188.397 1.00 17.05 ? 4302 ARG A O     1 
ATOM   21085 C  CB    . ARG A 1 4302 ? 148.708 260.577 189.939 1.00 11.76 ? 4302 ARG A CB    1 
ATOM   21086 C  CG    . ARG A 1 4302 ? 150.154 260.308 189.559 1.00 10.54 ? 4302 ARG A CG    1 
ATOM   21087 C  CD    . ARG A 1 4302 ? 150.509 258.839 189.661 1.00 13.28 ? 4302 ARG A CD    1 
ATOM   21088 N  NE    . ARG A 1 4302 ? 151.815 258.558 189.077 1.00 18.19 ? 4302 ARG A NE    1 
ATOM   21089 C  CZ    . ARG A 1 4302 ? 152.083 258.593 187.779 1.00 13.83 ? 4302 ARG A CZ    1 
ATOM   21090 N  NH1   . ARG A 1 4302 ? 151.143 258.854 186.886 1.00 11.03 ? 4302 ARG A NH1   1 
ATOM   21091 N  NH2   . ARG A 1 4302 ? 153.325 258.355 187.367 1.00 12.06 ? 4302 ARG A NH2   1 
ATOM   21092 N  N     . GLU A 1 4303 ? 148.170 262.235 187.317 1.00 17.50 ? 4303 GLU A N     1 
ATOM   21093 C  CA    . GLU A 1 4303 ? 148.670 262.622 186.000 1.00 13.85 ? 4303 GLU A CA    1 
ATOM   21094 C  C     . GLU A 1 4303 ? 148.749 264.134 185.845 1.00 16.44 ? 4303 GLU A C     1 
ATOM   21095 O  O     . GLU A 1 4303 ? 149.607 264.636 185.108 1.00 15.22 ? 4303 GLU A O     1 
ATOM   21096 C  CB    . GLU A 1 4303 ? 147.790 262.017 184.906 1.00 12.87 ? 4303 GLU A CB    1 
ATOM   21097 C  CG    . GLU A 1 4303 ? 146.303 262.232 185.113 1.00 20.97 ? 4303 GLU A CG    1 
ATOM   21098 C  CD    . GLU A 1 4303 ? 145.654 261.112 185.901 1.00 31.25 ? 4303 GLU A CD    1 
ATOM   21099 O  OE1   . GLU A 1 4303 ? 146.052 260.892 187.066 1.00 28.19 ? 4303 GLU A OE1   1 
ATOM   21100 O  OE2   . GLU A 1 4303 ? 144.744 260.451 185.358 1.00 35.90 ? 4303 GLU A OE2   1 
ATOM   21101 N  N     . GLU A 1 4304 ? 147.868 264.878 186.516 1.00 17.30 ? 4304 GLU A N     1 
ATOM   21102 C  CA    . GLU A 1 4304 ? 147.946 266.333 186.473 1.00 13.91 ? 4304 GLU A CA    1 
ATOM   21103 C  C     . GLU A 1 4304 ? 149.222 266.842 187.134 1.00 15.01 ? 4304 GLU A C     1 
ATOM   21104 O  O     . GLU A 1 4304 ? 149.860 267.772 186.628 1.00 22.30 ? 4304 GLU A O     1 
ATOM   21105 C  CB    . GLU A 1 4304 ? 146.718 266.949 187.137 1.00 19.08 ? 4304 GLU A CB    1 
ATOM   21106 C  CG    . GLU A 1 4304 ? 145.413 266.241 186.815 1.00 22.88 ? 4304 GLU A CG    1 
ATOM   21107 C  CD    . GLU A 1 4304 ? 144.220 266.912 187.465 1.00 26.82 ? 4304 GLU A CD    1 
ATOM   21108 O  OE1   . GLU A 1 4304 ? 144.117 268.153 187.380 1.00 30.94 ? 4304 GLU A OE1   1 
ATOM   21109 O  OE2   . GLU A 1 4304 ? 143.387 266.198 188.063 1.00 24.61 ? 4304 GLU A OE2   1 
ATOM   21110 N  N     . PHE A 1 4305 ? 149.604 266.251 188.271 1.00 13.61 ? 4305 PHE A N     1 
ATOM   21111 C  CA    . PHE A 1 4305 ? 150.829 266.670 188.942 1.00 8.64  ? 4305 PHE A CA    1 
ATOM   21112 C  C     . PHE A 1 4305 ? 152.061 266.311 188.120 1.00 8.94  ? 4305 PHE A C     1 
ATOM   21113 O  O     . PHE A 1 4305 ? 153.022 267.088 188.067 1.00 16.07 ? 4305 PHE A O     1 
ATOM   21114 C  CB    . PHE A 1 4305 ? 150.912 266.048 190.337 1.00 9.41  ? 4305 PHE A CB    1 
ATOM   21115 C  CG    . PHE A 1 4305 ? 149.854 266.537 191.285 1.00 6.50  ? 4305 PHE A CG    1 
ATOM   21116 C  CD1   . PHE A 1 4305 ? 149.896 267.827 191.785 1.00 8.23  ? 4305 PHE A CD1   1 
ATOM   21117 C  CD2   . PHE A 1 4305 ? 148.828 265.703 191.690 1.00 5.96  ? 4305 PHE A CD2   1 
ATOM   21118 C  CE1   . PHE A 1 4305 ? 148.928 268.278 192.661 1.00 8.05  ? 4305 PHE A CE1   1 
ATOM   21119 C  CE2   . PHE A 1 4305 ? 147.857 266.148 192.565 1.00 5.87  ? 4305 PHE A CE2   1 
ATOM   21120 C  CZ    . PHE A 1 4305 ? 147.908 267.436 193.050 1.00 10.88 ? 4305 PHE A CZ    1 
ATOM   21121 N  N     . VAL A 1 4306 ? 152.056 265.140 187.481 1.00 9.51  ? 4306 VAL A N     1 
ATOM   21122 C  CA    . VAL A 1 4306 ? 153.198 264.739 186.665 1.00 10.96 ? 4306 VAL A CA    1 
ATOM   21123 C  C     . VAL A 1 4306 ? 153.330 265.648 185.447 1.00 11.52 ? 4306 VAL A C     1 
ATOM   21124 O  O     . VAL A 1 4306 ? 154.442 265.956 185.004 1.00 11.06 ? 4306 VAL A O     1 
ATOM   21125 C  CB    . VAL A 1 4306 ? 153.075 263.256 186.268 1.00 13.39 ? 4306 VAL A CB    1 
ATOM   21126 C  CG1   . VAL A 1 4306 ? 154.320 262.793 185.535 1.00 8.12  ? 4306 VAL A CG1   1 
ATOM   21127 C  CG2   . VAL A 1 4306 ? 152.848 262.397 187.505 1.00 11.76 ? 4306 VAL A CG2   1 
ATOM   21128 N  N     . GLN A 1 4307 ? 152.201 266.088 184.887 1.00 11.71 ? 4307 GLN A N     1 
ATOM   21129 C  CA    . GLN A 1 4307 ? 152.251 267.063 183.802 1.00 10.59 ? 4307 GLN A CA    1 
ATOM   21130 C  C     . GLN A 1 4307 ? 152.849 268.381 184.280 1.00 10.02 ? 4307 GLN A C     1 
ATOM   21131 O  O     . GLN A 1 4307 ? 153.636 269.011 183.565 1.00 12.61 ? 4307 GLN A O     1 
ATOM   21132 C  CB    . GLN A 1 4307 ? 150.852 267.288 183.228 1.00 14.53 ? 4307 GLN A CB    1 
ATOM   21133 C  CG    . GLN A 1 4307 ? 150.408 266.228 182.236 1.00 21.86 ? 4307 GLN A CG    1 
ATOM   21134 C  CD    . GLN A 1 4307 ? 148.908 266.222 182.025 1.00 27.78 ? 4307 GLN A CD    1 
ATOM   21135 O  OE1   . GLN A 1 4307 ? 148.133 266.287 182.979 1.00 28.50 ? 4307 GLN A OE1   1 
ATOM   21136 N  NE2   . GLN A 1 4307 ? 148.488 266.144 180.767 1.00 30.98 ? 4307 GLN A NE2   1 
ATOM   21137 N  N     . TRP A 1 4308 ? 152.484 268.811 185.489 1.00 10.93 ? 4308 TRP A N     1 
ATOM   21138 C  CA    . TRP A 1 4308 ? 153.026 270.051 186.036 1.00 4.72  ? 4308 TRP A CA    1 
ATOM   21139 C  C     . TRP A 1 4308 ? 154.536 269.957 186.224 1.00 5.56  ? 4308 TRP A C     1 
ATOM   21140 O  O     . TRP A 1 4308 ? 155.262 270.920 185.951 1.00 9.23  ? 4308 TRP A O     1 
ATOM   21141 C  CB    . TRP A 1 4308 ? 152.331 270.375 187.359 1.00 6.27  ? 4308 TRP A CB    1 
ATOM   21142 C  CG    . TRP A 1 4308 ? 152.822 271.616 188.038 1.00 7.42  ? 4308 TRP A CG    1 
ATOM   21143 C  CD1   . TRP A 1 4308 ? 152.303 272.870 187.926 1.00 3.42  ? 4308 TRP A CD1   1 
ATOM   21144 C  CD2   . TRP A 1 4308 ? 153.925 271.720 188.946 1.00 4.11  ? 4308 TRP A CD2   1 
ATOM   21145 N  NE1   . TRP A 1 4308 ? 153.013 273.749 188.704 1.00 4.76  ? 4308 TRP A NE1   1 
ATOM   21146 C  CE2   . TRP A 1 4308 ? 154.014 273.068 189.341 1.00 4.49  ? 4308 TRP A CE2   1 
ATOM   21147 C  CE3   . TRP A 1 4308 ? 154.846 270.805 189.462 1.00 3.56  ? 4308 TRP A CE3   1 
ATOM   21148 C  CZ2   . TRP A 1 4308 ? 154.988 273.521 190.226 1.00 4.57  ? 4308 TRP A CZ2   1 
ATOM   21149 C  CZ3   . TRP A 1 4308 ? 155.810 271.259 190.339 1.00 2.80  ? 4308 TRP A CZ3   1 
ATOM   21150 C  CH2   . TRP A 1 4308 ? 155.874 272.603 190.712 1.00 3.83  ? 4308 TRP A CH2   1 
ATOM   21151 N  N     . VAL A 1 4309 ? 155.023 268.808 186.694 1.00 4.17  ? 4309 VAL A N     1 
ATOM   21152 C  CA    . VAL A 1 4309 ? 156.460 268.636 186.891 1.00 5.01  ? 4309 VAL A CA    1 
ATOM   21153 C  C     . VAL A 1 4309 ? 157.194 268.674 185.555 1.00 5.01  ? 4309 VAL A C     1 
ATOM   21154 O  O     . VAL A 1 4309 ? 158.267 269.278 185.441 1.00 8.13  ? 4309 VAL A O     1 
ATOM   21155 C  CB    . VAL A 1 4309 ? 156.738 267.331 187.661 1.00 6.86  ? 4309 VAL A CB    1 
ATOM   21156 C  CG1   . VAL A 1 4309 ? 158.231 267.082 187.774 1.00 2.01  ? 4309 VAL A CG1   1 
ATOM   21157 C  CG2   . VAL A 1 4309 ? 156.104 267.387 189.039 1.00 2.38  ? 4309 VAL A CG2   1 
ATOM   21158 N  N     . GLU A 1 4310 ? 156.630 268.035 184.526 1.00 10.69 ? 4310 GLU A N     1 
ATOM   21159 C  CA    . GLU A 1 4310 ? 157.260 268.040 183.210 1.00 5.72  ? 4310 GLU A CA    1 
ATOM   21160 C  C     . GLU A 1 4310 ? 157.269 269.421 182.571 1.00 9.31  ? 4310 GLU A C     1 
ATOM   21161 O  O     . GLU A 1 4310 ? 158.113 269.681 181.709 1.00 14.56 ? 4310 GLU A O     1 
ATOM   21162 C  CB    . GLU A 1 4310 ? 156.556 267.054 182.277 1.00 8.46  ? 4310 GLU A CB    1 
ATOM   21163 C  CG    . GLU A 1 4310 ? 156.738 265.595 182.643 1.00 8.23  ? 4310 GLU A CG    1 
ATOM   21164 C  CD    . GLU A 1 4310 ? 155.513 264.769 182.319 1.00 17.81 ? 4310 GLU A CD    1 
ATOM   21165 O  OE1   . GLU A 1 4310 ? 154.562 265.325 181.729 1.00 19.17 ? 4310 GLU A OE1   1 
ATOM   21166 O  OE2   . GLU A 1 4310 ? 155.500 263.564 182.645 1.00 16.97 ? 4310 GLU A OE2   1 
ATOM   21167 N  N     . LEU A 1 4311 ? 156.360 270.307 182.967 1.00 6.52  ? 4311 LEU A N     1 
ATOM   21168 C  CA    . LEU A 1 4311 ? 156.292 271.650 182.413 1.00 5.63  ? 4311 LEU A CA    1 
ATOM   21169 C  C     . LEU A 1 4311 ? 157.129 272.657 183.189 1.00 10.49 ? 4311 LEU A C     1 
ATOM   21170 O  O     . LEU A 1 4311 ? 157.091 273.848 182.867 1.00 14.02 ? 4311 LEU A O     1 
ATOM   21171 C  CB    . LEU A 1 4311 ? 154.839 272.129 182.351 1.00 6.67  ? 4311 LEU A CB    1 
ATOM   21172 C  CG    . LEU A 1 4311 ? 153.927 271.441 181.331 1.00 9.98  ? 4311 LEU A CG    1 
ATOM   21173 C  CD1   . LEU A 1 4311 ? 152.694 272.286 181.068 1.00 8.70  ? 4311 LEU A CD1   1 
ATOM   21174 C  CD2   . LEU A 1 4311 ? 154.668 271.152 180.036 1.00 9.42  ? 4311 LEU A CD2   1 
ATOM   21175 N  N     . LEU A 1 4312 ? 157.864 272.216 184.203 1.00 7.98  ? 4312 LEU A N     1 
ATOM   21176 C  CA    . LEU A 1 4312 ? 158.762 273.118 184.905 1.00 7.22  ? 4312 LEU A CA    1 
ATOM   21177 C  C     . LEU A 1 4312 ? 159.883 273.564 183.968 1.00 10.29 ? 4312 LEU A C     1 
ATOM   21178 O  O     . LEU A 1 4312 ? 160.391 272.763 183.179 1.00 11.00 ? 4312 LEU A O     1 
ATOM   21179 C  CB    . LEU A 1 4312 ? 159.355 272.445 186.141 1.00 6.34  ? 4312 LEU A CB    1 
ATOM   21180 C  CG    . LEU A 1 4312 ? 158.453 272.289 187.367 1.00 4.08  ? 4312 LEU A CG    1 
ATOM   21181 C  CD1   . LEU A 1 4312 ? 159.117 271.408 188.408 1.00 1.90  ? 4312 LEU A CD1   1 
ATOM   21182 C  CD2   . LEU A 1 4312 ? 158.097 273.644 187.959 1.00 2.87  ? 4312 LEU A CD2   1 
ATOM   21183 N  N     . PRO A 1 4313 ? 160.286 274.829 184.027 1.00 12.87 ? 4313 PRO A N     1 
ATOM   21184 C  CA    . PRO A 1 4313 ? 161.367 275.300 183.158 1.00 9.96  ? 4313 PRO A CA    1 
ATOM   21185 C  C     . PRO A 1 4313 ? 162.702 274.696 183.561 1.00 8.36  ? 4313 PRO A C     1 
ATOM   21186 O  O     . PRO A 1 4313 ? 162.880 274.170 184.660 1.00 15.42 ? 4313 PRO A O     1 
ATOM   21187 C  CB    . PRO A 1 4313 ? 161.350 276.816 183.368 1.00 11.01 ? 4313 PRO A CB    1 
ATOM   21188 C  CG    . PRO A 1 4313 ? 160.789 276.984 184.739 1.00 6.68  ? 4313 PRO A CG    1 
ATOM   21189 C  CD    . PRO A 1 4313 ? 159.759 275.902 184.885 1.00 6.30  ? 4313 PRO A CD    1 
ATOM   21190 N  N     . ASP A 1 4314 ? 163.659 274.778 182.636 1.00 10.57 ? 4314 ASP A N     1 
ATOM   21191 C  CA    . ASP A 1 4314 ? 165.025 274.344 182.891 1.00 13.36 ? 4314 ASP A CA    1 
ATOM   21192 C  C     . ASP A 1 4314 ? 165.879 275.486 183.431 1.00 13.84 ? 4314 ASP A C     1 
ATOM   21193 O  O     . ASP A 1 4314 ? 167.084 275.556 183.164 1.00 20.74 ? 4314 ASP A O     1 
ATOM   21194 C  CB    . ASP A 1 4314 ? 165.631 273.753 181.613 1.00 14.26 ? 4314 ASP A CB    1 
ATOM   21195 C  CG    . ASP A 1 4314 ? 166.934 273.000 181.863 1.00 21.82 ? 4314 ASP A CG    1 
ATOM   21196 O  OD1   . ASP A 1 4314 ? 167.387 272.927 183.023 1.00 18.02 ? 4314 ASP A OD1   1 
ATOM   21197 O  OD2   . ASP A 1 4314 ? 167.509 272.476 180.884 1.00 24.22 ? 4314 ASP A OD2   1 
ATOM   21198 N  N     . THR A 1 4315 ? 165.263 276.405 184.164 1.00 12.85 ? 4315 THR A N     1 
ATOM   21199 C  CA    . THR A 1 4315 ? 165.925 277.580 184.713 1.00 9.80  ? 4315 THR A CA    1 
ATOM   21200 C  C     . THR A 1 4315 ? 165.955 277.534 186.237 1.00 9.61  ? 4315 THR A C     1 
ATOM   21201 O  O     . THR A 1 4315 ? 165.725 278.540 186.910 1.00 16.02 ? 4315 THR A O     1 
ATOM   21202 C  CB    . THR A 1 4315 ? 165.237 278.855 184.233 1.00 18.37 ? 4315 THR A CB    1 
ATOM   21203 O  OG1   . THR A 1 4315 ? 163.960 278.978 184.872 1.00 17.66 ? 4315 THR A OG1   1 
ATOM   21204 C  CG2   . THR A 1 4315 ? 165.036 278.809 182.728 1.00 11.71 ? 4315 THR A CG2   1 
ATOM   21205 N  N     . GLN A 1 4316 ? 166.224 276.357 186.794 1.00 11.34 ? 4316 GLN A N     1 
ATOM   21206 C  CA    . GLN A 1 4316 ? 166.279 276.209 188.241 1.00 3.46  ? 4316 GLN A CA    1 
ATOM   21207 C  C     . GLN A 1 4316 ? 167.429 277.016 188.824 1.00 4.48  ? 4316 GLN A C     1 
ATOM   21208 O  O     . GLN A 1 4316 ? 168.549 277.006 188.305 1.00 8.39  ? 4316 GLN A O     1 
ATOM   21209 C  CB    . GLN A 1 4316 ? 166.434 274.739 188.627 1.00 3.44  ? 4316 GLN A CB    1 
ATOM   21210 C  CG    . GLN A 1 4316 ? 166.492 274.502 190.128 1.00 2.71  ? 4316 GLN A CG    1 
ATOM   21211 C  CD    . GLN A 1 4316 ? 166.828 273.069 190.485 1.00 5.47  ? 4316 GLN A CD    1 
ATOM   21212 O  OE1   . GLN A 1 4316 ? 166.203 272.133 189.992 1.00 7.07  ? 4316 GLN A OE1   1 
ATOM   21213 N  NE2   . GLN A 1 4316 ? 167.815 272.891 191.352 1.00 4.98  ? 4316 GLN A NE2   1 
ATOM   21214 N  N     . THR A 1 4317 ? 167.143 277.709 189.913 1.00 6.46  ? 4317 THR A N     1 
ATOM   21215 C  CA    . THR A 1 4317 ? 168.104 278.482 190.679 1.00 4.55  ? 4317 THR A CA    1 
ATOM   21216 C  C     . THR A 1 4317 ? 167.989 278.059 192.133 1.00 4.43  ? 4317 THR A C     1 
ATOM   21217 O  O     . THR A 1 4317 ? 166.973 277.486 192.537 1.00 5.95  ? 4317 THR A O     1 
ATOM   21218 C  CB    . THR A 1 4317 ? 167.843 279.989 190.542 1.00 9.34  ? 4317 THR A CB    1 
ATOM   21219 O  OG1   . THR A 1 4317 ? 166.490 280.277 190.911 1.00 8.38  ? 4317 THR A OG1   1 
ATOM   21220 C  CG2   . THR A 1 4317 ? 168.086 280.449 189.116 1.00 3.35  ? 4317 THR A CG2   1 
ATOM   21221 N  N     . PRO A 1 4318 ? 169.019 278.309 192.944 1.00 7.69  ? 4318 PRO A N     1 
ATOM   21222 C  CA    . PRO A 1 4318 ? 168.915 277.965 194.371 1.00 4.50  ? 4318 PRO A CA    1 
ATOM   21223 C  C     . PRO A 1 4318 ? 167.780 278.676 195.090 1.00 2.83  ? 4318 PRO A C     1 
ATOM   21224 O  O     . PRO A 1 4318 ? 167.400 278.247 196.185 1.00 4.63  ? 4318 PRO A O     1 
ATOM   21225 C  CB    . PRO A 1 4318 ? 170.287 278.365 194.937 1.00 6.90  ? 4318 PRO A CB    1 
ATOM   21226 C  CG    . PRO A 1 4318 ? 170.929 279.204 193.885 1.00 5.52  ? 4318 PRO A CG    1 
ATOM   21227 C  CD    . PRO A 1 4318 ? 170.374 278.749 192.583 1.00 4.87  ? 4318 PRO A CD    1 
ATOM   21228 N  N     . SER A 1 4319 ? 167.227 279.746 194.513 1.00 1.94  ? 4319 SER A N     1 
ATOM   21229 C  CA    . SER A 1 4319 ? 166.040 280.374 195.081 1.00 3.00  ? 4319 SER A CA    1 
ATOM   21230 C  C     . SER A 1 4319 ? 164.823 279.458 195.038 1.00 3.56  ? 4319 SER A C     1 
ATOM   21231 O  O     . SER A 1 4319 ? 163.870 279.681 195.791 1.00 6.56  ? 4319 SER A O     1 
ATOM   21232 C  CB    . SER A 1 4319 ? 165.735 281.683 194.352 1.00 6.03  ? 4319 SER A CB    1 
ATOM   21233 O  OG    . SER A 1 4319 ? 165.517 281.459 192.971 1.00 7.12  ? 4319 SER A OG    1 
ATOM   21234 N  N     . TRP A 1 4320 ? 164.826 278.443 194.170 1.00 3.21  ? 4320 TRP A N     1 
ATOM   21235 C  CA    . TRP A 1 4320 ? 163.786 277.420 194.229 1.00 2.97  ? 4320 TRP A CA    1 
ATOM   21236 C  C     . TRP A 1 4320 ? 163.790 276.713 195.575 1.00 2.80  ? 4320 TRP A C     1 
ATOM   21237 O  O     . TRP A 1 4320 ? 162.740 276.270 196.050 1.00 2.08  ? 4320 TRP A O     1 
ATOM   21238 C  CB    . TRP A 1 4320 ? 163.984 276.391 193.115 1.00 6.58  ? 4320 TRP A CB    1 
ATOM   21239 C  CG    . TRP A 1 4320 ? 163.647 276.867 191.743 1.00 4.40  ? 4320 TRP A CG    1 
ATOM   21240 C  CD1   . TRP A 1 4320 ? 163.750 278.137 191.262 1.00 4.94  ? 4320 TRP A CD1   1 
ATOM   21241 C  CD2   . TRP A 1 4320 ? 163.155 276.068 190.663 1.00 3.79  ? 4320 TRP A CD2   1 
ATOM   21242 N  NE1   . TRP A 1 4320 ? 163.350 278.180 189.951 1.00 5.83  ? 4320 TRP A NE1   1 
ATOM   21243 C  CE2   . TRP A 1 4320 ? 162.980 276.922 189.558 1.00 3.77  ? 4320 TRP A CE2   1 
ATOM   21244 C  CE3   . TRP A 1 4320 ? 162.845 274.712 190.525 1.00 5.11  ? 4320 TRP A CE3   1 
ATOM   21245 C  CZ2   . TRP A 1 4320 ? 162.508 276.466 188.331 1.00 5.25  ? 4320 TRP A CZ2   1 
ATOM   21246 C  CZ3   . TRP A 1 4320 ? 162.374 274.261 189.305 1.00 4.61  ? 4320 TRP A CZ3   1 
ATOM   21247 C  CH2   . TRP A 1 4320 ? 162.213 275.135 188.225 1.00 5.78  ? 4320 TRP A CH2   1 
ATOM   21248 N  N     . LEU A 1 4321 ? 164.961 276.601 196.192 1.00 3.40  ? 4321 LEU A N     1 
ATOM   21249 C  CA    . LEU A 1 4321 ? 165.143 275.893 197.449 1.00 1.13  ? 4321 LEU A CA    1 
ATOM   21250 C  C     . LEU A 1 4321 ? 165.033 276.806 198.660 1.00 2.55  ? 4321 LEU A C     1 
ATOM   21251 O  O     . LEU A 1 4321 ? 165.192 276.333 199.789 1.00 8.02  ? 4321 LEU A O     1 
ATOM   21252 C  CB    . LEU A 1 4321 ? 166.508 275.202 197.448 1.00 1.18  ? 4321 LEU A CB    1 
ATOM   21253 C  CG    . LEU A 1 4321 ? 166.874 274.464 196.159 1.00 0.96  ? 4321 LEU A CG    1 
ATOM   21254 C  CD1   . LEU A 1 4321 ? 168.289 273.927 196.230 1.00 0.51  ? 4321 LEU A CD1   1 
ATOM   21255 C  CD2   . LEU A 1 4321 ? 165.890 273.350 195.862 1.00 0.83  ? 4321 LEU A CD2   1 
ATOM   21256 N  N     . GLY A 1 4322 ? 164.767 278.095 198.456 1.00 1.31  ? 4322 GLY A N     1 
ATOM   21257 C  CA    . GLY A 1 4322 ? 164.797 279.068 199.525 1.00 1.75  ? 4322 GLY A CA    1 
ATOM   21258 C  C     . GLY A 1 4322 ? 166.155 279.681 199.791 1.00 2.28  ? 4322 GLY A C     1 
ATOM   21259 O  O     . GLY A 1 4322 ? 166.264 280.546 200.668 1.00 2.67  ? 4322 GLY A O     1 
ATOM   21260 N  N     . LEU A 1 4323 ? 167.182 279.263 199.069 1.00 1.99  ? 4323 LEU A N     1 
ATOM   21261 C  CA    . LEU A 1 4323 ? 168.541 279.764 199.189 1.00 2.03  ? 4323 LEU A CA    1 
ATOM   21262 C  C     . LEU A 1 4323 ? 168.718 281.033 198.370 1.00 2.32  ? 4323 LEU A C     1 
ATOM   21263 O  O     . LEU A 1 4323 ? 167.943 281.307 197.450 1.00 4.46  ? 4323 LEU A O     1 
ATOM   21264 C  CB    . LEU A 1 4323 ? 169.528 278.695 198.723 1.00 1.80  ? 4323 LEU A CB    1 
ATOM   21265 C  CG    . LEU A 1 4323 ? 169.768 277.530 199.684 1.00 1.36  ? 4323 LEU A CG    1 
ATOM   21266 C  CD1   . LEU A 1 4323 ? 170.504 276.403 198.986 1.00 1.83  ? 4323 LEU A CD1   1 
ATOM   21267 C  CD2   . LEU A 1 4323 ? 170.542 277.998 200.904 1.00 1.65  ? 4323 LEU A CD2   1 
ATOM   21268 N  N     . PRO A 1 4324 ? 169.718 281.853 198.692 1.00 3.76  ? 4324 PRO A N     1 
ATOM   21269 C  CA    . PRO A 1 4324 ? 170.049 282.977 197.810 1.00 4.68  ? 4324 PRO A CA    1 
ATOM   21270 C  C     . PRO A 1 4324 ? 170.596 282.487 196.479 1.00 4.55  ? 4324 PRO A C     1 
ATOM   21271 O  O     . PRO A 1 4324 ? 171.226 281.431 196.388 1.00 4.53  ? 4324 PRO A O     1 
ATOM   21272 C  CB    . PRO A 1 4324 ? 171.108 283.751 198.603 1.00 3.26  ? 4324 PRO A CB    1 
ATOM   21273 C  CG    . PRO A 1 4324 ? 171.694 282.750 199.533 1.00 3.82  ? 4324 PRO A CG    1 
ATOM   21274 C  CD    . PRO A 1 4324 ? 170.581 281.812 199.886 1.00 2.16  ? 4324 PRO A CD    1 
ATOM   21275 N  N     . ASN A 1 4325 ? 170.346 283.276 195.434 1.00 4.34  ? 4325 ASN A N     1 
ATOM   21276 C  CA    . ASN A 1 4325 ? 170.761 282.894 194.089 1.00 4.42  ? 4325 ASN A CA    1 
ATOM   21277 C  C     . ASN A 1 4325 ? 172.271 282.908 193.896 1.00 6.67  ? 4325 ASN A C     1 
ATOM   21278 O  O     . ASN A 1 4325 ? 172.755 282.321 192.923 1.00 16.37 ? 4325 ASN A O     1 
ATOM   21279 C  CB    . ASN A 1 4325 ? 170.092 283.805 193.062 1.00 7.25  ? 4325 ASN A CB    1 
ATOM   21280 C  CG    . ASN A 1 4325 ? 168.787 283.237 192.559 1.00 6.76  ? 4325 ASN A CG    1 
ATOM   21281 O  OD1   . ASN A 1 4325 ? 168.454 282.090 192.843 1.00 9.78  ? 4325 ASN A OD1   1 
ATOM   21282 N  ND2   . ASN A 1 4325 ? 168.032 284.040 191.825 1.00 9.30  ? 4325 ASN A ND2   1 
ATOM   21283 N  N     . ASN A 1 4326 ? 173.022 283.543 194.791 1.00 6.68  ? 4326 ASN A N     1 
ATOM   21284 C  CA    . ASN A 1 4326 ? 174.476 283.527 194.715 1.00 5.10  ? 4326 ASN A CA    1 
ATOM   21285 C  C     . ASN A 1 4326 ? 175.086 282.253 195.283 1.00 6.75  ? 4326 ASN A C     1 
ATOM   21286 O  O     . ASN A 1 4326 ? 176.307 282.086 195.210 1.00 11.38 ? 4326 ASN A O     1 
ATOM   21287 C  CB    . ASN A 1 4326 ? 175.058 284.743 195.442 1.00 6.15  ? 4326 ASN A CB    1 
ATOM   21288 C  CG    . ASN A 1 4326 ? 174.645 284.805 196.899 1.00 8.54  ? 4326 ASN A CG    1 
ATOM   21289 O  OD1   . ASN A 1 4326 ? 175.099 284.011 197.721 1.00 9.98  ? 4326 ASN A OD1   1 
ATOM   21290 N  ND2   . ASN A 1 4326 ? 173.781 285.755 197.225 1.00 11.52 ? 4326 ASN A ND2   1 
ATOM   21291 N  N     . ALA A 1 4327 ? 174.270 281.362 195.852 1.00 4.20  ? 4327 ALA A N     1 
ATOM   21292 C  CA    . ALA A 1 4327 ? 174.798 280.139 196.448 1.00 4.21  ? 4327 ALA A CA    1 
ATOM   21293 C  C     . ALA A 1 4327 ? 175.460 279.242 195.413 1.00 6.06  ? 4327 ALA A C     1 
ATOM   21294 O  O     . ALA A 1 4327 ? 176.378 278.486 195.747 1.00 10.16 ? 4327 ALA A O     1 
ATOM   21295 C  CB    . ALA A 1 4327 ? 173.683 279.383 197.169 1.00 5.13  ? 4327 ALA A CB    1 
ATOM   21296 N  N     . GLU A 1 4328 ? 175.009 279.304 194.163 1.00 7.23  ? 4328 GLU A N     1 
ATOM   21297 C  CA    . GLU A 1 4328 ? 175.565 278.475 193.103 1.00 5.29  ? 4328 GLU A CA    1 
ATOM   21298 C  C     . GLU A 1 4328 ? 176.710 279.142 192.350 1.00 7.27  ? 4328 GLU A C     1 
ATOM   21299 O  O     . GLU A 1 4328 ? 177.333 278.486 191.511 1.00 10.02 ? 4328 GLU A O     1 
ATOM   21300 C  CB    . GLU A 1 4328 ? 174.461 278.086 192.112 1.00 6.11  ? 4328 GLU A CB    1 
ATOM   21301 C  CG    . GLU A 1 4328 ? 174.158 279.152 191.071 1.00 6.44  ? 4328 GLU A CG    1 
ATOM   21302 C  CD    . GLU A 1 4328 ? 172.906 278.854 190.270 1.00 11.65 ? 4328 GLU A CD    1 
ATOM   21303 O  OE1   . GLU A 1 4328 ? 172.632 277.664 190.008 1.00 10.92 ? 4328 GLU A OE1   1 
ATOM   21304 O  OE2   . GLU A 1 4328 ? 172.195 279.811 189.898 1.00 18.41 ? 4328 GLU A OE2   1 
ATOM   21305 N  N     . ARG A 1 4329 ? 177.015 280.409 192.640 1.00 5.13  ? 4329 ARG A N     1 
ATOM   21306 C  CA    . ARG A 1 4329 ? 177.994 281.143 191.842 1.00 6.13  ? 4329 ARG A CA    1 
ATOM   21307 C  C     . ARG A 1 4329 ? 179.376 280.506 191.921 1.00 6.74  ? 4329 ARG A C     1 
ATOM   21308 O  O     . ARG A 1 4329 ? 180.018 280.262 190.895 1.00 10.81 ? 4329 ARG A O     1 
ATOM   21309 C  CB    . ARG A 1 4329 ? 178.050 282.601 192.292 1.00 5.14  ? 4329 ARG A CB    1 
ATOM   21310 C  CG    . ARG A 1 4329 ? 178.324 283.578 191.166 1.00 5.12  ? 4329 ARG A CG    1 
ATOM   21311 C  CD    . ARG A 1 4329 ? 178.680 284.953 191.702 1.00 11.28 ? 4329 ARG A CD    1 
ATOM   21312 N  NE    . ARG A 1 4329 ? 178.914 285.925 190.641 1.00 17.14 ? 4329 ARG A NE    1 
ATOM   21313 C  CZ    . ARG A 1 4329 ? 177.968 286.430 189.861 1.00 12.06 ? 4329 ARG A CZ    1 
ATOM   21314 N  NH1   . ARG A 1 4329 ? 176.701 286.077 189.988 1.00 10.66 ? 4329 ARG A NH1   1 
ATOM   21315 N  NH2   . ARG A 1 4329 ? 178.305 287.322 188.931 1.00 14.09 ? 4329 ARG A NH2   1 
ATOM   21316 N  N     . VAL A 1 4330 ? 179.855 280.236 193.135 1.00 5.83  ? 4330 VAL A N     1 
ATOM   21317 C  CA    . VAL A 1 4330 ? 181.170 279.624 193.290 1.00 7.01  ? 4330 VAL A CA    1 
ATOM   21318 C  C     . VAL A 1 4330 ? 181.152 278.184 192.788 1.00 7.93  ? 4330 VAL A C     1 
ATOM   21319 O  O     . VAL A 1 4330 ? 182.087 277.731 192.119 1.00 7.02  ? 4330 VAL A O     1 
ATOM   21320 C  CB    . VAL A 1 4330 ? 181.626 279.712 194.756 1.00 2.88  ? 4330 VAL A CB    1 
ATOM   21321 C  CG1   . VAL A 1 4330 ? 182.825 278.815 195.003 1.00 1.55  ? 4330 VAL A CG1   1 
ATOM   21322 C  CG2   . VAL A 1 4330 ? 181.943 281.153 195.123 1.00 2.74  ? 4330 VAL A CG2   1 
ATOM   21323 N  N     . LEU A 1 4331 ? 180.080 277.450 193.096 1.00 7.46  ? 4331 LEU A N     1 
ATOM   21324 C  CA    . LEU A 1 4331 ? 179.974 276.058 192.673 1.00 7.04  ? 4331 LEU A CA    1 
ATOM   21325 C  C     . LEU A 1 4331 ? 179.947 275.941 191.152 1.00 6.90  ? 4331 LEU A C     1 
ATOM   21326 O  O     . LEU A 1 4331 ? 180.581 275.045 190.582 1.00 8.01  ? 4331 LEU A O     1 
ATOM   21327 C  CB    . LEU A 1 4331 ? 178.728 275.432 193.306 1.00 11.67 ? 4331 LEU A CB    1 
ATOM   21328 C  CG    . LEU A 1 4331 ? 178.416 273.939 193.200 1.00 15.57 ? 4331 LEU A CG    1 
ATOM   21329 C  CD1   . LEU A 1 4331 ? 177.583 273.519 194.391 1.00 11.69 ? 4331 LEU A CD1   1 
ATOM   21330 C  CD2   . LEU A 1 4331 ? 177.640 273.649 191.939 1.00 12.69 ? 4331 LEU A CD2   1 
ATOM   21331 N  N     . LEU A 1 4332 ? 179.218 276.833 190.480 1.00 5.46  ? 4332 LEU A N     1 
ATOM   21332 C  CA    . LEU A 1 4332 ? 179.201 276.823 189.019 1.00 5.74  ? 4332 LEU A CA    1 
ATOM   21333 C  C     . LEU A 1 4332 ? 180.551 277.227 188.443 1.00 6.46  ? 4332 LEU A C     1 
ATOM   21334 O  O     . LEU A 1 4332 ? 181.008 276.645 187.453 1.00 6.98  ? 4332 LEU A O     1 
ATOM   21335 C  CB    . LEU A 1 4332 ? 178.101 277.743 188.497 1.00 6.79  ? 4332 LEU A CB    1 
ATOM   21336 C  CG    . LEU A 1 4332 ? 176.661 277.253 188.646 1.00 3.85  ? 4332 LEU A CG    1 
ATOM   21337 C  CD1   . LEU A 1 4332 ? 175.699 278.208 187.962 1.00 2.55  ? 4332 LEU A CD1   1 
ATOM   21338 C  CD2   . LEU A 1 4332 ? 176.517 275.846 188.098 1.00 1.74  ? 4332 LEU A CD2   1 
ATOM   21339 N  N     . THR A 1 4333 ? 181.199 278.228 189.044 1.00 8.61  ? 4333 THR A N     1 
ATOM   21340 C  CA    . THR A 1 4333 ? 182.479 278.707 188.531 1.00 6.68  ? 4333 THR A CA    1 
ATOM   21341 C  C     . THR A 1 4333 ? 183.546 277.623 188.604 1.00 5.54  ? 4333 THR A C     1 
ATOM   21342 O  O     . THR A 1 4333 ? 184.352 277.471 187.679 1.00 6.70  ? 4333 THR A O     1 
ATOM   21343 C  CB    . THR A 1 4333 ? 182.914 279.952 189.304 1.00 6.48  ? 4333 THR A CB    1 
ATOM   21344 O  OG1   . THR A 1 4333 ? 181.883 280.944 189.227 1.00 6.19  ? 4333 THR A OG1   1 
ATOM   21345 C  CG2   . THR A 1 4333 ? 184.196 280.526 188.727 1.00 4.85  ? 4333 THR A CG2   1 
ATOM   21346 N  N     . THR A 1 4334 ? 183.570 276.859 189.699 1.00 3.81  ? 4334 THR A N     1 
ATOM   21347 C  CA    . THR A 1 4334 ? 184.544 275.781 189.826 1.00 4.04  ? 4334 THR A CA    1 
ATOM   21348 C  C     . THR A 1 4334 ? 184.309 274.694 188.782 1.00 7.73  ? 4334 THR A C     1 
ATOM   21349 O  O     . THR A 1 4334 ? 185.264 274.186 188.185 1.00 6.92  ? 4334 THR A O     1 
ATOM   21350 C  CB    . THR A 1 4334 ? 184.496 275.190 191.235 1.00 5.97  ? 4334 THR A CB    1 
ATOM   21351 O  OG1   . THR A 1 4334 ? 184.605 276.241 192.200 1.00 8.21  ? 4334 THR A OG1   1 
ATOM   21352 C  CG2   . THR A 1 4334 ? 185.637 274.211 191.438 1.00 5.09  ? 4334 THR A CG2   1 
ATOM   21353 N  N     . GLN A 1 4335 ? 183.047 274.326 188.547 1.00 9.22  ? 4335 GLN A N     1 
ATOM   21354 C  CA    . GLN A 1 4335 ? 182.756 273.295 187.554 1.00 4.92  ? 4335 GLN A CA    1 
ATOM   21355 C  C     . GLN A 1 4335 ? 183.149 273.744 186.155 1.00 4.79  ? 4335 GLN A C     1 
ATOM   21356 O  O     . GLN A 1 4335 ? 183.676 272.951 185.366 1.00 8.43  ? 4335 GLN A O     1 
ATOM   21357 C  CB    . GLN A 1 4335 ? 181.276 272.917 187.583 1.00 7.32  ? 4335 GLN A CB    1 
ATOM   21358 C  CG    . GLN A 1 4335 ? 180.882 271.943 188.668 1.00 5.37  ? 4335 GLN A CG    1 
ATOM   21359 C  CD    . GLN A 1 4335 ? 179.403 271.619 188.626 1.00 16.23 ? 4335 GLN A CD    1 
ATOM   21360 O  OE1   . GLN A 1 4335 ? 178.998 270.588 188.089 1.00 12.65 ? 4335 GLN A OE1   1 
ATOM   21361 N  NE2   . GLN A 1 4335 ? 178.586 272.518 189.157 1.00 10.43 ? 4335 GLN A NE2   1 
ATOM   21362 N  N     . GLY A 1 4336 ? 182.886 275.010 185.821 1.00 5.57  ? 4336 GLY A N     1 
ATOM   21363 C  CA    . GLY A 1 4336 ? 183.288 275.518 184.521 1.00 4.61  ? 4336 GLY A CA    1 
ATOM   21364 C  C     . GLY A 1 4336 ? 184.785 275.432 184.306 1.00 6.90  ? 4336 GLY A C     1 
ATOM   21365 O  O     . GLY A 1 4336 ? 185.247 275.050 183.229 1.00 8.63  ? 4336 GLY A O     1 
ATOM   21366 N  N     . VAL A 1 4337 ? 185.564 275.784 185.331 1.00 5.99  ? 4337 VAL A N     1 
ATOM   21367 C  CA    . VAL A 1 4337 ? 187.008 275.590 185.266 1.00 6.75  ? 4337 VAL A CA    1 
ATOM   21368 C  C     . VAL A 1 4337 ? 187.341 274.102 185.248 1.00 7.54  ? 4337 VAL A C     1 
ATOM   21369 O  O     . VAL A 1 4337 ? 188.282 273.669 184.574 1.00 7.98  ? 4337 VAL A O     1 
ATOM   21370 C  CB    . VAL A 1 4337 ? 187.690 276.320 186.437 1.00 4.01  ? 4337 VAL A CB    1 
ATOM   21371 C  CG1   . VAL A 1 4337 ? 189.170 275.996 186.491 1.00 7.18  ? 4337 VAL A CG1   1 
ATOM   21372 C  CG2   . VAL A 1 4337 ? 187.472 277.819 186.320 1.00 4.85  ? 4337 VAL A CG2   1 
ATOM   21373 N  N     . ASP A 1 4338 ? 186.566 273.298 185.980 1.00 7.87  ? 4338 ASP A N     1 
ATOM   21374 C  CA    . ASP A 1 4338 ? 186.768 271.854 185.971 1.00 5.70  ? 4338 ASP A CA    1 
ATOM   21375 C  C     . ASP A 1 4338 ? 186.520 271.268 184.584 1.00 7.48  ? 4338 ASP A C     1 
ATOM   21376 O  O     . ASP A 1 4338 ? 187.238 270.363 184.147 1.00 6.13  ? 4338 ASP A O     1 
ATOM   21377 C  CB    . ASP A 1 4338 ? 185.860 271.199 187.013 1.00 8.21  ? 4338 ASP A CB    1 
ATOM   21378 C  CG    . ASP A 1 4338 ? 185.987 269.691 187.039 1.00 20.85 ? 4338 ASP A CG    1 
ATOM   21379 O  OD1   . ASP A 1 4338 ? 187.090 269.186 187.335 1.00 21.50 ? 4338 ASP A OD1   1 
ATOM   21380 O  OD2   . ASP A 1 4338 ? 184.974 269.011 186.769 1.00 26.54 ? 4338 ASP A OD2   1 
ATOM   21381 N  N     . MET A 1 4339 ? 185.504 271.773 183.879 1.00 7.96  ? 4339 MET A N     1 
ATOM   21382 C  CA    . MET A 1 4339 ? 185.247 271.312 182.517 1.00 5.73  ? 4339 MET A CA    1 
ATOM   21383 C  C     . MET A 1 4339 ? 186.403 271.658 181.587 1.00 9.02  ? 4339 MET A C     1 
ATOM   21384 O  O     . MET A 1 4339 ? 186.773 270.856 180.722 1.00 9.85  ? 4339 MET A O     1 
ATOM   21385 C  CB    . MET A 1 4339 ? 183.940 271.909 181.996 1.00 6.62  ? 4339 MET A CB    1 
ATOM   21386 C  CG    . MET A 1 4339 ? 183.743 271.748 180.499 1.00 8.27  ? 4339 MET A CG    1 
ATOM   21387 S  SD    . MET A 1 4339 ? 182.204 272.453 179.891 1.00 21.56 ? 4339 MET A SD    1 
ATOM   21388 C  CE    . MET A 1 4339 ? 182.628 274.190 179.847 1.00 4.85  ? 4339 MET A CE    1 
ATOM   21389 N  N     . ILE A 1 4340 ? 186.982 272.852 181.744 1.00 10.86 ? 4340 ILE A N     1 
ATOM   21390 C  CA    . ILE A 1 4340 ? 188.127 273.236 180.923 1.00 8.64  ? 4340 ILE A CA    1 
ATOM   21391 C  C     . ILE A 1 4340 ? 189.306 272.310 181.184 1.00 7.80  ? 4340 ILE A C     1 
ATOM   21392 O  O     . ILE A 1 4340 ? 189.970 271.847 180.249 1.00 9.48  ? 4340 ILE A O     1 
ATOM   21393 C  CB    . ILE A 1 4340 ? 188.506 274.706 181.182 1.00 12.01 ? 4340 ILE A CB    1 
ATOM   21394 C  CG1   . ILE A 1 4340 ? 187.331 275.629 180.872 1.00 8.09  ? 4340 ILE A CG1   1 
ATOM   21395 C  CG2   . ILE A 1 4340 ? 189.715 275.097 180.344 1.00 9.46  ? 4340 ILE A CG2   1 
ATOM   21396 C  CD1   . ILE A 1 4340 ? 186.891 275.568 179.450 1.00 8.86  ? 4340 ILE A CD1   1 
ATOM   21397 N  N     . SER A 1 4341 ? 189.585 272.028 182.458 1.00 6.56  ? 4341 SER A N     1 
ATOM   21398 C  CA    . SER A 1 4341 ? 190.707 271.160 182.800 1.00 5.56  ? 4341 SER A CA    1 
ATOM   21399 C  C     . SER A 1 4341 ? 190.510 269.757 182.243 1.00 8.64  ? 4341 SER A C     1 
ATOM   21400 O  O     . SER A 1 4341 ? 191.457 269.140 181.745 1.00 9.58  ? 4341 SER A O     1 
ATOM   21401 C  CB    . SER A 1 4341 ? 190.889 271.114 184.317 1.00 8.21  ? 4341 SER A CB    1 
ATOM   21402 O  OG    . SER A 1 4341 ? 191.236 272.389 184.825 1.00 20.12 ? 4341 SER A OG    1 
ATOM   21403 N  N     . LYS A 1 4342 ? 189.286 269.234 182.331 1.00 8.56  ? 4342 LYS A N     1 
ATOM   21404 C  CA    . LYS A 1 4342 ? 189.010 267.899 181.814 1.00 5.59  ? 4342 LYS A CA    1 
ATOM   21405 C  C     . LYS A 1 4342 ? 189.111 267.857 180.296 1.00 8.13  ? 4342 LYS A C     1 
ATOM   21406 O  O     . LYS A 1 4342 ? 189.656 266.903 179.731 1.00 7.80  ? 4342 LYS A O     1 
ATOM   21407 C  CB    . LYS A 1 4342 ? 187.633 267.433 182.283 1.00 4.60  ? 4342 LYS A CB    1 
ATOM   21408 C  CG    . LYS A 1 4342 ? 187.644 266.771 183.648 1.00 5.34  ? 4342 LYS A CG    1 
ATOM   21409 C  CD    . LYS A 1 4342 ? 186.353 267.016 184.406 1.00 8.05  ? 4342 LYS A CD    1 
ATOM   21410 C  CE    . LYS A 1 4342 ? 186.393 266.348 185.771 1.00 9.82  ? 4342 LYS A CE    1 
ATOM   21411 N  NZ    . LYS A 1 4342 ? 185.052 266.332 186.416 1.00 11.52 ? 4342 LYS A NZ    1 
ATOM   21412 N  N     . MET A 1 4343 ? 188.590 268.882 179.617 1.00 7.34  ? 4343 MET A N     1 
ATOM   21413 C  CA    . MET A 1 4343 ? 188.705 268.940 178.163 1.00 5.49  ? 4343 MET A CA    1 
ATOM   21414 C  C     . MET A 1 4343 ? 190.160 269.045 177.732 1.00 9.93  ? 4343 MET A C     1 
ATOM   21415 O  O     . MET A 1 4343 ? 190.584 268.380 176.781 1.00 15.34 ? 4343 MET A O     1 
ATOM   21416 C  CB    . MET A 1 4343 ? 187.903 270.121 177.615 1.00 5.94  ? 4343 MET A CB    1 
ATOM   21417 C  CG    . MET A 1 4343 ? 186.459 269.798 177.275 1.00 4.04  ? 4343 MET A CG    1 
ATOM   21418 S  SD    . MET A 1 4343 ? 185.508 271.276 176.876 1.00 14.49 ? 4343 MET A SD    1 
ATOM   21419 C  CE    . MET A 1 4343 ? 186.315 271.797 175.365 1.00 9.12  ? 4343 MET A CE    1 
ATOM   21420 N  N     . LEU A 1 4344 ? 190.939 269.880 178.423 1.00 11.76 ? 4344 LEU A N     1 
ATOM   21421 C  CA    . LEU A 1 4344 ? 192.349 270.043 178.086 1.00 13.22 ? 4344 LEU A CA    1 
ATOM   21422 C  C     . LEU A 1 4344 ? 193.124 268.751 178.300 1.00 12.83 ? 4344 LEU A C     1 
ATOM   21423 O  O     . LEU A 1 4344 ? 194.001 268.406 177.501 1.00 17.02 ? 4344 LEU A O     1 
ATOM   21424 C  CB    . LEU A 1 4344 ? 192.955 271.173 178.914 1.00 11.49 ? 4344 LEU A CB    1 
ATOM   21425 C  CG    . LEU A 1 4344 ? 194.379 271.600 178.561 1.00 18.43 ? 4344 LEU A CG    1 
ATOM   21426 C  CD1   . LEU A 1 4344 ? 194.512 271.900 177.074 1.00 14.71 ? 4344 LEU A CD1   1 
ATOM   21427 C  CD2   . LEU A 1 4344 ? 194.783 272.800 179.401 1.00 18.11 ? 4344 LEU A CD2   1 
ATOM   21428 N  N     . LYS A 1 4345 ? 192.821 268.031 179.381 1.00 8.45  ? 4345 LYS A N     1 
ATOM   21429 C  CA    . LYS A 1 4345 ? 193.545 266.802 179.684 1.00 8.52  ? 4345 LYS A CA    1 
ATOM   21430 C  C     . LYS A 1 4345 ? 193.325 265.748 178.605 1.00 15.62 ? 4345 LYS A C     1 
ATOM   21431 O  O     . LYS A 1 4345 ? 194.252 265.014 178.247 1.00 24.37 ? 4345 LYS A O     1 
ATOM   21432 C  CB    . LYS A 1 4345 ? 193.125 266.277 181.055 1.00 8.34  ? 4345 LYS A CB    1 
ATOM   21433 C  CG    . LYS A 1 4345 ? 193.822 265.000 181.474 1.00 14.75 ? 4345 LYS A CG    1 
ATOM   21434 C  CD    . LYS A 1 4345 ? 193.293 264.488 182.801 1.00 17.13 ? 4345 LYS A CD    1 
ATOM   21435 C  CE    . LYS A 1 4345 ? 193.285 265.584 183.854 1.00 17.16 ? 4345 LYS A CE    1 
ATOM   21436 N  NZ    . LYS A 1 4345 ? 192.660 265.128 185.125 1.00 18.07 ? 4345 LYS A NZ    1 
ATOM   21437 N  N     . MET A 1 4346 ? 192.104 265.655 178.073 1.00 10.37 ? 4346 MET A N     1 
ATOM   21438 C  CA    . MET A 1 4346 ? 191.836 264.672 177.030 1.00 10.14 ? 4346 MET A CA    1 
ATOM   21439 C  C     . MET A 1 4346 ? 192.383 265.086 175.668 1.00 13.13 ? 4346 MET A C     1 
ATOM   21440 O  O     . MET A 1 4346 ? 192.426 264.251 174.759 1.00 17.05 ? 4346 MET A O     1 
ATOM   21441 C  CB    . MET A 1 4346 ? 190.336 264.387 176.930 1.00 7.76  ? 4346 MET A CB    1 
ATOM   21442 C  CG    . MET A 1 4346 ? 189.838 263.384 177.957 1.00 8.37  ? 4346 MET A CG    1 
ATOM   21443 S  SD    . MET A 1 4346 ? 188.047 263.208 178.026 1.00 13.73 ? 4346 MET A SD    1 
ATOM   21444 C  CE    . MET A 1 4346 ? 187.556 264.868 178.455 1.00 6.00  ? 4346 MET A CE    1 
ATOM   21445 N  N     . GLN A 1 4347 ? 192.796 266.339 175.498 1.00 15.79 ? 4347 GLN A N     1 
ATOM   21446 C  CA    . GLN A 1 4347 ? 193.422 266.751 174.244 1.00 14.66 ? 4347 GLN A CA    1 
ATOM   21447 C  C     . GLN A 1 4347 ? 194.816 266.147 174.126 1.00 17.72 ? 4347 GLN A C     1 
ATOM   21448 O  O     . GLN A 1 4347 ? 195.543 266.045 175.114 1.00 25.57 ? 4347 GLN A O     1 
ATOM   21449 C  CB    . GLN A 1 4347 ? 193.504 268.276 174.129 1.00 14.76 ? 4347 GLN A CB    1 
ATOM   21450 C  CG    . GLN A 1 4347 ? 192.163 268.983 174.046 1.00 21.77 ? 4347 GLN A CG    1 
ATOM   21451 C  CD    . GLN A 1 4347 ? 191.371 268.593 172.815 1.00 27.16 ? 4347 GLN A CD    1 
ATOM   21452 O  OE1   . GLN A 1 4347 ? 190.357 267.901 172.909 1.00 23.78 ? 4347 GLN A OE1   1 
ATOM   21453 N  NE2   . GLN A 1 4347 ? 191.834 269.029 171.650 1.00 25.08 ? 4347 GLN A NE2   1 
ATOM   21454 N  N     . PRO A 1 4374 ? 220.325 270.370 196.797 1.00 28.80 ? 4374 PRO A N     1 
ATOM   21455 C  CA    . PRO A 1 4374 ? 219.145 270.193 195.942 1.00 27.17 ? 4374 PRO A CA    1 
ATOM   21456 C  C     . PRO A 1 4374 ? 218.291 271.456 195.848 1.00 31.60 ? 4374 PRO A C     1 
ATOM   21457 O  O     . PRO A 1 4374 ? 218.440 272.358 196.669 1.00 34.84 ? 4374 PRO A O     1 
ATOM   21458 C  CB    . PRO A 1 4374 ? 218.372 269.064 196.633 1.00 28.26 ? 4374 PRO A CB    1 
ATOM   21459 C  CG    . PRO A 1 4374 ? 219.384 268.362 197.475 1.00 28.60 ? 4374 PRO A CG    1 
ATOM   21460 C  CD    . PRO A 1 4374 ? 220.335 269.423 197.922 1.00 32.59 ? 4374 PRO A CD    1 
ATOM   21461 N  N     . ALA A 1 4375 ? 217.415 271.509 194.844 1.00 27.35 ? 4375 ALA A N     1 
ATOM   21462 C  CA    . ALA A 1 4375 ? 216.549 272.673 194.676 1.00 28.87 ? 4375 ALA A CA    1 
ATOM   21463 C  C     . ALA A 1 4375 ? 215.582 272.818 195.844 1.00 36.31 ? 4375 ALA A C     1 
ATOM   21464 O  O     . ALA A 1 4375 ? 215.338 273.933 196.318 1.00 35.68 ? 4375 ALA A O     1 
ATOM   21465 C  CB    . ALA A 1 4375 ? 215.787 272.574 193.355 1.00 30.19 ? 4375 ALA A CB    1 
ATOM   21466 N  N     . TRP A 1 4376 ? 215.018 271.704 196.315 1.00 35.34 ? 4376 TRP A N     1 
ATOM   21467 C  CA    . TRP A 1 4376 ? 214.107 271.761 197.454 1.00 27.87 ? 4376 TRP A CA    1 
ATOM   21468 C  C     . TRP A 1 4376 ? 214.822 272.235 198.712 1.00 28.33 ? 4376 TRP A C     1 
ATOM   21469 O  O     . TRP A 1 4376 ? 214.238 272.951 199.533 1.00 29.74 ? 4376 TRP A O     1 
ATOM   21470 C  CB    . TRP A 1 4376 ? 213.462 270.389 197.677 1.00 26.45 ? 4376 TRP A CB    1 
ATOM   21471 C  CG    . TRP A 1 4376 ? 214.380 269.368 198.287 1.00 28.68 ? 4376 TRP A CG    1 
ATOM   21472 C  CD1   . TRP A 1 4376 ? 215.096 268.417 197.623 1.00 31.83 ? 4376 TRP A CD1   1 
ATOM   21473 C  CD2   . TRP A 1 4376 ? 214.672 269.190 199.680 1.00 34.56 ? 4376 TRP A CD2   1 
ATOM   21474 N  NE1   . TRP A 1 4376 ? 215.822 267.664 198.513 1.00 32.93 ? 4376 TRP A NE1   1 
ATOM   21475 C  CE2   . TRP A 1 4376 ? 215.579 268.119 199.782 1.00 30.99 ? 4376 TRP A CE2   1 
ATOM   21476 C  CE3   . TRP A 1 4376 ? 214.260 269.838 200.849 1.00 26.84 ? 4376 TRP A CE3   1 
ATOM   21477 C  CZ2   . TRP A 1 4376 ? 216.079 267.677 201.004 1.00 27.23 ? 4376 TRP A CZ2   1 
ATOM   21478 C  CZ3   . TRP A 1 4376 ? 214.761 269.402 202.060 1.00 26.15 ? 4376 TRP A CZ3   1 
ATOM   21479 C  CH2   . TRP A 1 4376 ? 215.659 268.331 202.128 1.00 31.72 ? 4376 TRP A CH2   1 
ATOM   21480 N  N     . MET A 1 4377 ? 216.086 271.844 198.881 1.00 28.90 ? 4377 MET A N     1 
ATOM   21481 C  CA    . MET A 1 4377 ? 216.815 272.194 200.095 1.00 31.85 ? 4377 MET A CA    1 
ATOM   21482 C  C     . MET A 1 4377 ? 217.012 273.703 200.202 1.00 29.33 ? 4377 MET A C     1 
ATOM   21483 O  O     . MET A 1 4377 ? 216.930 274.270 201.298 1.00 31.06 ? 4377 MET A O     1 
ATOM   21484 C  CB    . MET A 1 4377 ? 218.153 271.457 200.120 1.00 27.30 ? 4377 MET A CB    1 
ATOM   21485 C  CG    . MET A 1 4377 ? 218.979 271.651 201.382 1.00 32.12 ? 4377 MET A CG    1 
ATOM   21486 S  SD    . MET A 1 4377 ? 220.476 270.644 201.322 1.00 53.08 ? 4377 MET A SD    1 
ATOM   21487 C  CE    . MET A 1 4377 ? 221.294 271.120 202.840 1.00 33.00 ? 4377 MET A CE    1 
ATOM   21488 N  N     . ARG A 1 4378 ? 217.271 274.369 199.075 1.00 29.78 ? 4378 ARG A N     1 
ATOM   21489 C  CA    . ARG A 1 4378 ? 217.430 275.821 199.094 1.00 27.30 ? 4378 ARG A CA    1 
ATOM   21490 C  C     . ARG A 1 4378 ? 216.088 276.531 199.249 1.00 26.83 ? 4378 ARG A C     1 
ATOM   21491 O  O     . ARG A 1 4378 ? 215.977 277.496 200.014 1.00 21.17 ? 4378 ARG A O     1 
ATOM   21492 C  CB    . ARG A 1 4378 ? 218.147 276.294 197.828 1.00 27.71 ? 4378 ARG A CB    1 
ATOM   21493 C  CG    . ARG A 1 4378 ? 219.675 276.262 197.899 1.00 27.51 ? 4378 ARG A CG    1 
ATOM   21494 C  CD    . ARG A 1 4378 ? 220.227 274.870 198.168 1.00 32.59 ? 4378 ARG A CD    1 
ATOM   21495 N  NE    . ARG A 1 4378 ? 221.673 274.882 198.365 1.00 34.52 ? 4378 ARG A NE    1 
ATOM   21496 C  CZ    . ARG A 1 4378 ? 222.401 273.807 198.633 1.00 37.22 ? 4378 ARG A CZ    1 
ATOM   21497 N  NH1   . ARG A 1 4378 ? 221.852 272.608 198.743 1.00 36.46 ? 4378 ARG A NH1   1 
ATOM   21498 N  NH2   . ARG A 1 4378 ? 223.716 273.938 198.794 1.00 30.14 ? 4378 ARG A NH2   1 
ATOM   21499 N  N     . THR A 1 4379 ? 215.060 276.073 198.529 1.00 26.96 ? 4379 THR A N     1 
ATOM   21500 C  CA    . THR A 1 4379 ? 213.757 276.731 198.597 1.00 26.64 ? 4379 THR A CA    1 
ATOM   21501 C  C     . THR A 1 4379 ? 213.140 276.611 199.986 1.00 26.99 ? 4379 THR A C     1 
ATOM   21502 O  O     . THR A 1 4379 ? 212.551 277.574 200.493 1.00 27.46 ? 4379 THR A O     1 
ATOM   21503 C  CB    . THR A 1 4379 ? 212.812 276.151 197.544 1.00 26.87 ? 4379 THR A CB    1 
ATOM   21504 O  OG1   . THR A 1 4379 ? 212.722 274.730 197.709 1.00 26.07 ? 4379 THR A OG1   1 
ATOM   21505 C  CG2   . THR A 1 4379 ? 213.311 276.470 196.140 1.00 30.30 ? 4379 THR A CG2   1 
ATOM   21506 N  N     . LEU A 1 4380 ? 213.260 275.440 200.611 1.00 24.54 ? 4380 LEU A N     1 
ATOM   21507 C  CA    . LEU A 1 4380 ? 212.699 275.257 201.945 1.00 21.53 ? 4380 LEU A CA    1 
ATOM   21508 C  C     . LEU A 1 4380 ? 213.452 276.073 202.989 1.00 19.90 ? 4380 LEU A C     1 
ATOM   21509 O  O     . LEU A 1 4380 ? 212.863 276.481 203.995 1.00 22.19 ? 4380 LEU A O     1 
ATOM   21510 C  CB    . LEU A 1 4380 ? 212.704 273.772 202.312 1.00 22.91 ? 4380 LEU A CB    1 
ATOM   21511 C  CG    . LEU A 1 4380 ? 212.076 273.347 203.643 1.00 18.77 ? 4380 LEU A CG    1 
ATOM   21512 C  CD1   . LEU A 1 4380 ? 210.723 274.005 203.836 1.00 14.91 ? 4380 LEU A CD1   1 
ATOM   21513 C  CD2   . LEU A 1 4380 ? 211.949 271.832 203.708 1.00 18.10 ? 4380 LEU A CD2   1 
ATOM   21514 N  N     . HIS A 1 4381 ? 214.747 276.318 202.771 1.00 20.68 ? 4381 HIS A N     1 
ATOM   21515 C  CA    . HIS A 1 4381 ? 215.511 277.126 203.716 1.00 27.62 ? 4381 HIS A CA    1 
ATOM   21516 C  C     . HIS A 1 4381 ? 214.984 278.553 203.780 1.00 22.73 ? 4381 HIS A C     1 
ATOM   21517 O  O     . HIS A 1 4381 ? 214.843 279.121 204.870 1.00 24.60 ? 4381 HIS A O     1 
ATOM   21518 C  CB    . HIS A 1 4381 ? 216.993 277.120 203.338 1.00 22.69 ? 4381 HIS A CB    1 
ATOM   21519 C  CG    . HIS A 1 4381 ? 217.844 277.964 204.232 1.00 23.95 ? 4381 HIS A CG    1 
ATOM   21520 N  ND1   . HIS A 1 4381 ? 217.992 279.324 204.055 1.00 32.87 ? 4381 HIS A ND1   1 
ATOM   21521 C  CD2   . HIS A 1 4381 ? 218.590 277.646 205.317 1.00 25.26 ? 4381 HIS A CD2   1 
ATOM   21522 C  CE1   . HIS A 1 4381 ? 218.792 279.804 204.989 1.00 26.92 ? 4381 HIS A CE1   1 
ATOM   21523 N  NE2   . HIS A 1 4381 ? 219.169 278.806 205.767 1.00 27.03 ? 4381 HIS A NE2   1 
ATOM   21524 N  N     . THR A 1 4382 ? 214.690 279.150 202.624 1.00 23.16 ? 4382 THR A N     1 
ATOM   21525 C  CA    . THR A 1 4382 ? 214.150 280.505 202.611 1.00 27.36 ? 4382 THR A CA    1 
ATOM   21526 C  C     . THR A 1 4382 ? 212.785 280.557 203.284 1.00 31.78 ? 4382 THR A C     1 
ATOM   21527 O  O     . THR A 1 4382 ? 212.499 281.482 204.053 1.00 31.91 ? 4382 THR A O     1 
ATOM   21528 C  CB    . THR A 1 4382 ? 214.054 281.020 201.175 1.00 27.48 ? 4382 THR A CB    1 
ATOM   21529 O  OG1   . THR A 1 4382 ? 213.255 280.121 200.398 1.00 31.37 ? 4382 THR A OG1   1 
ATOM   21530 C  CG2   . THR A 1 4382 ? 215.441 281.124 200.555 1.00 21.73 ? 4382 THR A CG2   1 
ATOM   21531 N  N     . THR A 1 4383 ? 211.933 279.568 203.009 1.00 23.27 ? 4383 THR A N     1 
ATOM   21532 C  CA    . THR A 1 4383 ? 210.585 279.563 203.567 1.00 22.89 ? 4383 THR A CA    1 
ATOM   21533 C  C     . THR A 1 4383 ? 210.609 279.441 205.086 1.00 25.72 ? 4383 THR A C     1 
ATOM   21534 O  O     . THR A 1 4383 ? 209.885 280.160 205.784 1.00 30.66 ? 4383 THR A O     1 
ATOM   21535 C  CB    . THR A 1 4383 ? 209.775 278.421 202.952 1.00 23.53 ? 4383 THR A CB    1 
ATOM   21536 O  OG1   . THR A 1 4383 ? 209.698 278.601 201.533 1.00 25.33 ? 4383 THR A OG1   1 
ATOM   21537 C  CG2   . THR A 1 4383 ? 208.367 278.402 203.523 1.00 19.64 ? 4383 THR A CG2   1 
ATOM   21538 N  N     . ALA A 1 4384 ? 211.433 278.536 205.615 1.00 27.56 ? 4384 ALA A N     1 
ATOM   21539 C  CA    . ALA A 1 4384 ? 211.491 278.346 207.062 1.00 23.39 ? 4384 ALA A CA    1 
ATOM   21540 C  C     . ALA A 1 4384 ? 212.077 279.567 207.759 1.00 26.45 ? 4384 ALA A C     1 
ATOM   21541 O  O     . ALA A 1 4384 ? 211.590 279.974 208.823 1.00 29.05 ? 4384 ALA A O     1 
ATOM   21542 C  CB    . ALA A 1 4384 ? 212.298 277.094 207.392 1.00 26.44 ? 4384 ALA A CB    1 
ATOM   21543 N  N     . SER A 1 4385 ? 213.124 280.163 207.185 1.00 29.10 ? 4385 SER A N     1 
ATOM   21544 C  CA    . SER A 1 4385 ? 213.689 281.378 207.763 1.00 29.93 ? 4385 SER A CA    1 
ATOM   21545 C  C     . SER A 1 4385 ? 212.678 282.518 207.737 1.00 29.86 ? 4385 SER A C     1 
ATOM   21546 O  O     . SER A 1 4385 ? 212.578 283.289 208.698 1.00 31.97 ? 4385 SER A O     1 
ATOM   21547 C  CB    . SER A 1 4385 ? 214.964 281.773 207.017 1.00 25.55 ? 4385 SER A CB    1 
ATOM   21548 O  OG    . SER A 1 4385 ? 215.941 280.751 207.097 1.00 29.63 ? 4385 SER A OG    1 
ATOM   21549 N  N     . ASN A 1 4386 ? 211.926 282.640 206.641 1.00 27.54 ? 4386 ASN A N     1 
ATOM   21550 C  CA    . ASN A 1 4386 ? 210.904 283.678 206.556 1.00 25.54 ? 4386 ASN A CA    1 
ATOM   21551 C  C     . ASN A 1 4386 ? 209.806 283.458 207.589 1.00 31.74 ? 4386 ASN A C     1 
ATOM   21552 O  O     . ASN A 1 4386 ? 209.327 284.415 208.208 1.00 34.18 ? 4386 ASN A O     1 
ATOM   21553 C  CB    . ASN A 1 4386 ? 210.315 283.718 205.146 1.00 23.82 ? 4386 ASN A CB    1 
ATOM   21554 C  CG    . ASN A 1 4386 ? 211.290 284.264 204.124 1.00 30.40 ? 4386 ASN A CG    1 
ATOM   21555 O  OD1   . ASN A 1 4386 ? 212.370 284.743 204.471 1.00 37.06 ? 4386 ASN A OD1   1 
ATOM   21556 N  ND2   . ASN A 1 4386 ? 210.918 284.189 202.853 1.00 31.13 ? 4386 ASN A ND2   1 
ATOM   21557 N  N     . TRP A 1 4387 ? 209.396 282.202 207.790 1.00 29.36 ? 4387 TRP A N     1 
ATOM   21558 C  CA    . TRP A 1 4387 ? 208.360 281.912 208.774 1.00 21.93 ? 4387 TRP A CA    1 
ATOM   21559 C  C     . TRP A 1 4387 ? 208.813 282.280 210.183 1.00 24.63 ? 4387 TRP A C     1 
ATOM   21560 O  O     . TRP A 1 4387 ? 208.007 282.744 210.998 1.00 33.54 ? 4387 TRP A O     1 
ATOM   21561 C  CB    . TRP A 1 4387 ? 207.966 280.437 208.707 1.00 18.72 ? 4387 TRP A CB    1 
ATOM   21562 C  CG    . TRP A 1 4387 ? 207.064 280.106 207.557 1.00 19.30 ? 4387 TRP A CG    1 
ATOM   21563 C  CD1   . TRP A 1 4387 ? 206.372 280.987 206.781 1.00 18.77 ? 4387 TRP A CD1   1 
ATOM   21564 C  CD2   . TRP A 1 4387 ? 206.745 278.801 207.065 1.00 18.47 ? 4387 TRP A CD2   1 
ATOM   21565 N  NE1   . TRP A 1 4387 ? 205.646 280.312 205.832 1.00 17.64 ? 4387 TRP A NE1   1 
ATOM   21566 C  CE2   . TRP A 1 4387 ? 205.858 278.968 205.985 1.00 15.98 ? 4387 TRP A CE2   1 
ATOM   21567 C  CE3   . TRP A 1 4387 ? 207.127 277.507 207.431 1.00 16.80 ? 4387 TRP A CE3   1 
ATOM   21568 C  CZ2   . TRP A 1 4387 ? 205.346 277.891 205.268 1.00 15.46 ? 4387 TRP A CZ2   1 
ATOM   21569 C  CZ3   . TRP A 1 4387 ? 206.617 276.441 206.718 1.00 18.32 ? 4387 TRP A CZ3   1 
ATOM   21570 C  CH2   . TRP A 1 4387 ? 205.738 276.638 205.649 1.00 21.01 ? 4387 TRP A CH2   1 
ATOM   21571 N  N     . LEU A 1 4388 ? 210.094 282.073 210.491 1.00 24.01 ? 4388 LEU A N     1 
ATOM   21572 C  CA    . LEU A 1 4388 ? 210.603 282.458 211.804 1.00 25.48 ? 4388 LEU A CA    1 
ATOM   21573 C  C     . LEU A 1 4388 ? 210.569 283.966 211.999 1.00 28.37 ? 4388 LEU A C     1 
ATOM   21574 O  O     . LEU A 1 4388 ? 210.518 284.442 213.139 1.00 28.62 ? 4388 LEU A O     1 
ATOM   21575 C  CB    . LEU A 1 4388 ? 212.023 281.929 211.999 1.00 23.10 ? 4388 LEU A CB    1 
ATOM   21576 C  CG    . LEU A 1 4388 ? 212.133 280.453 212.382 1.00 24.06 ? 4388 LEU A CG    1 
ATOM   21577 C  CD1   . LEU A 1 4388 ? 213.567 280.098 212.736 1.00 23.32 ? 4388 LEU A CD1   1 
ATOM   21578 C  CD2   . LEU A 1 4388 ? 211.196 280.132 213.535 1.00 27.84 ? 4388 LEU A CD2   1 
ATOM   21579 N  N     . HIS A 1 4389 ? 210.607 284.731 210.907 1.00 27.38 ? 4389 HIS A N     1 
ATOM   21580 C  CA    . HIS A 1 4389 ? 210.460 286.177 211.018 1.00 30.39 ? 4389 HIS A CA    1 
ATOM   21581 C  C     . HIS A 1 4389 ? 209.020 286.564 211.337 1.00 27.36 ? 4389 HIS A C     1 
ATOM   21582 O  O     . HIS A 1 4389 ? 208.779 287.418 212.197 1.00 28.17 ? 4389 HIS A O     1 
ATOM   21583 C  CB    . HIS A 1 4389 ? 210.927 286.851 209.728 1.00 27.90 ? 4389 HIS A CB    1 
ATOM   21584 C  CG    . HIS A 1 4389 ? 212.303 286.448 209.302 1.00 34.33 ? 4389 HIS A CG    1 
ATOM   21585 N  ND1   . HIS A 1 4389 ? 212.671 286.342 207.977 1.00 35.38 ? 4389 HIS A ND1   1 
ATOM   21586 C  CD2   . HIS A 1 4389 ? 213.403 286.131 210.024 1.00 33.90 ? 4389 HIS A CD2   1 
ATOM   21587 C  CE1   . HIS A 1 4389 ? 213.937 285.973 207.903 1.00 35.60 ? 4389 HIS A CE1   1 
ATOM   21588 N  NE2   . HIS A 1 4389 ? 214.405 285.839 209.131 1.00 39.97 ? 4389 HIS A NE2   1 
ATOM   21589 N  N     . LEU A 1 4390 ? 208.053 285.951 210.652 1.00 27.73 ? 4390 LEU A N     1 
ATOM   21590 C  CA    . LEU A 1 4390 ? 206.654 286.315 210.854 1.00 30.19 ? 4390 LEU A CA    1 
ATOM   21591 C  C     . LEU A 1 4390 ? 206.149 285.852 212.215 1.00 27.77 ? 4390 LEU A C     1 
ATOM   21592 O  O     . LEU A 1 4390 ? 205.512 286.619 212.946 1.00 31.74 ? 4390 LEU A O     1 
ATOM   21593 C  CB    . LEU A 1 4390 ? 205.791 285.726 209.737 1.00 24.19 ? 4390 LEU A CB    1 
ATOM   21594 C  CG    . LEU A 1 4390 ? 206.309 285.868 208.307 1.00 26.69 ? 4390 LEU A CG    1 
ATOM   21595 C  CD1   . LEU A 1 4390 ? 205.372 285.166 207.335 1.00 26.57 ? 4390 LEU A CD1   1 
ATOM   21596 C  CD2   . LEU A 1 4390 ? 206.477 287.333 207.934 1.00 24.74 ? 4390 LEU A CD2   1 
ATOM   21597 N  N     . ILE A 1 4391 ? 206.423 284.602 212.570 1.00 26.24 ? 4391 ILE A N     1 
ATOM   21598 C  CA    . ILE A 1 4391 ? 205.906 284.048 213.826 1.00 22.86 ? 4391 ILE A CA    1 
ATOM   21599 C  C     . ILE A 1 4391 ? 206.563 284.764 215.002 1.00 23.01 ? 4391 ILE A C     1 
ATOM   21600 O  O     . ILE A 1 4391 ? 207.794 284.941 215.006 1.00 25.69 ? 4391 ILE A O     1 
ATOM   21601 C  CB    . ILE A 1 4391 ? 206.156 282.539 213.884 1.00 21.76 ? 4391 ILE A CB    1 
ATOM   21602 C  CG1   . ILE A 1 4391 ? 205.393 281.830 212.763 1.00 21.22 ? 4391 ILE A CG1   1 
ATOM   21603 C  CG2   . ILE A 1 4391 ? 205.745 281.976 215.232 1.00 23.59 ? 4391 ILE A CG2   1 
ATOM   21604 C  CD1   . ILE A 1 4391 ? 205.776 280.379 212.578 1.00 25.23 ? 4391 ILE A CD1   1 
ATOM   21605 N  N     . PRO A 1 4392 ? 205.801 285.202 216.000 1.00 28.64 ? 4392 PRO A N     1 
ATOM   21606 C  CA    . PRO A 1 4392 ? 206.403 285.853 217.168 1.00 24.29 ? 4392 PRO A CA    1 
ATOM   21607 C  C     . PRO A 1 4392 ? 207.244 284.876 217.977 1.00 22.58 ? 4392 PRO A C     1 
ATOM   21608 O  O     . PRO A 1 4392 ? 207.200 283.659 217.791 1.00 30.43 ? 4392 PRO A O     1 
ATOM   21609 C  CB    . PRO A 1 4392 ? 205.191 286.345 217.964 1.00 26.82 ? 4392 PRO A CB    1 
ATOM   21610 C  CG    . PRO A 1 4392 ? 204.070 286.386 216.969 1.00 24.85 ? 4392 PRO A CG    1 
ATOM   21611 C  CD    . PRO A 1 4392 ? 204.331 285.240 216.050 1.00 27.76 ? 4392 PRO A CD    1 
ATOM   21612 N  N     . GLN A 1 4393 ? 208.023 285.438 218.902 1.00 24.24 ? 4393 GLN A N     1 
ATOM   21613 C  CA    . GLN A 1 4393 ? 209.025 284.673 219.628 1.00 23.31 ? 4393 GLN A CA    1 
ATOM   21614 C  C     . GLN A 1 4393 ? 208.787 284.574 221.128 1.00 27.76 ? 4393 GLN A C     1 
ATOM   21615 O  O     . GLN A 1 4393 ? 209.405 283.716 221.770 1.00 30.61 ? 4393 GLN A O     1 
ATOM   21616 C  CB    . GLN A 1 4393 ? 210.420 285.276 219.392 1.00 18.57 ? 4393 GLN A CB    1 
ATOM   21617 C  CG    . GLN A 1 4393 ? 210.606 285.874 218.008 1.00 24.48 ? 4393 GLN A CG    1 
ATOM   21618 C  CD    . GLN A 1 4393 ? 212.049 286.235 217.718 1.00 30.88 ? 4393 GLN A CD    1 
ATOM   21619 O  OE1   . GLN A 1 4393 ? 212.937 286.005 218.539 1.00 34.79 ? 4393 GLN A OE1   1 
ATOM   21620 N  NE2   . GLN A 1 4393 ? 212.291 286.806 216.545 1.00 26.22 ? 4393 GLN A NE2   1 
ATOM   21621 N  N     . THR A 1 4394 ? 207.917 285.401 221.706 1.00 24.20 ? 4394 THR A N     1 
ATOM   21622 C  CA    . THR A 1 4394 ? 207.747 285.458 223.151 1.00 25.92 ? 4394 THR A CA    1 
ATOM   21623 C  C     . THR A 1 4394 ? 206.288 285.240 223.527 1.00 24.61 ? 4394 THR A C     1 
ATOM   21624 O  O     . THR A 1 4394 ? 205.381 285.715 222.840 1.00 28.03 ? 4394 THR A O     1 
ATOM   21625 C  CB    . THR A 1 4394 ? 208.223 286.804 223.719 1.00 32.09 ? 4394 THR A CB    1 
ATOM   21626 O  OG1   . THR A 1 4394 ? 207.410 287.862 223.193 1.00 31.42 ? 4394 THR A OG1   1 
ATOM   21627 C  CG2   . THR A 1 4394 ? 209.677 287.057 223.346 1.00 25.83 ? 4394 THR A CG2   1 
ATOM   21628 N  N     . LEU A 1 4395 ? 206.071 284.517 224.629 1.00 21.76 ? 4395 LEU A N     1 
ATOM   21629 C  CA    . LEU A 1 4395 ? 204.726 284.337 225.177 1.00 24.22 ? 4395 LEU A CA    1 
ATOM   21630 C  C     . LEU A 1 4395 ? 204.886 284.017 226.663 1.00 29.48 ? 4395 LEU A C     1 
ATOM   21631 O  O     . LEU A 1 4395 ? 205.273 282.901 227.019 1.00 31.84 ? 4395 LEU A O     1 
ATOM   21632 C  CB    . LEU A 1 4395 ? 203.969 283.239 224.449 1.00 24.33 ? 4395 LEU A CB    1 
ATOM   21633 C  CG    . LEU A 1 4395 ? 202.445 283.306 224.563 1.00 23.03 ? 4395 LEU A CG    1 
ATOM   21634 C  CD1   . LEU A 1 4395 ? 201.956 284.732 224.351 1.00 25.94 ? 4395 LEU A CD1   1 
ATOM   21635 C  CD2   . LEU A 1 4395 ? 201.781 282.358 223.584 1.00 18.19 ? 4395 LEU A CD2   1 
ATOM   21636 N  N     . SER A 1 4396 ? 204.587 284.998 227.514 1.00 24.92 ? 4396 SER A N     1 
ATOM   21637 C  CA    . SER A 1 4396 ? 204.762 284.851 228.952 1.00 20.41 ? 4396 SER A CA    1 
ATOM   21638 C  C     . SER A 1 4396 ? 203.486 284.312 229.586 1.00 33.77 ? 4396 SER A C     1 
ATOM   21639 O  O     . SER A 1 4396 ? 202.393 284.833 229.341 1.00 34.85 ? 4396 SER A O     1 
ATOM   21640 C  CB    . SER A 1 4396 ? 205.143 286.190 229.585 1.00 23.65 ? 4396 SER A CB    1 
ATOM   21641 O  OG    . SER A 1 4396 ? 204.165 287.180 229.314 1.00 37.27 ? 4396 SER A OG    1 
ATOM   21642 N  N     . HIS A 1 4397 ? 203.631 283.270 230.403 1.00 26.56 ? 4397 HIS A N     1 
ATOM   21643 C  CA    . HIS A 1 4397 ? 202.490 282.684 231.085 1.00 21.31 ? 4397 HIS A CA    1 
ATOM   21644 C  C     . HIS A 1 4397 ? 201.879 283.676 232.068 1.00 33.21 ? 4397 HIS A C     1 
ATOM   21645 O  O     . HIS A 1 4397 ? 202.564 284.536 232.627 1.00 36.11 ? 4397 HIS A O     1 
ATOM   21646 C  CB    . HIS A 1 4397 ? 202.903 281.414 231.830 1.00 22.76 ? 4397 HIS A CB    1 
ATOM   21647 C  CG    . HIS A 1 4397 ? 203.122 280.230 230.940 1.00 29.92 ? 4397 HIS A CG    1 
ATOM   21648 N  ND1   . HIS A 1 4397 ? 202.764 278.951 231.305 1.00 34.59 ? 4397 HIS A ND1   1 
ATOM   21649 C  CD2   . HIS A 1 4397 ? 203.664 280.132 229.702 1.00 30.11 ? 4397 HIS A CD2   1 
ATOM   21650 C  CE1   . HIS A 1 4397 ? 203.075 278.115 230.331 1.00 29.47 ? 4397 HIS A CE1   1 
ATOM   21651 N  NE2   . HIS A 1 4397 ? 203.623 278.806 229.348 1.00 30.44 ? 4397 HIS A NE2   1 
ATOM   21652 N  N     . LEU A 1 4398 ? 200.569 283.555 232.264 1.00 29.60 ? 4398 LEU A N     1 
ATOM   21653 C  CA    . LEU A 1 4398 ? 199.882 284.385 233.242 1.00 24.69 ? 4398 LEU A CA    1 
ATOM   21654 C  C     . LEU A 1 4398 ? 200.315 284.003 234.652 1.00 25.43 ? 4398 LEU A C     1 
ATOM   21655 O  O     . LEU A 1 4398 ? 200.415 282.820 234.989 1.00 28.66 ? 4398 LEU A O     1 
ATOM   21656 C  CB    . LEU A 1 4398 ? 198.367 284.240 233.100 1.00 27.49 ? 4398 LEU A CB    1 
ATOM   21657 C  CG    . LEU A 1 4398 ? 197.726 284.551 231.744 1.00 28.48 ? 4398 LEU A CG    1 
ATOM   21658 C  CD1   . LEU A 1 4398 ? 196.212 284.600 231.874 1.00 22.45 ? 4398 LEU A CD1   1 
ATOM   21659 C  CD2   . LEU A 1 4398 ? 198.261 285.853 231.172 1.00 21.21 ? 4398 LEU A CD2   1 
ATOM   21660 N  N     . LYS A 1 4399 ? 200.567 285.011 235.481 1.00 30.00 ? 4399 LYS A N     1 
ATOM   21661 C  CA    . LYS A 1 4399 ? 201.009 284.779 236.850 1.00 26.14 ? 4399 LYS A CA    1 
ATOM   21662 C  C     . LYS A 1 4399 ? 199.814 284.406 237.717 1.00 25.76 ? 4399 LYS A C     1 
ATOM   21663 O  O     . LYS A 1 4399 ? 198.914 285.224 237.928 1.00 25.02 ? 4399 LYS A O     1 
ATOM   21664 C  CB    . LYS A 1 4399 ? 201.713 286.017 237.401 1.00 24.26 ? 4399 LYS A CB    1 
ATOM   21665 C  CG    . LYS A 1 4399 ? 202.215 285.856 238.827 1.00 22.39 ? 4399 LYS A CG    1 
ATOM   21666 C  CD    . LYS A 1 4399 ? 202.364 287.202 239.513 1.00 26.49 ? 4399 LYS A CD    1 
ATOM   21667 C  CE    . LYS A 1 4399 ? 201.026 287.906 239.654 1.00 25.59 ? 4399 LYS A CE    1 
ATOM   21668 N  NZ    . LYS A 1 4399 ? 201.160 289.219 240.339 1.00 29.58 ? 4399 LYS A NZ    1 
ATOM   21669 N  N     . ARG A 1 4400 ? 199.807 283.173 238.219 1.00 26.52 ? 4400 ARG A N     1 
ATOM   21670 C  CA    . ARG A 1 4400 ? 198.708 282.713 239.056 1.00 23.67 ? 4400 ARG A CA    1 
ATOM   21671 C  C     . ARG A 1 4400 ? 198.752 283.401 240.414 1.00 26.54 ? 4400 ARG A C     1 
ATOM   21672 O  O     . ARG A 1 4400 ? 199.813 283.520 241.034 1.00 33.06 ? 4400 ARG A O     1 
ATOM   21673 C  CB    . ARG A 1 4400 ? 198.764 281.195 239.217 1.00 18.35 ? 4400 ARG A CB    1 
ATOM   21674 C  CG    . ARG A 1 4400 ? 198.741 280.446 237.897 1.00 20.72 ? 4400 ARG A CG    1 
ATOM   21675 C  CD    . ARG A 1 4400 ? 198.528 278.955 238.092 1.00 24.13 ? 4400 ARG A CD    1 
ATOM   21676 N  NE    . ARG A 1 4400 ? 197.235 278.663 238.695 1.00 26.44 ? 4400 ARG A NE    1 
ATOM   21677 C  CZ    . ARG A 1 4400 ? 196.717 277.448 238.808 1.00 20.20 ? 4400 ARG A CZ    1 
ATOM   21678 N  NH1   . ARG A 1 4400 ? 197.334 276.385 238.323 1.00 17.35 ? 4400 ARG A NH1   1 
ATOM   21679 N  NH2   . ARG A 1 4400 ? 195.545 277.296 239.417 1.00 22.58 ? 4400 ARG A NH2   1 
ATOM   21680 N  N     . THR A 1 4401 ? 197.589 283.855 240.874 1.00 29.37 ? 4401 THR A N     1 
ATOM   21681 C  CA    . THR A 1 4401 ? 197.463 284.595 242.120 1.00 29.66 ? 4401 THR A CA    1 
ATOM   21682 C  C     . THR A 1 4401 ? 196.249 284.052 242.860 1.00 33.39 ? 4401 THR A C     1 
ATOM   21683 O  O     . THR A 1 4401 ? 195.353 283.456 242.259 1.00 30.56 ? 4401 THR A O     1 
ATOM   21684 C  CB    . THR A 1 4401 ? 197.338 286.107 241.848 1.00 27.68 ? 4401 THR A CB    1 
ATOM   21685 O  OG1   . THR A 1 4401 ? 198.489 286.555 241.124 1.00 26.41 ? 4401 THR A OG1   1 
ATOM   21686 C  CG2   . THR A 1 4401 ? 197.255 286.908 243.140 1.00 26.51 ? 4401 THR A CG2   1 
ATOM   21687 N  N     . VAL A 1 4402 ? 196.235 284.244 244.184 1.00 34.21 ? 4402 VAL A N     1 
ATOM   21688 C  CA    . VAL A 1 4402 ? 195.147 283.712 245.003 1.00 30.32 ? 4402 VAL A CA    1 
ATOM   21689 C  C     . VAL A 1 4402 ? 193.802 284.264 244.544 1.00 27.92 ? 4402 VAL A C     1 
ATOM   21690 O  O     . VAL A 1 4402 ? 192.799 283.542 244.510 1.00 32.17 ? 4402 VAL A O     1 
ATOM   21691 C  CB    . VAL A 1 4402 ? 195.406 284.001 246.493 1.00 31.50 ? 4402 VAL A CB    1 
ATOM   21692 C  CG1   . VAL A 1 4402 ? 196.509 283.101 247.022 1.00 27.49 ? 4402 VAL A CG1   1 
ATOM   21693 C  CG2   . VAL A 1 4402 ? 195.767 285.466 246.701 1.00 29.85 ? 4402 VAL A CG2   1 
ATOM   21694 N  N     . GLU A 1 4403 ? 193.755 285.547 244.183 1.00 28.09 ? 4403 GLU A N     1 
ATOM   21695 C  CA    . GLU A 1 4403 ? 192.512 286.147 243.713 1.00 26.08 ? 4403 GLU A CA    1 
ATOM   21696 C  C     . GLU A 1 4403 ? 192.365 286.111 242.196 1.00 30.26 ? 4403 GLU A C     1 
ATOM   21697 O  O     . GLU A 1 4403 ? 191.283 286.428 241.689 1.00 29.64 ? 4403 GLU A O     1 
ATOM   21698 C  CB    . GLU A 1 4403 ? 192.390 287.588 244.227 1.00 25.39 ? 4403 GLU A CB    1 
ATOM   21699 C  CG    . GLU A 1 4403 ? 193.479 288.554 243.777 1.00 30.97 ? 4403 GLU A CG    1 
ATOM   21700 C  CD    . GLU A 1 4403 ? 193.179 289.211 242.444 1.00 36.19 ? 4403 GLU A CD    1 
ATOM   21701 O  OE1   . GLU A 1 4403 ? 192.000 289.217 242.033 1.00 39.88 ? 4403 GLU A OE1   1 
ATOM   21702 O  OE2   . GLU A 1 4403 ? 194.119 289.746 241.819 1.00 37.74 ? 4403 GLU A OE2   1 
ATOM   21703 N  N     . ASN A 1 4404 ? 193.414 285.729 241.465 1.00 26.20 ? 4404 ASN A N     1 
ATOM   21704 C  CA    . ASN A 1 4404 ? 193.282 285.512 240.028 1.00 25.37 ? 4404 ASN A CA    1 
ATOM   21705 C  C     . ASN A 1 4404 ? 192.615 284.180 239.714 1.00 28.19 ? 4404 ASN A C     1 
ATOM   21706 O  O     . ASN A 1 4404 ? 191.931 284.062 238.691 1.00 29.38 ? 4404 ASN A O     1 
ATOM   21707 C  CB    . ASN A 1 4404 ? 194.650 285.587 239.349 1.00 23.68 ? 4404 ASN A CB    1 
ATOM   21708 C  CG    . ASN A 1 4404 ? 195.177 287.005 239.251 1.00 28.48 ? 4404 ASN A CG    1 
ATOM   21709 O  OD1   . ASN A 1 4404 ? 195.087 287.779 240.203 1.00 35.06 ? 4404 ASN A OD1   1 
ATOM   21710 N  ND2   . ASN A 1 4404 ? 195.749 287.348 238.104 1.00 26.97 ? 4404 ASN A ND2   1 
ATOM   21711 N  N     . ILE A 1 4405 ? 192.806 283.171 240.567 1.00 25.72 ? 4405 ILE A N     1 
ATOM   21712 C  CA    . ILE A 1 4405 ? 192.189 281.869 240.333 1.00 24.20 ? 4405 ILE A CA    1 
ATOM   21713 C  C     . ILE A 1 4405 ? 190.672 281.974 240.417 1.00 25.44 ? 4405 ILE A C     1 
ATOM   21714 O  O     . ILE A 1 4405 ? 189.952 281.291 239.678 1.00 27.94 ? 4405 ILE A O     1 
ATOM   21715 C  CB    . ILE A 1 4405 ? 192.745 280.829 241.326 1.00 23.10 ? 4405 ILE A CB    1 
ATOM   21716 C  CG1   . ILE A 1 4405 ? 194.263 280.719 241.199 1.00 25.38 ? 4405 ILE A CG1   1 
ATOM   21717 C  CG2   . ILE A 1 4405 ? 192.134 279.472 241.077 1.00 27.63 ? 4405 ILE A CG2   1 
ATOM   21718 C  CD1   . ILE A 1 4405 ? 194.755 280.592 239.774 1.00 24.95 ? 4405 ILE A CD1   1 
ATOM   21719 N  N     . LYS A 1 4406 ? 190.164 282.833 241.300 1.00 26.27 ? 4406 LYS A N     1 
ATOM   21720 C  CA    . LYS A 1 4406 ? 188.729 283.044 241.433 1.00 22.49 ? 4406 LYS A CA    1 
ATOM   21721 C  C     . LYS A 1 4406 ? 188.118 283.790 240.254 1.00 24.15 ? 4406 LYS A C     1 
ATOM   21722 O  O     . LYS A 1 4406 ? 186.887 283.856 240.156 1.00 26.56 ? 4406 LYS A O     1 
ATOM   21723 C  CB    . LYS A 1 4406 ? 188.430 283.804 242.729 1.00 23.37 ? 4406 LYS A CB    1 
ATOM   21724 C  CG    . LYS A 1 4406 ? 189.002 283.151 243.976 1.00 33.05 ? 4406 LYS A CG    1 
ATOM   21725 C  CD    . LYS A 1 4406 ? 188.642 283.935 245.229 1.00 30.20 ? 4406 LYS A CD    1 
ATOM   21726 C  CE    . LYS A 1 4406 ? 189.116 285.376 245.137 1.00 31.27 ? 4406 LYS A CE    1 
ATOM   21727 N  NZ    . LYS A 1 4406 ? 188.822 286.137 246.381 1.00 27.23 ? 4406 LYS A NZ    1 
ATOM   21728 N  N     . ASP A 1 4407 ? 188.933 284.354 239.366 1.00 27.46 ? 4407 ASP A N     1 
ATOM   21729 C  CA    . ASP A 1 4407 ? 188.423 285.092 238.219 1.00 24.00 ? 4407 ASP A CA    1 
ATOM   21730 C  C     . ASP A 1 4407 ? 188.199 284.136 237.055 1.00 26.42 ? 4407 ASP A C     1 
ATOM   21731 O  O     . ASP A 1 4407 ? 189.167 283.532 236.574 1.00 27.58 ? 4407 ASP A O     1 
ATOM   21732 C  CB    . ASP A 1 4407 ? 189.394 286.192 237.817 1.00 25.61 ? 4407 ASP A CB    1 
ATOM   21733 C  CG    . ASP A 1 4407 ? 188.835 287.106 236.746 1.00 29.36 ? 4407 ASP A CG    1 
ATOM   21734 O  OD1   . ASP A 1 4407 ? 187.661 286.935 236.354 1.00 29.69 ? 4407 ASP A OD1   1 
ATOM   21735 O  OD2   . ASP A 1 4407 ? 189.573 288.009 236.298 1.00 36.18 ? 4407 ASP A OD2   1 
ATOM   21736 N  N     . PRO A 1 4408 ? 186.962 283.963 236.582 1.00 24.97 ? 4408 PRO A N     1 
ATOM   21737 C  CA    . PRO A 1 4408 ? 186.731 283.046 235.450 1.00 22.32 ? 4408 PRO A CA    1 
ATOM   21738 C  C     . PRO A 1 4408 ? 187.464 283.440 234.181 1.00 18.49 ? 4408 PRO A C     1 
ATOM   21739 O  O     . PRO A 1 4408 ? 187.899 282.561 233.425 1.00 20.64 ? 4408 PRO A O     1 
ATOM   21740 C  CB    . PRO A 1 4408 ? 185.208 283.104 235.264 1.00 22.83 ? 4408 PRO A CB    1 
ATOM   21741 C  CG    . PRO A 1 4408 ? 184.783 284.365 235.941 1.00 20.11 ? 4408 PRO A CG    1 
ATOM   21742 C  CD    . PRO A 1 4408 ? 185.705 284.525 237.097 1.00 19.62 ? 4408 PRO A CD    1 
ATOM   21743 N  N     . LEU A 1 4409 ? 187.602 284.741 233.914 1.00 21.67 ? 4409 LEU A N     1 
ATOM   21744 C  CA    . LEU A 1 4409 ? 188.309 285.179 232.716 1.00 20.99 ? 4409 LEU A CA    1 
ATOM   21745 C  C     . LEU A 1 4409 ? 189.773 284.762 232.764 1.00 25.71 ? 4409 LEU A C     1 
ATOM   21746 O  O     . LEU A 1 4409 ? 190.336 284.326 231.754 1.00 25.51 ? 4409 LEU A O     1 
ATOM   21747 C  CB    . LEU A 1 4409 ? 188.184 286.693 232.554 1.00 16.92 ? 4409 LEU A CB    1 
ATOM   21748 C  CG    . LEU A 1 4409 ? 187.080 287.183 231.617 1.00 21.62 ? 4409 LEU A CG    1 
ATOM   21749 C  CD1   . LEU A 1 4409 ? 187.073 288.699 231.550 1.00 19.31 ? 4409 LEU A CD1   1 
ATOM   21750 C  CD2   . LEU A 1 4409 ? 187.244 286.585 230.228 1.00 17.85 ? 4409 LEU A CD2   1 
ATOM   21751 N  N     . PHE A 1 4410 ? 190.401 284.887 233.935 1.00 23.76 ? 4410 PHE A N     1 
ATOM   21752 C  CA    . PHE A 1 4410 ? 191.784 284.452 234.087 1.00 21.16 ? 4410 PHE A CA    1 
ATOM   21753 C  C     . PHE A 1 4410 ? 191.910 282.949 233.868 1.00 22.82 ? 4410 PHE A C     1 
ATOM   21754 O  O     . PHE A 1 4410 ? 192.871 282.484 233.246 1.00 21.10 ? 4410 PHE A O     1 
ATOM   21755 C  CB    . PHE A 1 4410 ? 192.296 284.847 235.474 1.00 23.86 ? 4410 PHE A CB    1 
ATOM   21756 C  CG    . PHE A 1 4410 ? 193.779 284.677 235.650 1.00 27.60 ? 4410 PHE A CG    1 
ATOM   21757 C  CD1   . PHE A 1 4410 ? 194.648 285.708 235.338 1.00 22.37 ? 4410 PHE A CD1   1 
ATOM   21758 C  CD2   . PHE A 1 4410 ? 194.301 283.495 236.146 1.00 30.35 ? 4410 PHE A CD2   1 
ATOM   21759 C  CE1   . PHE A 1 4410 ? 196.009 285.559 235.507 1.00 20.28 ? 4410 PHE A CE1   1 
ATOM   21760 C  CE2   . PHE A 1 4410 ? 195.661 283.339 236.316 1.00 28.76 ? 4410 PHE A CE2   1 
ATOM   21761 C  CZ    . PHE A 1 4410 ? 196.516 284.373 235.999 1.00 27.49 ? 4410 PHE A CZ    1 
ATOM   21762 N  N     . ARG A 1 4411 ? 190.940 282.175 234.363 1.00 20.09 ? 4411 ARG A N     1 
ATOM   21763 C  CA    . ARG A 1 4411 ? 191.006 280.723 234.229 1.00 22.46 ? 4411 ARG A CA    1 
ATOM   21764 C  C     . ARG A 1 4411 ? 190.977 280.291 232.767 1.00 25.00 ? 4411 ARG A C     1 
ATOM   21765 O  O     . ARG A 1 4411 ? 191.736 279.404 232.360 1.00 31.58 ? 4411 ARG A O     1 
ATOM   21766 C  CB    . ARG A 1 4411 ? 189.863 280.074 235.005 1.00 20.37 ? 4411 ARG A CB    1 
ATOM   21767 C  CG    . ARG A 1 4411 ? 189.890 280.336 236.497 1.00 13.03 ? 4411 ARG A CG    1 
ATOM   21768 C  CD    . ARG A 1 4411 ? 188.863 279.482 237.217 1.00 22.46 ? 4411 ARG A CD    1 
ATOM   21769 N  NE    . ARG A 1 4411 ? 187.498 279.853 236.864 1.00 23.91 ? 4411 ARG A NE    1 
ATOM   21770 C  CZ    . ARG A 1 4411 ? 186.566 280.202 237.739 1.00 25.41 ? 4411 ARG A CZ    1 
ATOM   21771 N  NH1   . ARG A 1 4411 ? 186.813 280.231 239.038 1.00 20.77 ? 4411 ARG A NH1   1 
ATOM   21772 N  NH2   . ARG A 1 4411 ? 185.355 280.528 237.300 1.00 28.17 ? 4411 ARG A NH2   1 
ATOM   21773 N  N     . PHE A 1 4412 ? 190.106 280.903 231.961 1.00 26.40 ? 4412 PHE A N     1 
ATOM   21774 C  CA    . PHE A 1 4412 ? 190.092 280.593 230.534 1.00 26.93 ? 4412 PHE A CA    1 
ATOM   21775 C  C     . PHE A 1 4412 ? 191.337 281.134 229.842 1.00 24.08 ? 4412 PHE A C     1 
ATOM   21776 O  O     . PHE A 1 4412 ? 191.975 280.432 229.048 1.00 26.99 ? 4412 PHE A O     1 
ATOM   21777 C  CB    . PHE A 1 4412 ? 188.831 281.158 229.877 1.00 22.25 ? 4412 PHE A CB    1 
ATOM   21778 C  CG    . PHE A 1 4412 ? 188.980 281.390 228.402 1.00 19.53 ? 4412 PHE A CG    1 
ATOM   21779 C  CD1   . PHE A 1 4412 ? 188.907 280.334 227.513 1.00 21.28 ? 4412 PHE A CD1   1 
ATOM   21780 C  CD2   . PHE A 1 4412 ? 189.214 282.662 227.908 1.00 16.71 ? 4412 PHE A CD2   1 
ATOM   21781 C  CE1   . PHE A 1 4412 ? 189.054 280.540 226.159 1.00 20.48 ? 4412 PHE A CE1   1 
ATOM   21782 C  CE2   . PHE A 1 4412 ? 189.365 282.874 226.555 1.00 15.03 ? 4412 PHE A CE2   1 
ATOM   21783 C  CZ    . PHE A 1 4412 ? 189.287 281.812 225.680 1.00 18.23 ? 4412 PHE A CZ    1 
ATOM   21784 N  N     . PHE A 1 4413 ? 191.695 282.388 230.125 1.00 19.19 ? 4413 PHE A N     1 
ATOM   21785 C  CA    . PHE A 1 4413 ? 192.836 283.007 229.457 1.00 19.46 ? 4413 PHE A CA    1 
ATOM   21786 C  C     . PHE A 1 4413 ? 194.152 282.341 229.841 1.00 25.44 ? 4413 PHE A C     1 
ATOM   21787 O  O     . PHE A 1 4413 ? 195.089 282.321 229.035 1.00 28.29 ? 4413 PHE A O     1 
ATOM   21788 C  CB    . PHE A 1 4413 ? 192.880 284.500 229.771 1.00 17.70 ? 4413 PHE A CB    1 
ATOM   21789 C  CG    . PHE A 1 4413 ? 192.000 285.331 228.885 1.00 21.62 ? 4413 PHE A CG    1 
ATOM   21790 C  CD1   . PHE A 1 4413 ? 191.936 285.081 227.524 1.00 19.71 ? 4413 PHE A CD1   1 
ATOM   21791 C  CD2   . PHE A 1 4413 ? 191.237 286.361 229.410 1.00 21.25 ? 4413 PHE A CD2   1 
ATOM   21792 C  CE1   . PHE A 1 4413 ? 191.129 285.842 226.705 1.00 19.92 ? 4413 PHE A CE1   1 
ATOM   21793 C  CE2   . PHE A 1 4413 ? 190.432 287.128 228.594 1.00 22.93 ? 4413 PHE A CE2   1 
ATOM   21794 C  CZ    . PHE A 1 4413 ? 190.376 286.867 227.239 1.00 25.67 ? 4413 PHE A CZ    1 
ATOM   21795 N  N     . GLU A 1 4414 ? 194.250 281.803 231.058 1.00 23.80 ? 4414 GLU A N     1 
ATOM   21796 C  CA    . GLU A 1 4414 ? 195.458 281.083 231.446 1.00 25.15 ? 4414 GLU A CA    1 
ATOM   21797 C  C     . GLU A 1 4414 ? 195.639 279.826 230.604 1.00 24.47 ? 4414 GLU A C     1 
ATOM   21798 O  O     . GLU A 1 4414 ? 196.763 279.483 230.218 1.00 26.38 ? 4414 GLU A O     1 
ATOM   21799 C  CB    . GLU A 1 4414 ? 195.406 280.734 232.934 1.00 24.26 ? 4414 GLU A CB    1 
ATOM   21800 C  CG    . GLU A 1 4414 ? 196.565 279.891 233.418 1.00 23.04 ? 4414 GLU A CG    1 
ATOM   21801 C  CD    . GLU A 1 4414 ? 196.188 279.019 234.595 1.00 31.08 ? 4414 GLU A CD    1 
ATOM   21802 O  OE1   . GLU A 1 4414 ? 195.669 277.905 234.368 1.00 35.71 ? 4414 GLU A OE1   1 
ATOM   21803 O  OE2   . GLU A 1 4414 ? 196.403 279.449 235.746 1.00 32.07 ? 4414 GLU A OE2   1 
ATOM   21804 N  N     . ARG A 1 4415 ? 194.542 279.126 230.311 1.00 24.24 ? 4415 ARG A N     1 
ATOM   21805 C  CA    . ARG A 1 4415 ? 194.618 277.955 229.445 1.00 19.30 ? 4415 ARG A CA    1 
ATOM   21806 C  C     . ARG A 1 4415 ? 195.122 278.326 228.058 1.00 26.09 ? 4415 ARG A C     1 
ATOM   21807 O  O     . ARG A 1 4415 ? 195.934 277.603 227.472 1.00 29.78 ? 4415 ARG A O     1 
ATOM   21808 C  CB    . ARG A 1 4415 ? 193.251 277.285 229.343 1.00 20.53 ? 4415 ARG A CB    1 
ATOM   21809 C  CG    . ARG A 1 4415 ? 192.840 276.499 230.564 1.00 24.49 ? 4415 ARG A CG    1 
ATOM   21810 C  CD    . ARG A 1 4415 ? 191.646 275.630 230.242 1.00 18.55 ? 4415 ARG A CD    1 
ATOM   21811 N  NE    . ARG A 1 4415 ? 191.684 275.174 228.859 1.00 18.82 ? 4415 ARG A NE    1 
ATOM   21812 C  CZ    . ARG A 1 4415 ? 190.870 274.263 228.345 1.00 24.40 ? 4415 ARG A CZ    1 
ATOM   21813 N  NH1   . ARG A 1 4415 ? 189.947 273.668 229.081 1.00 16.60 ? 4415 ARG A NH1   1 
ATOM   21814 N  NH2   . ARG A 1 4415 ? 190.989 273.938 227.060 1.00 23.92 ? 4415 ARG A NH2   1 
ATOM   21815 N  N     . GLU A 1 4416 ? 194.650 279.453 227.520 1.00 26.05 ? 4416 GLU A N     1 
ATOM   21816 C  CA    . GLU A 1 4416 ? 195.009 279.845 226.160 1.00 25.82 ? 4416 GLU A CA    1 
ATOM   21817 C  C     . GLU A 1 4416 ? 196.511 280.052 226.021 1.00 25.89 ? 4416 GLU A C     1 
ATOM   21818 O  O     . GLU A 1 4416 ? 197.133 279.561 225.071 1.00 31.04 ? 4416 GLU A O     1 
ATOM   21819 C  CB    . GLU A 1 4416 ? 194.254 281.115 225.766 1.00 23.55 ? 4416 GLU A CB    1 
ATOM   21820 C  CG    . GLU A 1 4416 ? 192.799 280.884 225.402 1.00 23.44 ? 4416 GLU A CG    1 
ATOM   21821 C  CD    . GLU A 1 4416 ? 192.638 280.046 224.152 1.00 25.14 ? 4416 GLU A CD    1 
ATOM   21822 O  OE1   . GLU A 1 4416 ? 193.171 280.444 223.095 1.00 28.51 ? 4416 GLU A OE1   1 
ATOM   21823 O  OE2   . GLU A 1 4416 ? 191.974 278.990 224.223 1.00 24.97 ? 4416 GLU A OE2   1 
ATOM   21824 N  N     . VAL A 1 4417 ? 197.116 280.780 226.962 1.00 23.02 ? 4417 VAL A N     1 
ATOM   21825 C  CA    . VAL A 1 4417 ? 198.554 281.019 226.890 1.00 24.78 ? 4417 VAL A CA    1 
ATOM   21826 C  C     . VAL A 1 4417 ? 199.328 279.738 227.177 1.00 24.26 ? 4417 VAL A C     1 
ATOM   21827 O  O     . VAL A 1 4417 ? 200.339 279.454 226.526 1.00 25.34 ? 4417 VAL A O     1 
ATOM   21828 C  CB    . VAL A 1 4417 ? 198.958 282.157 227.844 1.00 23.95 ? 4417 VAL A CB    1 
ATOM   21829 C  CG1   . VAL A 1 4417 ? 200.463 282.334 227.854 1.00 22.52 ? 4417 VAL A CG1   1 
ATOM   21830 C  CG2   . VAL A 1 4417 ? 198.297 283.449 227.408 1.00 22.08 ? 4417 VAL A CG2   1 
ATOM   21831 N  N     . LYS A 1 4418 ? 198.869 278.944 228.147 1.00 26.88 ? 4418 LYS A N     1 
ATOM   21832 C  CA    . LYS A 1 4418 ? 199.592 277.728 228.510 1.00 25.72 ? 4418 LYS A CA    1 
ATOM   21833 C  C     . LYS A 1 4418 ? 199.678 276.765 227.333 1.00 26.98 ? 4418 LYS A C     1 
ATOM   21834 O  O     . LYS A 1 4418 ? 200.755 276.242 227.024 1.00 31.00 ? 4418 LYS A O     1 
ATOM   21835 C  CB    . LYS A 1 4418 ? 198.927 277.055 229.710 1.00 24.19 ? 4418 LYS A CB    1 
ATOM   21836 C  CG    . LYS A 1 4418 ? 199.911 276.334 230.621 1.00 26.43 ? 4418 LYS A CG    1 
ATOM   21837 C  CD    . LYS A 1 4418 ? 199.245 275.817 231.884 1.00 23.29 ? 4418 LYS A CD    1 
ATOM   21838 C  CE    . LYS A 1 4418 ? 198.496 276.917 232.613 1.00 23.74 ? 4418 LYS A CE    1 
ATOM   21839 N  NZ    . LYS A 1 4418 ? 197.770 276.390 233.803 1.00 21.88 ? 4418 LYS A NZ    1 
ATOM   21840 N  N     . MET A 1 4419 ? 198.556 276.528 226.651 1.00 30.32 ? 4419 MET A N     1 
ATOM   21841 C  CA    . MET A 1 4419 ? 198.610 275.694 225.455 1.00 31.08 ? 4419 MET A CA    1 
ATOM   21842 C  C     . MET A 1 4419 ? 199.214 276.458 224.284 1.00 23.68 ? 4419 MET A C     1 
ATOM   21843 O  O     . MET A 1 4419 ? 199.825 275.860 223.392 1.00 28.13 ? 4419 MET A O     1 
ATOM   21844 C  CB    . MET A 1 4419 ? 197.216 275.172 225.097 1.00 24.97 ? 4419 MET A CB    1 
ATOM   21845 C  CG    . MET A 1 4419 ? 196.217 276.238 224.694 1.00 27.96 ? 4419 MET A CG    1 
ATOM   21846 S  SD    . MET A 1 4419 ? 194.615 275.528 224.274 1.00 57.74 ? 4419 MET A SD    1 
ATOM   21847 C  CE    . MET A 1 4419 ? 194.998 274.751 222.706 1.00 20.82 ? 4419 MET A CE    1 
ATOM   21848 N  N     . GLY A 1 4420 ? 199.058 277.784 224.275 1.00 20.57 ? 4420 GLY A N     1 
ATOM   21849 C  CA    . GLY A 1 4420 ? 199.632 278.587 223.212 1.00 19.46 ? 4420 GLY A CA    1 
ATOM   21850 C  C     . GLY A 1 4420 ? 201.138 278.718 223.297 1.00 22.83 ? 4420 GLY A C     1 
ATOM   21851 O  O     . GLY A 1 4420 ? 201.821 278.721 222.270 1.00 26.25 ? 4420 GLY A O     1 
ATOM   21852 N  N     . ALA A 1 4421 ? 201.676 278.845 224.512 1.00 23.12 ? 4421 ALA A N     1 
ATOM   21853 C  CA    . ALA A 1 4421 ? 203.122 278.957 224.668 1.00 18.22 ? 4421 ALA A CA    1 
ATOM   21854 C  C     . ALA A 1 4421 ? 203.824 277.669 224.264 1.00 19.89 ? 4421 ALA A C     1 
ATOM   21855 O  O     . ALA A 1 4421 ? 204.882 277.707 223.627 1.00 20.90 ? 4421 ALA A O     1 
ATOM   21856 C  CB    . ALA A 1 4421 ? 203.469 279.332 226.107 1.00 21.42 ? 4421 ALA A CB    1 
ATOM   21857 N  N     . LYS A 1 4422 ? 203.251 276.518 224.630 1.00 20.47 ? 4422 LYS A N     1 
ATOM   21858 C  CA    . LYS A 1 4422 ? 203.853 275.240 224.268 1.00 17.21 ? 4422 LYS A CA    1 
ATOM   21859 C  C     . LYS A 1 4422 ? 203.887 275.055 222.756 1.00 23.10 ? 4422 LYS A C     1 
ATOM   21860 O  O     . LYS A 1 4422 ? 204.899 274.613 222.201 1.00 27.55 ? 4422 LYS A O     1 
ATOM   21861 C  CB    . LYS A 1 4422 ? 203.089 274.096 224.932 1.00 22.92 ? 4422 LYS A CB    1 
ATOM   21862 C  CG    . LYS A 1 4422 ? 203.505 272.712 224.462 1.00 22.02 ? 4422 LYS A CG    1 
ATOM   21863 C  CD    . LYS A 1 4422 ? 202.552 271.647 224.975 1.00 16.85 ? 4422 LYS A CD    1 
ATOM   21864 C  CE    . LYS A 1 4422 ? 202.919 270.272 224.441 1.00 25.56 ? 4422 LYS A CE    1 
ATOM   21865 N  NZ    . LYS A 1 4422 ? 201.975 269.221 224.912 1.00 25.40 ? 4422 LYS A NZ    1 
ATOM   21866 N  N     . LEU A 1 4423 ? 202.791 275.392 222.073 1.00 23.79 ? 4423 LEU A N     1 
ATOM   21867 C  CA    . LEU A 1 4423 ? 202.760 275.282 220.619 1.00 21.09 ? 4423 LEU A CA    1 
ATOM   21868 C  C     . LEU A 1 4423 ? 203.738 276.253 219.968 1.00 15.24 ? 4423 LEU A C     1 
ATOM   21869 O  O     . LEU A 1 4423 ? 204.368 275.924 218.957 1.00 18.04 ? 4423 LEU A O     1 
ATOM   21870 C  CB    . LEU A 1 4423 ? 201.339 275.516 220.108 1.00 21.69 ? 4423 LEU A CB    1 
ATOM   21871 C  CG    . LEU A 1 4423 ? 201.097 275.441 218.600 1.00 23.48 ? 4423 LEU A CG    1 
ATOM   21872 C  CD1   . LEU A 1 4423 ? 201.720 274.190 218.004 1.00 19.28 ? 4423 LEU A CD1   1 
ATOM   21873 C  CD2   . LEU A 1 4423 ? 199.607 275.492 218.308 1.00 21.38 ? 4423 LEU A CD2   1 
ATOM   21874 N  N     . LEU A 1 4424 ? 203.875 277.454 220.532 1.00 18.33 ? 4424 LEU A N     1 
ATOM   21875 C  CA    . LEU A 1 4424 ? 204.782 278.446 219.965 1.00 17.31 ? 4424 LEU A CA    1 
ATOM   21876 C  C     . LEU A 1 4424 ? 206.228 277.967 220.013 1.00 20.62 ? 4424 LEU A C     1 
ATOM   21877 O  O     . LEU A 1 4424 ? 206.973 278.107 219.037 1.00 22.84 ? 4424 LEU A O     1 
ATOM   21878 C  CB    . LEU A 1 4424 ? 204.627 279.774 220.705 1.00 16.98 ? 4424 LEU A CB    1 
ATOM   21879 C  CG    . LEU A 1 4424 ? 205.467 280.945 220.192 1.00 23.86 ? 4424 LEU A CG    1 
ATOM   21880 C  CD1   . LEU A 1 4424 ? 205.086 281.298 218.771 1.00 18.97 ? 4424 LEU A CD1   1 
ATOM   21881 C  CD2   . LEU A 1 4424 ? 205.304 282.144 221.105 1.00 21.24 ? 4424 LEU A CD2   1 
ATOM   21882 N  N     . GLN A 1 4425 ? 206.645 277.398 221.146 1.00 22.77 ? 4425 GLN A N     1 
ATOM   21883 C  CA    . GLN A 1 4425 ? 208.017 276.912 221.266 1.00 22.91 ? 4425 GLN A CA    1 
ATOM   21884 C  C     . GLN A 1 4425 ? 208.272 275.725 220.346 1.00 21.20 ? 4425 GLN A C     1 
ATOM   21885 O  O     . GLN A 1 4425 ? 209.350 275.616 219.749 1.00 15.50 ? 4425 GLN A O     1 
ATOM   21886 C  CB    . GLN A 1 4425 ? 208.317 276.546 222.719 1.00 18.35 ? 4425 GLN A CB    1 
ATOM   21887 C  CG    . GLN A 1 4425 ? 208.216 277.716 223.687 1.00 23.11 ? 4425 GLN A CG    1 
ATOM   21888 C  CD    . GLN A 1 4425 ? 208.070 277.273 225.130 1.00 30.52 ? 4425 GLN A CD    1 
ATOM   21889 O  OE1   . GLN A 1 4425 ? 207.091 277.606 225.798 1.00 31.23 ? 4425 GLN A OE1   1 
ATOM   21890 N  NE2   . GLN A 1 4425 ? 209.047 276.517 225.619 1.00 23.18 ? 4425 GLN A NE2   1 
ATOM   21891 N  N     . ASP A 1 4426 ? 207.297 274.819 220.223 1.00 18.58 ? 4426 ASP A N     1 
ATOM   21892 C  CA    . ASP A 1 4426 ? 207.493 273.630 219.399 1.00 17.24 ? 4426 ASP A CA    1 
ATOM   21893 C  C     . ASP A 1 4426 ? 207.671 273.991 217.929 1.00 19.35 ? 4426 ASP A C     1 
ATOM   21894 O  O     . ASP A 1 4426 ? 208.554 273.451 217.254 1.00 20.21 ? 4426 ASP A O     1 
ATOM   21895 C  CB    . ASP A 1 4426 ? 206.318 272.668 219.575 1.00 21.21 ? 4426 ASP A CB    1 
ATOM   21896 C  CG    . ASP A 1 4426 ? 206.190 272.161 220.995 1.00 29.39 ? 4426 ASP A CG    1 
ATOM   21897 O  OD1   . ASP A 1 4426 ? 207.048 272.512 221.832 1.00 26.67 ? 4426 ASP A OD1   1 
ATOM   21898 O  OD2   . ASP A 1 4426 ? 205.231 271.411 221.277 1.00 34.43 ? 4426 ASP A OD2   1 
ATOM   21899 N  N     . VAL A 1 4427 ? 206.843 274.904 217.416 1.00 16.47 ? 4427 VAL A N     1 
ATOM   21900 C  CA    . VAL A 1 4427 ? 206.939 275.280 216.009 1.00 18.14 ? 4427 VAL A CA    1 
ATOM   21901 C  C     . VAL A 1 4427 ? 208.253 275.999 215.734 1.00 17.35 ? 4427 VAL A C     1 
ATOM   21902 O  O     . VAL A 1 4427 ? 208.922 275.734 214.728 1.00 18.26 ? 4427 VAL A O     1 
ATOM   21903 C  CB    . VAL A 1 4427 ? 205.727 276.136 215.600 1.00 13.75 ? 4427 VAL A CB    1 
ATOM   21904 C  CG1   . VAL A 1 4427 ? 205.898 276.655 214.186 1.00 11.98 ? 4427 VAL A CG1   1 
ATOM   21905 C  CG2   . VAL A 1 4427 ? 204.446 275.329 215.722 1.00 17.52 ? 4427 VAL A CG2   1 
ATOM   21906 N  N     . ARG A 1 4428 ? 208.643 276.924 216.615 1.00 17.00 ? 4428 ARG A N     1 
ATOM   21907 C  CA    . ARG A 1 4428 ? 209.887 277.659 216.413 1.00 20.55 ? 4428 ARG A CA    1 
ATOM   21908 C  C     . ARG A 1 4428 ? 211.091 276.730 216.455 1.00 19.47 ? 4428 ARG A C     1 
ATOM   21909 O  O     . ARG A 1 4428 ? 212.019 276.866 215.646 1.00 21.55 ? 4428 ARG A O     1 
ATOM   21910 C  CB    . ARG A 1 4428 ? 210.019 278.764 217.462 1.00 21.02 ? 4428 ARG A CB    1 
ATOM   21911 C  CG    . ARG A 1 4428 ? 209.012 279.891 217.306 1.00 24.22 ? 4428 ARG A CG    1 
ATOM   21912 C  CD    . ARG A 1 4428 ? 209.383 281.094 218.161 1.00 23.13 ? 4428 ARG A CD    1 
ATOM   21913 N  NE    . ARG A 1 4428 ? 210.661 281.678 217.769 1.00 26.24 ? 4428 ARG A NE    1 
ATOM   21914 C  CZ    . ARG A 1 4428 ? 210.869 282.355 216.648 1.00 24.76 ? 4428 ARG A CZ    1 
ATOM   21915 N  NH1   . ARG A 1 4428 ? 209.892 282.587 215.787 1.00 25.85 ? 4428 ARG A NH1   1 
ATOM   21916 N  NH2   . ARG A 1 4428 ? 212.087 282.819 216.387 1.00 22.52 ? 4428 ARG A NH2   1 
ATOM   21917 N  N     . GLN A 1 4429 ? 211.102 275.781 217.394 1.00 18.13 ? 4429 GLN A N     1 
ATOM   21918 C  CA    . GLN A 1 4429 ? 212.209 274.832 217.472 1.00 21.46 ? 4429 GLN A CA    1 
ATOM   21919 C  C     . GLN A 1 4429 ? 212.270 273.949 216.232 1.00 18.74 ? 4429 GLN A C     1 
ATOM   21920 O  O     . GLN A 1 4429 ? 213.356 273.702 215.694 1.00 26.80 ? 4429 GLN A O     1 
ATOM   21921 C  CB    . GLN A 1 4429 ? 212.084 273.980 218.734 1.00 20.95 ? 4429 GLN A CB    1 
ATOM   21922 C  CG    . GLN A 1 4429 ? 213.366 273.269 219.156 1.00 22.12 ? 4429 GLN A CG    1 
ATOM   21923 C  CD    . GLN A 1 4429 ? 214.614 274.116 218.960 1.00 27.51 ? 4429 GLN A CD    1 
ATOM   21924 O  OE1   . GLN A 1 4429 ? 215.216 274.122 217.886 1.00 26.97 ? 4429 GLN A OE1   1 
ATOM   21925 N  NE2   . GLN A 1 4429 ? 215.006 274.838 220.003 1.00 29.86 ? 4429 GLN A NE2   1 
ATOM   21926 N  N     . ASP A 1 4430 ? 211.116 273.467 215.765 1.00 16.31 ? 4430 ASP A N     1 
ATOM   21927 C  CA    . ASP A 1 4430 ? 211.094 272.642 214.559 1.00 17.56 ? 4430 ASP A CA    1 
ATOM   21928 C  C     . ASP A 1 4430 ? 211.577 273.424 213.347 1.00 19.07 ? 4430 ASP A C     1 
ATOM   21929 O  O     . ASP A 1 4430 ? 212.344 272.905 212.529 1.00 21.61 ? 4430 ASP A O     1 
ATOM   21930 C  CB    . ASP A 1 4430 ? 209.685 272.101 214.316 1.00 17.46 ? 4430 ASP A CB    1 
ATOM   21931 C  CG    . ASP A 1 4430 ? 209.260 271.091 215.356 1.00 21.36 ? 4430 ASP A CG    1 
ATOM   21932 O  OD1   . ASP A 1 4430 ? 210.115 270.666 216.160 1.00 22.82 ? 4430 ASP A OD1   1 
ATOM   21933 O  OD2   . ASP A 1 4430 ? 208.067 270.723 215.370 1.00 29.05 ? 4430 ASP A OD2   1 
ATOM   21934 N  N     . LEU A 1 4431 ? 211.136 274.676 213.213 1.00 19.83 ? 4431 LEU A N     1 
ATOM   21935 C  CA    . LEU A 1 4431 ? 211.562 275.498 212.084 1.00 20.09 ? 4431 LEU A CA    1 
ATOM   21936 C  C     . LEU A 1 4431 ? 213.058 275.782 212.140 1.00 20.33 ? 4431 LEU A C     1 
ATOM   21937 O  O     . LEU A 1 4431 ? 213.734 275.780 211.105 1.00 25.60 ? 4431 LEU A O     1 
ATOM   21938 C  CB    . LEU A 1 4431 ? 210.763 276.798 212.054 1.00 21.05 ? 4431 LEU A CB    1 
ATOM   21939 C  CG    . LEU A 1 4431 ? 209.366 276.699 211.439 1.00 20.36 ? 4431 LEU A CG    1 
ATOM   21940 C  CD1   . LEU A 1 4431 ? 208.617 278.010 211.596 1.00 22.38 ? 4431 LEU A CD1   1 
ATOM   21941 C  CD2   . LEU A 1 4431 ? 209.454 276.298 209.975 1.00 15.33 ? 4431 LEU A CD2   1 
ATOM   21942 N  N     . ALA A 1 4432 ? 213.593 276.030 213.338 1.00 21.05 ? 4432 ALA A N     1 
ATOM   21943 C  CA    . ALA A 1 4432 ? 215.021 276.296 213.469 1.00 18.79 ? 4432 ALA A CA    1 
ATOM   21944 C  C     . ALA A 1 4432 ? 215.847 275.077 213.077 1.00 24.70 ? 4432 ALA A C     1 
ATOM   21945 O  O     . ALA A 1 4432 ? 216.905 275.210 212.454 1.00 27.55 ? 4432 ALA A O     1 
ATOM   21946 C  CB    . ALA A 1 4432 ? 215.347 276.732 214.896 1.00 16.39 ? 4432 ALA A CB    1 
ATOM   21947 N  N     . ASP A 1 4433 ? 215.382 273.880 213.444 1.00 23.14 ? 4433 ASP A N     1 
ATOM   21948 C  CA    . ASP A 1 4433 ? 216.084 272.662 213.051 1.00 18.52 ? 4433 ASP A CA    1 
ATOM   21949 C  C     . ASP A 1 4433 ? 216.067 272.480 211.538 1.00 21.44 ? 4433 ASP A C     1 
ATOM   21950 O  O     . ASP A 1 4433 ? 217.069 272.066 210.945 1.00 28.94 ? 4433 ASP A O     1 
ATOM   21951 C  CB    . ASP A 1 4433 ? 215.469 271.453 213.749 1.00 20.22 ? 4433 ASP A CB    1 
ATOM   21952 C  CG    . ASP A 1 4433 ? 215.771 271.421 215.234 1.00 32.53 ? 4433 ASP A CG    1 
ATOM   21953 O  OD1   . ASP A 1 4433 ? 216.528 272.296 215.705 1.00 35.10 ? 4433 ASP A OD1   1 
ATOM   21954 O  OD2   . ASP A 1 4433 ? 215.253 270.522 215.929 1.00 32.59 ? 4433 ASP A OD2   1 
ATOM   21955 N  N     . VAL A 1 4434 ? 214.935 272.787 210.894 1.00 19.33 ? 4434 VAL A N     1 
ATOM   21956 C  CA    . VAL A 1 4434 ? 214.846 272.657 209.441 1.00 20.26 ? 4434 VAL A CA    1 
ATOM   21957 C  C     . VAL A 1 4434 ? 215.831 273.598 208.759 1.00 25.14 ? 4434 VAL A C     1 
ATOM   21958 O  O     . VAL A 1 4434 ? 216.512 273.218 207.799 1.00 23.26 ? 4434 VAL A O     1 
ATOM   21959 C  CB    . VAL A 1 4434 ? 213.402 272.909 208.968 1.00 23.35 ? 4434 VAL A CB    1 
ATOM   21960 C  CG1   . VAL A 1 4434 ? 213.358 273.076 207.458 1.00 19.29 ? 4434 VAL A CG1   1 
ATOM   21961 C  CG2   . VAL A 1 4434 ? 212.500 271.768 209.398 1.00 15.36 ? 4434 VAL A CG2   1 
ATOM   21962 N  N     . VAL A 1 4435 ? 215.927 274.838 209.247 1.00 27.68 ? 4435 VAL A N     1 
ATOM   21963 C  CA    . VAL A 1 4435 ? 216.900 275.779 208.696 1.00 28.44 ? 4435 VAL A CA    1 
ATOM   21964 C  C     . VAL A 1 4435 ? 218.313 275.238 208.860 1.00 29.30 ? 4435 VAL A C     1 
ATOM   21965 O  O     . VAL A 1 4435 ? 219.121 275.273 207.926 1.00 32.45 ? 4435 VAL A O     1 
ATOM   21966 C  CB    . VAL A 1 4435 ? 216.750 277.158 209.363 1.00 20.83 ? 4435 VAL A CB    1 
ATOM   21967 C  CG1   . VAL A 1 4435 ? 217.834 278.103 208.874 1.00 25.05 ? 4435 VAL A CG1   1 
ATOM   21968 C  CG2   . VAL A 1 4435 ? 215.377 277.735 209.088 1.00 28.81 ? 4435 VAL A CG2   1 
ATOM   21969 N  N     . GLN A 1 4436 ? 218.627 274.724 210.049 1.00 27.43 ? 4436 GLN A N     1 
ATOM   21970 C  CA    . GLN A 1 4436 ? 219.965 274.196 210.292 1.00 27.05 ? 4436 GLN A CA    1 
ATOM   21971 C  C     . GLN A 1 4436 ? 220.224 272.949 209.453 1.00 25.69 ? 4436 GLN A C     1 
ATOM   21972 O  O     . GLN A 1 4436 ? 221.351 272.727 208.995 1.00 26.39 ? 4436 GLN A O     1 
ATOM   21973 C  CB    . GLN A 1 4436 ? 220.140 273.910 211.783 1.00 19.16 ? 4436 GLN A CB    1 
ATOM   21974 C  CG    . GLN A 1 4436 ? 221.462 273.281 212.151 1.00 31.18 ? 4436 GLN A CG    1 
ATOM   21975 C  CD    . GLN A 1 4436 ? 221.698 273.258 213.646 1.00 34.42 ? 4436 GLN A CD    1 
ATOM   21976 O  OE1   . GLN A 1 4436 ? 220.881 273.755 214.422 1.00 32.60 ? 4436 GLN A OE1   1 
ATOM   21977 N  NE2   . GLN A 1 4436 ? 222.820 272.681 214.061 1.00 29.25 ? 4436 GLN A NE2   1 
ATOM   21978 N  N     . VAL A 1 4437 ? 219.194 272.128 209.236 1.00 24.86 ? 4437 VAL A N     1 
ATOM   21979 C  CA    . VAL A 1 4437 ? 219.334 270.976 208.347 1.00 24.36 ? 4437 VAL A CA    1 
ATOM   21980 C  C     . VAL A 1 4437 ? 219.627 271.441 206.925 1.00 22.15 ? 4437 VAL A C     1 
ATOM   21981 O  O     . VAL A 1 4437 ? 220.528 270.925 206.255 1.00 25.70 ? 4437 VAL A O     1 
ATOM   21982 C  CB    . VAL A 1 4437 ? 218.072 270.097 208.403 1.00 20.31 ? 4437 VAL A CB    1 
ATOM   21983 C  CG1   . VAL A 1 4437 ? 217.990 269.200 207.176 1.00 14.96 ? 4437 VAL A CG1   1 
ATOM   21984 C  CG2   . VAL A 1 4437 ? 218.063 269.268 209.666 1.00 19.78 ? 4437 VAL A CG2   1 
ATOM   21985 N  N     . CYS A 1 4438 ? 218.876 272.437 206.451 1.00 26.23 ? 4438 CYS A N     1 
ATOM   21986 C  CA    . CYS A 1 4438 ? 219.057 272.947 205.099 1.00 27.38 ? 4438 CYS A CA    1 
ATOM   21987 C  C     . CYS A 1 4438 ? 220.348 273.738 204.936 1.00 27.34 ? 4438 CYS A C     1 
ATOM   21988 O  O     . CYS A 1 4438 ? 220.701 274.085 203.804 1.00 33.98 ? 4438 CYS A O     1 
ATOM   21989 C  CB    . CYS A 1 4438 ? 217.859 273.808 204.699 1.00 22.33 ? 4438 CYS A CB    1 
ATOM   21990 S  SG    . CYS A 1 4438 ? 216.301 272.895 204.619 1.00 55.20 ? 4438 CYS A SG    1 
ATOM   21991 N  N     . GLU A 1 4439 ? 221.045 274.043 206.024 1.00 25.73 ? 4439 GLU A N     1 
ATOM   21992 C  CA    . GLU A 1 4439 ? 222.391 274.591 205.956 1.00 22.07 ? 4439 GLU A CA    1 
ATOM   21993 C  C     . GLU A 1 4439 ? 223.459 273.523 206.139 1.00 27.41 ? 4439 GLU A C     1 
ATOM   21994 O  O     . GLU A 1 4439 ? 224.649 273.855 206.183 1.00 34.31 ? 4439 GLU A O     1 
ATOM   21995 C  CB    . GLU A 1 4439 ? 222.568 275.696 207.000 1.00 25.83 ? 4439 GLU A CB    1 
ATOM   21996 C  CG    . GLU A 1 4439 ? 222.010 277.040 206.568 1.00 25.76 ? 4439 GLU A CG    1 
ATOM   21997 C  CD    . GLU A 1 4439 ? 222.104 278.090 207.659 1.00 34.30 ? 4439 GLU A CD    1 
ATOM   21998 O  OE1   . GLU A 1 4439 ? 222.578 277.760 208.765 1.00 35.20 ? 4439 GLU A OE1   1 
ATOM   21999 O  OE2   . GLU A 1 4439 ? 221.704 279.247 207.408 1.00 37.10 ? 4439 GLU A OE2   1 
ATOM   22000 N  N     . GLY A 1 4440 ? 223.064 272.258 206.239 1.00 28.04 ? 4440 GLY A N     1 
ATOM   22001 C  CA    . GLY A 1 4440 ? 224.017 271.173 206.408 1.00 23.27 ? 4440 GLY A CA    1 
ATOM   22002 C  C     . GLY A 1 4440 ? 224.807 271.239 207.696 1.00 27.55 ? 4440 GLY A C     1 
ATOM   22003 O  O     . GLY A 1 4440 ? 226.022 271.006 207.687 1.00 32.90 ? 4440 GLY A O     1 
ATOM   22004 N  N     . LYS A 1 4441 ? 224.142 271.551 208.810 1.00 25.86 ? 4441 LYS A N     1 
ATOM   22005 C  CA    . LYS A 1 4441 ? 224.810 271.647 210.098 1.00 27.07 ? 4441 LYS A CA    1 
ATOM   22006 C  C     . LYS A 1 4441 ? 224.340 270.627 211.126 1.00 28.13 ? 4441 LYS A C     1 
ATOM   22007 O  O     . LYS A 1 4441 ? 225.087 270.349 212.069 1.00 35.52 ? 4441 LYS A O     1 
ATOM   22008 C  CB    . LYS A 1 4441 ? 224.646 273.057 210.688 1.00 28.48 ? 4441 LYS A CB    1 
ATOM   22009 C  CG    . LYS A 1 4441 ? 225.178 274.170 209.798 1.00 29.43 ? 4441 LYS A CG    1 
ATOM   22010 C  CD    . LYS A 1 4441 ? 224.929 275.533 210.422 1.00 31.79 ? 4441 LYS A CD    1 
ATOM   22011 C  CE    . LYS A 1 4441 ? 225.562 276.643 209.600 1.00 34.04 ? 4441 LYS A CE    1 
ATOM   22012 N  NZ    . LYS A 1 4441 ? 225.288 277.985 210.184 1.00 33.58 ? 4441 LYS A NZ    1 
ATOM   22013 N  N     . LYS A 1 4442 ? 223.141 270.068 210.983 1.00 26.04 ? 4442 LYS A N     1 
ATOM   22014 C  CA    . LYS A 1 4442 ? 222.692 268.972 211.827 1.00 24.97 ? 4442 LYS A CA    1 
ATOM   22015 C  C     . LYS A 1 4442 ? 222.093 267.878 210.955 1.00 21.64 ? 4442 LYS A C     1 
ATOM   22016 O  O     . LYS A 1 4442 ? 221.480 268.161 209.921 1.00 14.92 ? 4442 LYS A O     1 
ATOM   22017 C  CB    . LYS A 1 4442 ? 221.679 269.438 212.886 1.00 25.31 ? 4442 LYS A CB    1 
ATOM   22018 C  CG    . LYS A 1 4442 ? 220.337 269.882 212.345 1.00 25.72 ? 4442 LYS A CG    1 
ATOM   22019 C  CD    . LYS A 1 4442 ? 219.307 269.996 213.456 1.00 22.36 ? 4442 LYS A CD    1 
ATOM   22020 C  CE    . LYS A 1 4442 ? 219.155 268.684 214.202 1.00 23.50 ? 4442 LYS A CE    1 
ATOM   22021 N  NZ    . LYS A 1 4442 ? 218.100 268.750 215.249 1.00 25.39 ? 4442 LYS A NZ    1 
ATOM   22022 N  N     . LYS A 1 4443 ? 222.284 266.631 211.375 1.00 24.09 ? 4443 LYS A N     1 
ATOM   22023 C  CA    . LYS A 1 4443 ? 221.911 265.481 210.564 1.00 16.96 ? 4443 LYS A CA    1 
ATOM   22024 C  C     . LYS A 1 4443 ? 220.405 265.241 210.619 1.00 17.49 ? 4443 LYS A C     1 
ATOM   22025 O  O     . LYS A 1 4443 ? 219.749 265.474 211.637 1.00 24.73 ? 4443 LYS A O     1 
ATOM   22026 C  CB    . LYS A 1 4443 ? 222.689 264.247 211.033 1.00 14.84 ? 4443 LYS A CB    1 
ATOM   22027 C  CG    . LYS A 1 4443 ? 222.431 262.952 210.273 1.00 18.02 ? 4443 LYS A CG    1 
ATOM   22028 C  CD    . LYS A 1 4443 ? 221.352 262.116 210.943 1.00 20.76 ? 4443 LYS A CD    1 
ATOM   22029 C  CE    . LYS A 1 4443 ? 221.852 261.536 212.253 1.00 23.16 ? 4443 LYS A CE    1 
ATOM   22030 N  NZ    . LYS A 1 4443 ? 220.820 260.704 212.927 1.00 25.99 ? 4443 LYS A NZ    1 
ATOM   22031 N  N     . GLN A 1 4444 ? 219.859 264.763 209.501 1.00 16.49 ? 4444 GLN A N     1 
ATOM   22032 C  CA    . GLN A 1 4444 ? 218.421 264.564 209.382 1.00 18.93 ? 4444 GLN A CA    1 
ATOM   22033 C  C     . GLN A 1 4444 ? 217.972 263.337 210.165 1.00 17.39 ? 4444 GLN A C     1 
ATOM   22034 O  O     . GLN A 1 4444 ? 218.399 262.214 209.881 1.00 21.31 ? 4444 GLN A O     1 
ATOM   22035 C  CB    . GLN A 1 4444 ? 218.035 264.416 207.913 1.00 15.69 ? 4444 GLN A CB    1 
ATOM   22036 C  CG    . GLN A 1 4444 ? 216.740 265.100 207.529 1.00 18.72 ? 4444 GLN A CG    1 
ATOM   22037 C  CD    . GLN A 1 4444 ? 216.581 265.228 206.029 1.00 24.01 ? 4444 GLN A CD    1 
ATOM   22038 O  OE1   . GLN A 1 4444 ? 217.521 264.993 205.272 1.00 31.98 ? 4444 GLN A OE1   1 
ATOM   22039 N  NE2   . GLN A 1 4444 ? 215.381 265.589 205.588 1.00 22.00 ? 4444 GLN A NE2   1 
ATOM   22040 N  N     . THR A 1 4445 ? 217.087 263.546 211.137 1.00 17.33 ? 4445 THR A N     1 
ATOM   22041 C  CA    . THR A 1 4445 ? 216.523 262.470 211.932 1.00 11.95 ? 4445 THR A CA    1 
ATOM   22042 C  C     . THR A 1 4445 ? 215.198 262.015 211.323 1.00 10.51 ? 4445 THR A C     1 
ATOM   22043 O  O     . THR A 1 4445 ? 214.713 262.575 210.338 1.00 15.12 ? 4445 THR A O     1 
ATOM   22044 C  CB    . THR A 1 4445 ? 216.335 262.915 213.385 1.00 7.28  ? 4445 THR A CB    1 
ATOM   22045 O  OG1   . THR A 1 4445 ? 215.161 263.730 213.491 1.00 8.76  ? 4445 THR A OG1   1 
ATOM   22046 C  CG2   . THR A 1 4445 ? 217.539 263.711 213.852 1.00 8.15  ? 4445 THR A CG2   1 
ATOM   22047 N  N     . ASN A 1 4446 ? 214.607 260.976 211.921 1.00 9.03  ? 4446 ASN A N     1 
ATOM   22048 C  CA    . ASN A 1 4446 ? 213.322 260.480 211.439 1.00 11.36 ? 4446 ASN A CA    1 
ATOM   22049 C  C     . ASN A 1 4446 ? 212.234 261.538 211.570 1.00 9.68  ? 4446 ASN A C     1 
ATOM   22050 O  O     . ASN A 1 4446 ? 211.420 261.719 210.657 1.00 13.52 ? 4446 ASN A O     1 
ATOM   22051 C  CB    . ASN A 1 4446 ? 212.923 259.214 212.197 1.00 5.86  ? 4446 ASN A CB    1 
ATOM   22052 C  CG    . ASN A 1 4446 ? 213.694 257.998 211.740 1.00 6.29  ? 4446 ASN A CG    1 
ATOM   22053 O  OD1   . ASN A 1 4446 ? 214.100 257.908 210.583 1.00 15.85 ? 4446 ASN A OD1   1 
ATOM   22054 N  ND2   . ASN A 1 4446 ? 213.901 257.052 212.648 1.00 4.13  ? 4446 ASN A ND2   1 
ATOM   22055 N  N     . TYR A 1 4447 ? 212.199 262.241 212.705 1.00 6.19  ? 4447 TYR A N     1 
ATOM   22056 C  CA    . TYR A 1 4447 ? 211.215 263.302 212.886 1.00 11.89 ? 4447 TYR A CA    1 
ATOM   22057 C  C     . TYR A 1 4447 ? 211.417 264.417 211.869 1.00 15.74 ? 4447 TYR A C     1 
ATOM   22058 O  O     . TYR A 1 4447 ? 210.450 264.913 211.279 1.00 12.64 ? 4447 TYR A O     1 
ATOM   22059 C  CB    . TYR A 1 4447 ? 211.298 263.856 214.308 1.00 8.59  ? 4447 TYR A CB    1 
ATOM   22060 C  CG    . TYR A 1 4447 ? 210.396 265.042 214.553 1.00 13.80 ? 4447 TYR A CG    1 
ATOM   22061 C  CD1   . TYR A 1 4447 ? 209.036 264.868 214.773 1.00 16.80 ? 4447 TYR A CD1   1 
ATOM   22062 C  CD2   . TYR A 1 4447 ? 210.901 266.336 214.555 1.00 19.25 ? 4447 TYR A CD2   1 
ATOM   22063 C  CE1   . TYR A 1 4447 ? 208.206 265.949 214.994 1.00 21.81 ? 4447 TYR A CE1   1 
ATOM   22064 C  CE2   . TYR A 1 4447 ? 210.078 267.424 214.775 1.00 18.76 ? 4447 TYR A CE2   1 
ATOM   22065 C  CZ    . TYR A 1 4447 ? 208.731 267.224 214.995 1.00 24.34 ? 4447 TYR A CZ    1 
ATOM   22066 O  OH    . TYR A 1 4447 ? 207.906 268.301 215.213 1.00 28.56 ? 4447 TYR A OH    1 
ATOM   22067 N  N     . LEU A 1 4448 ? 212.668 264.820 211.650 1.00 15.21 ? 4448 LEU A N     1 
ATOM   22068 C  CA    . LEU A 1 4448 ? 212.949 265.873 210.682 1.00 10.50 ? 4448 LEU A CA    1 
ATOM   22069 C  C     . LEU A 1 4448 ? 212.622 265.425 209.263 1.00 15.54 ? 4448 LEU A C     1 
ATOM   22070 O  O     . LEU A 1 4448 ? 212.106 266.213 208.465 1.00 24.80 ? 4448 LEU A O     1 
ATOM   22071 C  CB    . LEU A 1 4448 ? 214.408 266.310 210.794 1.00 12.51 ? 4448 LEU A CB    1 
ATOM   22072 C  CG    . LEU A 1 4448 ? 214.735 267.110 212.057 1.00 14.75 ? 4448 LEU A CG    1 
ATOM   22073 C  CD1   . LEU A 1 4448 ? 216.216 267.422 212.133 1.00 15.48 ? 4448 LEU A CD1   1 
ATOM   22074 C  CD2   . LEU A 1 4448 ? 213.910 268.390 212.109 1.00 11.32 ? 4448 LEU A CD2   1 
ATOM   22075 N  N     . ARG A 1 4449 ? 212.904 264.160 208.935 1.00 12.94 ? 4449 ARG A N     1 
ATOM   22076 C  CA    . ARG A 1 4449 ? 212.539 263.645 207.620 1.00 12.28 ? 4449 ARG A CA    1 
ATOM   22077 C  C     . ARG A 1 4449 ? 211.032 263.701 207.409 1.00 15.07 ? 4449 ARG A C     1 
ATOM   22078 O  O     . ARG A 1 4449 ? 210.560 264.082 206.330 1.00 16.55 ? 4449 ARG A O     1 
ATOM   22079 C  CB    . ARG A 1 4449 ? 213.050 262.213 207.451 1.00 12.18 ? 4449 ARG A CB    1 
ATOM   22080 C  CG    . ARG A 1 4449 ? 214.537 262.107 207.159 1.00 16.60 ? 4449 ARG A CG    1 
ATOM   22081 C  CD    . ARG A 1 4449 ? 214.925 260.688 206.756 1.00 15.62 ? 4449 ARG A CD    1 
ATOM   22082 N  NE    . ARG A 1 4449 ? 215.374 259.890 207.891 1.00 12.12 ? 4449 ARG A NE    1 
ATOM   22083 C  CZ    . ARG A 1 4449 ? 216.537 260.044 208.510 1.00 15.76 ? 4449 ARG A CZ    1 
ATOM   22084 N  NH1   . ARG A 1 4449 ? 217.416 260.951 208.114 1.00 17.61 ? 4449 ARG A NH1   1 
ATOM   22085 N  NH2   . ARG A 1 4449 ? 216.827 259.268 209.549 1.00 10.53 ? 4449 ARG A NH2   1 
ATOM   22086 N  N     . THR A 1 4450 ? 210.258 263.323 208.429 1.00 14.59 ? 4450 THR A N     1 
ATOM   22087 C  CA    . THR A 1 4450 ? 208.804 263.401 208.327 1.00 14.08 ? 4450 THR A CA    1 
ATOM   22088 C  C     . THR A 1 4450 ? 208.334 264.847 208.209 1.00 20.65 ? 4450 THR A C     1 
ATOM   22089 O  O     . THR A 1 4450 ? 207.463 265.161 207.388 1.00 16.88 ? 4450 THR A O     1 
ATOM   22090 C  CB    . THR A 1 4450 ? 208.161 262.722 209.538 1.00 10.15 ? 4450 THR A CB    1 
ATOM   22091 O  OG1   . THR A 1 4450 ? 208.357 261.306 209.451 1.00 24.96 ? 4450 THR A OG1   1 
ATOM   22092 C  CG2   . THR A 1 4450 ? 206.673 263.018 209.599 1.00 9.91  ? 4450 THR A CG2   1 
ATOM   22093 N  N     . LEU A 1 4451 ? 208.906 265.741 209.017 1.00 15.40 ? 4451 LEU A N     1 
ATOM   22094 C  CA    . LEU A 1 4451 ? 208.511 267.144 208.970 1.00 14.44 ? 4451 LEU A CA    1 
ATOM   22095 C  C     . LEU A 1 4451 ? 208.909 267.792 207.650 1.00 19.78 ? 4451 LEU A C     1 
ATOM   22096 O  O     . LEU A 1 4451 ? 208.136 268.563 207.072 1.00 23.75 ? 4451 LEU A O     1 
ATOM   22097 C  CB    . LEU A 1 4451 ? 209.129 267.898 210.147 1.00 16.71 ? 4451 LEU A CB    1 
ATOM   22098 C  CG    . LEU A 1 4451 ? 208.945 269.415 210.200 1.00 12.68 ? 4451 LEU A CG    1 
ATOM   22099 C  CD1   . LEU A 1 4451 ? 207.513 269.770 210.538 1.00 18.11 ? 4451 LEU A CD1   1 
ATOM   22100 C  CD2   . LEU A 1 4451 ? 209.897 270.019 211.214 1.00 15.33 ? 4451 LEU A CD2   1 
ATOM   22101 N  N     . ILE A 1 4452 ? 210.111 267.486 207.159 1.00 20.80 ? 4452 ILE A N     1 
ATOM   22102 C  CA    . ILE A 1 4452 ? 210.587 268.100 205.925 1.00 18.34 ? 4452 ILE A CA    1 
ATOM   22103 C  C     . ILE A 1 4452 ? 209.750 267.639 204.737 1.00 15.50 ? 4452 ILE A C     1 
ATOM   22104 O  O     . ILE A 1 4452 ? 209.445 268.428 203.834 1.00 19.95 ? 4452 ILE A O     1 
ATOM   22105 C  CB    . ILE A 1 4452 ? 212.086 267.805 205.734 1.00 14.64 ? 4452 ILE A CB    1 
ATOM   22106 C  CG1   . ILE A 1 4452 ? 212.911 268.722 206.639 1.00 18.55 ? 4452 ILE A CG1   1 
ATOM   22107 C  CG2   . ILE A 1 4452 ? 212.497 267.958 204.280 1.00 15.50 ? 4452 ILE A CG2   1 
ATOM   22108 C  CD1   . ILE A 1 4452 ? 214.403 268.613 206.441 1.00 19.22 ? 4452 ILE A CD1   1 
ATOM   22109 N  N     . ASN A 1 4453 ? 209.351 266.364 204.722 1.00 17.66 ? 4453 ASN A N     1 
ATOM   22110 C  CA    . ASN A 1 4453 ? 208.508 265.871 203.638 1.00 20.57 ? 4453 ASN A CA    1 
ATOM   22111 C  C     . ASN A 1 4453 ? 207.174 266.606 203.594 1.00 19.22 ? 4453 ASN A C     1 
ATOM   22112 O  O     . ASN A 1 4453 ? 206.698 266.975 202.513 1.00 20.55 ? 4453 ASN A O     1 
ATOM   22113 C  CB    . ASN A 1 4453 ? 208.288 264.365 203.779 1.00 18.03 ? 4453 ASN A CB    1 
ATOM   22114 C  CG    . ASN A 1 4453 ? 209.391 263.552 203.126 1.00 31.16 ? 4453 ASN A CG    1 
ATOM   22115 O  OD1   . ASN A 1 4453 ? 210.018 262.706 203.766 1.00 31.11 ? 4453 ASN A OD1   1 
ATOM   22116 N  ND2   . ASN A 1 4453 ? 209.636 263.808 201.847 1.00 28.58 ? 4453 ASN A ND2   1 
ATOM   22117 N  N     . GLU A 1 4454 ? 206.557 266.832 204.757 1.00 17.84 ? 4454 GLU A N     1 
ATOM   22118 C  CA    . GLU A 1 4454 ? 205.299 267.573 204.795 1.00 14.82 ? 4454 GLU A CA    1 
ATOM   22119 C  C     . GLU A 1 4454 ? 205.481 269.002 204.300 1.00 15.89 ? 4454 GLU A C     1 
ATOM   22120 O  O     . GLU A 1 4454 ? 204.656 269.514 203.537 1.00 15.49 ? 4454 GLU A O     1 
ATOM   22121 C  CB    . GLU A 1 4454 ? 204.732 267.574 206.214 1.00 16.19 ? 4454 GLU A CB    1 
ATOM   22122 C  CG    . GLU A 1 4454 ? 204.118 266.260 206.651 1.00 16.90 ? 4454 GLU A CG    1 
ATOM   22123 C  CD    . GLU A 1 4454 ? 204.127 266.094 208.158 1.00 24.88 ? 4454 GLU A CD    1 
ATOM   22124 O  OE1   . GLU A 1 4454 ? 204.712 266.956 208.846 1.00 22.25 ? 4454 GLU A OE1   1 
ATOM   22125 O  OE2   . GLU A 1 4454 ? 203.548 265.105 208.655 1.00 28.50 ? 4454 GLU A OE2   1 
ATOM   22126 N  N     . LEU A 1 4455 ? 206.562 269.661 204.723 1.00 16.88 ? 4455 LEU A N     1 
ATOM   22127 C  CA    . LEU A 1 4455 ? 206.788 271.049 204.336 1.00 19.03 ? 4455 LEU A CA    1 
ATOM   22128 C  C     . LEU A 1 4455 ? 207.018 271.181 202.834 1.00 20.21 ? 4455 LEU A C     1 
ATOM   22129 O  O     . LEU A 1 4455 ? 206.580 272.161 202.221 1.00 25.01 ? 4455 LEU A O     1 
ATOM   22130 C  CB    . LEU A 1 4455 ? 207.970 271.620 205.116 1.00 19.87 ? 4455 LEU A CB    1 
ATOM   22131 C  CG    . LEU A 1 4455 ? 207.715 271.848 206.607 1.00 20.55 ? 4455 LEU A CG    1 
ATOM   22132 C  CD1   . LEU A 1 4455 ? 208.909 272.518 207.270 1.00 14.98 ? 4455 LEU A CD1   1 
ATOM   22133 C  CD2   . LEU A 1 4455 ? 206.449 272.667 206.812 1.00 13.86 ? 4455 LEU A CD2   1 
ATOM   22134 N  N     . VAL A 1 4456 ? 207.712 270.215 202.229 1.00 18.64 ? 4456 VAL A N     1 
ATOM   22135 C  CA    . VAL A 1 4456 ? 207.904 270.239 200.781 1.00 20.54 ? 4456 VAL A CA    1 
ATOM   22136 C  C     . VAL A 1 4456 ? 206.571 270.087 200.061 1.00 20.18 ? 4456 VAL A C     1 
ATOM   22137 O  O     . VAL A 1 4456 ? 206.293 270.793 199.085 1.00 24.08 ? 4456 VAL A O     1 
ATOM   22138 C  CB    . VAL A 1 4456 ? 208.910 269.151 200.353 1.00 19.85 ? 4456 VAL A CB    1 
ATOM   22139 C  CG1   . VAL A 1 4456 ? 209.013 269.095 198.842 1.00 19.11 ? 4456 VAL A CG1   1 
ATOM   22140 C  CG2   . VAL A 1 4456 ? 210.274 269.437 200.951 1.00 12.21 ? 4456 VAL A CG2   1 
ATOM   22141 N  N     . LYS A 1 4457 ? 205.723 269.174 200.533 1.00 17.89 ? 4457 LYS A N     1 
ATOM   22142 C  CA    . LYS A 1 4457 ? 204.417 268.967 199.920 1.00 22.14 ? 4457 LYS A CA    1 
ATOM   22143 C  C     . LYS A 1 4457 ? 203.400 270.032 200.306 1.00 24.56 ? 4457 LYS A C     1 
ATOM   22144 O  O     . LYS A 1 4457 ? 202.297 270.039 199.752 1.00 27.47 ? 4457 LYS A O     1 
ATOM   22145 C  CB    . LYS A 1 4457 ? 203.868 267.586 200.287 1.00 21.95 ? 4457 LYS A CB    1 
ATOM   22146 C  CG    . LYS A 1 4457 ? 204.733 266.425 199.820 1.00 22.16 ? 4457 LYS A CG    1 
ATOM   22147 C  CD    . LYS A 1 4457 ? 204.188 265.093 200.316 1.00 22.94 ? 4457 LYS A CD    1 
ATOM   22148 C  CE    . LYS A 1 4457 ? 204.156 265.031 201.834 1.00 25.72 ? 4457 LYS A CE    1 
ATOM   22149 N  NZ    . LYS A 1 4457 ? 203.585 263.744 202.322 1.00 31.93 ? 4457 LYS A NZ    1 
ATOM   22150 N  N     . GLY A 1 4458 ? 203.735 270.922 201.240 1.00 21.26 ? 4458 GLY A N     1 
ATOM   22151 C  CA    . GLY A 1 4458 ? 202.818 271.964 201.646 1.00 19.42 ? 4458 GLY A CA    1 
ATOM   22152 C  C     . GLY A 1 4458 ? 201.726 271.528 202.594 1.00 23.15 ? 4458 GLY A C     1 
ATOM   22153 O  O     . GLY A 1 4458 ? 200.811 272.315 202.862 1.00 24.28 ? 4458 GLY A O     1 
ATOM   22154 N  N     . ILE A 1 4459 ? 201.784 270.304 203.102 1.00 21.49 ? 4459 ILE A N     1 
ATOM   22155 C  CA    . ILE A 1 4459 ? 200.791 269.820 204.052 1.00 18.74 ? 4459 ILE A CA    1 
ATOM   22156 C  C     . ILE A 1 4459 ? 201.142 270.333 205.441 1.00 25.46 ? 4459 ILE A C     1 
ATOM   22157 O  O     . ILE A 1 4459 ? 202.313 270.361 205.835 1.00 23.48 ? 4459 ILE A O     1 
ATOM   22158 C  CB    . ILE A 1 4459 ? 200.719 268.283 204.021 1.00 18.32 ? 4459 ILE A CB    1 
ATOM   22159 C  CG1   . ILE A 1 4459 ? 200.364 267.795 202.616 1.00 25.37 ? 4459 ILE A CG1   1 
ATOM   22160 C  CG2   . ILE A 1 4459 ? 199.708 267.770 205.034 1.00 20.18 ? 4459 ILE A CG2   1 
ATOM   22161 C  CD1   . ILE A 1 4459 ? 200.357 266.289 202.479 1.00 22.57 ? 4459 ILE A CD1   1 
ATOM   22162 N  N     . LEU A 1 4460 ? 200.124 270.763 206.179 1.00 24.68 ? 4460 LEU A N     1 
ATOM   22163 C  CA    . LEU A 1 4460 ? 200.330 271.210 207.546 1.00 19.54 ? 4460 LEU A CA    1 
ATOM   22164 C  C     . LEU A 1 4460 ? 200.773 270.034 208.411 1.00 22.70 ? 4460 LEU A C     1 
ATOM   22165 O  O     . LEU A 1 4460 ? 200.106 268.991 208.417 1.00 25.99 ? 4460 LEU A O     1 
ATOM   22166 C  CB    . LEU A 1 4460 ? 199.046 271.822 208.101 1.00 23.28 ? 4460 LEU A CB    1 
ATOM   22167 C  CG    . LEU A 1 4460 ? 198.983 272.088 209.605 1.00 20.96 ? 4460 LEU A CG    1 
ATOM   22168 C  CD1   . LEU A 1 4460 ? 199.985 273.155 210.004 1.00 18.27 ? 4460 LEU A CD1   1 
ATOM   22169 C  CD2   . LEU A 1 4460 ? 197.577 272.488 210.013 1.00 18.75 ? 4460 LEU A CD2   1 
ATOM   22170 N  N     . PRO A 1 4461 ? 201.890 270.147 209.132 1.00 24.44 ? 4461 PRO A N     1 
ATOM   22171 C  CA    . PRO A 1 4461 ? 202.343 269.036 209.974 1.00 17.96 ? 4461 PRO A CA    1 
ATOM   22172 C  C     . PRO A 1 4461 ? 201.313 268.684 211.037 1.00 22.54 ? 4461 PRO A C     1 
ATOM   22173 O  O     . PRO A 1 4461 ? 200.663 269.559 211.612 1.00 30.20 ? 4461 PRO A O     1 
ATOM   22174 C  CB    . PRO A 1 4461 ? 203.633 269.572 210.598 1.00 17.52 ? 4461 PRO A CB    1 
ATOM   22175 C  CG    . PRO A 1 4461 ? 204.114 270.587 209.624 1.00 17.13 ? 4461 PRO A CG    1 
ATOM   22176 C  CD    . PRO A 1 4461 ? 202.876 271.240 209.091 1.00 19.58 ? 4461 PRO A CD    1 
ATOM   22177 N  N     . ARG A 1 4462 ? 201.171 267.382 211.296 1.00 25.89 ? 4462 ARG A N     1 
ATOM   22178 C  CA    . ARG A 1 4462 ? 200.215 266.935 212.302 1.00 22.11 ? 4462 ARG A CA    1 
ATOM   22179 C  C     . ARG A 1 4462 ? 200.666 267.305 213.708 1.00 23.36 ? 4462 ARG A C     1 
ATOM   22180 O  O     . ARG A 1 4462 ? 199.827 267.477 214.600 1.00 24.87 ? 4462 ARG A O     1 
ATOM   22181 C  CB    . ARG A 1 4462 ? 199.996 265.426 212.188 1.00 19.76 ? 4462 ARG A CB    1 
ATOM   22182 C  CG    . ARG A 1 4462 ? 199.396 264.965 210.862 1.00 27.11 ? 4462 ARG A CG    1 
ATOM   22183 C  CD    . ARG A 1 4462 ? 198.026 265.585 210.590 1.00 28.89 ? 4462 ARG A CD    1 
ATOM   22184 N  NE    . ARG A 1 4462 ? 198.119 266.882 209.929 1.00 30.67 ? 4462 ARG A NE    1 
ATOM   22185 C  CZ    . ARG A 1 4462 ? 197.081 267.659 209.652 1.00 36.81 ? 4462 ARG A CZ    1 
ATOM   22186 N  NH1   . ARG A 1 4462 ? 195.846 267.304 209.966 1.00 37.98 ? 4462 ARG A NH1   1 
ATOM   22187 N  NH2   . ARG A 1 4462 ? 197.287 268.826 209.045 1.00 30.19 ? 4462 ARG A NH2   1 
ATOM   22188 N  N     . SER A 1 4463 ? 201.977 267.428 213.927 1.00 24.72 ? 4463 SER A N     1 
ATOM   22189 C  CA    . SER A 1 4463 ? 202.469 267.891 215.219 1.00 16.96 ? 4463 SER A CA    1 
ATOM   22190 C  C     . SER A 1 4463 ? 202.029 269.322 215.490 1.00 26.27 ? 4463 SER A C     1 
ATOM   22191 O  O     . SER A 1 4463 ? 201.648 269.661 216.617 1.00 24.33 ? 4463 SER A O     1 
ATOM   22192 C  CB    . SER A 1 4463 ? 203.992 267.781 215.270 1.00 20.23 ? 4463 SER A CB    1 
ATOM   22193 O  OG    . SER A 1 4463 ? 204.422 266.479 214.915 1.00 29.03 ? 4463 SER A OG    1 
ATOM   22194 N  N     . TRP A 1 4464 ? 202.075 270.176 214.463 1.00 21.98 ? 4464 TRP A N     1 
ATOM   22195 C  CA    . TRP A 1 4464 ? 201.678 271.568 214.627 1.00 17.61 ? 4464 TRP A CA    1 
ATOM   22196 C  C     . TRP A 1 4464 ? 200.183 271.703 214.887 1.00 17.43 ? 4464 TRP A C     1 
ATOM   22197 O  O     . TRP A 1 4464 ? 199.758 272.640 215.574 1.00 19.67 ? 4464 TRP A O     1 
ATOM   22198 C  CB    . TRP A 1 4464 ? 202.074 272.366 213.383 1.00 17.91 ? 4464 TRP A CB    1 
ATOM   22199 C  CG    . TRP A 1 4464 ? 203.554 272.554 213.233 1.00 20.06 ? 4464 TRP A CG    1 
ATOM   22200 C  CD1   . TRP A 1 4464 ? 204.535 271.950 213.962 1.00 19.42 ? 4464 TRP A CD1   1 
ATOM   22201 C  CD2   . TRP A 1 4464 ? 204.221 273.385 212.277 1.00 15.69 ? 4464 TRP A CD2   1 
ATOM   22202 N  NE1   . TRP A 1 4464 ? 205.769 272.363 213.529 1.00 20.47 ? 4464 TRP A NE1   1 
ATOM   22203 C  CE2   . TRP A 1 4464 ? 205.604 273.243 212.495 1.00 16.55 ? 4464 TRP A CE2   1 
ATOM   22204 C  CE3   . TRP A 1 4464 ? 203.782 274.241 211.262 1.00 16.14 ? 4464 TRP A CE3   1 
ATOM   22205 C  CZ2   . TRP A 1 4464 ? 206.553 273.922 211.734 1.00 20.37 ? 4464 TRP A CZ2   1 
ATOM   22206 C  CZ3   . TRP A 1 4464 ? 204.725 274.915 210.510 1.00 14.09 ? 4464 TRP A CZ3   1 
ATOM   22207 C  CH2   . TRP A 1 4464 ? 206.093 274.753 210.751 1.00 17.64 ? 4464 TRP A CH2   1 
ATOM   22208 N  N     . SER A 1 4465 ? 199.378 270.784 214.359 1.00 18.52 ? 4465 SER A N     1 
ATOM   22209 C  CA    . SER A 1 4465 ? 197.927 270.866 214.494 1.00 20.28 ? 4465 SER A CA    1 
ATOM   22210 C  C     . SER A 1 4465 ? 197.532 270.606 215.942 1.00 18.23 ? 4465 SER A C     1 
ATOM   22211 O  O     . SER A 1 4465 ? 197.505 269.457 216.392 1.00 28.53 ? 4465 SER A O     1 
ATOM   22212 C  CB    . SER A 1 4465 ? 197.254 269.869 213.557 1.00 21.60 ? 4465 SER A CB    1 
ATOM   22213 O  OG    . SER A 1 4465 ? 197.690 268.548 213.821 1.00 30.13 ? 4465 SER A OG    1 
ATOM   22214 N  N     . HIS A 1 4466 ? 197.221 271.675 216.671 1.00 19.65 ? 4466 HIS A N     1 
ATOM   22215 C  CA    . HIS A 1 4466 ? 196.802 271.578 218.062 1.00 23.47 ? 4466 HIS A CA    1 
ATOM   22216 C  C     . HIS A 1 4466 ? 195.495 272.291 218.359 1.00 22.35 ? 4466 HIS A C     1 
ATOM   22217 O  O     . HIS A 1 4466 ? 194.860 271.971 219.372 1.00 30.39 ? 4466 HIS A O     1 
ATOM   22218 C  CB    . HIS A 1 4466 ? 197.892 272.132 218.992 1.00 22.40 ? 4466 HIS A CB    1 
ATOM   22219 C  CG    . HIS A 1 4466 ? 199.070 271.222 219.146 1.00 25.26 ? 4466 HIS A CG    1 
ATOM   22220 N  ND1   . HIS A 1 4466 ? 200.310 271.670 219.547 1.00 28.78 ? 4466 HIS A ND1   1 
ATOM   22221 C  CD2   . HIS A 1 4466 ? 199.198 269.888 218.949 1.00 21.74 ? 4466 HIS A CD2   1 
ATOM   22222 C  CE1   . HIS A 1 4466 ? 201.150 270.652 219.591 1.00 29.84 ? 4466 HIS A CE1   1 
ATOM   22223 N  NE2   . HIS A 1 4466 ? 200.501 269.559 219.233 1.00 26.92 ? 4466 HIS A NE2   1 
ATOM   22224 N  N     . TYR A 1 4467 ? 195.074 273.239 217.529 1.00 18.59 ? 4467 TYR A N     1 
ATOM   22225 C  CA    . TYR A 1 4467 ? 193.769 273.869 217.638 1.00 19.64 ? 4467 TYR A CA    1 
ATOM   22226 C  C     . TYR A 1 4467 ? 192.962 273.568 216.384 1.00 21.05 ? 4467 TYR A C     1 
ATOM   22227 O  O     . TYR A 1 4467 ? 193.514 273.440 215.287 1.00 19.86 ? 4467 TYR A O     1 
ATOM   22228 C  CB    . TYR A 1 4467 ? 193.891 275.386 217.847 1.00 17.15 ? 4467 TYR A CB    1 
ATOM   22229 C  CG    . TYR A 1 4467 ? 194.743 276.096 216.819 1.00 14.10 ? 4467 TYR A CG    1 
ATOM   22230 C  CD1   . TYR A 1 4467 ? 194.194 276.569 215.637 1.00 18.05 ? 4467 TYR A CD1   1 
ATOM   22231 C  CD2   . TYR A 1 4467 ? 196.099 276.296 217.036 1.00 15.56 ? 4467 TYR A CD2   1 
ATOM   22232 C  CE1   . TYR A 1 4467 ? 194.972 277.223 214.702 1.00 15.86 ? 4467 TYR A CE1   1 
ATOM   22233 C  CE2   . TYR A 1 4467 ? 196.884 276.950 216.108 1.00 13.40 ? 4467 TYR A CE2   1 
ATOM   22234 C  CZ    . TYR A 1 4467 ? 196.315 277.408 214.941 1.00 15.32 ? 4467 TYR A CZ    1 
ATOM   22235 O  OH    . TYR A 1 4467 ? 197.093 278.057 214.011 1.00 17.35 ? 4467 TYR A OH    1 
ATOM   22236 N  N     . THR A 1 4468 ? 191.649 273.447 216.561 1.00 19.15 ? 4468 THR A N     1 
ATOM   22237 C  CA    . THR A 1 4468 ? 190.773 273.056 215.464 1.00 17.01 ? 4468 THR A CA    1 
ATOM   22238 C  C     . THR A 1 4468 ? 190.824 274.067 214.322 1.00 20.10 ? 4468 THR A C     1 
ATOM   22239 O  O     . THR A 1 4468 ? 190.811 275.283 214.539 1.00 21.61 ? 4468 THR A O     1 
ATOM   22240 C  CB    . THR A 1 4468 ? 189.343 272.873 215.983 1.00 18.64 ? 4468 THR A CB    1 
ATOM   22241 O  OG1   . THR A 1 4468 ? 188.509 272.337 214.946 1.00 33.53 ? 4468 THR A OG1   1 
ATOM   22242 C  CG2   . THR A 1 4468 ? 188.769 274.171 216.514 1.00 15.53 ? 4468 THR A CG2   1 
ATOM   22243 N  N     . VAL A 1 4469 ? 190.915 273.551 213.101 1.00 20.58 ? 4469 VAL A N     1 
ATOM   22244 C  CA    . VAL A 1 4469 ? 191.050 274.370 211.900 1.00 18.49 ? 4469 VAL A CA    1 
ATOM   22245 C  C     . VAL A 1 4469 ? 190.103 273.825 210.842 1.00 23.12 ? 4469 VAL A C     1 
ATOM   22246 O  O     . VAL A 1 4469 ? 189.715 272.646 210.887 1.00 24.71 ? 4469 VAL A O     1 
ATOM   22247 C  CB    . VAL A 1 4469 ? 192.509 274.387 211.381 1.00 16.32 ? 4469 VAL A CB    1 
ATOM   22248 C  CG1   . VAL A 1 4469 ? 193.410 275.127 212.345 1.00 21.34 ? 4469 VAL A CG1   1 
ATOM   22249 C  CG2   . VAL A 1 4469 ? 193.007 272.969 211.155 1.00 26.34 ? 4469 VAL A CG2   1 
ATOM   22250 N  N     . PRO A 1 4470 ? 189.698 274.656 209.880 1.00 23.62 ? 4470 PRO A N     1 
ATOM   22251 C  CA    . PRO A 1 4470 ? 188.862 274.147 208.790 1.00 18.08 ? 4470 PRO A CA    1 
ATOM   22252 C  C     . PRO A 1 4470 ? 189.601 273.091 207.983 1.00 22.77 ? 4470 PRO A C     1 
ATOM   22253 O  O     . PRO A 1 4470 ? 190.812 273.182 207.768 1.00 23.70 ? 4470 PRO A O     1 
ATOM   22254 C  CB    . PRO A 1 4470 ? 188.564 275.395 207.956 1.00 14.78 ? 4470 PRO A CB    1 
ATOM   22255 C  CG    . PRO A 1 4470 ? 189.700 276.304 208.230 1.00 12.74 ? 4470 PRO A CG    1 
ATOM   22256 C  CD    . PRO A 1 4470 ? 190.078 276.064 209.663 1.00 15.66 ? 4470 PRO A CD    1 
ATOM   22257 N  N     . ALA A 1 4471 ? 188.857 272.080 207.542 1.00 29.20 ? 4471 ALA A N     1 
ATOM   22258 C  CA    . ALA A 1 4471 ? 189.454 270.992 206.780 1.00 25.34 ? 4471 ALA A CA    1 
ATOM   22259 C  C     . ALA A 1 4471 ? 190.008 271.506 205.458 1.00 27.04 ? 4471 ALA A C     1 
ATOM   22260 O  O     . ALA A 1 4471 ? 189.409 272.361 204.804 1.00 26.99 ? 4471 ALA A O     1 
ATOM   22261 C  CB    . ALA A 1 4471 ? 188.420 269.894 206.532 1.00 23.16 ? 4471 ALA A CB    1 
ATOM   22262 N  N     . GLY A 1 4472 ? 191.165 270.977 205.069 1.00 23.71 ? 4472 GLY A N     1 
ATOM   22263 C  CA    . GLY A 1 4472 ? 191.807 271.384 203.837 1.00 22.98 ? 4472 GLY A CA    1 
ATOM   22264 C  C     . GLY A 1 4472 ? 192.653 272.634 203.924 1.00 28.43 ? 4472 GLY A C     1 
ATOM   22265 O  O     . GLY A 1 4472 ? 192.875 273.283 202.896 1.00 25.59 ? 4472 GLY A O     1 
ATOM   22266 N  N     . MET A 1 4473 ? 193.125 272.996 205.113 1.00 28.58 ? 4473 MET A N     1 
ATOM   22267 C  CA    . MET A 1 4473 ? 193.941 274.191 205.278 1.00 24.36 ? 4473 MET A CA    1 
ATOM   22268 C  C     . MET A 1 4473 ? 195.413 273.837 205.104 1.00 24.15 ? 4473 MET A C     1 
ATOM   22269 O  O     . MET A 1 4473 ? 195.915 272.907 205.741 1.00 28.03 ? 4473 MET A O     1 
ATOM   22270 C  CB    . MET A 1 4473 ? 193.690 274.807 206.654 1.00 20.30 ? 4473 MET A CB    1 
ATOM   22271 C  CG    . MET A 1 4473 ? 194.716 275.826 207.102 1.00 21.32 ? 4473 MET A CG    1 
ATOM   22272 S  SD    . MET A 1 4473 ? 194.266 276.533 208.697 1.00 38.00 ? 4473 MET A SD    1 
ATOM   22273 C  CE    . MET A 1 4473 ? 194.842 278.214 208.506 1.00 16.76 ? 4473 MET A CE    1 
ATOM   22274 N  N     . THR A 1 4474 ? 196.105 274.577 204.239 1.00 18.21 ? 4474 THR A N     1 
ATOM   22275 C  CA    . THR A 1 4474 ? 197.489 274.266 203.917 1.00 18.63 ? 4474 THR A CA    1 
ATOM   22276 C  C     . THR A 1 4474 ? 198.438 274.961 204.891 1.00 21.97 ? 4474 THR A C     1 
ATOM   22277 O  O     . THR A 1 4474 ? 198.039 275.789 205.712 1.00 27.81 ? 4474 THR A O     1 
ATOM   22278 C  CB    . THR A 1 4474 ? 197.806 274.647 202.470 1.00 24.79 ? 4474 THR A CB    1 
ATOM   22279 O  OG1   . THR A 1 4474 ? 199.114 274.173 202.127 1.00 35.34 ? 4474 THR A OG1   1 
ATOM   22280 C  CG2   . THR A 1 4474 ? 197.763 276.147 202.290 1.00 18.22 ? 4474 THR A CG2   1 
ATOM   22281 N  N     . VAL A 1 4475 ? 199.723 274.615 204.795 1.00 23.84 ? 4475 VAL A N     1 
ATOM   22282 C  CA    . VAL A 1 4475 ? 200.699 275.069 205.781 1.00 18.60 ? 4475 VAL A CA    1 
ATOM   22283 C  C     . VAL A 1 4475 ? 200.983 276.564 205.654 1.00 16.93 ? 4475 VAL A C     1 
ATOM   22284 O  O     . VAL A 1 4475 ? 201.280 277.225 206.657 1.00 17.34 ? 4475 VAL A O     1 
ATOM   22285 C  CB    . VAL A 1 4475 ? 201.990 274.232 205.677 1.00 20.36 ? 4475 VAL A CB    1 
ATOM   22286 C  CG1   . VAL A 1 4475 ? 202.744 274.538 204.393 1.00 18.97 ? 4475 VAL A CG1   1 
ATOM   22287 C  CG2   . VAL A 1 4475 ? 202.877 274.461 206.897 1.00 15.55 ? 4475 VAL A CG2   1 
ATOM   22288 N  N     . ILE A 1 4476 ? 200.906 277.125 204.445 1.00 19.13 ? 4476 ILE A N     1 
ATOM   22289 C  CA    . ILE A 1 4476 ? 201.204 278.547 204.286 1.00 15.96 ? 4476 ILE A CA    1 
ATOM   22290 C  C     . ILE A 1 4476 ? 200.135 279.406 204.954 1.00 22.47 ? 4476 ILE A C     1 
ATOM   22291 O  O     . ILE A 1 4476 ? 200.442 280.475 205.497 1.00 24.40 ? 4476 ILE A O     1 
ATOM   22292 C  CB    . ILE A 1 4476 ? 201.389 278.897 202.795 1.00 19.30 ? 4476 ILE A CB    1 
ATOM   22293 C  CG1   . ILE A 1 4476 ? 202.233 280.163 202.647 1.00 19.17 ? 4476 ILE A CG1   1 
ATOM   22294 C  CG2   . ILE A 1 4476 ? 200.053 279.060 202.084 1.00 21.25 ? 4476 ILE A CG2   1 
ATOM   22295 C  CD1   . ILE A 1 4476 ? 202.580 280.498 201.214 1.00 22.00 ? 4476 ILE A CD1   1 
ATOM   22296 N  N     . GLN A 1 4477 ? 198.875 278.962 204.940 1.00 15.63 ? 4477 GLN A N     1 
ATOM   22297 C  CA    . GLN A 1 4477 ? 197.823 279.712 205.618 1.00 18.35 ? 4477 GLN A CA    1 
ATOM   22298 C  C     . GLN A 1 4477 ? 197.902 279.530 207.126 1.00 19.81 ? 4477 GLN A C     1 
ATOM   22299 O  O     . GLN A 1 4477 ? 197.601 280.456 207.885 1.00 20.54 ? 4477 GLN A O     1 
ATOM   22300 C  CB    . GLN A 1 4477 ? 196.448 279.280 205.104 1.00 23.61 ? 4477 GLN A CB    1 
ATOM   22301 C  CG    . GLN A 1 4477 ? 196.375 279.086 203.603 1.00 16.86 ? 4477 GLN A CG    1 
ATOM   22302 C  CD    . GLN A 1 4477 ? 194.991 278.684 203.138 1.00 21.92 ? 4477 GLN A CD    1 
ATOM   22303 O  OE1   . GLN A 1 4477 ? 194.691 277.497 203.005 1.00 21.47 ? 4477 GLN A OE1   1 
ATOM   22304 N  NE2   . GLN A 1 4477 ? 194.140 279.670 202.887 1.00 25.41 ? 4477 GLN A NE2   1 
ATOM   22305 N  N     . TRP A 1 4478 ? 198.300 278.338 207.576 1.00 22.88 ? 4478 TRP A N     1 
ATOM   22306 C  CA    . TRP A 1 4478 ? 198.393 278.077 209.008 1.00 14.94 ? 4478 TRP A CA    1 
ATOM   22307 C  C     . TRP A 1 4478 ? 199.446 278.956 209.669 1.00 15.32 ? 4478 TRP A C     1 
ATOM   22308 O  O     . TRP A 1 4478 ? 199.234 279.458 210.779 1.00 15.79 ? 4478 TRP A O     1 
ATOM   22309 C  CB    . TRP A 1 4478 ? 198.697 276.600 209.251 1.00 11.41 ? 4478 TRP A CB    1 
ATOM   22310 C  CG    . TRP A 1 4478 ? 198.469 276.172 210.663 1.00 13.99 ? 4478 TRP A CG    1 
ATOM   22311 C  CD1   . TRP A 1 4478 ? 197.318 275.670 211.193 1.00 15.18 ? 4478 TRP A CD1   1 
ATOM   22312 C  CD2   . TRP A 1 4478 ? 199.423 276.204 211.729 1.00 12.92 ? 4478 TRP A CD2   1 
ATOM   22313 N  NE1   . TRP A 1 4478 ? 197.497 275.386 212.524 1.00 17.63 ? 4478 TRP A NE1   1 
ATOM   22314 C  CE2   . TRP A 1 4478 ? 198.781 275.706 212.878 1.00 15.12 ? 4478 TRP A CE2   1 
ATOM   22315 C  CE3   . TRP A 1 4478 ? 200.758 276.605 211.825 1.00 14.13 ? 4478 TRP A CE3   1 
ATOM   22316 C  CZ2   . TRP A 1 4478 ? 199.425 275.601 214.105 1.00 17.14 ? 4478 TRP A CZ2   1 
ATOM   22317 C  CZ3   . TRP A 1 4478 ? 201.396 276.499 213.043 1.00 18.49 ? 4478 TRP A CZ3   1 
ATOM   22318 C  CH2   . TRP A 1 4478 ? 200.731 276.001 214.168 1.00 17.44 ? 4478 TRP A CH2   1 
ATOM   22319 N  N     . VAL A 1 4479 ? 200.589 279.152 209.009 1.00 14.15 ? 4479 VAL A N     1 
ATOM   22320 C  CA    . VAL A 1 4479 ? 201.650 279.969 209.593 1.00 15.97 ? 4479 VAL A CA    1 
ATOM   22321 C  C     . VAL A 1 4479 ? 201.172 281.405 209.776 1.00 14.64 ? 4479 VAL A C     1 
ATOM   22322 O  O     . VAL A 1 4479 ? 201.393 282.025 210.822 1.00 22.32 ? 4479 VAL A O     1 
ATOM   22323 C  CB    . VAL A 1 4479 ? 202.923 279.901 208.728 1.00 18.36 ? 4479 VAL A CB    1 
ATOM   22324 C  CG1   . VAL A 1 4479 ? 203.919 280.958 209.168 1.00 18.05 ? 4479 VAL A CG1   1 
ATOM   22325 C  CG2   . VAL A 1 4479 ? 203.543 278.518 208.811 1.00 15.43 ? 4479 VAL A CG2   1 
ATOM   22326 N  N     . SER A 1 4480 ? 200.504 281.954 208.757 1.00 17.48 ? 4480 SER A N     1 
ATOM   22327 C  CA    . SER A 1 4480 ? 199.938 283.293 208.882 1.00 14.20 ? 4480 SER A CA    1 
ATOM   22328 C  C     . SER A 1 4480 ? 198.850 283.335 209.946 1.00 16.54 ? 4480 SER A C     1 
ATOM   22329 O  O     . SER A 1 4480 ? 198.784 284.279 210.741 1.00 23.34 ? 4480 SER A O     1 
ATOM   22330 C  CB    . SER A 1 4480 ? 199.389 283.755 207.533 1.00 17.40 ? 4480 SER A CB    1 
ATOM   22331 O  OG    . SER A 1 4480 ? 198.605 282.742 206.933 1.00 23.78 ? 4480 SER A OG    1 
ATOM   22332 N  N     . ASP A 1 4481 ? 197.983 282.321 209.974 1.00 15.28 ? 4481 ASP A N     1 
ATOM   22333 C  CA    . ASP A 1 4481 ? 196.951 282.259 211.002 1.00 16.12 ? 4481 ASP A CA    1 
ATOM   22334 C  C     . ASP A 1 4481 ? 197.561 282.097 212.390 1.00 18.51 ? 4481 ASP A C     1 
ATOM   22335 O  O     . ASP A 1 4481 ? 197.141 282.767 213.341 1.00 16.67 ? 4481 ASP A O     1 
ATOM   22336 C  CB    . ASP A 1 4481 ? 195.987 281.111 210.703 1.00 12.67 ? 4481 ASP A CB    1 
ATOM   22337 C  CG    . ASP A 1 4481 ? 194.651 281.269 211.404 1.00 20.37 ? 4481 ASP A CG    1 
ATOM   22338 O  OD1   . ASP A 1 4481 ? 194.579 282.012 212.405 1.00 25.80 ? 4481 ASP A OD1   1 
ATOM   22339 O  OD2   . ASP A 1 4481 ? 193.668 280.649 210.950 1.00 28.85 ? 4481 ASP A OD2   1 
ATOM   22340 N  N     . PHE A 1 4482 ? 198.559 281.220 212.522 1.00 17.10 ? 4482 PHE A N     1 
ATOM   22341 C  CA    . PHE A 1 4482 ? 199.184 280.999 213.821 1.00 14.74 ? 4482 PHE A CA    1 
ATOM   22342 C  C     . PHE A 1 4482 ? 199.889 282.251 214.321 1.00 17.67 ? 4482 PHE A C     1 
ATOM   22343 O  O     . PHE A 1 4482 ? 199.913 282.507 215.531 1.00 22.37 ? 4482 PHE A O     1 
ATOM   22344 C  CB    . PHE A 1 4482 ? 200.162 279.827 213.739 1.00 16.38 ? 4482 PHE A CB    1 
ATOM   22345 C  CG    . PHE A 1 4482 ? 200.920 279.579 215.007 1.00 14.82 ? 4482 PHE A CG    1 
ATOM   22346 C  CD1   . PHE A 1 4482 ? 200.281 279.065 216.121 1.00 14.99 ? 4482 PHE A CD1   1 
ATOM   22347 C  CD2   . PHE A 1 4482 ? 202.274 279.855 215.085 1.00 17.62 ? 4482 PHE A CD2   1 
ATOM   22348 C  CE1   . PHE A 1 4482 ? 200.974 278.835 217.290 1.00 17.09 ? 4482 PHE A CE1   1 
ATOM   22349 C  CE2   . PHE A 1 4482 ? 202.974 279.625 216.251 1.00 16.59 ? 4482 PHE A CE2   1 
ATOM   22350 C  CZ    . PHE A 1 4482 ? 202.324 279.115 217.354 1.00 17.90 ? 4482 PHE A CZ    1 
ATOM   22351 N  N     . SER A 1 4483 ? 200.469 283.037 213.414 1.00 16.81 ? 4483 SER A N     1 
ATOM   22352 C  CA    . SER A 1 4483 ? 201.148 284.260 213.826 1.00 18.64 ? 4483 SER A CA    1 
ATOM   22353 C  C     . SER A 1 4483 ? 200.168 285.268 214.418 1.00 19.56 ? 4483 SER A C     1 
ATOM   22354 O  O     . SER A 1 4483 ? 200.477 285.927 215.418 1.00 22.30 ? 4483 SER A O     1 
ATOM   22355 C  CB    . SER A 1 4483 ? 201.896 284.866 212.640 1.00 18.63 ? 4483 SER A CB    1 
ATOM   22356 O  OG    . SER A 1 4483 ? 202.540 286.073 213.007 1.00 32.12 ? 4483 SER A OG    1 
ATOM   22357 N  N     . GLU A 1 4484 ? 198.983 285.402 213.817 1.00 14.53 ? 4484 GLU A N     1 
ATOM   22358 C  CA    . GLU A 1 4484 ? 197.989 286.335 214.341 1.00 15.63 ? 4484 GLU A CA    1 
ATOM   22359 C  C     . GLU A 1 4484 ? 197.500 285.910 215.721 1.00 18.79 ? 4484 GLU A C     1 
ATOM   22360 O  O     . GLU A 1 4484 ? 197.301 286.755 216.601 1.00 17.93 ? 4484 GLU A O     1 
ATOM   22361 C  CB    . GLU A 1 4484 ? 196.811 286.451 213.371 1.00 17.46 ? 4484 GLU A CB    1 
ATOM   22362 C  CG    . GLU A 1 4484 ? 197.144 286.924 211.949 1.00 20.75 ? 4484 GLU A CG    1 
ATOM   22363 C  CD    . GLU A 1 4484 ? 198.271 287.949 211.853 1.00 27.22 ? 4484 GLU A CD    1 
ATOM   22364 O  OE1   . GLU A 1 4484 ? 198.421 288.804 212.753 1.00 26.67 ? 4484 GLU A OE1   1 
ATOM   22365 O  OE2   . GLU A 1 4484 ? 199.019 287.895 210.853 1.00 31.05 ? 4484 GLU A OE2   1 
ATOM   22366 N  N     . ARG A 1 4485 ? 197.291 284.607 215.924 1.00 20.08 ? 4485 ARG A N     1 
ATOM   22367 C  CA    . ARG A 1 4485 ? 196.808 284.126 217.213 1.00 16.59 ? 4485 ARG A CA    1 
ATOM   22368 C  C     . ARG A 1 4485 ? 197.812 284.411 218.323 1.00 19.26 ? 4485 ARG A C     1 
ATOM   22369 O  O     . ARG A 1 4485 ? 197.427 284.751 219.448 1.00 24.02 ? 4485 ARG A O     1 
ATOM   22370 C  CB    . ARG A 1 4485 ? 196.503 282.632 217.135 1.00 15.48 ? 4485 ARG A CB    1 
ATOM   22371 C  CG    . ARG A 1 4485 ? 195.453 282.268 216.100 1.00 13.39 ? 4485 ARG A CG    1 
ATOM   22372 C  CD    . ARG A 1 4485 ? 195.185 280.774 216.079 1.00 16.30 ? 4485 ARG A CD    1 
ATOM   22373 N  NE    . ARG A 1 4485 ? 194.119 280.432 215.146 1.00 16.38 ? 4485 ARG A NE    1 
ATOM   22374 C  CZ    . ARG A 1 4485 ? 192.981 279.844 215.488 1.00 15.93 ? 4485 ARG A CZ    1 
ATOM   22375 N  NH1   . ARG A 1 4485 ? 192.730 279.502 216.740 1.00 14.82 ? 4485 ARG A NH1   1 
ATOM   22376 N  NH2   . ARG A 1 4485 ? 192.075 279.592 214.549 1.00 22.55 ? 4485 ARG A NH2   1 
ATOM   22377 N  N     . ILE A 1 4486 ? 199.106 284.270 218.030 1.00 18.01 ? 4486 ILE A N     1 
ATOM   22378 C  CA    . ILE A 1 4486 ? 200.125 284.508 219.047 1.00 20.14 ? 4486 ILE A CA    1 
ATOM   22379 C  C     . ILE A 1 4486 ? 200.170 285.982 219.430 1.00 21.52 ? 4486 ILE A C     1 
ATOM   22380 O  O     . ILE A 1 4486 ? 200.361 286.323 220.604 1.00 25.75 ? 4486 ILE A O     1 
ATOM   22381 C  CB    . ILE A 1 4486 ? 201.497 284.000 218.563 1.00 19.31 ? 4486 ILE A CB    1 
ATOM   22382 C  CG1   . ILE A 1 4486 ? 201.453 282.487 218.328 1.00 17.51 ? 4486 ILE A CG1   1 
ATOM   22383 C  CG2   . ILE A 1 4486 ? 202.578 284.324 219.574 1.00 20.25 ? 4486 ILE A CG2   1 
ATOM   22384 C  CD1   . ILE A 1 4486 ? 200.987 281.695 219.521 1.00 13.03 ? 4486 ILE A CD1   1 
ATOM   22385 N  N     . LYS A 1 4487 ? 199.991 286.880 218.456 1.00 18.78 ? 4487 LYS A N     1 
ATOM   22386 C  CA    . LYS A 1 4487 ? 199.987 288.310 218.761 1.00 18.59 ? 4487 LYS A CA    1 
ATOM   22387 C  C     . LYS A 1 4487 ? 198.877 288.657 219.746 1.00 21.96 ? 4487 LYS A C     1 
ATOM   22388 O  O     . LYS A 1 4487 ? 199.097 289.392 220.714 1.00 23.93 ? 4487 LYS A O     1 
ATOM   22389 C  CB    . LYS A 1 4487 ? 199.836 289.132 217.480 1.00 18.27 ? 4487 LYS A CB    1 
ATOM   22390 C  CG    . LYS A 1 4487 ? 200.969 288.975 216.480 1.00 22.74 ? 4487 LYS A CG    1 
ATOM   22391 C  CD    . LYS A 1 4487 ? 200.582 289.566 215.135 1.00 20.30 ? 4487 LYS A CD    1 
ATOM   22392 C  CE    . LYS A 1 4487 ? 201.617 289.256 214.065 1.00 26.80 ? 4487 LYS A CE    1 
ATOM   22393 N  NZ    . LYS A 1 4487 ? 202.945 289.848 214.385 1.00 29.76 ? 4487 LYS A NZ    1 
ATOM   22394 N  N     . GLN A 1 4488 ? 197.673 288.128 219.515 1.00 19.81 ? 4488 GLN A N     1 
ATOM   22395 C  CA    . GLN A 1 4488 ? 196.584 288.339 220.461 1.00 17.14 ? 4488 GLN A CA    1 
ATOM   22396 C  C     . GLN A 1 4488 ? 196.909 287.731 221.818 1.00 21.34 ? 4488 GLN A C     1 
ATOM   22397 O  O     . GLN A 1 4488 ? 196.601 288.322 222.860 1.00 20.67 ? 4488 GLN A O     1 
ATOM   22398 C  CB    . GLN A 1 4488 ? 195.286 287.749 219.913 1.00 17.58 ? 4488 GLN A CB    1 
ATOM   22399 C  CG    . GLN A 1 4488 ? 194.147 287.801 220.914 1.00 19.14 ? 4488 GLN A CG    1 
ATOM   22400 C  CD    . GLN A 1 4488 ? 192.792 287.642 220.277 1.00 15.75 ? 4488 GLN A CD    1 
ATOM   22401 O  OE1   . GLN A 1 4488 ? 191.851 288.370 220.589 1.00 22.26 ? 4488 GLN A OE1   1 
ATOM   22402 N  NE2   . GLN A 1 4488 ? 192.686 286.690 219.365 1.00 14.10 ? 4488 GLN A NE2   1 
ATOM   22403 N  N     . LEU A 1 4489 ? 197.530 286.552 221.823 1.00 23.47 ? 4489 LEU A N     1 
ATOM   22404 C  CA    . LEU A 1 4489 ? 197.921 285.927 223.081 1.00 16.33 ? 4489 LEU A CA    1 
ATOM   22405 C  C     . LEU A 1 4489 ? 198.926 286.791 223.830 1.00 24.10 ? 4489 LEU A C     1 
ATOM   22406 O  O     . LEU A 1 4489 ? 198.874 286.892 225.062 1.00 28.31 ? 4489 LEU A O     1 
ATOM   22407 C  CB    . LEU A 1 4489 ? 198.493 284.536 222.813 1.00 16.34 ? 4489 LEU A CB    1 
ATOM   22408 C  CG    . LEU A 1 4489 ? 197.472 283.447 222.486 1.00 17.95 ? 4489 LEU A CG    1 
ATOM   22409 C  CD1   . LEU A 1 4489 ? 198.145 282.273 221.793 1.00 17.82 ? 4489 LEU A CD1   1 
ATOM   22410 C  CD2   . LEU A 1 4489 ? 196.744 282.987 223.739 1.00 17.65 ? 4489 LEU A CD2   1 
ATOM   22411 N  N     . GLN A 1 4490 ? 199.854 287.420 223.104 1.00 19.85 ? 4490 GLN A N     1 
ATOM   22412 C  CA    . GLN A 1 4490 ? 200.818 288.312 223.742 1.00 22.86 ? 4490 GLN A CA    1 
ATOM   22413 C  C     . GLN A 1 4490 ? 200.129 289.509 224.382 1.00 24.08 ? 4490 GLN A C     1 
ATOM   22414 O  O     . GLN A 1 4490 ? 200.461 289.897 225.507 1.00 25.45 ? 4490 GLN A O     1 
ATOM   22415 C  CB    . GLN A 1 4490 ? 201.854 288.783 222.723 1.00 24.69 ? 4490 GLN A CB    1 
ATOM   22416 C  CG    . GLN A 1 4490 ? 202.890 287.746 222.359 1.00 22.44 ? 4490 GLN A CG    1 
ATOM   22417 C  CD    . GLN A 1 4490 ? 203.793 288.212 221.241 1.00 27.24 ? 4490 GLN A CD    1 
ATOM   22418 O  OE1   . GLN A 1 4490 ? 203.564 289.259 220.639 1.00 25.67 ? 4490 GLN A OE1   1 
ATOM   22419 N  NE2   . GLN A 1 4490 ? 204.838 287.442 220.967 1.00 32.38 ? 4490 GLN A NE2   1 
ATOM   22420 N  N     . ASN A 1 4491 ? 199.167 290.111 223.677 1.00 20.90 ? 4491 ASN A N     1 
ATOM   22421 C  CA    . ASN A 1 4491 ? 198.485 291.285 224.213 1.00 20.71 ? 4491 ASN A CA    1 
ATOM   22422 C  C     . ASN A 1 4491 ? 197.692 290.939 225.465 1.00 18.92 ? 4491 ASN A C     1 
ATOM   22423 O  O     . ASN A 1 4491 ? 197.656 291.723 226.421 1.00 21.82 ? 4491 ASN A O     1 
ATOM   22424 C  CB    . ASN A 1 4491 ? 197.575 291.895 223.149 1.00 17.89 ? 4491 ASN A CB    1 
ATOM   22425 C  CG    . ASN A 1 4491 ? 198.307 292.193 221.857 1.00 21.50 ? 4491 ASN A CG    1 
ATOM   22426 O  OD1   . ASN A 1 4491 ? 199.520 292.009 221.760 1.00 21.49 ? 4491 ASN A OD1   1 
ATOM   22427 N  ND2   . ASN A 1 4491 ? 197.573 292.651 220.852 1.00 25.61 ? 4491 ASN A ND2   1 
ATOM   22428 N  N     . ILE A 1 4492 ? 197.049 289.770 225.475 1.00 23.97 ? 4492 ILE A N     1 
ATOM   22429 C  CA    . ILE A 1 4492 ? 196.286 289.343 226.645 1.00 19.27 ? 4492 ILE A CA    1 
ATOM   22430 C  C     . ILE A 1 4492 ? 197.206 289.176 227.847 1.00 24.09 ? 4492 ILE A C     1 
ATOM   22431 O  O     . ILE A 1 4492 ? 196.888 289.619 228.958 1.00 26.62 ? 4492 ILE A O     1 
ATOM   22432 C  CB    . ILE A 1 4492 ? 195.519 288.047 226.327 1.00 19.87 ? 4492 ILE A CB    1 
ATOM   22433 C  CG1   . ILE A 1 4492 ? 194.457 288.309 225.257 1.00 18.69 ? 4492 ILE A CG1   1 
ATOM   22434 C  CG2   . ILE A 1 4492 ? 194.874 287.486 227.579 1.00 19.08 ? 4492 ILE A CG2   1 
ATOM   22435 C  CD1   . ILE A 1 4492 ? 193.817 287.053 224.716 1.00 17.61 ? 4492 ILE A CD1   1 
ATOM   22436 N  N     . SER A 1 4493 ? 198.361 288.538 227.646 1.00 26.95 ? 4493 SER A N     1 
ATOM   22437 C  CA    . SER A 1 4493 ? 199.307 288.356 228.742 1.00 22.98 ? 4493 SER A CA    1 
ATOM   22438 C  C     . SER A 1 4493 ? 199.936 289.680 229.159 1.00 27.04 ? 4493 SER A C     1 
ATOM   22439 O  O     . SER A 1 4493 ? 200.233 289.887 230.341 1.00 29.96 ? 4493 SER A O     1 
ATOM   22440 C  CB    . SER A 1 4493 ? 200.385 287.349 228.344 1.00 26.29 ? 4493 SER A CB    1 
ATOM   22441 O  OG    . SER A 1 4493 ? 201.315 287.157 229.396 1.00 30.58 ? 4493 SER A OG    1 
ATOM   22442 N  N     . LEU A 1 4494 ? 200.159 290.583 228.201 1.00 25.87 ? 4494 LEU A N     1 
ATOM   22443 C  CA    . LEU A 1 4494 ? 200.719 291.891 228.533 1.00 23.39 ? 4494 LEU A CA    1 
ATOM   22444 C  C     . LEU A 1 4494 ? 199.777 292.679 229.436 1.00 29.62 ? 4494 LEU A C     1 
ATOM   22445 O  O     . LEU A 1 4494 ? 200.219 293.328 230.392 1.00 32.37 ? 4494 LEU A O     1 
ATOM   22446 C  CB    . LEU A 1 4494 ? 201.021 292.672 227.255 1.00 26.40 ? 4494 LEU A CB    1 
ATOM   22447 C  CG    . LEU A 1 4494 ? 201.531 294.105 227.416 1.00 24.92 ? 4494 LEU A CG    1 
ATOM   22448 C  CD1   . LEU A 1 4494 ? 202.734 294.151 228.351 1.00 28.38 ? 4494 LEU A CD1   1 
ATOM   22449 C  CD2   . LEU A 1 4494 ? 201.880 294.702 226.064 1.00 17.84 ? 4494 LEU A CD2   1 
ATOM   22450 N  N     . ALA A 1 4495 ? 198.476 292.641 229.143 1.00 26.59 ? 4495 ALA A N     1 
ATOM   22451 C  CA    . ALA A 1 4495 ? 197.508 293.313 230.000 1.00 25.76 ? 4495 ALA A CA    1 
ATOM   22452 C  C     . ALA A 1 4495 ? 197.488 292.705 231.396 1.00 28.11 ? 4495 ALA A C     1 
ATOM   22453 O  O     . ALA A 1 4495 ? 197.453 293.428 232.398 1.00 33.36 ? 4495 ALA A O     1 
ATOM   22454 C  CB    . ALA A 1 4495 ? 196.117 293.254 229.368 1.00 24.79 ? 4495 ALA A CB    1 
ATOM   22455 N  N     . ALA A 1 4496 ? 197.512 291.372 231.482 1.00 29.32 ? 4496 ALA A N     1 
ATOM   22456 C  CA    . ALA A 1 4496 ? 197.530 290.715 232.785 1.00 26.09 ? 4496 ALA A CA    1 
ATOM   22457 C  C     . ALA A 1 4496 ? 198.822 291.013 233.536 1.00 28.62 ? 4496 ALA A C     1 
ATOM   22458 O  O     . ALA A 1 4496 ? 198.802 291.235 234.752 1.00 28.96 ? 4496 ALA A O     1 
ATOM   22459 C  CB    . ALA A 1 4496 ? 197.340 289.208 232.617 1.00 24.03 ? 4496 ALA A CB    1 
ATOM   22460 N  N     . ALA A 1 4497 ? 199.955 291.012 232.833 1.00 27.58 ? 4497 ALA A N     1 
ATOM   22461 C  CA    . ALA A 1 4497 ? 201.226 291.328 233.478 1.00 28.87 ? 4497 ALA A CA    1 
ATOM   22462 C  C     . ALA A 1 4497 ? 201.282 292.793 233.898 1.00 28.97 ? 4497 ALA A C     1 
ATOM   22463 O  O     . ALA A 1 4497 ? 201.710 293.114 235.012 1.00 29.55 ? 4497 ALA A O     1 
ATOM   22464 C  CB    . ALA A 1 4497 ? 202.389 290.989 232.546 1.00 26.95 ? 4497 ALA A CB    1 
ATOM   22465 N  N     . SER A 1 4498 ? 200.853 293.694 233.019 1.00 27.46 ? 4498 SER A N     1 
ATOM   22466 C  CA    . SER A 1 4498 ? 200.867 295.131 233.279 1.00 28.61 ? 4498 SER A CA    1 
ATOM   22467 C  C     . SER A 1 4498 ? 199.423 295.610 233.401 1.00 29.30 ? 4498 SER A C     1 
ATOM   22468 O  O     . SER A 1 4498 ? 198.781 295.933 232.398 1.00 31.91 ? 4498 SER A O     1 
ATOM   22469 C  CB    . SER A 1 4498 ? 201.611 295.878 232.177 1.00 29.51 ? 4498 SER A CB    1 
ATOM   22470 O  OG    . SER A 1 4498 ? 202.934 295.392 232.035 1.00 37.99 ? 4498 SER A OG    1 
ATOM   22471 N  N     . GLY A 1 4499 ? 198.919 295.660 234.635 1.00 31.00 ? 4499 GLY A N     1 
ATOM   22472 C  CA    . GLY A 1 4499 ? 197.561 296.088 234.925 1.00 30.52 ? 4499 GLY A CA    1 
ATOM   22473 C  C     . GLY A 1 4499 ? 196.765 295.076 235.725 1.00 30.64 ? 4499 GLY A C     1 
ATOM   22474 O  O     . GLY A 1 4499 ? 195.861 295.460 236.476 1.00 35.96 ? 4499 GLY A O     1 
ATOM   22475 N  N     . GLY A 1 4500 ? 197.082 293.794 235.580 1.00 28.47 ? 4500 GLY A N     1 
ATOM   22476 C  CA    . GLY A 1 4500 ? 196.420 292.745 236.333 1.00 28.16 ? 4500 GLY A CA    1 
ATOM   22477 C  C     . GLY A 1 4500 ? 195.351 292.038 235.522 1.00 34.09 ? 4500 GLY A C     1 
ATOM   22478 O  O     . GLY A 1 4500 ? 195.059 292.376 234.370 1.00 34.61 ? 4500 GLY A O     1 
ATOM   22479 N  N     . ALA A 1 4501 ? 194.755 291.029 236.159 1.00 24.32 ? 4501 ALA A N     1 
ATOM   22480 C  CA    . ALA A 1 4501 ? 193.716 290.240 235.510 1.00 31.33 ? 4501 ALA A CA    1 
ATOM   22481 C  C     . ALA A 1 4501 ? 192.448 291.044 235.251 1.00 33.75 ? 4501 ALA A C     1 
ATOM   22482 O  O     . ALA A 1 4501 ? 191.603 290.606 234.465 1.00 33.80 ? 4501 ALA A O     1 
ATOM   22483 C  CB    . ALA A 1 4501 ? 193.386 289.005 236.350 1.00 28.41 ? 4501 ALA A CB    1 
ATOM   22484 N  N     . LYS A 1 4502 ? 192.290 292.202 235.898 1.00 30.22 ? 4502 LYS A N     1 
ATOM   22485 C  CA    . LYS A 1 4502 ? 191.128 293.044 235.646 1.00 27.42 ? 4502 LYS A CA    1 
ATOM   22486 C  C     . LYS A 1 4502 ? 191.139 293.638 234.244 1.00 31.94 ? 4502 LYS A C     1 
ATOM   22487 O  O     . LYS A 1 4502 ? 190.077 294.014 233.737 1.00 29.20 ? 4502 LYS A O     1 
ATOM   22488 C  CB    . LYS A 1 4502 ? 191.052 294.162 236.686 1.00 28.05 ? 4502 LYS A CB    1 
ATOM   22489 C  CG    . LYS A 1 4502 ? 192.234 295.116 236.660 1.00 28.69 ? 4502 LYS A CG    1 
ATOM   22490 C  CD    . LYS A 1 4502 ? 191.971 296.347 237.513 1.00 29.22 ? 4502 LYS A CD    1 
ATOM   22491 C  CE    . LYS A 1 4502 ? 193.101 297.354 237.392 1.00 29.77 ? 4502 LYS A CE    1 
ATOM   22492 N  NZ    . LYS A 1 4502 ? 192.839 298.582 238.193 1.00 26.26 ? 4502 LYS A NZ    1 
ATOM   22493 N  N     . GLU A 1 4503 ? 192.308 293.737 233.610 1.00 29.62 ? 4503 GLU A N     1 
ATOM   22494 C  CA    . GLU A 1 4503 ? 192.388 294.233 232.243 1.00 25.75 ? 4503 GLU A CA    1 
ATOM   22495 C  C     . GLU A 1 4503 ? 191.917 293.210 231.217 1.00 24.70 ? 4503 GLU A C     1 
ATOM   22496 O  O     . GLU A 1 4503 ? 191.762 293.564 230.044 1.00 28.42 ? 4503 GLU A O     1 
ATOM   22497 C  CB    . GLU A 1 4503 ? 193.821 294.666 231.923 1.00 25.84 ? 4503 GLU A CB    1 
ATOM   22498 C  CG    . GLU A 1 4503 ? 194.486 295.480 233.023 1.00 31.54 ? 4503 GLU A CG    1 
ATOM   22499 C  CD    . GLU A 1 4503 ? 193.980 296.908 233.089 1.00 35.91 ? 4503 GLU A CD    1 
ATOM   22500 O  OE1   . GLU A 1 4503 ? 193.214 297.316 232.190 1.00 32.05 ? 4503 GLU A OE1   1 
ATOM   22501 O  OE2   . GLU A 1 4503 ? 194.351 297.627 234.043 1.00 35.02 ? 4503 GLU A OE2   1 
ATOM   22502 N  N     . LEU A 1 4504 ? 191.699 291.959 231.627 1.00 18.52 ? 4504 LEU A N     1 
ATOM   22503 C  CA    . LEU A 1 4504 ? 191.176 290.949 230.712 1.00 24.14 ? 4504 LEU A CA    1 
ATOM   22504 C  C     . LEU A 1 4504 ? 189.767 291.276 230.242 1.00 25.12 ? 4504 LEU A C     1 
ATOM   22505 O  O     . LEU A 1 4504 ? 189.378 290.861 229.146 1.00 26.16 ? 4504 LEU A O     1 
ATOM   22506 C  CB    . LEU A 1 4504 ? 191.188 289.576 231.386 1.00 26.62 ? 4504 LEU A CB    1 
ATOM   22507 C  CG    . LEU A 1 4504 ? 192.549 289.016 231.806 1.00 26.78 ? 4504 LEU A CG    1 
ATOM   22508 C  CD1   . LEU A 1 4504 ? 192.382 287.658 232.472 1.00 26.85 ? 4504 LEU A CD1   1 
ATOM   22509 C  CD2   . LEU A 1 4504 ? 193.485 288.924 230.616 1.00 18.13 ? 4504 LEU A CD2   1 
ATOM   22510 N  N     . LYS A 1 4505 ? 188.997 292.008 231.048 1.00 26.12 ? 4505 LYS A N     1 
ATOM   22511 C  CA    . LYS A 1 4505 ? 187.616 292.322 230.700 1.00 23.24 ? 4505 LYS A CA    1 
ATOM   22512 C  C     . LYS A 1 4505 ? 187.520 293.424 229.652 1.00 23.64 ? 4505 LYS A C     1 
ATOM   22513 O  O     . LYS A 1 4505 ? 186.598 293.412 228.831 1.00 31.32 ? 4505 LYS A O     1 
ATOM   22514 C  CB    . LYS A 1 4505 ? 186.847 292.715 231.965 1.00 17.77 ? 4505 LYS A CB    1 
ATOM   22515 C  CG    . LYS A 1 4505 ? 185.377 293.042 231.761 1.00 19.89 ? 4505 LYS A CG    1 
ATOM   22516 C  CD    . LYS A 1 4505 ? 185.141 294.538 231.668 1.00 21.33 ? 4505 LYS A CD    1 
ATOM   22517 C  CE    . LYS A 1 4505 ? 183.865 294.845 230.915 1.00 23.09 ? 4505 LYS A CE    1 
ATOM   22518 N  NZ    . LYS A 1 4505 ? 183.728 296.300 230.639 1.00 29.22 ? 4505 LYS A NZ    1 
ATOM   22519 N  N     . ASN A 1 4506 ? 188.448 294.375 229.660 1.00 21.08 ? 4506 ASN A N     1 
ATOM   22520 C  CA    . ASN A 1 4506 ? 188.344 295.565 228.827 1.00 25.98 ? 4506 ASN A CA    1 
ATOM   22521 C  C     . ASN A 1 4506 ? 188.960 295.364 227.444 1.00 22.50 ? 4506 ASN A C     1 
ATOM   22522 O  O     . ASN A 1 4506 ? 188.735 296.186 226.551 1.00 20.54 ? 4506 ASN A O     1 
ATOM   22523 C  CB    . ASN A 1 4506 ? 189.013 296.745 229.552 1.00 21.35 ? 4506 ASN A CB    1 
ATOM   22524 C  CG    . ASN A 1 4506 ? 188.697 298.096 228.926 1.00 29.07 ? 4506 ASN A CG    1 
ATOM   22525 O  OD1   . ASN A 1 4506 ? 187.970 298.194 227.939 1.00 35.45 ? 4506 ASN A OD1   1 
ATOM   22526 N  ND2   . ASN A 1 4506 ? 189.252 299.151 229.509 1.00 30.04 ? 4506 ASN A ND2   1 
ATOM   22527 N  N     . ILE A 1 4507 ? 189.703 294.284 227.233 1.00 22.25 ? 4507 ILE A N     1 
ATOM   22528 C  CA    . ILE A 1 4507 ? 190.385 294.050 225.966 1.00 20.56 ? 4507 ILE A CA    1 
ATOM   22529 C  C     . ILE A 1 4507 ? 189.420 293.414 224.973 1.00 23.65 ? 4507 ILE A C     1 
ATOM   22530 O  O     . ILE A 1 4507 ? 188.652 292.510 225.322 1.00 21.94 ? 4507 ILE A O     1 
ATOM   22531 C  CB    . ILE A 1 4507 ? 191.644 293.185 226.165 1.00 17.66 ? 4507 ILE A CB    1 
ATOM   22532 C  CG1   . ILE A 1 4507 ? 192.511 293.205 224.903 1.00 19.98 ? 4507 ILE A CG1   1 
ATOM   22533 C  CG2   . ILE A 1 4507 ? 191.294 291.758 226.570 1.00 12.50 ? 4507 ILE A CG2   1 
ATOM   22534 C  CD1   . ILE A 1 4507 ? 193.101 294.559 224.590 1.00 19.38 ? 4507 ILE A CD1   1 
ATOM   22535 N  N     . HIS A 1 4508 ? 189.436 293.913 223.739 1.00 21.06 ? 4508 HIS A N     1 
ATOM   22536 C  CA    . HIS A 1 4508 ? 188.638 293.317 222.678 1.00 18.41 ? 4508 HIS A CA    1 
ATOM   22537 C  C     . HIS A 1 4508 ? 189.283 292.023 222.200 1.00 22.74 ? 4508 HIS A C     1 
ATOM   22538 O  O     . HIS A 1 4508 ? 190.510 291.912 222.126 1.00 24.23 ? 4508 HIS A O     1 
ATOM   22539 C  CB    . HIS A 1 4508 ? 188.480 294.293 221.515 1.00 18.13 ? 4508 HIS A CB    1 
ATOM   22540 C  CG    . HIS A 1 4508 ? 187.813 295.577 221.891 1.00 16.76 ? 4508 HIS A CG    1 
ATOM   22541 N  ND1   . HIS A 1 4508 ? 187.928 296.725 221.138 1.00 20.07 ? 4508 HIS A ND1   1 
ATOM   22542 C  CD2   . HIS A 1 4508 ? 187.025 295.896 222.944 1.00 16.55 ? 4508 HIS A CD2   1 
ATOM   22543 C  CE1   . HIS A 1 4508 ? 187.236 297.696 221.708 1.00 21.30 ? 4508 HIS A CE1   1 
ATOM   22544 N  NE2   . HIS A 1 4508 ? 186.678 297.219 222.806 1.00 23.53 ? 4508 HIS A NE2   1 
ATOM   22545 N  N     . VAL A 1 4509 ? 188.448 291.043 221.866 1.00 19.46 ? 4509 VAL A N     1 
ATOM   22546 C  CA    . VAL A 1 4509 ? 188.901 289.688 221.583 1.00 17.72 ? 4509 VAL A CA    1 
ATOM   22547 C  C     . VAL A 1 4509 ? 188.435 289.287 220.191 1.00 19.72 ? 4509 VAL A C     1 
ATOM   22548 O  O     . VAL A 1 4509 ? 187.262 289.463 219.846 1.00 24.29 ? 4509 VAL A O     1 
ATOM   22549 C  CB    . VAL A 1 4509 ? 188.385 288.692 222.638 1.00 19.99 ? 4509 VAL A CB    1 
ATOM   22550 C  CG1   . VAL A 1 4509 ? 188.396 287.281 222.091 1.00 14.26 ? 4509 VAL A CG1   1 
ATOM   22551 C  CG2   . VAL A 1 4509 ? 189.219 288.785 223.907 1.00 23.83 ? 4509 VAL A CG2   1 
ATOM   22552 N  N     . CYS A 1 4510 ? 189.357 288.756 219.391 1.00 15.83 ? 4510 CYS A N     1 
ATOM   22553 C  CA    . CYS A 1 4510 ? 189.026 288.100 218.133 1.00 13.31 ? 4510 CYS A CA    1 
ATOM   22554 C  C     . CYS A 1 4510 ? 188.711 286.640 218.434 1.00 14.34 ? 4510 CYS A C     1 
ATOM   22555 O  O     . CYS A 1 4510 ? 189.613 285.853 218.741 1.00 15.71 ? 4510 CYS A O     1 
ATOM   22556 C  CB    . CYS A 1 4510 ? 190.174 288.227 217.136 1.00 14.28 ? 4510 CYS A CB    1 
ATOM   22557 S  SG    . CYS A 1 4510 ? 189.848 287.503 215.516 1.00 34.97 ? 4510 CYS A SG    1 
ATOM   22558 N  N     . LEU A 1 4511 ? 187.427 286.278 218.353 1.00 16.60 ? 4511 LEU A N     1 
ATOM   22559 C  CA    . LEU A 1 4511 ? 187.016 284.922 218.703 1.00 12.03 ? 4511 LEU A CA    1 
ATOM   22560 C  C     . LEU A 1 4511 ? 187.649 283.883 217.789 1.00 11.26 ? 4511 LEU A C     1 
ATOM   22561 O  O     . LEU A 1 4511 ? 187.896 282.751 218.217 1.00 15.16 ? 4511 LEU A O     1 
ATOM   22562 C  CB    . LEU A 1 4511 ? 185.494 284.805 218.659 1.00 12.13 ? 4511 LEU A CB    1 
ATOM   22563 C  CG    . LEU A 1 4511 ? 184.771 285.073 219.975 1.00 10.91 ? 4511 LEU A CG    1 
ATOM   22564 C  CD1   . LEU A 1 4511 ? 183.272 284.943 219.789 1.00 9.65  ? 4511 LEU A CD1   1 
ATOM   22565 C  CD2   . LEU A 1 4511 ? 185.268 284.133 221.060 1.00 16.64 ? 4511 LEU A CD2   1 
ATOM   22566 N  N     . GLY A 1 4512 ? 187.911 284.241 216.531 1.00 14.87 ? 4512 GLY A N     1 
ATOM   22567 C  CA    . GLY A 1 4512 ? 188.574 283.309 215.636 1.00 12.25 ? 4512 GLY A CA    1 
ATOM   22568 C  C     . GLY A 1 4512 ? 189.971 282.951 216.100 1.00 12.60 ? 4512 GLY A C     1 
ATOM   22569 O  O     . GLY A 1 4512 ? 190.394 281.797 215.998 1.00 17.05 ? 4512 GLY A O     1 
ATOM   22570 N  N     . GLY A 1 4513 ? 190.706 283.937 216.622 1.00 14.70 ? 4513 GLY A N     1 
ATOM   22571 C  CA    . GLY A 1 4513 ? 192.061 283.686 217.079 1.00 12.14 ? 4513 GLY A CA    1 
ATOM   22572 C  C     . GLY A 1 4513 ? 192.141 282.766 218.280 1.00 15.77 ? 4513 GLY A C     1 
ATOM   22573 O  O     . GLY A 1 4513 ? 193.106 282.009 218.420 1.00 18.53 ? 4513 GLY A O     1 
ATOM   22574 N  N     . LEU A 1 4514 ? 191.144 282.818 219.163 1.00 14.07 ? 4514 LEU A N     1 
ATOM   22575 C  CA    . LEU A 1 4514 ? 191.176 282.004 220.370 1.00 15.98 ? 4514 LEU A CA    1 
ATOM   22576 C  C     . LEU A 1 4514 ? 191.151 280.520 220.028 1.00 15.95 ? 4514 LEU A C     1 
ATOM   22577 O  O     . LEU A 1 4514 ? 190.488 280.091 219.081 1.00 18.27 ? 4514 LEU A O     1 
ATOM   22578 C  CB    . LEU A 1 4514 ? 189.999 282.346 221.281 1.00 17.77 ? 4514 LEU A CB    1 
ATOM   22579 C  CG    . LEU A 1 4514 ? 189.982 283.743 221.894 1.00 19.48 ? 4514 LEU A CG    1 
ATOM   22580 C  CD1   . LEU A 1 4514 ? 188.809 283.864 222.840 1.00 15.55 ? 4514 LEU A CD1   1 
ATOM   22581 C  CD2   . LEU A 1 4514 ? 191.291 284.031 222.610 1.00 17.66 ? 4514 LEU A CD2   1 
ATOM   22582 N  N     . PHE A 1 4515 ? 191.885 279.736 220.818 1.00 16.05 ? 4515 PHE A N     1 
ATOM   22583 C  CA    . PHE A 1 4515 ? 191.969 278.303 220.562 1.00 17.99 ? 4515 PHE A CA    1 
ATOM   22584 C  C     . PHE A 1 4515 ? 190.664 277.602 220.921 1.00 19.67 ? 4515 PHE A C     1 
ATOM   22585 O  O     . PHE A 1 4515 ? 190.262 276.645 220.250 1.00 20.22 ? 4515 PHE A O     1 
ATOM   22586 C  CB    . PHE A 1 4515 ? 193.139 277.707 221.344 1.00 20.05 ? 4515 PHE A CB    1 
ATOM   22587 C  CG    . PHE A 1 4515 ? 194.483 278.141 220.838 1.00 20.66 ? 4515 PHE A CG    1 
ATOM   22588 C  CD1   . PHE A 1 4515 ? 194.653 278.515 219.515 1.00 20.29 ? 4515 PHE A CD1   1 
ATOM   22589 C  CD2   . PHE A 1 4515 ? 195.575 278.184 221.686 1.00 20.57 ? 4515 PHE A CD2   1 
ATOM   22590 C  CE1   . PHE A 1 4515 ? 195.887 278.924 219.051 1.00 19.58 ? 4515 PHE A CE1   1 
ATOM   22591 C  CE2   . PHE A 1 4515 ? 196.810 278.587 221.223 1.00 22.44 ? 4515 PHE A CE2   1 
ATOM   22592 C  CZ    . PHE A 1 4515 ? 196.968 278.956 219.903 1.00 21.87 ? 4515 PHE A CZ    1 
ATOM   22593 N  N     . VAL A 1 4516 ? 189.996 278.058 221.976 1.00 20.18 ? 4516 VAL A N     1 
ATOM   22594 C  CA    . VAL A 1 4516 ? 188.694 277.527 222.379 1.00 19.24 ? 4516 VAL A CA    1 
ATOM   22595 C  C     . VAL A 1 4516 ? 187.717 278.691 222.509 1.00 19.24 ? 4516 VAL A C     1 
ATOM   22596 O  O     . VAL A 1 4516 ? 187.484 279.180 223.622 1.00 20.14 ? 4516 VAL A O     1 
ATOM   22597 C  CB    . VAL A 1 4516 ? 188.785 276.732 223.691 1.00 20.41 ? 4516 VAL A CB    1 
ATOM   22598 C  CG1   . VAL A 1 4516 ? 187.513 275.932 223.910 1.00 22.88 ? 4516 VAL A CG1   1 
ATOM   22599 C  CG2   . VAL A 1 4516 ? 189.997 275.812 223.686 1.00 19.55 ? 4516 VAL A CG2   1 
ATOM   22600 N  N     . PRO A 1 4517 ? 187.142 279.173 221.405 1.00 19.78 ? 4517 PRO A N     1 
ATOM   22601 C  CA    . PRO A 1 4517 ? 186.213 280.312 221.501 1.00 17.84 ? 4517 PRO A CA    1 
ATOM   22602 C  C     . PRO A 1 4517 ? 184.969 280.028 222.327 1.00 18.55 ? 4517 PRO A C     1 
ATOM   22603 O  O     . PRO A 1 4517 ? 184.407 280.959 222.916 1.00 18.05 ? 4517 PRO A O     1 
ATOM   22604 C  CB    . PRO A 1 4517 ? 185.867 280.602 220.035 1.00 11.67 ? 4517 PRO A CB    1 
ATOM   22605 C  CG    . PRO A 1 4517 ? 186.152 279.328 219.318 1.00 16.12 ? 4517 PRO A CG    1 
ATOM   22606 C  CD    . PRO A 1 4517 ? 187.318 278.714 220.018 1.00 13.77 ? 4517 PRO A CD    1 
ATOM   22607 N  N     . GLU A 1 4518 ? 184.512 278.773 222.385 1.00 15.65 ? 4518 GLU A N     1 
ATOM   22608 C  CA    . GLU A 1 4518 ? 183.326 278.459 223.175 1.00 17.71 ? 4518 GLU A CA    1 
ATOM   22609 C  C     . GLU A 1 4518 ? 183.568 278.708 224.658 1.00 20.39 ? 4518 GLU A C     1 
ATOM   22610 O  O     . GLU A 1 4518 ? 182.681 279.194 225.369 1.00 20.18 ? 4518 GLU A O     1 
ATOM   22611 C  CB    . GLU A 1 4518 ? 182.900 277.009 222.943 1.00 19.06 ? 4518 GLU A CB    1 
ATOM   22612 C  CG    . GLU A 1 4518 ? 182.930 276.574 221.493 1.00 20.36 ? 4518 GLU A CG    1 
ATOM   22613 C  CD    . GLU A 1 4518 ? 184.200 275.826 221.139 1.00 24.95 ? 4518 GLU A CD    1 
ATOM   22614 O  OE1   . GLU A 1 4518 ? 185.297 276.355 221.415 1.00 26.35 ? 4518 GLU A OE1   1 
ATOM   22615 O  OE2   . GLU A 1 4518 ? 184.099 274.711 220.587 1.00 35.12 ? 4518 GLU A OE2   1 
ATOM   22616 N  N     . ALA A 1 4519 ? 184.767 278.375 225.143 1.00 21.26 ? 4519 ALA A N     1 
ATOM   22617 C  CA    . ALA A 1 4519 ? 185.083 278.569 226.553 1.00 16.64 ? 4519 ALA A CA    1 
ATOM   22618 C  C     . ALA A 1 4519 ? 185.088 280.044 226.934 1.00 15.73 ? 4519 ALA A C     1 
ATOM   22619 O  O     . ALA A 1 4519 ? 184.729 280.389 228.065 1.00 22.29 ? 4519 ALA A O     1 
ATOM   22620 C  CB    . ALA A 1 4519 ? 186.429 277.928 226.878 1.00 15.91 ? 4519 ALA A CB    1 
ATOM   22621 N  N     . TYR A 1 4520 ? 185.495 280.925 226.015 1.00 17.13 ? 4520 TYR A N     1 
ATOM   22622 C  CA    . TYR A 1 4520 ? 185.449 282.357 226.292 1.00 11.99 ? 4520 TYR A CA    1 
ATOM   22623 C  C     . TYR A 1 4520 ? 184.016 282.829 226.500 1.00 15.67 ? 4520 TYR A C     1 
ATOM   22624 O  O     . TYR A 1 4520 ? 183.749 283.663 227.372 1.00 20.06 ? 4520 TYR A O     1 
ATOM   22625 C  CB    . TYR A 1 4520 ? 186.109 283.133 225.154 1.00 13.23 ? 4520 TYR A CB    1 
ATOM   22626 C  CG    . TYR A 1 4520 ? 186.020 284.637 225.289 1.00 14.26 ? 4520 TYR A CG    1 
ATOM   22627 C  CD1   . TYR A 1 4520 ? 186.884 285.333 226.124 1.00 14.45 ? 4520 TYR A CD1   1 
ATOM   22628 C  CD2   . TYR A 1 4520 ? 185.080 285.363 224.568 1.00 14.07 ? 4520 TYR A CD2   1 
ATOM   22629 C  CE1   . TYR A 1 4520 ? 186.809 286.703 226.245 1.00 13.81 ? 4520 TYR A CE1   1 
ATOM   22630 C  CE2   . TYR A 1 4520 ? 184.999 286.734 224.684 1.00 14.74 ? 4520 TYR A CE2   1 
ATOM   22631 C  CZ    . TYR A 1 4520 ? 185.865 287.401 225.524 1.00 15.99 ? 4520 TYR A CZ    1 
ATOM   22632 O  OH    . TYR A 1 4520 ? 185.788 288.768 225.643 1.00 19.76 ? 4520 TYR A OH    1 
ATOM   22633 N  N     . ILE A 1 4521 ? 183.079 282.304 225.708 1.00 15.43 ? 4521 ILE A N     1 
ATOM   22634 C  CA    . ILE A 1 4521 ? 181.676 282.673 225.863 1.00 12.39 ? 4521 ILE A CA    1 
ATOM   22635 C  C     . ILE A 1 4521 ? 181.171 282.252 227.236 1.00 16.65 ? 4521 ILE A C     1 
ATOM   22636 O  O     . ILE A 1 4521 ? 180.466 283.008 227.916 1.00 20.54 ? 4521 ILE A O     1 
ATOM   22637 C  CB    . ILE A 1 4521 ? 180.834 282.053 224.731 1.00 16.10 ? 4521 ILE A CB    1 
ATOM   22638 C  CG1   . ILE A 1 4521 ? 181.261 282.627 223.379 1.00 16.17 ? 4521 ILE A CG1   1 
ATOM   22639 C  CG2   . ILE A 1 4521 ? 179.351 282.307 224.958 1.00 11.76 ? 4521 ILE A CG2   1 
ATOM   22640 C  CD1   . ILE A 1 4521 ? 181.163 284.123 223.294 1.00 13.69 ? 4521 ILE A CD1   1 
ATOM   22641 N  N     . THR A 1 4522 ? 181.527 281.038 227.666 1.00 18.05 ? 4522 THR A N     1 
ATOM   22642 C  CA    . THR A 1 4522 ? 181.144 280.568 228.993 1.00 17.61 ? 4522 THR A CA    1 
ATOM   22643 C  C     . THR A 1 4522 ? 181.802 281.397 230.091 1.00 21.15 ? 4522 THR A C     1 
ATOM   22644 O  O     . THR A 1 4522 ? 181.162 281.724 231.097 1.00 18.93 ? 4522 THR A O     1 
ATOM   22645 C  CB    . THR A 1 4522 ? 181.504 279.088 229.145 1.00 18.19 ? 4522 THR A CB    1 
ATOM   22646 O  OG1   . THR A 1 4522 ? 180.643 278.299 228.315 1.00 25.96 ? 4522 THR A OG1   1 
ATOM   22647 C  CG2   . THR A 1 4522 ? 181.354 278.637 230.592 1.00 23.71 ? 4522 THR A CG2   1 
ATOM   22648 N  N     . ALA A 1 4523 ? 183.076 281.754 229.911 1.00 19.72 ? 4523 ALA A N     1 
ATOM   22649 C  CA    . ALA A 1 4523 ? 183.781 282.526 230.929 1.00 17.16 ? 4523 ALA A CA    1 
ATOM   22650 C  C     . ALA A 1 4523 ? 183.137 283.888 231.143 1.00 19.34 ? 4523 ALA A C     1 
ATOM   22651 O  O     . ALA A 1 4523 ? 182.979 284.338 232.284 1.00 25.25 ? 4523 ALA A O     1 
ATOM   22652 C  CB    . ALA A 1 4523 ? 185.251 282.681 230.543 1.00 12.35 ? 4523 ALA A CB    1 
ATOM   22653 N  N     . THR A 1 4524 ? 182.760 284.565 230.055 1.00 24.43 ? 4524 THR A N     1 
ATOM   22654 C  CA    . THR A 1 4524 ? 182.084 285.852 230.180 1.00 19.41 ? 4524 THR A CA    1 
ATOM   22655 C  C     . THR A 1 4524 ? 180.729 285.698 230.857 1.00 17.23 ? 4524 THR A C     1 
ATOM   22656 O  O     . THR A 1 4524 ? 180.324 286.548 231.658 1.00 22.63 ? 4524 THR A O     1 
ATOM   22657 C  CB    . THR A 1 4524 ? 181.930 286.499 228.804 1.00 18.40 ? 4524 THR A CB    1 
ATOM   22658 O  OG1   . THR A 1 4524 ? 181.362 285.552 227.892 1.00 22.54 ? 4524 THR A OG1   1 
ATOM   22659 C  CG2   . THR A 1 4524 ? 183.281 286.952 228.279 1.00 16.21 ? 4524 THR A CG2   1 
ATOM   22660 N  N     . ARG A 1 4525 ? 180.008 284.623 230.536 1.00 16.47 ? 4525 ARG A N     1 
ATOM   22661 C  CA    . ARG A 1 4525 ? 178.755 284.335 231.226 1.00 16.10 ? 4525 ARG A CA    1 
ATOM   22662 C  C     . ARG A 1 4525 ? 178.995 284.069 232.707 1.00 20.33 ? 4525 ARG A C     1 
ATOM   22663 O  O     . ARG A 1 4525 ? 178.235 284.536 233.563 1.00 23.11 ? 4525 ARG A O     1 
ATOM   22664 C  CB    . ARG A 1 4525 ? 178.068 283.140 230.567 1.00 14.93 ? 4525 ARG A CB    1 
ATOM   22665 C  CG    . ARG A 1 4525 ? 176.668 282.852 231.068 1.00 15.43 ? 4525 ARG A CG    1 
ATOM   22666 C  CD    . ARG A 1 4525 ? 176.219 281.474 230.620 1.00 19.69 ? 4525 ARG A CD    1 
ATOM   22667 N  NE    . ARG A 1 4525 ? 174.769 281.368 230.515 1.00 23.66 ? 4525 ARG A NE    1 
ATOM   22668 C  CZ    . ARG A 1 4525 ? 174.126 281.012 229.411 1.00 25.99 ? 4525 ARG A CZ    1 
ATOM   22669 N  NH1   . ARG A 1 4525 ? 174.778 280.723 228.296 1.00 20.56 ? 4525 ARG A NH1   1 
ATOM   22670 N  NH2   . ARG A 1 4525 ? 172.799 280.944 229.428 1.00 24.49 ? 4525 ARG A NH2   1 
ATOM   22671 N  N     . GLN A 1 4526 ? 180.052 283.320 233.026 1.00 19.57 ? 4526 GLN A N     1 
ATOM   22672 C  CA    . GLN A 1 4526 ? 180.386 283.046 234.419 1.00 18.50 ? 4526 GLN A CA    1 
ATOM   22673 C  C     . GLN A 1 4526 ? 180.875 284.297 235.139 1.00 20.51 ? 4526 GLN A C     1 
ATOM   22674 O  O     . GLN A 1 4526 ? 180.659 284.440 236.347 1.00 29.62 ? 4526 GLN A O     1 
ATOM   22675 C  CB    . GLN A 1 4526 ? 181.431 281.931 234.484 1.00 21.22 ? 4526 GLN A CB    1 
ATOM   22676 C  CG    . GLN A 1 4526 ? 181.995 281.651 235.864 1.00 23.69 ? 4526 GLN A CG    1 
ATOM   22677 C  CD    . GLN A 1 4526 ? 180.934 281.235 236.856 1.00 23.81 ? 4526 GLN A CD    1 
ATOM   22678 O  OE1   . GLN A 1 4526 ? 180.262 280.221 236.676 1.00 19.53 ? 4526 GLN A OE1   1 
ATOM   22679 N  NE2   . GLN A 1 4526 ? 180.775 282.022 237.915 1.00 32.43 ? 4526 GLN A NE2   1 
ATOM   22680 N  N     . TYR A 1 4527 ? 181.530 285.211 234.418 1.00 16.66 ? 4527 TYR A N     1 
ATOM   22681 C  CA    . TYR A 1 4527 ? 182.031 286.435 235.036 1.00 21.26 ? 4527 TYR A CA    1 
ATOM   22682 C  C     . TYR A 1 4527 ? 180.887 287.315 235.526 1.00 21.46 ? 4527 TYR A C     1 
ATOM   22683 O  O     . TYR A 1 4527 ? 180.922 287.833 236.649 1.00 27.69 ? 4527 TYR A O     1 
ATOM   22684 C  CB    . TYR A 1 4527 ? 182.923 287.178 234.034 1.00 18.01 ? 4527 TYR A CB    1 
ATOM   22685 C  CG    . TYR A 1 4527 ? 183.404 288.563 234.435 1.00 20.61 ? 4527 TYR A CG    1 
ATOM   22686 C  CD1   . TYR A 1 4527 ? 182.554 289.664 234.410 1.00 17.57 ? 4527 TYR A CD1   1 
ATOM   22687 C  CD2   . TYR A 1 4527 ? 184.724 288.770 234.816 1.00 23.78 ? 4527 TYR A CD2   1 
ATOM   22688 C  CE1   . TYR A 1 4527 ? 183.000 290.920 234.767 1.00 22.46 ? 4527 TYR A CE1   1 
ATOM   22689 C  CE2   . TYR A 1 4527 ? 185.181 290.022 235.173 1.00 19.93 ? 4527 TYR A CE2   1 
ATOM   22690 C  CZ    . TYR A 1 4527 ? 184.315 291.093 235.146 1.00 24.12 ? 4527 TYR A CZ    1 
ATOM   22691 O  OH    . TYR A 1 4527 ? 184.766 292.342 235.503 1.00 32.10 ? 4527 TYR A OH    1 
ATOM   22692 N  N     . VAL A 1 4528 ? 179.865 287.506 234.689 1.00 20.04 ? 4528 VAL A N     1 
ATOM   22693 C  CA    . VAL A 1 4528 ? 178.782 288.423 235.034 1.00 19.30 ? 4528 VAL A CA    1 
ATOM   22694 C  C     . VAL A 1 4528 ? 177.917 287.848 236.148 1.00 26.20 ? 4528 VAL A C     1 
ATOM   22695 O  O     . VAL A 1 4528 ? 177.525 288.564 237.077 1.00 32.58 ? 4528 VAL A O     1 
ATOM   22696 C  CB    . VAL A 1 4528 ? 177.954 288.759 233.780 1.00 22.96 ? 4528 VAL A CB    1 
ATOM   22697 C  CG1   . VAL A 1 4528 ? 176.830 289.719 234.126 1.00 17.16 ? 4528 VAL A CG1   1 
ATOM   22698 C  CG2   . VAL A 1 4528 ? 178.853 289.353 232.705 1.00 16.23 ? 4528 VAL A CG2   1 
ATOM   22699 N  N     . ALA A 1 4529 ? 177.608 286.551 236.080 1.00 23.43 ? 4529 ALA A N     1 
ATOM   22700 C  CA    . ALA A 1 4529 ? 176.792 285.934 237.122 1.00 25.26 ? 4529 ALA A CA    1 
ATOM   22701 C  C     . ALA A 1 4529 ? 177.501 285.937 238.469 1.00 30.87 ? 4529 ALA A C     1 
ATOM   22702 O  O     . ALA A 1 4529 ? 176.842 285.909 239.515 1.00 29.38 ? 4529 ALA A O     1 
ATOM   22703 C  CB    . ALA A 1 4529 ? 176.418 284.508 236.729 1.00 26.67 ? 4529 ALA A CB    1 
ATOM   22704 N  N     . GLN A 1 4530 ? 178.835 285.961 238.468 1.00 27.90 ? 4530 GLN A N     1 
ATOM   22705 C  CA    . GLN A 1 4530 ? 179.569 286.001 239.727 1.00 25.43 ? 4530 GLN A CA    1 
ATOM   22706 C  C     . GLN A 1 4530 ? 179.386 287.335 240.438 1.00 31.53 ? 4530 GLN A C     1 
ATOM   22707 O  O     . GLN A 1 4530 ? 179.139 287.369 241.651 1.00 38.68 ? 4530 GLN A O     1 
ATOM   22708 C  CB    . GLN A 1 4530 ? 181.048 285.725 239.473 1.00 26.02 ? 4530 GLN A CB    1 
ATOM   22709 C  CG    . GLN A 1 4530 ? 181.848 285.463 240.731 1.00 25.22 ? 4530 GLN A CG    1 
ATOM   22710 C  CD    . GLN A 1 4530 ? 183.134 284.714 240.449 1.00 33.52 ? 4530 GLN A CD    1 
ATOM   22711 O  OE1   . GLN A 1 4530 ? 183.413 284.350 239.309 1.00 32.23 ? 4530 GLN A OE1   1 
ATOM   22712 N  NE2   . GLN A 1 4530 ? 183.925 284.481 241.491 1.00 36.59 ? 4530 GLN A NE2   1 
ATOM   22713 N  N     . ALA A 1 4531 ? 179.495 288.445 239.704 1.00 26.43 ? 4531 ALA A N     1 
ATOM   22714 C  CA    . ALA A 1 4531 ? 179.363 289.759 240.327 1.00 26.53 ? 4531 ALA A CA    1 
ATOM   22715 C  C     . ALA A 1 4531 ? 177.953 289.985 240.854 1.00 30.50 ? 4531 ALA A C     1 
ATOM   22716 O  O     . ALA A 1 4531 ? 177.771 290.572 241.927 1.00 34.70 ? 4531 ALA A O     1 
ATOM   22717 C  CB    . ALA A 1 4531 ? 179.745 290.854 239.331 1.00 24.32 ? 4531 ALA A CB    1 
ATOM   22718 N  N     . ASN A 1 4532 ? 176.947 289.524 240.119 1.00 31.16 ? 4532 ASN A N     1 
ATOM   22719 C  CA    . ASN A 1 4532 ? 175.552 289.729 240.475 1.00 29.35 ? 4532 ASN A CA    1 
ATOM   22720 C  C     . ASN A 1 4532 ? 174.972 288.573 241.280 1.00 31.41 ? 4532 ASN A C     1 
ATOM   22721 O  O     . ASN A 1 4532 ? 173.769 288.574 241.559 1.00 31.78 ? 4532 ASN A O     1 
ATOM   22722 C  CB    . ASN A 1 4532 ? 174.725 289.954 239.208 1.00 29.36 ? 4532 ASN A CB    1 
ATOM   22723 C  CG    . ASN A 1 4532 ? 175.315 291.021 238.310 1.00 33.34 ? 4532 ASN A CG    1 
ATOM   22724 O  OD1   . ASN A 1 4532 ? 175.609 290.770 237.140 1.00 34.63 ? 4532 ASN A OD1   1 
ATOM   22725 N  ND2   . ASN A 1 4532 ? 175.505 292.217 238.855 1.00 34.20 ? 4532 ASN A ND2   1 
ATOM   22726 N  N     . SER A 1 4533 ? 175.801 287.593 241.650 1.00 29.98 ? 4533 SER A N     1 
ATOM   22727 C  CA    . SER A 1 4533 ? 175.380 286.448 242.460 1.00 28.51 ? 4533 SER A CA    1 
ATOM   22728 C  C     . SER A 1 4533 ? 174.226 285.688 241.807 1.00 29.42 ? 4533 SER A C     1 
ATOM   22729 O  O     . SER A 1 4533 ? 173.287 285.252 242.477 1.00 30.43 ? 4533 SER A O     1 
ATOM   22730 C  CB    . SER A 1 4533 ? 175.011 286.880 243.882 1.00 28.42 ? 4533 SER A CB    1 
ATOM   22731 O  OG    . SER A 1 4533 ? 174.725 285.757 244.696 1.00 29.99 ? 4533 SER A OG    1 
ATOM   22732 N  N     . TRP A 1 4534 ? 174.297 285.521 240.492 1.00 27.74 ? 4534 TRP A N     1 
ATOM   22733 C  CA    . TRP A 1 4534 ? 173.273 284.820 239.733 1.00 25.28 ? 4534 TRP A CA    1 
ATOM   22734 C  C     . TRP A 1 4534 ? 173.806 283.486 239.224 1.00 25.68 ? 4534 TRP A C     1 
ATOM   22735 O  O     . TRP A 1 4534 ? 174.988 283.161 239.365 1.00 27.45 ? 4534 TRP A O     1 
ATOM   22736 C  CB    . TRP A 1 4534 ? 172.780 285.673 238.559 1.00 25.98 ? 4534 TRP A CB    1 
ATOM   22737 C  CG    . TRP A 1 4534 ? 172.020 286.892 238.968 1.00 27.98 ? 4534 TRP A CG    1 
ATOM   22738 C  CD1   . TRP A 1 4534 ? 171.273 287.051 240.098 1.00 28.16 ? 4534 TRP A CD1   1 
ATOM   22739 C  CD2   . TRP A 1 4534 ? 171.913 288.121 238.241 1.00 27.46 ? 4534 TRP A CD2   1 
ATOM   22740 N  NE1   . TRP A 1 4534 ? 170.717 288.306 240.124 1.00 32.23 ? 4534 TRP A NE1   1 
ATOM   22741 C  CE2   . TRP A 1 4534 ? 171.093 288.981 238.994 1.00 27.30 ? 4534 TRP A CE2   1 
ATOM   22742 C  CE3   . TRP A 1 4534 ? 172.436 288.577 237.026 1.00 29.03 ? 4534 TRP A CE3   1 
ATOM   22743 C  CZ2   . TRP A 1 4534 ? 170.784 290.274 238.575 1.00 29.05 ? 4534 TRP A CZ2   1 
ATOM   22744 C  CZ3   . TRP A 1 4534 ? 172.128 289.861 236.613 1.00 30.05 ? 4534 TRP A CZ3   1 
ATOM   22745 C  CH2   . TRP A 1 4534 ? 171.310 290.694 237.384 1.00 29.73 ? 4534 TRP A CH2   1 
ATOM   22746 N  N     . SER A 1 4535 ? 172.904 282.709 238.636 1.00 25.76 ? 4535 SER A N     1 
ATOM   22747 C  CA    . SER A 1 4535 ? 173.255 281.452 237.997 1.00 27.37 ? 4535 SER A CA    1 
ATOM   22748 C  C     . SER A 1 4535 ? 173.471 281.664 236.505 1.00 31.07 ? 4535 SER A C     1 
ATOM   22749 O  O     . SER A 1 4535 ? 172.928 282.597 235.906 1.00 33.00 ? 4535 SER A O     1 
ATOM   22750 C  CB    . SER A 1 4535 ? 172.162 280.406 238.224 1.00 27.69 ? 4535 SER A CB    1 
ATOM   22751 O  OG    . SER A 1 4535 ? 172.409 279.237 237.464 1.00 32.65 ? 4535 SER A OG    1 
ATOM   22752 N  N     . LEU A 1 4536 ? 174.276 280.781 235.905 1.00 24.35 ? 4536 LEU A N     1 
ATOM   22753 C  CA    . LEU A 1 4536 ? 174.563 280.902 234.480 1.00 26.22 ? 4536 LEU A CA    1 
ATOM   22754 C  C     . LEU A 1 4536 ? 173.302 280.741 233.643 1.00 32.76 ? 4536 LEU A C     1 
ATOM   22755 O  O     . LEU A 1 4536 ? 173.163 281.391 232.601 1.00 32.26 ? 4536 LEU A O     1 
ATOM   22756 C  CB    . LEU A 1 4536 ? 175.613 279.875 234.055 1.00 26.07 ? 4536 LEU A CB    1 
ATOM   22757 C  CG    . LEU A 1 4536 ? 177.004 279.966 234.688 1.00 29.55 ? 4536 LEU A CG    1 
ATOM   22758 C  CD1   . LEU A 1 4536 ? 177.078 279.130 235.961 1.00 25.09 ? 4536 LEU A CD1   1 
ATOM   22759 C  CD2   . LEU A 1 4536 ? 178.078 279.550 233.701 1.00 22.50 ? 4536 LEU A CD2   1 
ATOM   22760 N  N     . GLU A 1 4537 ? 172.379 279.881 234.079 1.00 32.26 ? 4537 GLU A N     1 
ATOM   22761 C  CA    . GLU A 1 4537 ? 171.121 279.711 233.359 1.00 25.63 ? 4537 GLU A CA    1 
ATOM   22762 C  C     . GLU A 1 4537 ? 170.254 280.959 233.436 1.00 30.05 ? 4537 GLU A C     1 
ATOM   22763 O  O     . GLU A 1 4537 ? 169.372 281.152 232.589 1.00 36.34 ? 4537 GLU A O     1 
ATOM   22764 C  CB    . GLU A 1 4537 ? 170.358 278.505 233.907 1.00 27.43 ? 4537 GLU A CB    1 
ATOM   22765 C  CG    . GLU A 1 4537 ? 171.126 277.197 233.831 1.00 30.96 ? 4537 GLU A CG    1 
ATOM   22766 C  CD    . GLU A 1 4537 ? 170.376 276.045 234.471 1.00 35.51 ? 4537 GLU A CD    1 
ATOM   22767 O  OE1   . GLU A 1 4537 ? 169.246 275.751 234.028 1.00 31.75 ? 4537 GLU A OE1   1 
ATOM   22768 O  OE2   . GLU A 1 4537 ? 170.919 275.432 235.415 1.00 32.45 ? 4537 GLU A OE2   1 
ATOM   22769 N  N     . GLU A 1 4538 ? 170.480 281.813 234.432 1.00 25.04 ? 4538 GLU A N     1 
ATOM   22770 C  CA    . GLU A 1 4538 ? 169.676 283.016 234.601 1.00 31.00 ? 4538 GLU A CA    1 
ATOM   22771 C  C     . GLU A 1 4538 ? 170.167 284.185 233.760 1.00 27.28 ? 4538 GLU A C     1 
ATOM   22772 O  O     . GLU A 1 4538 ? 169.601 285.277 233.870 1.00 25.61 ? 4538 GLU A O     1 
ATOM   22773 C  CB    . GLU A 1 4538 ? 169.641 283.419 236.077 1.00 32.69 ? 4538 GLU A CB    1 
ATOM   22774 C  CG    . GLU A 1 4538 ? 169.226 282.299 237.015 1.00 32.88 ? 4538 GLU A CG    1 
ATOM   22775 C  CD    . GLU A 1 4538 ? 169.496 282.628 238.469 1.00 39.56 ? 4538 GLU A CD    1 
ATOM   22776 O  OE1   . GLU A 1 4538 ? 170.025 283.725 238.745 1.00 40.24 ? 4538 GLU A OE1   1 
ATOM   22777 O  OE2   . GLU A 1 4538 ? 169.177 281.789 239.338 1.00 39.94 ? 4538 GLU A OE2   1 
ATOM   22778 N  N     . LEU A 1 4539 ? 171.197 283.995 232.938 1.00 28.07 ? 4539 LEU A N     1 
ATOM   22779 C  CA    . LEU A 1 4539 ? 171.724 285.047 232.076 1.00 23.03 ? 4539 LEU A CA    1 
ATOM   22780 C  C     . LEU A 1 4539 ? 171.437 284.692 230.623 1.00 23.03 ? 4539 LEU A C     1 
ATOM   22781 O  O     . LEU A 1 4539 ? 171.801 283.608 230.157 1.00 27.78 ? 4539 LEU A O     1 
ATOM   22782 C  CB    . LEU A 1 4539 ? 173.222 285.237 232.292 1.00 18.40 ? 4539 LEU A CB    1 
ATOM   22783 C  CG    . LEU A 1 4539 ? 173.689 285.769 233.643 1.00 18.92 ? 4539 LEU A CG    1 
ATOM   22784 C  CD1   . LEU A 1 4539 ? 175.199 285.756 233.683 1.00 24.80 ? 4539 LEU A CD1   1 
ATOM   22785 C  CD2   . LEU A 1 4539 ? 173.159 287.171 233.877 1.00 20.09 ? 4539 LEU A CD2   1 
ATOM   22786 N  N     . CYS A 1 4540 ? 170.787 285.606 229.914 1.00 19.89 ? 4540 CYS A N     1 
ATOM   22787 C  CA    . CYS A 1 4540 ? 170.631 285.520 228.472 1.00 18.06 ? 4540 CYS A CA    1 
ATOM   22788 C  C     . CYS A 1 4540 ? 171.596 286.495 227.809 1.00 24.14 ? 4540 CYS A C     1 
ATOM   22789 O  O     . CYS A 1 4540 ? 171.923 287.545 228.366 1.00 24.14 ? 4540 CYS A O     1 
ATOM   22790 C  CB    . CYS A 1 4540 ? 169.193 285.826 228.052 1.00 17.90 ? 4540 CYS A CB    1 
ATOM   22791 S  SG    . CYS A 1 4540 ? 168.663 287.522 228.368 1.00 51.10 ? 4540 CYS A SG    1 
ATOM   22792 N  N     . LEU A 1 4541 ? 172.060 286.131 226.620 1.00 22.09 ? 4541 LEU A N     1 
ATOM   22793 C  CA    . LEU A 1 4541 ? 173.074 286.903 225.912 1.00 17.38 ? 4541 LEU A CA    1 
ATOM   22794 C  C     . LEU A 1 4541 ? 172.400 287.904 224.983 1.00 15.41 ? 4541 LEU A C     1 
ATOM   22795 O  O     . LEU A 1 4541 ? 171.694 287.512 224.049 1.00 25.07 ? 4541 LEU A O     1 
ATOM   22796 C  CB    . LEU A 1 4541 ? 174.007 285.985 225.124 1.00 15.60 ? 4541 LEU A CB    1 
ATOM   22797 C  CG    . LEU A 1 4541 ? 175.090 286.680 224.296 1.00 19.57 ? 4541 LEU A CG    1 
ATOM   22798 C  CD1   . LEU A 1 4541 ? 175.907 287.623 225.165 1.00 18.93 ? 4541 LEU A CD1   1 
ATOM   22799 C  CD2   . LEU A 1 4541 ? 175.989 285.654 223.626 1.00 16.38 ? 4541 LEU A CD2   1 
ATOM   22800 N  N     . GLU A 1 4542 ? 172.620 289.188 225.244 1.00 18.35 ? 4542 GLU A N     1 
ATOM   22801 C  CA    . GLU A 1 4542 ? 172.183 290.257 224.360 1.00 14.75 ? 4542 GLU A CA    1 
ATOM   22802 C  C     . GLU A 1 4542 ? 173.368 290.734 223.533 1.00 15.92 ? 4542 GLU A C     1 
ATOM   22803 O  O     . GLU A 1 4542 ? 174.478 290.889 224.050 1.00 20.55 ? 4542 GLU A O     1 
ATOM   22804 C  CB    . GLU A 1 4542 ? 171.587 291.424 225.150 1.00 16.44 ? 4542 GLU A CB    1 
ATOM   22805 C  CG    . GLU A 1 4542 ? 170.209 291.147 225.719 1.00 20.38 ? 4542 GLU A CG    1 
ATOM   22806 C  CD    . GLU A 1 4542 ? 169.254 290.578 224.687 1.00 33.42 ? 4542 GLU A CD    1 
ATOM   22807 O  OE1   . GLU A 1 4542 ? 168.908 289.384 224.789 1.00 29.95 ? 4542 GLU A OE1   1 
ATOM   22808 O  OE2   . GLU A 1 4542 ? 168.847 291.329 223.776 1.00 28.74 ? 4542 GLU A OE2   1 
ATOM   22809 N  N     . VAL A 1 4543 ? 173.129 290.957 222.244 1.00 15.95 ? 4543 VAL A N     1 
ATOM   22810 C  CA    . VAL A 1 4543 ? 174.183 291.259 221.287 1.00 11.77 ? 4543 VAL A CA    1 
ATOM   22811 C  C     . VAL A 1 4543 ? 173.967 292.667 220.751 1.00 11.45 ? 4543 VAL A C     1 
ATOM   22812 O  O     . VAL A 1 4543 ? 172.861 293.009 220.319 1.00 17.13 ? 4543 VAL A O     1 
ATOM   22813 C  CB    . VAL A 1 4543 ? 174.213 290.233 220.141 1.00 14.35 ? 4543 VAL A CB    1 
ATOM   22814 C  CG1   . VAL A 1 4543 ? 174.990 290.774 218.955 1.00 9.71  ? 4543 VAL A CG1   1 
ATOM   22815 C  CG2   . VAL A 1 4543 ? 174.812 288.922 220.625 1.00 12.60 ? 4543 VAL A CG2   1 
ATOM   22816 N  N     . ASN A 1 4544 ? 175.020 293.479 220.790 1.00 15.39 ? 4544 ASN A N     1 
ATOM   22817 C  CA    . ASN A 1 4544 ? 175.010 294.812 220.207 1.00 11.56 ? 4544 ASN A CA    1 
ATOM   22818 C  C     . ASN A 1 4544 ? 176.195 294.943 219.265 1.00 13.96 ? 4544 ASN A C     1 
ATOM   22819 O  O     . ASN A 1 4544 ? 177.323 294.592 219.629 1.00 17.00 ? 4544 ASN A O     1 
ATOM   22820 C  CB    . ASN A 1 4544 ? 175.062 295.897 221.287 1.00 17.05 ? 4544 ASN A CB    1 
ATOM   22821 C  CG    . ASN A 1 4544 ? 175.285 297.281 220.715 1.00 21.03 ? 4544 ASN A CG    1 
ATOM   22822 O  OD1   . ASN A 1 4544 ? 174.354 297.921 220.234 1.00 22.95 ? 4544 ASN A OD1   1 
ATOM   22823 N  ND2   . ASN A 1 4544 ? 176.525 297.750 220.764 1.00 22.46 ? 4544 ASN A ND2   1 
ATOM   22824 N  N     . VAL A 1 4545 ? 175.938 295.440 218.060 1.00 15.77 ? 4545 VAL A N     1 
ATOM   22825 C  CA    . VAL A 1 4545 ? 176.950 295.601 217.023 1.00 15.19 ? 4545 VAL A CA    1 
ATOM   22826 C  C     . VAL A 1 4545 ? 177.182 297.088 216.816 1.00 17.82 ? 4545 VAL A C     1 
ATOM   22827 O  O     . VAL A 1 4545 ? 176.230 297.848 216.601 1.00 24.83 ? 4545 VAL A O     1 
ATOM   22828 C  CB    . VAL A 1 4545 ? 176.524 294.916 215.712 1.00 18.98 ? 4545 VAL A CB    1 
ATOM   22829 C  CG1   . VAL A 1 4545 ? 177.436 295.339 214.571 1.00 23.25 ? 4545 VAL A CG1   1 
ATOM   22830 C  CG2   . VAL A 1 4545 ? 176.527 293.404 215.876 1.00 10.75 ? 4545 VAL A CG2   1 
ATOM   22831 N  N     . THR A 1 4546 ? 178.443 297.503 216.884 1.00 18.86 ? 4546 THR A N     1 
ATOM   22832 C  CA    . THR A 1 4546 ? 178.816 298.905 216.787 1.00 16.97 ? 4546 THR A CA    1 
ATOM   22833 C  C     . THR A 1 4546 ? 179.282 299.242 215.377 1.00 25.09 ? 4546 THR A C     1 
ATOM   22834 O  O     . THR A 1 4546 ? 179.823 298.396 214.660 1.00 28.31 ? 4546 THR A O     1 
ATOM   22835 C  CB    . THR A 1 4546 ? 179.923 299.247 217.785 1.00 22.04 ? 4546 THR A CB    1 
ATOM   22836 O  OG1   . THR A 1 4546 ? 181.190 298.858 217.241 1.00 30.80 ? 4546 THR A OG1   1 
ATOM   22837 C  CG2   . THR A 1 4546 ? 179.702 298.514 219.091 1.00 20.05 ? 4546 THR A CG2   1 
ATOM   22838 N  N     . THR A 1 4547 ? 179.066 300.501 214.989 1.00 26.80 ? 4547 THR A N     1 
ATOM   22839 C  CA    . THR A 1 4547 ? 179.538 300.969 213.690 1.00 29.66 ? 4547 THR A CA    1 
ATOM   22840 C  C     . THR A 1 4547 ? 181.059 300.948 213.617 1.00 32.00 ? 4547 THR A C     1 
ATOM   22841 O  O     . THR A 1 4547 ? 181.634 300.592 212.582 1.00 34.03 ? 4547 THR A O     1 
ATOM   22842 C  CB    . THR A 1 4547 ? 179.007 302.376 213.414 1.00 30.30 ? 4547 THR A CB    1 
ATOM   22843 O  OG1   . THR A 1 4547 ? 177.585 302.393 213.585 1.00 35.57 ? 4547 THR A OG1   1 
ATOM   22844 C  CG2   . THR A 1 4547 ? 179.345 302.806 211.994 1.00 25.31 ? 4547 THR A CG2   1 
ATOM   22845 N  N     . SER A 1 4548 ? 181.728 301.322 214.704 1.00 29.72 ? 4548 SER A N     1 
ATOM   22846 C  CA    . SER A 1 4548 ? 183.182 301.329 214.755 1.00 31.01 ? 4548 SER A CA    1 
ATOM   22847 C  C     . SER A 1 4548 ? 183.640 300.704 216.063 1.00 30.50 ? 4548 SER A C     1 
ATOM   22848 O  O     . SER A 1 4548 ? 182.909 300.678 217.056 1.00 28.30 ? 4548 SER A O     1 
ATOM   22849 C  CB    . SER A 1 4548 ? 183.748 302.750 214.620 1.00 29.17 ? 4548 SER A CB    1 
ATOM   22850 O  OG    . SER A 1 4548 ? 183.421 303.538 215.751 1.00 30.02 ? 4548 SER A OG    1 
ATOM   22851 N  N     . GLN A 1 4549 ? 184.871 300.200 216.051 1.00 33.72 ? 4549 GLN A N     1 
ATOM   22852 C  CA    . GLN A 1 4549 ? 185.462 299.618 217.245 1.00 28.35 ? 4549 GLN A CA    1 
ATOM   22853 C  C     . GLN A 1 4549 ? 185.863 300.717 218.226 1.00 29.41 ? 4549 GLN A C     1 
ATOM   22854 O  O     . GLN A 1 4549 ? 185.879 301.908 217.902 1.00 34.83 ? 4549 GLN A O     1 
ATOM   22855 C  CB    . GLN A 1 4549 ? 186.674 298.762 216.880 1.00 23.31 ? 4549 GLN A CB    1 
ATOM   22856 C  CG    . GLN A 1 4549 ? 186.350 297.546 216.024 1.00 24.15 ? 4549 GLN A CG    1 
ATOM   22857 C  CD    . GLN A 1 4549 ? 186.399 297.849 214.539 1.00 31.31 ? 4549 GLN A CD    1 
ATOM   22858 O  OE1   . GLN A 1 4549 ? 186.481 299.009 214.132 1.00 29.85 ? 4549 GLN A OE1   1 
ATOM   22859 N  NE2   . GLN A 1 4549 ? 186.356 296.804 213.720 1.00 28.23 ? 4549 GLN A NE2   1 
ATOM   22860 N  N     . GLY A 1 4550 ? 186.191 300.300 219.446 1.00 28.58 ? 4550 GLY A N     1 
ATOM   22861 C  CA    . GLY A 1 4550 ? 186.590 301.234 220.479 1.00 28.49 ? 4550 GLY A CA    1 
ATOM   22862 C  C     . GLY A 1 4550 ? 185.438 302.068 221.002 1.00 35.30 ? 4550 GLY A C     1 
ATOM   22863 O  O     . GLY A 1 4550 ? 185.439 303.295 220.871 1.00 34.41 ? 4550 GLY A O     1 
ATOM   22864 N  N     . ALA A 1 4551 ? 184.448 301.408 221.599 1.00 34.28 ? 4551 ALA A N     1 
ATOM   22865 C  CA    . ALA A 1 4551 ? 183.276 302.074 222.142 1.00 33.38 ? 4551 ALA A CA    1 
ATOM   22866 C  C     . ALA A 1 4551 ? 183.229 301.869 223.650 1.00 33.23 ? 4551 ALA A C     1 
ATOM   22867 O  O     . ALA A 1 4551 ? 184.028 301.120 224.222 1.00 36.21 ? 4551 ALA A O     1 
ATOM   22868 C  CB    . ALA A 1 4551 ? 181.983 301.556 221.497 1.00 28.51 ? 4551 ALA A CB    1 
ATOM   22869 N  N     . THR A 1 4552 ? 182.283 302.551 224.289 1.00 31.91 ? 4552 THR A N     1 
ATOM   22870 C  CA    . THR A 1 4552 ? 182.121 302.447 225.735 1.00 30.54 ? 4552 THR A CA    1 
ATOM   22871 C  C     . THR A 1 4552 ? 181.757 301.022 226.130 1.00 32.39 ? 4552 THR A C     1 
ATOM   22872 O  O     . THR A 1 4552 ? 180.746 300.478 225.677 1.00 35.55 ? 4552 THR A O     1 
ATOM   22873 C  CB    . THR A 1 4552 ? 181.043 303.422 226.213 1.00 32.53 ? 4552 THR A CB    1 
ATOM   22874 O  OG1   . THR A 1 4552 ? 179.793 303.094 225.597 1.00 37.30 ? 4552 THR A OG1   1 
ATOM   22875 C  CG2   . THR A 1 4552 ? 181.422 304.850 225.852 1.00 24.54 ? 4552 THR A CG2   1 
ATOM   22876 N  N     . LEU A 1 4553 ? 182.584 300.421 226.981 1.00 30.88 ? 4553 LEU A N     1 
ATOM   22877 C  CA    . LEU A 1 4553 ? 182.394 299.045 227.421 1.00 28.55 ? 4553 LEU A CA    1 
ATOM   22878 C  C     . LEU A 1 4553 ? 181.732 299.052 228.794 1.00 29.71 ? 4553 LEU A C     1 
ATOM   22879 O  O     . LEU A 1 4553 ? 182.333 299.493 229.781 1.00 34.38 ? 4553 LEU A O     1 
ATOM   22880 C  CB    . LEU A 1 4553 ? 183.724 298.297 227.451 1.00 27.28 ? 4553 LEU A CB    1 
ATOM   22881 C  CG    . LEU A 1 4553 ? 184.181 297.709 226.112 1.00 30.54 ? 4553 LEU A CG    1 
ATOM   22882 C  CD1   . LEU A 1 4553 ? 185.351 296.756 226.307 1.00 24.39 ? 4553 LEU A CD1   1 
ATOM   22883 C  CD2   . LEU A 1 4553 ? 183.024 297.012 225.414 1.00 17.43 ? 4553 LEU A CD2   1 
ATOM   22884 N  N     . ASP A 1 4554 ? 180.498 298.563 228.853 1.00 30.24 ? 4554 ASP A N     1 
ATOM   22885 C  CA    . ASP A 1 4554 ? 179.785 298.451 230.113 1.00 25.05 ? 4554 ASP A CA    1 
ATOM   22886 C  C     . ASP A 1 4554 ? 180.393 297.337 230.962 1.00 26.53 ? 4554 ASP A C     1 
ATOM   22887 O  O     . ASP A 1 4554 ? 181.153 296.494 230.478 1.00 30.40 ? 4554 ASP A O     1 
ATOM   22888 C  CB    . ASP A 1 4554 ? 178.299 298.190 229.856 1.00 26.61 ? 4554 ASP A CB    1 
ATOM   22889 C  CG    . ASP A 1 4554 ? 177.450 298.292 231.113 1.00 34.37 ? 4554 ASP A CG    1 
ATOM   22890 O  OD1   . ASP A 1 4554 ? 178.008 298.541 232.204 1.00 35.21 ? 4554 ASP A OD1   1 
ATOM   22891 O  OD2   . ASP A 1 4554 ? 176.217 298.124 231.008 1.00 40.28 ? 4554 ASP A OD2   1 
ATOM   22892 N  N     . ALA A 1 4555 ? 180.052 297.348 232.252 1.00 29.44 ? 4555 ALA A N     1 
ATOM   22893 C  CA    . ALA A 1 4555 ? 180.586 296.349 233.173 1.00 26.34 ? 4555 ALA A CA    1 
ATOM   22894 C  C     . ALA A 1 4555 ? 180.170 294.942 232.763 1.00 23.56 ? 4555 ALA A C     1 
ATOM   22895 O  O     . ALA A 1 4555 ? 180.965 293.999 232.842 1.00 27.89 ? 4555 ALA A O     1 
ATOM   22896 C  CB    . ALA A 1 4555 ? 180.128 296.654 234.599 1.00 21.27 ? 4555 ALA A CB    1 
ATOM   22897 N  N     . CYS A 1 4556 ? 178.920 294.780 232.324 1.00 24.44 ? 4556 CYS A N     1 
ATOM   22898 C  CA    . CYS A 1 4556 ? 178.396 293.486 231.902 1.00 23.18 ? 4556 CYS A CA    1 
ATOM   22899 C  C     . CYS A 1 4556 ? 178.451 293.290 230.391 1.00 24.83 ? 4556 CYS A C     1 
ATOM   22900 O  O     . CYS A 1 4556 ? 177.608 292.577 229.834 1.00 21.91 ? 4556 CYS A O     1 
ATOM   22901 C  CB    . CYS A 1 4556 ? 176.966 293.313 232.411 1.00 21.44 ? 4556 CYS A CB    1 
ATOM   22902 S  SG    . CYS A 1 4556 ? 175.814 294.595 231.858 1.00 53.93 ? 4556 CYS A SG    1 
ATOM   22903 N  N     . SER A 1 4557 ? 179.424 293.900 229.713 1.00 25.38 ? 4557 SER A N     1 
ATOM   22904 C  CA    . SER A 1 4557 ? 179.545 293.812 228.265 1.00 20.31 ? 4557 SER A CA    1 
ATOM   22905 C  C     . SER A 1 4557 ? 180.972 293.448 227.883 1.00 21.35 ? 4557 SER A C     1 
ATOM   22906 O  O     . SER A 1 4557 ? 181.925 293.763 228.601 1.00 29.57 ? 4557 SER A O     1 
ATOM   22907 C  CB    . SER A 1 4557 ? 179.144 295.127 227.592 1.00 21.26 ? 4557 SER A CB    1 
ATOM   22908 O  OG    . SER A 1 4557 ? 177.735 295.276 227.559 1.00 32.21 ? 4557 SER A OG    1 
ATOM   22909 N  N     . PHE A 1 4558 ? 181.112 292.777 226.742 1.00 15.87 ? 4558 PHE A N     1 
ATOM   22910 C  CA    . PHE A 1 4558 ? 182.413 292.342 226.255 1.00 16.60 ? 4558 PHE A CA    1 
ATOM   22911 C  C     . PHE A 1 4558 ? 182.513 292.607 224.761 1.00 14.00 ? 4558 PHE A C     1 
ATOM   22912 O  O     . PHE A 1 4558 ? 181.556 292.376 224.019 1.00 17.60 ? 4558 PHE A O     1 
ATOM   22913 C  CB    . PHE A 1 4558 ? 182.648 290.857 226.547 1.00 13.96 ? 4558 PHE A CB    1 
ATOM   22914 C  CG    . PHE A 1 4558 ? 182.643 290.522 228.006 1.00 17.18 ? 4558 PHE A CG    1 
ATOM   22915 C  CD1   . PHE A 1 4558 ? 183.800 290.625 228.757 1.00 18.68 ? 4558 PHE A CD1   1 
ATOM   22916 C  CD2   . PHE A 1 4558 ? 181.477 290.118 228.634 1.00 19.99 ? 4558 PHE A CD2   1 
ATOM   22917 C  CE1   . PHE A 1 4558 ? 183.796 290.323 230.102 1.00 15.17 ? 4558 PHE A CE1   1 
ATOM   22918 C  CE2   . PHE A 1 4558 ? 181.467 289.818 229.979 1.00 18.21 ? 4558 PHE A CE2   1 
ATOM   22919 C  CZ    . PHE A 1 4558 ? 182.628 289.919 230.713 1.00 17.36 ? 4558 PHE A CZ    1 
ATOM   22920 N  N     . GLY A 1 4559 ? 183.677 293.080 224.326 1.00 15.62 ? 4559 GLY A N     1 
ATOM   22921 C  CA    . GLY A 1 4559 ? 183.908 293.406 222.930 1.00 18.18 ? 4559 GLY A CA    1 
ATOM   22922 C  C     . GLY A 1 4559 ? 184.545 292.244 222.193 1.00 14.15 ? 4559 GLY A C     1 
ATOM   22923 O  O     . GLY A 1 4559 ? 185.533 291.665 222.652 1.00 21.94 ? 4559 GLY A O     1 
ATOM   22924 N  N     . VAL A 1 4560 ? 183.967 291.910 221.042 1.00 14.21 ? 4560 VAL A N     1 
ATOM   22925 C  CA    . VAL A 1 4560 ? 184.427 290.810 220.204 1.00 12.63 ? 4560 VAL A CA    1 
ATOM   22926 C  C     . VAL A 1 4560 ? 184.638 291.337 218.791 1.00 12.60 ? 4560 VAL A C     1 
ATOM   22927 O  O     . VAL A 1 4560 ? 183.784 292.056 218.260 1.00 18.76 ? 4560 VAL A O     1 
ATOM   22928 C  CB    . VAL A 1 4560 ? 183.432 289.633 220.209 1.00 12.20 ? 4560 VAL A CB    1 
ATOM   22929 C  CG1   . VAL A 1 4560 ? 183.838 288.579 219.194 1.00 13.68 ? 4560 VAL A CG1   1 
ATOM   22930 C  CG2   . VAL A 1 4560 ? 183.350 289.024 221.594 1.00 10.19 ? 4560 VAL A CG2   1 
ATOM   22931 N  N     . THR A 1 4561 ? 185.772 290.990 218.191 1.00 17.38 ? 4561 THR A N     1 
ATOM   22932 C  CA    . THR A 1 4561 ? 186.103 291.406 216.837 1.00 17.77 ? 4561 THR A CA    1 
ATOM   22933 C  C     . THR A 1 4561 ? 186.240 290.185 215.936 1.00 13.61 ? 4561 THR A C     1 
ATOM   22934 O  O     . THR A 1 4561 ? 186.509 289.073 216.395 1.00 16.45 ? 4561 THR A O     1 
ATOM   22935 C  CB    . THR A 1 4561 ? 187.402 292.223 216.799 1.00 15.79 ? 4561 THR A CB    1 
ATOM   22936 O  OG1   . THR A 1 4561 ? 188.527 291.341 216.881 1.00 21.03 ? 4561 THR A OG1   1 
ATOM   22937 C  CG2   . THR A 1 4561 ? 187.453 293.202 217.957 1.00 18.49 ? 4561 THR A CG2   1 
ATOM   22938 N  N     . GLY A 1 4562 ? 186.047 290.407 214.637 1.00 13.56 ? 4562 GLY A N     1 
ATOM   22939 C  CA    . GLY A 1 4562 ? 186.227 289.367 213.647 1.00 12.56 ? 4562 GLY A CA    1 
ATOM   22940 C  C     . GLY A 1 4562 ? 184.996 288.559 213.298 1.00 15.16 ? 4562 GLY A C     1 
ATOM   22941 O  O     . GLY A 1 4562 ? 185.092 287.656 212.458 1.00 14.64 ? 4562 GLY A O     1 
ATOM   22942 N  N     . LEU A 1 4563 ? 183.850 288.836 213.915 1.00 17.87 ? 4563 LEU A N     1 
ATOM   22943 C  CA    . LEU A 1 4563 ? 182.621 288.153 213.537 1.00 10.31 ? 4563 LEU A CA    1 
ATOM   22944 C  C     . LEU A 1 4563 ? 182.210 288.551 212.125 1.00 11.61 ? 4563 LEU A C     1 
ATOM   22945 O  O     . LEU A 1 4563 ? 182.238 289.730 211.762 1.00 13.14 ? 4563 LEU A O     1 
ATOM   22946 C  CB    . LEU A 1 4563 ? 181.500 288.480 214.521 1.00 9.35  ? 4563 LEU A CB    1 
ATOM   22947 C  CG    . LEU A 1 4563 ? 181.633 287.962 215.955 1.00 9.62  ? 4563 LEU A CG    1 
ATOM   22948 C  CD1   . LEU A 1 4563 ? 180.345 288.196 216.723 1.00 6.80  ? 4563 LEU A CD1   1 
ATOM   22949 C  CD2   . LEU A 1 4563 ? 182.011 286.492 215.971 1.00 8.59  ? 4563 LEU A CD2   1 
ATOM   22950 N  N     . LYS A 1 4564 ? 181.828 287.559 211.324 1.00 12.53 ? 4564 LYS A N     1 
ATOM   22951 C  CA    . LYS A 1 4564 ? 181.444 287.772 209.934 1.00 9.88  ? 4564 LYS A CA    1 
ATOM   22952 C  C     . LYS A 1 4564 ? 180.004 287.322 209.745 1.00 9.00  ? 4564 LYS A C     1 
ATOM   22953 O  O     . LYS A 1 4564 ? 179.670 286.164 210.018 1.00 10.28 ? 4564 LYS A O     1 
ATOM   22954 C  CB    . LYS A 1 4564 ? 182.374 287.014 208.984 1.00 8.97  ? 4564 LYS A CB    1 
ATOM   22955 C  CG    . LYS A 1 4564 ? 183.812 287.504 208.987 1.00 13.00 ? 4564 LYS A CG    1 
ATOM   22956 C  CD    . LYS A 1 4564 ? 183.908 288.939 208.503 1.00 15.46 ? 4564 LYS A CD    1 
ATOM   22957 C  CE    . LYS A 1 4564 ? 185.353 289.370 208.317 1.00 16.58 ? 4564 LYS A CE    1 
ATOM   22958 N  NZ    . LYS A 1 4564 ? 186.125 289.314 209.588 1.00 20.28 ? 4564 LYS A NZ    1 
ATOM   22959 N  N     . LEU A 1 4565 ? 179.157 288.232 209.274 1.00 7.44  ? 4565 LEU A N     1 
ATOM   22960 C  CA    . LEU A 1 4565 ? 177.751 287.927 209.043 1.00 4.32  ? 4565 LEU A CA    1 
ATOM   22961 C  C     . LEU A 1 4565 ? 177.578 287.362 207.637 1.00 6.65  ? 4565 LEU A C     1 
ATOM   22962 O  O     . LEU A 1 4565 ? 177.969 288.001 206.653 1.00 5.07  ? 4565 LEU A O     1 
ATOM   22963 C  CB    . LEU A 1 4565 ? 176.905 289.182 209.234 1.00 4.27  ? 4565 LEU A CB    1 
ATOM   22964 C  CG    . LEU A 1 4565 ? 175.392 289.054 209.052 1.00 5.89  ? 4565 LEU A CG    1 
ATOM   22965 C  CD1   . LEU A 1 4565 ? 174.828 287.942 209.916 1.00 3.37  ? 4565 LEU A CD1   1 
ATOM   22966 C  CD2   . LEU A 1 4565 ? 174.723 290.374 209.363 1.00 8.24  ? 4565 LEU A CD2   1 
ATOM   22967 N  N     . GLN A 1 4566 ? 176.991 286.173 207.540 1.00 4.90  ? 4566 GLN A N     1 
ATOM   22968 C  CA    . GLN A 1 4566 ? 176.823 285.481 206.268 1.00 6.22  ? 4566 GLN A CA    1 
ATOM   22969 C  C     . GLN A 1 4566 ? 175.383 285.625 205.795 1.00 7.51  ? 4566 GLN A C     1 
ATOM   22970 O  O     . GLN A 1 4566 ? 174.451 285.212 206.494 1.00 8.42  ? 4566 GLN A O     1 
ATOM   22971 C  CB    . GLN A 1 4566 ? 177.195 284.005 206.398 1.00 7.08  ? 4566 GLN A CB    1 
ATOM   22972 C  CG    . GLN A 1 4566 ? 178.482 283.741 207.155 1.00 5.82  ? 4566 GLN A CG    1 
ATOM   22973 C  CD    . GLN A 1 4566 ? 179.709 284.263 206.433 1.00 9.36  ? 4566 GLN A CD    1 
ATOM   22974 O  OE1   . GLN A 1 4566 ? 180.422 285.128 206.942 1.00 8.66  ? 4566 GLN A OE1   1 
ATOM   22975 N  NE2   . GLN A 1 4566 ? 179.969 283.732 205.246 1.00 9.85  ? 4566 GLN A NE2   1 
ATOM   22976 N  N     . GLY A 1 4567 ? 175.204 286.200 204.607 1.00 7.13  ? 4567 GLY A N     1 
ATOM   22977 C  CA    . GLY A 1 4567 ? 173.903 286.300 203.983 1.00 6.22  ? 4567 GLY A CA    1 
ATOM   22978 C  C     . GLY A 1 4567 ? 173.030 287.445 204.450 1.00 6.59  ? 4567 GLY A C     1 
ATOM   22979 O  O     . GLY A 1 4567 ? 171.869 287.522 204.032 1.00 7.97  ? 4567 GLY A O     1 
ATOM   22980 N  N     . ALA A 1 4568 ? 173.543 288.336 205.295 1.00 9.80  ? 4568 ALA A N     1 
ATOM   22981 C  CA    . ALA A 1 4568 ? 172.753 289.453 205.789 1.00 6.66  ? 4568 ALA A CA    1 
ATOM   22982 C  C     . ALA A 1 4568 ? 173.677 290.624 206.085 1.00 5.92  ? 4568 ALA A C     1 
ATOM   22983 O  O     . ALA A 1 4568 ? 174.902 290.492 206.091 1.00 10.06 ? 4568 ALA A O     1 
ATOM   22984 C  CB    . ALA A 1 4568 ? 171.952 289.065 207.036 1.00 7.60  ? 4568 ALA A CB    1 
ATOM   22985 N  N     . THR A 1 4569 ? 173.070 291.784 206.323 1.00 8.69  ? 4569 THR A N     1 
ATOM   22986 C  CA    . THR A 1 4569 ? 173.782 292.975 206.762 1.00 10.98 ? 4569 THR A CA    1 
ATOM   22987 C  C     . THR A 1 4569 ? 173.195 293.456 208.080 1.00 10.28 ? 4569 THR A C     1 
ATOM   22988 O  O     . THR A 1 4569 ? 171.987 293.350 208.308 1.00 14.68 ? 4569 THR A O     1 
ATOM   22989 C  CB    . THR A 1 4569 ? 173.703 294.100 205.723 1.00 11.64 ? 4569 THR A CB    1 
ATOM   22990 O  OG1   . THR A 1 4569 ? 172.343 294.273 205.304 1.00 14.40 ? 4569 THR A OG1   1 
ATOM   22991 C  CG2   . THR A 1 4569 ? 174.568 293.777 204.518 1.00 11.46 ? 4569 THR A CG2   1 
ATOM   22992 N  N     . CYS A 1 4570 ? 174.054 293.983 208.945 1.00 18.10 ? 4570 CYS A N     1 
ATOM   22993 C  CA    . CYS A 1 4570 ? 173.642 294.509 210.240 1.00 17.47 ? 4570 CYS A CA    1 
ATOM   22994 C  C     . CYS A 1 4570 ? 173.698 296.028 210.192 1.00 14.74 ? 4570 CYS A C     1 
ATOM   22995 O  O     . CYS A 1 4570 ? 174.750 296.605 209.900 1.00 20.60 ? 4570 CYS A O     1 
ATOM   22996 C  CB    . CYS A 1 4570 ? 174.530 293.971 211.360 1.00 10.54 ? 4570 CYS A CB    1 
ATOM   22997 S  SG    . CYS A 1 4570 ? 173.924 294.336 213.016 1.00 33.37 ? 4570 CYS A SG    1 
ATOM   22998 N  N     . ASN A 1 4571 ? 172.568 296.670 210.478 1.00 15.13 ? 4571 ASN A N     1 
ATOM   22999 C  CA    . ASN A 1 4571 ? 172.478 298.124 210.515 1.00 16.16 ? 4571 ASN A CA    1 
ATOM   23000 C  C     . ASN A 1 4571 ? 171.644 298.524 211.722 1.00 20.44 ? 4571 ASN A C     1 
ATOM   23001 O  O     . ASN A 1 4571 ? 170.444 298.236 211.771 1.00 18.84 ? 4571 ASN A O     1 
ATOM   23002 C  CB    . ASN A 1 4571 ? 171.866 298.675 209.226 1.00 14.45 ? 4571 ASN A CB    1 
ATOM   23003 C  CG    . ASN A 1 4571 ? 172.914 299.072 208.209 1.00 23.18 ? 4571 ASN A CG    1 
ATOM   23004 O  OD1   . ASN A 1 4571 ? 173.334 300.228 208.150 1.00 30.35 ? 4571 ASN A OD1   1 
ATOM   23005 N  ND2   . ASN A 1 4571 ? 173.347 298.112 207.398 1.00 20.96 ? 4571 ASN A ND2   1 
ATOM   23006 N  N     . ASN A 1 4572 ? 172.282 299.190 212.687 1.00 20.90 ? 4572 ASN A N     1 
ATOM   23007 C  CA    . ASN A 1 4572 ? 171.619 299.641 213.912 1.00 22.47 ? 4572 ASN A CA    1 
ATOM   23008 C  C     . ASN A 1 4572 ? 170.971 298.474 214.654 1.00 22.56 ? 4572 ASN A C     1 
ATOM   23009 O  O     . ASN A 1 4572 ? 169.843 298.574 215.138 1.00 23.75 ? 4572 ASN A O     1 
ATOM   23010 C  CB    . ASN A 1 4572 ? 170.590 300.733 213.614 1.00 21.79 ? 4572 ASN A CB    1 
ATOM   23011 C  CG    . ASN A 1 4572 ? 171.125 301.795 212.683 1.00 24.24 ? 4572 ASN A CG    1 
ATOM   23012 O  OD1   . ASN A 1 4572 ? 172.064 302.515 213.018 1.00 29.48 ? 4572 ASN A OD1   1 
ATOM   23013 N  ND2   . ASN A 1 4572 ? 170.534 301.893 211.497 1.00 27.18 ? 4572 ASN A ND2   1 
ATOM   23014 N  N     . ASN A 1 4573 ? 171.694 297.353 214.729 1.00 19.32 ? 4573 ASN A N     1 
ATOM   23015 C  CA    . ASN A 1 4573 ? 171.229 296.143 215.408 1.00 16.57 ? 4573 ASN A CA    1 
ATOM   23016 C  C     . ASN A 1 4573 ? 169.956 295.588 214.784 1.00 18.73 ? 4573 ASN A C     1 
ATOM   23017 O  O     . ASN A 1 4573 ? 169.138 294.967 215.467 1.00 25.65 ? 4573 ASN A O     1 
ATOM   23018 C  CB    . ASN A 1 4573 ? 171.019 296.388 216.903 1.00 18.33 ? 4573 ASN A CB    1 
ATOM   23019 C  CG    . ASN A 1 4573 ? 172.294 296.736 217.611 1.00 20.58 ? 4573 ASN A CG    1 
ATOM   23020 O  OD1   . ASN A 1 4573 ? 173.214 295.924 217.708 1.00 18.32 ? 4573 ASN A OD1   1 
ATOM   23021 N  ND2   . ASN A 1 4573 ? 172.361 297.952 218.118 1.00 25.21 ? 4573 ASN A ND2   1 
ATOM   23022 N  N     . LYS A 1 4574 ? 169.779 295.799 213.483 1.00 19.08 ? 4574 LYS A N     1 
ATOM   23023 C  CA    . LYS A 1 4574 ? 168.596 295.336 212.767 1.00 14.62 ? 4574 LYS A CA    1 
ATOM   23024 C  C     . LYS A 1 4574 ? 169.049 294.660 211.483 1.00 18.81 ? 4574 LYS A C     1 
ATOM   23025 O  O     . LYS A 1 4574 ? 169.472 295.331 210.538 1.00 19.25 ? 4574 LYS A O     1 
ATOM   23026 C  CB    . LYS A 1 4574 ? 167.638 296.491 212.482 1.00 16.00 ? 4574 LYS A CB    1 
ATOM   23027 C  CG    . LYS A 1 4574 ? 166.981 297.056 213.732 1.00 21.50 ? 4574 LYS A CG    1 
ATOM   23028 C  CD    . LYS A 1 4574 ? 166.094 298.248 213.417 1.00 24.77 ? 4574 LYS A CD    1 
ATOM   23029 C  CE    . LYS A 1 4574 ? 164.845 297.818 212.670 1.00 27.10 ? 4574 LYS A CE    1 
ATOM   23030 N  NZ    . LYS A 1 4574 ? 163.941 297.002 213.523 1.00 26.44 ? 4574 LYS A NZ    1 
ATOM   23031 N  N     . LEU A 1 4575 ? 168.961 293.332 211.454 1.00 21.05 ? 4575 LEU A N     1 
ATOM   23032 C  CA    . LEU A 1 4575 ? 169.415 292.564 210.307 1.00 10.94 ? 4575 LEU A CA    1 
ATOM   23033 C  C     . LEU A 1 4575 ? 168.444 292.693 209.144 1.00 13.84 ? 4575 LEU A C     1 
ATOM   23034 O  O     . LEU A 1 4575 ? 167.225 292.706 209.331 1.00 20.21 ? 4575 LEU A O     1 
ATOM   23035 C  CB    . LEU A 1 4575 ? 169.566 291.088 210.668 1.00 11.97 ? 4575 LEU A CB    1 
ATOM   23036 C  CG    . LEU A 1 4575 ? 170.614 290.682 211.695 1.00 10.15 ? 4575 LEU A CG    1 
ATOM   23037 C  CD1   . LEU A 1 4575 ? 170.674 289.173 211.769 1.00 7.09  ? 4575 LEU A CD1   1 
ATOM   23038 C  CD2   . LEU A 1 4575 ? 171.973 291.272 211.382 1.00 11.18 ? 4575 LEU A CD2   1 
ATOM   23039 N  N     . SER A 1 4576 ? 168.995 292.784 207.939 1.00 15.01 ? 4576 SER A N     1 
ATOM   23040 C  CA    . SER A 1 4576 ? 168.222 292.700 206.711 1.00 14.28 ? 4576 SER A CA    1 
ATOM   23041 C  C     . SER A 1 4576 ? 168.906 291.704 205.790 1.00 10.65 ? 4576 SER A C     1 
ATOM   23042 O  O     . SER A 1 4576 ? 170.131 291.567 205.817 1.00 11.95 ? 4576 SER A O     1 
ATOM   23043 C  CB    . SER A 1 4576 ? 168.094 294.063 206.019 1.00 16.88 ? 4576 SER A CB    1 
ATOM   23044 O  OG    . SER A 1 4576 ? 169.352 294.522 205.558 1.00 26.28 ? 4576 SER A OG    1 
ATOM   23045 N  N     . LEU A 1 4577 ? 168.111 291.000 204.990 1.00 13.11 ? 4577 LEU A N     1 
ATOM   23046 C  CA    . LEU A 1 4577 ? 168.674 290.012 204.081 1.00 8.77  ? 4577 LEU A CA    1 
ATOM   23047 C  C     . LEU A 1 4577 ? 169.530 290.691 203.024 1.00 10.51 ? 4577 LEU A C     1 
ATOM   23048 O  O     . LEU A 1 4577 ? 169.194 291.764 202.516 1.00 15.15 ? 4577 LEU A O     1 
ATOM   23049 C  CB    . LEU A 1 4577 ? 167.560 289.197 203.424 1.00 6.96  ? 4577 LEU A CB    1 
ATOM   23050 C  CG    . LEU A 1 4577 ? 166.952 288.115 204.321 1.00 8.60  ? 4577 LEU A CG    1 
ATOM   23051 C  CD1   . LEU A 1 4577 ? 165.770 287.444 203.646 1.00 11.12 ? 4577 LEU A CD1   1 
ATOM   23052 C  CD2   . LEU A 1 4577 ? 168.004 287.093 204.713 1.00 5.75  ? 4577 LEU A CD2   1 
ATOM   23053 N  N     . SER A 1 4578 ? 170.650 290.056 202.695 1.00 5.78  ? 4578 SER A N     1 
ATOM   23054 C  CA    . SER A 1 4578 ? 171.613 290.596 201.751 1.00 7.11  ? 4578 SER A CA    1 
ATOM   23055 C  C     . SER A 1 4578 ? 171.975 289.535 200.722 1.00 11.32 ? 4578 SER A C     1 
ATOM   23056 O  O     . SER A 1 4578 ? 171.948 288.335 201.009 1.00 14.81 ? 4578 SER A O     1 
ATOM   23057 C  CB    . SER A 1 4578 ? 172.881 291.082 202.465 1.00 13.38 ? 4578 SER A CB    1 
ATOM   23058 O  OG    . SER A 1 4578 ? 173.925 291.344 201.547 1.00 13.95 ? 4578 SER A OG    1 
ATOM   23059 N  N     . ASN A 1 4579 ? 172.314 289.989 199.521 1.00 11.65 ? 4579 ASN A N     1 
ATOM   23060 C  CA    . ASN A 1 4579 ? 172.786 289.104 198.468 1.00 9.22  ? 4579 ASN A CA    1 
ATOM   23061 C  C     . ASN A 1 4579 ? 174.300 288.956 198.462 1.00 9.84  ? 4579 ASN A C     1 
ATOM   23062 O  O     . ASN A 1 4579 ? 174.838 288.279 197.580 1.00 15.15 ? 4579 ASN A O     1 
ATOM   23063 C  CB    . ASN A 1 4579 ? 172.301 289.601 197.102 1.00 11.85 ? 4579 ASN A CB    1 
ATOM   23064 C  CG    . ASN A 1 4579 ? 170.817 289.361 196.894 1.00 19.62 ? 4579 ASN A CG    1 
ATOM   23065 O  OD1   . ASN A 1 4579 ? 170.056 290.292 196.626 1.00 21.00 ? 4579 ASN A OD1   1 
ATOM   23066 N  ND2   . ASN A 1 4579 ? 170.397 288.108 197.021 1.00 13.52 ? 4579 ASN A ND2   1 
ATOM   23067 N  N     . ALA A 1 4580 ? 174.994 289.569 199.416 1.00 11.25 ? 4580 ALA A N     1 
ATOM   23068 C  CA    . ALA A 1 4580 ? 176.431 289.402 199.551 1.00 6.96  ? 4580 ALA A CA    1 
ATOM   23069 C  C     . ALA A 1 4580 ? 176.749 288.159 200.377 1.00 10.00 ? 4580 ALA A C     1 
ATOM   23070 O  O     . ALA A 1 4580 ? 175.900 287.622 201.092 1.00 16.04 ? 4580 ALA A O     1 
ATOM   23071 C  CB    . ALA A 1 4580 ? 177.063 290.638 200.192 1.00 6.75  ? 4580 ALA A CB    1 
ATOM   23072 N  N     . ILE A 1 4581 ? 177.997 287.705 200.275 1.00 11.38 ? 4581 ILE A N     1 
ATOM   23073 C  CA    . ILE A 1 4581 ? 178.393 286.466 200.936 1.00 8.80  ? 4581 ILE A CA    1 
ATOM   23074 C  C     . ILE A 1 4581 ? 178.677 286.707 202.412 1.00 11.19 ? 4581 ILE A C     1 
ATOM   23075 O  O     . ILE A 1 4581 ? 178.012 286.141 203.287 1.00 11.87 ? 4581 ILE A O     1 
ATOM   23076 C  CB    . ILE A 1 4581 ? 179.609 285.846 200.223 1.00 11.75 ? 4581 ILE A CB    1 
ATOM   23077 C  CG1   . ILE A 1 4581 ? 179.277 285.558 198.759 1.00 14.40 ? 4581 ILE A CG1   1 
ATOM   23078 C  CG2   . ILE A 1 4581 ? 180.042 284.570 200.924 1.00 10.63 ? 4581 ILE A CG2   1 
ATOM   23079 C  CD1   . ILE A 1 4581 ? 178.145 284.582 198.572 1.00 10.54 ? 4581 ILE A CD1   1 
ATOM   23080 N  N     . SER A 1 4582 ? 179.662 287.545 202.715 1.00 12.00 ? 4582 SER A N     1 
ATOM   23081 C  CA    . SER A 1 4582 ? 180.063 287.816 204.086 1.00 9.36  ? 4582 SER A CA    1 
ATOM   23082 C  C     . SER A 1 4582 ? 180.082 289.317 204.318 1.00 10.88 ? 4582 SER A C     1 
ATOM   23083 O  O     . SER A 1 4582 ? 180.618 290.069 203.498 1.00 15.86 ? 4582 SER A O     1 
ATOM   23084 C  CB    . SER A 1 4582 ? 181.438 287.220 204.396 1.00 10.70 ? 4582 SER A CB    1 
ATOM   23085 O  OG    . SER A 1 4582 ? 181.418 285.810 204.299 1.00 18.73 ? 4582 SER A OG    1 
ATOM   23086 N  N     . THR A 1 4583 ? 179.493 289.746 205.429 1.00 8.75  ? 4583 THR A N     1 
ATOM   23087 C  CA    . THR A 1 4583 ? 179.521 291.137 205.857 1.00 8.18  ? 4583 THR A CA    1 
ATOM   23088 C  C     . THR A 1 4583 ? 180.274 291.208 207.176 1.00 13.32 ? 4583 THR A C     1 
ATOM   23089 O  O     . THR A 1 4583 ? 179.915 290.522 208.137 1.00 13.72 ? 4583 THR A O     1 
ATOM   23090 C  CB    . THR A 1 4583 ? 178.106 291.699 206.009 1.00 12.15 ? 4583 THR A CB    1 
ATOM   23091 O  OG1   . THR A 1 4583 ? 177.543 291.941 204.713 1.00 24.50 ? 4583 THR A OG1   1 
ATOM   23092 C  CG2   . THR A 1 4583 ? 178.131 293.000 206.793 1.00 10.56 ? 4583 THR A CG2   1 
ATOM   23093 N  N     . ALA A 1 4584 ? 181.313 292.036 207.221 1.00 20.92 ? 4584 ALA A N     1 
ATOM   23094 C  CA    . ALA A 1 4584 ? 182.117 292.154 208.428 1.00 14.98 ? 4584 ALA A CA    1 
ATOM   23095 C  C     . ALA A 1 4584 ? 181.365 292.940 209.495 1.00 17.43 ? 4584 ALA A C     1 
ATOM   23096 O  O     . ALA A 1 4584 ? 180.798 293.999 209.216 1.00 16.93 ? 4584 ALA A O     1 
ATOM   23097 C  CB    . ALA A 1 4584 ? 183.450 292.825 208.114 1.00 17.12 ? 4584 ALA A CB    1 
ATOM   23098 N  N     . LEU A 1 4585 ? 181.353 292.410 210.718 1.00 14.55 ? 4585 LEU A N     1 
ATOM   23099 C  CA    . LEU A 1 4585 ? 180.826 293.135 211.863 1.00 13.78 ? 4585 LEU A CA    1 
ATOM   23100 C  C     . LEU A 1 4585 ? 181.976 293.832 212.565 1.00 17.71 ? 4585 LEU A C     1 
ATOM   23101 O  O     . LEU A 1 4585 ? 182.896 293.150 213.043 1.00 24.08 ? 4585 LEU A O     1 
ATOM   23102 C  CB    . LEU A 1 4585 ? 180.113 292.191 212.825 1.00 13.87 ? 4585 LEU A CB    1 
ATOM   23103 C  CG    . LEU A 1 4585 ? 178.973 291.344 212.256 1.00 11.40 ? 4585 LEU A CG    1 
ATOM   23104 C  CD1   . LEU A 1 4585 ? 178.502 290.329 213.282 1.00 7.42  ? 4585 LEU A CD1   1 
ATOM   23105 C  CD2   . LEU A 1 4585 ? 177.822 292.222 211.806 1.00 12.79 ? 4585 LEU A CD2   1 
ATOM   23106 N  N     . PRO A 1 4586 ? 181.985 295.166 212.636 1.00 19.78 ? 4586 PRO A N     1 
ATOM   23107 C  CA    . PRO A 1 4586 ? 183.155 295.875 213.181 1.00 15.29 ? 4586 PRO A CA    1 
ATOM   23108 C  C     . PRO A 1 4586 ? 183.488 295.480 214.611 1.00 16.19 ? 4586 PRO A C     1 
ATOM   23109 O  O     . PRO A 1 4586 ? 184.598 295.018 214.891 1.00 24.00 ? 4586 PRO A O     1 
ATOM   23110 C  CB    . PRO A 1 4586 ? 182.741 297.349 213.095 1.00 20.11 ? 4586 PRO A CB    1 
ATOM   23111 C  CG    . PRO A 1 4586 ? 181.690 297.388 212.034 1.00 22.44 ? 4586 PRO A CG    1 
ATOM   23112 C  CD    . PRO A 1 4586 ? 180.953 296.092 212.145 1.00 15.93 ? 4586 PRO A CD    1 
ATOM   23113 N  N     . LEU A 1 4587 ? 182.533 295.652 215.518 1.00 19.06 ? 4587 LEU A N     1 
ATOM   23114 C  CA    . LEU A 1 4587 ? 182.738 295.312 216.921 1.00 13.47 ? 4587 LEU A CA    1 
ATOM   23115 C  C     . LEU A 1 4587 ? 181.406 294.888 217.515 1.00 17.18 ? 4587 LEU A C     1 
ATOM   23116 O  O     . LEU A 1 4587 ? 180.457 295.677 217.534 1.00 18.70 ? 4587 LEU A O     1 
ATOM   23117 C  CB    . LEU A 1 4587 ? 183.321 296.493 217.698 1.00 17.94 ? 4587 LEU A CB    1 
ATOM   23118 C  CG    . LEU A 1 4587 ? 183.587 296.251 219.183 1.00 16.23 ? 4587 LEU A CG    1 
ATOM   23119 C  CD1   . LEU A 1 4587 ? 184.911 295.543 219.387 1.00 15.41 ? 4587 LEU A CD1   1 
ATOM   23120 C  CD2   . LEU A 1 4587 ? 183.552 297.565 219.941 1.00 20.78 ? 4587 LEU A CD2   1 
ATOM   23121 N  N     . THR A 1 4588 ? 181.341 293.653 217.997 1.00 16.07 ? 4588 THR A N     1 
ATOM   23122 C  CA    . THR A 1 4588 ? 180.127 293.097 218.577 1.00 17.10 ? 4588 THR A CA    1 
ATOM   23123 C  C     . THR A 1 4588 ? 180.263 293.088 220.094 1.00 18.07 ? 4588 THR A C     1 
ATOM   23124 O  O     . THR A 1 4588 ? 181.209 292.501 220.633 1.00 15.74 ? 4588 THR A O     1 
ATOM   23125 C  CB    . THR A 1 4588 ? 179.874 291.685 218.048 1.00 15.52 ? 4588 THR A CB    1 
ATOM   23126 O  OG1   . THR A 1 4588 ? 179.727 291.726 216.624 1.00 21.06 ? 4588 THR A OG1   1 
ATOM   23127 C  CG2   . THR A 1 4588 ? 178.613 291.104 218.657 1.00 11.40 ? 4588 THR A CG2   1 
ATOM   23128 N  N     . GLN A 1 4589 ? 179.325 293.737 220.779 1.00 14.56 ? 4589 GLN A N     1 
ATOM   23129 C  CA    . GLN A 1 4589 ? 179.308 293.765 222.237 1.00 11.62 ? 4589 GLN A CA    1 
ATOM   23130 C  C     . GLN A 1 4589 ? 178.436 292.621 222.742 1.00 16.51 ? 4589 GLN A C     1 
ATOM   23131 O  O     . GLN A 1 4589 ? 177.227 292.598 222.497 1.00 27.24 ? 4589 GLN A O     1 
ATOM   23132 C  CB    . GLN A 1 4589 ? 178.801 295.105 222.762 1.00 14.39 ? 4589 GLN A CB    1 
ATOM   23133 C  CG    . GLN A 1 4589 ? 179.275 296.321 221.993 1.00 15.55 ? 4589 GLN A CG    1 
ATOM   23134 C  CD    . GLN A 1 4589 ? 179.382 297.544 222.880 1.00 19.79 ? 4589 GLN A CD    1 
ATOM   23135 O  OE1   . GLN A 1 4589 ? 178.943 297.528 224.029 1.00 28.18 ? 4589 GLN A OE1   1 
ATOM   23136 N  NE2   . GLN A 1 4589 ? 179.969 298.611 222.354 1.00 27.98 ? 4589 GLN A NE2   1 
ATOM   23137 N  N     . LEU A 1 4590 ? 179.052 291.679 223.447 1.00 11.66 ? 4590 LEU A N     1 
ATOM   23138 C  CA    . LEU A 1 4590 ? 178.332 290.574 224.067 1.00 11.93 ? 4590 LEU A CA    1 
ATOM   23139 C  C     . LEU A 1 4590 ? 177.993 290.971 225.498 1.00 18.63 ? 4590 LEU A C     1 
ATOM   23140 O  O     . LEU A 1 4590 ? 178.876 291.021 226.361 1.00 25.07 ? 4590 LEU A O     1 
ATOM   23141 C  CB    . LEU A 1 4590 ? 179.163 289.296 224.027 1.00 14.33 ? 4590 LEU A CB    1 
ATOM   23142 C  CG    . LEU A 1 4590 ? 179.635 288.875 222.635 1.00 14.93 ? 4590 LEU A CG    1 
ATOM   23143 C  CD1   . LEU A 1 4590 ? 180.261 287.500 222.688 1.00 16.82 ? 4590 LEU A CD1   1 
ATOM   23144 C  CD2   . LEU A 1 4590 ? 178.483 288.901 221.649 1.00 10.69 ? 4590 LEU A CD2   1 
ATOM   23145 N  N     . ARG A 1 4591 ? 176.720 291.251 225.750 1.00 19.65 ? 4591 ARG A N     1 
ATOM   23146 C  CA    . ARG A 1 4591 ? 176.262 291.737 227.042 1.00 18.99 ? 4591 ARG A CA    1 
ATOM   23147 C  C     . ARG A 1 4591 ? 175.410 290.670 227.714 1.00 21.36 ? 4591 ARG A C     1 
ATOM   23148 O  O     . ARG A 1 4591 ? 174.476 290.139 227.104 1.00 22.17 ? 4591 ARG A O     1 
ATOM   23149 C  CB    . ARG A 1 4591 ? 175.470 293.036 226.886 1.00 17.13 ? 4591 ARG A CB    1 
ATOM   23150 C  CG    . ARG A 1 4591 ? 174.539 293.343 228.039 1.00 20.00 ? 4591 ARG A CG    1 
ATOM   23151 C  CD    . ARG A 1 4591 ? 173.700 294.576 227.753 1.00 23.41 ? 4591 ARG A CD    1 
ATOM   23152 N  NE    . ARG A 1 4591 ? 174.266 295.776 228.354 1.00 28.04 ? 4591 ARG A NE    1 
ATOM   23153 C  CZ    . ARG A 1 4591 ? 174.807 296.773 227.668 1.00 33.32 ? 4591 ARG A CZ    1 
ATOM   23154 N  NH1   . ARG A 1 4591 ? 174.875 296.745 226.347 1.00 23.37 ? 4591 ARG A NH1   1 
ATOM   23155 N  NH2   . ARG A 1 4591 ? 175.292 297.824 228.323 1.00 28.54 ? 4591 ARG A NH2   1 
ATOM   23156 N  N     . TRP A 1 4592 ? 175.733 290.361 228.965 1.00 19.45 ? 4592 TRP A N     1 
ATOM   23157 C  CA    . TRP A 1 4592 ? 174.991 289.388 229.755 1.00 14.44 ? 4592 TRP A CA    1 
ATOM   23158 C  C     . TRP A 1 4592 ? 174.061 290.133 230.705 1.00 20.44 ? 4592 TRP A C     1 
ATOM   23159 O  O     . TRP A 1 4592 ? 174.512 290.975 231.489 1.00 23.02 ? 4592 TRP A O     1 
ATOM   23160 C  CB    . TRP A 1 4592 ? 175.946 288.478 230.526 1.00 17.84 ? 4592 TRP A CB    1 
ATOM   23161 C  CG    . TRP A 1 4592 ? 176.757 287.597 229.634 1.00 18.91 ? 4592 TRP A CG    1 
ATOM   23162 C  CD1   . TRP A 1 4592 ? 178.050 287.788 229.247 1.00 15.19 ? 4592 TRP A CD1   1 
ATOM   23163 C  CD2   . TRP A 1 4592 ? 176.322 286.390 228.997 1.00 18.91 ? 4592 TRP A CD2   1 
ATOM   23164 N  NE1   . TRP A 1 4592 ? 178.450 286.774 228.418 1.00 16.09 ? 4592 TRP A NE1   1 
ATOM   23165 C  CE2   . TRP A 1 4592 ? 177.408 285.901 228.246 1.00 18.66 ? 4592 TRP A CE2   1 
ATOM   23166 C  CE3   . TRP A 1 4592 ? 175.121 285.675 228.992 1.00 18.10 ? 4592 TRP A CE3   1 
ATOM   23167 C  CZ2   . TRP A 1 4592 ? 177.329 284.730 227.497 1.00 13.61 ? 4592 TRP A CZ2   1 
ATOM   23168 C  CZ3   . TRP A 1 4592 ? 175.046 284.513 228.251 1.00 19.08 ? 4592 TRP A CZ3   1 
ATOM   23169 C  CH2   . TRP A 1 4592 ? 176.143 284.052 227.514 1.00 15.01 ? 4592 TRP A CH2   1 
ATOM   23170 N  N     . VAL A 1 4593 ? 172.767 289.824 230.628 1.00 19.16 ? 4593 VAL A N     1 
ATOM   23171 C  CA    . VAL A 1 4593 ? 171.755 290.474 231.446 1.00 20.06 ? 4593 VAL A CA    1 
ATOM   23172 C  C     . VAL A 1 4593 ? 170.911 289.411 232.130 1.00 27.05 ? 4593 VAL A C     1 
ATOM   23173 O  O     . VAL A 1 4593 ? 170.874 288.250 231.718 1.00 25.52 ? 4593 VAL A O     1 
ATOM   23174 C  CB    . VAL A 1 4593 ? 170.850 291.424 230.631 1.00 21.79 ? 4593 VAL A CB    1 
ATOM   23175 C  CG1   . VAL A 1 4593 ? 171.676 292.483 229.932 1.00 19.52 ? 4593 VAL A CG1   1 
ATOM   23176 C  CG2   . VAL A 1 4593 ? 170.022 290.637 229.628 1.00 18.01 ? 4593 VAL A CG2   1 
ATOM   23177 N  N     . LYS A 1 4594 ? 170.227 289.830 233.193 1.00 28.68 ? 4594 LYS A N     1 
ATOM   23178 C  CA    . LYS A 1 4594 ? 169.316 288.936 233.894 1.00 28.06 ? 4594 LYS A CA    1 
ATOM   23179 C  C     . LYS A 1 4594 ? 168.183 288.521 232.964 1.00 27.38 ? 4594 LYS A C     1 
ATOM   23180 O  O     . LYS A 1 4594 ? 167.529 289.368 232.345 1.00 28.24 ? 4594 LYS A O     1 
ATOM   23181 C  CB    . LYS A 1 4594 ? 168.761 289.626 235.139 1.00 30.82 ? 4594 LYS A CB    1 
ATOM   23182 C  CG    . LYS A 1 4594 ? 168.023 288.705 236.096 1.00 30.02 ? 4594 LYS A CG    1 
ATOM   23183 C  CD    . LYS A 1 4594 ? 168.920 287.580 236.582 1.00 26.88 ? 4594 LYS A CD    1 
ATOM   23184 C  CE    . LYS A 1 4594 ? 168.116 286.509 237.301 1.00 34.15 ? 4594 LYS A CE    1 
ATOM   23185 N  NZ    . LYS A 1 4594 ? 167.167 285.823 236.382 1.00 34.24 ? 4594 LYS A NZ    1 
ATOM   23186 N  N     . GLN A 1 4595 ? 167.954 287.215 232.865 1.00 28.57 ? 4595 GLN A N     1 
ATOM   23187 C  CA    . GLN A 1 4595 ? 166.923 286.707 231.970 1.00 28.30 ? 4595 GLN A CA    1 
ATOM   23188 C  C     . GLN A 1 4595 ? 165.538 287.074 232.488 1.00 33.38 ? 4595 GLN A C     1 
ATOM   23189 O  O     . GLN A 1 4595 ? 165.267 287.006 233.690 1.00 37.47 ? 4595 GLN A O     1 
ATOM   23190 C  CB    . GLN A 1 4595 ? 167.048 285.192 231.821 1.00 26.64 ? 4595 GLN A CB    1 
ATOM   23191 C  CG    . GLN A 1 4595 ? 166.181 284.605 230.720 1.00 27.43 ? 4595 GLN A CG    1 
ATOM   23192 C  CD    . GLN A 1 4595 ? 166.357 283.107 230.574 1.00 36.84 ? 4595 GLN A CD    1 
ATOM   23193 O  OE1   . GLN A 1 4595 ? 167.122 282.486 231.312 1.00 38.25 ? 4595 GLN A OE1   1 
ATOM   23194 N  NE2   . GLN A 1 4595 ? 165.647 282.517 229.621 1.00 36.03 ? 4595 GLN A NE2   1 
ATOM   23195 N  N     . THR A 1 4596 ? 164.658 287.470 231.568 1.00 32.45 ? 4596 THR A N     1 
ATOM   23196 C  CA    . THR A 1 4596 ? 163.298 287.868 231.910 1.00 32.69 ? 4596 THR A CA    1 
ATOM   23197 C  C     . THR A 1 4596 ? 162.244 286.994 231.241 1.00 36.05 ? 4596 THR A C     1 
ATOM   23198 O  O     . THR A 1 4596 ? 161.059 287.344 231.281 1.00 39.19 ? 4596 THR A O     1 
ATOM   23199 C  CB    . THR A 1 4596 ? 163.064 289.335 231.539 1.00 33.41 ? 4596 THR A CB    1 
ATOM   23200 O  OG1   . THR A 1 4596 ? 163.220 289.503 230.124 1.00 40.32 ? 4596 THR A OG1   1 
ATOM   23201 C  CG2   . THR A 1 4596 ? 164.054 290.234 232.264 1.00 32.84 ? 4596 THR A CG2   1 
ATOM   23202 N  N     . ASN A 1 4597 ? 162.658 285.900 230.590 1.00 30.67 ? 4597 ASN A N     1 
ATOM   23203 C  CA    . ASN A 1 4597 ? 161.814 284.865 229.988 1.00 34.04 ? 4597 ASN A CA    1 
ATOM   23204 C  C     . ASN A 1 4597 ? 160.515 285.393 229.383 1.00 36.49 ? 4597 ASN A C     1 
ATOM   23205 O  O     . ASN A 1 4597 ? 159.440 284.827 229.608 1.00 37.77 ? 4597 ASN A O     1 
ATOM   23206 C  CB    . ASN A 1 4597 ? 161.542 283.734 231.001 1.00 31.16 ? 4597 ASN A CB    1 
ATOM   23207 C  CG    . ASN A 1 4597 ? 160.747 284.174 232.231 1.00 37.75 ? 4597 ASN A CG    1 
ATOM   23208 O  OD1   . ASN A 1 4597 ? 160.057 285.190 232.232 1.00 34.84 ? 4597 ASN A OD1   1 
ATOM   23209 N  ND2   . ASN A 1 4597 ? 160.852 283.387 233.294 1.00 36.24 ? 4597 ASN A ND2   1 
ATOM   23210 N  N     . THR A 1 4598 ? 160.610 286.460 228.588 1.00 37.81 ? 4598 THR A N     1 
ATOM   23211 C  CA    . THR A 1 4598 ? 159.462 287.041 227.907 1.00 33.88 ? 4598 THR A CA    1 
ATOM   23212 C  C     . THR A 1 4598 ? 159.304 286.520 226.482 1.00 36.87 ? 4598 THR A C     1 
ATOM   23213 O  O     . THR A 1 4598 ? 158.720 287.211 225.640 1.00 38.88 ? 4598 THR A O     1 
ATOM   23214 C  CB    . THR A 1 4598 ? 159.562 288.567 227.899 1.00 36.69 ? 4598 THR A CB    1 
ATOM   23215 O  OG1   . THR A 1 4598 ? 160.875 288.961 227.484 1.00 43.12 ? 4598 THR A OG1   1 
ATOM   23216 C  CG2   . THR A 1 4598 ? 159.278 289.131 229.284 1.00 29.89 ? 4598 THR A CG2   1 
ATOM   23217 N  N     . GLU A 1 4599 ? 159.829 285.324 226.199 1.00 37.50 ? 4599 GLU A N     1 
ATOM   23218 C  CA    . GLU A 1 4599 ? 159.740 284.703 224.879 1.00 31.28 ? 4599 GLU A CA    1 
ATOM   23219 C  C     . GLU A 1 4599 ? 160.385 285.574 223.809 1.00 32.71 ? 4599 GLU A C     1 
ATOM   23220 O  O     . GLU A 1 4599 ? 161.171 286.475 224.120 1.00 37.17 ? 4599 GLU A O     1 
ATOM   23221 C  CB    . GLU A 1 4599 ? 158.283 284.402 224.517 1.00 31.67 ? 4599 GLU A CB    1 
ATOM   23222 C  CG    . GLU A 1 4599 ? 157.561 283.521 225.522 1.00 33.90 ? 4599 GLU A CG    1 
ATOM   23223 C  CD    . GLU A 1 4599 ? 156.102 283.312 225.167 1.00 36.90 ? 4599 GLU A CD    1 
ATOM   23224 O  OE1   . GLU A 1 4599 ? 155.825 282.763 224.081 1.00 32.49 ? 4599 GLU A OE1   1 
ATOM   23225 O  OE2   . GLU A 1 4599 ? 155.232 283.698 225.975 1.00 39.54 ? 4599 GLU A OE2   1 
ATOM   23226 N  N     . LYS A 1 4600 ? 160.064 285.308 222.545 1.00 31.13 ? 4600 LYS A N     1 
ATOM   23227 C  CA    . LYS A 1 4600 ? 160.610 286.079 221.436 1.00 31.55 ? 4600 LYS A CA    1 
ATOM   23228 C  C     . LYS A 1 4600 ? 159.780 287.346 221.240 1.00 33.64 ? 4600 LYS A C     1 
ATOM   23229 O  O     . LYS A 1 4600 ? 158.924 287.694 222.060 1.00 35.78 ? 4600 LYS A O     1 
ATOM   23230 C  CB    . LYS A 1 4600 ? 160.666 285.219 220.176 1.00 32.07 ? 4600 LYS A CB    1 
ATOM   23231 C  CG    . LYS A 1 4600 ? 161.584 284.011 220.293 1.00 36.70 ? 4600 LYS A CG    1 
ATOM   23232 C  CD    . LYS A 1 4600 ? 162.987 284.422 220.715 1.00 34.49 ? 4600 LYS A CD    1 
ATOM   23233 C  CE    . LYS A 1 4600 ? 163.904 283.216 220.833 1.00 33.84 ? 4600 LYS A CE    1 
ATOM   23234 N  NZ    . LYS A 1 4600 ? 165.303 283.606 221.167 1.00 35.92 ? 4600 LYS A NZ    1 
ATOM   23235 N  N     . LYS A 1 4601 ? 160.025 288.059 220.139 1.00 32.22 ? 4601 LYS A N     1 
ATOM   23236 C  CA    . LYS A 1 4601 ? 159.342 289.317 219.867 1.00 34.14 ? 4601 LYS A CA    1 
ATOM   23237 C  C     . LYS A 1 4601 ? 158.685 289.335 218.489 1.00 34.65 ? 4601 LYS A C     1 
ATOM   23238 O  O     . LYS A 1 4601 ? 158.326 290.413 218.002 1.00 32.18 ? 4601 LYS A O     1 
ATOM   23239 C  CB    . LYS A 1 4601 ? 160.321 290.491 219.999 1.00 31.59 ? 4601 LYS A CB    1 
ATOM   23240 C  CG    . LYS A 1 4601 ? 159.676 291.829 220.338 1.00 29.57 ? 4601 LYS A CG    1 
ATOM   23241 C  CD    . LYS A 1 4601 ? 160.689 292.960 220.279 1.00 37.25 ? 4601 LYS A CD    1 
ATOM   23242 C  CE    . LYS A 1 4601 ? 161.889 292.675 221.167 1.00 34.73 ? 4601 LYS A CE    1 
ATOM   23243 N  NZ    . LYS A 1 4601 ? 162.878 293.788 221.138 1.00 31.96 ? 4601 LYS A NZ    1 
ATOM   23244 N  N     . ALA A 1 4602 ? 158.533 288.176 217.846 1.00 31.54 ? 4602 ALA A N     1 
ATOM   23245 C  CA    . ALA A 1 4602 ? 157.948 287.998 216.519 1.00 25.43 ? 4602 ALA A CA    1 
ATOM   23246 C  C     . ALA A 1 4602 ? 158.780 288.648 215.421 1.00 31.00 ? 4602 ALA A C     1 
ATOM   23247 O  O     . ALA A 1 4602 ? 158.404 288.564 214.245 1.00 29.28 ? 4602 ALA A O     1 
ATOM   23248 C  CB    . ALA A 1 4602 ? 156.506 288.522 216.432 1.00 26.55 ? 4602 ALA A CB    1 
ATOM   23249 N  N     . SER A 1 4603 ? 159.894 289.294 215.761 1.00 26.59 ? 4603 SER A N     1 
ATOM   23250 C  CA    . SER A 1 4603 ? 160.820 289.855 214.786 1.00 18.98 ? 4603 SER A CA    1 
ATOM   23251 C  C     . SER A 1 4603 ? 162.263 289.544 215.160 1.00 20.19 ? 4603 SER A C     1 
ATOM   23252 O  O     . SER A 1 4603 ? 163.169 290.305 214.807 1.00 25.99 ? 4603 SER A O     1 
ATOM   23253 C  CB    . SER A 1 4603 ? 160.620 291.366 214.651 1.00 22.81 ? 4603 SER A CB    1 
ATOM   23254 O  OG    . SER A 1 4603 ? 160.539 291.983 215.924 1.00 27.68 ? 4603 SER A OG    1 
ATOM   23255 N  N     . VAL A 1 4604 ? 162.493 288.444 215.871 1.00 18.35 ? 4604 VAL A N     1 
ATOM   23256 C  CA    . VAL A 1 4604 ? 163.809 288.079 216.379 1.00 17.93 ? 4604 VAL A CA    1 
ATOM   23257 C  C     . VAL A 1 4604 ? 164.205 286.741 215.775 1.00 17.02 ? 4604 VAL A C     1 
ATOM   23258 O  O     . VAL A 1 4604 ? 163.416 285.791 215.788 1.00 17.67 ? 4604 VAL A O     1 
ATOM   23259 C  CB    . VAL A 1 4604 ? 163.821 288.011 217.918 1.00 16.90 ? 4604 VAL A CB    1 
ATOM   23260 C  CG1   . VAL A 1 4604 ? 165.089 287.329 218.416 1.00 13.76 ? 4604 VAL A CG1   1 
ATOM   23261 C  CG2   . VAL A 1 4604 ? 163.694 289.403 218.505 1.00 18.14 ? 4604 VAL A CG2   1 
ATOM   23262 N  N     . VAL A 1 4605 ? 165.421 286.675 215.238 1.00 12.51 ? 4605 VAL A N     1 
ATOM   23263 C  CA    . VAL A 1 4605 ? 165.986 285.443 214.703 1.00 9.39  ? 4605 VAL A CA    1 
ATOM   23264 C  C     . VAL A 1 4605 ? 167.190 285.062 215.550 1.00 9.59  ? 4605 VAL A C     1 
ATOM   23265 O  O     . VAL A 1 4605 ? 167.994 285.923 215.925 1.00 9.06  ? 4605 VAL A O     1 
ATOM   23266 C  CB    . VAL A 1 4605 ? 166.370 285.580 213.216 1.00 8.62  ? 4605 VAL A CB    1 
ATOM   23267 C  CG1   . VAL A 1 4605 ? 165.147 285.877 212.385 1.00 11.67 ? 4605 VAL A CG1   1 
ATOM   23268 C  CG2   . VAL A 1 4605 ? 167.417 286.668 213.009 1.00 14.72 ? 4605 VAL A CG2   1 
ATOM   23269 N  N     . THR A 1 4606 ? 167.290 283.779 215.885 1.00 13.08 ? 4606 THR A N     1 
ATOM   23270 C  CA    . THR A 1 4606 ? 168.461 283.248 216.565 1.00 6.77  ? 4606 THR A CA    1 
ATOM   23271 C  C     . THR A 1 4606 ? 169.435 282.731 215.515 1.00 6.76  ? 4606 THR A C     1 
ATOM   23272 O  O     . THR A 1 4606 ? 169.116 281.799 214.770 1.00 10.65 ? 4606 THR A O     1 
ATOM   23273 C  CB    . THR A 1 4606 ? 168.078 282.137 217.544 1.00 9.27  ? 4606 THR A CB    1 
ATOM   23274 O  OG1   . THR A 1 4606 ? 167.227 282.671 218.564 1.00 16.76 ? 4606 THR A OG1   1 
ATOM   23275 C  CG2   . THR A 1 4606 ? 169.319 281.550 218.188 1.00 7.71  ? 4606 THR A CG2   1 
ATOM   23276 N  N     . LEU A 1 4607 ? 170.610 283.341 215.449 1.00 9.22  ? 4607 LEU A N     1 
ATOM   23277 C  CA    . LEU A 1 4607 ? 171.590 282.991 214.441 1.00 7.03  ? 4607 LEU A CA    1 
ATOM   23278 C  C     . LEU A 1 4607 ? 172.681 282.127 215.042 1.00 4.26  ? 4607 LEU A C     1 
ATOM   23279 O  O     . LEU A 1 4607 ? 173.264 282.501 216.068 1.00 6.16  ? 4607 LEU A O     1 
ATOM   23280 C  CB    . LEU A 1 4607 ? 172.210 284.248 213.828 1.00 4.25  ? 4607 LEU A CB    1 
ATOM   23281 C  CG    . LEU A 1 4607 ? 171.334 285.065 212.880 1.00 6.41  ? 4607 LEU A CG    1 
ATOM   23282 C  CD1   . LEU A 1 4607 ? 172.202 286.014 212.081 1.00 4.95  ? 4607 LEU A CD1   1 
ATOM   23283 C  CD2   . LEU A 1 4607 ? 170.522 284.164 211.964 1.00 6.08  ? 4607 LEU A CD2   1 
ATOM   23284 N  N     . PRO A 1 4608 ? 172.975 280.972 214.456 1.00 4.59  ? 4608 PRO A N     1 
ATOM   23285 C  CA    . PRO A 1 4608 ? 174.146 280.211 214.896 1.00 6.39  ? 4608 PRO A CA    1 
ATOM   23286 C  C     . PRO A 1 4608 ? 175.423 280.979 214.605 1.00 6.97  ? 4608 PRO A C     1 
ATOM   23287 O  O     . PRO A 1 4608 ? 175.525 281.693 213.604 1.00 7.08  ? 4608 PRO A O     1 
ATOM   23288 C  CB    . PRO A 1 4608 ? 174.063 278.924 214.072 1.00 3.87  ? 4608 PRO A CB    1 
ATOM   23289 C  CG    . PRO A 1 4608 ? 173.316 279.317 212.848 1.00 2.92  ? 4608 PRO A CG    1 
ATOM   23290 C  CD    . PRO A 1 4608 ? 172.339 280.376 213.268 1.00 4.59  ? 4608 PRO A CD    1 
ATOM   23291 N  N     . VAL A 1 4609 ? 176.398 280.836 215.494 1.00 3.29  ? 4609 VAL A N     1 
ATOM   23292 C  CA    . VAL A 1 4609 ? 177.728 281.399 215.305 1.00 4.56  ? 4609 VAL A CA    1 
ATOM   23293 C  C     . VAL A 1 4609 ? 178.696 280.232 215.190 1.00 5.39  ? 4609 VAL A C     1 
ATOM   23294 O  O     . VAL A 1 4609 ? 179.006 279.574 216.191 1.00 8.17  ? 4609 VAL A O     1 
ATOM   23295 C  CB    . VAL A 1 4609 ? 178.132 282.345 216.442 1.00 5.29  ? 4609 VAL A CB    1 
ATOM   23296 C  CG1   . VAL A 1 4609 ? 179.483 282.971 216.147 1.00 3.95  ? 4609 VAL A CG1   1 
ATOM   23297 C  CG2   . VAL A 1 4609 ? 177.083 283.419 216.626 1.00 4.96  ? 4609 VAL A CG2   1 
ATOM   23298 N  N     . TYR A 1 4610 ? 179.169 279.973 213.979 1.00 6.69  ? 4610 TYR A N     1 
ATOM   23299 C  CA    . TYR A 1 4610 ? 180.110 278.894 213.741 1.00 5.04  ? 4610 TYR A CA    1 
ATOM   23300 C  C     . TYR A 1 4610 ? 181.539 279.420 213.761 1.00 7.45  ? 4610 TYR A C     1 
ATOM   23301 O  O     . TYR A 1 4610 ? 181.790 280.619 213.625 1.00 14.69 ? 4610 TYR A O     1 
ATOM   23302 C  CB    . TYR A 1 4610 ? 179.818 278.204 212.407 1.00 4.84  ? 4610 TYR A CB    1 
ATOM   23303 C  CG    . TYR A 1 4610 ? 178.464 277.542 212.351 1.00 3.57  ? 4610 TYR A CG    1 
ATOM   23304 C  CD1   . TYR A 1 4610 ? 178.239 276.332 212.991 1.00 6.04  ? 4610 TYR A CD1   1 
ATOM   23305 C  CD2   . TYR A 1 4610 ? 177.412 278.124 211.660 1.00 3.53  ? 4610 TYR A CD2   1 
ATOM   23306 C  CE1   . TYR A 1 4610 ? 177.004 275.721 212.942 1.00 4.82  ? 4610 TYR A CE1   1 
ATOM   23307 C  CE2   . TYR A 1 4610 ? 176.174 277.520 211.605 1.00 3.67  ? 4610 TYR A CE2   1 
ATOM   23308 C  CZ    . TYR A 1 4610 ? 175.976 276.319 212.250 1.00 4.39  ? 4610 TYR A CZ    1 
ATOM   23309 O  OH    . TYR A 1 4610 ? 174.744 275.712 212.201 1.00 7.07  ? 4610 TYR A OH    1 
ATOM   23310 N  N     . LEU A 1 4611 ? 182.482 278.497 213.944 1.00 7.82  ? 4611 LEU A N     1 
ATOM   23311 C  CA    . LEU A 1 4611 ? 183.883 278.889 214.039 1.00 9.32  ? 4611 LEU A CA    1 
ATOM   23312 C  C     . LEU A 1 4611 ? 184.427 279.348 212.692 1.00 11.20 ? 4611 LEU A C     1 
ATOM   23313 O  O     . LEU A 1 4611 ? 185.084 280.391 212.600 1.00 19.29 ? 4611 LEU A O     1 
ATOM   23314 C  CB    . LEU A 1 4611 ? 184.711 277.734 214.592 1.00 7.70  ? 4611 LEU A CB    1 
ATOM   23315 C  CG    . LEU A 1 4611 ? 186.202 278.028 214.725 1.00 13.19 ? 4611 LEU A CG    1 
ATOM   23316 C  CD1   . LEU A 1 4611 ? 186.442 279.192 215.672 1.00 14.37 ? 4611 LEU A CD1   1 
ATOM   23317 C  CD2   . LEU A 1 4611 ? 186.923 276.795 215.201 1.00 11.60 ? 4611 LEU A CD2   1 
ATOM   23318 N  N     . ASN A 1 4612 ? 184.162 278.588 211.632 1.00 11.19 ? 4612 ASN A N     1 
ATOM   23319 C  CA    . ASN A 1 4612 ? 184.674 278.915 210.307 1.00 9.27  ? 4612 ASN A CA    1 
ATOM   23320 C  C     . ASN A 1 4612 ? 183.610 278.572 209.270 1.00 8.97  ? 4612 ASN A C     1 
ATOM   23321 O  O     . ASN A 1 4612 ? 182.486 278.185 209.604 1.00 9.84  ? 4612 ASN A O     1 
ATOM   23322 C  CB    . ASN A 1 4612 ? 186.004 278.196 210.044 1.00 7.81  ? 4612 ASN A CB    1 
ATOM   23323 C  CG    . ASN A 1 4612 ? 185.938 276.716 210.335 1.00 9.00  ? 4612 ASN A CG    1 
ATOM   23324 O  OD1   . ASN A 1 4612 ? 185.270 275.965 209.630 1.00 12.39 ? 4612 ASN A OD1   1 
ATOM   23325 N  ND2   . ASN A 1 4612 ? 186.634 276.288 211.378 1.00 13.45 ? 4612 ASN A ND2   1 
ATOM   23326 N  N     . PHE A 1 4613 ? 183.982 278.715 207.996 1.00 8.93  ? 4613 PHE A N     1 
ATOM   23327 C  CA    . PHE A 1 4613 ? 183.039 278.571 206.892 1.00 4.57  ? 4613 PHE A CA    1 
ATOM   23328 C  C     . PHE A 1 4613 ? 182.481 277.159 206.769 1.00 5.90  ? 4613 PHE A C     1 
ATOM   23329 O  O     . PHE A 1 4613 ? 181.410 276.986 206.181 1.00 10.61 ? 4613 PHE A O     1 
ATOM   23330 C  CB    . PHE A 1 4613 ? 183.712 278.983 205.582 1.00 6.63  ? 4613 PHE A CB    1 
ATOM   23331 C  CG    . PHE A 1 4613 ? 184.814 278.060 205.146 1.00 6.79  ? 4613 PHE A CG    1 
ATOM   23332 C  CD1   . PHE A 1 4613 ? 184.551 276.980 204.319 1.00 8.41  ? 4613 PHE A CD1   1 
ATOM   23333 C  CD2   . PHE A 1 4613 ? 186.114 278.262 205.579 1.00 10.36 ? 4613 PHE A CD2   1 
ATOM   23334 C  CE1   . PHE A 1 4613 ? 185.560 276.127 203.927 1.00 11.88 ? 4613 PHE A CE1   1 
ATOM   23335 C  CE2   . PHE A 1 4613 ? 187.129 277.411 205.188 1.00 14.86 ? 4613 PHE A CE2   1 
ATOM   23336 C  CZ    . PHE A 1 4613 ? 186.851 276.343 204.362 1.00 19.45 ? 4613 PHE A CZ    1 
ATOM   23337 N  N     . THR A 1 4614 ? 183.177 276.151 207.295 1.00 7.49  ? 4614 THR A N     1 
ATOM   23338 C  CA    . THR A 1 4614 ? 182.679 274.783 207.198 1.00 7.76  ? 4614 THR A CA    1 
ATOM   23339 C  C     . THR A 1 4614 ? 181.434 274.556 208.047 1.00 8.68  ? 4614 THR A C     1 
ATOM   23340 O  O     . THR A 1 4614 ? 180.700 273.595 207.795 1.00 15.91 ? 4614 THR A O     1 
ATOM   23341 C  CB    . THR A 1 4614 ? 183.769 273.788 207.600 1.00 6.86  ? 4614 THR A CB    1 
ATOM   23342 O  OG1   . THR A 1 4614 ? 183.938 273.802 209.022 1.00 12.78 ? 4614 THR A OG1   1 
ATOM   23343 C  CG2   . THR A 1 4614 ? 185.084 274.140 206.929 1.00 7.31  ? 4614 THR A CG2   1 
ATOM   23344 N  N     . ARG A 1 4615 ? 181.192 275.410 209.044 1.00 6.47  ? 4615 ARG A N     1 
ATOM   23345 C  CA    . ARG A 1 4615 ? 180.019 275.326 209.916 1.00 5.65  ? 4615 ARG A CA    1 
ATOM   23346 C  C     . ARG A 1 4615 ? 179.939 273.985 210.637 1.00 5.06  ? 4615 ARG A C     1 
ATOM   23347 O  O     . ARG A 1 4615 ? 178.852 273.515 210.980 1.00 11.06 ? 4615 ARG A O     1 
ATOM   23348 C  CB    . ARG A 1 4615 ? 178.725 275.592 209.140 1.00 4.70  ? 4615 ARG A CB    1 
ATOM   23349 C  CG    . ARG A 1 4615 ? 178.674 276.966 208.501 1.00 3.04  ? 4615 ARG A CG    1 
ATOM   23350 C  CD    . ARG A 1 4615 ? 177.287 277.309 207.994 1.00 3.67  ? 4615 ARG A CD    1 
ATOM   23351 N  NE    . ARG A 1 4615 ? 177.286 278.593 207.305 1.00 6.51  ? 4615 ARG A NE    1 
ATOM   23352 C  CZ    . ARG A 1 4615 ? 176.201 279.206 206.852 1.00 2.20  ? 4615 ARG A CZ    1 
ATOM   23353 N  NH1   . ARG A 1 4615 ? 174.996 278.689 207.017 1.00 2.18  ? 4615 ARG A NH1   1 
ATOM   23354 N  NH2   . ARG A 1 4615 ? 176.330 280.371 206.227 1.00 2.41  ? 4615 ARG A NH2   1 
ATOM   23355 N  N     . ALA A 1 4616 ? 181.088 273.358 210.876 1.00 6.95  ? 4616 ALA A N     1 
ATOM   23356 C  CA    . ALA A 1 4616 ? 181.134 272.074 211.556 1.00 5.92  ? 4616 ALA A CA    1 
ATOM   23357 C  C     . ALA A 1 4616 ? 181.161 272.199 213.072 1.00 8.80  ? 4616 ALA A C     1 
ATOM   23358 O  O     . ALA A 1 4616 ? 180.977 271.191 213.762 1.00 17.80 ? 4616 ALA A O     1 
ATOM   23359 C  CB    . ALA A 1 4616 ? 182.356 271.276 211.092 1.00 6.21  ? 4616 ALA A CB    1 
ATOM   23360 N  N     . ASP A 1 4617 ? 181.378 273.398 213.605 1.00 11.57 ? 4617 ASP A N     1 
ATOM   23361 C  CA    . ASP A 1 4617 ? 181.538 273.596 215.045 1.00 14.13 ? 4617 ASP A CA    1 
ATOM   23362 C  C     . ASP A 1 4617 ? 180.737 274.820 215.464 1.00 9.23  ? 4617 ASP A C     1 
ATOM   23363 O  O     . ASP A 1 4617 ? 181.048 275.939 215.047 1.00 10.43 ? 4617 ASP A O     1 
ATOM   23364 C  CB    . ASP A 1 4617 ? 183.012 273.758 215.415 1.00 10.27 ? 4617 ASP A CB    1 
ATOM   23365 C  CG    . ASP A 1 4617 ? 183.865 272.602 214.933 1.00 20.40 ? 4617 ASP A CG    1 
ATOM   23366 O  OD1   . ASP A 1 4617 ? 184.629 272.790 213.965 1.00 19.30 ? 4617 ASP A OD1   1 
ATOM   23367 O  OD2   . ASP A 1 4617 ? 183.767 271.506 215.522 1.00 24.06 ? 4617 ASP A OD2   1 
ATOM   23368 N  N     . LEU A 1 4618 ? 179.719 274.608 216.291 1.00 9.04  ? 4618 LEU A N     1 
ATOM   23369 C  CA    . LEU A 1 4618 ? 178.940 275.712 216.835 1.00 8.23  ? 4618 LEU A CA    1 
ATOM   23370 C  C     . LEU A 1 4618 ? 179.634 276.276 218.067 1.00 9.92  ? 4618 LEU A C     1 
ATOM   23371 O  O     . LEU A 1 4618 ? 180.072 275.524 218.942 1.00 17.40 ? 4618 LEU A O     1 
ATOM   23372 C  CB    . LEU A 1 4618 ? 177.528 275.248 217.185 1.00 8.25  ? 4618 LEU A CB    1 
ATOM   23373 C  CG    . LEU A 1 4618 ? 176.581 276.342 217.679 1.00 10.31 ? 4618 LEU A CG    1 
ATOM   23374 C  CD1   . LEU A 1 4618 ? 176.239 277.302 216.551 1.00 7.67  ? 4618 LEU A CD1   1 
ATOM   23375 C  CD2   . LEU A 1 4618 ? 175.324 275.740 218.281 1.00 8.65  ? 4618 LEU A CD2   1 
ATOM   23376 N  N     . ILE A 1 4619 ? 179.738 277.601 218.131 1.00 5.06  ? 4619 ILE A N     1 
ATOM   23377 C  CA    . ILE A 1 4619 ? 180.373 278.270 219.260 1.00 10.03 ? 4619 ILE A CA    1 
ATOM   23378 C  C     . ILE A 1 4619 ? 179.299 278.722 220.242 1.00 8.79  ? 4619 ILE A C     1 
ATOM   23379 O  O     . ILE A 1 4619 ? 179.295 278.311 221.407 1.00 10.18 ? 4619 ILE A O     1 
ATOM   23380 C  CB    . ILE A 1 4619 ? 181.234 279.458 218.797 1.00 10.71 ? 4619 ILE A CB    1 
ATOM   23381 C  CG1   . ILE A 1 4619 ? 182.202 279.023 217.695 1.00 13.17 ? 4619 ILE A CG1   1 
ATOM   23382 C  CG2   . ILE A 1 4619 ? 181.997 280.050 219.969 1.00 7.71  ? 4619 ILE A CG2   1 
ATOM   23383 C  CD1   . ILE A 1 4619 ? 183.061 277.836 218.068 1.00 10.83 ? 4619 ILE A CD1   1 
ATOM   23384 N  N     . PHE A 1 4620 ? 178.386 279.569 219.777 1.00 5.65  ? 4620 PHE A N     1 
ATOM   23385 C  CA    . PHE A 1 4620 ? 177.285 280.055 220.598 1.00 5.56  ? 4620 PHE A CA    1 
ATOM   23386 C  C     . PHE A 1 4620 ? 176.198 280.582 219.671 1.00 8.29  ? 4620 PHE A C     1 
ATOM   23387 O  O     . PHE A 1 4620 ? 176.283 280.458 218.447 1.00 9.00  ? 4620 PHE A O     1 
ATOM   23388 C  CB    . PHE A 1 4620 ? 177.761 281.114 221.600 1.00 6.10  ? 4620 PHE A CB    1 
ATOM   23389 C  CG    . PHE A 1 4620 ? 178.236 282.394 220.971 1.00 5.75  ? 4620 PHE A CG    1 
ATOM   23390 C  CD1   . PHE A 1 4620 ? 179.457 282.456 220.321 1.00 8.75  ? 4620 PHE A CD1   1 
ATOM   23391 C  CD2   . PHE A 1 4620 ? 177.477 283.547 221.060 1.00 5.93  ? 4620 PHE A CD2   1 
ATOM   23392 C  CE1   . PHE A 1 4620 ? 179.900 283.633 219.753 1.00 5.65  ? 4620 PHE A CE1   1 
ATOM   23393 C  CE2   . PHE A 1 4620 ? 177.919 284.729 220.499 1.00 6.25  ? 4620 PHE A CE2   1 
ATOM   23394 C  CZ    . PHE A 1 4620 ? 179.130 284.772 219.842 1.00 7.27  ? 4620 PHE A CZ    1 
ATOM   23395 N  N     . THR A 1 4621 ? 175.161 281.160 220.267 1.00 8.00  ? 4621 THR A N     1 
ATOM   23396 C  CA    . THR A 1 4621 ? 174.012 281.662 219.530 1.00 6.28  ? 4621 THR A CA    1 
ATOM   23397 C  C     . THR A 1 4621 ? 173.796 283.132 219.853 1.00 11.07 ? 4621 THR A C     1 
ATOM   23398 O  O     . THR A 1 4621 ? 173.984 283.564 220.994 1.00 12.46 ? 4621 THR A O     1 
ATOM   23399 C  CB    . THR A 1 4621 ? 172.741 280.872 219.869 1.00 10.78 ? 4621 THR A CB    1 
ATOM   23400 O  OG1   . THR A 1 4621 ? 172.442 281.019 221.262 1.00 12.85 ? 4621 THR A OG1   1 
ATOM   23401 C  CG2   . THR A 1 4621 ? 172.935 279.399 219.559 1.00 9.14  ? 4621 THR A CG2   1 
ATOM   23402 N  N     . VAL A 1 4622 ? 173.401 283.895 218.841 1.00 8.43  ? 4622 VAL A N     1 
ATOM   23403 C  CA    . VAL A 1 4622 ? 173.076 285.305 218.997 1.00 8.71  ? 4622 VAL A CA    1 
ATOM   23404 C  C     . VAL A 1 4622 ? 171.626 285.522 218.598 1.00 10.39 ? 4622 VAL A C     1 
ATOM   23405 O  O     . VAL A 1 4622 ? 171.059 284.781 217.789 1.00 12.41 ? 4622 VAL A O     1 
ATOM   23406 C  CB    . VAL A 1 4622 ? 174.011 286.211 218.168 1.00 10.82 ? 4622 VAL A CB    1 
ATOM   23407 C  CG1   . VAL A 1 4622 ? 175.447 285.950 218.526 1.00 11.19 ? 4622 VAL A CG1   1 
ATOM   23408 C  CG2   . VAL A 1 4622 ? 173.804 285.957 216.688 1.00 8.56  ? 4622 VAL A CG2   1 
ATOM   23409 N  N     . ASP A 1 4623 ? 171.022 286.552 219.185 1.00 12.39 ? 4623 ASP A N     1 
ATOM   23410 C  CA    . ASP A 1 4623 ? 169.662 286.960 218.866 1.00 12.00 ? 4623 ASP A CA    1 
ATOM   23411 C  C     . ASP A 1 4623 ? 169.712 288.351 218.257 1.00 9.89  ? 4623 ASP A C     1 
ATOM   23412 O  O     . ASP A 1 4623 ? 170.293 289.270 218.846 1.00 13.09 ? 4623 ASP A O     1 
ATOM   23413 C  CB    . ASP A 1 4623 ? 168.771 286.948 220.109 1.00 10.73 ? 4623 ASP A CB    1 
ATOM   23414 C  CG    . ASP A 1 4623 ? 168.507 285.554 220.622 1.00 18.88 ? 4623 ASP A CG    1 
ATOM   23415 O  OD1   . ASP A 1 4623 ? 168.503 284.610 219.805 1.00 23.12 ? 4623 ASP A OD1   1 
ATOM   23416 O  OD2   . ASP A 1 4623 ? 168.300 285.396 221.845 1.00 30.85 ? 4623 ASP A OD2   1 
ATOM   23417 N  N     . PHE A 1 4624 ? 169.116 288.501 217.082 1.00 11.18 ? 4624 PHE A N     1 
ATOM   23418 C  CA    . PHE A 1 4624 ? 169.012 289.784 216.412 1.00 10.18 ? 4624 PHE A CA    1 
ATOM   23419 C  C     . PHE A 1 4624 ? 167.554 290.089 216.113 1.00 12.82 ? 4624 PHE A C     1 
ATOM   23420 O  O     . PHE A 1 4624 ? 166.719 289.192 216.001 1.00 16.82 ? 4624 PHE A O     1 
ATOM   23421 C  CB    . PHE A 1 4624 ? 169.808 289.809 215.105 1.00 8.49  ? 4624 PHE A CB    1 
ATOM   23422 C  CG    . PHE A 1 4624 ? 171.282 289.988 215.289 1.00 7.40  ? 4624 PHE A CG    1 
ATOM   23423 C  CD1   . PHE A 1 4624 ? 171.818 291.250 215.475 1.00 10.16 ? 4624 PHE A CD1   1 
ATOM   23424 C  CD2   . PHE A 1 4624 ? 172.138 288.903 215.244 1.00 8.89  ? 4624 PHE A CD2   1 
ATOM   23425 C  CE1   . PHE A 1 4624 ? 173.178 291.423 215.632 1.00 14.90 ? 4624 PHE A CE1   1 
ATOM   23426 C  CE2   . PHE A 1 4624 ? 173.499 289.074 215.399 1.00 10.90 ? 4624 PHE A CE2   1 
ATOM   23427 C  CZ    . PHE A 1 4624 ? 174.018 290.333 215.594 1.00 12.80 ? 4624 PHE A CZ    1 
ATOM   23428 N  N     . GLU A 1 4625 ? 167.254 291.380 215.956 1.00 12.06 ? 4625 GLU A N     1 
ATOM   23429 C  CA    . GLU A 1 4625 ? 165.878 291.775 215.559 1.00 14.26 ? 4625 GLU A CA    1 
ATOM   23430 C  C     . GLU A 1 4625 ? 165.889 292.061 214.050 1.00 17.02 ? 4625 GLU A C     1 
ATOM   23431 O  O     . GLU A 1 4625 ? 166.738 292.864 213.607 1.00 20.05 ? 4625 GLU A O     1 
ATOM   23432 C  CB    . GLU A 1 4625 ? 165.405 293.008 216.324 1.00 14.96 ? 4625 GLU A CB    1 
ATOM   23433 C  CG    . GLU A 1 4625 ? 164.080 293.555 215.805 1.00 17.06 ? 4625 GLU A CG    1 
ATOM   23434 C  CD    . GLU A 1 4625 ? 163.741 294.947 216.306 1.00 28.49 ? 4625 GLU A CD    1 
ATOM   23435 O  OE1   . GLU A 1 4625 ? 164.545 295.506 217.082 1.00 32.56 ? 4625 GLU A OE1   1 
ATOM   23436 O  OE2   . GLU A 1 4625 ? 162.677 295.471 215.921 1.00 28.61 ? 4625 GLU A OE2   1 
ATOM   23437 N  N     . ILE A 1 4626 ? 164.993 291.421 213.300 1.00 13.85 ? 4626 ILE A N     1 
ATOM   23438 C  CA    . ILE A 1 4626 ? 164.916 291.642 211.825 1.00 17.32 ? 4626 ILE A CA    1 
ATOM   23439 C  C     . ILE A 1 4626 ? 164.208 292.982 211.566 1.00 19.37 ? 4626 ILE A C     1 
ATOM   23440 O  O     . ILE A 1 4626 ? 163.608 293.524 212.516 1.00 22.00 ? 4626 ILE A O     1 
ATOM   23441 C  CB    . ILE A 1 4626 ? 164.198 290.468 211.138 1.00 18.34 ? 4626 ILE A CB    1 
ATOM   23442 C  CG1   . ILE A 1 4626 ? 162.753 290.343 211.611 1.00 17.33 ? 4626 ILE A CG1   1 
ATOM   23443 C  CG2   . ILE A 1 4626 ? 164.972 289.166 211.343 1.00 15.57 ? 4626 ILE A CG2   1 
ATOM   23444 C  CD1   . ILE A 1 4626 ? 162.113 289.005 211.295 1.00 21.74 ? 4626 ILE A CD1   1 
ATOM   23445 N  N     . ALA A 1 4627 ? 164.273 293.481 210.328 1.00 21.36 ? 4627 ALA A N     1 
ATOM   23446 C  CA    . ALA A 1 4627 ? 163.662 294.790 210.001 1.00 25.35 ? 4627 ALA A CA    1 
ATOM   23447 C  C     . ALA A 1 4627 ? 162.605 294.626 208.908 1.00 28.12 ? 4627 ALA A C     1 
ATOM   23448 O  O     . ALA A 1 4627 ? 162.471 293.507 208.365 1.00 31.56 ? 4627 ALA A O     1 
ATOM   23449 C  CB    . ALA A 1 4627 ? 164.741 295.762 209.577 1.00 21.46 ? 4627 ALA A CB    1 
ATOM   23450 N  N     . THR A 1 4628 ? 161.861 295.697 208.612 1.00 29.19 ? 4628 THR A N     1 
ATOM   23451 C  CA    . THR A 1 4628 ? 160.847 295.667 207.531 1.00 35.08 ? 4628 THR A CA    1 
ATOM   23452 C  C     . THR A 1 4628 ? 159.918 294.486 207.723 1.00 31.16 ? 4628 THR A C     1 
ATOM   23453 O  O     . THR A 1 4628 ? 159.589 294.172 208.887 1.00 31.25 ? 4628 THR A O     1 
ATOM   23454 C  CB    . THR A 1 4628 ? 161.537 295.625 206.167 1.00 28.98 ? 4628 THR A CB    1 
ATOM   23455 O  OG1   . THR A 1 4628 ? 162.033 294.299 206.010 1.00 27.59 ? 4628 THR A OG1   1 
ATOM   23456 C  CG2   . THR A 1 4628 ? 162.677 296.623 206.062 1.00 26.52 ? 4628 THR A CG2   1 
ATOM   23457 N  N     . LYS A 1 4629 ? 159.506 293.853 206.621 1.00 26.01 ? 4629 LYS A N     1 
ATOM   23458 C  CA    . LYS A 1 4629 ? 158.566 292.705 206.695 1.00 34.15 ? 4629 LYS A CA    1 
ATOM   23459 C  C     . LYS A 1 4629 ? 159.349 291.398 206.499 1.00 33.34 ? 4629 LYS A C     1 
ATOM   23460 O  O     . LYS A 1 4629 ? 158.707 290.356 206.237 1.00 34.17 ? 4629 LYS A O     1 
ATOM   23461 C  CB    . LYS A 1 4629 ? 157.475 292.852 205.631 1.00 31.43 ? 4629 LYS A CB    1 
ATOM   23462 C  CG    . LYS A 1 4629 ? 157.989 292.906 204.199 1.00 31.81 ? 4629 LYS A CG    1 
ATOM   23463 C  CD    . LYS A 1 4629 ? 156.885 293.142 203.174 1.00 32.82 ? 4629 LYS A CD    1 
ATOM   23464 C  CE    . LYS A 1 4629 ? 156.162 294.429 203.413 1.00 35.60 ? 4629 LYS A CE    1 
ATOM   23465 N  NZ    . LYS A 1 4629 ? 155.100 294.644 202.426 1.00 37.30 ? 4629 LYS A NZ    1 
ATOM   23466 N  N     . GLU A 1 4630 ? 160.677 291.455 206.626 1.00 26.47 ? 4630 GLU A N     1 
ATOM   23467 C  CA    . GLU A 1 4630 ? 161.517 290.247 206.422 1.00 24.22 ? 4630 GLU A CA    1 
ATOM   23468 C  C     . GLU A 1 4630 ? 160.938 289.091 207.250 1.00 28.73 ? 4630 GLU A C     1 
ATOM   23469 O  O     . GLU A 1 4630 ? 160.821 289.249 208.483 1.00 22.35 ? 4630 GLU A O     1 
ATOM   23470 C  CB    . GLU A 1 4630 ? 162.967 290.519 206.821 1.00 20.53 ? 4630 GLU A CB    1 
ATOM   23471 C  CG    . GLU A 1 4630 ? 163.607 291.659 206.035 1.00 24.84 ? 4630 GLU A CG    1 
ATOM   23472 C  CD    . GLU A 1 4630 ? 163.550 291.470 204.531 1.00 34.20 ? 4630 GLU A CD    1 
ATOM   23473 O  OE1   . GLU A 1 4630 ? 164.121 290.477 204.035 1.00 33.74 ? 4630 GLU A OE1   1 
ATOM   23474 O  OE2   . GLU A 1 4630 ? 162.925 292.317 203.856 1.00 32.61 ? 4630 GLU A OE2   1 
ATOM   23475 N  N     . ASP A 1 4631 ? 160.594 287.978 206.597 1.00 25.11 ? 4631 ASP A N     1 
ATOM   23476 C  CA    . ASP A 1 4631 ? 160.084 286.785 207.326 1.00 17.54 ? 4631 ASP A CA    1 
ATOM   23477 C  C     . ASP A 1 4631 ? 161.262 286.108 208.030 1.00 14.75 ? 4631 ASP A C     1 
ATOM   23478 O  O     . ASP A 1 4631 ? 162.237 285.750 207.340 1.00 17.94 ? 4631 ASP A O     1 
ATOM   23479 C  CB    . ASP A 1 4631 ? 159.359 285.828 206.394 1.00 20.23 ? 4631 ASP A CB    1 
ATOM   23480 C  CG    . ASP A 1 4631 ? 158.843 284.543 207.028 1.00 24.07 ? 4631 ASP A CG    1 
ATOM   23481 O  OD1   . ASP A 1 4631 ? 159.015 284.378 208.254 1.00 20.85 ? 4631 ASP A OD1   1 
ATOM   23482 O  OD2   . ASP A 1 4631 ? 158.274 283.712 206.288 1.00 28.15 ? 4631 ASP A OD2   1 
ATOM   23483 N  N     . PRO A 1 4632 ? 161.230 285.911 209.364 1.00 13.90 ? 4632 PRO A N     1 
ATOM   23484 C  CA    . PRO A 1 4632 ? 162.307 285.190 210.060 1.00 15.16 ? 4632 PRO A CA    1 
ATOM   23485 C  C     . PRO A 1 4632 ? 162.563 283.810 209.483 1.00 13.88 ? 4632 PRO A C     1 
ATOM   23486 O  O     . PRO A 1 4632 ? 163.682 283.294 209.594 1.00 10.77 ? 4632 PRO A O     1 
ATOM   23487 C  CB    . PRO A 1 4632 ? 161.801 285.120 211.510 1.00 13.02 ? 4632 PRO A CB    1 
ATOM   23488 C  CG    . PRO A 1 4632 ? 160.331 285.394 211.425 1.00 15.98 ? 4632 PRO A CG    1 
ATOM   23489 C  CD    . PRO A 1 4632 ? 160.183 286.357 210.296 1.00 13.76 ? 4632 PRO A CD    1 
ATOM   23490 N  N     . ARG A 1 4633 ? 161.550 283.201 208.869 1.00 17.18 ? 4633 ARG A N     1 
ATOM   23491 C  CA    . ARG A 1 4633 ? 161.727 281.895 208.244 1.00 13.26 ? 4633 ARG A CA    1 
ATOM   23492 C  C     . ARG A 1 4633 ? 162.639 281.980 207.026 1.00 12.56 ? 4633 ARG A C     1 
ATOM   23493 O  O     . ARG A 1 4633 ? 163.347 281.017 206.704 1.00 13.93 ? 4633 ARG A O     1 
ATOM   23494 C  CB    . ARG A 1 4633 ? 160.360 281.322 207.877 1.00 10.69 ? 4633 ARG A CB    1 
ATOM   23495 C  CG    . ARG A 1 4633 ? 159.507 281.013 209.100 1.00 14.62 ? 4633 ARG A CG    1 
ATOM   23496 C  CD    . ARG A 1 4633 ? 158.248 280.246 208.749 1.00 17.20 ? 4633 ARG A CD    1 
ATOM   23497 N  NE    . ARG A 1 4633 ? 157.332 281.042 207.940 1.00 14.01 ? 4633 ARG A NE    1 
ATOM   23498 C  CZ    . ARG A 1 4633 ? 156.930 280.707 206.724 1.00 18.85 ? 4633 ARG A CZ    1 
ATOM   23499 N  NH1   . ARG A 1 4633 ? 157.347 279.598 206.140 1.00 24.29 ? 4633 ARG A NH1   1 
ATOM   23500 N  NH2   . ARG A 1 4633 ? 156.086 281.506 206.078 1.00 20.56 ? 4633 ARG A NH2   1 
ATOM   23501 N  N     . SER A 1 4634 ? 162.635 283.121 206.332 1.00 9.02  ? 4634 SER A N     1 
ATOM   23502 C  CA    . SER A 1 4634 ? 163.536 283.302 205.199 1.00 6.69  ? 4634 SER A CA    1 
ATOM   23503 C  C     . SER A 1 4634 ? 164.991 283.326 205.652 1.00 8.47  ? 4634 SER A C     1 
ATOM   23504 O  O     . SER A 1 4634 ? 165.879 282.844 204.940 1.00 11.92 ? 4634 SER A O     1 
ATOM   23505 C  CB    . SER A 1 4634 ? 163.189 284.583 204.441 1.00 8.98  ? 4634 SER A CB    1 
ATOM   23506 O  OG    . SER A 1 4634 ? 163.396 285.728 205.248 1.00 17.77 ? 4634 SER A OG    1 
ATOM   23507 N  N     . PHE A 1 4635 ? 165.252 283.893 206.831 1.00 9.62  ? 4635 PHE A N     1 
ATOM   23508 C  CA    . PHE A 1 4635 ? 166.593 283.834 207.401 1.00 5.68  ? 4635 PHE A CA    1 
ATOM   23509 C  C     . PHE A 1 4635 ? 167.021 282.394 207.645 1.00 5.97  ? 4635 PHE A C     1 
ATOM   23510 O  O     . PHE A 1 4635 ? 168.187 282.040 207.443 1.00 6.79  ? 4635 PHE A O     1 
ATOM   23511 C  CB    . PHE A 1 4635 ? 166.646 284.639 208.700 1.00 6.72  ? 4635 PHE A CB    1 
ATOM   23512 C  CG    . PHE A 1 4635 ? 166.727 286.120 208.491 1.00 7.99  ? 4635 PHE A CG    1 
ATOM   23513 C  CD1   . PHE A 1 4635 ? 165.581 286.868 208.289 1.00 8.66  ? 4635 PHE A CD1   1 
ATOM   23514 C  CD2   . PHE A 1 4635 ? 167.949 286.771 208.511 1.00 8.20  ? 4635 PHE A CD2   1 
ATOM   23515 C  CE1   . PHE A 1 4635 ? 165.654 288.232 208.095 1.00 10.29 ? 4635 PHE A CE1   1 
ATOM   23516 C  CE2   . PHE A 1 4635 ? 168.027 288.135 208.320 1.00 6.65  ? 4635 PHE A CE2   1 
ATOM   23517 C  CZ    . PHE A 1 4635 ? 166.878 288.867 208.113 1.00 9.72  ? 4635 PHE A CZ    1 
ATOM   23518 N  N     . TYR A 1 4636 ? 166.086 281.550 208.086 1.00 8.33  ? 4636 TYR A N     1 
ATOM   23519 C  CA    . TYR A 1 4636 ? 166.409 280.152 208.333 1.00 5.05  ? 4636 TYR A CA    1 
ATOM   23520 C  C     . TYR A 1 4636 ? 166.702 279.421 207.028 1.00 4.29  ? 4636 TYR A C     1 
ATOM   23521 O  O     . TYR A 1 4636 ? 167.624 278.602 206.960 1.00 5.61  ? 4636 TYR A O     1 
ATOM   23522 C  CB    . TYR A 1 4636 ? 165.255 279.475 209.071 1.00 7.58  ? 4636 TYR A CB    1 
ATOM   23523 C  CG    . TYR A 1 4636 ? 164.882 280.136 210.376 1.00 7.63  ? 4636 TYR A CG    1 
ATOM   23524 C  CD1   . TYR A 1 4636 ? 163.586 280.059 210.862 1.00 10.45 ? 4636 TYR A CD1   1 
ATOM   23525 C  CD2   . TYR A 1 4636 ? 165.812 280.865 211.102 1.00 6.54  ? 4636 TYR A CD2   1 
ATOM   23526 C  CE1   . TYR A 1 4636 ? 163.232 280.669 212.044 1.00 11.82 ? 4636 TYR A CE1   1 
ATOM   23527 C  CE2   . TYR A 1 4636 ? 165.463 281.483 212.282 1.00 8.92  ? 4636 TYR A CE2   1 
ATOM   23528 C  CZ    . TYR A 1 4636 ? 164.173 281.378 212.751 1.00 12.89 ? 4636 TYR A CZ    1 
ATOM   23529 O  OH    . TYR A 1 4636 ? 163.822 281.989 213.933 1.00 18.38 ? 4636 TYR A OH    1 
ATOM   23530 N  N     . GLU A 1 4637 ? 165.931 279.719 205.978 1.00 4.43  ? 4637 GLU A N     1 
ATOM   23531 C  CA    . GLU A 1 4637 ? 166.060 278.991 204.718 1.00 3.99  ? 4637 GLU A CA    1 
ATOM   23532 C  C     . GLU A 1 4637 ? 167.300 279.416 203.943 1.00 4.18  ? 4637 GLU A C     1 
ATOM   23533 O  O     . GLU A 1 4637 ? 167.885 278.610 203.212 1.00 11.67 ? 4637 GLU A O     1 
ATOM   23534 C  CB    . GLU A 1 4637 ? 164.804 279.192 203.872 1.00 5.25  ? 4637 GLU A CB    1 
ATOM   23535 C  CG    . GLU A 1 4637 ? 163.587 278.468 204.404 1.00 7.20  ? 4637 GLU A CG    1 
ATOM   23536 C  CD    . GLU A 1 4637 ? 162.454 278.430 203.406 1.00 18.45 ? 4637 GLU A CD    1 
ATOM   23537 O  OE1   . GLU A 1 4637 ? 162.615 278.993 202.305 1.00 12.78 ? 4637 GLU A OE1   1 
ATOM   23538 O  OE2   . GLU A 1 4637 ? 161.403 277.834 203.723 1.00 25.75 ? 4637 GLU A OE2   1 
ATOM   23539 N  N     . ARG A 1 4638 ? 167.710 280.673 204.079 1.00 4.99  ? 4638 ARG A N     1 
ATOM   23540 C  CA    . ARG A 1 4638 ? 168.876 281.156 203.352 1.00 3.94  ? 4638 ARG A CA    1 
ATOM   23541 C  C     . ARG A 1 4638 ? 170.185 280.815 204.052 1.00 5.79  ? 4638 ARG A C     1 
ATOM   23542 O  O     . ARG A 1 4638 ? 171.253 281.149 203.530 1.00 6.19  ? 4638 ARG A O     1 
ATOM   23543 C  CB    . ARG A 1 4638 ? 168.767 282.667 203.137 1.00 3.10  ? 4638 ARG A CB    1 
ATOM   23544 C  CG    . ARG A 1 4638 ? 167.656 283.052 202.172 1.00 3.14  ? 4638 ARG A CG    1 
ATOM   23545 C  CD    . ARG A 1 4638 ? 167.484 284.551 202.056 1.00 5.73  ? 4638 ARG A CD    1 
ATOM   23546 N  NE    . ARG A 1 4638 ? 168.716 285.224 201.668 1.00 7.94  ? 4638 ARG A NE    1 
ATOM   23547 C  CZ    . ARG A 1 4638 ? 168.855 285.950 200.567 1.00 5.80  ? 4638 ARG A CZ    1 
ATOM   23548 N  NH1   . ARG A 1 4638 ? 167.858 286.115 199.715 1.00 3.18  ? 4638 ARG A NH1   1 
ATOM   23549 N  NH2   . ARG A 1 4638 ? 170.028 286.525 200.314 1.00 12.31 ? 4638 ARG A NH2   1 
ATOM   23550 N  N     . GLY A 1 4639 ? 170.125 280.151 205.201 1.00 4.01  ? 4639 GLY A N     1 
ATOM   23551 C  CA    . GLY A 1 4639 ? 171.326 279.785 205.926 1.00 3.28  ? 4639 GLY A CA    1 
ATOM   23552 C  C     . GLY A 1 4639 ? 172.083 280.966 206.487 1.00 4.22  ? 4639 GLY A C     1 
ATOM   23553 O  O     . GLY A 1 4639 ? 173.320 280.981 206.446 1.00 9.33  ? 4639 GLY A O     1 
ATOM   23554 N  N     . VAL A 1 4640 ? 171.369 281.965 207.007 1.00 4.06  ? 4640 VAL A N     1 
ATOM   23555 C  CA    . VAL A 1 4640 ? 172.030 283.109 207.614 1.00 3.87  ? 4640 VAL A CA    1 
ATOM   23556 C  C     . VAL A 1 4640 ? 172.702 282.673 208.907 1.00 5.69  ? 4640 VAL A C     1 
ATOM   23557 O  O     . VAL A 1 4640 ? 172.090 282.026 209.766 1.00 8.65  ? 4640 VAL A O     1 
ATOM   23558 C  CB    . VAL A 1 4640 ? 171.021 284.242 207.857 1.00 3.94  ? 4640 VAL A CB    1 
ATOM   23559 C  CG1   . VAL A 1 4640 ? 171.711 285.445 208.473 1.00 5.48  ? 4640 VAL A CG1   1 
ATOM   23560 C  CG2   . VAL A 1 4640 ? 170.331 284.620 206.560 1.00 4.97  ? 4640 VAL A CG2   1 
ATOM   23561 N  N     . ALA A 1 4641 ? 173.975 283.026 209.048 1.00 8.24  ? 4641 ALA A N     1 
ATOM   23562 C  CA    . ALA A 1 4641 ? 174.772 282.601 210.190 1.00 3.48  ? 4641 ALA A CA    1 
ATOM   23563 C  C     . ALA A 1 4641 ? 175.890 283.612 210.403 1.00 5.87  ? 4641 ALA A C     1 
ATOM   23564 O  O     . ALA A 1 4641 ? 176.066 284.550 209.622 1.00 5.98  ? 4641 ALA A O     1 
ATOM   23565 C  CB    . ALA A 1 4641 ? 175.328 281.188 209.982 1.00 3.24  ? 4641 ALA A CB    1 
ATOM   23566 N  N     . VAL A 1 4642 ? 176.648 283.409 211.477 1.00 8.28  ? 4642 VAL A N     1 
ATOM   23567 C  CA    . VAL A 1 4642 ? 177.786 284.249 211.823 1.00 3.64  ? 4642 VAL A CA    1 
ATOM   23568 C  C     . VAL A 1 4642 ? 179.013 283.360 211.941 1.00 4.68  ? 4642 VAL A C     1 
ATOM   23569 O  O     . VAL A 1 4642 ? 178.949 282.275 212.529 1.00 5.31  ? 4642 VAL A O     1 
ATOM   23570 C  CB    . VAL A 1 4642 ? 177.540 285.028 213.134 1.00 5.64  ? 4642 VAL A CB    1 
ATOM   23571 C  CG1   . VAL A 1 4642 ? 178.786 285.796 213.549 1.00 4.76  ? 4642 VAL A CG1   1 
ATOM   23572 C  CG2   . VAL A 1 4642 ? 176.358 285.970 212.978 1.00 3.75  ? 4642 VAL A CG2   1 
ATOM   23573 N  N     . LEU A 1 4643 ? 180.125 283.807 211.366 1.00 7.50  ? 4643 LEU A N     1 
ATOM   23574 C  CA    . LEU A 1 4643 ? 181.384 283.081 211.423 1.00 5.09  ? 4643 LEU A CA    1 
ATOM   23575 C  C     . LEU A 1 4643 ? 182.363 283.805 212.335 1.00 7.81  ? 4643 LEU A C     1 
ATOM   23576 O  O     . LEU A 1 4643 ? 182.454 285.036 212.312 1.00 10.28 ? 4643 LEU A O     1 
ATOM   23577 C  CB    . LEU A 1 4643 ? 181.999 282.923 210.032 1.00 7.42  ? 4643 LEU A CB    1 
ATOM   23578 C  CG    . LEU A 1 4643 ? 181.164 282.220 208.962 1.00 4.86  ? 4643 LEU A CG    1 
ATOM   23579 C  CD1   . LEU A 1 4643 ? 181.994 282.006 207.708 1.00 4.60  ? 4643 LEU A CD1   1 
ATOM   23580 C  CD2   . LEU A 1 4643 ? 180.600 280.907 209.474 1.00 5.03  ? 4643 LEU A CD2   1 
ATOM   23581 N  N     . CYS A 1 4644 ? 183.093 283.033 213.141 1.00 10.70 ? 4644 CYS A N     1 
ATOM   23582 C  CA    . CYS A 1 4644 ? 184.095 283.626 214.021 1.00 11.80 ? 4644 CYS A CA    1 
ATOM   23583 C  C     . CYS A 1 4644 ? 185.322 284.085 213.243 1.00 8.77  ? 4644 CYS A C     1 
ATOM   23584 O  O     . CYS A 1 4644 ? 185.976 285.054 213.640 1.00 15.47 ? 4644 CYS A O     1 
ATOM   23585 C  CB    . CYS A 1 4644 ? 184.498 282.631 215.110 1.00 11.64 ? 4644 CYS A CB    1 
ATOM   23586 S  SG    . CYS A 1 4644 ? 183.233 282.344 216.365 1.00 38.35 ? 4644 CYS A SG    1 
ATOM   23587 N  N     . THR A 1 4645 ? 185.650 283.408 212.147 1.00 8.55  ? 4645 THR A N     1 
ATOM   23588 C  CA    . THR A 1 4645 ? 186.809 283.774 211.341 1.00 12.85 ? 4645 THR A CA    1 
ATOM   23589 C  C     . THR A 1 4645 ? 186.544 283.561 209.853 1.00 10.61 ? 4645 THR A C     1 
ATOM   23590 O  O     . THR A 1 4645 ? 185.421 283.268 209.448 1.00 13.35 ? 4645 THR A O     1 
ATOM   23591 C  CB    . THR A 1 4645 ? 188.056 282.968 211.745 1.00 22.72 ? 4645 THR A CB    1 
ATOM   23592 O  OG1   . THR A 1 4645 ? 189.212 283.520 211.105 1.00 31.56 ? 4645 THR A OG1   1 
ATOM   23593 C  CG2   . THR A 1 4645 ? 187.905 281.508 211.337 1.00 8.63  ? 4645 THR A CG2   1 
HETATM 23594 P  PB    . ADP B 2 .    ? 175.755 255.416 224.848 1.00 0.03  ? 4701 ADP A PB    1 
HETATM 23595 O  O1B   . ADP B 2 .    ? 177.252 255.375 224.988 1.00 0.73  ? 4701 ADP A O1B   1 
HETATM 23596 O  O2B   . ADP B 2 .    ? 175.271 256.553 223.990 1.00 1.20  ? 4701 ADP A O2B   1 
HETATM 23597 O  O3B   . ADP B 2 .    ? 175.170 254.088 224.446 1.00 0.36  ? 4701 ADP A O3B   1 
HETATM 23598 P  PA    . ADP B 2 .    ? 174.656 254.742 227.469 1.00 0.07  ? 4701 ADP A PA    1 
HETATM 23599 O  O1A   . ADP B 2 .    ? 173.370 254.144 227.007 1.00 0.10  ? 4701 ADP A O1A   1 
HETATM 23600 O  O2A   . ADP B 2 .    ? 175.759 253.826 227.877 1.00 11.38 ? 4701 ADP A O2A   1 
HETATM 23601 O  O3A   . ADP B 2 .    ? 175.192 255.716 226.321 1.00 0.72  ? 4701 ADP A O3A   1 
HETATM 23602 O  "O5'" . ADP B 2 .    ? 174.377 255.793 228.645 1.00 1.64  ? 4701 ADP A "O5'" 1 
HETATM 23603 C  "C5'" . ADP B 2 .    ? 175.502 256.520 229.198 1.00 0.68  ? 4701 ADP A "C5'" 1 
HETATM 23604 C  "C4'" . ADP B 2 .    ? 175.217 256.865 230.639 1.00 0.84  ? 4701 ADP A "C4'" 1 
HETATM 23605 O  "O4'" . ADP B 2 .    ? 174.142 257.840 230.687 1.00 2.06  ? 4701 ADP A "O4'" 1 
HETATM 23606 C  "C3'" . ADP B 2 .    ? 174.746 255.703 231.522 1.00 0.86  ? 4701 ADP A "C3'" 1 
HETATM 23607 O  "O3'" . ADP B 2 .    ? 175.179 255.881 232.864 1.00 9.72  ? 4701 ADP A "O3'" 1 
HETATM 23608 C  "C2'" . ADP B 2 .    ? 173.225 255.821 231.406 1.00 0.35  ? 4701 ADP A "C2'" 1 
HETATM 23609 O  "O2'" . ADP B 2 .    ? 172.518 255.175 232.442 1.00 1.76  ? 4701 ADP A "O2'" 1 
HETATM 23610 C  "C1'" . ADP B 2 .    ? 173.069 257.336 231.448 1.00 0.82  ? 4701 ADP A "C1'" 1 
HETATM 23611 N  N9    . ADP B 2 .    ? 171.824 257.808 230.857 1.00 0.92  ? 4701 ADP A N9    1 
HETATM 23612 C  C8    . ADP B 2 .    ? 171.591 258.055 229.528 1.00 0.23  ? 4701 ADP A C8    1 
HETATM 23613 N  N7    . ADP B 2 .    ? 170.375 258.467 229.281 1.00 0.11  ? 4701 ADP A N7    1 
HETATM 23614 C  C5    . ADP B 2 .    ? 169.763 258.499 230.525 1.00 0.16  ? 4701 ADP A C5    1 
HETATM 23615 C  C6    . ADP B 2 .    ? 168.464 258.856 230.931 1.00 0.17  ? 4701 ADP A C6    1 
HETATM 23616 N  N6    . ADP B 2 .    ? 167.513 259.262 230.097 1.00 0.22  ? 4701 ADP A N6    1 
HETATM 23617 N  N1    . ADP B 2 .    ? 168.179 258.776 232.252 1.00 0.27  ? 4701 ADP A N1    1 
HETATM 23618 C  C2    . ADP B 2 .    ? 169.140 258.366 233.089 1.00 0.30  ? 4701 ADP A C2    1 
HETATM 23619 N  N3    . ADP B 2 .    ? 170.392 258.005 232.822 1.00 0.25  ? 4701 ADP A N3    1 
HETATM 23620 C  C4    . ADP B 2 .    ? 170.647 258.095 231.507 1.00 0.29  ? 4701 ADP A C4    1 
HETATM 23621 P  PG    . ATP C 3 .    ? 205.454 251.960 235.330 1.00 0.00  ? 4702 ATP A PG    1 
HETATM 23622 O  O1G   . ATP C 3 .    ? 205.047 253.270 234.718 1.00 0.13  ? 4702 ATP A O1G   1 
HETATM 23623 O  O2G   . ATP C 3 .    ? 204.369 250.923 235.261 1.00 0.08  ? 4702 ATP A O2G   1 
HETATM 23624 O  O3G   . ATP C 3 .    ? 206.762 251.458 234.803 1.00 0.32  ? 4702 ATP A O3G   1 
HETATM 23625 P  PB    . ATP C 3 .    ? 204.770 252.795 238.083 1.00 0.00  ? 4702 ATP A PB    1 
HETATM 23626 O  O1B   . ATP C 3 .    ? 204.414 254.212 237.797 1.00 0.06  ? 4702 ATP A O1B   1 
HETATM 23627 O  O2B   . ATP C 3 .    ? 203.693 251.798 238.332 1.00 0.02  ? 4702 ATP A O2B   1 
HETATM 23628 O  O3B   . ATP C 3 .    ? 205.696 252.255 236.894 1.00 0.05  ? 4702 ATP A O3B   1 
HETATM 23629 P  PA    . ATP C 3 .    ? 206.183 251.692 240.415 1.00 0.00  ? 4702 ATP A PA    1 
HETATM 23630 O  O1A   . ATP C 3 .    ? 206.024 250.324 239.846 1.00 3.21  ? 4702 ATP A O1A   1 
HETATM 23631 O  O2A   . ATP C 3 .    ? 205.446 252.016 241.669 1.00 0.02  ? 4702 ATP A O2A   1 
HETATM 23632 O  O3A   . ATP C 3 .    ? 205.807 252.776 239.298 1.00 0.03  ? 4702 ATP A O3A   1 
HETATM 23633 O  "O5'" . ATP C 3 .    ? 207.744 251.991 240.607 1.00 5.30  ? 4702 ATP A "O5'" 1 
HETATM 23634 C  "C5'" . ATP C 3 .    ? 208.172 253.183 241.307 1.00 1.34  ? 4702 ATP A "C5'" 1 
HETATM 23635 C  "C4'" . ATP C 3 .    ? 209.611 253.014 241.723 1.00 0.91  ? 4702 ATP A "C4'" 1 
HETATM 23636 O  "O4'" . ATP C 3 .    ? 209.822 253.710 242.974 1.00 4.12  ? 4702 ATP A "O4'" 1 
HETATM 23637 C  "C3'" . ATP C 3 .    ? 210.046 251.585 242.048 1.00 1.62  ? 4702 ATP A "C3'" 1 
HETATM 23638 O  "O3'" . ATP C 3 .    ? 211.462 251.474 242.080 1.00 23.47 ? 4702 ATP A "O3'" 1 
HETATM 23639 C  "C2'" . ATP C 3 .    ? 209.447 251.417 243.445 1.00 1.27  ? 4702 ATP A "C2'" 1 
HETATM 23640 O  "O2'" . ATP C 3 .    ? 210.101 250.434 244.218 1.00 11.03 ? 4702 ATP A "O2'" 1 
HETATM 23641 C  "C1'" . ATP C 3 .    ? 209.624 252.813 244.043 1.00 1.12  ? 4702 ATP A "C1'" 1 
HETATM 23642 N  N9    . ATP C 3 .    ? 208.460 253.256 244.799 1.00 0.46  ? 4702 ATP A N9    1 
HETATM 23643 C  C8    . ATP C 3 .    ? 207.153 253.273 244.384 1.00 0.22  ? 4702 ATP A C8    1 
HETATM 23644 N  N7    . ATP C 3 .    ? 206.335 253.718 245.309 1.00 0.30  ? 4702 ATP A N7    1 
HETATM 23645 C  C5    . ATP C 3 .    ? 207.153 253.989 246.397 1.00 0.33  ? 4702 ATP A C5    1 
HETATM 23646 C  C6    . ATP C 3 .    ? 206.888 254.484 247.688 1.00 0.46  ? 4702 ATP A C6    1 
HETATM 23647 N  N6    . ATP C 3 .    ? 205.672 254.801 248.121 1.00 0.46  ? 4702 ATP A N6    1 
HETATM 23648 N  N1    . ATP C 3 .    ? 207.941 254.636 248.524 1.00 0.79  ? 4702 ATP A N1    1 
HETATM 23649 C  C2    . ATP C 3 .    ? 209.163 254.313 248.082 1.00 0.73  ? 4702 ATP A C2    1 
HETATM 23650 N  N3    . ATP C 3 .    ? 209.531 253.839 246.894 1.00 0.84  ? 4702 ATP A N3    1 
HETATM 23651 C  C4    . ATP C 3 .    ? 208.464 253.702 246.090 1.00 0.42  ? 4702 ATP A C4    1 
HETATM 23652 P  PB    . ADP D 2 .    ? 228.126 246.395 216.219 1.00 0.01  ? 4703 ADP A PB    1 
HETATM 23653 O  O1B   . ADP D 2 .    ? 227.753 245.439 217.315 1.00 1.10  ? 4703 ADP A O1B   1 
HETATM 23654 O  O2B   . ADP D 2 .    ? 227.238 246.277 215.014 1.00 1.80  ? 4703 ADP A O2B   1 
HETATM 23655 O  O3B   . ADP D 2 .    ? 228.263 247.812 216.709 1.00 0.24  ? 4703 ADP A O3B   1 
HETATM 23656 P  PA    . ADP D 2 .    ? 230.412 244.587 215.818 1.00 0.11  ? 4703 ADP A PA    1 
HETATM 23657 O  O1A   . ADP D 2 .    ? 230.863 244.388 217.225 1.00 0.29  ? 4703 ADP A O1A   1 
HETATM 23658 O  O2A   . ADP D 2 .    ? 229.597 243.511 215.182 1.00 3.75  ? 4703 ADP A O2A   1 
HETATM 23659 O  O3A   . ADP D 2 .    ? 229.600 245.964 215.732 1.00 1.85  ? 4703 ADP A O3A   1 
HETATM 23660 O  "O5'" . ADP D 2 .    ? 231.672 244.911 214.884 1.00 1.08  ? 4703 ADP A "O5'" 1 
HETATM 23661 C  "C5'" . ADP D 2 .    ? 232.549 246.009 215.228 1.00 1.21  ? 4703 ADP A "C5'" 1 
HETATM 23662 C  "C4'" . ADP D 2 .    ? 233.682 246.062 214.234 1.00 0.60  ? 4703 ADP A "C4'" 1 
HETATM 23663 O  "O4'" . ADP D 2 .    ? 234.687 246.990 214.718 1.00 0.64  ? 4703 ADP A "O4'" 1 
HETATM 23664 C  "C3'" . ADP D 2 .    ? 234.429 244.744 213.996 1.00 1.07  ? 4703 ADP A "C3'" 1 
HETATM 23665 O  "O3'" . ADP D 2 .    ? 234.902 244.670 212.657 1.00 9.37  ? 4703 ADP A "O3'" 1 
HETATM 23666 C  "C2'" . ADP D 2 .    ? 235.581 244.850 214.995 1.00 0.59  ? 4703 ADP A "C2'" 1 
HETATM 23667 O  "O2'" . ADP D 2 .    ? 236.680 244.026 214.672 1.00 3.64  ? 4703 ADP A "O2'" 1 
HETATM 23668 C  "C1'" . ADP D 2 .    ? 235.921 246.332 214.885 1.00 0.52  ? 4703 ADP A "C1'" 1 
HETATM 23669 N  N9    . ADP D 2 .    ? 236.556 246.871 216.081 1.00 0.46  ? 4703 ADP A N9    1 
HETATM 23670 C  C8    . ADP D 2 .    ? 236.270 248.074 216.673 1.00 0.38  ? 4703 ADP A C8    1 
HETATM 23671 N  N7    . ADP D 2 .    ? 236.992 248.314 217.737 1.00 0.90  ? 4703 ADP A N7    1 
HETATM 23672 C  C5    . ADP D 2 .    ? 237.815 247.204 217.853 1.00 0.43  ? 4703 ADP A C5    1 
HETATM 23673 C  C6    . ADP D 2 .    ? 238.810 246.861 218.786 1.00 0.30  ? 4703 ADP A C6    1 
HETATM 23674 N  N6    . ADP D 2 .    ? 239.157 247.631 219.812 1.00 0.58  ? 4703 ADP A N6    1 
HETATM 23675 N  N1    . ADP D 2 .    ? 239.446 245.679 218.614 1.00 0.51  ? 4703 ADP A N1    1 
HETATM 23676 C  C2    . ADP D 2 .    ? 239.091 244.909 217.577 1.00 0.57  ? 4703 ADP A C2    1 
HETATM 23677 N  N3    . ADP D 2 .    ? 238.172 245.129 216.642 1.00 0.35  ? 4703 ADP A N3    1 
HETATM 23678 C  C4    . ADP D 2 .    ? 237.560 246.306 216.834 1.00 0.31  ? 4703 ADP A C4    1 
HETATM 23679 P  PB    . ADP E 2 .    ? 219.255 238.147 186.236 1.00 0.44  ? 4704 ADP A PB    1 
HETATM 23680 O  O1B   . ADP E 2 .    ? 220.068 239.408 186.108 1.00 1.06  ? 4704 ADP A O1B   1 
HETATM 23681 O  O2B   . ADP E 2 .    ? 219.702 237.275 187.378 1.00 1.45  ? 4704 ADP A O2B   1 
HETATM 23682 O  O3B   . ADP E 2 .    ? 217.774 238.409 186.249 1.00 1.03  ? 4704 ADP A O3B   1 
HETATM 23683 P  PA    . ADP E 2 .    ? 219.805 235.746 184.628 1.00 0.14  ? 4704 ADP A PA    1 
HETATM 23684 O  O1A   . ADP E 2 .    ? 221.096 235.362 185.267 1.00 0.49  ? 4704 ADP A O1A   1 
HETATM 23685 O  O2A   . ADP E 2 .    ? 218.580 234.979 184.995 1.00 3.90  ? 4704 ADP A O2A   1 
HETATM 23686 O  O3A   . ADP E 2 .    ? 219.545 237.303 184.897 1.00 0.95  ? 4704 ADP A O3A   1 
HETATM 23687 O  "O5'" . ADP E 2 .    ? 219.976 235.741 183.035 1.00 1.57  ? 4704 ADP A "O5'" 1 
HETATM 23688 C  "C5'" . ADP E 2 .    ? 218.803 235.916 182.204 1.00 1.25  ? 4704 ADP A "C5'" 1 
HETATM 23689 C  "C4'" . ADP E 2 .    ? 219.176 235.653 180.767 1.00 1.41  ? 4704 ADP A "C4'" 1 
HETATM 23690 O  "O4'" . ADP E 2 .    ? 219.876 236.801 180.224 1.00 2.11  ? 4704 ADP A "O4'" 1 
HETATM 23691 C  "C3'" . ADP E 2 .    ? 220.142 234.491 180.524 1.00 1.91  ? 4704 ADP A "C3'" 1 
HETATM 23692 O  "O3'" . ADP E 2 .    ? 219.472 233.236 180.525 1.00 12.37 ? 4704 ADP A "O3'" 1 
HETATM 23693 C  "C2'" . ADP E 2 .    ? 220.700 234.854 179.147 1.00 2.55  ? 4704 ADP A "C2'" 1 
HETATM 23694 O  "O2'" . ADP E 2 .    ? 219.829 234.484 178.103 1.00 2.11  ? 4704 ADP A "O2'" 1 
HETATM 23695 C  "C1'" . ADP E 2 .    ? 220.807 236.374 179.252 1.00 0.76  ? 4704 ADP A "C1'" 1 
HETATM 23696 N  N9    . ADP E 2 .    ? 222.130 236.855 179.632 1.00 0.60  ? 4704 ADP A N9    1 
HETATM 23697 C  C8    . ADP E 2 .    ? 222.521 237.303 180.868 1.00 1.29  ? 4704 ADP A C8    1 
HETATM 23698 N  N7    . ADP E 2 .    ? 223.774 237.674 180.913 1.00 1.66  ? 4704 ADP A N7    1 
HETATM 23699 C  C5    . ADP E 2 .    ? 224.247 237.445 179.632 1.00 0.72  ? 4704 ADP A C5    1 
HETATM 23700 C  C6    . ADP E 2 .    ? 225.513 237.630 179.042 1.00 0.99  ? 4704 ADP A C6    1 
HETATM 23701 N  N6    . ADP E 2 .    ? 226.567 238.110 179.690 1.00 0.77  ? 4704 ADP A N6    1 
HETATM 23702 N  N1    . ADP E 2 .    ? 225.648 237.299 177.736 1.00 1.61  ? 4704 ADP A N1    1 
HETATM 23703 C  C2    . ADP E 2 .    ? 224.581 236.817 177.087 1.00 1.18  ? 4704 ADP A C2    1 
HETATM 23704 N  N3    . ADP E 2 .    ? 223.349 236.599 177.536 1.00 0.85  ? 4704 ADP A N3    1 
HETATM 23705 C  C4    . ADP E 2 .    ? 223.244 236.936 178.832 1.00 0.57  ? 4704 ADP A C4    1 
HETATM 23706 MG MG    . MG  F 4 .    ? 176.281 252.330 224.140 1.00 0.63  ? 4705 MG  A MG    1 
HETATM 23707 MG MG    . MG  G 4 .    ? 203.676 250.101 237.032 1.00 0.04  ? 4706 MG  A MG    1 
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